data_9CZF
# 
_entry.id   9CZF 
# 
_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   9CZF         pdb_00009czf 10.2210/pdb9czf/pdb 
WWPDB D_1000287048 ?            ?                   
# 
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                        9CZF 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-05 
_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 . 9CZD unspecified 
PDB . 9CZA unspecified 
PDB . 9CZ7 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)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
748.682   1  ? ? ? ? 
8  non-polymer man 'CALCIUM ION' 40.078    6  ? ? ? ? 
9  non-polymer syn alpha-D-mannopyranose 180.156   2  ? ? ? ? 
10 non-polymer syn GLYCEROL 92.094    8  ? ? ? ? 
11 non-polymer syn 'MAGNESIUM ION' 24.305    1  ? ? ? ? 
12 non-polymer syn 
;(2S)-{5-fluoro-2-[(6S)-5-oxaspiro[2.5]octan-6-yl]phenyl}{(3R)-3-[4-(5,6,7,8-tetrahydro-1,8-naphthyridin-2-yl)butoxy]pyrrolidin-1-yl}acetic acid
;
537.665   1  ? ? ? ? 
13 non-polymer syn 'ACETATE ION' 59.044    2  ? ? ? ? 
14 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   1  ? ? ? ? 
15 non-polymer syn 'CHLORIDE ION' 35.453    1  ? ? ? ? 
16 water       nat water 18.015    81 ? ? ? ? 
# 
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  alpha-D-mannopyranose MAN   
10 GLYCEROL GOL   
11 'MAGNESIUM ION' MG    
12 
;(2S)-{5-fluoro-2-[(6S)-5-oxaspiro[2.5]octan-6-yl]phenyl}{(3R)-3-[4-(5,6,7,8-tetrahydro-1,8-naphthyridin-2-yl)butoxy]pyrrolidin-1-yl}acetic acid
;
A1A6I 
13 'ACETATE ION' ACT   
14 2-acetamido-2-deoxy-beta-D-glucopyranose NAG   
15 'CHLORIDE ION' CL    
16 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 DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                                
'Glycam Condensed Sequence' GMML       1.0   
8 7 'WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1'                         
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]{}}}}'                                       
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 ? 
# 
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 
A1A6I non-polymer                   . 
;(2S)-{5-fluoro-2-[(6S)-5-oxaspiro[2.5]octan-6-yl]phenyl}{(3R)-3-[4-(5,6,7,8-tetrahydro-1,8-naphthyridin-2-yl)butoxy]pyrrolidin-1-yl}acetic acid
;
MORF-627 'C31 H40 F N3 O4' 537.665 
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  
CL    non-polymer                   . 'CHLORIDE ION' ? 'Cl -1'           35.453  
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 I NAG 1 I NAG 1 n 
E 5 NAG 2 I NAG 2 I NAG 2 n 
E 5 BMA 3 I BMA 3 I BMA 3 n 
F 6 NAG 1 E NAG 1 E NAG 1 n 
F 6 NAG 2 E NAG 2 E NAG 2 n 
F 6 BMA 3 E BMA 3 E BMA 3 n 
F 6 MAN 4 E MAN 4 E MAN 4 n 
F 6 MAN 5 E MAN 5 E MAN 5 n 
F 6 MAN 6 E MAN 6 E MAN 6 n 
G 7 NAG 1 F NAG 1 F NAG 1 n 
G 7 NAG 2 F NAG 2 F NAG 2 n 
G 7 BMA 3 F BMA 3 F BMA 3 n 
G 7 MAN 4 F MAN 4 F MAN 4 n 
H 5 NAG 1 G NAG 1 G NAG 1 n 
H 5 NAG 2 G NAG 2 G NAG 2 n 
H 5 BMA 3 G BMA 3 G BMA 3 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1A6I ? ? A1A6I ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MAN   ? ? MAN   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NAG   ? ? NAG   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
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  MAN   1  2005 3270 MAN   MAN A . 
N  9  MAN   1  2006 3271 MAN   MAN A . 
O  10 GOL   1  2007 3    GOL   GOL A . 
P  10 GOL   1  2008 4    GOL   GOL A . 
Q  10 GOL   1  2009 5    GOL   GOL A . 
R  10 GOL   1  2010 9    GOL   GOL A . 
S  11 MG    1  2001 2001 MG    MG  B . 
T  8  CA    1  2002 2002 CA    CA  B . 
U  8  CA    1  2003 2003 CA    CA  B . 
V  12 A1A6I 1  2004 1    A1A6I 027 B . 
W  10 GOL   1  2005 6    GOL   GOL B . 
X  10 GOL   1  2006 8    GOL   GOL B . 
Y  13 ACT   1  2007 3    ACT   ACT B . 
Z  14 NAG   1  2008 2    NAG   NAG B . 
AA 15 CL    1  2009 1    CL    CL  B . 
BA 10 GOL   1  301  1    GOL   GOL C . 
CA 10 GOL   1  301  7    GOL   GOL D . 
DA 13 ACT   1  302  2    ACT   ACT D . 
EA 16 HOH   1  2101 71   HOH   HOH A . 
EA 16 HOH   2  2102 14   HOH   HOH A . 
EA 16 HOH   3  2103 16   HOH   HOH A . 
EA 16 HOH   4  2104 9    HOH   HOH A . 
EA 16 HOH   5  2105 74   HOH   HOH A . 
EA 16 HOH   6  2106 6    HOH   HOH A . 
EA 16 HOH   7  2107 73   HOH   HOH A . 
EA 16 HOH   8  2108 8    HOH   HOH A . 
EA 16 HOH   9  2109 7    HOH   HOH A . 
EA 16 HOH   10 2110 54   HOH   HOH A . 
EA 16 HOH   11 2111 53   HOH   HOH A . 
EA 16 HOH   12 2112 35   HOH   HOH A . 
EA 16 HOH   13 2113 79   HOH   HOH A . 
EA 16 HOH   14 2114 15   HOH   HOH A . 
EA 16 HOH   15 2115 22   HOH   HOH A . 
EA 16 HOH   16 2116 65   HOH   HOH A . 
EA 16 HOH   17 2117 47   HOH   HOH A . 
EA 16 HOH   18 2118 11   HOH   HOH A . 
EA 16 HOH   19 2119 56   HOH   HOH A . 
EA 16 HOH   20 2120 33   HOH   HOH A . 
EA 16 HOH   21 2121 37   HOH   HOH A . 
EA 16 HOH   22 2122 36   HOH   HOH A . 
EA 16 HOH   23 2123 67   HOH   HOH A . 
EA 16 HOH   24 2124 75   HOH   HOH A . 
EA 16 HOH   25 2125 62   HOH   HOH A . 
EA 16 HOH   26 2126 69   HOH   HOH A . 
EA 16 HOH   27 2127 45   HOH   HOH A . 
EA 16 HOH   28 2128 26   HOH   HOH A . 
EA 16 HOH   29 2129 39   HOH   HOH A . 
EA 16 HOH   30 2130 63   HOH   HOH A . 
EA 16 HOH   31 2131 13   HOH   HOH A . 
EA 16 HOH   32 2132 32   HOH   HOH A . 
EA 16 HOH   33 2133 57   HOH   HOH A . 
EA 16 HOH   34 2134 80   HOH   HOH A . 
EA 16 HOH   35 2135 83   HOH   HOH A . 
EA 16 HOH   36 2136 38   HOH   HOH A . 
EA 16 HOH   37 2137 51   HOH   HOH A . 
EA 16 HOH   38 2138 41   HOH   HOH A . 
EA 16 HOH   39 2139 58   HOH   HOH A . 
EA 16 HOH   40 2140 46   HOH   HOH A . 
EA 16 HOH   41 2141 40   HOH   HOH A . 
EA 16 HOH   42 2142 52   HOH   HOH A . 
EA 16 HOH   43 2143 34   HOH   HOH A . 
FA 16 HOH   1  2101 43   HOH   HOH B . 
FA 16 HOH   2  2102 20   HOH   HOH B . 
FA 16 HOH   3  2103 23   HOH   HOH B . 
FA 16 HOH   4  2104 12   HOH   HOH B . 
FA 16 HOH   5  2105 3    HOH   HOH B . 
FA 16 HOH   6  2106 84   HOH   HOH B . 
FA 16 HOH   7  2107 18   HOH   HOH B . 
FA 16 HOH   8  2108 24   HOH   HOH B . 
FA 16 HOH   9  2109 50   HOH   HOH B . 
FA 16 HOH   10 2110 2    HOH   HOH B . 
FA 16 HOH   11 2111 31   HOH   HOH B . 
FA 16 HOH   12 2112 19   HOH   HOH B . 
FA 16 HOH   13 2113 25   HOH   HOH B . 
FA 16 HOH   14 2114 85   HOH   HOH B . 
FA 16 HOH   15 2115 48   HOH   HOH B . 
FA 16 HOH   16 2116 49   HOH   HOH B . 
FA 16 HOH   17 2117 70   HOH   HOH B . 
FA 16 HOH   18 2118 17   HOH   HOH B . 
FA 16 HOH   19 2119 1    HOH   HOH B . 
FA 16 HOH   20 2120 44   HOH   HOH B . 
FA 16 HOH   21 2121 4    HOH   HOH B . 
FA 16 HOH   22 2122 78   HOH   HOH B . 
FA 16 HOH   23 2123 42   HOH   HOH B . 
FA 16 HOH   24 2124 10   HOH   HOH B . 
FA 16 HOH   25 2125 60   HOH   HOH B . 
FA 16 HOH   26 2126 21   HOH   HOH B . 
FA 16 HOH   27 2127 27   HOH   HOH B . 
FA 16 HOH   28 2128 82   HOH   HOH B . 
FA 16 HOH   29 2129 5    HOH   HOH B . 
FA 16 HOH   30 2130 77   HOH   HOH B . 
FA 16 HOH   31 2131 28   HOH   HOH B . 
FA 16 HOH   32 2132 76   HOH   HOH B . 
GA 16 HOH   1  401  30   HOH   HOH D . 
GA 16 HOH   2  402  55   HOH   HOH D . 
GA 16 HOH   3  403  64   HOH   HOH D . 
GA 16 HOH   4  404  86   HOH   HOH D . 
GA 16 HOH   5  405  81   HOH   HOH D . 
GA 16 HOH   6  406  66   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 G NAG 1    ? O1 ? H NAG 1 O1 
2 1 N 1 A MAN 2005 ? O1 ? M MAN 1 O1 
3 1 N 1 A MAN 2006 ? O1 ? N MAN 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                     9CZF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     95.840 
_cell.length_a_esd                 ? 
_cell.length_b                     133.130 
_cell.length_b_esd                 ? 
_cell.length_c                     169.550 
_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                         9CZF 
_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                   9CZF 
_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             3.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.93 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, 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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-05-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9792 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9792 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CZF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.53 
_reflns.d_resolution_low                               54.67 
_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                                     73086 
_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                           99.91 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.56 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.53 
_reflns_shell.d_res_low                                     2.6 
_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                             5348 
_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                                  0.314 
_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                                 9CZF 
_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                            2.53 
_refine.ls_d_res_low                             54.67 
_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                     72983 
_refine.ls_number_reflns_R_free                  3641 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2145 
_refine.ls_R_factor_R_free                       0.2452 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2129 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            0.2366 
_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                 26.50 
_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                            0.38 
_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                       2.53 
_refine_hist.d_res_low                        54.67 
_refine_hist.number_atoms_solvent             81 
_refine_hist.number_atoms_total               11854 
_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         339 
_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' ? 0.002  ? 12030 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.589  ? 16302 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.103 ? 4444  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.045  ? 1846  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003  ? 2093  ? 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' 2.53 2.56  . . 136 2626 100.00 . . . . 0.3356 . . . . . . . . . . . 0.3356 
'X-RAY DIFFRACTION' 2.56 2.60  . . 124 2648 100.00 . . . . 0.3278 . . . . . . . . . . . 0.3278 
'X-RAY DIFFRACTION' 2.60 2.64  . . 144 2587 100.00 . . . . 0.3287 . . . . . . . . . . . 0.3546 
'X-RAY DIFFRACTION' 2.64 2.67  . . 148 2623 100.00 . . . . 0.3311 . . . . . . . . . . . 0.3889 
'X-RAY DIFFRACTION' 2.67 2.72  . . 142 2646 100.00 . . . . 0.3398 . . . . . . . . . . . 0.3569 
'X-RAY DIFFRACTION' 2.72 2.76  . . 147 2610 100.00 . . . . 0.3192 . . . . . . . . . . . 0.3522 
'X-RAY DIFFRACTION' 2.76 2.81  . . 142 2654 100.00 . . . . 0.3147 . . . . . . . . . . . 0.3731 
'X-RAY DIFFRACTION' 2.81 2.86  . . 121 2639 100.00 . . . . 0.3057 . . . . . . . . . . . 0.3057 
'X-RAY DIFFRACTION' 2.86 2.91  . . 140 2671 100.00 . . . . 0.2648 . . . . . . . . . . . 0.2648 
'X-RAY DIFFRACTION' 2.91 2.97  . . 116 2654 100.00 . . . . 0.2812 . . . . . . . . . . . 0.2831 
'X-RAY DIFFRACTION' 2.97 3.04  . . 155 2655 100.00 . . . . 0.2782 . . . . . . . . . . . 0.3248 
'X-RAY DIFFRACTION' 3.04 3.11  . . 130 2646 100.00 . . . . 0.2707 . . . . . . . . . . . 0.2781 
'X-RAY DIFFRACTION' 3.11 3.19  . . 129 2661 100.00 . . . . 0.2680 . . . . . . . . . . . 0.2772 
'X-RAY DIFFRACTION' 3.19 3.27  . . 151 2631 100.00 . . . . 0.2699 . . . . . . . . . . . 0.2881 
'X-RAY DIFFRACTION' 3.27 3.37  . . 134 2661 100.00 . . . . 0.2595 . . . . . . . . . . . 0.2595 
'X-RAY DIFFRACTION' 3.37 3.48  . . 135 2671 100.00 . . . . 0.2462 . . . . . . . . . . . 0.2843 
'X-RAY DIFFRACTION' 3.48 3.60  . . 158 2632 100.00 . . . . 0.2295 . . . . . . . . . . . 0.2640 
'X-RAY DIFFRACTION' 3.60 3.75  . . 157 2652 100.00 . . . . 0.2211 . . . . . . . . . . . 0.2697 
'X-RAY DIFFRACTION' 3.75 3.92  . . 127 2690 100.00 . . . . 0.1926 . . . . . . . . . . . 0.2189 
'X-RAY DIFFRACTION' 3.92 4.12  . . 138 2669 100.00 . . . . 0.1819 . . . . . . . . . . . 0.2276 
'X-RAY DIFFRACTION' 4.12 4.38  . . 146 2675 100.00 . . . . 0.1617 . . . . . . . . . . . 0.1938 
'X-RAY DIFFRACTION' 4.38 4.72  . . 134 2712 100.00 . . . . 0.1480 . . . . . . . . . . . 0.2007 
'X-RAY DIFFRACTION' 4.72 5.20  . . 163 2660 100.00 . . . . 0.1478 . . . . . . . . . . . 0.1799 
'X-RAY DIFFRACTION' 5.20 5.95  . . 119 2754 100.00 . . . . 0.1764 . . . . . . . . . . . 0.2097 
'X-RAY DIFFRACTION' 5.95 7.49  . . 158 2754 100.00 . . . . 0.2027 . . . . . . . . . . . 0.2634 
'X-RAY DIFFRACTION' 7.49 54.67 . . 147 2861 99.00  . . . . 0.1880 . . . . . . . . . . . 0.2137 
# 
_struct.entry_id                     9CZF 
_struct.title                        'Crystal structure of integrin avb6 headpiece in complex with compound MORF-627' 
_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        9CZF 
_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 6  ? 
G  N N 7  ? 
H  N N 5  ? 
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 10 ? 
P  N N 10 ? 
Q  N N 10 ? 
R  N N 10 ? 
S  N N 11 ? 
T  N N 8  ? 
U  N N 8  ? 
V  N N 12 ? 
W  N N 10 ? 
X  N N 10 ? 
Y  N N 13 ? 
Z  N N 14 ? 
AA N N 15 ? 
BA N N 10 ? 
CA N N 10 ? 
DA N N 13 ? 
EA N N 16 ? 
FA N N 16 ? 
GA N N 16 ? 
# 
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 9CZF       9CZF   ? 3 ? 1  
4 PDB 9CZF       9CZF   ? 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 9CZF A 1 ? 595 ? P06756 31 ? 625 ? 1 595 
2 2 9CZF B 1 ? 470 ? P18564 22 ? 491 ? 5 474 
3 3 9CZF C 1 ? 214 ? 9CZF   1  ? 214 ? 1 214 
4 4 9CZF D 1 ? 218 ? 9CZF   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 9CZF CYS A 400 ? UNP P06756 MET 430 conflict         400 1  
1 9CZF GLY A 596 ? UNP P06756 ?   ?   'expression tag' 596 2  
1 9CZF GLY A 597 ? UNP P06756 ?   ?   'expression tag' 597 3  
1 9CZF SER A 598 ? UNP P06756 ?   ?   'expression tag' 598 4  
1 9CZF LEU A 599 ? UNP P06756 ?   ?   'expression tag' 599 5  
1 9CZF GLU A 600 ? UNP P06756 ?   ?   'expression tag' 600 6  
1 9CZF VAL A 601 ? UNP P06756 ?   ?   'expression tag' 601 7  
1 9CZF LEU A 602 ? UNP P06756 ?   ?   'expression tag' 602 8  
1 9CZF PHE A 603 ? UNP P06756 ?   ?   'expression tag' 603 9  
1 9CZF GLN A 604 ? UNP P06756 ?   ?   'expression tag' 604 10 
1 9CZF GLY A 605 ? UNP P06756 ?   ?   'expression tag' 605 11 
2 9CZF CYS B 266 ? UNP P18564 ILE 287 conflict         270 12 
2 9CZF SER B 471 ? UNP P18564 ?   ?   'expression tag' 475 13 
2 9CZF GLY B 472 ? UNP P18564 ?   ?   'expression tag' 476 14 
2 9CZF HIS B 473 ? UNP P18564 ?   ?   'expression tag' 477 15 
2 9CZF SER B 474 ? UNP P18564 ?   ?   'expression tag' 478 16 
2 9CZF LEU B 475 ? UNP P18564 ?   ?   'expression tag' 479 17 
2 9CZF GLU B 476 ? UNP P18564 ?   ?   'expression tag' 480 18 
2 9CZF VAL B 477 ? UNP P18564 ?   ?   'expression tag' 481 19 
2 9CZF LEU B 478 ? UNP P18564 ?   ?   'expression tag' 482 20 
2 9CZF PHE B 479 ? UNP P18564 ?   ?   'expression tag' 483 21 
2 9CZF GLN B 480 ? UNP P18564 ?   ?   'expression tag' 484 22 
2 9CZF 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,FA,GA 
# 
_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 ? GLU B 438 ? CYS B 437 GLU B 442 5 ? 6  
HELX_P HELX_P25 AC7 SER B 443 ? HIS B 447 ? SER B 447 HIS B 451 5 ? 5  
HELX_P HELX_P26 AC8 ASP C 79  ? ILE C 83  ? ASP C 79  ILE C 83  5 ? 5  
HELX_P HELX_P27 AC9 SER C 121 ? SER C 127 ? SER C 121 SER C 127 1 ? 7  
HELX_P HELX_P28 AD1 THR C 182 ? HIS C 189 ? THR C 182 HIS C 189 1 ? 8  
HELX_P HELX_P29 AD2 THR D 28  ? PHE D 32  ? THR D 28  PHE D 32  5 ? 5  
HELX_P HELX_P30 AD3 GLU D 62  ? ASP D 66  ? GLU D 62  ASP D 66  5 ? 5  
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 ? ? ? ? ? ? ? 2.036 ? ? 
disulf2  disulf ?    ? A CYS 108 SG  ? ? ? 1_555 A  CYS   128 SG  ? ? A CYS 108  A CYS   128  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf3  disulf ?    ? A CYS 142 SG  ? ? ? 1_555 A  CYS   155 SG  ? ? A CYS 142  A CYS   155  1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf4  disulf ?    ? A CYS 400 SG  ? ? ? 1_555 B  CYS   266 SG  ? ? A CYS 400  B CYS   270  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf5  disulf ?    ? A CYS 461 SG  ? ? ? 1_555 A  CYS   472 SG  ? ? A CYS 461  A CYS   472  1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf6  disulf ?    ? A CYS 478 SG  ? ? ? 1_555 A  CYS   535 SG  ? ? A CYS 478  A CYS   535  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf7  disulf ?    ? B CYS 2   SG  ? ? ? 1_555 B  CYS   20  SG  ? ? B CYS 6    B CYS   24   1_555 ? ? ? ? ? ? ? 2.026 ? ? 
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 ? ? ? ? ? ? ? 2.029 ? ? 
disulf10 disulf ?    ? B CYS 23  SG  ? ? ? 1_555 B  CYS   49  SG  ? ? B CYS 27   B CYS   53   1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf11 disulf ?    ? B CYS 176 SG  ? ? ? 1_555 B  CYS   183 SG  ? ? B CYS 180  B CYS   187  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf12 disulf ?    ? B CYS 231 SG  ? ? ? 1_555 B  CYS   272 SG  ? ? B CYS 235  B CYS   276  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf13 disulf ?    ? B CYS 373 SG  ? ? ? 1_555 B  CYS   385 SG  ? ? B CYS 377  B CYS   389  1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf14 disulf ?    ? B CYS 405 SG  ? ? ? 1_555 B  CYS   431 SG  ? ? B CYS 409  B CYS   435  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf15 disulf ?    ? B CYS 435 SG  ? ? ? 1_555 B  CYS   455 SG  ? ? B CYS 439  B CYS   459  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf16 disulf ?    ? B CYS 446 SG  ? ? ? 1_555 B  CYS   458 SG  ? ? B CYS 450  B CYS   462  1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf17 disulf ?    ? B CYS 460 SG  ? ? ? 1_555 B  CYS   469 SG  ? ? B CYS 464  B CYS   473  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf18 disulf ?    ? C CYS 23  SG  ? ? ? 1_555 C  CYS   88  SG  ? ? C CYS 23   C CYS   88   1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf19 disulf ?    ? C CYS 134 SG  ? ? ? 1_555 C  CYS   194 SG  ? ? C CYS 134  C CYS   194  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
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 ? ? ? ? ? ? ? 2.032 ? ? 
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 E  NAG   .   C1  ? ? A ASN 44   I NAG   1    1_555 ? ? ? ? ? ? ? 1.440 ? 
N-Glycosylation 
covale2  covale one  ? A ASN 260 ND2 ? ? ? 1_555 F  NAG   .   C1  ? ? A ASN 260  E NAG   1    1_555 ? ? ? ? ? ? ? 1.439 ? 
N-Glycosylation 
covale3  covale one  ? A ASN 266 ND2 ? ? ? 1_555 G  NAG   .   C1  ? ? A ASN 266  F NAG   1    1_555 ? ? ? ? ? ? ? 1.438 ? 
N-Glycosylation 
covale4  covale one  ? B ASN 239 ND2 ? ? ? 1_555 Z  NAG   .   C1  ? ? B ASN 243  B NAG   2008 1_555 ? ? ? ? ? ? ? 1.451 ? 
N-Glycosylation 
covale5  covale both ? E NAG .   O4  ? ? ? 1_555 E  NAG   .   C1  ? ? I NAG 1    I NAG   2    1_555 ? ? ? ? ? ? ? 1.436 ? ? 
covale6  covale both ? E NAG .   O4  ? ? ? 1_555 E  BMA   .   C1  ? ? I NAG 2    I BMA   3    1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale7  covale both ? F NAG .   O4  ? ? ? 1_555 F  NAG   .   C1  ? ? E NAG 1    E NAG   2    1_555 ? ? ? ? ? ? ? 1.446 ? ? 
covale8  covale both ? F NAG .   O4  ? ? ? 1_555 F  BMA   .   C1  ? ? E NAG 2    E BMA   3    1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale9  covale both ? F BMA .   O6  ? ? ? 1_555 F  MAN   .   C1  ? ? E BMA 3    E MAN   4    1_555 ? ? ? ? ? ? ? 1.447 ? ? 
covale10 covale both ? F MAN .   O3  ? ? ? 1_555 F  MAN   .   C1  ? ? E MAN 4    E MAN   5    1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale11 covale both ? F MAN .   O6  ? ? ? 1_555 F  MAN   .   C1  ? ? E MAN 4    E MAN   6    1_555 ? ? ? ? ? ? ? 1.441 ? ? 
covale12 covale both ? G NAG .   O4  ? ? ? 1_555 G  NAG   .   C1  ? ? F NAG 1    F NAG   2    1_555 ? ? ? ? ? ? ? 1.433 ? ? 
covale13 covale both ? G NAG .   O4  ? ? ? 1_555 G  BMA   .   C1  ? ? F NAG 2    F BMA   3    1_555 ? ? ? ? ? ? ? 1.441 ? ? 
covale14 covale both ? G BMA .   O3  ? ? ? 1_555 G  MAN   .   C1  ? ? F BMA 3    F MAN   4    1_555 ? ? ? ? ? ? ? 1.441 ? ? 
covale15 covale both ? H NAG .   O4  ? ? ? 1_555 H  NAG   .   C1  ? ? G NAG 1    G NAG   2    1_555 ? ? ? ? ? ? ? 1.443 ? ? 
covale16 covale both ? H NAG .   O4  ? ? ? 1_555 H  BMA   .   C1  ? ? G NAG 2    G BMA   3    1_555 ? ? ? ? ? ? ? 1.443 ? ? 
metalc1  metalc ?    ? A ASP 230 OD1 ? ? ? 1_555 I  CA    .   CA  ? ? A ASP 230  A CA    2001 1_555 ? ? ? ? ? ? ? 2.362 ? ? 
metalc2  metalc ?    ? A ASN 232 OD1 ? ? ? 1_555 I  CA    .   CA  ? ? A ASN 232  A CA    2001 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc3  metalc ?    ? A ASP 234 OD1 ? ? ? 1_555 I  CA    .   CA  ? ? A ASP 234  A CA    2001 1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc4  metalc ?    ? A ILE 236 O   ? ? ? 1_555 I  CA    .   CA  ? ? A ILE 236  A CA    2001 1_555 ? ? ? ? ? ? ? 2.239 ? ? 
metalc5  metalc ?    ? A ASP 238 OD1 ? ? ? 1_555 I  CA    .   CA  ? ? A ASP 238  A CA    2001 1_555 ? ? ? ? ? ? ? 2.387 ? ? 
metalc6  metalc ?    ? A ASP 238 OD2 ? ? ? 1_555 I  CA    .   CA  ? ? A ASP 238  A CA    2001 1_555 ? ? ? ? ? ? ? 2.417 ? ? 
metalc7  metalc ?    ? A ASP 284 OD1 ? ? ? 1_555 L  CA    .   CA  ? ? A ASP 284  A CA    2004 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc8  metalc ?    ? A ASN 286 OD1 ? ? ? 1_555 L  CA    .   CA  ? ? A ASN 286  A CA    2004 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc9  metalc ?    ? A ASP 288 OD1 ? ? ? 1_555 L  CA    .   CA  ? ? A ASP 288  A CA    2004 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc10 metalc ?    ? A TYR 290 O   ? ? ? 1_555 L  CA    .   CA  ? ? A TYR 290  A CA    2004 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc11 metalc ?    ? A ASP 292 OD1 ? ? ? 1_555 L  CA    .   CA  ? ? A ASP 292  A CA    2004 1_555 ? ? ? ? ? ? ? 2.355 ? ? 
metalc12 metalc ?    ? A ASP 292 OD2 ? ? ? 1_555 L  CA    .   CA  ? ? A ASP 292  A CA    2004 1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc13 metalc ?    ? A ASP 349 OD1 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 349  A CA    2002 1_555 ? ? ? ? ? ? ? 2.403 ? ? 
metalc14 metalc ?    ? A ASP 351 OD1 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 351  A CA    2002 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc15 metalc ?    ? A ASP 353 OD1 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 353  A CA    2002 1_555 ? ? ? ? ? ? ? 2.418 ? ? 
metalc16 metalc ?    ? A PHE 355 O   ? ? ? 1_555 J  CA    .   CA  ? ? A PHE 355  A CA    2002 1_555 ? ? ? ? ? ? ? 2.207 ? ? 
metalc17 metalc ?    ? A ASP 357 OD1 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 357  A CA    2002 1_555 ? ? ? ? ? ? ? 2.379 ? ? 
metalc18 metalc ?    ? A ASP 357 OD2 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 357  A CA    2002 1_555 ? ? ? ? ? ? ? 2.444 ? ? 
metalc19 metalc ?    ? A ASP 413 OD1 ? ? ? 1_555 K  CA    .   CA  ? ? A ASP 413  A CA    2003 1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc20 metalc ?    ? A ASP 415 OD1 ? ? ? 1_555 K  CA    .   CA  ? ? A ASP 415  A CA    2003 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc21 metalc ?    ? A ASN 417 OD1 ? ? ? 1_555 K  CA    .   CA  ? ? A ASN 417  A CA    2003 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc22 metalc ?    ? A TYR 419 O   ? ? ? 1_555 K  CA    .   CA  ? ? A TYR 419  A CA    2003 1_555 ? ? ? ? ? ? ? 2.253 ? ? 
metalc23 metalc ?    ? A ASP 421 OD1 ? ? ? 1_555 K  CA    .   CA  ? ? A ASP 421  A CA    2003 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc24 metalc ?    ? A ASP 421 OD2 ? ? ? 1_555 K  CA    .   CA  ? ? A ASP 421  A CA    2003 1_555 ? ? ? ? ? ? ? 2.405 ? ? 
metalc25 metalc ?    ? I CA  .   CA  ? ? ? 1_555 EA HOH   .   O   ? ? A CA  2001 A HOH   2106 1_555 ? ? ? ? ? ? ? 2.373 ? ? 
metalc26 metalc ?    ? J CA  .   CA  ? ? ? 1_555 EA HOH   .   O   ? ? A CA  2002 A HOH   2109 1_555 ? ? ? ? ? ? ? 2.468 ? ? 
metalc27 metalc ?    ? K CA  .   CA  ? ? ? 1_555 EA HOH   .   O   ? ? A CA  2003 A HOH   2108 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc28 metalc ?    ? L CA  .   CA  ? ? ? 1_555 EA HOH   .   O   ? ? A CA  2004 A HOH   2104 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc29 metalc ?    ? B SER 121 OG  ? ? ? 1_555 S  MG    .   MG  ? ? B SER 125  B MG    2001 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
metalc30 metalc ?    ? B SER 123 O   ? ? ? 1_555 U  CA    .   CA  ? ? B SER 127  B CA    2003 1_555 ? ? ? ? ? ? ? 2.440 ? ? 
metalc31 metalc ?    ? B ASP 126 OD1 ? ? ? 1_555 U  CA    .   CA  ? ? B ASP 130  B CA    2003 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc32 metalc ?    ? B ASP 126 OD2 ? ? ? 1_555 U  CA    .   CA  ? ? B ASP 130  B CA    2003 1_555 ? ? ? ? ? ? ? 2.446 ? ? 
metalc33 metalc ?    ? B ASP 127 OD1 ? ? ? 1_555 U  CA    .   CA  ? ? B ASP 131  B CA    2003 1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc34 metalc ?    ? B GLU 158 OE2 ? ? ? 1_555 T  CA    .   CA  ? ? B GLU 162  B CA    2002 1_555 ? ? ? ? ? ? ? 2.386 ? ? 
metalc35 metalc ?    ? B ASN 214 OD1 ? ? ? 1_555 T  CA    .   CA  ? ? B ASN 218  B CA    2002 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc36 metalc ?    ? B ASP 216 O   ? ? ? 1_555 T  CA    .   CA  ? ? B ASP 220  B CA    2002 1_555 ? ? ? ? ? ? ? 2.390 ? ? 
metalc37 metalc ?    ? B ASP 216 OD1 ? ? ? 1_555 T  CA    .   CA  ? ? B ASP 220  B CA    2002 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc38 metalc ?    ? B PRO 218 O   ? ? ? 1_555 T  CA    .   CA  ? ? B PRO 222  B CA    2002 1_555 ? ? ? ? ? ? ? 2.178 ? ? 
metalc39 metalc ?    ? B GLU 219 OE2 ? ? ? 1_555 S  MG    .   MG  ? ? B GLU 223  B MG    2001 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc40 metalc ?    ? B GLU 219 OE1 ? ? ? 1_555 T  CA    .   CA  ? ? B GLU 223  B CA    2002 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc41 metalc ?    ? B LYS 334 O   ? ? ? 1_555 U  CA    .   CA  ? ? B LYS 338  B CA    2003 1_555 ? ? ? ? ? ? ? 2.429 ? ? 
metalc42 metalc ?    ? S MG  .   MG  ? ? ? 1_555 V  A1A6I .   O01 ? ? B MG  2001 B A1A6I 2004 1_555 ? ? ? ? ? ? ? 2.215 ? ? 
metalc43 metalc ?    ? S MG  .   MG  ? ? ? 1_555 FA HOH   .   O   ? ? B MG  2001 B HOH   2105 1_555 ? ? ? ? ? ? ? 2.181 ? ? 
metalc44 metalc ?    ? S MG  .   MG  ? ? ? 1_555 FA HOH   .   O   ? ? B MG  2001 B HOH   2110 1_555 ? ? ? ? ? ? ? 2.196 ? ? 
metalc45 metalc ?    ? S MG  .   MG  ? ? ? 1_555 FA HOH   .   O   ? ? B MG  2001 B HOH   2119 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc46 metalc ?    ? U CA  .   CA  ? ? ? 1_555 FA HOH   .   O   ? ? B CA  2003 B HOH   2121 1_555 ? ? ? ? ? ? ? 2.461 ? ? 
metalc47 metalc ?    ? U CA  .   CA  ? ? ? 1_555 FA HOH   .   O   ? ? B CA  2003 B HOH   2129 1_555 ? ? ? ? ? ? ? 2.391 ? ? 
# 
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 79.0  ? 
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 78.3  ? 
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 76.8  ? 
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 75.7  ? 
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_555 154.3 ? 
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 93.5  ? 
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_555 128.5 ? 
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_555 108.2 ? 
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_555 153.1 ? 
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 91.3  ? 
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 79.1  ? 
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 78.6  ? 
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_555 149.2 ? 
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_555 100.8 ? 
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 54.3  ? 
16  OD1 ? A  ASP   230 ? A ASP   230  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? EA HOH   .   ? A HOH   2106 ? 1_555 153.1 ? 
17  OD1 ? A  ASN   232 ? A ASN   232  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? EA HOH   .   ? A HOH   2106 ? 1_555 92.9  ? 
18  OD1 ? A  ASP   234 ? A ASP   234  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? EA HOH   .   ? A HOH   2106 ? 1_555 74.9  ? 
19  O   ? A  ILE   236 ? A ILE   236  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? EA HOH   .   ? A HOH   2106 ? 1_555 107.6 ? 
20  OD1 ? A  ASP   238 ? A ASP   238  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? EA HOH   .   ? A HOH   2106 ? 1_555 78.4  ? 
21  OD2 ? A  ASP   238 ? A ASP   238  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? EA HOH   .   ? A HOH   2106 ? 1_555 124.8 ? 
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 75.5  ? 
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 72.3  ? 
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 82.9  ? 
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 88.7  ? 
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_555 164.1 ? 
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 90.8  ? 
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_555 137.6 ? 
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_555 113.7 ? 
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_555 147.2 ? 
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 79.2  ? 
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 91.5  ? 
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 76.6  ? 
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_555 156.6 ? 
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_555 105.9 ? 
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 54.5  ? 
37  OD1 ? A  ASP   284 ? A ASP   284  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? EA HOH   .   ? A HOH   2104 ? 1_555 150.4 ? 
38  OD1 ? A  ASN   286 ? A ASN   286  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? EA HOH   .   ? A HOH   2104 ? 1_555 96.4  ? 
39  OD1 ? A  ASP   288 ? A ASP   288  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? EA HOH   .   ? A HOH   2104 ? 1_555 78.5  ? 
40  O   ? A  TYR   290 ? A TYR   290  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? EA HOH   .   ? A HOH   2104 ? 1_555 96.7  ? 
41  OD1 ? A  ASP   292 ? A ASP   292  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? EA HOH   .   ? A HOH   2104 ? 1_555 71.8  ? 
42  OD2 ? A  ASP   292 ? A ASP   292  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? EA HOH   .   ? A HOH   2104 ? 1_555 114.6 ? 
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 86.3  ? 
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 74.3  ? 
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 89.2  ? 
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 73.6  ? 
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_555 159.8 ? 
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 87.3  ? 
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_555 136.8 ? 
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_555 107.3 ? 
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_555 144.1 ? 
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 86.8  ? 
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 95.0  ? 
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 72.1  ? 
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_555 159.2 ? 
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_555 107.1 ? 
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 54.0  ? 
58  OD1 ? A  ASP   349 ? A ASP   349  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? EA HOH   .   ? A HOH   2109 ? 1_555 149.2 ? 
59  OD1 ? A  ASP   351 ? A ASP   351  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? EA HOH   .   ? A HOH   2109 ? 1_555 101.9 ? 
60  OD1 ? A  ASP   353 ? A ASP   353  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? EA HOH   .   ? A HOH   2109 ? 1_555 76.1  ? 
61  O   ? A  PHE   355 ? A PHE   355  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? EA HOH   .   ? A HOH   2109 ? 1_555 96.6  ? 
62  OD1 ? A  ASP   357 ? A ASP   357  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? EA HOH   .   ? A HOH   2109 ? 1_555 69.4  ? 
63  OD2 ? A  ASP   357 ? A ASP   357  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? EA HOH   .   ? A HOH   2109 ? 1_555 115.8 ? 
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 69.3  ? 
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 74.9  ? 
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 76.1  ? 
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 80.1  ? 
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_555 147.4 ? 
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 85.5  ? 
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_555 145.8 ? 
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_555 122.7 ? 
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_555 136.8 ? 
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 89.0  ? 
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 98.5  ? 
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 86.8  ? 
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_555 162.9 ? 
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_555 109.2 ? 
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 54.6  ? 
79  OD1 ? A  ASP   413 ? A ASP   413  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? EA HOH   .   ? A HOH   2108 ? 1_555 138.6 ? 
80  OD1 ? A  ASP   415 ? A ASP   415  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? EA HOH   .   ? A HOH   2108 ? 1_555 74.7  ? 
81  OD1 ? A  ASN   417 ? A ASN   417  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? EA HOH   .   ? A HOH   2108 ? 1_555 77.2  ? 
82  O   ? A  TYR   419 ? A TYR   419  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? EA HOH   .   ? A HOH   2108 ? 1_555 127.4 ? 
83  OD1 ? A  ASP   421 ? A ASP   421  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? EA HOH   .   ? A HOH   2108 ? 1_555 72.5  ? 
84  OD2 ? A  ASP   421 ? A ASP   421  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? EA HOH   .   ? A HOH   2108 ? 1_555 99.3  ? 
85  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 97.8  ? 
86  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O01 ? V  A1A6I .   ? B A1A6I 2004 ? 1_555 110.1 ? 
87  OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O01 ? V  A1A6I .   ? B A1A6I 2004 ? 1_555 95.2  ? 
88  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2105 ? 1_555 79.1  ? 
89  OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2105 ? 1_555 101.0 ? 
90  O01 ? V  A1A6I .   ? B A1A6I 2004 ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2105 ? 1_555 160.2 ? 
91  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2110 ? 1_555 112.8 ? 
92  OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2110 ? 1_555 149.3 ? 
93  O01 ? V  A1A6I .   ? B A1A6I 2004 ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2110 ? 1_555 73.1  ? 
94  O   ? FA HOH   .   ? B HOH   2105 ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2110 ? 1_555 87.2  ? 
95  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2119 ? 1_555 166.1 ? 
96  OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2119 ? 1_555 80.5  ? 
97  O01 ? V  A1A6I .   ? B A1A6I 2004 ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2119 ? 1_555 83.9  ? 
98  O   ? FA HOH   .   ? B HOH   2105 ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2119 ? 1_555 87.6  ? 
99  O   ? FA HOH   .   ? B HOH   2110 ? 1_555 MG ? S MG . ? B MG 2001 ? 1_555 O   ? FA HOH   .   ? B HOH   2119 ? 1_555 70.3  ? 
100 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 78.3  ? 
101 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 130.3 ? 
102 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 54.4  ? 
103 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 93.8  ? 
104 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 78.3  ? 
105 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 91.0  ? 
106 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? B  LYS   334 ? B LYS   338  ? 1_555 159.2 ? 
107 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? B  LYS   334 ? B LYS   338  ? 1_555 119.1 ? 
108 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? B  LYS   334 ? B LYS   338  ? 1_555 70.0  ? 
109 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? B  LYS   334 ? B LYS   338  ? 1_555 79.9  ? 
110 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2121 ? 1_555 87.7  ? 
111 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2121 ? 1_555 162.1 ? 
112 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2121 ? 1_555 141.6 ? 
113 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2121 ? 1_555 91.7  ? 
114 O   ? B  LYS   334 ? B LYS   338  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2121 ? 1_555 72.8  ? 
115 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2129 ? 1_555 92.4  ? 
116 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2129 ? 1_555 99.1  ? 
117 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2129 ? 1_555 82.0  ? 
118 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2129 ? 1_555 172.7 ? 
119 O   ? B  LYS   334 ? B LYS   338  ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2129 ? 1_555 95.6  ? 
120 O   ? FA HOH   .   ? B HOH   2121 ? 1_555 CA ? U CA . ? B CA 2003 ? 1_555 O   ? FA HOH   .   ? B HOH   2129 ? 1_555 92.4  ? 
121 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 111.2 ? 
122 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 O   ? B  ASP   216 ? B ASP   220  ? 1_555 154.0 ? 
123 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 O   ? B  ASP   216 ? B ASP   220  ? 1_555 78.4  ? 
124 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 91.4  ? 
125 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 77.2  ? 
126 O   ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 66.5  ? 
127 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 O   ? B  PRO   218 ? B PRO   222  ? 1_555 74.5  ? 
128 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 O   ? B  PRO   218 ? B PRO   222  ? 1_555 174.3 ? 
129 O   ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 O   ? B  PRO   218 ? B PRO   222  ? 1_555 96.1  ? 
130 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 O   ? B  PRO   218 ? B PRO   222  ? 1_555 102.4 ? 
131 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 103.4 ? 
132 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 81.8  ? 
133 O   ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 101.9 ? 
134 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 157.6 ? 
135 O   ? B  PRO   218 ? B PRO   222  ? 1_555 CA ? T CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 97.7  ? 
# 
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 E .   ? ASN A 44  ? NAG I 1    ? 1_555 ASN A 44  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG F .   ? ASN A 260 ? NAG E 1    ? 1_555 ASN A 260 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG G .   ? ASN A 266 ? NAG F 1    ? 1_555 ASN A 266 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG Z .   ? ASN B 239 ? NAG B 2008 ? 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 -1.12 
2 ALA 84  B . ? ALA 88  B PRO 85  B ? PRO 89  B 1 -1.66 
3 SER 162 B . ? SER 166 B PRO 163 B ? PRO 167 B 1 2.72  
4 ILE 179 B . ? ILE 183 B PRO 180 B ? PRO 184 B 1 -3.16 
5 PHE 94  C . ? PHE 94  C PRO 95  C ? PRO 95  C 1 -1.52 
6 TYR 140 C . ? TYR 140 C PRO 141 C ? PRO 141 C 1 -0.55 
7 PHE 151 D . ? PHE 151 D PRO 152 D ? PRO 152 D 1 -4.10 
8 GLU 153 D . ? GLU 153 D PRO 154 D ? PRO 154 D 1 1.56  
9 TRP 193 D . ? TRP 193 D PRO 194 D ? PRO 194 D 1 2.10  
# 
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 ? 2 ? 
AB3 ? 5 ? 
AB4 ? 5 ? 
AB5 ? 2 ? 
AB6 ? 6 ? 
AB7 ? 5 ? 
AB8 ? 6 ? 
AB9 ? 2 ? 
AC1 ? 2 ? 
AC2 ? 4 ? 
AC3 ? 6 ? 
AC4 ? 4 ? 
AC5 ? 4 ? 
AC6 ? 3 ? 
AC7 ? 4 ? 
AC8 ? 6 ? 
AC9 ? 4 ? 
AD1 ? 4 ? 
AD2 ? 4 ? 
AD3 ? 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 
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 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? parallel      
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB6 5 6 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB7 4 5 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? parallel      
AB8 3 4 ? parallel      
AB8 4 5 ? parallel      
AB8 5 6 ? parallel      
AB9 1 2 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? parallel      
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC3 4 5 ? anti-parallel 
AC3 5 6 ? anti-parallel 
AC4 1 2 ? parallel      
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC7 3 4 ? anti-parallel 
AC8 1 2 ? parallel      
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC8 4 5 ? anti-parallel 
AC8 5 6 ? anti-parallel 
AC9 1 2 ? parallel      
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD1 2 3 ? anti-parallel 
AD1 3 4 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 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 SER A 407 ? THR A 412 ? SER A 407 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  ? SER A 100 ? VAL A 98  SER A 100 
AA5 2 ILE A 105 ? ALA A 109 ? ILE A 105 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 ? PHE A 376 ? ILE A 372 PHE A 376 
AB1 4 GLN A 389 ? GLU A 392 ? GLN A 389 GLU A 392 
AB2 1 GLY A 378 ? ARG A 379 ? GLY A 378 ARG A 379 
AB2 2 GLY A 382 ? LEU A 383 ? GLY A 382 LEU A 383 
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 PHE A 493 ? LEU A 499 ? PHE A 493 LEU A 499 
AB4 5 SER A 520 ? ASN A 524 ? SER A 520 ASN A 524 
AB5 1 LYS A 490 ? LEU A 491 ? LYS A 490 LEU A 491 
AB5 2 ILE A 527 ? SER A 528 ? ILE A 527 SER A 528 
AB6 1 GLN B 60  ? LYS B 65  ? GLN B 64  LYS B 69  
AB6 2 SER B 87  ? LEU B 92  ? SER B 91  LEU B 96  
AB6 3 LEU B 423 ? PRO B 429 ? LEU B 427 PRO B 433 
AB6 4 ARG B 410 ? PRO B 416 ? ARG B 414 PRO B 420 
AB6 5 VAL B 354 ? GLY B 360 ? VAL B 358 GLY B 364 
AB6 6 LYS B 384 ? CYS B 385 ? LYS B 388 CYS B 389 
AB7 1 ILE B 83  ? ALA B 84  ? ILE B 87  ALA B 88  
AB7 2 ALA B 97  ? ARG B 105 ? ALA B 101 ARG B 109 
AB7 3 THR B 393 ? ASN B 401 ? THR B 397 ASN B 405 
AB7 4 ASN B 366 ? CYS B 373 ? ASN B 370 CYS B 377 
AB7 5 LEU B 378 ? GLN B 380 ? LEU B 382 GLN B 384 
AB8 1 PHE B 189 ? THR B 196 ? PHE B 193 THR B 200 
AB8 2 PHE B 149 ? PHE B 156 ? PHE B 153 PHE B 160 
AB8 3 VAL B 112 ? ASP B 119 ? VAL B 116 ASP B 123 
AB8 4 LEU B 242 ? SER B 249 ? LEU B 246 SER B 253 
AB8 5 LEU B 304 ? THR B 310 ? LEU B 308 THR B 314 
AB8 6 THR B 328 ? LEU B 332 ? THR B 332 LEU B 336 
AB9 1 GLY B 451 ? PHE B 453 ? GLY B 455 PHE B 457 
AB9 2 CYS B 458 ? CYS B 460 ? CYS B 462 CYS B 464 
AC1 1 HIS B 464 ? MET B 465 ? HIS B 468 MET B 469 
AC1 2 SER B 471 ? GLY B 472 ? SER B 475 GLY B 476 
AC2 1 MET C 4   ? THR C 5   ? MET C 4   THR C 5   
AC2 2 VAL C 19  ? ALA C 25  ? VAL C 19  ALA C 25  
AC2 3 ASP C 70  ? ILE C 75  ? ASP C 70  ILE C 75  
AC2 4 PHE C 62  ? SER C 67  ? PHE C 62  SER C 67  
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 LEU C 33  ? GLN C 38  ? LEU C 33  GLN C 38  
AC3 5 VAL C 44  ? PHE C 49  ? VAL C 44  PHE C 49  
AC3 6 LYS C 53  ? LEU C 54  ? LYS C 53  LEU C 54  
AC4 1 SER C 10  ? ALA C 13  ? SER C 10  ALA C 13  
AC4 2 THR C 102 ? MET C 106 ? THR C 102 MET C 106 
AC4 3 THR C 85  ? GLN C 90  ? THR C 85  GLN C 90  
AC4 4 THR C 97  ? PHE C 98  ? THR C 97  PHE C 98  
AC5 1 THR C 114 ? PHE C 118 ? THR C 114 PHE C 118 
AC5 2 ALA C 130 ? PHE C 139 ? ALA C 130 PHE C 139 
AC5 3 TYR C 173 ? LEU C 181 ? TYR C 173 LEU C 181 
AC5 4 VAL C 159 ? TRP C 163 ? VAL C 159 TRP C 163 
AC6 1 ASN C 145 ? LYS C 149 ? ASN C 145 LYS C 149 
AC6 2 SER C 191 ? THR C 197 ? SER C 191 THR C 197 
AC6 3 ILE C 205 ? ASN C 210 ? ILE C 205 ASN C 210 
AC7 1 GLN D 3   ? GLN D 6   ? GLN D 3   GLN D 6   
AC7 2 VAL D 18  ? SER D 25  ? VAL D 18  SER D 25  
AC7 3 THR D 78  ? LEU D 83  ? THR D 78  LEU D 83  
AC7 4 ALA D 68  ? ASP D 73  ? ALA D 68  ASP D 73  
AC8 1 GLU D 10  ? ALA D 12  ? GLU D 10  ALA D 12  
AC8 2 THR D 112 ? VAL D 116 ? THR D 112 VAL D 116 
AC8 3 ALA D 92  ? GLY D 101 ? ALA D 92  GLY D 101 
AC8 4 MET D 34  ? GLN D 39  ? MET D 34  GLN D 39  
AC8 5 LEU D 45  ? ILE D 51  ? LEU D 45  ILE D 51  
AC8 6 THR D 58  ? CYS D 60  ? THR D 58  CYS D 60  
AC9 1 GLU D 10  ? ALA D 12  ? GLU D 10  ALA D 12  
AC9 2 THR D 112 ? VAL D 116 ? THR D 112 VAL D 116 
AC9 3 ALA D 92  ? GLY D 101 ? ALA D 92  GLY D 101 
AC9 4 ALA D 104 ? TRP D 108 ? ALA D 104 TRP D 108 
AD1 1 SER D 125 ? LEU D 129 ? SER D 125 LEU D 129 
AD1 2 SER D 140 ? TYR D 150 ? SER D 140 TYR D 150 
AD1 3 LEU D 179 ? VAL D 189 ? LEU D 179 VAL D 189 
AD1 4 VAL D 168 ? THR D 170 ? VAL D 168 THR D 170 
AD2 1 SER D 125 ? LEU D 129 ? SER D 125 LEU D 129 
AD2 2 SER D 140 ? TYR D 150 ? SER D 140 TYR D 150 
AD2 3 LEU D 179 ? VAL D 189 ? LEU D 179 VAL D 189 
AD2 4 VAL D 174 ? GLN D 176 ? VAL D 174 GLN D 176 
AD3 1 THR D 156 ? TRP D 159 ? THR D 156 TRP D 159 
AD3 2 THR D 199 ? HIS D 204 ? THR D 199 HIS D 204 
AD3 3 THR D 209 ? LYS D 214 ? THR D 209 LYS D 214 
# 
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 ALA A 9   ? N ALA A 9   O LEU A 434 ? O LEU A 434 
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 VAL A 38  ? N VAL A 38  O LEU A 57  ? O LEU A 57  
AA2 3 4 N LYS A 58  ? N LYS A 58  O GLN A 68  ? O GLN A 68  
AA3 1 2 N ALA A 81  ? N ALA A 81  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 LEU A 130 ? N LEU A 130 O VAL A 137 ? O VAL A 137 
AA6 1 2 N ASP A 162 ? N ASP A 162 O LEU A 170 ? O LEU A 170 
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 360 ? N ILE A 360 O TYR A 374 ? O TYR A 374 
AB1 3 4 N VAL A 373 ? N VAL A 373 O LEU A 391 ? O LEU A 391 
AB2 1 2 N ARG A 379 ? N ARG A 379 O GLY A 382 ? O GLY A 382 
AB3 1 2 N LEU A 512 ? N LEU A 512 O TYR A 541 ? O TYR A 541 
AB3 2 3 O ALA A 540 ? O ALA A 540 N PHE A 473 ? N PHE A 473 
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 ARG A 562 ? O ARG A 562 N GLN A 494 ? N GLN A 494 
AB4 4 5 N VAL A 495 ? N VAL A 495 O LYS A 523 ? O LYS A 523 
AB5 1 2 N LEU A 491 ? N LEU A 491 O ILE A 527 ? O ILE A 527 
AB6 1 2 N GLU B 62  ? N GLU B 66  O ILE B 89  ? O ILE B 93  
AB6 2 3 N LEU B 90  ? N LEU B 94  O LEU B 426 ? O LEU B 430 
AB6 3 4 O LEU B 425 ? O LEU B 429 N ILE B 412 ? N ILE B 416 
AB6 4 5 O ILE B 413 ? O ILE B 417 N LEU B 359 ? N LEU B 363 
AB6 5 6 N VAL B 354 ? N VAL B 358 O CYS B 385 ? O CYS B 389 
AB7 1 2 N ALA B 84  ? N ALA B 88  O HIS B 103 ? O HIS B 107 
AB7 2 3 N LEU B 100 ? N LEU B 104 O VAL B 398 ? O VAL B 402 
AB7 3 4 O SER B 397 ? O SER B 401 N THR B 370 ? N THR B 374 
AB7 4 5 N ALA B 371 ? N ALA B 375 O GLN B 380 ? O GLN B 384 
AB8 1 2 O LYS B 190 ? O LYS B 194 N SER B 155 ? N SER B 159 
AB8 2 3 O GLY B 152 ? O GLY B 156 N TYR B 116 ? N TYR B 120 
AB8 3 4 N ASP B 119 ? N ASP B 123 O VAL B 248 ? O VAL B 252 
AB8 4 5 N PHE B 247 ? N PHE B 251 O ALA B 308 ? O ALA B 312 
AB8 5 6 N PHE B 307 ? N PHE B 311 O GLY B 330 ? O GLY B 334 
AB9 1 2 N SER B 452 ? N SER B 456 O ALA B 459 ? O ALA B 463 
AC1 1 2 N MET B 465 ? N MET B 469 O SER B 471 ? O SER B 475 
AC2 1 2 N THR C 5   ? N THR C 5   O ARG C 24  ? O ARG C 24  
AC2 2 3 N VAL C 19  ? N VAL C 19  O ILE C 75  ? O ILE C 75  
AC2 3 4 O THR C 74  ? O THR C 74  N SER C 63  ? N SER C 63  
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 O THR C 85  ? O THR C 85  N GLN C 38  ? N GLN C 38  
AC3 4 5 N TRP C 35  ? N TRP C 35  O LEU C 47  ? O LEU C 47  
AC3 5 6 N PHE C 49  ? N PHE C 49  O LYS C 53  ? O LYS C 53  
AC4 1 2 N LEU C 11  ? N LEU C 11  O LYS C 103 ? O LYS C 103 
AC4 2 3 O THR C 102 ? O THR C 102 N TYR C 86  ? N TYR C 86  
AC4 3 4 N GLN C 90  ? N GLN C 90  O THR C 97  ? O THR C 97  
AC5 1 2 N SER C 116 ? N SER C 116 O PHE C 135 ? O PHE C 135 
AC5 2 3 N CYS C 134 ? N CYS C 134 O SER C 177 ? O SER C 177 
AC5 3 4 O SER C 176 ? O SER C 176 N SER C 162 ? N SER C 162 
AC6 1 2 N LYS C 147 ? N LYS C 147 O GLU C 195 ? O GLU C 195 
AC6 2 3 N CYS C 194 ? N CYS C 194 O LYS C 207 ? O LYS C 207 
AC7 1 2 N GLN D 5   ? N GLN D 5   O LYS D 23  ? O LYS D 23  
AC7 2 3 N CYS D 22  ? N CYS D 22  O ALA D 79  ? O ALA D 79  
AC7 3 4 O THR D 78  ? O THR D 78  N ASP D 73  ? N ASP D 73  
AC8 1 2 N GLU D 10  ? N GLU D 10  O SER D 113 ? O SER D 113 
AC8 2 3 O VAL D 114 ? O VAL D 114 N ALA D 92  ? N ALA D 92  
AC8 3 4 O ALA D 97  ? O ALA D 97  N HIS D 35  ? N HIS D 35  
AC8 4 5 N LYS D 38  ? N LYS D 38  O GLU D 46  ? O GLU D 46  
AC8 5 6 N TYR D 50  ? N TYR D 50  O GLU D 59  ? O GLU D 59  
AC9 1 2 N GLU D 10  ? N GLU D 10  O SER D 113 ? O SER D 113 
AC9 2 3 O VAL D 114 ? O VAL D 114 N ALA D 92  ? N ALA D 92  
AC9 3 4 N SER D 98  ? N SER D 98  O TYR D 107 ? O TYR D 107 
AD1 1 2 N TYR D 127 ? N TYR D 127 O LEU D 146 ? O LEU D 146 
AD1 2 3 N VAL D 147 ? N VAL D 147 O LEU D 182 ? O LEU D 182 
AD1 3 4 O SER D 185 ? O SER D 185 N HIS D 169 ? N HIS D 169 
AD2 1 2 N TYR D 127 ? N TYR D 127 O LEU D 146 ? O LEU D 146 
AD2 2 3 N VAL D 147 ? N VAL D 147 O LEU D 182 ? O LEU D 182 
AD2 3 4 O LEU D 179 ? O LEU D 179 N GLN D 176 ? N GLN D 176 
AD3 1 2 N THR D 158 ? N THR D 158 O ASN D 201 ? O ASN D 201 
AD3 2 3 N CYS D 200 ? N CYS D 200 O LYS D 213 ? O LYS D 213 
# 
_pdbx_entry_details.entry_id                   9CZF 
_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 HZ3 B LYS 388 ? ? O3 B GOL 2005 ? ? 1.57 
2 1 OD1 A ASN 377 ? ? HG A SER 388  ? ? 1.58 
# 
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 ALA A 30  ? ? -141.06 21.21   
2  1 SER A 62  ? ? 69.18   -5.32   
3  1 ARG A 115 ? ? -73.20  -80.88  
4  1 THR A 116 ? ? 157.23  -176.96 
5  1 ASP A 132 ? ? -95.38  -64.77  
6  1 ASP A 148 ? ? 150.69  -169.93 
7  1 LYS A 469 ? ? 62.26   71.15   
8  1 ALA A 568 ? ? -95.94  31.19   
9  1 GLN B 29  ? ? 79.03   -6.19   
10 1 PRO B 89  ? ? -69.57  -178.78 
11 1 VAL B 161 ? ? -125.94 -65.25  
12 1 SER B 216 ? ? -118.34 -169.94 
13 1 ASN B 378 ? ? 53.52   85.22   
14 1 ASN B 379 ? ? -20.92  -66.24  
15 1 HIS B 451 ? ? 61.03   64.38   
16 1 THR C 51  ? ? 74.21   -17.63  
17 1 PRO C 141 ? ? -71.92  -163.43 
18 1 ILE C 150 ? ? -91.03  -63.45  
19 1 ALA D 16  ? ? -79.55  -168.27 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 LYS A 101 ? ? GLN A 102 ? ? -141.82 
2 1 ILE A 147 ? ? ASP A 148 ? ? 140.57  
3 1 ASN B 378 ? ? ASN B 379 ? ? -136.21 
# 
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 12.8838 -33.6233 9.7052   0.4355 ? 0.0797  ? 0.1170  ? 0.5253 ? -0.0077 ? 0.5032 ? 2.3601 ? 
0.6461  ? 1.6641  ? 0.9652 ? 0.3644  ? 2.5956 ? 0.0873  ? -0.4766 ? 0.0220  ? 0.2507  ? -0.1223 ? 0.0719  ? 0.1030  ? -0.3542 ? 
0.0548  ? 
2  'X-RAY DIFFRACTION' ? refined 8.3319  -35.6155 -2.2883  0.3920 ? 0.0220  ? 0.0072  ? 0.4806 ? 0.0059  ? 0.4498 ? 1.6688 ? 
0.0245  ? 0.1061  ? 2.1825 ? -0.6444 ? 3.7000 ? -0.0169 ? -0.2208 ? 0.0558  ? 0.1931  ? 0.0073  ? 0.2060  ? -0.0209 ? -0.2034 ? 
0.0104  ? 
3  'X-RAY DIFFRACTION' ? refined 27.0856 -31.2569 15.2002  0.4979 ? 0.1275  ? 0.1190  ? 0.6869 ? 0.0191  ? 0.5392 ? 6.0861 ? 
7.0485  ? 2.0723  ? 8.8153 ? 2.1737  ? 1.2047 ? 0.1641  ? -0.2484 ? -0.4108 ? 0.0186  ? 0.0252  ? -0.6242 ? 0.0707  ? 0.0093  ? 
-0.2106 ? 
4  'X-RAY DIFFRACTION' ? refined 27.1927 -8.2073  20.3658  0.7810 ? 0.1556  ? 0.0334  ? 0.8021 ? -0.0448 ? 0.8424 ? 3.2135 ? 
2.6233  ? -0.3344 ? 2.3658 ? 0.3402  ? 1.7466 ? 0.0853  ? -0.2187 ? 0.8716  ? 0.0252  ? -0.3640 ? 0.6742  ? -0.3632 ? -0.1129 ? 
0.2105  ? 
5  'X-RAY DIFFRACTION' ? refined 43.0986 19.7907  18.6992  1.2326 ? 0.0260  ? -0.1972 ? 0.8947 ? -0.1606 ? 1.3573 ? 4.2564 ? 
-1.1214 ? -1.2785 ? 5.4503 ? -2.4499 ? 1.9480 ? 0.4665  ? -0.0087 ? 0.2043  ? 0.4283  ? -0.1510 ? -0.2925 ? -0.2977 ? -0.1467 ? 
-0.3372 ? 
6  'X-RAY DIFFRACTION' ? refined -4.8477 -47.0766 -67.9354 0.8090 ? 0.0740  ? -0.2809 ? 0.7558 ? -0.1069 ? 0.7580 ? 6.0236 ? 
1.9343  ? -4.5726 ? 4.5630 ? -2.4849 ? 6.9509 ? 0.4554  ? 0.8348  ? 0.1325  ? -0.7378 ? -0.2332 ? 0.9288  ? 0.1658  ? -1.2761 ? 
-0.2033 ? 
7  'X-RAY DIFFRACTION' ? refined -0.5326 -42.6547 -60.6806 0.5922 ? 0.0567  ? -0.1640 ? 0.6036 ? -0.0544 ? 0.5845 ? 2.2429 ? 
-1.2766 ? -0.7794 ? 3.6178 ? 0.7718  ? 8.7222 ? -0.0513 ? 0.4086  ? -0.0089 ? -0.3933 ? -0.3616 ? 0.2760  ? -0.2323 ? -0.6220 ? 
0.3863  ? 
8  'X-RAY DIFFRACTION' ? refined 1.6818  -49.7472 -83.1741 1.1901 ? 0.3194  ? -0.2160 ? 0.7812 ? -0.1020 ? 0.5815 ? 1.8006 ? 
-2.7534 ? -2.9123 ? 4.2185 ? 4.5035  ? 4.7976 ? 1.0155  ? 1.0180  ? -0.4274 ? -1.5312 ? -1.5934 ? 0.6963  ? -1.2406 ? -1.5422 ? 
0.5338  ? 
9  'X-RAY DIFFRACTION' ? refined 8.2284  -71.7446 -85.5013 0.7906 ? 0.0796  ? -0.1293 ? 0.8326 ? -0.1888 ? 0.7881 ? 6.7063 ? 
-4.3198 ? 0.4422  ? 3.3150 ? -1.5030 ? 3.2949 ? 0.2982  ? 0.6214  ? -0.7855 ? -0.7632 ? -0.4722 ? 1.0789  ? 0.3914  ? -0.7753 ? 
0.1985  ? 
10 'X-RAY DIFFRACTION' ? refined 8.4524  -70.3385 -83.8887 0.7238 ? 0.1077  ? -0.1652 ? 0.8332 ? -0.1190 ? 0.7269 ? 6.0705 ? 
-4.2430 ? -0.0962 ? 3.0557 ? 0.7150  ? 3.3465 ? 0.2833  ? 0.7566  ? -1.1297 ? -1.2246 ? -0.4888 ? 2.0080  ? 0.1731  ? -0.1590 ? 
0.1893  ? 
11 'X-RAY DIFFRACTION' ? refined 4.5531  -70.6688 -94.5382 0.9085 ? 0.0918  ? -0.2566 ? 1.1022 ? -0.3755 ? 1.0192 ? 2.4091 ? 
0.9291  ? 2.7339  ? 6.1433 ? -0.4905 ? 8.5596 ? 0.9769  ? 1.2751  ? -1.6560 ? -2.1583 ? -1.2838 ? 1.6743  ? 0.2570  ? -1.0098 ? 
0.2663  ? 
12 'X-RAY DIFFRACTION' ? refined 17.9117 -52.8104 -50.2034 0.5895 ? 0.1618  ? -0.0911 ? 0.5375 ? 0.0134  ? 0.4356 ? 2.7648 ? 
-1.2566 ? -0.9365 ? 7.8286 ? 4.7451  ? 5.0112 ? -0.1926 ? -0.1145 ? -0.2278 ? 0.1594  ? 0.3603  ? -0.3080 ? 0.6569  ? 0.6506  ? 
-0.2008 ? 
13 'X-RAY DIFFRACTION' ? refined 7.2363  -56.1499 -47.0841 0.9047 ? 0.0533  ? -0.0200 ? 0.5370 ? -0.0446 ? 0.6424 ? 5.2557 ? 
0.1976  ? 2.2605  ? 2.5639 ? -2.1456 ? 8.4922 ? 0.1776  ? -0.0387 ? -0.5751 ? 0.3256  ? 0.0541  ? 0.3899  ? 1.3601  ? -0.2712 ? 
-0.3706 ? 
14 'X-RAY DIFFRACTION' ? refined 13.6739 -57.5700 -53.6050 0.6664 ? 0.0797  ? -0.0907 ? 0.5323 ? 0.0225  ? 0.4765 ? 1.8440 ? 
-1.4235 ? -1.5370 ? 5.6881 ? 4.1658  ? 4.3480 ? -0.0255 ? -0.0986 ? -0.1842 ? 0.4054  ? -0.0447 ? -0.1769 ? 0.8431  ? 0.2488  ? 
0.0766  ? 
15 'X-RAY DIFFRACTION' ? refined 21.7397 -66.1424 -82.7286 0.5380 ? 0.0932  ? -0.0118 ? 0.6824 ? 0.0033  ? 0.5632 ? 7.5227 ? 
-1.0534 ? 0.0904  ? 8.0091 ? -3.7569 ? 4.3818 ? 0.0410  ? 1.1235  ? 0.2856  ? -0.2544 ? -0.4934 ? -0.5736 ? -0.0294 ? 0.6807  ? 
0.3895  ? 
16 'X-RAY DIFFRACTION' ? refined 22.9119 -66.3327 -82.1403 0.6144 ? 0.0830  ? -0.0003 ? 0.4589 ? -0.0111 ? 0.5868 ? 9.2942 ? 
-2.9798 ? -0.1625 ? 7.3771 ? -0.2003 ? 5.8760 ? 0.0460  ? 0.8347  ? 0.0387  ? -0.4806 ? -0.3557 ? -0.5281 ? -0.1094 ? 0.2379  ? 
0.3371  ? 
17 'X-RAY DIFFRACTION' ? refined 14.3118 -24.0640 -33.3315 0.4567 ? 0.0019  ? -0.0817 ? 0.4823 ? 0.0743  ? 0.4592 ? 1.7437 ? 
0.0853  ? 0.5346  ? 1.3061 ? 0.2783  ? 2.1485 ? -0.0995 ? 0.2326  ? 0.2780  ? -0.1864 ? -0.0710 ? 0.0619  ? -0.2862 ? 0.0662  ? 
0.1666  ? 
18 'X-RAY DIFFRACTION' ? refined 30.4353 -9.1213  -17.6052 0.5464 ? -0.0802 ? -0.1646 ? 0.5422 ? 0.1187  ? 0.5590 ? 1.3953 ? 
-0.0089 ? -0.0729 ? 1.7983 ? 0.4902  ? 0.3826 ? -0.0726 ? 0.0032  ? 0.3342  ? 0.0311  ? 0.0167  ? -0.1759 ? -0.2625 ? 0.1737  ? 
0.0509  ? 
19 'X-RAY DIFFRACTION' ? refined 47.4787 18.0704  -9.9313  0.8075 ? 0.0086  ? -0.1104 ? 0.7067 ? -0.0868 ? 1.1679 ? 4.4984 ? 
0.6541  ? 1.8219  ? 3.6899 ? 0.4931  ? 4.0945 ? -0.6227 ? -0.3012 ? 1.3271  ? -0.2772 ? 0.3887  ? 0.1337  ? -0.8955 ? -0.2805 ? 
0.2474  ? 
20 'X-RAY DIFFRACTION' ? refined 47.5044 0.8095   21.1945  0.9515 ? 0.0216  ? -0.1868 ? 0.7568 ? 0.2119  ? 1.4587 ? 8.4484 ? 
6.9586  ? 0.2504  ? 9.4777 ? 4.4229  ? 5.2142 ? -0.0269 ? -0.2123 ? -1.3221 ? 0.4853  ? -0.1066 ? -2.4203 ? -0.0727 ? 0.8792  ? 
0.1533  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 51 through 192 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 193 through 342 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 343 through 413 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 414 through 447 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 448 through 477 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 1 through 18 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 19 through 102 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 103 through 113 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 114 through 158 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 159 through 197 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 198 through 214 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 1 through 33 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 34 through 73 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 74 through 124 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 125 through 167 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 168 through 217 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 275 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 276 through 460 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 461 through 595 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 5 through 50 )
;
# 
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 
A1A6I C13  C  N N 1   
A1A6I C14  C  N N 2   
A1A6I C15  C  Y N 3   
A1A6I C19  C  N N 4   
A1A6I C20  C  N N 5   
A1A6I C21  C  N N 6   
A1A6I C23  C  Y N 7   
A1A6I C24  C  Y N 8   
A1A6I C25  C  Y N 9   
A1A6I C26  C  Y N 10  
A1A6I C27  C  Y N 11  
A1A6I C02  C  N N 12  
A1A6I C04  C  N S 13  
A1A6I C06  C  N N 14  
A1A6I C07  C  N N 15  
A1A6I C08  C  N R 16  
A1A6I C09  C  N N 17  
A1A6I C11  C  N N 18  
A1A6I C12  C  N N 19  
A1A6I C17  C  Y N 20  
A1A6I C18  C  Y N 21  
A1A6I C29  C  Y N 22  
A1A6I C30  C  Y N 23  
A1A6I C31  C  Y N 24  
A1A6I C32  C  N S 25  
A1A6I C33  C  N N 26  
A1A6I C34  C  N N 27  
A1A6I C35  C  N N 28  
A1A6I C36  C  N N 29  
A1A6I C37  C  N N 30  
A1A6I C38  C  N N 31  
A1A6I F28  F  N N 32  
A1A6I N05  N  N N 33  
A1A6I N16  N  Y N 34  
A1A6I N22  N  N N 35  
A1A6I O01  O  N N 36  
A1A6I O03  O  N N 37  
A1A6I O10  O  N N 38  
A1A6I O39  O  N N 39  
A1A6I H1   H  N N 40  
A1A6I H2   H  N N 41  
A1A6I H3   H  N N 42  
A1A6I H4   H  N N 43  
A1A6I H5   H  N N 44  
A1A6I H6   H  N N 45  
A1A6I H7   H  N N 46  
A1A6I H8   H  N N 47  
A1A6I H9   H  N N 48  
A1A6I H10  H  N N 49  
A1A6I H11  H  N N 50  
A1A6I H12  H  N N 51  
A1A6I H13  H  N N 52  
A1A6I H14  H  N N 53  
A1A6I H15  H  N N 54  
A1A6I H16  H  N N 55  
A1A6I H17  H  N N 56  
A1A6I H18  H  N N 57  
A1A6I H19  H  N N 58  
A1A6I H20  H  N N 59  
A1A6I H21  H  N N 60  
A1A6I H22  H  N N 61  
A1A6I H23  H  N N 62  
A1A6I H24  H  N N 63  
A1A6I H25  H  N N 64  
A1A6I H26  H  N N 65  
A1A6I H27  H  N N 66  
A1A6I H28  H  N N 67  
A1A6I H29  H  N N 68  
A1A6I H30  H  N N 69  
A1A6I H31  H  N N 70  
A1A6I H32  H  N N 71  
A1A6I H33  H  N N 72  
A1A6I H34  H  N N 73  
A1A6I H35  H  N N 74  
A1A6I H36  H  N N 75  
A1A6I H37  H  N N 76  
A1A6I H38  H  N N 77  
A1A6I H40  H  N N 78  
A1A6I H41  H  N N 79  
ACT   C    C  N N 80  
ACT   O    O  N N 81  
ACT   OXT  O  N N 82  
ACT   CH3  C  N N 83  
ACT   H1   H  N N 84  
ACT   H2   H  N N 85  
ACT   H3   H  N N 86  
ALA   N    N  N N 87  
ALA   CA   C  N S 88  
ALA   C    C  N N 89  
ALA   O    O  N N 90  
ALA   CB   C  N N 91  
ALA   OXT  O  N N 92  
ALA   H    H  N N 93  
ALA   H2   H  N N 94  
ALA   HA   H  N N 95  
ALA   HB1  H  N N 96  
ALA   HB2  H  N N 97  
ALA   HB3  H  N N 98  
ALA   HXT  H  N N 99  
ARG   N    N  N N 100 
ARG   CA   C  N S 101 
ARG   C    C  N N 102 
ARG   O    O  N N 103 
ARG   CB   C  N N 104 
ARG   CG   C  N N 105 
ARG   CD   C  N N 106 
ARG   NE   N  N N 107 
ARG   CZ   C  N N 108 
ARG   NH1  N  N N 109 
ARG   NH2  N  N N 110 
ARG   OXT  O  N N 111 
ARG   H    H  N N 112 
ARG   H2   H  N N 113 
ARG   HA   H  N N 114 
ARG   HB2  H  N N 115 
ARG   HB3  H  N N 116 
ARG   HG2  H  N N 117 
ARG   HG3  H  N N 118 
ARG   HD2  H  N N 119 
ARG   HD3  H  N N 120 
ARG   HE   H  N N 121 
ARG   HH11 H  N N 122 
ARG   HH12 H  N N 123 
ARG   HH21 H  N N 124 
ARG   HH22 H  N N 125 
ARG   HXT  H  N N 126 
ASN   N    N  N N 127 
ASN   CA   C  N S 128 
ASN   C    C  N N 129 
ASN   O    O  N N 130 
ASN   CB   C  N N 131 
ASN   CG   C  N N 132 
ASN   OD1  O  N N 133 
ASN   ND2  N  N N 134 
ASN   OXT  O  N N 135 
ASN   H    H  N N 136 
ASN   H2   H  N N 137 
ASN   HA   H  N N 138 
ASN   HB2  H  N N 139 
ASN   HB3  H  N N 140 
ASN   HD21 H  N N 141 
ASN   HD22 H  N N 142 
ASN   HXT  H  N N 143 
ASP   N    N  N N 144 
ASP   CA   C  N S 145 
ASP   C    C  N N 146 
ASP   O    O  N N 147 
ASP   CB   C  N N 148 
ASP   CG   C  N N 149 
ASP   OD1  O  N N 150 
ASP   OD2  O  N N 151 
ASP   OXT  O  N N 152 
ASP   H    H  N N 153 
ASP   H2   H  N N 154 
ASP   HA   H  N N 155 
ASP   HB2  H  N N 156 
ASP   HB3  H  N N 157 
ASP   HD2  H  N N 158 
ASP   HXT  H  N N 159 
BMA   C1   C  N R 160 
BMA   C2   C  N S 161 
BMA   C3   C  N S 162 
BMA   C4   C  N S 163 
BMA   C5   C  N R 164 
BMA   C6   C  N N 165 
BMA   O1   O  N N 166 
BMA   O2   O  N N 167 
BMA   O3   O  N N 168 
BMA   O4   O  N N 169 
BMA   O5   O  N N 170 
BMA   O6   O  N N 171 
BMA   H1   H  N N 172 
BMA   H2   H  N N 173 
BMA   H3   H  N N 174 
BMA   H4   H  N N 175 
BMA   H5   H  N N 176 
BMA   H61  H  N N 177 
BMA   H62  H  N N 178 
BMA   HO1  H  N N 179 
BMA   HO2  H  N N 180 
BMA   HO3  H  N N 181 
BMA   HO4  H  N N 182 
BMA   HO6  H  N N 183 
CA    CA   CA N N 184 
CL    CL   CL N N 185 
CYS   N    N  N N 186 
CYS   CA   C  N R 187 
CYS   C    C  N N 188 
CYS   O    O  N N 189 
CYS   CB   C  N N 190 
CYS   SG   S  N N 191 
CYS   OXT  O  N N 192 
CYS   H    H  N N 193 
CYS   H2   H  N N 194 
CYS   HA   H  N N 195 
CYS   HB2  H  N N 196 
CYS   HB3  H  N N 197 
CYS   HG   H  N N 198 
CYS   HXT  H  N N 199 
GLN   N    N  N N 200 
GLN   CA   C  N S 201 
GLN   C    C  N N 202 
GLN   O    O  N N 203 
GLN   CB   C  N N 204 
GLN   CG   C  N N 205 
GLN   CD   C  N N 206 
GLN   OE1  O  N N 207 
GLN   NE2  N  N N 208 
GLN   OXT  O  N N 209 
GLN   H    H  N N 210 
GLN   H2   H  N N 211 
GLN   HA   H  N N 212 
GLN   HB2  H  N N 213 
GLN   HB3  H  N N 214 
GLN   HG2  H  N N 215 
GLN   HG3  H  N N 216 
GLN   HE21 H  N N 217 
GLN   HE22 H  N N 218 
GLN   HXT  H  N N 219 
GLU   N    N  N N 220 
GLU   CA   C  N S 221 
GLU   C    C  N N 222 
GLU   O    O  N N 223 
GLU   CB   C  N N 224 
GLU   CG   C  N N 225 
GLU   CD   C  N N 226 
GLU   OE1  O  N N 227 
GLU   OE2  O  N N 228 
GLU   OXT  O  N N 229 
GLU   H    H  N N 230 
GLU   H2   H  N N 231 
GLU   HA   H  N N 232 
GLU   HB2  H  N N 233 
GLU   HB3  H  N N 234 
GLU   HG2  H  N N 235 
GLU   HG3  H  N N 236 
GLU   HE2  H  N N 237 
GLU   HXT  H  N N 238 
GLY   N    N  N N 239 
GLY   CA   C  N N 240 
GLY   C    C  N N 241 
GLY   O    O  N N 242 
GLY   OXT  O  N N 243 
GLY   H    H  N N 244 
GLY   H2   H  N N 245 
GLY   HA2  H  N N 246 
GLY   HA3  H  N N 247 
GLY   HXT  H  N N 248 
GOL   C1   C  N N 249 
GOL   O1   O  N N 250 
GOL   C2   C  N N 251 
GOL   O2   O  N N 252 
GOL   C3   C  N N 253 
GOL   O3   O  N N 254 
GOL   H11  H  N N 255 
GOL   H12  H  N N 256 
GOL   HO1  H  N N 257 
GOL   H2   H  N N 258 
GOL   HO2  H  N N 259 
GOL   H31  H  N N 260 
GOL   H32  H  N N 261 
GOL   HO3  H  N N 262 
HIS   N    N  N N 263 
HIS   CA   C  N S 264 
HIS   C    C  N N 265 
HIS   O    O  N N 266 
HIS   CB   C  N N 267 
HIS   CG   C  Y N 268 
HIS   ND1  N  Y N 269 
HIS   CD2  C  Y N 270 
HIS   CE1  C  Y N 271 
HIS   NE2  N  Y N 272 
HIS   OXT  O  N N 273 
HIS   H    H  N N 274 
HIS   H2   H  N N 275 
HIS   HA   H  N N 276 
HIS   HB2  H  N N 277 
HIS   HB3  H  N N 278 
HIS   HD1  H  N N 279 
HIS   HD2  H  N N 280 
HIS   HE1  H  N N 281 
HIS   HE2  H  N N 282 
HIS   HXT  H  N N 283 
HOH   O    O  N N 284 
HOH   H1   H  N N 285 
HOH   H2   H  N N 286 
ILE   N    N  N N 287 
ILE   CA   C  N S 288 
ILE   C    C  N N 289 
ILE   O    O  N N 290 
ILE   CB   C  N S 291 
ILE   CG1  C  N N 292 
ILE   CG2  C  N N 293 
ILE   CD1  C  N N 294 
ILE   OXT  O  N N 295 
ILE   H    H  N N 296 
ILE   H2   H  N N 297 
ILE   HA   H  N N 298 
ILE   HB   H  N N 299 
ILE   HG12 H  N N 300 
ILE   HG13 H  N N 301 
ILE   HG21 H  N N 302 
ILE   HG22 H  N N 303 
ILE   HG23 H  N N 304 
ILE   HD11 H  N N 305 
ILE   HD12 H  N N 306 
ILE   HD13 H  N N 307 
ILE   HXT  H  N N 308 
LEU   N    N  N N 309 
LEU   CA   C  N S 310 
LEU   C    C  N N 311 
LEU   O    O  N N 312 
LEU   CB   C  N N 313 
LEU   CG   C  N N 314 
LEU   CD1  C  N N 315 
LEU   CD2  C  N N 316 
LEU   OXT  O  N N 317 
LEU   H    H  N N 318 
LEU   H2   H  N N 319 
LEU   HA   H  N N 320 
LEU   HB2  H  N N 321 
LEU   HB3  H  N N 322 
LEU   HG   H  N N 323 
LEU   HD11 H  N N 324 
LEU   HD12 H  N N 325 
LEU   HD13 H  N N 326 
LEU   HD21 H  N N 327 
LEU   HD22 H  N N 328 
LEU   HD23 H  N N 329 
LEU   HXT  H  N N 330 
LYS   N    N  N N 331 
LYS   CA   C  N S 332 
LYS   C    C  N N 333 
LYS   O    O  N N 334 
LYS   CB   C  N N 335 
LYS   CG   C  N N 336 
LYS   CD   C  N N 337 
LYS   CE   C  N N 338 
LYS   NZ   N  N N 339 
LYS   OXT  O  N N 340 
LYS   H    H  N N 341 
LYS   H2   H  N N 342 
LYS   HA   H  N N 343 
LYS   HB2  H  N N 344 
LYS   HB3  H  N N 345 
LYS   HG2  H  N N 346 
LYS   HG3  H  N N 347 
LYS   HD2  H  N N 348 
LYS   HD3  H  N N 349 
LYS   HE2  H  N N 350 
LYS   HE3  H  N N 351 
LYS   HZ1  H  N N 352 
LYS   HZ2  H  N N 353 
LYS   HZ3  H  N N 354 
LYS   HXT  H  N N 355 
MAN   C1   C  N S 356 
MAN   C2   C  N S 357 
MAN   C3   C  N S 358 
MAN   C4   C  N S 359 
MAN   C5   C  N R 360 
MAN   C6   C  N N 361 
MAN   O1   O  N N 362 
MAN   O2   O  N N 363 
MAN   O3   O  N N 364 
MAN   O4   O  N N 365 
MAN   O5   O  N N 366 
MAN   O6   O  N N 367 
MAN   H1   H  N N 368 
MAN   H2   H  N N 369 
MAN   H3   H  N N 370 
MAN   H4   H  N N 371 
MAN   H5   H  N N 372 
MAN   H61  H  N N 373 
MAN   H62  H  N N 374 
MAN   HO1  H  N N 375 
MAN   HO2  H  N N 376 
MAN   HO3  H  N N 377 
MAN   HO4  H  N N 378 
MAN   HO6  H  N N 379 
MET   N    N  N N 380 
MET   CA   C  N S 381 
MET   C    C  N N 382 
MET   O    O  N N 383 
MET   CB   C  N N 384 
MET   CG   C  N N 385 
MET   SD   S  N N 386 
MET   CE   C  N N 387 
MET   OXT  O  N N 388 
MET   H    H  N N 389 
MET   H2   H  N N 390 
MET   HA   H  N N 391 
MET   HB2  H  N N 392 
MET   HB3  H  N N 393 
MET   HG2  H  N N 394 
MET   HG3  H  N N 395 
MET   HE1  H  N N 396 
MET   HE2  H  N N 397 
MET   HE3  H  N N 398 
MET   HXT  H  N N 399 
MG    MG   MG N N 400 
NAG   C1   C  N R 401 
NAG   C2   C  N R 402 
NAG   C3   C  N R 403 
NAG   C4   C  N S 404 
NAG   C5   C  N R 405 
NAG   C6   C  N N 406 
NAG   C7   C  N N 407 
NAG   C8   C  N N 408 
NAG   N2   N  N N 409 
NAG   O1   O  N N 410 
NAG   O3   O  N N 411 
NAG   O4   O  N N 412 
NAG   O5   O  N N 413 
NAG   O6   O  N N 414 
NAG   O7   O  N N 415 
NAG   H1   H  N N 416 
NAG   H2   H  N N 417 
NAG   H3   H  N N 418 
NAG   H4   H  N N 419 
NAG   H5   H  N N 420 
NAG   H61  H  N N 421 
NAG   H62  H  N N 422 
NAG   H81  H  N N 423 
NAG   H82  H  N N 424 
NAG   H83  H  N N 425 
NAG   HN2  H  N N 426 
NAG   HO1  H  N N 427 
NAG   HO3  H  N N 428 
NAG   HO4  H  N N 429 
NAG   HO6  H  N N 430 
PHE   N    N  N N 431 
PHE   CA   C  N S 432 
PHE   C    C  N N 433 
PHE   O    O  N N 434 
PHE   CB   C  N N 435 
PHE   CG   C  Y N 436 
PHE   CD1  C  Y N 437 
PHE   CD2  C  Y N 438 
PHE   CE1  C  Y N 439 
PHE   CE2  C  Y N 440 
PHE   CZ   C  Y N 441 
PHE   OXT  O  N N 442 
PHE   H    H  N N 443 
PHE   H2   H  N N 444 
PHE   HA   H  N N 445 
PHE   HB2  H  N N 446 
PHE   HB3  H  N N 447 
PHE   HD1  H  N N 448 
PHE   HD2  H  N N 449 
PHE   HE1  H  N N 450 
PHE   HE2  H  N N 451 
PHE   HZ   H  N N 452 
PHE   HXT  H  N N 453 
PRO   N    N  N N 454 
PRO   CA   C  N S 455 
PRO   C    C  N N 456 
PRO   O    O  N N 457 
PRO   CB   C  N N 458 
PRO   CG   C  N N 459 
PRO   CD   C  N N 460 
PRO   OXT  O  N N 461 
PRO   H    H  N N 462 
PRO   HA   H  N N 463 
PRO   HB2  H  N N 464 
PRO   HB3  H  N N 465 
PRO   HG2  H  N N 466 
PRO   HG3  H  N N 467 
PRO   HD2  H  N N 468 
PRO   HD3  H  N N 469 
PRO   HXT  H  N N 470 
SER   N    N  N N 471 
SER   CA   C  N S 472 
SER   C    C  N N 473 
SER   O    O  N N 474 
SER   CB   C  N N 475 
SER   OG   O  N N 476 
SER   OXT  O  N N 477 
SER   H    H  N N 478 
SER   H2   H  N N 479 
SER   HA   H  N N 480 
SER   HB2  H  N N 481 
SER   HB3  H  N N 482 
SER   HG   H  N N 483 
SER   HXT  H  N N 484 
THR   N    N  N N 485 
THR   CA   C  N S 486 
THR   C    C  N N 487 
THR   O    O  N N 488 
THR   CB   C  N R 489 
THR   OG1  O  N N 490 
THR   CG2  C  N N 491 
THR   OXT  O  N N 492 
THR   H    H  N N 493 
THR   H2   H  N N 494 
THR   HA   H  N N 495 
THR   HB   H  N N 496 
THR   HG1  H  N N 497 
THR   HG21 H  N N 498 
THR   HG22 H  N N 499 
THR   HG23 H  N N 500 
THR   HXT  H  N N 501 
TRP   N    N  N N 502 
TRP   CA   C  N S 503 
TRP   C    C  N N 504 
TRP   O    O  N N 505 
TRP   CB   C  N N 506 
TRP   CG   C  Y N 507 
TRP   CD1  C  Y N 508 
TRP   CD2  C  Y N 509 
TRP   NE1  N  Y N 510 
TRP   CE2  C  Y N 511 
TRP   CE3  C  Y N 512 
TRP   CZ2  C  Y N 513 
TRP   CZ3  C  Y N 514 
TRP   CH2  C  Y N 515 
TRP   OXT  O  N N 516 
TRP   H    H  N N 517 
TRP   H2   H  N N 518 
TRP   HA   H  N N 519 
TRP   HB2  H  N N 520 
TRP   HB3  H  N N 521 
TRP   HD1  H  N N 522 
TRP   HE1  H  N N 523 
TRP   HE3  H  N N 524 
TRP   HZ2  H  N N 525 
TRP   HZ3  H  N N 526 
TRP   HH2  H  N N 527 
TRP   HXT  H  N N 528 
TYR   N    N  N N 529 
TYR   CA   C  N S 530 
TYR   C    C  N N 531 
TYR   O    O  N N 532 
TYR   CB   C  N N 533 
TYR   CG   C  Y N 534 
TYR   CD1  C  Y N 535 
TYR   CD2  C  Y N 536 
TYR   CE1  C  Y N 537 
TYR   CE2  C  Y N 538 
TYR   CZ   C  Y N 539 
TYR   OH   O  N N 540 
TYR   OXT  O  N N 541 
TYR   H    H  N N 542 
TYR   H2   H  N N 543 
TYR   HA   H  N N 544 
TYR   HB2  H  N N 545 
TYR   HB3  H  N N 546 
TYR   HD1  H  N N 547 
TYR   HD2  H  N N 548 
TYR   HE1  H  N N 549 
TYR   HE2  H  N N 550 
TYR   HH   H  N N 551 
TYR   HXT  H  N N 552 
VAL   N    N  N N 553 
VAL   CA   C  N S 554 
VAL   C    C  N N 555 
VAL   O    O  N N 556 
VAL   CB   C  N N 557 
VAL   CG1  C  N N 558 
VAL   CG2  C  N N 559 
VAL   OXT  O  N N 560 
VAL   H    H  N N 561 
VAL   H2   H  N N 562 
VAL   HA   H  N N 563 
VAL   HB   H  N N 564 
VAL   HG11 H  N N 565 
VAL   HG12 H  N N 566 
VAL   HG13 H  N N 567 
VAL   HG21 H  N N 568 
VAL   HG22 H  N N 569 
VAL   HG23 H  N N 570 
VAL   HXT  H  N N 571 
# 
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 
A1A6I C20 C19  sing N N 1   
A1A6I C20 C21  sing N N 2   
A1A6I C19 C18  sing N N 3   
A1A6I C21 N22  sing N N 4   
A1A6I C18 C23  doub Y N 5   
A1A6I C18 C17  sing Y N 6   
A1A6I N22 C17  sing N N 7   
A1A6I C23 C24  sing Y N 8   
A1A6I C17 N16  doub Y N 9   
A1A6I C24 C15  doub Y N 10  
A1A6I N16 C15  sing Y N 11  
A1A6I C15 C14  sing N N 12  
A1A6I C37 C36  sing N N 13  
A1A6I C37 C35  sing N N 14  
A1A6I C36 C35  sing N N 15  
A1A6I C14 C13  sing N N 16  
A1A6I C13 C12  sing N N 17  
A1A6I C35 C38  sing N N 18  
A1A6I C35 C34  sing N N 19  
A1A6I C38 O39  sing N N 20  
A1A6I C11 C12  sing N N 21  
A1A6I C11 O10  sing N N 22  
A1A6I C34 C33  sing N N 23  
A1A6I O39 C32  sing N N 24  
A1A6I O10 C08  sing N N 25  
A1A6I C08 C07  sing N N 26  
A1A6I C08 C09  sing N N 27  
A1A6I C33 C32  sing N N 28  
A1A6I C32 C31  sing N N 29  
A1A6I C07 C06  sing N N 30  
A1A6I C09 N05  sing N N 31  
A1A6I C31 C30  doub Y N 32  
A1A6I C31 C25  sing Y N 33  
A1A6I C30 C29  sing Y N 34  
A1A6I C06 N05  sing N N 35  
A1A6I N05 C04  sing N N 36  
A1A6I C04 C25  sing N N 37  
A1A6I C04 C02  sing N N 38  
A1A6I C25 C26  doub Y N 39  
A1A6I C29 C27  doub Y N 40  
A1A6I C26 C27  sing Y N 41  
A1A6I C27 F28  sing N N 42  
A1A6I C02 O03  doub N N 43  
A1A6I C02 O01  sing N N 44  
A1A6I C13 H1   sing N N 45  
A1A6I C13 H2   sing N N 46  
A1A6I C14 H3   sing N N 47  
A1A6I C14 H4   sing N N 48  
A1A6I C19 H5   sing N N 49  
A1A6I C19 H6   sing N N 50  
A1A6I C20 H7   sing N N 51  
A1A6I C20 H8   sing N N 52  
A1A6I C21 H9   sing N N 53  
A1A6I C21 H10  sing N N 54  
A1A6I C23 H11  sing N N 55  
A1A6I C24 H12  sing N N 56  
A1A6I C26 H13  sing N N 57  
A1A6I C04 H14  sing N N 58  
A1A6I C06 H15  sing N N 59  
A1A6I C06 H16  sing N N 60  
A1A6I C07 H17  sing N N 61  
A1A6I C07 H18  sing N N 62  
A1A6I C08 H19  sing N N 63  
A1A6I C09 H20  sing N N 64  
A1A6I C09 H21  sing N N 65  
A1A6I C11 H22  sing N N 66  
A1A6I C11 H23  sing N N 67  
A1A6I C12 H24  sing N N 68  
A1A6I C12 H25  sing N N 69  
A1A6I C29 H26  sing N N 70  
A1A6I C30 H27  sing N N 71  
A1A6I C32 H28  sing N N 72  
A1A6I C33 H29  sing N N 73  
A1A6I C33 H30  sing N N 74  
A1A6I C34 H31  sing N N 75  
A1A6I C34 H32  sing N N 76  
A1A6I C36 H33  sing N N 77  
A1A6I C36 H34  sing N N 78  
A1A6I C37 H35  sing N N 79  
A1A6I C37 H36  sing N N 80  
A1A6I C38 H37  sing N N 81  
A1A6I C38 H38  sing N N 82  
A1A6I N22 H40  sing N N 83  
A1A6I O01 H41  sing N N 84  
ACT   C   O    doub N N 85  
ACT   C   OXT  sing N N 86  
ACT   C   CH3  sing N N 87  
ACT   CH3 H1   sing N N 88  
ACT   CH3 H2   sing N N 89  
ACT   CH3 H3   sing N N 90  
ALA   N   CA   sing N N 91  
ALA   N   H    sing N N 92  
ALA   N   H2   sing N N 93  
ALA   CA  C    sing N N 94  
ALA   CA  CB   sing N N 95  
ALA   CA  HA   sing N N 96  
ALA   C   O    doub N N 97  
ALA   C   OXT  sing N N 98  
ALA   CB  HB1  sing N N 99  
ALA   CB  HB2  sing N N 100 
ALA   CB  HB3  sing N N 101 
ALA   OXT HXT  sing N N 102 
ARG   N   CA   sing N N 103 
ARG   N   H    sing N N 104 
ARG   N   H2   sing N N 105 
ARG   CA  C    sing N N 106 
ARG   CA  CB   sing N N 107 
ARG   CA  HA   sing N N 108 
ARG   C   O    doub N N 109 
ARG   C   OXT  sing N N 110 
ARG   CB  CG   sing N N 111 
ARG   CB  HB2  sing N N 112 
ARG   CB  HB3  sing N N 113 
ARG   CG  CD   sing N N 114 
ARG   CG  HG2  sing N N 115 
ARG   CG  HG3  sing N N 116 
ARG   CD  NE   sing N N 117 
ARG   CD  HD2  sing N N 118 
ARG   CD  HD3  sing N N 119 
ARG   NE  CZ   sing N N 120 
ARG   NE  HE   sing N N 121 
ARG   CZ  NH1  sing N N 122 
ARG   CZ  NH2  doub N N 123 
ARG   NH1 HH11 sing N N 124 
ARG   NH1 HH12 sing N N 125 
ARG   NH2 HH21 sing N N 126 
ARG   NH2 HH22 sing N N 127 
ARG   OXT HXT  sing N N 128 
ASN   N   CA   sing N N 129 
ASN   N   H    sing N N 130 
ASN   N   H2   sing N N 131 
ASN   CA  C    sing N N 132 
ASN   CA  CB   sing N N 133 
ASN   CA  HA   sing N N 134 
ASN   C   O    doub N N 135 
ASN   C   OXT  sing N N 136 
ASN   CB  CG   sing N N 137 
ASN   CB  HB2  sing N N 138 
ASN   CB  HB3  sing N N 139 
ASN   CG  OD1  doub N N 140 
ASN   CG  ND2  sing N N 141 
ASN   ND2 HD21 sing N N 142 
ASN   ND2 HD22 sing N N 143 
ASN   OXT HXT  sing N N 144 
ASP   N   CA   sing N N 145 
ASP   N   H    sing N N 146 
ASP   N   H2   sing N N 147 
ASP   CA  C    sing N N 148 
ASP   CA  CB   sing N N 149 
ASP   CA  HA   sing N N 150 
ASP   C   O    doub N N 151 
ASP   C   OXT  sing N N 152 
ASP   CB  CG   sing N N 153 
ASP   CB  HB2  sing N N 154 
ASP   CB  HB3  sing N N 155 
ASP   CG  OD1  doub N N 156 
ASP   CG  OD2  sing N N 157 
ASP   OD2 HD2  sing N N 158 
ASP   OXT HXT  sing N N 159 
BMA   C1  C2   sing N N 160 
BMA   C1  O1   sing N N 161 
BMA   C1  O5   sing N N 162 
BMA   C1  H1   sing N N 163 
BMA   C2  C3   sing N N 164 
BMA   C2  O2   sing N N 165 
BMA   C2  H2   sing N N 166 
BMA   C3  C4   sing N N 167 
BMA   C3  O3   sing N N 168 
BMA   C3  H3   sing N N 169 
BMA   C4  C5   sing N N 170 
BMA   C4  O4   sing N N 171 
BMA   C4  H4   sing N N 172 
BMA   C5  C6   sing N N 173 
BMA   C5  O5   sing N N 174 
BMA   C5  H5   sing N N 175 
BMA   C6  O6   sing N N 176 
BMA   C6  H61  sing N N 177 
BMA   C6  H62  sing N N 178 
BMA   O1  HO1  sing N N 179 
BMA   O2  HO2  sing N N 180 
BMA   O3  HO3  sing N N 181 
BMA   O4  HO4  sing N N 182 
BMA   O6  HO6  sing N N 183 
CYS   N   CA   sing N N 184 
CYS   N   H    sing N N 185 
CYS   N   H2   sing N N 186 
CYS   CA  C    sing N N 187 
CYS   CA  CB   sing N N 188 
CYS   CA  HA   sing N N 189 
CYS   C   O    doub N N 190 
CYS   C   OXT  sing N N 191 
CYS   CB  SG   sing N N 192 
CYS   CB  HB2  sing N N 193 
CYS   CB  HB3  sing N N 194 
CYS   SG  HG   sing N N 195 
CYS   OXT HXT  sing N N 196 
GLN   N   CA   sing N N 197 
GLN   N   H    sing N N 198 
GLN   N   H2   sing N N 199 
GLN   CA  C    sing N N 200 
GLN   CA  CB   sing N N 201 
GLN   CA  HA   sing N N 202 
GLN   C   O    doub N N 203 
GLN   C   OXT  sing N N 204 
GLN   CB  CG   sing N N 205 
GLN   CB  HB2  sing N N 206 
GLN   CB  HB3  sing N N 207 
GLN   CG  CD   sing N N 208 
GLN   CG  HG2  sing N N 209 
GLN   CG  HG3  sing N N 210 
GLN   CD  OE1  doub N N 211 
GLN   CD  NE2  sing N N 212 
GLN   NE2 HE21 sing N N 213 
GLN   NE2 HE22 sing N N 214 
GLN   OXT HXT  sing N N 215 
GLU   N   CA   sing N N 216 
GLU   N   H    sing N N 217 
GLU   N   H2   sing N N 218 
GLU   CA  C    sing N N 219 
GLU   CA  CB   sing N N 220 
GLU   CA  HA   sing N N 221 
GLU   C   O    doub N N 222 
GLU   C   OXT  sing N N 223 
GLU   CB  CG   sing N N 224 
GLU   CB  HB2  sing N N 225 
GLU   CB  HB3  sing N N 226 
GLU   CG  CD   sing N N 227 
GLU   CG  HG2  sing N N 228 
GLU   CG  HG3  sing N N 229 
GLU   CD  OE1  doub N N 230 
GLU   CD  OE2  sing N N 231 
GLU   OE2 HE2  sing N N 232 
GLU   OXT HXT  sing N N 233 
GLY   N   CA   sing N N 234 
GLY   N   H    sing N N 235 
GLY   N   H2   sing N N 236 
GLY   CA  C    sing N N 237 
GLY   CA  HA2  sing N N 238 
GLY   CA  HA3  sing N N 239 
GLY   C   O    doub N N 240 
GLY   C   OXT  sing N N 241 
GLY   OXT HXT  sing N N 242 
GOL   C1  O1   sing N N 243 
GOL   C1  C2   sing N N 244 
GOL   C1  H11  sing N N 245 
GOL   C1  H12  sing N N 246 
GOL   O1  HO1  sing N N 247 
GOL   C2  O2   sing N N 248 
GOL   C2  C3   sing N N 249 
GOL   C2  H2   sing N N 250 
GOL   O2  HO2  sing N N 251 
GOL   C3  O3   sing N N 252 
GOL   C3  H31  sing N N 253 
GOL   C3  H32  sing N N 254 
GOL   O3  HO3  sing N N 255 
HIS   N   CA   sing N N 256 
HIS   N   H    sing N N 257 
HIS   N   H2   sing N N 258 
HIS   CA  C    sing N N 259 
HIS   CA  CB   sing N N 260 
HIS   CA  HA   sing N N 261 
HIS   C   O    doub N N 262 
HIS   C   OXT  sing N N 263 
HIS   CB  CG   sing N N 264 
HIS   CB  HB2  sing N N 265 
HIS   CB  HB3  sing N N 266 
HIS   CG  ND1  sing Y N 267 
HIS   CG  CD2  doub Y N 268 
HIS   ND1 CE1  doub Y N 269 
HIS   ND1 HD1  sing N N 270 
HIS   CD2 NE2  sing Y N 271 
HIS   CD2 HD2  sing N N 272 
HIS   CE1 NE2  sing Y N 273 
HIS   CE1 HE1  sing N N 274 
HIS   NE2 HE2  sing N N 275 
HIS   OXT HXT  sing N N 276 
HOH   O   H1   sing N N 277 
HOH   O   H2   sing N N 278 
ILE   N   CA   sing N N 279 
ILE   N   H    sing N N 280 
ILE   N   H2   sing N N 281 
ILE   CA  C    sing N N 282 
ILE   CA  CB   sing N N 283 
ILE   CA  HA   sing N N 284 
ILE   C   O    doub N N 285 
ILE   C   OXT  sing N N 286 
ILE   CB  CG1  sing N N 287 
ILE   CB  CG2  sing N N 288 
ILE   CB  HB   sing N N 289 
ILE   CG1 CD1  sing N N 290 
ILE   CG1 HG12 sing N N 291 
ILE   CG1 HG13 sing N N 292 
ILE   CG2 HG21 sing N N 293 
ILE   CG2 HG22 sing N N 294 
ILE   CG2 HG23 sing N N 295 
ILE   CD1 HD11 sing N N 296 
ILE   CD1 HD12 sing N N 297 
ILE   CD1 HD13 sing N N 298 
ILE   OXT HXT  sing N N 299 
LEU   N   CA   sing N N 300 
LEU   N   H    sing N N 301 
LEU   N   H2   sing N N 302 
LEU   CA  C    sing N N 303 
LEU   CA  CB   sing N N 304 
LEU   CA  HA   sing N N 305 
LEU   C   O    doub N N 306 
LEU   C   OXT  sing N N 307 
LEU   CB  CG   sing N N 308 
LEU   CB  HB2  sing N N 309 
LEU   CB  HB3  sing N N 310 
LEU   CG  CD1  sing N N 311 
LEU   CG  CD2  sing N N 312 
LEU   CG  HG   sing N N 313 
LEU   CD1 HD11 sing N N 314 
LEU   CD1 HD12 sing N N 315 
LEU   CD1 HD13 sing N N 316 
LEU   CD2 HD21 sing N N 317 
LEU   CD2 HD22 sing N N 318 
LEU   CD2 HD23 sing N N 319 
LEU   OXT HXT  sing N N 320 
LYS   N   CA   sing N N 321 
LYS   N   H    sing N N 322 
LYS   N   H2   sing N N 323 
LYS   CA  C    sing N N 324 
LYS   CA  CB   sing N N 325 
LYS   CA  HA   sing N N 326 
LYS   C   O    doub N N 327 
LYS   C   OXT  sing N N 328 
LYS   CB  CG   sing N N 329 
LYS   CB  HB2  sing N N 330 
LYS   CB  HB3  sing N N 331 
LYS   CG  CD   sing N N 332 
LYS   CG  HG2  sing N N 333 
LYS   CG  HG3  sing N N 334 
LYS   CD  CE   sing N N 335 
LYS   CD  HD2  sing N N 336 
LYS   CD  HD3  sing N N 337 
LYS   CE  NZ   sing N N 338 
LYS   CE  HE2  sing N N 339 
LYS   CE  HE3  sing N N 340 
LYS   NZ  HZ1  sing N N 341 
LYS   NZ  HZ2  sing N N 342 
LYS   NZ  HZ3  sing N N 343 
LYS   OXT HXT  sing N N 344 
MAN   C1  C2   sing N N 345 
MAN   C1  O1   sing N N 346 
MAN   C1  O5   sing N N 347 
MAN   C1  H1   sing N N 348 
MAN   C2  C3   sing N N 349 
MAN   C2  O2   sing N N 350 
MAN   C2  H2   sing N N 351 
MAN   C3  C4   sing N N 352 
MAN   C3  O3   sing N N 353 
MAN   C3  H3   sing N N 354 
MAN   C4  C5   sing N N 355 
MAN   C4  O4   sing N N 356 
MAN   C4  H4   sing N N 357 
MAN   C5  C6   sing N N 358 
MAN   C5  O5   sing N N 359 
MAN   C5  H5   sing N N 360 
MAN   C6  O6   sing N N 361 
MAN   C6  H61  sing N N 362 
MAN   C6  H62  sing N N 363 
MAN   O1  HO1  sing N N 364 
MAN   O2  HO2  sing N N 365 
MAN   O3  HO3  sing N N 366 
MAN   O4  HO4  sing N N 367 
MAN   O6  HO6  sing N N 368 
MET   N   CA   sing N N 369 
MET   N   H    sing N N 370 
MET   N   H2   sing N N 371 
MET   CA  C    sing N N 372 
MET   CA  CB   sing N N 373 
MET   CA  HA   sing N N 374 
MET   C   O    doub N N 375 
MET   C   OXT  sing N N 376 
MET   CB  CG   sing N N 377 
MET   CB  HB2  sing N N 378 
MET   CB  HB3  sing N N 379 
MET   CG  SD   sing N N 380 
MET   CG  HG2  sing N N 381 
MET   CG  HG3  sing N N 382 
MET   SD  CE   sing N N 383 
MET   CE  HE1  sing N N 384 
MET   CE  HE2  sing N N 385 
MET   CE  HE3  sing N N 386 
MET   OXT HXT  sing N N 387 
NAG   C1  C2   sing N N 388 
NAG   C1  O1   sing N N 389 
NAG   C1  O5   sing N N 390 
NAG   C1  H1   sing N N 391 
NAG   C2  C3   sing N N 392 
NAG   C2  N2   sing N N 393 
NAG   C2  H2   sing N N 394 
NAG   C3  C4   sing N N 395 
NAG   C3  O3   sing N N 396 
NAG   C3  H3   sing N N 397 
NAG   C4  C5   sing N N 398 
NAG   C4  O4   sing N N 399 
NAG   C4  H4   sing N N 400 
NAG   C5  C6   sing N N 401 
NAG   C5  O5   sing N N 402 
NAG   C5  H5   sing N N 403 
NAG   C6  O6   sing N N 404 
NAG   C6  H61  sing N N 405 
NAG   C6  H62  sing N N 406 
NAG   C7  C8   sing N N 407 
NAG   C7  N2   sing N N 408 
NAG   C7  O7   doub N N 409 
NAG   C8  H81  sing N N 410 
NAG   C8  H82  sing N N 411 
NAG   C8  H83  sing N N 412 
NAG   N2  HN2  sing N N 413 
NAG   O1  HO1  sing N N 414 
NAG   O3  HO3  sing N N 415 
NAG   O4  HO4  sing N N 416 
NAG   O6  HO6  sing N N 417 
PHE   N   CA   sing N N 418 
PHE   N   H    sing N N 419 
PHE   N   H2   sing N N 420 
PHE   CA  C    sing N N 421 
PHE   CA  CB   sing N N 422 
PHE   CA  HA   sing N N 423 
PHE   C   O    doub N N 424 
PHE   C   OXT  sing N N 425 
PHE   CB  CG   sing N N 426 
PHE   CB  HB2  sing N N 427 
PHE   CB  HB3  sing N N 428 
PHE   CG  CD1  doub Y N 429 
PHE   CG  CD2  sing Y N 430 
PHE   CD1 CE1  sing Y N 431 
PHE   CD1 HD1  sing N N 432 
PHE   CD2 CE2  doub Y N 433 
PHE   CD2 HD2  sing N N 434 
PHE   CE1 CZ   doub Y N 435 
PHE   CE1 HE1  sing N N 436 
PHE   CE2 CZ   sing Y N 437 
PHE   CE2 HE2  sing N N 438 
PHE   CZ  HZ   sing N N 439 
PHE   OXT HXT  sing N N 440 
PRO   N   CA   sing N N 441 
PRO   N   CD   sing N N 442 
PRO   N   H    sing N N 443 
PRO   CA  C    sing N N 444 
PRO   CA  CB   sing N N 445 
PRO   CA  HA   sing N N 446 
PRO   C   O    doub N N 447 
PRO   C   OXT  sing N N 448 
PRO   CB  CG   sing N N 449 
PRO   CB  HB2  sing N N 450 
PRO   CB  HB3  sing N N 451 
PRO   CG  CD   sing N N 452 
PRO   CG  HG2  sing N N 453 
PRO   CG  HG3  sing N N 454 
PRO   CD  HD2  sing N N 455 
PRO   CD  HD3  sing N N 456 
PRO   OXT HXT  sing N N 457 
SER   N   CA   sing N N 458 
SER   N   H    sing N N 459 
SER   N   H2   sing N N 460 
SER   CA  C    sing N N 461 
SER   CA  CB   sing N N 462 
SER   CA  HA   sing N N 463 
SER   C   O    doub N N 464 
SER   C   OXT  sing N N 465 
SER   CB  OG   sing N N 466 
SER   CB  HB2  sing N N 467 
SER   CB  HB3  sing N N 468 
SER   OG  HG   sing N N 469 
SER   OXT HXT  sing N N 470 
THR   N   CA   sing N N 471 
THR   N   H    sing N N 472 
THR   N   H2   sing N N 473 
THR   CA  C    sing N N 474 
THR   CA  CB   sing N N 475 
THR   CA  HA   sing N N 476 
THR   C   O    doub N N 477 
THR   C   OXT  sing N N 478 
THR   CB  OG1  sing N N 479 
THR   CB  CG2  sing N N 480 
THR   CB  HB   sing N N 481 
THR   OG1 HG1  sing N N 482 
THR   CG2 HG21 sing N N 483 
THR   CG2 HG22 sing N N 484 
THR   CG2 HG23 sing N N 485 
THR   OXT HXT  sing N N 486 
TRP   N   CA   sing N N 487 
TRP   N   H    sing N N 488 
TRP   N   H2   sing N N 489 
TRP   CA  C    sing N N 490 
TRP   CA  CB   sing N N 491 
TRP   CA  HA   sing N N 492 
TRP   C   O    doub N N 493 
TRP   C   OXT  sing N N 494 
TRP   CB  CG   sing N N 495 
TRP   CB  HB2  sing N N 496 
TRP   CB  HB3  sing N N 497 
TRP   CG  CD1  doub Y N 498 
TRP   CG  CD2  sing Y N 499 
TRP   CD1 NE1  sing Y N 500 
TRP   CD1 HD1  sing N N 501 
TRP   CD2 CE2  doub Y N 502 
TRP   CD2 CE3  sing Y N 503 
TRP   NE1 CE2  sing Y N 504 
TRP   NE1 HE1  sing N N 505 
TRP   CE2 CZ2  sing Y N 506 
TRP   CE3 CZ3  doub Y N 507 
TRP   CE3 HE3  sing N N 508 
TRP   CZ2 CH2  doub Y N 509 
TRP   CZ2 HZ2  sing N N 510 
TRP   CZ3 CH2  sing Y N 511 
TRP   CZ3 HZ3  sing N N 512 
TRP   CH2 HH2  sing N N 513 
TRP   OXT HXT  sing N N 514 
TYR   N   CA   sing N N 515 
TYR   N   H    sing N N 516 
TYR   N   H2   sing N N 517 
TYR   CA  C    sing N N 518 
TYR   CA  CB   sing N N 519 
TYR   CA  HA   sing N N 520 
TYR   C   O    doub N N 521 
TYR   C   OXT  sing N N 522 
TYR   CB  CG   sing N N 523 
TYR   CB  HB2  sing N N 524 
TYR   CB  HB3  sing N N 525 
TYR   CG  CD1  doub Y N 526 
TYR   CG  CD2  sing Y N 527 
TYR   CD1 CE1  sing Y N 528 
TYR   CD1 HD1  sing N N 529 
TYR   CD2 CE2  doub Y N 530 
TYR   CD2 HD2  sing N N 531 
TYR   CE1 CZ   doub Y N 532 
TYR   CE1 HE1  sing N N 533 
TYR   CE2 CZ   sing Y N 534 
TYR   CE2 HE2  sing N N 535 
TYR   CZ  OH   sing N N 536 
TYR   OH  HH   sing N N 537 
TYR   OXT HXT  sing N N 538 
VAL   N   CA   sing N N 539 
VAL   N   H    sing N N 540 
VAL   N   H2   sing N N 541 
VAL   CA  C    sing N N 542 
VAL   CA  CB   sing N N 543 
VAL   CA  HA   sing N N 544 
VAL   C   O    doub N N 545 
VAL   C   OXT  sing N N 546 
VAL   CB  CG1  sing N N 547 
VAL   CB  CG2  sing N N 548 
VAL   CB  HB   sing N N 549 
VAL   CG1 HG11 sing N N 550 
VAL   CG1 HG12 sing N N 551 
VAL   CG1 HG13 sing N N 552 
VAL   CG2 HG21 sing N N 553 
VAL   CG2 HG22 sing N N 554 
VAL   CG2 HG23 sing N N 555 
VAL   OXT HXT  sing N N 556 
# 
_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 
# 
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 ? 
# 
_atom_sites.entry_id                    9CZF 
_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]   0.010434 
_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]   0.007511 
_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]   0.005898 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
CL 
F  
H  
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N    . PHE   A  1  1   ? 31.957  -1.497  -19.636  1.00 69.71  ? 1    PHE   A N    1 
ATOM   2     C  CA   . PHE   A  1  1   ? 31.823  -0.311  -18.740  1.00 71.82  ? 1    PHE   A CA   1 
ATOM   3     C  C    . PHE   A  1  1   ? 31.151  0.873   -19.434  1.00 76.22  ? 1    PHE   A C    1 
ATOM   4     O  O    . PHE   A  1  1   ? 30.735  1.826   -18.775  1.00 78.73  ? 1    PHE   A O    1 
ATOM   5     C  CB   . PHE   A  1  1   ? 33.202  0.121   -18.222  1.00 72.70  ? 1    PHE   A CB   1 
ATOM   6     C  CG   . PHE   A  1  1   ? 34.169  0.492   -19.312  1.00 76.32  ? 1    PHE   A CG   1 
ATOM   7     C  CD1  . PHE   A  1  1   ? 34.223  1.788   -19.800  1.00 82.03  ? 1    PHE   A CD1  1 
ATOM   8     C  CD2  . PHE   A  1  1   ? 35.025  -0.455  -19.849  1.00 79.21  ? 1    PHE   A CD2  1 
ATOM   9     C  CE1  . PHE   A  1  1   ? 35.110  2.130   -20.803  1.00 89.16  ? 1    PHE   A CE1  1 
ATOM   10    C  CE2  . PHE   A  1  1   ? 35.914  -0.118  -20.851  1.00 86.26  ? 1    PHE   A CE2  1 
ATOM   11    C  CZ   . PHE   A  1  1   ? 35.957  1.175   -21.328  1.00 91.35  ? 1    PHE   A CZ   1 
ATOM   12    H  H1   . PHE   A  1  1   ? 32.222  -2.200  -19.159  1.00 83.63  ? 1    PHE   A H1   1 
ATOM   13    H  H2   . PHE   A  1  1   ? 31.170  -1.673  -20.013  1.00 83.63  ? 1    PHE   A H2   1 
ATOM   14    H  H3   . PHE   A  1  1   ? 32.557  -1.324  -20.269  1.00 83.63  ? 1    PHE   A H3   1 
ATOM   15    H  HA   . PHE   A  1  1   ? 31.264  -0.565  -17.989  1.00 86.16  ? 1    PHE   A HA   1 
ATOM   16    H  HB2  . PHE   A  1  1   ? 33.091  0.895   -17.649  1.00 87.22  ? 1    PHE   A HB2  1 
ATOM   17    H  HB3  . PHE   A  1  1   ? 33.590  -0.612  -17.719  1.00 87.22  ? 1    PHE   A HB3  1 
ATOM   18    H  HD1  . PHE   A  1  1   ? 33.655  2.435   -19.449  1.00 98.42  ? 1    PHE   A HD1  1 
ATOM   19    H  HD2  . PHE   A  1  1   ? 35.000  -1.329  -19.531  1.00 95.04  ? 1    PHE   A HD2  1 
ATOM   20    H  HE1  . PHE   A  1  1   ? 35.137  3.002   -21.124  1.00 106.98 ? 1    PHE   A HE1  1 
ATOM   21    H  HE2  . PHE   A  1  1   ? 36.483  -0.763  -21.204  1.00 103.50 ? 1    PHE   A HE2  1 
ATOM   22    H  HZ   . PHE   A  1  1   ? 36.555  1.403   -22.003  1.00 109.60 ? 1    PHE   A HZ   1 
ATOM   23    N  N    . ASN   A  1  2   ? 31.036  0.809   -20.760  1.00 76.33  ? 2    ASN   A N    1 
ATOM   24    C  CA   . ASN   A  1  2   ? 30.628  1.958   -21.557  1.00 78.49  ? 2    ASN   A CA   1 
ATOM   25    C  C    . ASN   A  1  2   ? 29.177  1.891   -22.024  1.00 79.25  ? 2    ASN   A C    1 
ATOM   26    O  O    . ASN   A  1  2   ? 28.751  2.754   -22.798  1.00 82.39  ? 2    ASN   A O    1 
ATOM   27    C  CB   . ASN   A  1  2   ? 31.551  2.107   -22.770  1.00 77.96  ? 2    ASN   A CB   1 
ATOM   28    C  CG   . ASN   A  1  2   ? 31.602  0.857   -23.618  1.00 74.58  ? 2    ASN   A CG   1 
ATOM   29    O  OD1  . ASN   A  1  2   ? 31.639  -0.256  -23.095  1.00 71.10  ? 2    ASN   A OD1  1 
ATOM   30    N  ND2  . ASN   A  1  2   ? 31.602  1.031   -24.935  1.00 76.67  ? 2    ASN   A ND2  1 
ATOM   31    H  H    . ASN   A  1  2   ? 31.193  0.102   -21.223  1.00 91.57  ? 2    ASN   A H    1 
ATOM   32    H  HA   . ASN   A  1  2   ? 30.715  2.749   -21.002  1.00 94.16  ? 2    ASN   A HA   1 
ATOM   33    H  HB2  . ASN   A  1  2   ? 31.228  2.834   -23.325  1.00 93.53  ? 2    ASN   A HB2  1 
ATOM   34    H  HB3  . ASN   A  1  2   ? 32.450  2.299   -22.462  1.00 93.53  ? 2    ASN   A HB3  1 
ATOM   35    H  HD21 . ASN   A  1  2   ? 31.631  0.349   -25.459  1.00 91.98  ? 2    ASN   A HD21 1 
ATOM   36    H  HD22 . ASN   A  1  2   ? 31.574  1.825   -25.264  1.00 91.98  ? 2    ASN   A HD22 1 
ATOM   37    N  N    . LEU   A  1  3   ? 28.409  0.899   -21.582  1.00 76.58  ? 3    LEU   A N    1 
ATOM   38    C  CA   . LEU   A  1  3   ? 27.006  0.833   -21.970  1.00 75.19  ? 3    LEU   A CA   1 
ATOM   39    C  C    . LEU   A  1  3   ? 26.227  1.982   -21.340  1.00 79.98  ? 3    LEU   A C    1 
ATOM   40    O  O    . LEU   A  1  3   ? 26.426  2.324   -20.171  1.00 82.57  ? 3    LEU   A O    1 
ATOM   41    C  CB   . LEU   A  1  3   ? 26.394  -0.506  -21.556  1.00 67.16  ? 3    LEU   A CB   1 
ATOM   42    C  CG   . LEU   A  1  3   ? 26.638  -1.695  -22.489  1.00 66.25  ? 3    LEU   A CG   1 
ATOM   43    C  CD1  . LEU   A  1  3   ? 26.082  -2.975  -21.881  1.00 61.81  ? 3    LEU   A CD1  1 
ATOM   44    C  CD2  . LEU   A  1  3   ? 26.021  -1.458  -23.862  1.00 66.10  ? 3    LEU   A CD2  1 
ATOM   45    H  H    . LEU   A  1  3   ? 28.672  0.263   -21.067  1.00 91.87  ? 3    LEU   A H    1 
ATOM   46    H  HA   . LEU   A  1  3   ? 26.936  0.906   -22.934  1.00 90.21  ? 3    LEU   A HA   1 
ATOM   47    H  HB2  . LEU   A  1  3   ? 26.759  -0.746  -20.690  1.00 80.58  ? 3    LEU   A HB2  1 
ATOM   48    H  HB3  . LEU   A  1  3   ? 25.434  -0.389  -21.491  1.00 80.58  ? 3    LEU   A HB3  1 
ATOM   49    H  HG   . LEU   A  1  3   ? 27.596  -1.797  -22.607  1.00 79.48  ? 3    LEU   A HG   1 
ATOM   50    H  HD11 . LEU   A  1  3   ? 26.351  -3.729  -22.430  1.00 74.15  ? 3    LEU   A HD11 1 
ATOM   51    H  HD12 . LEU   A  1  3   ? 26.434  -3.078  -20.984  1.00 74.15  ? 3    LEU   A HD12 1 
ATOM   52    H  HD13 . LEU   A  1  3   ? 25.114  -2.917  -21.852  1.00 74.15  ? 3    LEU   A HD13 1 
ATOM   53    H  HD21 . LEU   A  1  3   ? 26.145  -2.252  -24.405  1.00 79.30  ? 3    LEU   A HD21 1 
ATOM   54    H  HD22 . LEU   A  1  3   ? 25.075  -1.273  -23.755  1.00 79.30  ? 3    LEU   A HD22 1 
ATOM   55    H  HD23 . LEU   A  1  3   ? 26.461  -0.700  -24.279  1.00 79.30  ? 3    LEU   A HD23 1 
ATOM   56    N  N    . ASP   A  1  4   ? 25.333  2.581   -22.125  1.00 81.46  ? 4    ASP   A N    1 
ATOM   57    C  CA   . ASP   A  1  4   ? 24.523  3.708   -21.671  1.00 81.51  ? 4    ASP   A CA   1 
ATOM   58    C  C    . ASP   A  1  4   ? 23.281  3.167   -20.973  1.00 82.05  ? 4    ASP   A C    1 
ATOM   59    O  O    . ASP   A  1  4   ? 22.372  2.641   -21.624  1.00 78.25  ? 4    ASP   A O    1 
ATOM   60    C  CB   . ASP   A  1  4   ? 24.149  4.613   -22.843  1.00 80.22  ? 4    ASP   A CB   1 
ATOM   61    C  CG   . ASP   A  1  4   ? 23.266  5.776   -22.427  1.00 81.82  ? 4    ASP   A CG   1 
ATOM   62    O  OD1  . ASP   A  1  4   ? 22.148  5.536   -21.924  1.00 80.09  ? 4    ASP   A OD1  1 
ATOM   63    O  OD2  . ASP   A  1  4   ? 23.694  6.937   -22.599  1.00 88.13  ? 4    ASP   A OD2  1 
ATOM   64    H  H    . ASP   A  1  4   ? 25.175  2.348   -22.938  1.00 97.74  ? 4    ASP   A H    1 
ATOM   65    H  HA   . ASP   A  1  4   ? 25.032  4.232   -21.033  1.00 97.79  ? 4    ASP   A HA   1 
ATOM   66    H  HB2  . ASP   A  1  4   ? 24.959  4.976   -23.234  1.00 96.25  ? 4    ASP   A HB2  1 
ATOM   67    H  HB3  . ASP   A  1  4   ? 23.667  4.091   -23.504  1.00 96.25  ? 4    ASP   A HB3  1 
ATOM   68    N  N    . VAL   A  1  5   ? 23.243  3.301   -19.646  1.00 86.14  ? 5    VAL   A N    1 
ATOM   69    C  CA   . VAL   A  1  5   ? 22.096  2.860   -18.859  1.00 86.50  ? 5    VAL   A CA   1 
ATOM   70    C  C    . VAL   A  1  5   ? 21.162  4.007   -18.498  1.00 93.28  ? 5    VAL   A C    1 
ATOM   71    O  O    . VAL   A  1  5   ? 20.064  3.754   -17.976  1.00 98.54  ? 5    VAL   A O    1 
ATOM   72    C  CB   . VAL   A  1  5   ? 22.554  2.141   -17.570  1.00 80.18  ? 5    VAL   A CB   1 
ATOM   73    C  CG1  . VAL   A  1  5   ? 23.478  0.980   -17.910  1.00 73.09  ? 5    VAL   A CG1  1 
ATOM   74    C  CG2  . VAL   A  1  5   ? 23.246  3.118   -16.625  1.00 80.89  ? 5    VAL   A CG2  1 
ATOM   75    H  H    . VAL   A  1  5   ? 23.875  3.646   -19.176  1.00 103.35 ? 5    VAL   A H    1 
ATOM   76    H  HA   . VAL   A  1  5   ? 21.590  2.228   -19.392  1.00 103.78 ? 5    VAL   A HA   1 
ATOM   77    H  HB   . VAL   A  1  5   ? 21.773  1.787   -17.117  1.00 96.19  ? 5    VAL   A HB   1 
ATOM   78    H  HG11 . VAL   A  1  5   ? 23.738  0.532   -17.089  1.00 87.69  ? 5    VAL   A HG11 1 
ATOM   79    H  HG12 . VAL   A  1  5   ? 23.008  0.361   -18.490  1.00 87.69  ? 5    VAL   A HG12 1 
ATOM   80    H  HG13 . VAL   A  1  5   ? 24.265  1.324   -18.362  1.00 87.69  ? 5    VAL   A HG13 1 
ATOM   81    H  HG21 . VAL   A  1  5   ? 23.607  2.625   -15.872  1.00 97.05  ? 5    VAL   A HG21 1 
ATOM   82    H  HG22 . VAL   A  1  5   ? 23.962  3.565   -17.102  1.00 97.05  ? 5    VAL   A HG22 1 
ATOM   83    H  HG23 . VAL   A  1  5   ? 22.598  3.769   -16.314  1.00 97.05  ? 5    VAL   A HG23 1 
ATOM   84    N  N    . ASP   A  1  6   ? 21.557  5.255   -18.760  1.00 94.06  ? 6    ASP   A N    1 
ATOM   85    C  CA   . ASP   A  1  6   ? 20.744  6.394   -18.345  1.00 95.84  ? 6    ASP   A CA   1 
ATOM   86    C  C    . ASP   A  1  6   ? 19.468  6.500   -19.170  1.00 95.59  ? 6    ASP   A C    1 
ATOM   87    O  O    . ASP   A  1  6   ? 18.403  6.827   -18.634  1.00 96.60  ? 6    ASP   A O    1 
ATOM   88    C  CB   . ASP   A  1  6   ? 21.559  7.682   -18.459  1.00 99.23  ? 6    ASP   A CB   1 
ATOM   89    C  CG   . ASP   A  1  6   ? 22.813  7.654   -17.610  1.00 104.08 ? 6    ASP   A CG   1 
ATOM   90    O  OD1  . ASP   A  1  6   ? 22.778  7.052   -16.517  1.00 104.07 ? 6    ASP   A OD1  1 
ATOM   91    O  OD2  . ASP   A  1  6   ? 23.835  8.231   -18.038  1.00 108.39 ? 6    ASP   A OD2  1 
ATOM   92    H  H    . ASP   A  1  6   ? 22.282  5.465   -19.171  1.00 112.86 ? 6    ASP   A H    1 
ATOM   93    H  HA   . ASP   A  1  6   ? 20.491  6.272   -17.417  1.00 114.99 ? 6    ASP   A HA   1 
ATOM   94    H  HB2  . ASP   A  1  6   ? 21.824  7.808   -19.384  1.00 119.06 ? 6    ASP   A HB2  1 
ATOM   95    H  HB3  . ASP   A  1  6   ? 21.014  8.428   -18.166  1.00 119.06 ? 6    ASP   A HB3  1 
ATOM   96    N  N    . SER   A  1  7   ? 19.553  6.234   -20.472  1.00 94.53  ? 7    SER   A N    1 
ATOM   97    C  CA   . SER   A  1  7   ? 18.417  6.372   -21.385  1.00 92.54  ? 7    SER   A CA   1 
ATOM   98    C  C    . SER   A  1  7   ? 18.487  5.277   -22.441  1.00 86.91  ? 7    SER   A C    1 
ATOM   99    O  O    . SER   A  1  7   ? 18.802  5.530   -23.608  1.00 85.04  ? 7    SER   A O    1 
ATOM   100   C  CB   . SER   A  1  7   ? 18.406  7.760   -22.030  1.00 98.76  ? 7    SER   A CB   1 
ATOM   101   O  OG   . SER   A  1  7   ? 19.677  8.077   -22.572  1.00 104.06 ? 7    SER   A OG   1 
ATOM   102   H  H    . SER   A  1  7   ? 20.273  5.967   -20.859  1.00 113.41 ? 7    SER   A H    1 
ATOM   103   H  HA   . SER   A  1  7   ? 17.594  6.256   -20.885  1.00 111.03 ? 7    SER   A HA   1 
ATOM   104   H  HB2  . SER   A  1  7   ? 17.748  7.772   -22.741  1.00 118.49 ? 7    SER   A HB2  1 
ATOM   105   H  HB3  . SER   A  1  7   ? 18.178  8.419   -21.355  1.00 118.49 ? 7    SER   A HB3  1 
ATOM   106   H  HG   . SER   A  1  7   ? 19.914  7.481   -23.115  1.00 124.85 ? 7    SER   A HG   1 
ATOM   107   N  N    . PRO   A  1  8   ? 18.196  4.038   -22.056  1.00 83.89  ? 8    PRO   A N    1 
ATOM   108   C  CA   . PRO   A  1  8   ? 18.162  2.941   -23.027  1.00 80.77  ? 8    PRO   A CA   1 
ATOM   109   C  C    . PRO   A  1  8   ? 16.817  2.846   -23.731  1.00 80.54  ? 8    PRO   A C    1 
ATOM   110   O  O    . PRO   A  1  8   ? 15.779  3.273   -23.222  1.00 84.11  ? 8    PRO   A O    1 
ATOM   111   C  CB   . PRO   A  1  8   ? 18.413  1.706   -22.154  1.00 77.82  ? 8    PRO   A CB   1 
ATOM   112   C  CG   . PRO   A  1  8   ? 17.771  2.060   -20.853  1.00 77.71  ? 8    PRO   A CG   1 
ATOM   113   C  CD   . PRO   A  1  8   ? 17.940  3.560   -20.684  1.00 81.86  ? 8    PRO   A CD   1 
ATOM   114   H  HA   . PRO   A  1  8   ? 18.867  3.033   -23.687  1.00 96.90  ? 8    PRO   A HA   1 
ATOM   115   H  HB2  . PRO   A  1  8   ? 17.997  0.925   -22.550  1.00 93.36  ? 8    PRO   A HB2  1 
ATOM   116   H  HB3  . PRO   A  1  8   ? 19.365  1.557   -22.048  1.00 93.36  ? 8    PRO   A HB3  1 
ATOM   117   H  HG2  . PRO   A  1  8   ? 16.831  1.824   -20.879  1.00 93.24  ? 8    PRO   A HG2  1 
ATOM   118   H  HG3  . PRO   A  1  8   ? 18.213  1.584   -20.132  1.00 93.24  ? 8    PRO   A HG3  1 
ATOM   119   H  HD2  . PRO   A  1  8   ? 17.132  3.960   -20.326  1.00 98.21  ? 8    PRO   A HD2  1 
ATOM   120   H  HD3  . PRO   A  1  8   ? 18.693  3.758   -20.106  1.00 98.21  ? 8    PRO   A HD3  1 
ATOM   121   N  N    . ALA   A  1  9   ? 16.852  2.270   -24.931  1.00 76.52  ? 9    ALA   A N    1 
ATOM   122   C  CA   . ALA   A  1  9   ? 15.628  2.063   -25.691  1.00 75.24  ? 9    ALA   A CA   1 
ATOM   123   C  C    . ALA   A  1  9   ? 14.821  0.934   -25.064  1.00 75.93  ? 9    ALA   A C    1 
ATOM   124   O  O    . ALA   A  1  9   ? 15.362  -0.130  -24.747  1.00 74.94  ? 9    ALA   A O    1 
ATOM   125   C  CB   . ALA   A  1  9   ? 15.947  1.747   -27.150  1.00 75.33  ? 9    ALA   A CB   1 
ATOM   126   H  H    . ALA   A  1  9   ? 17.567  1.993   -25.322  1.00 91.80  ? 9    ALA   A H    1 
ATOM   127   H  HA   . ALA   A  1  9   ? 15.095  2.874   -25.676  1.00 90.27  ? 9    ALA   A HA   1 
ATOM   128   H  HB1  . ALA   A  1  9   ? 15.372  2.279   -27.722  1.00 90.38  ? 9    ALA   A HB1  1 
ATOM   129   H  HB2  . ALA   A  1  9   ? 16.877  1.961   -27.324  1.00 90.38  ? 9    ALA   A HB2  1 
ATOM   130   H  HB3  . ALA   A  1  9   ? 15.790  0.803   -27.310  1.00 90.38  ? 9    ALA   A HB3  1 
ATOM   131   N  N    . GLU   A  1  10  ? 13.523  1.166   -24.888  1.00 78.12  ? 10   GLU   A N    1 
ATOM   132   C  CA   . GLU   A  1  10  ? 12.645  0.254   -24.168  1.00 79.30  ? 10   GLU   A CA   1 
ATOM   133   C  C    . GLU   A  1  10  ? 11.462  -0.108  -25.053  1.00 76.17  ? 10   GLU   A C    1 
ATOM   134   O  O    . GLU   A  1  10  ? 10.799  0.777   -25.603  1.00 77.58  ? 10   GLU   A O    1 
ATOM   135   C  CB   . GLU   A  1  10  ? 12.176  0.892   -22.854  1.00 84.99  ? 10   GLU   A CB   1 
ATOM   136   C  CG   . GLU   A  1  10  ? 11.126  0.104   -22.093  1.00 90.51  ? 10   GLU   A CG   1 
ATOM   137   C  CD   . GLU   A  1  10  ? 10.746  0.772   -20.788  1.00 95.75  ? 10   GLU   A CD   1 
ATOM   138   O  OE1  . GLU   A  1  10  ? 11.527  1.621   -20.307  1.00 96.11  ? 10   GLU   A OE1  1 
ATOM   139   O  OE2  . GLU   A  1  10  ? 9.667   0.453   -20.246  1.00 97.24  ? 10   GLU   A OE2  1 
ATOM   140   H  H    . GLU   A  1  10  ? 13.119  1.865   -25.185  1.00 93.73  ? 10   GLU   A H    1 
ATOM   141   H  HA   . GLU   A  1  10  ? 13.113  -0.570  -23.960  1.00 95.14  ? 10   GLU   A HA   1 
ATOM   142   H  HB2  . GLU   A  1  10  ? 12.945  0.990   -22.270  1.00 101.97 ? 10   GLU   A HB2  1 
ATOM   143   H  HB3  . GLU   A  1  10  ? 11.798  1.762   -23.054  1.00 101.97 ? 10   GLU   A HB3  1 
ATOM   144   H  HG2  . GLU   A  1  10  ? 10.328  0.029   -22.638  1.00 108.60 ? 10   GLU   A HG2  1 
ATOM   145   H  HG3  . GLU   A  1  10  ? 11.475  -0.778  -21.890  1.00 108.60 ? 10   GLU   A HG3  1 
ATOM   146   N  N    . TYR   A  1  11  ? 11.208  -1.407  -25.191  1.00 72.81  ? 11   TYR   A N    1 
ATOM   147   C  CA   . TYR   A  1  11  ? 10.136  -1.929  -26.026  1.00 74.17  ? 11   TYR   A CA   1 
ATOM   148   C  C    . TYR   A  1  11  ? 9.222   -2.809  -25.186  1.00 74.00  ? 11   TYR   A C    1 
ATOM   149   O  O    . TYR   A  1  11  ? 9.689   -3.553  -24.317  1.00 72.35  ? 11   TYR   A O    1 
ATOM   150   C  CB   . TYR   A  1  11  ? 10.696  -2.733  -27.203  1.00 75.01  ? 11   TYR   A CB   1 
ATOM   151   C  CG   . TYR   A  1  11  ? 11.568  -1.921  -28.132  1.00 76.29  ? 11   TYR   A CG   1 
ATOM   152   C  CD1  . TYR   A  1  11  ? 12.902  -1.686  -27.833  1.00 78.48  ? 11   TYR   A CD1  1 
ATOM   153   C  CD2  . TYR   A  1  11  ? 11.056  -1.391  -29.309  1.00 78.37  ? 11   TYR   A CD2  1 
ATOM   154   C  CE1  . TYR   A  1  11  ? 13.703  -0.947  -28.678  1.00 81.51  ? 11   TYR   A CE1  1 
ATOM   155   C  CE2  . TYR   A  1  11  ? 11.850  -0.648  -30.160  1.00 83.24  ? 11   TYR   A CE2  1 
ATOM   156   C  CZ   . TYR   A  1  11  ? 13.171  -0.429  -29.839  1.00 82.98  ? 11   TYR   A CZ   1 
ATOM   157   O  OH   . TYR   A  1  11  ? 13.968  0.310   -30.683  1.00 81.64  ? 11   TYR   A OH   1 
ATOM   158   H  H    . TYR   A  1  11  ? 11.659  -2.024  -24.796  1.00 87.35  ? 11   TYR   A H    1 
ATOM   159   H  HA   . TYR   A  1  11  ? 9.612   -1.195  -26.383  1.00 88.98  ? 11   TYR   A HA   1 
ATOM   160   H  HB2  . TYR   A  1  11  ? 11.233  -3.462  -26.856  1.00 90.00  ? 11   TYR   A HB2  1 
ATOM   161   H  HB3  . TYR   A  1  11  ? 9.956   -3.083  -27.722  1.00 90.00  ? 11   TYR   A HB3  1 
ATOM   162   H  HD1  . TYR   A  1  11  ? 13.263  -2.034  -27.050  1.00 94.16  ? 11   TYR   A HD1  1 
ATOM   163   H  HD2  . TYR   A  1  11  ? 10.164  -1.539  -29.528  1.00 94.03  ? 11   TYR   A HD2  1 
ATOM   164   H  HE1  . TYR   A  1  11  ? 14.596  -0.798  -28.466  1.00 97.79  ? 11   TYR   A HE1  1 
ATOM   165   H  HE2  . TYR   A  1  11  ? 11.494  -0.299  -30.945  1.00 99.87  ? 11   TYR   A HE2  1 
ATOM   166   H  HH   . TYR   A  1  11  ? 13.500  0.862   -31.109  1.00 97.95  ? 11   TYR   A HH   1 
ATOM   167   N  N    . SER   A  1  12  ? 7.921   -2.722  -25.449  1.00 73.48  ? 12   SER   A N    1 
ATOM   168   C  CA   . SER   A  1  12  ? 6.919   -3.456  -24.693  1.00 72.69  ? 12   SER   A CA   1 
ATOM   169   C  C    . SER   A  1  12  ? 6.067   -4.302  -25.629  1.00 69.33  ? 12   SER   A C    1 
ATOM   170   O  O    . SER   A  1  12  ? 5.930   -4.000  -26.818  1.00 69.43  ? 12   SER   A O    1 
ATOM   171   C  CB   . SER   A  1  12  ? 6.020   -2.503  -23.896  1.00 76.67  ? 12   SER   A CB   1 
ATOM   172   O  OG   . SER   A  1  12  ? 5.204   -1.728  -24.757  1.00 83.16  ? 12   SER   A OG   1 
ATOM   173   H  H    . SER   A  1  12  ? 7.590   -2.234  -26.075  1.00 88.16  ? 12   SER   A H    1 
ATOM   174   H  HA   . SER   A  1  12  ? 7.362   -4.054  -24.071  1.00 87.21  ? 12   SER   A HA   1 
ATOM   175   H  HB2  . SER   A  1  12  ? 5.451   -3.025  -23.309  1.00 91.99  ? 12   SER   A HB2  1 
ATOM   176   H  HB3  . SER   A  1  12  ? 6.579   -1.908  -23.373  1.00 91.99  ? 12   SER   A HB3  1 
ATOM   177   H  HG   . SER   A  1  12  ? 4.720   -1.211  -24.306  1.00 99.77  ? 12   SER   A HG   1 
ATOM   178   N  N    . GLY   A  1  13  ? 5.499   -5.371  -25.076  1.00 66.91  ? 13   GLY   A N    1 
ATOM   179   C  CA   . GLY   A  1  13  ? 4.614   -6.240  -25.813  1.00 63.77  ? 13   GLY   A CA   1 
ATOM   180   C  C    . GLY   A  1  13  ? 3.342   -6.529  -25.043  1.00 65.27  ? 13   GLY   A C    1 
ATOM   181   O  O    . GLY   A  1  13  ? 3.162   -6.081  -23.906  1.00 70.74  ? 13   GLY   A O    1 
ATOM   182   H  H    . GLY   A  1  13  ? 5.619   -5.612  -24.259  1.00 80.27  ? 13   GLY   A H    1 
ATOM   183   H  HA2  . GLY   A  1  13  ? 4.376   -5.820  -26.654  1.00 76.50  ? 13   GLY   A HA2  1 
ATOM   184   H  HA3  . GLY   A  1  13  ? 5.063   -7.080  -25.994  1.00 76.50  ? 13   GLY   A HA3  1 
ATOM   185   N  N    . PRO   A  1  14  ? 2.429   -7.284  -25.653  1.00 64.12  ? 14   PRO   A N    1 
ATOM   186   C  CA   . PRO   A  1  14  ? 1.165   -7.600  -24.975  1.00 65.23  ? 14   PRO   A CA   1 
ATOM   187   C  C    . PRO   A  1  14  ? 1.398   -8.267  -23.626  1.00 64.01  ? 14   PRO   A C    1 
ATOM   188   O  O    . PRO   A  1  14  ? 2.274   -9.121  -23.474  1.00 61.38  ? 14   PRO   A O    1 
ATOM   189   C  CB   . PRO   A  1  14  ? 0.462   -8.545  -25.957  1.00 64.29  ? 14   PRO   A CB   1 
ATOM   190   C  CG   . PRO   A  1  14  ? 1.053   -8.220  -27.289  1.00 63.27  ? 14   PRO   A CG   1 
ATOM   191   C  CD   . PRO   A  1  14  ? 2.477   -7.821  -27.024  1.00 63.25  ? 14   PRO   A CD   1 
ATOM   192   H  HA   . PRO   A  1  14  ? 0.636   -6.797  -24.851  1.00 78.25  ? 14   PRO   A HA   1 
ATOM   193   H  HB2  . PRO   A  1  14  ? 0.640   -9.467  -25.714  1.00 77.13  ? 14   PRO   A HB2  1 
ATOM   194   H  HB3  . PRO   A  1  14  ? -0.493  -8.378  -25.950  1.00 77.13  ? 14   PRO   A HB3  1 
ATOM   195   H  HG2  . PRO   A  1  14  ? 1.016   -9.002  -27.862  1.00 75.90  ? 14   PRO   A HG2  1 
ATOM   196   H  HG3  . PRO   A  1  14  ? 0.561   -7.489  -27.694  1.00 75.90  ? 14   PRO   A HG3  1 
ATOM   197   H  HD2  . PRO   A  1  14  ? 3.066   -8.591  -27.073  1.00 75.88  ? 14   PRO   A HD2  1 
ATOM   198   H  HD3  . PRO   A  1  14  ? 2.767   -7.141  -27.652  1.00 75.88  ? 14   PRO   A HD3  1 
ATOM   199   N  N    . GLU   A  1  15  ? 0.594   -7.867  -22.641  1.00 65.85  ? 15   GLU   A N    1 
ATOM   200   C  CA   . GLU   A  1  15  ? 0.723   -8.416  -21.297  1.00 70.98  ? 15   GLU   A CA   1 
ATOM   201   C  C    . GLU   A  1  15  ? 0.450   -9.915  -21.305  1.00 70.91  ? 15   GLU   A C    1 
ATOM   202   O  O    . GLU   A  1  15  ? -0.570  -10.371 -21.830  1.00 72.18  ? 15   GLU   A O    1 
ATOM   203   C  CB   . GLU   A  1  15  ? -0.241  -7.705  -20.346  1.00 77.48  ? 15   GLU   A CB   1 
ATOM   204   C  CG   . GLU   A  1  15  ? -0.185  -8.203  -18.909  1.00 83.73  ? 15   GLU   A CG   1 
ATOM   205   C  CD   . GLU   A  1  15  ? -1.115  -7.434  -17.989  1.00 93.80  ? 15   GLU   A CD   1 
ATOM   206   O  OE1  . GLU   A  1  15  ? -0.614  -6.745  -17.075  1.00 97.28  ? 15   GLU   A OE1  1 
ATOM   207   O  OE2  . GLU   A  1  15  ? -2.346  -7.513  -18.184  1.00 96.24  ? 15   GLU   A OE2  1 
ATOM   208   H  H    . GLU   A  1  15  ? -0.031  -7.282  -22.727  1.00 79.00  ? 15   GLU   A H    1 
ATOM   209   H  HA   . GLU   A  1  15  ? 1.628   -8.273  -20.977  1.00 85.15  ? 15   GLU   A HA   1 
ATOM   210   H  HB2  . GLU   A  1  15  ? -0.026  -6.759  -20.338  1.00 92.96  ? 15   GLU   A HB2  1 
ATOM   211   H  HB3  . GLU   A  1  15  ? -1.146  -7.836  -20.668  1.00 92.96  ? 15   GLU   A HB3  1 
ATOM   212   H  HG2  . GLU   A  1  15  ? -0.446  -9.137  -18.887  1.00 100.46 ? 15   GLU   A HG2  1 
ATOM   213   H  HG3  . GLU   A  1  15  ? 0.720   -8.103  -18.573  1.00 100.46 ? 15   GLU   A HG3  1 
ATOM   214   N  N    . GLY   A  1  16  ? 1.368   -10.680 -20.717  1.00 70.09  ? 16   GLY   A N    1 
ATOM   215   C  CA   . GLY   A  1  16  ? 1.229   -12.118 -20.636  1.00 69.96  ? 16   GLY   A CA   1 
ATOM   216   C  C    . GLY   A  1  16  ? 1.716   -12.880 -21.848  1.00 68.05  ? 16   GLY   A C    1 
ATOM   217   O  O    . GLY   A  1  16  ? 1.590   -14.111 -21.874  1.00 65.06  ? 16   GLY   A O    1 
ATOM   218   H  H    . GLY   A  1  16  ? 2.087   -10.379 -20.354  1.00 84.09  ? 16   GLY   A H    1 
ATOM   219   H  HA2  . GLY   A  1  16  ? 1.730   -12.434 -19.868  1.00 83.93  ? 16   GLY   A HA2  1 
ATOM   220   H  HA3  . GLY   A  1  16  ? 0.291   -12.331 -20.512  1.00 83.93  ? 16   GLY   A HA3  1 
ATOM   221   N  N    . SER   A  1  17  ? 2.272   -12.197 -22.846  1.00 68.55  ? 17   SER   A N    1 
ATOM   222   C  CA   . SER   A  1  17  ? 2.761   -12.838 -24.059  1.00 65.96  ? 17   SER   A CA   1 
ATOM   223   C  C    . SER   A  1  17  ? 4.222   -13.253 -23.963  1.00 64.93  ? 17   SER   A C    1 
ATOM   224   O  O    . SER   A  1  17  ? 4.752   -13.826 -24.920  1.00 63.97  ? 17   SER   A O    1 
ATOM   225   C  CB   . SER   A  1  17  ? 2.579   -11.899 -25.258  1.00 68.51  ? 17   SER   A CB   1 
ATOM   226   O  OG   . SER   A  1  17  ? 3.384   -10.739 -25.126  1.00 68.95  ? 17   SER   A OG   1 
ATOM   227   H  H    . SER   A  1  17  ? 2.378   -11.344 -22.843  1.00 82.24  ? 17   SER   A H    1 
ATOM   228   H  HA   . SER   A  1  17  ? 2.234   -13.637 -24.219  1.00 79.13  ? 17   SER   A HA   1 
ATOM   229   H  HB2  . SER   A  1  17  ? 2.835   -12.369 -26.067  1.00 82.20  ? 17   SER   A HB2  1 
ATOM   230   H  HB3  . SER   A  1  17  ? 1.648   -11.632 -25.310  1.00 82.20  ? 17   SER   A HB3  1 
ATOM   231   H  HG   . SER   A  1  17  ? 3.191   -10.335 -24.415  1.00 82.72  ? 17   SER   A HG   1 
ATOM   232   N  N    . TYR   A  1  18  ? 4.884   -12.981 -22.838  1.00 66.36  ? 18   TYR   A N    1 
ATOM   233   C  CA   . TYR   A  1  18  ? 6.305   -13.283 -22.676  1.00 65.86  ? 18   TYR   A CA   1 
ATOM   234   C  C    . TYR   A  1  18  ? 7.137   -12.575 -23.746  1.00 62.71  ? 18   TYR   A C    1 
ATOM   235   O  O    . TYR   A  1  18  ? 8.125   -13.113 -24.251  1.00 57.98  ? 18   TYR   A O    1 
ATOM   236   C  CB   . TYR   A  1  18  ? 6.558   -14.794 -22.695  1.00 64.91  ? 18   TYR   A CB   1 
ATOM   237   C  CG   . TYR   A  1  18  ? 6.124   -15.524 -21.435  1.00 63.57  ? 18   TYR   A CG   1 
ATOM   238   C  CD1  . TYR   A  1  18  ? 5.384   -14.883 -20.446  1.00 61.24  ? 18   TYR   A CD1  1 
ATOM   239   C  CD2  . TYR   A  1  18  ? 6.469   -16.854 -21.232  1.00 63.01  ? 18   TYR   A CD2  1 
ATOM   240   C  CE1  . TYR   A  1  18  ? 4.995   -15.551 -19.298  1.00 61.70  ? 18   TYR   A CE1  1 
ATOM   241   C  CE2  . TYR   A  1  18  ? 6.084   -17.527 -20.087  1.00 61.88  ? 18   TYR   A CE2  1 
ATOM   242   C  CZ   . TYR   A  1  18  ? 5.348   -16.871 -19.124  1.00 62.26  ? 18   TYR   A CZ   1 
ATOM   243   O  OH   . TYR   A  1  18  ? 4.963   -17.536 -17.983  1.00 60.38  ? 18   TYR   A OH   1 
ATOM   244   H  H    . TYR   A  1  18  ? 4.526   -12.618 -22.145  1.00 79.62  ? 18   TYR   A H    1 
ATOM   245   H  HA   . TYR   A  1  18  ? 6.595   -12.950 -21.813  1.00 79.01  ? 18   TYR   A HA   1 
ATOM   246   H  HB2  . TYR   A  1  18  ? 6.069   -15.179 -23.439  1.00 77.87  ? 18   TYR   A HB2  1 
ATOM   247   H  HB3  . TYR   A  1  18  ? 7.509   -14.946 -22.808  1.00 77.87  ? 18   TYR   A HB3  1 
ATOM   248   H  HD1  . TYR   A  1  18  ? 5.148   -13.991 -20.559  1.00 73.47  ? 18   TYR   A HD1  1 
ATOM   249   H  HD2  . TYR   A  1  18  ? 6.967   -17.300 -21.878  1.00 75.59  ? 18   TYR   A HD2  1 
ATOM   250   H  HE1  . TYR   A  1  18  ? 4.497   -15.110 -18.648  1.00 74.02  ? 18   TYR   A HE1  1 
ATOM   251   H  HE2  . TYR   A  1  18  ? 6.321   -18.418 -19.967  1.00 74.24  ? 18   TYR   A HE2  1 
ATOM   252   H  HH   . TYR   A  1  18  ? 5.261   -18.322 -17.995  1.00 72.43  ? 18   TYR   A HH   1 
ATOM   253   N  N    . PHE   A  1  19  ? 6.724   -11.358 -24.097  1.00 64.84  ? 19   PHE   A N    1 
ATOM   254   C  CA   . PHE   A  1  19  ? 7.503   -10.521 -25.001  1.00 63.85  ? 19   PHE   A CA   1 
ATOM   255   C  C    . PHE   A  1  19  ? 8.897   -10.300 -24.428  1.00 60.57  ? 19   PHE   A C    1 
ATOM   256   O  O    . PHE   A  1  19  ? 9.048   -9.734  -23.342  1.00 60.26  ? 19   PHE   A O    1 
ATOM   257   C  CB   . PHE   A  1  19  ? 6.787   -9.186  -25.214  1.00 66.98  ? 19   PHE   A CB   1 
ATOM   258   C  CG   . PHE   A  1  19  ? 7.548   -8.210  -26.070  1.00 67.71  ? 19   PHE   A CG   1 
ATOM   259   C  CD1  . PHE   A  1  19  ? 8.452   -7.327  -25.501  1.00 67.12  ? 19   PHE   A CD1  1 
ATOM   260   C  CD2  . PHE   A  1  19  ? 7.343   -8.161  -27.440  1.00 66.66  ? 19   PHE   A CD2  1 
ATOM   261   C  CE1  . PHE   A  1  19  ? 9.147   -6.423  -26.283  1.00 66.49  ? 19   PHE   A CE1  1 
ATOM   262   C  CE2  . PHE   A  1  19  ? 8.035   -7.258  -28.228  1.00 67.36  ? 19   PHE   A CE2  1 
ATOM   263   C  CZ   . PHE   A  1  19  ? 8.937   -6.387  -27.648  1.00 66.95  ? 19   PHE   A CZ   1 
ATOM   264   H  H    . PHE   A  1  19  ? 5.994   -10.994 -23.824  1.00 77.79  ? 19   PHE   A H    1 
ATOM   265   H  HA   . PHE   A  1  19  ? 7.590   -10.957 -25.863  1.00 76.60  ? 19   PHE   A HA   1 
ATOM   266   H  HB2  . PHE   A  1  19  ? 5.936   -9.356  -25.647  1.00 80.35  ? 19   PHE   A HB2  1 
ATOM   267   H  HB3  . PHE   A  1  19  ? 6.643   -8.770  -24.350  1.00 80.35  ? 19   PHE   A HB3  1 
ATOM   268   H  HD1  . PHE   A  1  19  ? 8.593   -7.343  -24.582  1.00 80.52  ? 19   PHE   A HD1  1 
ATOM   269   H  HD2  . PHE   A  1  19  ? 6.733   -8.742  -27.834  1.00 79.98  ? 19   PHE   A HD2  1 
ATOM   270   H  HE1  . PHE   A  1  19  ? 9.756   -5.840  -25.890  1.00 79.77  ? 19   PHE   A HE1  1 
ATOM   271   H  HE2  . PHE   A  1  19  ? 7.893   -7.238  -29.147  1.00 80.81  ? 19   PHE   A HE2  1 
ATOM   272   H  HZ   . PHE   A  1  19  ? 9.402   -5.778  -28.176  1.00 80.32  ? 19   PHE   A HZ   1 
ATOM   273   N  N    . GLY   A  1  20  ? 9.914   -10.751 -25.159  1.00 58.00  ? 20   GLY   A N    1 
ATOM   274   C  CA   . GLY   A  1  20  ? 11.288  -10.682 -24.703  1.00 56.58  ? 20   GLY   A CA   1 
ATOM   275   C  C    . GLY   A  1  20  ? 11.889  -12.017 -24.322  1.00 55.53  ? 20   GLY   A C    1 
ATOM   276   O  O    . GLY   A  1  20  ? 13.053  -12.056 -23.906  1.00 50.88  ? 20   GLY   A O    1 
ATOM   277   H  H    . GLY   A  1  20  ? 9.827   -11.108 -25.936  1.00 69.58  ? 20   GLY   A H    1 
ATOM   278   H  HA2  . GLY   A  1  20  ? 11.833  -10.301 -25.409  1.00 67.87  ? 20   GLY   A HA2  1 
ATOM   279   H  HA3  . GLY   A  1  20  ? 11.331  -10.104 -23.925  1.00 67.87  ? 20   GLY   A HA3  1 
ATOM   280   N  N    . PHE   A  1  21  ? 11.133  -13.111 -24.443  1.00 56.67  ? 21   PHE   A N    1 
ATOM   281   C  CA   . PHE   A  1  21  ? 11.680  -14.431 -24.149  1.00 57.12  ? 21   PHE   A CA   1 
ATOM   282   C  C    . PHE   A  1  21  ? 12.861  -14.752 -25.055  1.00 55.91  ? 21   PHE   A C    1 
ATOM   283   O  O    . PHE   A  1  21  ? 13.769  -15.491 -24.658  1.00 54.25  ? 21   PHE   A O    1 
ATOM   284   C  CB   . PHE   A  1  21  ? 10.582  -15.484 -24.300  1.00 57.69  ? 21   PHE   A CB   1 
ATOM   285   C  CG   . PHE   A  1  21  ? 10.970  -16.847 -23.806  1.00 54.33  ? 21   PHE   A CG   1 
ATOM   286   C  CD1  . PHE   A  1  21  ? 10.859  -17.169 -22.464  1.00 54.99  ? 21   PHE   A CD1  1 
ATOM   287   C  CD2  . PHE   A  1  21  ? 11.433  -17.811 -24.685  1.00 53.98  ? 21   PHE   A CD2  1 
ATOM   288   C  CE1  . PHE   A  1  21  ? 11.211  -18.423 -22.006  1.00 53.45  ? 21   PHE   A CE1  1 
ATOM   289   C  CE2  . PHE   A  1  21  ? 11.786  -19.069 -24.234  1.00 53.58  ? 21   PHE   A CE2  1 
ATOM   290   C  CZ   . PHE   A  1  21  ? 11.675  -19.375 -22.893  1.00 51.67  ? 21   PHE   A CZ   1 
ATOM   291   H  H    . PHE   A  1  21  ? 10.309  -13.114 -24.690  1.00 67.99  ? 21   PHE   A H    1 
ATOM   292   H  HA   . PHE   A  1  21  ? 11.996  -14.454 -23.232  1.00 68.53  ? 21   PHE   A HA   1 
ATOM   293   H  HB2  . PHE   A  1  21  ? 9.805   -15.197 -23.795  1.00 69.21  ? 21   PHE   A HB2  1 
ATOM   294   H  HB3  . PHE   A  1  21  ? 10.355  -15.565 -25.240  1.00 69.21  ? 21   PHE   A HB3  1 
ATOM   295   H  HD1  . PHE   A  1  21  ? 10.544  -16.532 -21.863  1.00 65.97  ? 21   PHE   A HD1  1 
ATOM   296   H  HD2  . PHE   A  1  21  ? 11.507  -17.610 -25.590  1.00 64.76  ? 21   PHE   A HD2  1 
ATOM   297   H  HE1  . PHE   A  1  21  ? 11.136  -18.627 -21.102  1.00 64.12  ? 21   PHE   A HE1  1 
ATOM   298   H  HE2  . PHE   A  1  21  ? 12.099  -19.708 -24.833  1.00 64.28  ? 21   PHE   A HE2  1 
ATOM   299   H  HZ   . PHE   A  1  21  ? 11.912  -20.221 -22.587  1.00 61.98  ? 21   PHE   A HZ   1 
ATOM   300   N  N    . ALA   A  1  22  ? 12.867  -14.203 -26.268  1.00 55.61  ? 22   ALA   A N    1 
ATOM   301   C  CA   . ALA   A  1  22  ? 13.969  -14.355 -27.206  1.00 56.79  ? 22   ALA   A CA   1 
ATOM   302   C  C    . ALA   A  1  22  ? 14.209  -13.016 -27.886  1.00 56.35  ? 22   ALA   A C    1 
ATOM   303   O  O    . ALA   A  1  22  ? 13.257  -12.297 -28.204  1.00 56.92  ? 22   ALA   A O    1 
ATOM   304   C  CB   . ALA   A  1  22  ? 13.673  -15.434 -28.253  1.00 53.65  ? 22   ALA   A CB   1 
ATOM   305   H  H    . ALA   A  1  22  ? 12.223  -13.725 -26.578  1.00 66.72  ? 22   ALA   A H    1 
ATOM   306   H  HA   . ALA   A  1  22  ? 14.776  -14.614 -26.734  1.00 68.12  ? 22   ALA   A HA   1 
ATOM   307   H  HB1  . ALA   A  1  22  ? 14.432  -15.510 -28.852  1.00 64.37  ? 22   ALA   A HB1  1 
ATOM   308   H  HB2  . ALA   A  1  22  ? 13.522  -16.279 -27.801  1.00 64.37  ? 22   ALA   A HB2  1 
ATOM   309   H  HB3  . ALA   A  1  22  ? 12.881  -15.181 -28.753  1.00 64.37  ? 22   ALA   A HB3  1 
ATOM   310   N  N    . VAL   A  1  23  ? 15.480  -12.681 -28.104  1.00 53.23  ? 23   VAL   A N    1 
ATOM   311   C  CA   . VAL   A  1  23  ? 15.854  -11.418 -28.727  1.00 56.55  ? 23   VAL   A CA   1 
ATOM   312   C  C    . VAL   A  1  23  ? 16.995  -11.654 -29.704  1.00 58.56  ? 23   VAL   A C    1 
ATOM   313   O  O    . VAL   A  1  23  ? 17.860  -12.509 -29.486  1.00 62.36  ? 23   VAL   A O    1 
ATOM   314   C  CB   . VAL   A  1  23  ? 16.258  -10.353 -27.680  1.00 55.78  ? 23   VAL   A CB   1 
ATOM   315   C  CG1  . VAL   A  1  23  ? 15.039  -9.885  -26.900  1.00 56.14  ? 23   VAL   A CG1  1 
ATOM   316   C  CG2  . VAL   A  1  23  ? 17.326  -10.901 -26.738  1.00 54.44  ? 23   VAL   A CG2  1 
ATOM   317   H  H    . VAL   A  1  23  ? 16.151  -13.178 -27.896  1.00 63.86  ? 23   VAL   A H    1 
ATOM   318   H  HA   . VAL   A  1  23  ? 15.092  -11.085 -29.228  1.00 67.84  ? 23   VAL   A HA   1 
ATOM   319   H  HB   . VAL   A  1  23  ? 16.633  -9.587  -28.142  1.00 66.92  ? 23   VAL   A HB   1 
ATOM   320   H  HG11 . VAL   A  1  23  ? 15.305  -9.172  -26.298  1.00 67.35  ? 23   VAL   A HG11 1 
ATOM   321   H  HG12 . VAL   A  1  23  ? 14.371  -9.560  -27.524  1.00 67.35  ? 23   VAL   A HG12 1 
ATOM   322   H  HG13 . VAL   A  1  23  ? 14.683  -10.631 -26.393  1.00 67.35  ? 23   VAL   A HG13 1 
ATOM   323   H  HG21 . VAL   A  1  23  ? 17.575  -10.208 -26.106  1.00 65.30  ? 23   VAL   A HG21 1 
ATOM   324   H  HG22 . VAL   A  1  23  ? 16.966  -11.667 -26.264  1.00 65.30  ? 23   VAL   A HG22 1 
ATOM   325   H  HG23 . VAL   A  1  23  ? 18.100  -11.167 -27.258  1.00 65.30  ? 23   VAL   A HG23 1 
ATOM   326   N  N    . ASP   A  1  24  ? 16.990  -10.888 -30.793  1.00 59.39  ? 24   ASP   A N    1 
ATOM   327   C  CA   . ASP   A  1  24  ? 18.084  -10.916 -31.754  1.00 60.82  ? 24   ASP   A CA   1 
ATOM   328   C  C    . ASP   A  1  24  ? 18.080  -9.611  -32.539  1.00 58.82  ? 24   ASP   A C    1 
ATOM   329   O  O    . ASP   A  1  24  ? 17.159  -8.798  -32.431  1.00 56.67  ? 24   ASP   A O    1 
ATOM   330   C  CB   . ASP   A  1  24  ? 17.974  -12.118 -32.697  1.00 60.76  ? 24   ASP   A CB   1 
ATOM   331   C  CG   . ASP   A  1  24  ? 19.291  -12.450 -33.366  1.00 66.24  ? 24   ASP   A CG   1 
ATOM   332   O  OD1  . ASP   A  1  24  ? 20.232  -11.637 -33.264  1.00 71.00  ? 24   ASP   A OD1  1 
ATOM   333   O  OD2  . ASP   A  1  24  ? 19.389  -13.526 -33.988  1.00 69.33  ? 24   ASP   A OD2  1 
ATOM   334   H  H    . ASP   A  1  24  ? 16.358  -10.341 -30.997  1.00 71.25  ? 24   ASP   A H    1 
ATOM   335   H  HA   . ASP   A  1  24  ? 18.922  -10.980 -31.271  1.00 72.96  ? 24   ASP   A HA   1 
ATOM   336   H  HB2  . ASP   A  1  24  ? 17.690  -12.894 -32.190  1.00 72.89  ? 24   ASP   A HB2  1 
ATOM   337   H  HB3  . ASP   A  1  24  ? 17.326  -11.919 -33.391  1.00 72.89  ? 24   ASP   A HB3  1 
ATOM   338   N  N    . PHE   A  1  25  ? 19.136  -9.419  -33.325  1.00 59.14  ? 25   PHE   A N    1 
ATOM   339   C  CA   . PHE   A  1  25  ? 19.259  -8.295  -34.241  1.00 62.85  ? 25   PHE   A CA   1 
ATOM   340   C  C    . PHE   A  1  25  ? 18.851  -8.722  -35.646  1.00 65.67  ? 25   PHE   A C    1 
ATOM   341   O  O    . PHE   A  1  25  ? 18.947  -9.897  -36.006  1.00 64.13  ? 25   PHE   A O    1 
ATOM   342   C  CB   . PHE   A  1  25  ? 20.695  -7.764  -34.269  1.00 63.26  ? 25   PHE   A CB   1 
ATOM   343   C  CG   . PHE   A  1  25  ? 21.065  -6.925  -33.077  1.00 63.13  ? 25   PHE   A CG   1 
ATOM   344   C  CD1  . PHE   A  1  25  ? 20.783  -5.570  -33.056  1.00 65.14  ? 25   PHE   A CD1  1 
ATOM   345   C  CD2  . PHE   A  1  25  ? 21.716  -7.486  -31.990  1.00 61.88  ? 25   PHE   A CD2  1 
ATOM   346   C  CE1  . PHE   A  1  25  ? 21.131  -4.790  -31.967  1.00 65.49  ? 25   PHE   A CE1  1 
ATOM   347   C  CE2  . PHE   A  1  25  ? 22.067  -6.710  -30.898  1.00 62.02  ? 25   PHE   A CE2  1 
ATOM   348   C  CZ   . PHE   A  1  25  ? 21.776  -5.361  -30.889  1.00 64.56  ? 25   PHE   A CZ   1 
ATOM   349   H  H    . PHE   A  1  25  ? 19.816  -9.945  -33.344  1.00 70.94  ? 25   PHE   A H    1 
ATOM   350   H  HA   . PHE   A  1  25  ? 18.675  -7.577  -33.949  1.00 75.40  ? 25   PHE   A HA   1 
ATOM   351   H  HB2  . PHE   A  1  25  ? 21.304  -8.519  -34.298  1.00 75.90  ? 25   PHE   A HB2  1 
ATOM   352   H  HB3  . PHE   A  1  25  ? 20.807  -7.216  -35.061  1.00 75.90  ? 25   PHE   A HB3  1 
ATOM   353   H  HD1  . PHE   A  1  25  ? 20.354  -5.179  -33.782  1.00 78.15  ? 25   PHE   A HD1  1 
ATOM   354   H  HD2  . PHE   A  1  25  ? 21.918  -8.394  -31.993  1.00 74.24  ? 25   PHE   A HD2  1 
ATOM   355   H  HE1  . PHE   A  1  25  ? 20.931  -3.882  -31.962  1.00 78.57  ? 25   PHE   A HE1  1 
ATOM   356   H  HE2  . PHE   A  1  25  ? 22.499  -7.098  -30.171  1.00 74.40  ? 25   PHE   A HE2  1 
ATOM   357   H  HZ   . PHE   A  1  25  ? 22.014  -4.837  -30.158  1.00 77.45  ? 25   PHE   A HZ   1 
ATOM   358   N  N    . PHE   A  1  26  ? 18.398  -7.755  -36.442  1.00 69.33  ? 26   PHE   A N    1 
ATOM   359   C  CA   . PHE   A  1  26  ? 18.056  -7.985  -37.842  1.00 69.72  ? 26   PHE   A CA   1 
ATOM   360   C  C    . PHE   A  1  26  ? 18.859  -7.024  -38.707  1.00 72.89  ? 26   PHE   A C    1 
ATOM   361   O  O    . PHE   A  1  26  ? 18.786  -5.805  -38.517  1.00 72.83  ? 26   PHE   A O    1 
ATOM   362   C  CB   . PHE   A  1  26  ? 16.558  -7.800  -38.091  1.00 72.95  ? 26   PHE   A CB   1 
ATOM   363   C  CG   . PHE   A  1  26  ? 16.115  -8.203  -39.476  1.00 73.52  ? 26   PHE   A CG   1 
ATOM   364   C  CD1  . PHE   A  1  26  ? 16.765  -9.217  -40.164  1.00 71.21  ? 26   PHE   A CD1  1 
ATOM   365   C  CD2  . PHE   A  1  26  ? 15.054  -7.561  -40.092  1.00 74.37  ? 26   PHE   A CD2  1 
ATOM   366   C  CE1  . PHE   A  1  26  ? 16.361  -9.586  -41.434  1.00 70.83  ? 26   PHE   A CE1  1 
ATOM   367   C  CE2  . PHE   A  1  26  ? 14.646  -7.926  -41.364  1.00 73.63  ? 26   PHE   A CE2  1 
ATOM   368   C  CZ   . PHE   A  1  26  ? 15.303  -8.939  -42.035  1.00 72.31  ? 26   PHE   A CZ   1 
ATOM   369   H  H    . PHE   A  1  26  ? 18.279  -6.942  -36.188  1.00 83.18  ? 26   PHE   A H    1 
ATOM   370   H  HA   . PHE   A  1  26  ? 18.295  -8.894  -38.082  1.00 83.64  ? 26   PHE   A HA   1 
ATOM   371   H  HB2  . PHE   A  1  26  ? 16.067  -8.343  -37.454  1.00 87.52  ? 26   PHE   A HB2  1 
ATOM   372   H  HB3  . PHE   A  1  26  ? 16.335  -6.864  -37.970  1.00 87.52  ? 26   PHE   A HB3  1 
ATOM   373   H  HD1  . PHE   A  1  26  ? 17.482  -9.655  -39.766  1.00 85.43  ? 26   PHE   A HD1  1 
ATOM   374   H  HD2  . PHE   A  1  26  ? 14.610  -6.876  -39.646  1.00 89.23  ? 26   PHE   A HD2  1 
ATOM   375   H  HE1  . PHE   A  1  26  ? 16.803  -10.270 -41.883  1.00 84.98  ? 26   PHE   A HE1  1 
ATOM   376   H  HE2  . PHE   A  1  26  ? 13.930  -7.490  -41.765  1.00 88.34  ? 26   PHE   A HE2  1 
ATOM   377   H  HZ   . PHE   A  1  26  ? 15.032  -9.183  -42.891  1.00 86.75  ? 26   PHE   A HZ   1 
ATOM   378   N  N    . VAL   A  1  27  ? 19.614  -7.572  -39.655  1.00 76.14  ? 27   VAL   A N    1 
ATOM   379   C  CA   . VAL   A  1  27  ? 20.444  -6.772  -40.552  1.00 80.64  ? 27   VAL   A CA   1 
ATOM   380   C  C    . VAL   A  1  27  ? 20.102  -7.112  -41.998  1.00 77.73  ? 27   VAL   A C    1 
ATOM   381   O  O    . VAL   A  1  27  ? 20.813  -7.906  -42.630  1.00 68.62  ? 27   VAL   A O    1 
ATOM   382   C  CB   . VAL   A  1  27  ? 21.941  -6.994  -40.273  1.00 88.29  ? 27   VAL   A CB   1 
ATOM   383   C  CG1  . VAL   A  1  27  ? 22.358  -6.246  -39.019  1.00 86.29  ? 27   VAL   A CG1  1 
ATOM   384   C  CG2  . VAL   A  1  27  ? 22.258  -8.482  -40.141  1.00 93.51  ? 27   VAL   A CG2  1 
ATOM   385   H  H    . VAL   A  1  27  ? 19.663  -8.418  -39.801  1.00 91.35  ? 27   VAL   A H    1 
ATOM   386   H  HA   . VAL   A  1  27  ? 20.239  -5.835  -40.407  1.00 96.75  ? 27   VAL   A HA   1 
ATOM   387   H  HB   . VAL   A  1  27  ? 22.451  -6.648  -41.022  1.00 105.93 ? 27   VAL   A HB   1 
ATOM   388   H  HG11 . VAL   A  1  27  ? 23.290  -6.438  -38.832  1.00 103.53 ? 27   VAL   A HG11 1 
ATOM   389   H  HG12 . VAL   A  1  27  ? 22.238  -5.295  -39.164  1.00 103.53 ? 27   VAL   A HG12 1 
ATOM   390   H  HG13 . VAL   A  1  27  ? 21.805  -6.540  -38.278  1.00 103.53 ? 27   VAL   A HG13 1 
ATOM   391   H  HG21 . VAL   A  1  27  ? 23.211  -8.590  -39.998  1.00 112.20 ? 27   VAL   A HG21 1 
ATOM   392   H  HG22 . VAL   A  1  27  ? 21.767  -8.844  -39.387  1.00 112.20 ? 27   VAL   A HG22 1 
ATOM   393   H  HG23 . VAL   A  1  27  ? 21.992  -8.935  -40.956  1.00 112.20 ? 27   VAL   A HG23 1 
ATOM   394   N  N    . PRO   A  1  28  ? 19.037  -6.543  -42.562  1.00 88.60  ? 28   PRO   A N    1 
ATOM   395   C  CA   . PRO   A  1  28  ? 18.725  -6.802  -43.972  1.00 95.69  ? 28   PRO   A CA   1 
ATOM   396   C  C    . PRO   A  1  28  ? 19.948  -6.587  -44.853  1.00 102.67 ? 28   PRO   A C    1 
ATOM   397   O  O    . PRO   A  1  28  ? 20.725  -5.651  -44.653  1.00 103.11 ? 28   PRO   A O    1 
ATOM   398   C  CB   . PRO   A  1  28  ? 17.614  -5.791  -44.279  1.00 99.89  ? 28   PRO   A CB   1 
ATOM   399   C  CG   . PRO   A  1  28  ? 16.975  -5.523  -42.958  1.00 97.80  ? 28   PRO   A CG   1 
ATOM   400   C  CD   . PRO   A  1  28  ? 18.077  -5.614  -41.940  1.00 92.83  ? 28   PRO   A CD   1 
ATOM   401   H  HA   . PRO   A  1  28  ? 18.387  -7.703  -44.095  1.00 114.81 ? 28   PRO   A HA   1 
ATOM   402   H  HB2  . PRO   A  1  28  ? 17.997  -4.981  -44.653  1.00 119.85 ? 28   PRO   A HB2  1 
ATOM   403   H  HB3  . PRO   A  1  28  ? 16.979  -6.175  -44.903  1.00 119.85 ? 28   PRO   A HB3  1 
ATOM   404   H  HG2  . PRO   A  1  28  ? 16.582  -4.636  -42.960  1.00 117.34 ? 28   PRO   A HG2  1 
ATOM   405   H  HG3  . PRO   A  1  28  ? 16.292  -6.189  -42.785  1.00 117.34 ? 28   PRO   A HG3  1 
ATOM   406   H  HD2  . PRO   A  1  28  ? 18.483  -4.745  -41.793  1.00 111.37 ? 28   PRO   A HD2  1 
ATOM   407   H  HD3  . PRO   A  1  28  ? 17.743  -5.971  -41.102  1.00 111.37 ? 28   PRO   A HD3  1 
ATOM   408   N  N    . SER   A  1  29  ? 20.118  -7.471  -45.838  1.00 109.78 ? 29   SER   A N    1 
ATOM   409   C  CA   . SER   A  1  29  ? 21.327  -7.489  -46.662  1.00 118.19 ? 29   SER   A CA   1 
ATOM   410   C  C    . SER   A  1  29  ? 21.225  -6.483  -47.811  1.00 123.51 ? 29   SER   A C    1 
ATOM   411   O  O    . SER   A  1  29  ? 21.335  -6.813  -48.991  1.00 125.80 ? 29   SER   A O    1 
ATOM   412   C  CB   . SER   A  1  29  ? 21.583  -8.897  -47.184  1.00 120.79 ? 29   SER   A CB   1 
ATOM   413   O  OG   . SER   A  1  29  ? 22.789  -8.951  -47.927  1.00 123.90 ? 29   SER   A OG   1 
ATOM   414   H  H    . SER   A  1  29  ? 19.543  -8.075  -46.049  1.00 131.71 ? 29   SER   A H    1 
ATOM   415   H  HA   . SER   A  1  29  ? 22.077  -7.226  -46.105  1.00 141.80 ? 29   SER   A HA   1 
ATOM   416   H  HB2  . SER   A  1  29  ? 21.649  -9.505  -46.431  1.00 144.92 ? 29   SER   A HB2  1 
ATOM   417   H  HB3  . SER   A  1  29  ? 20.847  -9.158  -47.759  1.00 144.92 ? 29   SER   A HB3  1 
ATOM   418   H  HG   . SER   A  1  29  ? 22.730  -8.462  -48.607  1.00 148.66 ? 29   SER   A HG   1 
ATOM   419   N  N    . ALA   A  1  30  ? 20.994  -5.224  -47.434  1.00 125.57 ? 30   ALA   A N    1 
ATOM   420   C  CA   . ALA   A  1  30  ? 21.095  -4.115  -48.374  1.00 129.16 ? 30   ALA   A CA   1 
ATOM   421   C  C    . ALA   A  1  30  ? 21.726  -2.891  -47.716  1.00 139.75 ? 30   ALA   A C    1 
ATOM   422   O  O    . ALA   A  1  30  ? 21.543  -1.770  -48.209  1.00 147.94 ? 30   ALA   A O    1 
ATOM   423   C  CB   . ALA   A  1  30  ? 19.720  -3.754  -48.945  1.00 122.96 ? 30   ALA   A CB   1 
ATOM   424   H  H    . ALA   A  1  30  ? 20.777  -4.988  -46.636  1.00 150.67 ? 30   ALA   A H    1 
ATOM   425   H  HA   . ALA   A  1  30  ? 21.657  -4.379  -49.119  1.00 154.97 ? 30   ALA   A HA   1 
ATOM   426   H  HB1  . ALA   A  1  30  ? 19.809  -2.972  -49.511  1.00 147.53 ? 30   ALA   A HB1  1 
ATOM   427   H  HB2  . ALA   A  1  30  ? 19.388  -4.502  -49.464  1.00 147.53 ? 30   ALA   A HB2  1 
ATOM   428   H  HB3  . ALA   A  1  30  ? 19.114  -3.564  -48.212  1.00 147.53 ? 30   ALA   A HB3  1 
ATOM   429   N  N    . SER   A  1  31  ? 22.466  -3.078  -46.621  1.00 137.55 ? 31   SER   A N    1 
ATOM   430   C  CA   . SER   A  1  31  ? 22.956  -1.965  -45.808  1.00 134.00 ? 31   SER   A CA   1 
ATOM   431   C  C    . SER   A  1  31  ? 21.808  -1.039  -45.418  1.00 132.06 ? 31   SER   A C    1 
ATOM   432   O  O    . SER   A  1  31  ? 21.988  0.169   -45.246  1.00 131.27 ? 31   SER   A O    1 
ATOM   433   C  CB   . SER   A  1  31  ? 24.057  -1.190  -46.535  1.00 132.37 ? 31   SER   A CB   1 
ATOM   434   O  OG   . SER   A  1  31  ? 23.604  -0.700  -47.785  1.00 130.37 ? 31   SER   A OG   1 
ATOM   435   H  H    . SER   A  1  31  ? 22.700  -3.851  -46.324  1.00 165.04 ? 31   SER   A H    1 
ATOM   436   H  HA   . SER   A  1  31  ? 23.342  -2.321  -44.993  1.00 160.78 ? 31   SER   A HA   1 
ATOM   437   H  HB2  . SER   A  1  31  ? 24.329  -0.439  -45.983  1.00 158.82 ? 31   SER   A HB2  1 
ATOM   438   H  HB3  . SER   A  1  31  ? 24.811  -1.781  -46.684  1.00 158.82 ? 31   SER   A HB3  1 
ATOM   439   H  HG   . SER   A  1  31  ? 22.824  -0.397  -47.709  1.00 156.42 ? 31   SER   A HG   1 
ATOM   440   N  N    . SER   A  1  32  ? 20.617  -1.614  -45.274  1.00 129.76 ? 32   SER   A N    1 
ATOM   441   C  CA   . SER   A  1  32  ? 19.410  -0.854  -44.991  1.00 127.88 ? 32   SER   A CA   1 
ATOM   442   C  C    . SER   A  1  32  ? 19.327  -0.552  -43.497  1.00 124.75 ? 32   SER   A C    1 
ATOM   443   O  O    . SER   A  1  32  ? 20.287  -0.729  -42.741  1.00 127.11 ? 32   SER   A O    1 
ATOM   444   C  CB   . SER   A  1  32  ? 18.179  -1.621  -45.469  1.00 124.30 ? 32   SER   A CB   1 
ATOM   445   O  OG   . SER   A  1  32  ? 18.263  -1.918  -46.849  1.00 123.91 ? 32   SER   A OG   1 
ATOM   446   H  H    . SER   A  1  32  ? 20.482  -2.461  -45.338  1.00 155.70 ? 32   SER   A H    1 
ATOM   447   H  HA   . SER   A  1  32  ? 19.469  -0.016  -45.476  1.00 153.43 ? 32   SER   A HA   1 
ATOM   448   H  HB2  . SER   A  1  32  ? 18.115  -2.452  -44.972  1.00 149.14 ? 32   SER   A HB2  1 
ATOM   449   H  HB3  . SER   A  1  32  ? 17.391  -1.078  -45.311  1.00 149.14 ? 32   SER   A HB3  1 
ATOM   450   H  HG   . SER   A  1  32  ? 17.619  -2.407  -47.077  1.00 148.68 ? 32   SER   A HG   1 
ATOM   451   N  N    . ARG   A  1  33  ? 18.161  -0.085  -43.059  1.00 116.36 ? 33   ARG   A N    1 
ATOM   452   C  CA   . ARG   A  1  33  ? 17.920  0.116   -41.641  1.00 103.27 ? 33   ARG   A CA   1 
ATOM   453   C  C    . ARG   A  1  33  ? 18.129  -1.196  -40.890  1.00 92.68  ? 33   ARG   A C    1 
ATOM   454   O  O    . ARG   A  1  33  ? 18.106  -2.287  -41.468  1.00 87.65  ? 33   ARG   A O    1 
ATOM   455   C  CB   . ARG   A  1  33  ? 16.499  0.630   -41.398  1.00 99.04  ? 33   ARG   A CB   1 
ATOM   456   C  CG   . ARG   A  1  33  ? 15.978  1.606   -42.450  1.00 99.54  ? 33   ARG   A CG   1 
ATOM   457   C  CD   . ARG   A  1  33  ? 14.575  2.096   -42.130  1.00 100.21 ? 33   ARG   A CD   1 
ATOM   458   N  NE   . ARG   A  1  33  ? 13.853  2.462   -43.346  1.00 103.69 ? 33   ARG   A NE   1 
ATOM   459   C  CZ   . ARG   A  1  33  ? 14.080  3.566   -44.051  1.00 107.37 ? 33   ARG   A CZ   1 
ATOM   460   N  NH1  . ARG   A  1  33  ? 13.372  3.809   -45.144  1.00 109.22 ? 33   ARG   A NH1  1 
ATOM   461   N  NH2  . ARG   A  1  33  ? 15.015  4.426   -43.669  1.00 107.65 ? 33   ARG   A NH2  1 
ATOM   462   H  H    . ARG   A  1  33  ? 17.497  0.122   -43.565  1.00 139.61 ? 33   ARG   A H    1 
ATOM   463   H  HA   . ARG   A  1  33  ? 18.539  0.779   -41.299  1.00 123.91 ? 33   ARG   A HA   1 
ATOM   464   H  HB2  . ARG   A  1  33  ? 15.896  -0.129  -41.381  1.00 118.83 ? 33   ARG   A HB2  1 
ATOM   465   H  HB3  . ARG   A  1  33  ? 16.480  1.087   -40.542  1.00 118.83 ? 33   ARG   A HB3  1 
ATOM   466   H  HG2  . ARG   A  1  33  ? 16.566  2.377   -42.488  1.00 119.43 ? 33   ARG   A HG2  1 
ATOM   467   H  HG3  . ARG   A  1  33  ? 15.955  1.163   -43.312  1.00 119.43 ? 33   ARG   A HG3  1 
ATOM   468   H  HD2  . ARG   A  1  33  ? 14.082  1.391   -41.682  1.00 120.23 ? 33   ARG   A HD2  1 
ATOM   469   H  HD3  . ARG   A  1  33  ? 14.629  2.878   -41.559  1.00 120.23 ? 33   ARG   A HD3  1 
ATOM   470   H  HE   . ARG   A  1  33  ? 13.240  1.928   -43.624  1.00 124.41 ? 33   ARG   A HE   1 
ATOM   471   H  HH11 . ARG   A  1  33  ? 12.766  3.253   -45.397  1.00 131.04 ? 33   ARG   A HH11 1 
ATOM   472   H  HH12 . ARG   A  1  33  ? 13.517  4.523   -45.601  1.00 131.04 ? 33   ARG   A HH12 1 
ATOM   473   H  HH21 . ARG   A  1  33  ? 15.480  4.270   -42.963  1.00 129.16 ? 33   ARG   A HH21 1 
ATOM   474   H  HH22 . ARG   A  1  33  ? 15.158  5.138   -44.129  1.00 129.16 ? 33   ARG   A HH22 1 
ATOM   475   N  N    . MET   A  1  34  ? 18.336  -1.080  -39.584  1.00 87.82  ? 34   MET   A N    1 
ATOM   476   C  CA   . MET   A  1  34  ? 18.455  -2.231  -38.705  1.00 81.21  ? 34   MET   A CA   1 
ATOM   477   C  C    . MET   A  1  34  ? 17.264  -2.266  -37.758  1.00 74.53  ? 34   MET   A C    1 
ATOM   478   O  O    . MET   A  1  34  ? 16.678  -1.229  -37.432  1.00 75.65  ? 34   MET   A O    1 
ATOM   479   C  CB   . MET   A  1  34  ? 19.763  -2.188  -37.913  1.00 86.32  ? 34   MET   A CB   1 
ATOM   480   C  CG   . MET   A  1  34  ? 21.004  -2.321  -38.783  1.00 92.78  ? 34   MET   A CG   1 
ATOM   481   S  SD   . MET   A  1  34  ? 22.536  -2.114  -37.858  1.00 100.07 ? 34   MET   A SD   1 
ATOM   482   C  CE   . MET   A  1  34  ? 23.751  -2.424  -39.137  1.00 104.06 ? 34   MET   A CE   1 
ATOM   483   H  H    . MET   A  1  34  ? 18.413  -0.327  -39.177  1.00 105.36 ? 34   MET   A H    1 
ATOM   484   H  HA   . MET   A  1  34  ? 18.465  -3.046  -39.232  1.00 97.43  ? 34   MET   A HA   1 
ATOM   485   H  HB2  . MET   A  1  34  ? 19.817  -1.340  -37.445  1.00 103.56 ? 34   MET   A HB2  1 
ATOM   486   H  HB3  . MET   A  1  34  ? 19.767  -2.920  -37.276  1.00 103.56 ? 34   MET   A HB3  1 
ATOM   487   H  HG2  . MET   A  1  34  ? 21.014  -3.203  -39.185  1.00 111.32 ? 34   MET   A HG2  1 
ATOM   488   H  HG3  . MET   A  1  34  ? 20.978  -1.641  -39.474  1.00 111.32 ? 34   MET   A HG3  1 
ATOM   489   H  HE1  . MET   A  1  34  ? 24.639  -2.361  -38.751  1.00 124.85 ? 34   MET   A HE1  1 
ATOM   490   H  HE2  . MET   A  1  34  ? 23.610  -3.314  -39.497  1.00 124.85 ? 34   MET   A HE2  1 
ATOM   491   H  HE3  . MET   A  1  34  ? 23.647  -1.763  -39.838  1.00 124.85 ? 34   MET   A HE3  1 
ATOM   492   N  N    . PHE   A  1  35  ? 16.907  -3.471  -37.326  1.00 68.02  ? 35   PHE   A N    1 
ATOM   493   C  CA   . PHE   A  1  35  ? 15.742  -3.688  -36.486  1.00 65.47  ? 35   PHE   A CA   1 
ATOM   494   C  C    . PHE   A  1  35  ? 16.105  -4.621  -35.341  1.00 65.20  ? 35   PHE   A C    1 
ATOM   495   O  O    . PHE   A  1  35  ? 17.196  -5.197  -35.295  1.00 63.53  ? 35   PHE   A O    1 
ATOM   496   C  CB   . PHE   A  1  35  ? 14.576  -4.283  -37.288  1.00 64.93  ? 35   PHE   A CB   1 
ATOM   497   C  CG   . PHE   A  1  35  ? 14.212  -3.490  -38.508  1.00 70.26  ? 35   PHE   A CG   1 
ATOM   498   C  CD1  . PHE   A  1  35  ? 14.907  -3.662  -39.693  1.00 74.67  ? 35   PHE   A CD1  1 
ATOM   499   C  CD2  . PHE   A  1  35  ? 13.170  -2.580  -38.473  1.00 74.81  ? 35   PHE   A CD2  1 
ATOM   500   C  CE1  . PHE   A  1  35  ? 14.574  -2.936  -40.819  1.00 80.71  ? 35   PHE   A CE1  1 
ATOM   501   C  CE2  . PHE   A  1  35  ? 12.831  -1.850  -39.596  1.00 81.66  ? 35   PHE   A CE2  1 
ATOM   502   C  CZ   . PHE   A  1  35  ? 13.534  -2.029  -40.771  1.00 84.45  ? 35   PHE   A CZ   1 
ATOM   503   H  H    . PHE   A  1  35  ? 17.336  -4.193  -37.512  1.00 81.60  ? 35   PHE   A H    1 
ATOM   504   H  HA   . PHE   A  1  35  ? 15.461  -2.838  -36.113  1.00 78.54  ? 35   PHE   A HA   1 
ATOM   505   H  HB2  . PHE   A  1  35  ? 14.820  -5.176  -37.578  1.00 77.90  ? 35   PHE   A HB2  1 
ATOM   506   H  HB3  . PHE   A  1  35  ? 13.793  -4.322  -36.717  1.00 77.90  ? 35   PHE   A HB3  1 
ATOM   507   H  HD1  . PHE   A  1  35  ? 15.606  -4.274  -39.731  1.00 89.59  ? 35   PHE   A HD1  1 
ATOM   508   H  HD2  . PHE   A  1  35  ? 12.693  -2.457  -37.684  1.00 89.76  ? 35   PHE   A HD2  1 
ATOM   509   H  HE1  . PHE   A  1  35  ? 15.049  -3.058  -41.609  1.00 96.83  ? 35   PHE   A HE1  1 
ATOM   510   H  HE2  . PHE   A  1  35  ? 12.130  -1.240  -39.561  1.00 97.97  ? 35   PHE   A HE2  1 
ATOM   511   H  HZ   . PHE   A  1  35  ? 13.307  -1.539  -41.528  1.00 101.32 ? 35   PHE   A HZ   1 
ATOM   512   N  N    . LEU   A  1  36  ? 15.170  -4.761  -34.408  1.00 68.04  ? 36   LEU   A N    1 
ATOM   513   C  CA   . LEU   A  1  36  ? 15.259  -5.740  -33.337  1.00 68.68  ? 36   LEU   A CA   1 
ATOM   514   C  C    . LEU   A  1  36  ? 14.205  -6.815  -33.559  1.00 68.96  ? 36   LEU   A C    1 
ATOM   515   O  O    . LEU   A  1  36  ? 13.067  -6.513  -33.931  1.00 75.27  ? 36   LEU   A O    1 
ATOM   516   C  CB   . LEU   A  1  36  ? 15.053  -5.094  -31.964  1.00 71.55  ? 36   LEU   A CB   1 
ATOM   517   C  CG   . LEU   A  1  36  ? 16.124  -4.134  -31.444  1.00 77.04  ? 36   LEU   A CG   1 
ATOM   518   C  CD1  . LEU   A  1  36  ? 16.121  -2.824  -32.211  1.00 82.37  ? 36   LEU   A CD1  1 
ATOM   519   C  CD2  . LEU   A  1  36  ? 15.913  -3.880  -29.957  1.00 77.41  ? 36   LEU   A CD2  1 
ATOM   520   H  H    . LEU   A  1  36  ? 14.455  -4.284  -34.375  1.00 81.62  ? 36   LEU   A H    1 
ATOM   521   H  HA   . LEU   A  1  36  ? 16.140  -6.147  -33.343  1.00 82.39  ? 36   LEU   A HA   1 
ATOM   522   H  HB2  . LEU   A  1  36  ? 14.224  -4.591  -31.998  1.00 85.85  ? 36   LEU   A HB2  1 
ATOM   523   H  HB3  . LEU   A  1  36  ? 14.981  -5.808  -31.312  1.00 85.85  ? 36   LEU   A HB3  1 
ATOM   524   H  HG   . LEU   A  1  36  ? 16.995  -4.540  -31.575  1.00 92.42  ? 36   LEU   A HG   1 
ATOM   525   H  HD11 . LEU   A  1  36  ? 16.742  -2.209  -31.789  1.00 98.82  ? 36   LEU   A HD11 1 
ATOM   526   H  HD12 . LEU   A  1  36  ? 16.394  -2.993  -33.126  1.00 98.82  ? 36   LEU   A HD12 1 
ATOM   527   H  HD13 . LEU   A  1  36  ? 15.225  -2.451  -32.196  1.00 98.82  ? 36   LEU   A HD13 1 
ATOM   528   H  HD21 . LEU   A  1  36  ? 16.599  -3.272  -29.640  1.00 92.87  ? 36   LEU   A HD21 1 
ATOM   529   H  HD22 . LEU   A  1  36  ? 15.036  -3.486  -29.826  1.00 92.87  ? 36   LEU   A HD22 1 
ATOM   530   H  HD23 . LEU   A  1  36  ? 15.972  -4.723  -29.481  1.00 92.87  ? 36   LEU   A HD23 1 
ATOM   531   N  N    . LEU   A  1  37  ? 14.592  -8.067  -33.342  1.00 60.93  ? 37   LEU   A N    1 
ATOM   532   C  CA   . LEU   A  1  37  ? 13.669  -9.191  -33.378  1.00 58.80  ? 37   LEU   A CA   1 
ATOM   533   C  C    . LEU   A  1  37  ? 13.392  -9.637  -31.949  1.00 59.85  ? 37   LEU   A C    1 
ATOM   534   O  O    . LEU   A  1  37  ? 14.327  -9.888  -31.182  1.00 60.93  ? 37   LEU   A O    1 
ATOM   535   C  CB   . LEU   A  1  37  ? 14.241  -10.349 -34.197  1.00 61.33  ? 37   LEU   A CB   1 
ATOM   536   C  CG   . LEU   A  1  37  ? 14.612  -10.040 -35.650  1.00 65.98  ? 37   LEU   A CG   1 
ATOM   537   C  CD1  . LEU   A  1  37  ? 15.110  -11.297 -36.345  1.00 65.45  ? 37   LEU   A CD1  1 
ATOM   538   C  CD2  . LEU   A  1  37  ? 13.438  -9.442  -36.410  1.00 71.49  ? 37   LEU   A CD2  1 
ATOM   539   H  H    . LEU   A  1  37  ? 15.403  -8.294  -33.168  1.00 73.10  ? 37   LEU   A H    1 
ATOM   540   H  HA   . LEU   A  1  37  ? 12.834  -8.923  -33.793  1.00 70.54  ? 37   LEU   A HA   1 
ATOM   541   H  HB2  . LEU   A  1  37  ? 15.048  -10.658 -33.756  1.00 73.57  ? 37   LEU   A HB2  1 
ATOM   542   H  HB3  . LEU   A  1  37  ? 13.581  -11.059 -34.216  1.00 73.57  ? 37   LEU   A HB3  1 
ATOM   543   H  HG   . LEU   A  1  37  ? 15.325  -9.382  -35.652  1.00 79.16  ? 37   LEU   A HG   1 
ATOM   544   H  HD11 . LEU   A  1  37  ? 15.353  -11.078 -37.258  1.00 78.52  ? 37   LEU   A HD11 1 
ATOM   545   H  HD12 . LEU   A  1  37  ? 15.884  -11.636 -35.869  1.00 78.52  ? 37   LEU   A HD12 1 
ATOM   546   H  HD13 . LEU   A  1  37  ? 14.403  -11.961 -36.342  1.00 78.52  ? 37   LEU   A HD13 1 
ATOM   547   H  HD21 . LEU   A  1  37  ? 13.694  -9.314  -37.337  1.00 85.77  ? 37   LEU   A HD21 1 
ATOM   548   H  HD22 . LEU   A  1  37  ? 12.684  -10.050 -36.356  1.00 85.77  ? 37   LEU   A HD22 1 
ATOM   549   H  HD23 . LEU   A  1  37  ? 13.205  -8.589  -36.010  1.00 85.77  ? 37   LEU   A HD23 1 
ATOM   550   N  N    . VAL   A  1  38  ? 12.113  -9.722  -31.592  1.00 60.43  ? 38   VAL   A N    1 
ATOM   551   C  CA   . VAL   A  1  38  ? 11.698  -10.078 -30.241  1.00 59.29  ? 38   VAL   A CA   1 
ATOM   552   C  C    . VAL   A  1  38  ? 10.635  -11.163 -30.328  1.00 59.00  ? 38   VAL   A C    1 
ATOM   553   O  O    . VAL   A  1  38  ? 9.620   -10.992 -31.013  1.00 59.05  ? 38   VAL   A O    1 
ATOM   554   C  CB   . VAL   A  1  38  ? 11.159  -8.862  -29.465  1.00 59.92  ? 38   VAL   A CB   1 
ATOM   555   C  CG1  . VAL   A  1  38  ? 10.803  -9.265  -28.043  1.00 59.86  ? 38   VAL   A CG1  1 
ATOM   556   C  CG2  . VAL   A  1  38  ? 12.178  -7.733  -29.470  1.00 61.67  ? 38   VAL   A CG2  1 
ATOM   557   H  H    . VAL   A  1  38  ? 11.456  -9.574  -32.126  1.00 72.50  ? 38   VAL   A H    1 
ATOM   558   H  HA   . VAL   A  1  38  ? 12.461  -10.437 -29.762  1.00 71.12  ? 38   VAL   A HA   1 
ATOM   559   H  HB   . VAL   A  1  38  ? 10.355  -8.537  -29.898  1.00 71.88  ? 38   VAL   A HB   1 
ATOM   560   H  HG11 . VAL   A  1  38  ? 10.667  -8.465  -27.512  1.00 71.81  ? 38   VAL   A HG11 1 
ATOM   561   H  HG12 . VAL   A  1  38  ? 9.990   -9.794  -28.059  1.00 71.81  ? 38   VAL   A HG12 1 
ATOM   562   H  HG13 . VAL   A  1  38  ? 11.530  -9.788  -27.671  1.00 71.81  ? 38   VAL   A HG13 1 
ATOM   563   H  HG21 . VAL   A  1  38  ? 11.829  -6.990  -28.954  1.00 73.98  ? 38   VAL   A HG21 1 
ATOM   564   H  HG22 . VAL   A  1  38  ? 13.004  -8.052  -29.073  1.00 73.98  ? 38   VAL   A HG22 1 
ATOM   565   H  HG23 . VAL   A  1  38  ? 12.337  -7.455  -30.385  1.00 73.98  ? 38   VAL   A HG23 1 
ATOM   566   N  N    . GLY   A  1  39  ? 10.867  -12.271 -29.629  1.00 55.02  ? 39   GLY   A N    1 
ATOM   567   C  CA   . GLY   A  1  39  ? 9.906   -13.355 -29.581  1.00 56.15  ? 39   GLY   A CA   1 
ATOM   568   C  C    . GLY   A  1  39  ? 8.914   -13.169 -28.444  1.00 61.38  ? 39   GLY   A C    1 
ATOM   569   O  O    . GLY   A  1  39  ? 9.281   -12.788 -27.334  1.00 64.14  ? 39   GLY   A O    1 
ATOM   570   H  H    . GLY   A  1  39  ? 11.582  -12.416 -29.172  1.00 66.00  ? 39   GLY   A H    1 
ATOM   571   H  HA2  . GLY   A  1  39  ? 9.415   -13.392 -30.417  1.00 67.36  ? 39   GLY   A HA2  1 
ATOM   572   H  HA3  . GLY   A  1  39  ? 10.371  -14.197 -29.451  1.00 67.36  ? 39   GLY   A HA3  1 
ATOM   573   N  N    . ALA   A  1  40  ? 7.645   -13.438 -28.744  1.00 62.00  ? 40   ALA   A N    1 
ATOM   574   C  CA   . ALA   A  1  40  ? 6.558   -13.398 -27.765  1.00 60.20  ? 40   ALA   A CA   1 
ATOM   575   C  C    . ALA   A  1  40  ? 5.814   -14.723 -27.876  1.00 58.64  ? 40   ALA   A C    1 
ATOM   576   O  O    . ALA   A  1  40  ? 4.757   -14.806 -28.516  1.00 60.03  ? 40   ALA   A O    1 
ATOM   577   C  CB   . ALA   A  1  40  ? 5.635   -12.204 -28.005  1.00 55.39  ? 40   ALA   A CB   1 
ATOM   578   H  H    . ALA   A  1  40  ? 7.380   -13.654 -29.533  1.00 74.38  ? 40   ALA   A H    1 
ATOM   579   H  HA   . ALA   A  1  40  ? 6.915   -13.311 -26.867  1.00 72.22  ? 40   ALA   A HA   1 
ATOM   580   H  HB1  . ALA   A  1  40  ? 5.077   -12.073 -27.222  1.00 66.45  ? 40   ALA   A HB1  1 
ATOM   581   H  HB2  . ALA   A  1  40  ? 6.175   -11.413 -28.162  1.00 66.45  ? 40   ALA   A HB2  1 
ATOM   582   H  HB3  . ALA   A  1  40  ? 5.079   -12.384 -28.779  1.00 66.45  ? 40   ALA   A HB3  1 
ATOM   583   N  N    . PRO   A  1  41  ? 6.340   -15.787 -27.261  1.00 60.13  ? 41   PRO   A N    1 
ATOM   584   C  CA   . PRO   A  1  41  ? 5.823   -17.136 -27.550  1.00 59.86  ? 41   PRO   A CA   1 
ATOM   585   C  C    . PRO   A  1  41  ? 4.429   -17.411 -27.010  1.00 59.68  ? 41   PRO   A C    1 
ATOM   586   O  O    . PRO   A  1  41  ? 3.841   -18.434 -27.384  1.00 59.85  ? 41   PRO   A O    1 
ATOM   587   C  CB   . PRO   A  1  41  ? 6.862   -18.057 -26.896  1.00 57.97  ? 41   PRO   A CB   1 
ATOM   588   C  CG   . PRO   A  1  41  ? 7.474   -17.234 -25.817  1.00 58.41  ? 41   PRO   A CG   1 
ATOM   589   C  CD   . PRO   A  1  41  ? 7.462   -15.813 -26.306  1.00 59.99  ? 41   PRO   A CD   1 
ATOM   590   H  HA   . PRO   A  1  41  ? 5.818   -17.282 -28.509  1.00 71.81  ? 41   PRO   A HA   1 
ATOM   591   H  HB2  . PRO   A  1  41  ? 6.425   -18.841 -26.529  1.00 69.55  ? 41   PRO   A HB2  1 
ATOM   592   H  HB3  . PRO   A  1  41  ? 7.527   -18.322 -27.550  1.00 69.55  ? 41   PRO   A HB3  1 
ATOM   593   H  HG2  . PRO   A  1  41  ? 6.949   -17.320 -25.006  1.00 70.07  ? 41   PRO   A HG2  1 
ATOM   594   H  HG3  . PRO   A  1  41  ? 8.383   -17.532 -25.658  1.00 70.07  ? 41   PRO   A HG3  1 
ATOM   595   H  HD2  . PRO   A  1  41  ? 7.305   -15.198 -25.573  1.00 71.96  ? 41   PRO   A HD2  1 
ATOM   596   H  HD3  . PRO   A  1  41  ? 8.297   -15.594 -26.749  1.00 71.96  ? 41   PRO   A HD3  1 
ATOM   597   N  N    . LYS   A  1  42  ? 3.877   -16.550 -26.156  1.00 58.69  ? 42   LYS   A N    1 
ATOM   598   C  CA   . LYS   A  1  42  ? 2.517   -16.719 -25.659  1.00 60.94  ? 42   LYS   A CA   1 
ATOM   599   C  C    . LYS   A  1  42  ? 1.548   -15.707 -26.256  1.00 65.79  ? 42   LYS   A C    1 
ATOM   600   O  O    . LYS   A  1  42  ? 0.396   -15.630 -25.815  1.00 69.39  ? 42   LYS   A O    1 
ATOM   601   C  CB   . LYS   A  1  42  ? 2.495   -16.623 -24.131  1.00 62.68  ? 42   LYS   A CB   1 
ATOM   602   C  CG   . LYS   A  1  42  ? 2.935   -17.896 -23.422  1.00 62.56  ? 42   LYS   A CG   1 
ATOM   603   C  CD   . LYS   A  1  42  ? 2.640   -17.830 -21.930  1.00 69.28  ? 42   LYS   A CD   1 
ATOM   604   C  CE   . LYS   A  1  42  ? 2.941   -19.152 -21.242  1.00 78.94  ? 42   LYS   A CE   1 
ATOM   605   N  NZ   . LYS   A  1  42  ? 2.656   -19.102 -19.782  1.00 87.88  ? 42   LYS   A NZ   1 
ATOM   606   H  H    . LYS   A  1  42  ? 4.276   -15.853 -25.849  1.00 70.41  ? 42   LYS   A H    1 
ATOM   607   H  HA   . LYS   A  1  42  ? 2.211   -17.606 -25.906  1.00 73.11  ? 42   LYS   A HA   1 
ATOM   608   H  HB2  . LYS   A  1  42  ? 3.093   -15.911 -23.856  1.00 75.20  ? 42   LYS   A HB2  1 
ATOM   609   H  HB3  . LYS   A  1  42  ? 1.590   -16.425 -23.846  1.00 75.20  ? 42   LYS   A HB3  1 
ATOM   610   H  HG2  . LYS   A  1  42  ? 2.458   -18.653 -23.795  1.00 75.05  ? 42   LYS   A HG2  1 
ATOM   611   H  HG3  . LYS   A  1  42  ? 3.891   -18.015 -23.539  1.00 75.05  ? 42   LYS   A HG3  1 
ATOM   612   H  HD2  . LYS   A  1  42  ? 3.192   -17.143 -21.523  1.00 83.11  ? 42   LYS   A HD2  1 
ATOM   613   H  HD3  . LYS   A  1  42  ? 1.702   -17.624 -21.796  1.00 83.11  ? 42   LYS   A HD3  1 
ATOM   614   H  HE2  . LYS   A  1  42  ? 2.390   -19.848 -21.634  1.00 94.71  ? 42   LYS   A HE2  1 
ATOM   615   H  HE3  . LYS   A  1  42  ? 3.880   -19.367 -21.360  1.00 94.71  ? 42   LYS   A HE3  1 
ATOM   616   H  HZ1  . LYS   A  1  42  ? 2.775   -19.906 -19.420  1.00 105.44 ? 42   LYS   A HZ1  1 
ATOM   617   H  HZ2  . LYS   A  1  42  ? 3.203   -18.523 -19.385  1.00 105.44 ? 42   LYS   A HZ2  1 
ATOM   618   H  HZ3  . LYS   A  1  42  ? 1.815   -18.845 -19.644  1.00 105.44 ? 42   LYS   A HZ3  1 
ATOM   619   N  N    . ALA   A  1  43  ? 1.979   -14.937 -27.251  1.00 65.76  ? 43   ALA   A N    1 
ATOM   620   C  CA   . ALA   A  1  43  ? 1.134   -13.889 -27.804  1.00 63.72  ? 43   ALA   A CA   1 
ATOM   621   C  C    . ALA   A  1  43  ? 0.020   -14.481 -28.657  1.00 60.55  ? 43   ALA   A C    1 
ATOM   622   O  O    . ALA   A  1  43  ? 0.228   -15.438 -29.408  1.00 58.39  ? 43   ALA   A O    1 
ATOM   623   C  CB   . ALA   A  1  43  ? 1.967   -12.919 -28.641  1.00 66.96  ? 43   ALA   A CB   1 
ATOM   624   H  H    . ALA   A  1  43  ? 2.753   -15.002 -27.621  1.00 78.89  ? 43   ALA   A H    1 
ATOM   625   H  HA   . ALA   A  1  43  ? 0.727   -13.396 -27.075  1.00 76.45  ? 43   ALA   A HA   1 
ATOM   626   H  HB1  . ALA   A  1  43  ? 1.944   -12.043 -28.225  1.00 80.33  ? 43   ALA   A HB1  1 
ATOM   627   H  HB2  . ALA   A  1  43  ? 2.881   -13.242 -28.682  1.00 80.33  ? 43   ALA   A HB2  1 
ATOM   628   H  HB3  . ALA   A  1  43  ? 1.592   -12.871 -29.534  1.00 80.33  ? 43   ALA   A HB3  1 
ATOM   629   N  N    . ASN   A  1  44  ? -1.168  -13.900 -28.538  1.00 64.94  ? 44   ASN   A N    1 
ATOM   630   C  CA   . ASN   A  1  44  ? -2.281  -14.299 -29.383  1.00 62.02  ? 44   ASN   A CA   1 
ATOM   631   C  C    . ASN   A  1  44  ? -2.095  -13.752 -30.792  1.00 65.21  ? 44   ASN   A C    1 
ATOM   632   O  O    . ASN   A  1  44  ? -1.529  -12.676 -30.997  1.00 68.35  ? 44   ASN   A O    1 
ATOM   633   C  CB   . ASN   A  1  44  ? -3.598  -13.805 -28.794  1.00 59.58  ? 44   ASN   A CB   1 
ATOM   634   C  CG   . ASN   A  1  44  ? -4.094  -14.691 -27.676  1.00 65.25  ? 44   ASN   A CG   1 
ATOM   635   O  OD1  . ASN   A  1  44  ? -4.100  -15.916 -27.803  1.00 60.78  ? 44   ASN   A OD1  1 
ATOM   636   N  ND2  . ASN   A  1  44  ? -4.508  -14.087 -26.571  1.00 84.08  ? 44   ASN   A ND2  1 
ATOM   637   H  H    . ASN   A  1  44  ? -1.354  -13.274 -27.978  1.00 77.91  ? 44   ASN   A H    1 
ATOM   638   H  HA   . ASN   A  1  44  ? -2.324  -15.266 -29.436  1.00 74.40  ? 44   ASN   A HA   1 
ATOM   639   H  HB2  . ASN   A  1  44  ? -3.471  -12.912 -28.437  1.00 71.48  ? 44   ASN   A HB2  1 
ATOM   640   H  HB3  . ASN   A  1  44  ? -4.272  -13.791 -29.491  1.00 71.48  ? 44   ASN   A HB3  1 
ATOM   641   H  HD21 . ASN   A  1  44  ? -4.489  -13.230 -26.499  1.00 100.88 ? 44   ASN   A HD21 1 
ATOM   642   N  N    . THR   A  1  45  ? -2.577  -14.514 -31.768  1.00 66.40  ? 45   THR   A N    1 
ATOM   643   C  CA   . THR   A  1  45  ? -2.415  -14.184 -33.174  1.00 65.49  ? 45   THR   A CA   1 
ATOM   644   C  C    . THR   A  1  45  ? -3.775  -14.197 -33.854  1.00 64.38  ? 45   THR   A C    1 
ATOM   645   O  O    . THR   A  1  45  ? -4.790  -14.577 -33.263  1.00 65.51  ? 45   THR   A O    1 
ATOM   646   C  CB   . THR   A  1  45  ? -1.466  -15.169 -33.874  1.00 65.69  ? 45   THR   A CB   1 
ATOM   647   O  OG1  . THR   A  1  45  ? -2.062  -16.472 -33.908  1.00 65.71  ? 45   THR   A OG1  1 
ATOM   648   C  CG2  . THR   A  1  45  ? -0.138  -15.243 -33.137  1.00 64.21  ? 45   THR   A CG2  1 
ATOM   649   H  H    . THR   A  1  45  ? -3.013  -15.243 -31.635  1.00 79.67  ? 45   THR   A H    1 
ATOM   650   H  HA   . THR   A  1  45  ? -2.041  -13.293 -33.251  1.00 78.57  ? 45   THR   A HA   1 
ATOM   651   H  HB   . THR   A  1  45  ? -1.299  -14.866 -34.780  1.00 78.81  ? 45   THR   A HB   1 
ATOM   652   H  HG1  . THR   A  1  45  ? -1.544  -17.015 -34.286  1.00 78.83  ? 45   THR   A HG1  1 
ATOM   653   H  HG21 . THR   A  1  45  ? 0.460   -15.857 -33.593  1.00 77.03  ? 45   THR   A HG21 1 
ATOM   654   H  HG22 . THR   A  1  45  ? 0.275   -14.366 -33.108  1.00 77.03  ? 45   THR   A HG22 1 
ATOM   655   H  HG23 . THR   A  1  45  ? -0.278  -15.556 -32.230  1.00 77.03  ? 45   THR   A HG23 1 
ATOM   656   N  N    . THR   A  1  46  ? -3.785  -13.768 -35.113  1.00 65.86  ? 46   THR   A N    1 
ATOM   657   C  CA   . THR   A  1  46  ? -4.993  -13.792 -35.926  1.00 66.99  ? 46   THR   A CA   1 
ATOM   658   C  C    . THR   A  1  46  ? -5.224  -15.142 -36.591  1.00 67.21  ? 46   THR   A C    1 
ATOM   659   O  O    . THR   A  1  46  ? -6.234  -15.308 -37.283  1.00 70.90  ? 46   THR   A O    1 
ATOM   660   C  CB   . THR   A  1  46  ? -4.927  -12.699 -36.996  1.00 68.25  ? 46   THR   A CB   1 
ATOM   661   O  OG1  . THR   A  1  46  ? -3.781  -12.910 -37.831  1.00 67.34  ? 46   THR   A OG1  1 
ATOM   662   C  CG2  . THR   A  1  46  ? -4.837  -11.326 -36.343  1.00 71.65  ? 46   THR   A CG2  1 
ATOM   663   H  H    . THR   A  1  46  ? -3.097  -13.456 -35.523  1.00 79.01  ? 46   THR   A H    1 
ATOM   664   H  HA   . THR   A  1  46  ? -5.755  -13.605 -35.356  1.00 80.37  ? 46   THR   A HA   1 
ATOM   665   H  HB   . THR   A  1  46  ? -5.729  -12.727 -37.541  1.00 81.88  ? 46   THR   A HB   1 
ATOM   666   H  HG1  . THR   A  1  46  ? -3.726  -12.298 -38.403  1.00 80.79  ? 46   THR   A HG1  1 
ATOM   667   H  HG21 . THR   A  1  46  ? -4.813  -10.636 -37.024  1.00 85.96  ? 46   THR   A HG21 1 
ATOM   668   H  HG22 . THR   A  1  46  ? -5.607  -11.179 -35.772  1.00 85.96  ? 46   THR   A HG22 1 
ATOM   669   H  HG23 . THR   A  1  46  ? -4.031  -11.267 -35.806  1.00 85.96  ? 46   THR   A HG23 1 
ATOM   670   N  N    . GLN   A  1  47  ? -4.320  -16.096 -36.404  1.00 68.52  ? 47   GLN   A N    1 
ATOM   671   C  CA   . GLN   A  1  47  ? -4.475  -17.419 -36.988  1.00 68.27  ? 47   GLN   A CA   1 
ATOM   672   C  C    . GLN   A  1  47  ? -5.815  -18.014 -36.567  1.00 70.90  ? 47   GLN   A C    1 
ATOM   673   O  O    . GLN   A  1  47  ? -6.082  -18.122 -35.361  1.00 73.68  ? 47   GLN   A O    1 
ATOM   674   C  CB   . GLN   A  1  47  ? -3.326  -18.322 -36.552  1.00 63.48  ? 47   GLN   A CB   1 
ATOM   675   C  CG   . GLN   A  1  47  ? -1.963  -17.859 -37.044  1.00 62.86  ? 47   GLN   A CG   1 
ATOM   676   C  CD   . GLN   A  1  47  ? -0.826  -18.685 -36.477  1.00 62.57  ? 47   GLN   A CD   1 
ATOM   677   O  OE1  . GLN   A  1  47  ? -0.374  -18.451 -35.357  1.00 65.95  ? 47   GLN   A OE1  1 
ATOM   678   N  NE2  . GLN   A  1  47  ? -0.359  -19.659 -37.249  1.00 60.91  ? 47   GLN   A NE2  1 
ATOM   679   H  H    . GLN   A  1  47  ? -3.603  -16.000 -35.939  1.00 82.21  ? 47   GLN   A H    1 
ATOM   680   H  HA   . GLN   A  1  47  ? -4.457  -17.356 -37.956  1.00 81.90  ? 47   GLN   A HA   1 
ATOM   681   H  HB2  . GLN   A  1  47  ? -3.299  -18.346 -35.583  1.00 76.16  ? 47   GLN   A HB2  1 
ATOM   682   H  HB3  . GLN   A  1  47  ? -3.480  -19.214 -36.901  1.00 76.16  ? 47   GLN   A HB3  1 
ATOM   683   H  HG2  . GLN   A  1  47  ? -1.934  -17.932 -38.011  1.00 75.42  ? 47   GLN   A HG2  1 
ATOM   684   H  HG3  . GLN   A  1  47  ? -1.827  -16.937 -36.777  1.00 75.42  ? 47   GLN   A HG3  1 
ATOM   685   H  HE21 . GLN   A  1  47  ? -0.701  -19.793 -38.027  1.00 73.08  ? 47   GLN   A HE21 1 
ATOM   686   H  HE22 . GLN   A  1  47  ? 0.286   -20.156 -36.972  1.00 73.08  ? 47   GLN   A HE22 1 
ATOM   687   N  N    . PRO   A  1  48  ? -6.679  -18.403 -37.505  1.00 70.33  ? 48   PRO   A N    1 
ATOM   688   C  CA   . PRO   A  1  48  ? -8.018  -18.870 -37.120  1.00 70.35  ? 48   PRO   A CA   1 
ATOM   689   C  C    . PRO   A  1  48  ? -7.956  -20.037 -36.145  1.00 68.18  ? 48   PRO   A C    1 
ATOM   690   O  O    . PRO   A  1  48  ? -7.291  -21.045 -36.393  1.00 66.19  ? 48   PRO   A O    1 
ATOM   691   C  CB   . PRO   A  1  48  ? -8.647  -19.282 -38.456  1.00 68.76  ? 48   PRO   A CB   1 
ATOM   692   C  CG   . PRO   A  1  48  ? -7.905  -18.509 -39.485  1.00 69.58  ? 48   PRO   A CG   1 
ATOM   693   C  CD   . PRO   A  1  48  ? -6.504  -18.386 -38.969  1.00 69.93  ? 48   PRO   A CD   1 
ATOM   694   H  HA   . PRO   A  1  48  ? -8.524  -18.145 -36.721  1.00 84.39  ? 48   PRO   A HA   1 
ATOM   695   H  HB2  . PRO   A  1  48  ? -8.538  -20.236 -38.593  1.00 82.49  ? 48   PRO   A HB2  1 
ATOM   696   H  HB3  . PRO   A  1  48  ? -9.590  -19.052 -38.462  1.00 82.49  ? 48   PRO   A HB3  1 
ATOM   697   H  HG2  . PRO   A  1  48  ? -7.920  -18.987 -40.328  1.00 83.48  ? 48   PRO   A HG2  1 
ATOM   698   H  HG3  . PRO   A  1  48  ? -8.310  -17.634 -39.592  1.00 83.48  ? 48   PRO   A HG3  1 
ATOM   699   H  HD2  . PRO   A  1  48  ? -5.962  -19.135 -39.260  1.00 83.89  ? 48   PRO   A HD2  1 
ATOM   700   H  HD3  . PRO   A  1  48  ? -6.101  -17.552 -39.259  1.00 83.89  ? 48   PRO   A HD3  1 
ATOM   701   N  N    . GLY   A  1  49  ? -8.658  -19.886 -35.023  1.00 67.89  ? 49   GLY   A N    1 
ATOM   702   C  CA   . GLY   A  1  49  ? -8.803  -20.961 -34.064  1.00 62.05  ? 49   GLY   A CA   1 
ATOM   703   C  C    . GLY   A  1  49  ? -7.585  -21.260 -33.222  1.00 60.63  ? 49   GLY   A C    1 
ATOM   704   O  O    . GLY   A  1  49  ? -7.600  -22.240 -32.471  1.00 61.05  ? 49   GLY   A O    1 
ATOM   705   H  H    . GLY   A  1  49  ? -9.061  -19.161 -34.797  1.00 81.44  ? 49   GLY   A H    1 
ATOM   706   H  HA2  . GLY   A  1  49  ? -9.528  -20.738 -33.459  1.00 74.45  ? 49   GLY   A HA2  1 
ATOM   707   H  HA3  . GLY   A  1  49  ? -9.032  -21.772 -34.544  1.00 74.45  ? 49   GLY   A HA3  1 
ATOM   708   N  N    . ILE   A  1  50  ? -6.534  -20.450 -33.311  1.00 60.40  ? 50   ILE   A N    1 
ATOM   709   C  CA   . ILE   A  1  50  ? -5.291  -20.690 -32.588  1.00 57.92  ? 50   ILE   A CA   1 
ATOM   710   C  C    . ILE   A  1  50  ? -5.225  -19.747 -31.396  1.00 60.93  ? 50   ILE   A C    1 
ATOM   711   O  O    . ILE   A  1  50  ? -5.393  -18.530 -31.545  1.00 64.28  ? 50   ILE   A O    1 
ATOM   712   C  CB   . ILE   A  1  50  ? -4.068  -20.505 -33.504  1.00 55.59  ? 50   ILE   A CB   1 
ATOM   713   C  CG1  . ILE   A  1  50  ? -4.196  -21.390 -34.749  1.00 58.30  ? 50   ILE   A CG1  1 
ATOM   714   C  CG2  . ILE   A  1  50  ? -2.779  -20.810 -32.748  1.00 49.32  ? 50   ILE   A CG2  1 
ATOM   715   C  CD1  . ILE   A  1  50  ? -4.522  -22.844 -34.455  1.00 58.52  ? 50   ILE   A CD1  1 
ATOM   716   H  H    . ILE   A  1  50  ? -6.518  -19.739 -33.795  1.00 72.46  ? 50   ILE   A H    1 
ATOM   717   H  HA   . ILE   A  1  50  ? -5.289  -21.601 -32.254  1.00 69.48  ? 50   ILE   A HA   1 
ATOM   718   H  HB   . ILE   A  1  50  ? -4.038  -19.579 -33.791  1.00 66.69  ? 50   ILE   A HB   1 
ATOM   719   H  HG12 . ILE   A  1  50  ? -4.907  -21.037 -35.307  1.00 69.94  ? 50   ILE   A HG12 1 
ATOM   720   H  HG13 . ILE   A  1  50  ? -3.355  -21.370 -35.230  1.00 69.94  ? 50   ILE   A HG13 1 
ATOM   721   H  HG21 . ILE   A  1  50  ? -2.031  -20.751 -33.363  1.00 59.16  ? 50   ILE   A HG21 1 
ATOM   722   H  HG22 . ILE   A  1  50  ? -2.672  -20.163 -32.033  1.00 59.16  ? 50   ILE   A HG22 1 
ATOM   723   H  HG23 . ILE   A  1  50  ? -2.834  -21.705 -32.379  1.00 59.16  ? 50   ILE   A HG23 1 
ATOM   724   H  HD11 . ILE   A  1  50  ? -4.457  -23.354 -35.277  1.00 70.21  ? 50   ILE   A HD11 1 
ATOM   725   H  HD12 . ILE   A  1  50  ? -3.889  -23.184 -33.803  1.00 70.21  ? 50   ILE   A HD12 1 
ATOM   726   H  HD13 . ILE   A  1  50  ? -5.424  -22.900 -34.101  1.00 70.21  ? 50   ILE   A HD13 1 
ATOM   727   N  N    . VAL   A  1  51  ? -4.980  -20.309 -30.215  1.00 61.46  ? 51   VAL   A N    1 
ATOM   728   C  CA   . VAL   A  1  51  ? -4.831  -19.550 -28.979  1.00 60.18  ? 51   VAL   A CA   1 
ATOM   729   C  C    . VAL   A  1  51  ? -3.359  -19.556 -28.592  1.00 62.73  ? 51   VAL   A C    1 
ATOM   730   O  O    . VAL   A  1  51  ? -2.730  -20.620 -28.532  1.00 60.82  ? 51   VAL   A O    1 
ATOM   731   C  CB   . VAL   A  1  51  ? -5.696  -20.135 -27.850  1.00 57.70  ? 51   VAL   A CB   1 
ATOM   732   C  CG1  . VAL   A  1  51  ? -5.518  -19.333 -26.568  1.00 61.02  ? 51   VAL   A CG1  1 
ATOM   733   C  CG2  . VAL   A  1  51  ? -7.156  -20.162 -28.266  1.00 55.37  ? 51   VAL   A CG2  1 
ATOM   734   H  H    . VAL   A  1  51  ? -4.892  -21.157 -30.102  1.00 73.73  ? 51   VAL   A H    1 
ATOM   735   H  HA   . VAL   A  1  51  ? -5.106  -18.632 -29.131  1.00 72.20  ? 51   VAL   A HA   1 
ATOM   736   H  HB   . VAL   A  1  51  ? -5.412  -21.045 -27.675  1.00 69.22  ? 51   VAL   A HB   1 
ATOM   737   H  HG11 . VAL   A  1  51  ? -6.125  -19.677 -25.893  1.00 73.20  ? 51   VAL   A HG11 1 
ATOM   738   H  HG12 . VAL   A  1  51  ? -4.601  -19.422 -26.264  1.00 73.20  ? 51   VAL   A HG12 1 
ATOM   739   H  HG13 . VAL   A  1  51  ? -5.718  -18.401 -26.748  1.00 73.20  ? 51   VAL   A HG13 1 
ATOM   740   H  HG21 . VAL   A  1  51  ? -7.688  -20.507 -27.531  1.00 66.43  ? 51   VAL   A HG21 1 
ATOM   741   H  HG22 . VAL   A  1  51  ? -7.439  -19.261 -28.485  1.00 66.43  ? 51   VAL   A HG22 1 
ATOM   742   H  HG23 . VAL   A  1  51  ? -7.253  -20.737 -29.042  1.00 66.43  ? 51   VAL   A HG23 1 
ATOM   743   N  N    . GLU   A  1  52  ? -2.815  -18.369 -28.332  1.00 63.81  ? 52   GLU   A N    1 
ATOM   744   C  CA   . GLU   A  1  52  ? -1.426  -18.210 -27.906  1.00 61.40  ? 52   GLU   A CA   1 
ATOM   745   C  C    . GLU   A  1  52  ? -0.478  -18.996 -28.808  1.00 57.26  ? 52   GLU   A C    1 
ATOM   746   O  O    . GLU   A  1  52  ? 0.400   -19.729 -28.348  1.00 55.67  ? 52   GLU   A O    1 
ATOM   747   C  CB   . GLU   A  1  52  ? -1.256  -18.622 -26.443  1.00 64.26  ? 52   GLU   A CB   1 
ATOM   748   C  CG   . GLU   A  1  52  ? -1.982  -17.716 -25.467  1.00 70.97  ? 52   GLU   A CG   1 
ATOM   749   C  CD   . GLU   A  1  52  ? -1.566  -17.949 -24.030  1.00 72.10  ? 52   GLU   A CD   1 
ATOM   750   O  OE1  . GLU   A  1  52  ? -0.814  -18.914 -23.773  1.00 71.43  ? 52   GLU   A OE1  1 
ATOM   751   O  OE2  . GLU   A  1  52  ? -1.992  -17.162 -23.158  1.00 72.34  ? 52   GLU   A OE2  1 
ATOM   752   H  H    . GLU   A  1  52  ? -3.240  -17.623 -28.396  1.00 76.55  ? 52   GLU   A H    1 
ATOM   753   H  HA   . GLU   A  1  52  ? -1.191  -17.272 -27.985  1.00 73.66  ? 52   GLU   A HA   1 
ATOM   754   H  HB2  . GLU   A  1  52  ? -1.604  -19.520 -26.329  1.00 77.10  ? 52   GLU   A HB2  1 
ATOM   755   H  HB3  . GLU   A  1  52  ? -0.312  -18.602 -26.221  1.00 77.10  ? 52   GLU   A HB3  1 
ATOM   756   H  HG2  . GLU   A  1  52  ? -1.787  -16.792 -25.689  1.00 85.15  ? 52   GLU   A HG2  1 
ATOM   757   H  HG3  . GLU   A  1  52  ? -2.935  -17.879 -25.533  1.00 85.15  ? 52   GLU   A HG3  1 
ATOM   758   N  N    . GLY   A  1  53  ? -0.670  -18.841 -30.119  1.00 58.12  ? 53   GLY   A N    1 
ATOM   759   C  CA   . GLY   A  1  53  ? 0.260   -19.421 -31.070  1.00 59.14  ? 53   GLY   A CA   1 
ATOM   760   C  C    . GLY   A  1  53  ? 1.638   -18.799 -31.024  1.00 60.12  ? 53   GLY   A C    1 
ATOM   761   O  O    . GLY   A  1  53  ? 2.599   -19.410 -31.502  1.00 59.13  ? 53   GLY   A O    1 
ATOM   762   H  H    . GLY   A  1  53  ? -1.324  -18.409 -30.474  1.00 69.73  ? 53   GLY   A H    1 
ATOM   763   H  HA2  . GLY   A  1  53  ? 0.351   -20.369 -30.885  1.00 70.95  ? 53   GLY   A HA2  1 
ATOM   764   H  HA3  . GLY   A  1  53  ? -0.092  -19.306 -31.966  1.00 70.95  ? 53   GLY   A HA3  1 
ATOM   765   N  N    . GLY   A  1  54  ? 1.757   -17.607 -30.452  1.00 58.21  ? 54   GLY   A N    1 
ATOM   766   C  CA   . GLY   A  1  54  ? 3.021   -16.910 -30.387  1.00 58.89  ? 54   GLY   A CA   1 
ATOM   767   C  C    . GLY   A  1  54  ? 3.351   -16.193 -31.684  1.00 60.10  ? 54   GLY   A C    1 
ATOM   768   O  O    . GLY   A  1  54  ? 2.782   -16.455 -32.743  1.00 59.84  ? 54   GLY   A O    1 
ATOM   769   H  H    . GLY   A  1  54  ? 1.105   -17.179 -30.090  1.00 69.83  ? 54   GLY   A H    1 
ATOM   770   H  HA2  . GLY   A  1  54  ? 2.990   -16.254 -29.674  1.00 70.65  ? 54   GLY   A HA2  1 
ATOM   771   H  HA3  . GLY   A  1  54  ? 3.729   -17.546 -30.200  1.00 70.65  ? 54   GLY   A HA3  1 
ATOM   772   N  N    . GLN   A  1  55  ? 4.297   -15.262 -31.591  1.00 62.69  ? 55   GLN   A N    1 
ATOM   773   C  CA   . GLN   A  1  55  ? 4.690   -14.488 -32.759  1.00 64.31  ? 55   GLN   A CA   1 
ATOM   774   C  C    . GLN   A  1  55  ? 6.046   -13.845 -32.510  1.00 61.38  ? 55   GLN   A C    1 
ATOM   775   O  O    . GLN   A  1  55  ? 6.507   -13.736 -31.371  1.00 61.38  ? 55   GLN   A O    1 
ATOM   776   C  CB   . GLN   A  1  55  ? 3.641   -13.422 -33.100  1.00 61.99  ? 55   GLN   A CB   1 
ATOM   777   C  CG   . GLN   A  1  55  ? 3.345   -12.447 -31.969  1.00 57.51  ? 55   GLN   A CG   1 
ATOM   778   C  CD   . GLN   A  1  55  ? 2.209   -11.498 -32.300  1.00 60.27  ? 55   GLN   A CD   1 
ATOM   779   O  OE1  . GLN   A  1  55  ? 1.513   -11.671 -33.300  1.00 62.31  ? 55   GLN   A OE1  1 
ATOM   780   N  NE2  . GLN   A  1  55  ? 2.016   -10.487 -31.460  1.00 58.91  ? 55   GLN   A NE2  1 
ATOM   781   H  H    . GLN   A  1  55  ? 4.720   -15.064 -30.869  1.00 75.21  ? 55   GLN   A H    1 
ATOM   782   H  HA   . GLN   A  1  55  ? 4.784   -15.086 -33.516  1.00 77.15  ? 55   GLN   A HA   1 
ATOM   783   H  HB2  . GLN   A  1  55  ? 3.959   -12.905 -33.857  1.00 74.37  ? 55   GLN   A HB2  1 
ATOM   784   H  HB3  . GLN   A  1  55  ? 2.810   -13.867 -33.328  1.00 74.37  ? 55   GLN   A HB3  1 
ATOM   785   H  HG2  . GLN   A  1  55  ? 3.097   -12.948 -31.176  1.00 69.00  ? 55   GLN   A HG2  1 
ATOM   786   H  HG3  . GLN   A  1  55  ? 4.138   -11.917 -31.792  1.00 69.00  ? 55   GLN   A HG3  1 
ATOM   787   H  HE21 . GLN   A  1  55  ? 2.523   -10.398 -30.771  1.00 70.67  ? 55   GLN   A HE21 1 
ATOM   788   H  HE22 . GLN   A  1  55  ? 1.384   -9.922  -31.605  1.00 70.67  ? 55   GLN   A HE22 1 
ATOM   789   N  N    . VAL   A  1  56  ? 6.679   -13.427 -33.604  1.00 59.32  ? 56   VAL   A N    1 
ATOM   790   C  CA   . VAL   A  1  56  ? 7.960   -12.732 -33.580  1.00 56.51  ? 56   VAL   A CA   1 
ATOM   791   C  C    . VAL   A  1  56  ? 7.729   -11.326 -34.112  1.00 61.74  ? 56   VAL   A C    1 
ATOM   792   O  O    . VAL   A  1  56  ? 7.056   -11.148 -35.135  1.00 64.28  ? 56   VAL   A O    1 
ATOM   793   C  CB   . VAL   A  1  56  ? 9.021   -13.468 -34.419  1.00 55.25  ? 56   VAL   A CB   1 
ATOM   794   C  CG1  . VAL   A  1  56  ? 10.346  -12.714 -34.399  1.00 56.41  ? 56   VAL   A CG1  1 
ATOM   795   C  CG2  . VAL   A  1  56  ? 9.208   -14.894 -33.916  1.00 52.23  ? 56   VAL   A CG2  1 
ATOM   796   H  H    . VAL   A  1  56  ? 6.373   -13.541 -34.399  1.00 71.16  ? 56   VAL   A H    1 
ATOM   797   H  HA   . VAL   A  1  56  ? 8.285   -12.673 -32.668  1.00 67.80  ? 56   VAL   A HA   1 
ATOM   798   H  HB   . VAL   A  1  56  ? 8.714   -13.509 -35.339  1.00 66.28  ? 56   VAL   A HB   1 
ATOM   799   H  HG11 . VAL   A  1  56  ? 11.010  -13.229 -34.883  1.00 67.68  ? 56   VAL   A HG11 1 
ATOM   800   H  HG12 . VAL   A  1  56  ? 10.224  -11.850 -34.823  1.00 67.68  ? 56   VAL   A HG12 1 
ATOM   801   H  HG13 . VAL   A  1  56  ? 10.627  -12.594 -33.478  1.00 67.68  ? 56   VAL   A HG13 1 
ATOM   802   H  HG21 . VAL   A  1  56  ? 9.900   -15.326 -34.440  1.00 62.66  ? 56   VAL   A HG21 1 
ATOM   803   H  HG22 . VAL   A  1  56  ? 9.468   -14.868 -32.982  1.00 62.66  ? 56   VAL   A HG22 1 
ATOM   804   H  HG23 . VAL   A  1  56  ? 8.371   -15.375 -34.013  1.00 62.66  ? 56   VAL   A HG23 1 
ATOM   805   N  N    . LEU   A  1  57  ? 8.282   -10.332 -33.425  1.00 63.05  ? 57   LEU   A N    1 
ATOM   806   C  CA   . LEU   A  1  57  ? 8.061   -8.935  -33.768  1.00 65.58  ? 57   LEU   A CA   1 
ATOM   807   C  C    . LEU   A  1  57  ? 9.345   -8.293  -34.271  1.00 60.68  ? 57   LEU   A C    1 
ATOM   808   O  O    . LEU   A  1  57  ? 10.431  -8.543  -33.738  1.00 53.17  ? 57   LEU   A O    1 
ATOM   809   C  CB   . LEU   A  1  57  ? 7.533   -8.149  -32.565  1.00 69.23  ? 57   LEU   A CB   1 
ATOM   810   C  CG   . LEU   A  1  57  ? 6.168   -8.584  -32.030  1.00 71.12  ? 57   LEU   A CG   1 
ATOM   811   C  CD1  . LEU   A  1  57  ? 6.325   -9.605  -30.916  1.00 74.03  ? 57   LEU   A CD1  1 
ATOM   812   C  CD2  . LEU   A  1  57  ? 5.365   -7.381  -31.556  1.00 71.94  ? 57   LEU   A CD2  1 
ATOM   813   H  H    . LEU   A  1  57  ? 8.797   -10.445 -32.746  1.00 75.63  ? 57   LEU   A H    1 
ATOM   814   H  HA   . LEU   A  1  57  ? 7.405   -8.891  -34.481  1.00 78.68  ? 57   LEU   A HA   1 
ATOM   815   H  HB2  . LEU   A  1  57  ? 8.170   -8.242  -31.839  1.00 83.05  ? 57   LEU   A HB2  1 
ATOM   816   H  HB3  . LEU   A  1  57  ? 7.457   -7.216  -32.822  1.00 83.05  ? 57   LEU   A HB3  1 
ATOM   817   H  HG   . LEU   A  1  57  ? 5.671   -9.006  -32.749  1.00 85.33  ? 57   LEU   A HG   1 
ATOM   818   H  HD11 . LEU   A  1  57  ? 5.445   -9.869  -30.603  1.00 88.82  ? 57   LEU   A HD11 1 
ATOM   819   H  HD12 . LEU   A  1  57  ? 6.799   -10.377 -31.260  1.00 88.82  ? 57   LEU   A HD12 1 
ATOM   820   H  HD13 . LEU   A  1  57  ? 6.827   -9.204  -30.189  1.00 88.82  ? 57   LEU   A HD13 1 
ATOM   821   H  HD21 . LEU   A  1  57  ? 4.513   -7.687  -31.207  1.00 86.31  ? 57   LEU   A HD21 1 
ATOM   822   H  HD22 . LEU   A  1  57  ? 5.863   -6.924  -30.860  1.00 86.31  ? 57   LEU   A HD22 1 
ATOM   823   H  HD23 . LEU   A  1  57  ? 5.220   -6.783  -32.306  1.00 86.31  ? 57   LEU   A HD23 1 
ATOM   824   N  N    . LYS   A  1  58  ? 9.208   -7.470  -35.308  1.00 60.41  ? 58   LYS   A N    1 
ATOM   825   C  CA   . LYS   A  1  58  ? 10.282  -6.621  -35.803  1.00 59.97  ? 58   LYS   A CA   1 
ATOM   826   C  C    . LYS   A  1  58  ? 10.057  -5.211  -35.275  1.00 63.04  ? 58   LYS   A C    1 
ATOM   827   O  O    . LYS   A  1  58  ? 8.961   -4.659  -35.418  1.00 66.42  ? 58   LYS   A O    1 
ATOM   828   C  CB   . LYS   A  1  58  ? 10.317  -6.626  -37.332  1.00 66.34  ? 58   LYS   A CB   1 
ATOM   829   C  CG   . LYS   A  1  58  ? 11.419  -5.771  -37.943  1.00 77.98  ? 58   LYS   A CG   1 
ATOM   830   C  CD   . LYS   A  1  58  ? 11.683  -6.150  -39.398  1.00 85.01  ? 58   LYS   A CD   1 
ATOM   831   C  CE   . LYS   A  1  58  ? 10.508  -5.812  -40.308  1.00 90.25  ? 58   LYS   A CE   1 
ATOM   832   N  NZ   . LYS   A  1  58  ? 10.683  -6.395  -41.669  1.00 92.55  ? 58   LYS   A NZ   1 
ATOM   833   H  H    . LYS   A  1  58  ? 8.477   -7.385  -35.753  1.00 72.47  ? 58   LYS   A H    1 
ATOM   834   H  HA   . LYS   A  1  58  ? 11.142  -6.942  -35.490  1.00 71.94  ? 58   LYS   A HA   1 
ATOM   835   H  HB2  . LYS   A  1  58  ? 10.451  -7.537  -37.635  1.00 79.59  ? 58   LYS   A HB2  1 
ATOM   836   H  HB3  . LYS   A  1  58  ? 9.469   -6.288  -37.662  1.00 79.59  ? 58   LYS   A HB3  1 
ATOM   837   H  HG2  . LYS   A  1  58  ? 11.155  -4.838  -37.914  1.00 93.55  ? 58   LYS   A HG2  1 
ATOM   838   H  HG3  . LYS   A  1  58  ? 12.239  -5.900  -37.441  1.00 93.55  ? 58   LYS   A HG3  1 
ATOM   839   H  HD2  . LYS   A  1  58  ? 12.460  -5.664  -39.716  1.00 102.00 ? 58   LYS   A HD2  1 
ATOM   840   H  HD3  . LYS   A  1  58  ? 11.842  -7.105  -39.454  1.00 102.00 ? 58   LYS   A HD3  1 
ATOM   841   H  HE2  . LYS   A  1  58  ? 9.692   -6.170  -39.925  1.00 108.28 ? 58   LYS   A HE2  1 
ATOM   842   H  HE3  . LYS   A  1  58  ? 10.437  -4.848  -40.396  1.00 108.28 ? 58   LYS   A HE3  1 
ATOM   843   H  HZ1  . LYS   A  1  58  ? 9.990   -6.178  -42.185  1.00 111.04 ? 58   LYS   A HZ1  1 
ATOM   844   H  HZ2  . LYS   A  1  58  ? 11.428  -6.082  -42.041  1.00 111.04 ? 58   LYS   A HZ2  1 
ATOM   845   H  HZ3  . LYS   A  1  58  ? 10.737  -7.282  -41.616  1.00 111.04 ? 58   LYS   A HZ3  1 
ATOM   846   N  N    . CYS   A  1  59  ? 11.087  -4.634  -34.661  1.00 65.46  ? 59   CYS   A N    1 
ATOM   847   C  CA   . CYS   A  1  59  ? 10.965  -3.365  -33.957  1.00 71.30  ? 59   CYS   A CA   1 
ATOM   848   C  C    . CYS   A  1  59  ? 11.914  -2.338  -34.560  1.00 72.45  ? 59   CYS   A C    1 
ATOM   849   O  O    . CYS   A  1  59  ? 13.122  -2.581  -34.655  1.00 69.09  ? 59   CYS   A O    1 
ATOM   850   C  CB   . CYS   A  1  59  ? 11.260  -3.543  -32.463  1.00 73.55  ? 59   CYS   A CB   1 
ATOM   851   S  SG   . CYS   A  1  59  ? 10.236  -4.779  -31.618  1.00 73.42  ? 59   CYS   A SG   1 
ATOM   852   H  H    . CYS   A  1  59  ? 11.880  -4.966  -34.640  1.00 78.53  ? 59   CYS   A H    1 
ATOM   853   H  HA   . CYS   A  1  59  ? 10.062  -3.028  -34.061  1.00 85.54  ? 59   CYS   A HA   1 
ATOM   854   H  HB2  . CYS   A  1  59  ? 12.185  -3.816  -32.364  1.00 88.24  ? 59   CYS   A HB2  1 
ATOM   855   H  HB3  . CYS   A  1  59  ? 11.115  -2.693  -32.019  1.00 88.24  ? 59   CYS   A HB3  1 
ATOM   856   N  N    . ASP   A  1  60  ? 11.363  -1.194  -34.961  1.00 76.68  ? 60   ASP   A N    1 
ATOM   857   C  CA   . ASP   A  1  60  ? 12.186  -0.093  -35.441  1.00 82.46  ? 60   ASP   A CA   1 
ATOM   858   C  C    . ASP   A  1  60  ? 13.099  0.406   -34.329  1.00 79.06  ? 60   ASP   A C    1 
ATOM   859   O  O    . ASP   A  1  60  ? 12.773  0.319   -33.142  1.00 75.03  ? 60   ASP   A O    1 
ATOM   860   C  CB   . ASP   A  1  60  ? 11.313  1.061   -35.937  1.00 92.79  ? 60   ASP   A CB   1 
ATOM   861   C  CG   . ASP   A  1  60  ? 10.552  0.721   -37.202  1.00 98.87  ? 60   ASP   A CG   1 
ATOM   862   O  OD1  . ASP   A  1  60  ? 10.632  -0.440  -37.656  1.00 100.48 ? 60   ASP   A OD1  1 
ATOM   863   O  OD2  . ASP   A  1  60  ? 9.878   1.620   -37.747  1.00 103.57 ? 60   ASP   A OD2  1 
ATOM   864   H  H    . ASP   A  1  60  ? 10.518  -1.032  -34.964  1.00 92.00  ? 60   ASP   A H    1 
ATOM   865   H  HA   . ASP   A  1  60  ? 12.729  -0.404  -36.183  1.00 98.93  ? 60   ASP   A HA   1 
ATOM   866   H  HB2  . ASP   A  1  60  ? 10.666  1.285   -35.250  1.00 111.33 ? 60   ASP   A HB2  1 
ATOM   867   H  HB3  . ASP   A  1  60  ? 11.878  1.827   -36.123  1.00 111.33 ? 60   ASP   A HB3  1 
ATOM   868   N  N    . TRP   A  1  61  ? 14.249  0.945   -34.724  1.00 82.15  ? 61   TRP   A N    1 
ATOM   869   C  CA   . TRP   A  1  61  ? 15.196  1.536   -33.784  1.00 86.09  ? 61   TRP   A CA   1 
ATOM   870   C  C    . TRP   A  1  61  ? 15.085  3.055   -33.855  1.00 95.06  ? 61   TRP   A C    1 
ATOM   871   O  O    . TRP   A  1  61  ? 15.550  3.679   -34.812  1.00 95.30  ? 61   TRP   A O    1 
ATOM   872   C  CB   . TRP   A  1  61  ? 16.627  1.097   -34.073  1.00 82.85  ? 61   TRP   A CB   1 
ATOM   873   C  CG   . TRP   A  1  61  ? 17.607  1.886   -33.272  1.00 83.97  ? 61   TRP   A CG   1 
ATOM   874   C  CD1  . TRP   A  1  61  ? 17.825  1.796   -31.929  1.00 81.85  ? 61   TRP   A CD1  1 
ATOM   875   C  CD2  . TRP   A  1  61  ? 18.491  2.903   -33.755  1.00 92.72  ? 61   TRP   A CD2  1 
ATOM   876   N  NE1  . TRP   A  1  61  ? 18.793  2.691   -31.545  1.00 87.17  ? 61   TRP   A NE1  1 
ATOM   877   C  CE2  . TRP   A  1  61  ? 19.219  3.382   -32.648  1.00 92.72  ? 61   TRP   A CE2  1 
ATOM   878   C  CE3  . TRP   A  1  61  ? 18.740  3.453   -35.015  1.00 101.15 ? 61   TRP   A CE3  1 
ATOM   879   C  CZ2  . TRP   A  1  61  ? 20.178  4.383   -32.765  1.00 99.97  ? 61   TRP   A CZ2  1 
ATOM   880   C  CZ3  . TRP   A  1  61  ? 19.694  4.444   -35.129  1.00 106.42 ? 61   TRP   A CZ3  1 
ATOM   881   C  CH2  . TRP   A  1  61  ? 20.402  4.899   -34.011  1.00 106.93 ? 61   TRP   A CH2  1 
ATOM   882   H  H    . TRP   A  1  61  ? 14.507  0.981   -35.544  1.00 98.57  ? 61   TRP   A H    1 
ATOM   883   H  HA   . TRP   A  1  61  ? 14.949  1.242   -32.893  1.00 103.29 ? 61   TRP   A HA   1 
ATOM   884   H  HB2  . TRP   A  1  61  ? 16.728  0.159   -33.844  1.00 99.40  ? 61   TRP   A HB2  1 
ATOM   885   H  HB3  . TRP   A  1  61  ? 16.821  1.231   -35.014  1.00 99.40  ? 61   TRP   A HB3  1 
ATOM   886   H  HD1  . TRP   A  1  61  ? 17.381  1.214   -31.356  1.00 98.20  ? 61   TRP   A HD1  1 
ATOM   887   H  HE1  . TRP   A  1  61  ? 19.084  2.799   -30.743  1.00 104.59 ? 61   TRP   A HE1  1 
ATOM   888   H  HE3  . TRP   A  1  61  ? 18.273  3.156   -35.763  1.00 121.36 ? 61   TRP   A HE3  1 
ATOM   889   H  HZ2  . TRP   A  1  61  ? 20.649  4.689   -32.023  1.00 119.94 ? 61   TRP   A HZ2  1 
ATOM   890   H  HZ3  . TRP   A  1  61  ? 19.869  4.817   -35.963  1.00 127.69 ? 61   TRP   A HZ3  1 
ATOM   891   H  HH2  . TRP   A  1  61  ? 21.039  5.568   -34.118  1.00 128.29 ? 61   TRP   A HH2  1 
ATOM   892   N  N    . SER   A  1  62  ? 14.448  3.642   -32.842  1.00 103.92 ? 62   SER   A N    1 
ATOM   893   C  CA   . SER   A  1  62  ? 14.491  5.080   -32.601  1.00 112.70 ? 62   SER   A CA   1 
ATOM   894   C  C    . SER   A  1  62  ? 13.746  5.890   -33.655  1.00 118.96 ? 62   SER   A C    1 
ATOM   895   O  O    . SER   A  1  62  ? 13.611  7.111   -33.515  1.00 121.49 ? 62   SER   A O    1 
ATOM   896   C  CB   . SER   A  1  62  ? 15.946  5.551   -32.520  1.00 116.52 ? 62   SER   A CB   1 
ATOM   897   O  OG   . SER   A  1  62  ? 16.021  6.902   -32.101  1.00 121.18 ? 62   SER   A OG   1 
ATOM   898   H  H    . SER   A  1  62  ? 13.972  3.217   -32.265  1.00 124.69 ? 62   SER   A H    1 
ATOM   899   H  HA   . SER   A  1  62  ? 14.043  5.247   -31.757  1.00 135.22 ? 62   SER   A HA   1 
ATOM   900   H  HB2  . SER   A  1  62  ? 16.421  4.996   -31.881  1.00 139.80 ? 62   SER   A HB2  1 
ATOM   901   H  HB3  . SER   A  1  62  ? 16.353  5.470   -33.397  1.00 139.80 ? 62   SER   A HB3  1 
ATOM   902   H  HG   . SER   A  1  62  ? 15.565  7.387   -32.612  1.00 145.40 ? 62   SER   A HG   1 
ATOM   903   N  N    . SER   A  1  63  ? 13.249  5.236   -34.705  1.00 123.87 ? 63   SER   A N    1 
ATOM   904   C  CA   . SER   A  1  63  ? 12.364  5.927   -35.637  1.00 131.32 ? 63   SER   A CA   1 
ATOM   905   C  C    . SER   A  1  63  ? 11.010  6.176   -34.989  1.00 131.14 ? 63   SER   A C    1 
ATOM   906   O  O    . SER   A  1  63  ? 10.513  7.308   -34.969  1.00 131.52 ? 63   SER   A O    1 
ATOM   907   C  CB   . SER   A  1  63  ? 12.207  5.112   -36.921  1.00 133.14 ? 63   SER   A CB   1 
ATOM   908   O  OG   . SER   A  1  63  ? 13.424  5.055   -37.644  1.00 134.37 ? 63   SER   A OG   1 
ATOM   909   H  H    . SER   A  1  63  ? 13.405  4.412   -34.895  1.00 148.63 ? 63   SER   A H    1 
ATOM   910   H  HA   . SER   A  1  63  ? 12.756  6.781   -35.878  1.00 157.56 ? 63   SER   A HA   1 
ATOM   911   H  HB2  . SER   A  1  63  ? 11.936  4.210   -36.690  1.00 159.75 ? 63   SER   A HB2  1 
ATOM   912   H  HB3  . SER   A  1  63  ? 11.530  5.529   -37.477  1.00 159.75 ? 63   SER   A HB3  1 
ATOM   913   H  HG   . SER   A  1  63  ? 13.300  4.683   -38.386  1.00 161.23 ? 63   SER   A HG   1 
ATOM   914   N  N    . THR   A  1  64  ? 10.400  5.119   -34.455  1.00 128.86 ? 64   THR   A N    1 
ATOM   915   C  CA   . THR   A  1  64  ? 9.190   5.230   -33.653  1.00 124.14 ? 64   THR   A CA   1 
ATOM   916   C  C    . THR   A  1  64  ? 9.216   4.352   -32.411  1.00 117.95 ? 64   THR   A C    1 
ATOM   917   O  O    . THR   A  1  64  ? 8.342   4.514   -31.554  1.00 120.95 ? 64   THR   A O    1 
ATOM   918   C  CB   . THR   A  1  64  ? 7.957   4.863   -34.489  1.00 120.53 ? 64   THR   A CB   1 
ATOM   919   O  OG1  . THR   A  1  64  ? 7.952   3.452   -34.739  1.00 121.74 ? 64   THR   A OG1  1 
ATOM   920   C  CG2  . THR   A  1  64  ? 7.967   5.609   -35.819  1.00 115.13 ? 64   THR   A CG2  1 
ATOM   921   H  H    . THR   A  1  64  ? 10.675  4.309   -34.547  1.00 154.62 ? 64   THR   A H    1 
ATOM   922   H  HA   . THR   A  1  64  ? 9.082   6.152   -33.370  1.00 148.95 ? 64   THR   A HA   1 
ATOM   923   H  HB   . THR   A  1  64  ? 7.154   5.112   -34.006  1.00 144.62 ? 64   THR   A HB   1 
ATOM   924   H  HG1  . THR   A  1  64  ? 7.327   3.255   -35.264  1.00 146.07 ? 64   THR   A HG1  1 
ATOM   925   H  HG21 . THR   A  1  64  ? 7.150   5.426   -36.308  1.00 138.13 ? 64   THR   A HG21 1 
ATOM   926   H  HG22 . THR   A  1  64  ? 8.033   6.564   -35.663  1.00 138.13 ? 64   THR   A HG22 1 
ATOM   927   H  HG23 . THR   A  1  64  ? 8.724   5.324   -36.354  1.00 138.13 ? 64   THR   A HG23 1 
ATOM   928   N  N    . ARG   A  1  65  ? 10.183  3.440   -32.278  1.00 108.06 ? 65   ARG   A N    1 
ATOM   929   C  CA   . ARG   A  1  65  ? 10.195  2.431   -31.218  1.00 101.16 ? 65   ARG   A CA   1 
ATOM   930   C  C    . ARG   A  1  65  ? 8.969   1.525   -31.296  1.00 93.85  ? 65   ARG   A C    1 
ATOM   931   O  O    . ARG   A  1  65  ? 8.504   0.999   -30.282  1.00 90.36  ? 65   ARG   A O    1 
ATOM   932   C  CB   . ARG   A  1  65  ? 10.296  3.068   -29.828  1.00 105.38 ? 65   ARG   A CB   1 
ATOM   933   C  CG   . ARG   A  1  65  ? 11.646  3.700   -29.518  1.00 111.90 ? 65   ARG   A CG   1 
ATOM   934   C  CD   . ARG   A  1  65  ? 11.974  3.611   -28.031  1.00 118.36 ? 65   ARG   A CD   1 
ATOM   935   N  NE   . ARG   A  1  65  ? 10.843  3.983   -27.184  1.00 125.41 ? 65   ARG   A NE   1 
ATOM   936   C  CZ   . ARG   A  1  65  ? 10.908  4.127   -25.864  1.00 128.60 ? 65   ARG   A CZ   1 
ATOM   937   N  NH1  . ARG   A  1  65  ? 12.054  3.942   -25.225  1.00 127.02 ? 65   ARG   A NH1  1 
ATOM   938   N  NH2  . ARG   A  1  65  ? 9.823   4.464   -25.180  1.00 130.98 ? 65   ARG   A NH2  1 
ATOM   939   H  H    . ARG   A  1  65  ? 10.860  3.385   -32.804  1.00 129.65 ? 65   ARG   A H    1 
ATOM   940   H  HA   . ARG   A  1  65  ? 10.982  1.878   -31.343  1.00 121.37 ? 65   ARG   A HA   1 
ATOM   941   H  HB2  . ARG   A  1  65  ? 9.624   3.764   -29.758  1.00 126.44 ? 65   ARG   A HB2  1 
ATOM   942   H  HB3  . ARG   A  1  65  ? 10.134  2.382   -29.161  1.00 126.44 ? 65   ARG   A HB3  1 
ATOM   943   H  HG2  . ARG   A  1  65  ? 12.339  3.235   -30.012  1.00 134.26 ? 65   ARG   A HG2  1 
ATOM   944   H  HG3  . ARG   A  1  65  ? 11.628  4.636   -29.771  1.00 134.26 ? 65   ARG   A HG3  1 
ATOM   945   H  HD2  . ARG   A  1  65  ? 12.224  2.698   -27.815  1.00 142.01 ? 65   ARG   A HD2  1 
ATOM   946   H  HD3  . ARG   A  1  65  ? 12.709  4.211   -27.832  1.00 142.01 ? 65   ARG   A HD3  1 
ATOM   947   H  HE   . ARG   A  1  65  ? 10.084  4.118   -27.566  1.00 150.47 ? 65   ARG   A HE   1 
ATOM   948   H  HH11 . ARG   A  1  65  ? 12.762  3.727   -25.664  1.00 152.40 ? 65   ARG   A HH11 1 
ATOM   949   H  HH12 . ARG   A  1  65  ? 12.091  4.036   -24.371  1.00 152.40 ? 65   ARG   A HH12 1 
ATOM   950   H  HH21 . ARG   A  1  65  ? 9.078   4.590   -25.590  1.00 157.16 ? 65   ARG   A HH21 1 
ATOM   951   H  HH22 . ARG   A  1  65  ? 9.865   4.558   -24.326  1.00 157.16 ? 65   ARG   A HH22 1 
ATOM   952   N  N    . ARG   A  1  66  ? 8.444   1.330   -32.502  1.00 92.28  ? 66   ARG   A N    1 
ATOM   953   C  CA   . ARG   A  1  66  ? 7.259   0.518   -32.723  1.00 92.30  ? 66   ARG   A CA   1 
ATOM   954   C  C    . ARG   A  1  66  ? 7.654   -0.895  -33.134  1.00 82.81  ? 66   ARG   A C    1 
ATOM   955   O  O    . ARG   A  1  66  ? 8.651   -1.104  -33.828  1.00 78.05  ? 66   ARG   A O    1 
ATOM   956   C  CB   . ARG   A  1  66  ? 6.371   1.141   -33.803  1.00 103.87 ? 66   ARG   A CB   1 
ATOM   957   C  CG   . ARG   A  1  66  ? 5.074   0.389   -34.067  1.00 114.01 ? 66   ARG   A CG   1 
ATOM   958   C  CD   . ARG   A  1  66  ? 4.274   1.049   -35.179  1.00 125.64 ? 66   ARG   A CD   1 
ATOM   959   N  NE   . ARG   A  1  66  ? 4.975   1.001   -36.460  1.00 133.66 ? 66   ARG   A NE   1 
ATOM   960   C  CZ   . ARG   A  1  66  ? 4.615   1.686   -37.541  1.00 141.06 ? 66   ARG   A CZ   1 
ATOM   961   N  NH1  . ARG   A  1  66  ? 3.559   2.488   -37.506  1.00 144.07 ? 66   ARG   A NH1  1 
ATOM   962   N  NH2  . ARG   A  1  66  ? 5.317   1.573   -38.660  1.00 143.76 ? 66   ARG   A NH2  1 
ATOM   963   H  H    . ARG   A  1  66  ? 8.767   1.667   -33.224  1.00 110.71 ? 66   ARG   A H    1 
ATOM   964   H  HA   . ARG   A  1  66  ? 6.746   0.463   -31.901  1.00 110.74 ? 66   ARG   A HA   1 
ATOM   965   H  HB2  . ARG   A  1  66  ? 6.136   2.041   -33.527  1.00 124.63 ? 66   ARG   A HB2  1 
ATOM   966   H  HB3  . ARG   A  1  66  ? 6.868   1.168   -34.635  1.00 124.63 ? 66   ARG   A HB3  1 
ATOM   967   H  HG2  . ARG   A  1  66  ? 5.278   -0.521  -34.334  1.00 136.79 ? 66   ARG   A HG2  1 
ATOM   968   H  HG3  . ARG   A  1  66  ? 4.534   0.384   -33.261  1.00 136.79 ? 66   ARG   A HG3  1 
ATOM   969   H  HD2  . ARG   A  1  66  ? 3.426   0.588   -35.280  1.00 150.74 ? 66   ARG   A HD2  1 
ATOM   970   H  HD3  . ARG   A  1  66  ? 4.120   1.980   -34.953  1.00 150.74 ? 66   ARG   A HD3  1 
ATOM   971   H  HE   . ARG   A  1  66  ? 5.668   0.495   -36.518  1.00 160.37 ? 66   ARG   A HE   1 
ATOM   972   H  HH11 . ARG   A  1  66  ? 3.103   2.567   -36.782  1.00 172.87 ? 66   ARG   A HH11 1 
ATOM   973   H  HH12 . ARG   A  1  66  ? 3.330   2.928   -38.209  1.00 172.87 ? 66   ARG   A HH12 1 
ATOM   974   H  HH21 . ARG   A  1  66  ? 6.004   1.057   -38.686  1.00 172.50 ? 66   ARG   A HH21 1 
ATOM   975   H  HH22 . ARG   A  1  66  ? 5.084   2.015   -39.360  1.00 172.50 ? 66   ARG   A HH22 1 
ATOM   976   N  N    . CYS   A  1  67  ? 6.858   -1.864  -32.691  1.00 81.31  ? 67   CYS   A N    1 
ATOM   977   C  CA   . CYS   A  1  67  ? 7.038   -3.263  -33.047  1.00 78.98  ? 67   CYS   A CA   1 
ATOM   978   C  C    . CYS   A  1  67  ? 5.812   -3.752  -33.804  1.00 79.80  ? 67   CYS   A C    1 
ATOM   979   O  O    . CYS   A  1  67  ? 4.675   -3.446  -33.429  1.00 86.33  ? 67   CYS   A O    1 
ATOM   980   C  CB   . CYS   A  1  67  ? 7.254   -4.134  -31.805  1.00 77.42  ? 67   CYS   A CB   1 
ATOM   981   S  SG   . CYS   A  1  67  ? 8.704   -3.714  -30.803  1.00 82.16  ? 67   CYS   A SG   1 
ATOM   982   H  H    . CYS   A  1  67  ? 6.189   -1.729  -32.168  1.00 97.56  ? 67   CYS   A H    1 
ATOM   983   H  HA   . CYS   A  1  67  ? 7.816   -3.353  -33.618  1.00 94.75  ? 67   CYS   A HA   1 
ATOM   984   H  HB2  . CYS   A  1  67  ? 6.474   -4.050  -31.234  1.00 92.88  ? 67   CYS   A HB2  1 
ATOM   985   H  HB3  . CYS   A  1  67  ? 7.357   -5.055  -32.092  1.00 92.88  ? 67   CYS   A HB3  1 
ATOM   986   N  N    . GLN   A  1  68  ? 6.048   -4.511  -34.872  1.00 74.51  ? 68   GLN   A N    1 
ATOM   987   C  CA   . GLN   A  1  68  ? 4.978   -5.125  -35.641  1.00 73.84  ? 68   GLN   A CA   1 
ATOM   988   C  C    . GLN   A  1  68  ? 5.279   -6.604  -35.838  1.00 69.61  ? 68   GLN   A C    1 
ATOM   989   O  O    . GLN   A  1  68  ? 6.435   -6.975  -36.073  1.00 68.67  ? 68   GLN   A O    1 
ATOM   990   C  CB   . GLN   A  1  68  ? 4.811   -4.437  -37.002  1.00 80.33  ? 68   GLN   A CB   1 
ATOM   991   C  CG   . GLN   A  1  68  ? 4.136   -3.078  -36.919  1.00 91.80  ? 68   GLN   A CG   1 
ATOM   992   C  CD   . GLN   A  1  68  ? 4.087   -2.366  -38.256  1.00 103.98 ? 68   GLN   A CD   1 
ATOM   993   O  OE1  . GLN   A  1  68  ? 4.555   -2.887  -39.268  1.00 109.08 ? 68   GLN   A OE1  1 
ATOM   994   N  NE2  . GLN   A  1  68  ? 3.518   -1.167  -38.265  1.00 109.30 ? 68   GLN   A NE2  1 
ATOM   995   H  H    . GLN   A  1  68  ? 6.834   -4.686  -35.174  1.00 89.39  ? 68   GLN   A H    1 
ATOM   996   H  HA   . GLN   A  1  68  ? 4.140   -5.041  -35.160  1.00 88.59  ? 68   GLN   A HA   1 
ATOM   997   H  HB2  . GLN   A  1  68  ? 5.687   -4.310  -37.398  1.00 96.38  ? 68   GLN   A HB2  1 
ATOM   998   H  HB3  . GLN   A  1  68  ? 4.268   -5.003  -37.574  1.00 96.38  ? 68   GLN   A HB3  1 
ATOM   999   H  HG2  . GLN   A  1  68  ? 3.225   -3.196  -36.608  1.00 110.15 ? 68   GLN   A HG2  1 
ATOM   1000  H  HG3  . GLN   A  1  68  ? 4.629   -2.518  -36.299  1.00 110.15 ? 68   GLN   A HG3  1 
ATOM   1001  H  HE21 . GLN   A  1  68  ? 3.203   -0.835  -37.537  1.00 131.14 ? 68   GLN   A HE21 1 
ATOM   1002  H  HE22 . GLN   A  1  68  ? 3.466   -0.722  -38.999  1.00 131.14 ? 68   GLN   A HE22 1 
ATOM   1003  N  N    . PRO   A  1  69  ? 4.273   -7.473  -35.743  1.00 67.02  ? 69   PRO   A N    1 
ATOM   1004  C  CA   . PRO   A  1  69  ? 4.534   -8.906  -35.917  1.00 63.78  ? 69   PRO   A CA   1 
ATOM   1005  C  C    . PRO   A  1  69  ? 4.981   -9.228  -37.333  1.00 64.14  ? 69   PRO   A C    1 
ATOM   1006  O  O    . PRO   A  1  69  ? 4.539   -8.616  -38.308  1.00 70.97  ? 69   PRO   A O    1 
ATOM   1007  C  CB   . PRO   A  1  69  ? 3.182   -9.561  -35.603  1.00 64.03  ? 69   PRO   A CB   1 
ATOM   1008  C  CG   . PRO   A  1  69  ? 2.394   -8.523  -34.876  1.00 66.27  ? 69   PRO   A CG   1 
ATOM   1009  C  CD   . PRO   A  1  69  ? 2.860   -7.212  -35.415  1.00 67.04  ? 69   PRO   A CD   1 
ATOM   1010  H  HA   . PRO   A  1  69  ? 5.202   -9.211  -35.284  1.00 76.52  ? 69   PRO   A HA   1 
ATOM   1011  H  HB2  . PRO   A  1  69  ? 2.740   -9.813  -36.429  1.00 76.82  ? 69   PRO   A HB2  1 
ATOM   1012  H  HB3  . PRO   A  1  69  ? 3.318   -10.343 -35.047  1.00 76.82  ? 69   PRO   A HB3  1 
ATOM   1013  H  HG2  . PRO   A  1  69  ? 1.448   -8.649  -35.049  1.00 79.51  ? 69   PRO   A HG2  1 
ATOM   1014  H  HG3  . PRO   A  1  69  ? 2.569   -8.586  -33.924  1.00 79.51  ? 69   PRO   A HG3  1 
ATOM   1015  H  HD2  . PRO   A  1  69  ? 2.360   -6.966  -36.208  1.00 80.42  ? 69   PRO   A HD2  1 
ATOM   1016  H  HD3  . PRO   A  1  69  ? 2.783   -6.515  -34.744  1.00 80.42  ? 69   PRO   A HD3  1 
ATOM   1017  N  N    . ILE   A  1  70  ? 5.877   -10.204 -37.435  1.00 63.87  ? 70   ILE   A N    1 
ATOM   1018  C  CA   . ILE   A  1  70  ? 6.304   -10.740 -38.721  1.00 65.20  ? 70   ILE   A CA   1 
ATOM   1019  C  C    . ILE   A  1  70  ? 5.365   -11.877 -39.094  1.00 70.43  ? 70   ILE   A C    1 
ATOM   1020  O  O    . ILE   A  1  70  ? 5.158   -12.808 -38.306  1.00 73.74  ? 70   ILE   A O    1 
ATOM   1021  C  CB   . ILE   A  1  70  ? 7.763   -11.223 -38.665  1.00 61.26  ? 70   ILE   A CB   1 
ATOM   1022  C  CG1  . ILE   A  1  70  ? 8.697   -10.066 -38.301  1.00 61.83  ? 70   ILE   A CG1  1 
ATOM   1023  C  CG2  . ILE   A  1  70  ? 8.175   -11.837 -40.004  1.00 60.10  ? 70   ILE   A CG2  1 
ATOM   1024  C  CD1  . ILE   A  1  70  ? 10.152  -10.478 -38.138  1.00 62.03  ? 70   ILE   A CD1  1 
ATOM   1025  H  H    . ILE   A  1  70  ? 6.258   -10.579 -36.761  1.00 76.62  ? 70   ILE   A H    1 
ATOM   1026  H  HA   . ILE   A  1  70  ? 6.244   -10.047 -39.398  1.00 78.22  ? 70   ILE   A HA   1 
ATOM   1027  H  HB   . ILE   A  1  70  ? 7.830   -11.903 -37.977  1.00 73.49  ? 70   ILE   A HB   1 
ATOM   1028  H  HG12 . ILE   A  1  70  ? 8.656   -9.400  -39.005  1.00 74.18  ? 70   ILE   A HG12 1 
ATOM   1029  H  HG13 . ILE   A  1  70  ? 8.403   -9.681  -37.461  1.00 74.18  ? 70   ILE   A HG13 1 
ATOM   1030  H  HG21 . ILE   A  1  70  ? 9.089   -12.154 -39.938  1.00 72.10  ? 70   ILE   A HG21 1 
ATOM   1031  H  HG22 . ILE   A  1  70  ? 7.582   -12.577 -40.208  1.00 72.10  ? 70   ILE   A HG22 1 
ATOM   1032  H  HG23 . ILE   A  1  70  ? 8.109   -11.160 -40.696  1.00 72.10  ? 70   ILE   A HG23 1 
ATOM   1033  H  HD11 . ILE   A  1  70  ? 10.658  -9.722  -37.802  1.00 74.42  ? 70   ILE   A HD11 1 
ATOM   1034  H  HD12 . ILE   A  1  70  ? 10.203  -11.216 -37.510  1.00 74.42  ? 70   ILE   A HD12 1 
ATOM   1035  H  HD13 . ILE   A  1  70  ? 10.501  -10.753 -39.000  1.00 74.42  ? 70   ILE   A HD13 1 
ATOM   1036  N  N    . GLU   A  1  71  ? 4.796   -11.808 -40.295  1.00 72.95  ? 71   GLU   A N    1 
ATOM   1037  C  CA   . GLU   A  1  71  ? 3.864   -12.830 -40.766  1.00 71.62  ? 71   GLU   A CA   1 
ATOM   1038  C  C    . GLU   A  1  71  ? 4.663   -14.018 -41.286  1.00 67.11  ? 71   GLU   A C    1 
ATOM   1039  O  O    . GLU   A  1  71  ? 4.977   -14.115 -42.474  1.00 66.79  ? 71   GLU   A O    1 
ATOM   1040  C  CB   . GLU   A  1  71  ? 2.941   -12.271 -41.842  1.00 77.41  ? 71   GLU   A CB   1 
ATOM   1041  C  CG   . GLU   A  1  71  ? 1.949   -13.290 -42.387  1.00 84.31  ? 71   GLU   A CG   1 
ATOM   1042  C  CD   . GLU   A  1  71  ? 1.121   -12.748 -43.534  1.00 95.16  ? 71   GLU   A CD   1 
ATOM   1043  O  OE1  . GLU   A  1  71  ? 0.851   -11.528 -43.553  1.00 100.91 ? 71   GLU   A OE1  1 
ATOM   1044  O  OE2  . GLU   A  1  71  ? 0.744   -13.542 -44.421  1.00 98.45  ? 71   GLU   A OE2  1 
ATOM   1045  H  H    . GLU   A  1  71  ? 4.935   -11.174 -40.860  1.00 87.53  ? 71   GLU   A H    1 
ATOM   1046  H  HA   . GLU   A  1  71  ? 3.322   -13.128 -40.018  1.00 85.92  ? 71   GLU   A HA   1 
ATOM   1047  H  HB2  . GLU   A  1  71  ? 2.433   -11.535 -41.466  1.00 92.87  ? 71   GLU   A HB2  1 
ATOM   1048  H  HB3  . GLU   A  1  71  ? 3.481   -11.957 -42.584  1.00 92.87  ? 71   GLU   A HB3  1 
ATOM   1049  H  HG2  . GLU   A  1  71  ? 2.437   -14.064 -42.708  1.00 101.15 ? 71   GLU   A HG2  1 
ATOM   1050  H  HG3  . GLU   A  1  71  ? 1.342   -13.551 -41.677  1.00 101.15 ? 71   GLU   A HG3  1 
ATOM   1051  N  N    . PHE   A  1  72  ? 5.000   -14.938 -40.381  1.00 64.01  ? 72   PHE   A N    1 
ATOM   1052  C  CA   . PHE   A  1  72  ? 5.589   -16.205 -40.799  1.00 64.68  ? 72   PHE   A CA   1 
ATOM   1053  C  C    . PHE   A  1  72  ? 4.523   -17.154 -41.331  1.00 68.93  ? 72   PHE   A C    1 
ATOM   1054  O  O    . PHE   A  1  72  ? 4.711   -17.788 -42.375  1.00 72.36  ? 72   PHE   A O    1 
ATOM   1055  C  CB   . PHE   A  1  72  ? 6.331   -16.863 -39.634  1.00 64.99  ? 72   PHE   A CB   1 
ATOM   1056  C  CG   . PHE   A  1  72  ? 7.671   -16.252 -39.335  1.00 63.46  ? 72   PHE   A CG   1 
ATOM   1057  C  CD1  . PHE   A  1  72  ? 8.809   -16.689 -39.992  1.00 61.52  ? 72   PHE   A CD1  1 
ATOM   1058  C  CD2  . PHE   A  1  72  ? 7.795   -15.252 -38.385  1.00 66.23  ? 72   PHE   A CD2  1 
ATOM   1059  C  CE1  . PHE   A  1  72  ? 10.044  -16.133 -39.714  1.00 64.56  ? 72   PHE   A CE1  1 
ATOM   1060  C  CE2  . PHE   A  1  72  ? 9.027   -14.692 -38.103  1.00 67.27  ? 72   PHE   A CE2  1 
ATOM   1061  C  CZ   . PHE   A  1  72  ? 10.152  -15.134 -38.768  1.00 67.24  ? 72   PHE   A CZ   1 
ATOM   1062  H  H    . PHE   A  1  72  ? 4.898   -14.853 -39.531  1.00 76.80  ? 72   PHE   A H    1 
ATOM   1063  H  HA   . PHE   A  1  72  ? 6.231   -16.025 -41.503  1.00 77.60  ? 72   PHE   A HA   1 
ATOM   1064  H  HB2  . PHE   A  1  72  ? 5.787   -16.785 -38.835  1.00 77.97  ? 72   PHE   A HB2  1 
ATOM   1065  H  HB3  . PHE   A  1  72  ? 6.476   -17.798 -39.847  1.00 77.97  ? 72   PHE   A HB3  1 
ATOM   1066  H  HD1  . PHE   A  1  72  ? 8.741   -17.364 -40.627  1.00 73.81  ? 72   PHE   A HD1  1 
ATOM   1067  H  HD2  . PHE   A  1  72  ? 7.040   -14.953 -37.931  1.00 79.46  ? 72   PHE   A HD2  1 
ATOM   1068  H  HE1  . PHE   A  1  72  ? 10.801  -16.432 -40.164  1.00 77.45  ? 72   PHE   A HE1  1 
ATOM   1069  H  HE2  . PHE   A  1  72  ? 9.098   -14.019 -37.466  1.00 80.70  ? 72   PHE   A HE2  1 
ATOM   1070  H  HZ   . PHE   A  1  72  ? 10.982  -14.759 -38.579  1.00 80.67  ? 72   PHE   A HZ   1 
ATOM   1071  N  N    . ASP   A  1  73  ? 3.400   -17.261 -40.622  1.00 68.65  ? 73   ASP   A N    1 
ATOM   1072  C  CA   . ASP   A  1  73  ? 2.326   -18.178 -40.988  1.00 64.91  ? 73   ASP   A CA   1 
ATOM   1073  C  C    . ASP   A  1  73  ? 1.015   -17.618 -40.461  1.00 67.57  ? 73   ASP   A C    1 
ATOM   1074  O  O    . ASP   A  1  73  ? 0.843   -17.482 -39.245  1.00 70.59  ? 73   ASP   A O    1 
ATOM   1075  C  CB   . ASP   A  1  73  ? 2.586   -19.576 -40.423  1.00 59.78  ? 73   ASP   A CB   1 
ATOM   1076  C  CG   . ASP   A  1  73  ? 1.319   -20.395 -40.281  1.00 59.48  ? 73   ASP   A CG   1 
ATOM   1077  O  OD1  . ASP   A  1  73  ? 0.524   -20.437 -41.244  1.00 60.30  ? 73   ASP   A OD1  1 
ATOM   1078  O  OD2  . ASP   A  1  73  ? 1.123   -21.007 -39.209  1.00 58.80  ? 73   ASP   A OD2  1 
ATOM   1079  H  H    . ASP   A  1  73  ? 3.234   -16.804 -39.913  1.00 82.37  ? 73   ASP   A H    1 
ATOM   1080  H  HA   . ASP   A  1  73  ? 2.265   -18.244 -41.954  1.00 77.87  ? 73   ASP   A HA   1 
ATOM   1081  H  HB2  . ASP   A  1  73  ? 3.186   -20.052 -41.019  1.00 71.72  ? 73   ASP   A HB2  1 
ATOM   1082  H  HB3  . ASP   A  1  73  ? 2.989   -19.493 -39.544  1.00 71.72  ? 73   ASP   A HB3  1 
ATOM   1083  N  N    . ALA   A  1  74  ? 0.098   -17.296 -41.371  1.00 67.63  ? 74   ALA   A N    1 
ATOM   1084  C  CA   . ALA   A  1  74  ? -1.187  -16.708 -41.021  1.00 70.17  ? 74   ALA   A CA   1 
ATOM   1085  C  C    . ALA   A  1  74  ? -2.306  -17.735 -40.924  1.00 66.71  ? 74   ALA   A C    1 
ATOM   1086  O  O    . ALA   A  1  74  ? -3.454  -17.356 -40.671  1.00 66.23  ? 74   ALA   A O    1 
ATOM   1087  C  CB   . ALA   A  1  74  ? -1.571  -15.637 -42.049  1.00 73.26  ? 74   ALA   A CB   1 
ATOM   1088  H  H    . ALA   A  1  74  ? 0.202   -17.413 -42.217  1.00 81.13  ? 74   ALA   A H    1 
ATOM   1089  H  HA   . ALA   A  1  74  ? -1.101  -16.280 -40.155  1.00 84.18  ? 74   ALA   A HA   1 
ATOM   1090  H  HB1  . ALA   A  1  74  ? -2.429  -15.257 -41.804  1.00 87.89  ? 74   ALA   A HB1  1 
ATOM   1091  H  HB2  . ALA   A  1  74  ? -0.892  -14.944 -42.052  1.00 87.89  ? 74   ALA   A HB2  1 
ATOM   1092  H  HB3  . ALA   A  1  74  ? -1.629  -16.047 -42.926  1.00 87.89  ? 74   ALA   A HB3  1 
ATOM   1093  N  N    . THR   A  1  75  ? -2.005  -19.016 -41.113  1.00 62.22  ? 75   THR   A N    1 
ATOM   1094  C  CA   . THR   A  1  75  ? -3.019  -20.058 -41.159  1.00 60.08  ? 75   THR   A CA   1 
ATOM   1095  C  C    . THR   A  1  75  ? -3.163  -20.737 -39.802  1.00 60.54  ? 75   THR   A C    1 
ATOM   1096  O  O    . THR   A  1  75  ? -2.292  -20.644 -38.933  1.00 59.25  ? 75   THR   A O    1 
ATOM   1097  C  CB   . THR   A  1  75  ? -2.675  -21.108 -42.222  1.00 58.14  ? 75   THR   A CB   1 
ATOM   1098  O  OG1  . THR   A  1  75  ? -1.529  -21.864 -41.805  1.00 57.23  ? 75   THR   A OG1  1 
ATOM   1099  C  CG2  . THR   A  1  75  ? -2.377  -20.443 -43.555  1.00 55.40  ? 75   THR   A CG2  1 
ATOM   1100  H  H    . THR   A  1  75  ? -1.204  -19.309 -41.220  1.00 74.64  ? 75   THR   A H    1 
ATOM   1101  H  HA   . THR   A  1  75  ? -3.870  -19.653 -41.389  1.00 72.08  ? 75   THR   A HA   1 
ATOM   1102  H  HB   . THR   A  1  75  ? -3.431  -21.704 -42.338  1.00 69.74  ? 75   THR   A HB   1 
ATOM   1103  H  HG1  . THR   A  1  75  ? -0.878  -21.351 -41.672  1.00 68.65  ? 75   THR   A HG1  1 
ATOM   1104  H  HG21 . THR   A  1  75  ? -2.203  -21.118 -44.230  1.00 66.46  ? 75   THR   A HG21 1 
ATOM   1105  H  HG22 . THR   A  1  75  ? -3.134  -19.905 -43.834  1.00 66.46  ? 75   THR   A HG22 1 
ATOM   1106  H  HG23 . THR   A  1  75  ? -1.597  -19.871 -43.474  1.00 66.46  ? 75   THR   A HG23 1 
ATOM   1107  N  N    . GLY   A  1  76  ? -4.284  -21.425 -39.635  1.00 59.31  ? 76   GLY   A N    1 
ATOM   1108  C  CA   . GLY   A  1  76  ? -4.547  -22.224 -38.455  1.00 59.71  ? 76   GLY   A CA   1 
ATOM   1109  C  C    . GLY   A  1  76  ? -4.014  -23.631 -38.598  1.00 59.89  ? 76   GLY   A C    1 
ATOM   1110  O  O    . GLY   A  1  76  ? -2.990  -23.874 -39.244  1.00 59.00  ? 76   GLY   A O    1 
ATOM   1111  H  H    . GLY   A  1  76  ? -4.924  -21.442 -40.209  1.00 71.15  ? 76   GLY   A H    1 
ATOM   1112  H  HA2  . GLY   A  1  76  ? -4.125  -21.811 -37.686  1.00 71.63  ? 76   GLY   A HA2  1 
ATOM   1113  H  HA3  . GLY   A  1  76  ? -5.504  -22.271 -38.304  1.00 71.63  ? 76   GLY   A HA3  1 
ATOM   1114  N  N    . ASN   A  1  77  ? -4.726  -24.577 -37.992  1.00 60.90  ? 77   ASN   A N    1 
ATOM   1115  C  CA   . ASN   A  1  77  ? -4.326  -25.976 -38.043  1.00 57.67  ? 77   ASN   A CA   1 
ATOM   1116  C  C    . ASN   A  1  77  ? -4.820  -26.620 -39.331  1.00 58.06  ? 77   ASN   A C    1 
ATOM   1117  O  O    . ASN   A  1  77  ? -6.002  -26.517 -39.675  1.00 60.59  ? 77   ASN   A O    1 
ATOM   1118  C  CB   . ASN   A  1  77  ? -4.881  -26.736 -36.839  1.00 55.24  ? 77   ASN   A CB   1 
ATOM   1119  C  CG   . ASN   A  1  77  ? -4.268  -26.286 -35.532  1.00 57.23  ? 77   ASN   A CG   1 
ATOM   1120  O  OD1  . ASN   A  1  77  ? -3.146  -25.782 -35.499  1.00 57.18  ? 77   ASN   A OD1  1 
ATOM   1121  N  ND2  . ASN   A  1  77  ? -5.002  -26.472 -34.442  1.00 57.41  ? 77   ASN   A ND2  1 
ATOM   1122  H  H    . ASN   A  1  77  ? -5.445  -24.433 -37.544  1.00 73.06  ? 77   ASN   A H    1 
ATOM   1123  H  HA   . ASN   A  1  77  ? -3.358  -26.028 -38.022  1.00 69.19  ? 77   ASN   A HA   1 
ATOM   1124  H  HB2  . ASN   A  1  77  ? -5.838  -26.591 -36.787  1.00 66.26  ? 77   ASN   A HB2  1 
ATOM   1125  H  HB3  . ASN   A  1  77  ? -4.694  -27.681 -36.948  1.00 66.26  ? 77   ASN   A HB3  1 
ATOM   1126  H  HD21 . ASN   A  1  77  ? -4.698  -26.233 -33.673  1.00 68.87  ? 77   ASN   A HD21 1 
ATOM   1127  H  HD22 . ASN   A  1  77  ? -5.780  -26.832 -34.503  1.00 68.87  ? 77   ASN   A HD22 1 
ATOM   1128  N  N    . ARG   A  1  78  ? -3.912  -27.281 -40.044  1.00 56.62  ? 78   ARG   A N    1 
ATOM   1129  C  CA   . ARG   A  1  78  ? -4.310  -28.108 -41.171  1.00 57.07  ? 78   ARG   A CA   1 
ATOM   1130  C  C    . ARG   A  1  78  ? -5.118  -29.304 -40.682  1.00 59.85  ? 78   ARG   A C    1 
ATOM   1131  O  O    . ARG   A  1  78  ? -4.975  -29.755 -39.542  1.00 62.83  ? 78   ARG   A O    1 
ATOM   1132  C  CB   . ARG   A  1  78  ? -3.084  -28.585 -41.948  1.00 56.45  ? 78   ARG   A CB   1 
ATOM   1133  C  CG   . ARG   A  1  78  ? -2.472  -27.523 -42.846  1.00 55.07  ? 78   ARG   A CG   1 
ATOM   1134  C  CD   . ARG   A  1  78  ? -1.164  -27.995 -43.454  1.00 54.79  ? 78   ARG   A CD   1 
ATOM   1135  N  NE   . ARG   A  1  78  ? -0.079  -28.005 -42.476  1.00 57.73  ? 78   ARG   A NE   1 
ATOM   1136  C  CZ   . ARG   A  1  78  ? 1.194   -28.244 -42.772  1.00 59.61  ? 78   ARG   A CZ   1 
ATOM   1137  N  NH1  . ARG   A  1  78  ? 1.552   -28.494 -44.025  1.00 61.51  ? 78   ARG   A NH1  1 
ATOM   1138  N  NH2  . ARG   A  1  78  ? 2.113   -28.232 -41.815  1.00 57.25  ? 78   ARG   A NH2  1 
ATOM   1139  H  H    . ARG   A  1  78  ? -3.065  -27.266 -39.894  1.00 67.93  ? 78   ARG   A H    1 
ATOM   1140  H  HA   . ARG   A  1  78  ? -4.861  -27.590 -41.779  1.00 68.47  ? 78   ARG   A HA   1 
ATOM   1141  H  HB2  . ARG   A  1  78  ? -2.404  -28.864 -41.315  1.00 67.73  ? 78   ARG   A HB2  1 
ATOM   1142  H  HB3  . ARG   A  1  78  ? -3.342  -29.333 -42.509  1.00 67.73  ? 78   ARG   A HB3  1 
ATOM   1143  H  HG2  . ARG   A  1  78  ? -3.087  -27.319 -43.567  1.00 66.07  ? 78   ARG   A HG2  1 
ATOM   1144  H  HG3  . ARG   A  1  78  ? -2.295  -26.724 -42.324  1.00 66.07  ? 78   ARG   A HG3  1 
ATOM   1145  H  HD2  . ARG   A  1  78  ? -1.276  -28.897 -43.792  1.00 65.73  ? 78   ARG   A HD2  1 
ATOM   1146  H  HD3  . ARG   A  1  78  ? -0.915  -27.398 -44.176  1.00 65.73  ? 78   ARG   A HD3  1 
ATOM   1147  H  HE   . ARG   A  1  78  ? -0.278  -27.846 -41.654  1.00 69.26  ? 78   ARG   A HE   1 
ATOM   1148  H  HH11 . ARG   A  1  78  ? 0.959   -28.501 -44.648  1.00 73.80  ? 78   ARG   A HH11 1 
ATOM   1149  H  HH12 . ARG   A  1  78  ? 2.377   -28.648 -44.214  1.00 73.80  ? 78   ARG   A HH12 1 
ATOM   1150  H  HH21 . ARG   A  1  78  ? 1.884   -28.069 -41.002  1.00 68.68  ? 78   ARG   A HH21 1 
ATOM   1151  H  HH22 . ARG   A  1  78  ? 2.937   -28.387 -42.007  1.00 68.68  ? 78   ARG   A HH22 1 
ATOM   1152  N  N    . ASP   A  1  79  ? -5.979  -29.813 -41.556  1.00 60.09  ? 79   ASP   A N    1 
ATOM   1153  C  CA   . ASP   A  1  79  ? -6.832  -30.951 -41.249  1.00 62.63  ? 79   ASP   A CA   1 
ATOM   1154  C  C    . ASP   A  1  79  ? -6.313  -32.193 -41.958  1.00 62.64  ? 79   ASP   A C    1 
ATOM   1155  O  O    . ASP   A  1  79  ? -6.062  -32.163 -43.168  1.00 62.84  ? 79   ASP   A O    1 
ATOM   1156  C  CB   . ASP   A  1  79  ? -8.280  -30.687 -41.670  1.00 62.28  ? 79   ASP   A CB   1 
ATOM   1157  C  CG   . ASP   A  1  79  ? -9.033  -29.831 -40.673  1.00 65.29  ? 79   ASP   A CG   1 
ATOM   1158  O  OD1  . ASP   A  1  79  ? -8.421  -29.396 -39.675  1.00 66.32  ? 79   ASP   A OD1  1 
ATOM   1159  O  OD2  . ASP   A  1  79  ? -10.242 -29.598 -40.886  1.00 67.85  ? 79   ASP   A OD2  1 
ATOM   1160  H  H    . ASP   A  1  79  ? -6.089  -29.506 -42.352  1.00 72.09  ? 79   ASP   A H    1 
ATOM   1161  H  HA   . ASP   A  1  79  ? -6.808  -31.110 -40.292  1.00 75.13  ? 79   ASP   A HA   1 
ATOM   1162  H  HB2  . ASP   A  1  79  ? -8.281  -30.226 -42.524  1.00 74.71  ? 79   ASP   A HB2  1 
ATOM   1163  H  HB3  . ASP   A  1  79  ? -8.745  -31.535 -41.750  1.00 74.71  ? 79   ASP   A HB3  1 
ATOM   1164  N  N    . TYR   A  1  80  ? -6.146  -33.279 -41.201  1.00 63.23  ? 80   TYR   A N    1 
ATOM   1165  C  CA   . TYR   A  1  80  ? -5.999  -34.586 -41.829  1.00 64.85  ? 80   TYR   A CA   1 
ATOM   1166  C  C    . TYR   A  1  80  ? -7.331  -35.068 -42.387  1.00 63.61  ? 80   TYR   A C    1 
ATOM   1167  O  O    . TYR   A  1  80  ? -7.365  -35.742 -43.422  1.00 64.01  ? 80   TYR   A O    1 
ATOM   1168  C  CB   . TYR   A  1  80  ? -5.448  -35.602 -40.829  1.00 67.09  ? 80   TYR   A CB   1 
ATOM   1169  C  CG   . TYR   A  1  80  ? -5.458  -37.024 -41.347  1.00 70.36  ? 80   TYR   A CG   1 
ATOM   1170  C  CD1  . TYR   A  1  80  ? -4.374  -37.537 -42.046  1.00 69.82  ? 80   TYR   A CD1  1 
ATOM   1171  C  CD2  . TYR   A  1  80  ? -6.555  -37.851 -41.140  1.00 73.19  ? 80   TYR   A CD2  1 
ATOM   1172  C  CE1  . TYR   A  1  80  ? -4.381  -38.834 -42.523  1.00 73.02  ? 80   TYR   A CE1  1 
ATOM   1173  C  CE2  . TYR   A  1  80  ? -6.572  -39.149 -41.614  1.00 75.41  ? 80   TYR   A CE2  1 
ATOM   1174  C  CZ   . TYR   A  1  80  ? -5.482  -39.635 -42.304  1.00 76.11  ? 80   TYR   A CZ   1 
ATOM   1175  O  OH   . TYR   A  1  80  ? -5.493  -40.927 -42.777  1.00 81.65  ? 80   TYR   A OH   1 
ATOM   1176  H  H    . TYR   A  1  80  ? -6.116  -33.284 -40.341  1.00 75.85  ? 80   TYR   A H    1 
ATOM   1177  H  HA   . TYR   A  1  80  ? -5.360  -34.518 -42.556  1.00 77.80  ? 80   TYR   A HA   1 
ATOM   1178  H  HB2  . TYR   A  1  80  ? -4.530  -35.368 -40.620  1.00 80.49  ? 80   TYR   A HB2  1 
ATOM   1179  H  HB3  . TYR   A  1  80  ? -5.989  -35.574 -40.025  1.00 80.49  ? 80   TYR   A HB3  1 
ATOM   1180  H  HD1  . TYR   A  1  80  ? -3.630  -36.999 -42.196  1.00 83.77  ? 80   TYR   A HD1  1 
ATOM   1181  H  HD2  . TYR   A  1  80  ? -7.292  -37.526 -40.674  1.00 87.81  ? 80   TYR   A HD2  1 
ATOM   1182  H  HE1  . TYR   A  1  80  ? -3.647  -39.165 -42.989  1.00 87.60  ? 80   TYR   A HE1  1 
ATOM   1183  H  HE2  . TYR   A  1  80  ? -7.314  -39.691 -41.469  1.00 90.47  ? 80   TYR   A HE2  1 
ATOM   1184  H  HH   . TYR   A  1  80  ? -4.778  -41.089 -43.187  1.00 97.97  ? 80   TYR   A HH   1 
ATOM   1185  N  N    . ALA   A  1  81  ? -8.426  -34.734 -41.711  1.00 64.80  ? 81   ALA   A N    1 
ATOM   1186  C  CA   . ALA   A  1  81  ? -9.775  -35.033 -42.172  1.00 67.09  ? 81   ALA   A CA   1 
ATOM   1187  C  C    . ALA   A  1  81  ? -10.719 -34.075 -41.455  1.00 73.07  ? 81   ALA   A C    1 
ATOM   1188  O  O    . ALA   A  1  81  ? -10.299 -33.284 -40.605  1.00 75.00  ? 81   ALA   A O    1 
ATOM   1189  C  CB   . ALA   A  1  81  ? -10.140 -36.497 -41.914  1.00 64.70  ? 81   ALA   A CB   1 
ATOM   1190  H  H    . ALA   A  1  81  ? -8.412  -34.321 -40.957  1.00 77.74  ? 81   ALA   A H    1 
ATOM   1191  H  HA   . ALA   A  1  81  ? -9.837  -34.879 -43.127  1.00 80.49  ? 81   ALA   A HA   1 
ATOM   1192  H  HB1  . ALA   A  1  81  ? -11.043 -36.657 -42.231  1.00 77.62  ? 81   ALA   A HB1  1 
ATOM   1193  H  HB2  . ALA   A  1  81  ? -9.516  -37.067 -42.391  1.00 77.62  ? 81   ALA   A HB2  1 
ATOM   1194  H  HB3  . ALA   A  1  81  ? -10.088 -36.673 -40.962  1.00 77.62  ? 81   ALA   A HB3  1 
ATOM   1195  N  N    . LYS   A  1  82  ? -12.002 -34.144 -41.802  1.00 74.78  ? 82   LYS   A N    1 
ATOM   1196  C  CA   . LYS   A  1  82  ? -12.981 -33.272 -41.167  1.00 78.49  ? 82   LYS   A CA   1 
ATOM   1197  C  C    . LYS   A  1  82  ? -13.003 -33.529 -39.666  1.00 81.19  ? 82   LYS   A C    1 
ATOM   1198  O  O    . LYS   A  1  82  ? -13.157 -34.670 -39.221  1.00 85.52  ? 82   LYS   A O    1 
ATOM   1199  C  CB   . LYS   A  1  82  ? -14.369 -33.498 -41.763  1.00 81.76  ? 82   LYS   A CB   1 
ATOM   1200  C  CG   . LYS   A  1  82  ? -15.329 -32.330 -41.550  1.00 88.42  ? 82   LYS   A CG   1 
ATOM   1201  C  CD   . LYS   A  1  82  ? -16.762 -32.703 -41.907  1.00 96.13  ? 82   LYS   A CD   1 
ATOM   1202  C  CE   . LYS   A  1  82  ? -17.639 -31.471 -42.098  1.00 102.23 ? 82   LYS   A CE   1 
ATOM   1203  N  NZ   . LYS   A  1  82  ? -17.279 -30.709 -43.327  1.00 105.76 ? 82   LYS   A NZ   1 
ATOM   1204  H  H    . LYS   A  1  82  ? -12.325 -34.680 -42.393  1.00 89.71  ? 82   LYS   A H    1 
ATOM   1205  H  HA   . LYS   A  1  82  ? -12.738 -32.346 -41.325  1.00 94.17  ? 82   LYS   A HA   1 
ATOM   1206  H  HB2  . LYS   A  1  82  ? -14.279 -33.636 -42.719  1.00 98.09  ? 82   LYS   A HB2  1 
ATOM   1207  H  HB3  . LYS   A  1  82  ? -14.762 -34.282 -41.350  1.00 98.09  ? 82   LYS   A HB3  1 
ATOM   1208  H  HG2  . LYS   A  1  82  ? -15.308 -32.064 -40.618  1.00 106.09 ? 82   LYS   A HG2  1 
ATOM   1209  H  HG3  . LYS   A  1  82  ? -15.060 -31.587 -42.113  1.00 106.09 ? 82   LYS   A HG3  1 
ATOM   1210  H  HD2  . LYS   A  1  82  ? -16.765 -33.209 -42.735  1.00 115.34 ? 82   LYS   A HD2  1 
ATOM   1211  H  HD3  . LYS   A  1  82  ? -17.141 -33.238 -41.192  1.00 115.34 ? 82   LYS   A HD3  1 
ATOM   1212  H  HE2  . LYS   A  1  82  ? -18.565 -31.748 -42.174  1.00 122.65 ? 82   LYS   A HE2  1 
ATOM   1213  H  HE3  . LYS   A  1  82  ? -17.530 -30.882 -41.335  1.00 122.65 ? 82   LYS   A HE3  1 
ATOM   1214  H  HZ1  . LYS   A  1  82  ? -17.929 -30.137 -43.530  1.00 126.89 ? 82   LYS   A HZ1  1 
ATOM   1215  H  HZ2  . LYS   A  1  82  ? -16.525 -30.255 -43.194  1.00 126.89 ? 82   LYS   A HZ2  1 
ATOM   1216  H  HZ3  . LYS   A  1  82  ? -17.163 -31.269 -44.009  1.00 126.89 ? 82   LYS   A HZ3  1 
ATOM   1217  N  N    . ASP   A  1  83  ? -12.838 -32.464 -38.884  1.00 78.21  ? 83   ASP   A N    1 
ATOM   1218  C  CA   . ASP   A  1  83  ? -12.787 -32.550 -37.427  1.00 78.78  ? 83   ASP   A CA   1 
ATOM   1219  C  C    . ASP   A  1  83  ? -11.636 -33.426 -36.945  1.00 75.15  ? 83   ASP   A C    1 
ATOM   1220  O  O    . ASP   A  1  83  ? -11.675 -33.950 -35.827  1.00 76.25  ? 83   ASP   A O    1 
ATOM   1221  C  CB   . ASP   A  1  83  ? -14.114 -33.069 -36.860  1.00 87.36  ? 83   ASP   A CB   1 
ATOM   1222  C  CG   . ASP   A  1  83  ? -15.280 -32.164 -37.191  1.00 95.59  ? 83   ASP   A CG   1 
ATOM   1223  O  OD1  . ASP   A  1  83  ? -15.204 -30.957 -36.877  1.00 97.66  ? 83   ASP   A OD1  1 
ATOM   1224  O  OD2  . ASP   A  1  83  ? -16.268 -32.656 -37.776  1.00 99.13  ? 83   ASP   A OD2  1 
ATOM   1225  H  H    . ASP   A  1  83  ? -12.750 -31.662 -39.182  1.00 93.83  ? 83   ASP   A H    1 
ATOM   1226  H  HA   . ASP   A  1  83  ? -12.640 -31.658 -37.075  1.00 94.52  ? 83   ASP   A HA   1 
ATOM   1227  H  HB2  . ASP   A  1  83  ? -14.298 -33.945 -37.235  1.00 104.82 ? 83   ASP   A HB2  1 
ATOM   1228  H  HB3  . ASP   A  1  83  ? -14.044 -33.130 -35.895  1.00 104.82 ? 83   ASP   A HB3  1 
ATOM   1229  N  N    . ASP   A  1  84  ? -10.606 -33.595 -37.774  1.00 70.63  ? 84   ASP   A N    1 
ATOM   1230  C  CA   . ASP   A  1  84  ? -9.432  -34.400 -37.438  1.00 66.08  ? 84   ASP   A CA   1 
ATOM   1231  C  C    . ASP   A  1  84  ? -8.200  -33.587 -37.812  1.00 61.60  ? 84   ASP   A C    1 
ATOM   1232  O  O    . ASP   A  1  84  ? -7.657  -33.733 -38.915  1.00 61.49  ? 84   ASP   A O    1 
ATOM   1233  C  CB   . ASP   A  1  84  ? -9.457  -35.746 -38.159  1.00 67.38  ? 84   ASP   A CB   1 
ATOM   1234  C  CG   . ASP   A  1  84  ? -8.511  -36.758 -37.540  1.00 68.32  ? 84   ASP   A CG   1 
ATOM   1235  O  OD1  . ASP   A  1  84  ? -7.513  -36.341 -36.916  1.00 66.78  ? 84   ASP   A OD1  1 
ATOM   1236  O  OD2  . ASP   A  1  84  ? -8.768  -37.972 -37.679  1.00 71.52  ? 84   ASP   A OD2  1 
ATOM   1237  H  H    . ASP   A  1  84  ? -10.563 -33.244 -38.558  1.00 84.73  ? 84   ASP   A H    1 
ATOM   1238  H  HA   . ASP   A  1  84  ? -9.412  -34.577 -36.484  1.00 79.28  ? 84   ASP   A HA   1 
ATOM   1239  H  HB2  . ASP   A  1  84  ? -10.356 -36.110 -38.118  1.00 80.84  ? 84   ASP   A HB2  1 
ATOM   1240  H  HB3  . ASP   A  1  84  ? -9.195  -35.615 -39.084  1.00 80.84  ? 84   ASP   A HB3  1 
ATOM   1241  N  N    . PRO   A  1  85  ? -7.733  -32.716 -36.920  1.00 58.92  ? 85   PRO   A N    1 
ATOM   1242  C  CA   . PRO   A  1  85  ? -6.621  -31.828 -37.277  1.00 57.18  ? 85   PRO   A CA   1 
ATOM   1243  C  C    . PRO   A  1  85  ? -5.322  -32.587 -37.485  1.00 60.12  ? 85   PRO   A C    1 
ATOM   1244  O  O    . PRO   A  1  85  ? -5.041  -33.590 -36.825  1.00 61.53  ? 85   PRO   A O    1 
ATOM   1245  C  CB   . PRO   A  1  85  ? -6.517  -30.878 -36.076  1.00 55.18  ? 85   PRO   A CB   1 
ATOM   1246  C  CG   . PRO   A  1  85  ? -7.798  -31.038 -35.324  1.00 56.72  ? 85   PRO   A CG   1 
ATOM   1247  C  CD   . PRO   A  1  85  ? -8.236  -32.445 -35.563  1.00 61.36  ? 85   PRO   A CD   1 
ATOM   1248  H  HA   . PRO   A  1  85  ? -6.836  -31.327 -38.080  1.00 68.59  ? 85   PRO   A HA   1 
ATOM   1249  H  HB2  . PRO   A  1  85  ? -5.760  -31.130 -35.524  1.00 66.20  ? 85   PRO   A HB2  1 
ATOM   1250  H  HB3  . PRO   A  1  85  ? -6.412  -29.966 -36.387  1.00 66.20  ? 85   PRO   A HB3  1 
ATOM   1251  H  HG2  . PRO   A  1  85  ? -7.645  -30.882 -34.379  1.00 68.05  ? 85   PRO   A HG2  1 
ATOM   1252  H  HG3  . PRO   A  1  85  ? -8.457  -30.411 -35.661  1.00 68.05  ? 85   PRO   A HG3  1 
ATOM   1253  H  HD2  . PRO   A  1  85  ? -7.835  -33.048 -34.918  1.00 73.61  ? 85   PRO   A HD2  1 
ATOM   1254  H  HD3  . PRO   A  1  85  ? -9.202  -32.519 -35.530  1.00 73.61  ? 85   PRO   A HD3  1 
ATOM   1255  N  N    . LEU   A  1  86  ? -4.522  -32.085 -38.426  1.00 58.29  ? 86   LEU   A N    1 
ATOM   1256  C  CA   . LEU   A  1  86  ? -3.201  -32.648 -38.670  1.00 54.45  ? 86   LEU   A CA   1 
ATOM   1257  C  C    . LEU   A  1  86  ? -2.167  -32.110 -37.691  1.00 54.66  ? 86   LEU   A C    1 
ATOM   1258  O  O    . LEU   A  1  86  ? -1.199  -32.809 -37.372  1.00 54.55  ? 86   LEU   A O    1 
ATOM   1259  C  CB   . LEU   A  1  86  ? -2.762  -32.344 -40.102  1.00 54.27  ? 86   LEU   A CB   1 
ATOM   1260  C  CG   . LEU   A  1  86  ? -1.393  -32.872 -40.533  1.00 53.38  ? 86   LEU   A CG   1 
ATOM   1261  C  CD1  . LEU   A  1  86  ? -1.429  -34.381 -40.703  1.00 54.58  ? 86   LEU   A CD1  1 
ATOM   1262  C  CD2  . LEU   A  1  86  ? -0.949  -32.190 -41.815  1.00 55.65  ? 86   LEU   A CD2  1 
ATOM   1263  H  H    . LEU   A  1  86  ? -4.721  -31.420 -38.934  1.00 69.93  ? 86   LEU   A H    1 
ATOM   1264  H  HA   . LEU   A  1  86  ? -3.246  -33.612 -38.564  1.00 65.32  ? 86   LEU   A HA   1 
ATOM   1265  H  HB2  . LEU   A  1  86  ? -3.417  -32.731 -40.704  1.00 65.10  ? 86   LEU   A HB2  1 
ATOM   1266  H  HB3  . LEU   A  1  86  ? -2.741  -31.380 -40.210  1.00 65.10  ? 86   LEU   A HB3  1 
ATOM   1267  H  HG   . LEU   A  1  86  ? -0.742  -32.672 -39.843  1.00 64.03  ? 86   LEU   A HG   1 
ATOM   1268  H  HD11 . LEU   A  1  86  ? -0.551  -34.688 -40.980  1.00 65.48  ? 86   LEU   A HD11 1 
ATOM   1269  H  HD12 . LEU   A  1  86  ? -1.670  -34.789 -39.857  1.00 65.48  ? 86   LEU   A HD12 1 
ATOM   1270  H  HD13 . LEU   A  1  86  ? -2.087  -34.607 -41.379  1.00 65.48  ? 86   LEU   A HD13 1 
ATOM   1271  H  HD21 . LEU   A  1  86  ? -0.080  -32.535 -42.073  1.00 66.76  ? 86   LEU   A HD21 1 
ATOM   1272  H  HD22 . LEU   A  1  86  ? -1.598  -32.374 -42.512  1.00 66.76  ? 86   LEU   A HD22 1 
ATOM   1273  H  HD23 . LEU   A  1  86  ? -0.893  -31.234 -41.661  1.00 66.76  ? 86   LEU   A HD23 1 
ATOM   1274  N  N    . GLU   A  1  87  ? -2.355  -30.885 -37.205  1.00 55.78  ? 87   GLU   A N    1 
ATOM   1275  C  CA   . GLU   A  1  87  ? -1.386  -30.226 -36.345  1.00 52.32  ? 87   GLU   A CA   1 
ATOM   1276  C  C    . GLU   A  1  87  ? -2.127  -29.417 -35.290  1.00 50.10  ? 87   GLU   A C    1 
ATOM   1277  O  O    . GLU   A  1  87  ? -3.336  -29.190 -35.384  1.00 50.59  ? 87   GLU   A O    1 
ATOM   1278  C  CB   . GLU   A  1  87  ? -0.442  -29.332 -37.161  1.00 53.83  ? 87   GLU   A CB   1 
ATOM   1279  C  CG   . GLU   A  1  87  ? -1.151  -28.354 -38.091  1.00 54.36  ? 87   GLU   A CG   1 
ATOM   1280  C  CD   . GLU   A  1  87  ? -0.225  -27.770 -39.138  1.00 55.15  ? 87   GLU   A CD   1 
ATOM   1281  O  OE1  . GLU   A  1  87  ? 0.935   -28.223 -39.229  1.00 57.24  ? 87   GLU   A OE1  1 
ATOM   1282  O  OE2  . GLU   A  1  87  ? -0.660  -26.862 -39.875  1.00 57.34  ? 87   GLU   A OE2  1 
ATOM   1283  H  H    . GLU   A  1  87  ? -3.053  -30.408 -37.366  1.00 66.92  ? 87   GLU   A H    1 
ATOM   1284  H  HA   . GLU   A  1  87  ? -0.852  -30.892 -35.885  1.00 62.76  ? 87   GLU   A HA   1 
ATOM   1285  H  HB2  . GLU   A  1  87  ? 0.100   -28.813 -36.547  1.00 64.58  ? 87   GLU   A HB2  1 
ATOM   1286  H  HB3  . GLU   A  1  87  ? 0.126   -29.898 -37.707  1.00 64.58  ? 87   GLU   A HB3  1 
ATOM   1287  H  HG2  . GLU   A  1  87  ? -1.869  -28.818 -38.549  1.00 65.21  ? 87   GLU   A HG2  1 
ATOM   1288  H  HG3  . GLU   A  1  87  ? -1.511  -27.622 -37.566  1.00 65.21  ? 87   GLU   A HG3  1 
ATOM   1289  N  N    . PHE   A  1  88  ? -1.385  -28.984 -34.271  1.00 51.76  ? 88   PHE   A N    1 
ATOM   1290  C  CA   . PHE   A  1  88  ? -1.938  -28.223 -33.151  1.00 52.86  ? 88   PHE   A CA   1 
ATOM   1291  C  C    . PHE   A  1  88  ? -1.009  -27.043 -32.876  1.00 54.77  ? 88   PHE   A C    1 
ATOM   1292  O  O    . PHE   A  1  88  ? 0.060   -27.210 -32.280  1.00 53.54  ? 88   PHE   A O    1 
ATOM   1293  C  CB   . PHE   A  1  88  ? -2.101  -29.108 -31.919  1.00 52.45  ? 88   PHE   A CB   1 
ATOM   1294  C  CG   . PHE   A  1  88  ? -2.886  -30.361 -32.180  1.00 51.95  ? 88   PHE   A CG   1 
ATOM   1295  C  CD1  . PHE   A  1  88  ? -2.245  -31.528 -32.563  1.00 52.20  ? 88   PHE   A CD1  1 
ATOM   1296  C  CD2  . PHE   A  1  88  ? -4.266  -30.370 -32.054  1.00 51.59  ? 88   PHE   A CD2  1 
ATOM   1297  C  CE1  . PHE   A  1  88  ? -2.964  -32.680 -32.810  1.00 49.94  ? 88   PHE   A CE1  1 
ATOM   1298  C  CE2  . PHE   A  1  88  ? -4.990  -31.521 -32.299  1.00 51.55  ? 88   PHE   A CE2  1 
ATOM   1299  C  CZ   . PHE   A  1  88  ? -4.338  -32.677 -32.678  1.00 50.73  ? 88   PHE   A CZ   1 
ATOM   1300  H  H    . PHE   A  1  88  ? -0.539  -29.122 -34.205  1.00 62.09  ? 88   PHE   A H    1 
ATOM   1301  H  HA   . PHE   A  1  88  ? -2.808  -27.871 -33.395  1.00 63.41  ? 88   PHE   A HA   1 
ATOM   1302  H  HB2  . PHE   A  1  88  ? -1.222  -29.369 -31.603  1.00 62.92  ? 88   PHE   A HB2  1 
ATOM   1303  H  HB3  . PHE   A  1  88  ? -2.565  -28.605 -31.232  1.00 62.92  ? 88   PHE   A HB3  1 
ATOM   1304  H  HD1  . PHE   A  1  88  ? -1.320  -31.534 -32.656  1.00 62.62  ? 88   PHE   A HD1  1 
ATOM   1305  H  HD2  . PHE   A  1  88  ? -4.709  -29.593 -31.801  1.00 61.89  ? 88   PHE   A HD2  1 
ATOM   1306  H  HE1  . PHE   A  1  88  ? -2.522  -33.458 -33.064  1.00 59.91  ? 88   PHE   A HE1  1 
ATOM   1307  H  HE2  . PHE   A  1  88  ? -5.916  -31.516 -32.209  1.00 61.84  ? 88   PHE   A HE2  1 
ATOM   1308  H  HZ   . PHE   A  1  88  ? -4.823  -33.453 -32.844  1.00 60.86  ? 88   PHE   A HZ   1 
ATOM   1309  N  N    . LYS   A  1  89  ? -1.423  -25.852 -33.309  1.00 56.73  ? 89   LYS   A N    1 
ATOM   1310  C  CA   . LYS   A  1  89  ? -0.597  -24.658 -33.195  1.00 54.40  ? 89   LYS   A CA   1 
ATOM   1311  C  C    . LYS   A  1  89  ? -0.867  -23.854 -31.931  1.00 55.33  ? 89   LYS   A C    1 
ATOM   1312  O  O    . LYS   A  1  89  ? -0.051  -22.995 -31.577  1.00 58.14  ? 89   LYS   A O    1 
ATOM   1313  C  CB   . LYS   A  1  89  ? -0.811  -23.758 -34.416  1.00 51.45  ? 89   LYS   A CB   1 
ATOM   1314  C  CG   . LYS   A  1  89  ? -0.339  -24.376 -35.722  1.00 52.48  ? 89   LYS   A CG   1 
ATOM   1315  C  CD   . LYS   A  1  89  ? -0.678  -23.497 -36.913  1.00 54.45  ? 89   LYS   A CD   1 
ATOM   1316  C  CE   . LYS   A  1  89  ? -0.205  -24.126 -38.212  1.00 56.41  ? 89   LYS   A CE   1 
ATOM   1317  N  NZ   . LYS   A  1  89  ? -0.525  -23.286 -39.400  1.00 60.71  ? 89   LYS   A NZ   1 
ATOM   1318  H  H    . LYS   A  1  89  ? -2.187  -25.711 -33.677  1.00 68.05  ? 89   LYS   A H    1 
ATOM   1319  H  HA   . LYS   A  1  89  ? 0.334   -24.930 -33.174  1.00 65.26  ? 89   LYS   A HA   1 
ATOM   1320  H  HB2  . LYS   A  1  89  ? -1.758  -23.571 -34.503  1.00 61.72  ? 89   LYS   A HB2  1 
ATOM   1321  H  HB3  . LYS   A  1  89  ? -0.319  -22.933 -34.284  1.00 61.72  ? 89   LYS   A HB3  1 
ATOM   1322  H  HG2  . LYS   A  1  89  ? 0.624   -24.490 -35.693  1.00 62.95  ? 89   LYS   A HG2  1 
ATOM   1323  H  HG3  . LYS   A  1  89  ? -0.772  -25.235 -35.845  1.00 62.95  ? 89   LYS   A HG3  1 
ATOM   1324  H  HD2  . LYS   A  1  89  ? -1.640  -23.379 -36.962  1.00 65.32  ? 89   LYS   A HD2  1 
ATOM   1325  H  HD3  . LYS   A  1  89  ? -0.243  -22.636 -36.813  1.00 65.32  ? 89   LYS   A HD3  1 
ATOM   1326  H  HE2  . LYS   A  1  89  ? 0.757   -24.242 -38.176  1.00 67.67  ? 89   LYS   A HE2  1 
ATOM   1327  H  HE3  . LYS   A  1  89  ? -0.639  -24.986 -38.325  1.00 67.67  ? 89   LYS   A HE3  1 
ATOM   1328  H  HZ1  . LYS   A  1  89  ? -0.197  -23.663 -40.136  1.00 72.83  ? 89   LYS   A HZ1  1 
ATOM   1329  H  HZ2  . LYS   A  1  89  ? -1.407  -23.204 -39.486  1.00 72.83  ? 89   LYS   A HZ2  1 
ATOM   1330  H  HZ3  . LYS   A  1  89  ? -0.167  -22.477 -39.306  1.00 72.83  ? 89   LYS   A HZ3  1 
ATOM   1331  N  N    . SER   A  1  90  ? -1.980  -24.104 -31.246  1.00 53.77  ? 90   SER   A N    1 
ATOM   1332  C  CA   . SER   A  1  90  ? -2.282  -23.363 -30.029  1.00 53.69  ? 90   SER   A CA   1 
ATOM   1333  C  C    . SER   A  1  90  ? -1.241  -23.662 -28.959  1.00 53.61  ? 90   SER   A C    1 
ATOM   1334  O  O    . SER   A  1  90  ? -0.905  -24.822 -28.705  1.00 49.61  ? 90   SER   A O    1 
ATOM   1335  C  CB   . SER   A  1  90  ? -3.680  -23.720 -29.524  1.00 50.15  ? 90   SER   A CB   1 
ATOM   1336  O  OG   . SER   A  1  90  ? -4.674  -23.288 -30.436  1.00 54.18  ? 90   SER   A OG   1 
ATOM   1337  H  H    . SER   A  1  90  ? -2.569  -24.692 -31.464  1.00 64.51  ? 90   SER   A H    1 
ATOM   1338  H  HA   . SER   A  1  90  ? -2.266  -22.412 -30.219  1.00 64.41  ? 90   SER   A HA   1 
ATOM   1339  H  HB2  . SER   A  1  90  ? -3.742  -24.683 -29.423  1.00 60.16  ? 90   SER   A HB2  1 
ATOM   1340  H  HB3  . SER   A  1  90  ? -3.826  -23.287 -28.669  1.00 60.16  ? 90   SER   A HB3  1 
ATOM   1341  H  HG   . SER   A  1  90  ? -5.310  -23.836 -30.449  1.00 64.99  ? 90   SER   A HG   1 
ATOM   1342  N  N    . HIS   A  1  91  ? -0.728  -22.604 -28.332  1.00 57.70  ? 91   HIS   A N    1 
ATOM   1343  C  CA   . HIS   A  1  91  ? 0.287   -22.722 -27.288  1.00 58.36  ? 91   HIS   A CA   1 
ATOM   1344  C  C    . HIS   A  1  91  ? 1.547   -23.410 -27.805  1.00 56.40  ? 91   HIS   A C    1 
ATOM   1345  O  O    . HIS   A  1  91  ? 2.279   -24.045 -27.041  1.00 54.42  ? 91   HIS   A O    1 
ATOM   1346  C  CB   . HIS   A  1  91  ? -0.261  -23.467 -26.068  1.00 58.42  ? 91   HIS   A CB   1 
ATOM   1347  C  CG   . HIS   A  1  91  ? -1.550  -22.911 -25.552  1.00 64.05  ? 91   HIS   A CG   1 
ATOM   1348  N  ND1  . HIS   A  1  91  ? -1.617  -21.753 -24.806  1.00 67.06  ? 91   HIS   A ND1  1 
ATOM   1349  C  CD2  . HIS   A  1  91  ? -2.824  -23.353 -25.675  1.00 66.36  ? 91   HIS   A CD2  1 
ATOM   1350  C  CE1  . HIS   A  1  91  ? -2.876  -21.506 -24.493  1.00 67.77  ? 91   HIS   A CE1  1 
ATOM   1351  N  NE2  . HIS   A  1  91  ? -3.629  -22.461 -25.007  1.00 66.31  ? 91   HIS   A NE2  1 
ATOM   1352  H  H    . HIS   A  1  91  ? -0.957  -21.791 -28.498  1.00 69.22  ? 91   HIS   A H    1 
ATOM   1353  H  HA   . HIS   A  1  91  ? 0.539   -21.829 -27.008  1.00 70.01  ? 91   HIS   A HA   1 
ATOM   1354  H  HB2  . HIS   A  1  91  ? -0.414  -24.394 -26.311  1.00 70.09  ? 91   HIS   A HB2  1 
ATOM   1355  H  HB3  . HIS   A  1  91  ? 0.392   -23.415 -25.352  1.00 70.09  ? 91   HIS   A HB3  1 
ATOM   1356  H  HD2  . HIS   A  1  91  ? -3.103  -24.116 -26.126  1.00 79.62  ? 91   HIS   A HD2  1 
ATOM   1357  H  HE1  . HIS   A  1  91  ? -3.181  -20.782 -23.994  1.00 81.30  ? 91   HIS   A HE1  1 
ATOM   1358  H  HE2  . HIS   A  1  91  ? -4.484  -22.517 -24.936  1.00 79.56  ? 91   HIS   A HE2  1 
ATOM   1359  N  N    . GLN   A  1  92  ? 1.811   -23.290 -29.107  1.00 57.00  ? 92   GLN   A N    1 
ATOM   1360  C  CA   . GLN   A  1  92  ? 3.001   -23.895 -29.691  1.00 55.96  ? 92   GLN   A CA   1 
ATOM   1361  C  C    . GLN   A  1  92  ? 4.280   -23.157 -29.321  1.00 57.45  ? 92   GLN   A C    1 
ATOM   1362  O  O    . GLN   A  1  92  ? 5.369   -23.654 -29.627  1.00 55.18  ? 92   GLN   A O    1 
ATOM   1363  C  CB   . GLN   A  1  92  ? 2.871   -23.942 -31.213  1.00 55.14  ? 92   GLN   A CB   1 
ATOM   1364  C  CG   . GLN   A  1  92  ? 2.876   -22.574 -31.868  1.00 54.81  ? 92   GLN   A CG   1 
ATOM   1365  C  CD   . GLN   A  1  92  ? 2.538   -22.634 -33.343  1.00 53.33  ? 92   GLN   A CD   1 
ATOM   1366  O  OE1  . GLN   A  1  92  ? 2.661   -23.681 -33.982  1.00 51.88  ? 92   GLN   A OE1  1 
ATOM   1367  N  NE2  . GLN   A  1  92  ? 2.102   -21.508 -33.893  1.00 55.18  ? 92   GLN   A NE2  1 
ATOM   1368  H  H    . GLN   A  1  92  ? 1.318   -22.865 -29.668  1.00 68.38  ? 92   GLN   A H    1 
ATOM   1369  H  HA   . GLN   A  1  92  ? 3.073   -24.805 -29.364  1.00 67.14  ? 92   GLN   A HA   1 
ATOM   1370  H  HB2  . GLN   A  1  92  ? 3.616   -24.447 -31.574  1.00 66.15  ? 92   GLN   A HB2  1 
ATOM   1371  H  HB3  . GLN   A  1  92  ? 2.034   -24.377 -31.441  1.00 66.15  ? 92   GLN   A HB3  1 
ATOM   1372  H  HG2  . GLN   A  1  92  ? 2.218   -22.011 -31.431  1.00 65.75  ? 92   GLN   A HG2  1 
ATOM   1373  H  HG3  . GLN   A  1  92  ? 3.759   -22.183 -31.777  1.00 65.75  ? 92   GLN   A HG3  1 
ATOM   1374  H  HE21 . GLN   A  1  92  ? 2.026   -20.797 -33.414  1.00 66.20  ? 92   GLN   A HE21 1 
ATOM   1375  H  HE22 . GLN   A  1  92  ? 1.897   -21.488 -34.728  1.00 66.20  ? 92   GLN   A HE22 1 
ATOM   1376  N  N    . TRP   A  1  93  ? 4.176   -21.988 -28.687  1.00 60.09  ? 93   TRP   A N    1 
ATOM   1377  C  CA   . TRP   A  1  93  ? 5.345   -21.221 -28.259  1.00 56.02  ? 93   TRP   A CA   1 
ATOM   1378  C  C    . TRP   A  1  93  ? 6.190   -20.776 -29.452  1.00 52.02  ? 93   TRP   A C    1 
ATOM   1379  O  O    . TRP   A  1  93  ? 7.422   -20.780 -29.397  1.00 52.52  ? 93   TRP   A O    1 
ATOM   1380  C  CB   . TRP   A  1  93  ? 6.194   -22.022 -27.269  1.00 55.30  ? 93   TRP   A CB   1 
ATOM   1381  C  CG   . TRP   A  1  93  ? 5.724   -21.936 -25.853  1.00 56.64  ? 93   TRP   A CG   1 
ATOM   1382  C  CD1  . TRP   A  1  93  ? 4.575   -22.458 -25.333  1.00 56.08  ? 93   TRP   A CD1  1 
ATOM   1383  C  CD2  . TRP   A  1  93  ? 6.404   -21.298 -24.767  1.00 54.79  ? 93   TRP   A CD2  1 
ATOM   1384  N  NE1  . TRP   A  1  93  ? 4.497   -22.180 -23.989  1.00 58.40  ? 93   TRP   A NE1  1 
ATOM   1385  C  CE2  . TRP   A  1  93  ? 5.607   -21.468 -23.618  1.00 55.92  ? 93   TRP   A CE2  1 
ATOM   1386  C  CE3  . TRP   A  1  93  ? 7.609   -20.598 -24.655  1.00 49.97  ? 93   TRP   A CE3  1 
ATOM   1387  C  CZ2  . TRP   A  1  93  ? 5.976   -20.962 -22.373  1.00 53.26  ? 93   TRP   A CZ2  1 
ATOM   1388  C  CZ3  . TRP   A  1  93  ? 7.973   -20.096 -23.419  1.00 48.95  ? 93   TRP   A CZ3  1 
ATOM   1389  C  CH2  . TRP   A  1  93  ? 7.160   -20.280 -22.295  1.00 50.20  ? 93   TRP   A CH2  1 
ATOM   1390  H  H    . TRP   A  1  93  ? 3.428   -21.613 -28.491  1.00 72.09  ? 93   TRP   A H    1 
ATOM   1391  H  HA   . TRP   A  1  93  ? 5.032   -20.419 -27.813  1.00 67.20  ? 93   TRP   A HA   1 
ATOM   1392  H  HB2  . TRP   A  1  93  ? 6.175   -22.957 -27.529  1.00 66.34  ? 93   TRP   A HB2  1 
ATOM   1393  H  HB3  . TRP   A  1  93  ? 7.104   -21.688 -27.298  1.00 66.34  ? 93   TRP   A HB3  1 
ATOM   1394  H  HD1  . TRP   A  1  93  ? 3.939   -22.933 -25.817  1.00 67.27  ? 93   TRP   A HD1  1 
ATOM   1395  H  HE1  . TRP   A  1  93  ? 3.855   -22.414 -23.467  1.00 70.06  ? 93   TRP   A HE1  1 
ATOM   1396  H  HE3  . TRP   A  1  93  ? 8.154   -20.472 -25.398  1.00 59.95  ? 93   TRP   A HE3  1 
ATOM   1397  H  HZ2  . TRP   A  1  93  ? 5.439   -21.083 -21.624  1.00 63.89  ? 93   TRP   A HZ2  1 
ATOM   1398  H  HZ3  . TRP   A  1  93  ? 8.772   -19.628 -23.333  1.00 58.72  ? 93   TRP   A HZ3  1 
ATOM   1399  H  HH2  . TRP   A  1  93  ? 7.430   -19.931 -21.476  1.00 60.22  ? 93   TRP   A HH2  1 
ATOM   1400  N  N    . PHE   A  1  94  ? 5.532   -20.381 -30.540  1.00 52.85  ? 94   PHE   A N    1 
ATOM   1401  C  CA   . PHE   A  1  94  ? 6.272   -19.860 -31.681  1.00 57.51  ? 94   PHE   A CA   1 
ATOM   1402  C  C    . PHE   A  1  94  ? 6.989   -18.577 -31.286  1.00 58.37  ? 94   PHE   A C    1 
ATOM   1403  O  O    . PHE   A  1  94  ? 6.387   -17.666 -30.710  1.00 60.01  ? 94   PHE   A O    1 
ATOM   1404  C  CB   . PHE   A  1  94  ? 5.355   -19.594 -32.872  1.00 58.42  ? 94   PHE   A CB   1 
ATOM   1405  C  CG   . PHE   A  1  94  ? 6.080   -19.031 -34.063  1.00 56.36  ? 94   PHE   A CG   1 
ATOM   1406  C  CD1  . PHE   A  1  94  ? 6.919   -19.833 -34.817  1.00 54.64  ? 94   PHE   A CD1  1 
ATOM   1407  C  CD2  . PHE   A  1  94  ? 5.940   -17.698 -34.415  1.00 57.24  ? 94   PHE   A CD2  1 
ATOM   1408  C  CE1  . PHE   A  1  94  ? 7.597   -19.320 -35.906  1.00 54.82  ? 94   PHE   A CE1  1 
ATOM   1409  C  CE2  . PHE   A  1  94  ? 6.614   -17.180 -35.504  1.00 56.86  ? 94   PHE   A CE2  1 
ATOM   1410  C  CZ   . PHE   A  1  94  ? 7.443   -17.991 -36.249  1.00 55.40  ? 94   PHE   A CZ   1 
ATOM   1411  H  H    . PHE   A  1  94  ? 4.678   -20.403 -30.638  1.00 63.39  ? 94   PHE   A H    1 
ATOM   1412  H  HA   . PHE   A  1  94  ? 6.921   -20.526 -31.959  1.00 68.99  ? 94   PHE   A HA   1 
ATOM   1413  H  HB2  . PHE   A  1  94  ? 4.940   -20.428 -33.142  1.00 70.08  ? 94   PHE   A HB2  1 
ATOM   1414  H  HB3  . PHE   A  1  94  ? 4.674   -18.955 -32.607  1.00 70.08  ? 94   PHE   A HB3  1 
ATOM   1415  H  HD1  . PHE   A  1  94  ? 7.028   -20.728 -34.588  1.00 65.55  ? 94   PHE   A HD1  1 
ATOM   1416  H  HD2  . PHE   A  1  94  ? 5.385   -17.146 -33.913  1.00 68.67  ? 94   PHE   A HD2  1 
ATOM   1417  H  HE1  . PHE   A  1  94  ? 8.156   -19.869 -36.407  1.00 65.77  ? 94   PHE   A HE1  1 
ATOM   1418  H  HE2  . PHE   A  1  94  ? 6.509   -16.285 -35.733  1.00 68.21  ? 94   PHE   A HE2  1 
ATOM   1419  H  HZ   . PHE   A  1  94  ? 7.897   -17.643 -36.983  1.00 66.47  ? 94   PHE   A HZ   1 
ATOM   1420  N  N    . GLY   A  1  95  ? 8.274   -18.503 -31.612  1.00 55.63  ? 95   GLY   A N    1 
ATOM   1421  C  CA   . GLY   A  1  95  ? 9.109   -17.400 -31.196  1.00 54.96  ? 95   GLY   A CA   1 
ATOM   1422  C  C    . GLY   A  1  95  ? 9.907   -17.655 -29.938  1.00 58.45  ? 95   GLY   A C    1 
ATOM   1423  O  O    . GLY   A  1  95  ? 10.617  -16.750 -29.483  1.00 63.00  ? 95   GLY   A O    1 
ATOM   1424  H  H    . GLY   A  1  95  ? 8.687   -19.093 -32.081  1.00 66.74  ? 95   GLY   A H    1 
ATOM   1425  H  HA2  . GLY   A  1  95  ? 9.735   -17.197 -31.908  1.00 65.93  ? 95   GLY   A HA2  1 
ATOM   1426  H  HA3  . GLY   A  1  95  ? 8.547   -16.625 -31.039  1.00 65.93  ? 95   GLY   A HA3  1 
ATOM   1427  N  N    . ALA   A  1  96  ? 9.812   -18.854 -29.357  1.00 59.06  ? 96   ALA   A N    1 
ATOM   1428  C  CA   . ALA   A  1  96  ? 10.654  -19.193 -28.218  1.00 57.97  ? 96   ALA   A CA   1 
ATOM   1429  C  C    . ALA   A  1  96  ? 12.131  -19.141 -28.576  1.00 60.55  ? 96   ALA   A C    1 
ATOM   1430  O  O    . ALA   A  1  96  ? 12.974  -19.010 -27.682  1.00 61.64  ? 96   ALA   A O    1 
ATOM   1431  C  CB   . ALA   A  1  96  ? 10.296  -20.583 -27.689  1.00 51.39  ? 96   ALA   A CB   1 
ATOM   1432  H  H    . ALA   A  1  96  ? 9.274   -19.478 -29.603  1.00 70.86  ? 96   ALA   A H    1 
ATOM   1433  H  HA   . ALA   A  1  96  ? 10.490  -18.555 -27.505  1.00 69.54  ? 96   ALA   A HA   1 
ATOM   1434  H  HB1  . ALA   A  1  96  ? 10.861  -20.787 -26.928  1.00 61.65  ? 96   ALA   A HB1  1 
ATOM   1435  H  HB2  . ALA   A  1  96  ? 9.364   -20.588 -27.420  1.00 61.65  ? 96   ALA   A HB2  1 
ATOM   1436  H  HB3  . ALA   A  1  96  ? 10.440  -21.235 -28.393  1.00 61.65  ? 96   ALA   A HB3  1 
ATOM   1437  N  N    . SER   A  1  97  ? 12.460  -19.243 -29.861  1.00 61.30  ? 97   SER   A N    1 
ATOM   1438  C  CA   . SER   A  1  97  ? 13.830  -19.123 -30.335  1.00 60.14  ? 97   SER   A CA   1 
ATOM   1439  C  C    . SER   A  1  97  ? 13.804  -18.391 -31.665  1.00 56.99  ? 97   SER   A C    1 
ATOM   1440  O  O    . SER   A  1  97  ? 13.005  -18.727 -32.545  1.00 55.79  ? 97   SER   A O    1 
ATOM   1441  C  CB   . SER   A  1  97  ? 14.491  -20.496 -30.489  1.00 60.41  ? 97   SER   A CB   1 
ATOM   1442  O  OG   . SER   A  1  97  ? 13.758  -21.312 -31.383  1.00 64.83  ? 97   SER   A OG   1 
ATOM   1443  H  H    . SER   A  1  97  ? 11.892  -19.384 -30.490  1.00 73.54  ? 97   SER   A H    1 
ATOM   1444  H  HA   . SER   A  1  97  ? 14.361  -18.611 -29.704  1.00 72.15  ? 97   SER   A HA   1 
ATOM   1445  H  HB2  . SER   A  1  97  ? 15.389  -20.377 -30.836  1.00 72.47  ? 97   SER   A HB2  1 
ATOM   1446  H  HB3  . SER   A  1  97  ? 14.525  -20.929 -29.622  1.00 72.47  ? 97   SER   A HB3  1 
ATOM   1447  H  HG   . SER   A  1  97  ? 14.098  -22.080 -31.416  1.00 77.77  ? 97   SER   A HG   1 
ATOM   1448  N  N    . VAL   A  1  98  ? 14.668  -17.391 -31.805  1.00 56.28  ? 98   VAL   A N    1 
ATOM   1449  C  CA   . VAL   A  1  98  ? 14.730  -16.568 -33.006  1.00 58.34  ? 98   VAL   A CA   1 
ATOM   1450  C  C    . VAL   A  1  98  ? 16.192  -16.295 -33.314  1.00 58.28  ? 98   VAL   A C    1 
ATOM   1451  O  O    . VAL   A  1  98  ? 16.963  -15.930 -32.421  1.00 57.42  ? 98   VAL   A O    1 
ATOM   1452  C  CB   . VAL   A  1  98  ? 13.955  -15.246 -32.842  1.00 59.87  ? 98   VAL   A CB   1 
ATOM   1453  C  CG1  . VAL   A  1  98  ? 14.120  -14.371 -34.078  1.00 60.16  ? 98   VAL   A CG1  1 
ATOM   1454  C  CG2  . VAL   A  1  98  ? 12.485  -15.528 -32.579  1.00 63.17  ? 98   VAL   A CG2  1 
ATOM   1455  H  H    . VAL   A  1  98  ? 15.241  -17.166 -31.205  1.00 67.52  ? 98   VAL   A H    1 
ATOM   1456  H  HA   . VAL   A  1  98  ? 14.342  -17.054 -33.751  1.00 69.99  ? 98   VAL   A HA   1 
ATOM   1457  H  HB   . VAL   A  1  98  ? 14.315  -14.763 -32.082  1.00 71.82  ? 98   VAL   A HB   1 
ATOM   1458  H  HG11 . VAL   A  1  98  ? 13.473  -13.649 -34.043  1.00 72.17  ? 98   VAL   A HG11 1 
ATOM   1459  H  HG12 . VAL   A  1  98  ? 15.019  -14.008 -34.091  1.00 72.17  ? 98   VAL   A HG12 1 
ATOM   1460  H  HG13 . VAL   A  1  98  ? 13.969  -14.911 -34.870  1.00 72.17  ? 98   VAL   A HG13 1 
ATOM   1461  H  HG21 . VAL   A  1  98  ? 11.999  -14.689 -32.577  1.00 75.78  ? 98   VAL   A HG21 1 
ATOM   1462  H  HG22 . VAL   A  1  98  ? 12.145  -16.107 -33.278  1.00 75.78  ? 98   VAL   A HG22 1 
ATOM   1463  H  HG23 . VAL   A  1  98  ? 12.397  -15.963 -31.717  1.00 75.78  ? 98   VAL   A HG23 1 
ATOM   1464  N  N    . ARG   A  1  99  ? 16.572  -16.469 -34.575  1.00 59.52  ? 99   ARG   A N    1 
ATOM   1465  C  CA   A ARG   A  1  99  ? 17.940  -16.257 -35.022  0.53 62.97  ? 99   ARG   A CA   1 
ATOM   1466  C  CA   B ARG   A  1  99  ? 17.936  -16.221 -35.007  0.47 63.02  ? 99   ARG   A CA   1 
ATOM   1467  C  C    . ARG   A  1  99  ? 17.912  -15.611 -36.397  1.00 64.97  ? 99   ARG   A C    1 
ATOM   1468  O  O    . ARG   A  1  99  ? 17.083  -15.971 -37.237  1.00 66.71  ? 99   ARG   A O    1 
ATOM   1469  C  CB   A ARG   A  1  99  ? 18.719  -17.575 -35.070  0.53 60.79  ? 99   ARG   A CB   1 
ATOM   1470  C  CB   B ARG   A  1  99  ? 18.779  -17.501 -34.997  0.47 60.85  ? 99   ARG   A CB   1 
ATOM   1471  C  CG   A ARG   A  1  99  ? 19.339  -17.964 -33.742  0.53 63.35  ? 99   ARG   A CG   1 
ATOM   1472  C  CG   B ARG   A  1  99  ? 19.289  -17.885 -33.613  0.47 63.25  ? 99   ARG   A CG   1 
ATOM   1473  C  CD   A ARG   A  1  99  ? 20.599  -17.165 -33.464  0.53 60.95  ? 99   ARG   A CD   1 
ATOM   1474  C  CD   B ARG   A  1  99  ? 20.293  -16.875 -33.040  0.47 61.09  ? 99   ARG   A CD   1 
ATOM   1475  N  NE   A ARG   A  1  99  ? 21.222  -17.563 -32.205  0.53 62.15  ? 99   ARG   A NE   1 
ATOM   1476  N  NE   B ARG   A  1  99  ? 21.633  -17.020 -33.612  0.47 63.04  ? 99   ARG   A NE   1 
ATOM   1477  C  CZ   A ARG   A  1  99  ? 20.771  -17.215 -31.004  0.53 61.05  ? 99   ARG   A CZ   1 
ATOM   1478  C  CZ   B ARG   A  1  99  ? 22.287  -16.080 -34.296  0.47 60.99  ? 99   ARG   A CZ   1 
ATOM   1479  N  NH1  A ARG   A  1  99  ? 19.684  -16.463 -30.890  0.53 61.82  ? 99   ARG   A NH1  1 
ATOM   1480  N  NH1  B ARG   A  1  99  ? 23.502  -16.341 -34.758  0.47 58.37  ? 99   ARG   A NH1  1 
ATOM   1481  N  NH2  A ARG   A  1  99  ? 21.404  -17.625 -29.915  0.53 59.79  ? 99   ARG   A NH2  1 
ATOM   1482  N  NH2  B ARG   A  1  99  ? 21.752  -14.884 -34.516  0.47 59.00  ? 99   ARG   A NH2  1 
ATOM   1483  H  H    A ARG   A  1  99  ? 16.040  -16.717 -35.205  0.53 71.40  ? 99   ARG   A H    1 
ATOM   1484  H  H    B ARG   A  1  99  ? 16.049  -16.734 -35.204  0.47 71.40  ? 99   ARG   A H    1 
ATOM   1485  H  HA   A ARG   A  1  99  ? 18.401  -15.659 -34.414  0.53 75.55  ? 99   ARG   A HA   1 
ATOM   1486  H  HA   B ARG   A  1  99  ? 18.360  -15.588 -34.406  0.47 75.61  ? 99   ARG   A HA   1 
ATOM   1487  H  HB2  A ARG   A  1  99  ? 18.115  -18.286 -35.334  0.53 72.93  ? 99   ARG   A HB2  1 
ATOM   1488  H  HB2  B ARG   A  1  99  ? 18.238  -18.234 -35.328  0.47 73.01  ? 99   ARG   A HB2  1 
ATOM   1489  H  HB3  A ARG   A  1  99  ? 19.436  -17.491 -35.718  0.53 72.93  ? 99   ARG   A HB3  1 
ATOM   1490  H  HB3  B ARG   A  1  99  ? 19.550  -17.372 -35.572  0.47 73.01  ? 99   ARG   A HB3  1 
ATOM   1491  H  HG2  A ARG   A  1  99  ? 18.705  -17.792 -33.029  0.53 76.01  ? 99   ARG   A HG2  1 
ATOM   1492  H  HG2  B ARG   A  1  99  ? 18.537  -17.936 -33.003  0.47 75.88  ? 99   ARG   A HG2  1 
ATOM   1493  H  HG3  A ARG   A  1  99  ? 19.571  -18.906 -33.759  0.53 76.01  ? 99   ARG   A HG3  1 
ATOM   1494  H  HG3  B ARG   A  1  99  ? 19.731  -18.746 -33.668  0.47 75.88  ? 99   ARG   A HG3  1 
ATOM   1495  H  HD2  A ARG   A  1  99  ? 21.237  -17.314 -34.180  0.53 73.12  ? 99   ARG   A HD2  1 
ATOM   1496  H  HD2  B ARG   A  1  99  ? 19.981  -15.977 -33.232  0.47 73.29  ? 99   ARG   A HD2  1 
ATOM   1497  H  HD3  A ARG   A  1  99  ? 20.376  -16.223 -33.409  0.53 73.12  ? 99   ARG   A HD3  1 
ATOM   1498  H  HD3  B ARG   A  1  99  ? 20.360  -17.006 -32.082  0.47 73.29  ? 99   ARG   A HD3  1 
ATOM   1499  H  HE   A ARG   A  1  99  ? 21.927  -18.055 -32.243  0.53 74.56  ? 99   ARG   A HE   1 
ATOM   1500  H  HE   B ARG   A  1  99  ? 22.031  -17.773 -33.497  0.47 75.63  ? 99   ARG   A HE   1 
ATOM   1501  H  HH11 A ARG   A  1  99  ? 19.268  -16.198 -31.595  0.53 74.16  ? 99   ARG   A HH11 1 
ATOM   1502  H  HH11 B ARG   A  1  99  ? 23.861  -17.109 -34.615  0.47 70.02  ? 99   ARG   A HH11 1 
ATOM   1503  H  HH12 A ARG   A  1  99  ? 19.395  -16.240 -30.111  0.53 74.16  ? 99   ARG   A HH12 1 
ATOM   1504  H  HH12 B ARG   A  1  99  ? 23.932  -15.741 -35.200  0.47 70.02  ? 99   ARG   A HH12 1 
ATOM   1505  H  HH21 A ARG   A  1  99  ? 22.107  -18.116 -29.985  0.53 71.72  ? 99   ARG   A HH21 1 
ATOM   1506  H  HH21 B ARG   A  1  99  ? 20.967  -14.702 -34.215  0.47 70.77  ? 99   ARG   A HH21 1 
ATOM   1507  H  HH22 A ARG   A  1  99  ? 21.113  -17.400 -29.138  0.53 71.72  ? 99   ARG   A HH22 1 
ATOM   1508  H  HH22 B ARG   A  1  99  ? 22.191  -14.292 -34.960  0.47 70.77  ? 99   ARG   A HH22 1 
ATOM   1509  N  N    . SER   A  1  100 ? 18.826  -14.673 -36.622  1.00 67.09  ? 100  SER   A N    1 
ATOM   1510  C  CA   . SER   A  1  100 ? 18.834  -13.875 -37.839  1.00 67.92  ? 100  SER   A CA   1 
ATOM   1511  C  C    . SER   A  1  100 ? 20.244  -13.832 -38.403  1.00 69.51  ? 100  SER   A C    1 
ATOM   1512  O  O    . SER   A  1  100 ? 21.159  -13.294 -37.771  1.00 75.24  ? 100  SER   A O    1 
ATOM   1513  C  CB   . SER   A  1  100 ? 18.315  -12.466 -37.560  1.00 68.09  ? 100  SER   A CB   1 
ATOM   1514  O  OG   . SER   A  1  100 ? 18.164  -11.727 -38.757  1.00 75.45  ? 100  SER   A OG   1 
ATOM   1515  H  H    . SER   A  1  100 ? 19.460  -14.478 -36.075  1.00 80.49  ? 100  SER   A H    1 
ATOM   1516  H  HA   . SER   A  1  100 ? 18.267  -14.299 -38.502  1.00 81.48  ? 100  SER   A HA   1 
ATOM   1517  H  HB2  . SER   A  1  100 ? 17.453  -12.530 -37.120  1.00 81.69  ? 100  SER   A HB2  1 
ATOM   1518  H  HB3  . SER   A  1  100 ? 18.947  -12.006 -36.986  1.00 81.69  ? 100  SER   A HB3  1 
ATOM   1519  H  HG   . SER   A  1  100 ? 18.917  -11.565 -39.091  1.00 90.53  ? 100  SER   A HG   1 
ATOM   1520  N  N    . LYS   A  1  101 ? 20.413  -14.428 -39.572  1.00 67.33  ? 101  LYS   A N    1 
ATOM   1521  C  CA   . LYS   A  1  101 ? 21.553  -14.187 -40.437  1.00 69.38  ? 101  LYS   A CA   1 
ATOM   1522  C  C    . LYS   A  1  101 ? 21.031  -13.415 -41.643  1.00 69.91  ? 101  LYS   A C    1 
ATOM   1523  O  O    . LYS   A  1  101 ? 19.837  -13.442 -41.950  1.00 75.37  ? 101  LYS   A O    1 
ATOM   1524  C  CB   . LYS   A  1  101 ? 22.232  -15.505 -40.822  1.00 72.22  ? 101  LYS   A CB   1 
ATOM   1525  C  CG   . LYS   A  1  101 ? 23.579  -15.384 -41.524  1.00 75.41  ? 101  LYS   A CG   1 
ATOM   1526  C  CD   . LYS   A  1  101 ? 24.064  -16.759 -41.973  1.00 78.76  ? 101  LYS   A CD   1 
ATOM   1527  C  CE   . LYS   A  1  101 ? 25.418  -16.707 -42.670  1.00 83.88  ? 101  LYS   A CE   1 
ATOM   1528  N  NZ   . LYS   A  1  101 ? 26.401  -15.853 -41.953  1.00 90.05  ? 101  LYS   A NZ   1 
ATOM   1529  H  H    . LYS   A  1  101 ? 19.858  -14.999 -39.898  1.00 80.78  ? 101  LYS   A H    1 
ATOM   1530  H  HA   . LYS   A  1  101 ? 22.246  -13.661 -40.008  1.00 83.23  ? 101  LYS   A HA   1 
ATOM   1531  H  HB2  . LYS   A  1  101 ? 22.377  -16.019 -40.012  1.00 86.64  ? 101  LYS   A HB2  1 
ATOM   1532  H  HB3  . LYS   A  1  101 ? 21.640  -15.987 -41.420  1.00 86.64  ? 101  LYS   A HB3  1 
ATOM   1533  H  HG2  . LYS   A  1  101 ? 23.490  -14.815 -42.305  1.00 90.47  ? 101  LYS   A HG2  1 
ATOM   1534  H  HG3  . LYS   A  1  101 ? 24.233  -15.009 -40.913  1.00 90.47  ? 101  LYS   A HG3  1 
ATOM   1535  H  HD2  . LYS   A  1  101 ? 24.149  -17.334 -41.197  1.00 94.50  ? 101  LYS   A HD2  1 
ATOM   1536  H  HD3  . LYS   A  1  101 ? 23.421  -17.133 -42.595  1.00 94.50  ? 101  LYS   A HD3  1 
ATOM   1537  H  HE2  . LYS   A  1  101 ? 25.781  -17.604 -42.722  1.00 100.64 ? 101  LYS   A HE2  1 
ATOM   1538  H  HE3  . LYS   A  1  101 ? 25.301  -16.344 -43.562  1.00 100.64 ? 101  LYS   A HE3  1 
ATOM   1539  H  HZ1  . LYS   A  1  101 ? 27.226  -16.041 -42.229  1.00 108.05 ? 101  LYS   A HZ1  1 
ATOM   1540  H  HZ2  . LYS   A  1  101 ? 26.232  -14.994 -42.112  1.00 108.05 ? 101  LYS   A HZ2  1 
ATOM   1541  H  HZ3  . LYS   A  1  101 ? 26.350  -16.000 -41.077  1.00 108.05 ? 101  LYS   A HZ3  1 
ATOM   1542  N  N    . GLN   A  1  102 ? 21.948  -12.796 -42.376  1.00 70.97  ? 102  GLN   A N    1 
ATOM   1543  C  CA   . GLN   A  1  102 ? 21.729  -11.482 -42.973  1.00 72.11  ? 102  GLN   A CA   1 
ATOM   1544  C  C    . GLN   A  1  102 ? 20.300  -11.153 -43.406  1.00 74.50  ? 102  GLN   A C    1 
ATOM   1545  O  O    . GLN   A  1  102 ? 19.664  -10.294 -42.787  1.00 77.57  ? 102  GLN   A O    1 
ATOM   1546  C  CB   . GLN   A  1  102 ? 22.653  -11.380 -44.192  1.00 79.65  ? 102  GLN   A CB   1 
ATOM   1547  C  CG   . GLN   A  1  102 ? 24.126  -11.657 -43.879  1.00 91.68  ? 102  GLN   A CG   1 
ATOM   1548  C  CD   . GLN   A  1  102 ? 24.795  -12.539 -44.917  1.00 102.33 ? 102  GLN   A CD   1 
ATOM   1549  O  OE1  . GLN   A  1  102 ? 24.221  -13.527 -45.381  1.00 100.14 ? 102  GLN   A OE1  1 
ATOM   1550  N  NE2  . GLN   A  1  102 ? 26.018  -12.187 -45.281  1.00 111.47 ? 102  GLN   A NE2  1 
ATOM   1551  H  H    . GLN   A  1  102 ? 22.725  -13.122 -42.547  1.00 85.15  ? 102  GLN   A H    1 
ATOM   1552  H  HA   . GLN   A  1  102 ? 21.919  -10.827 -42.284  1.00 86.52  ? 102  GLN   A HA   1 
ATOM   1553  H  HB2  . GLN   A  1  102 ? 22.366  -12.025 -44.856  1.00 95.56  ? 102  GLN   A HB2  1 
ATOM   1554  H  HB3  . GLN   A  1  102 ? 22.593  -10.482 -44.554  1.00 95.56  ? 102  GLN   A HB3  1 
ATOM   1555  H  HG2  . GLN   A  1  102 ? 24.606  -10.815 -43.848  1.00 110.00 ? 102  GLN   A HG2  1 
ATOM   1556  H  HG3  . GLN   A  1  102 ? 24.186  -12.106 -43.021  1.00 110.00 ? 102  GLN   A HG3  1 
ATOM   1557  H  HE21 . GLN   A  1  102 ? 26.388  -11.493 -44.933  1.00 133.75 ? 102  GLN   A HE21 1 
ATOM   1558  H  HE22 . GLN   A  1  102 ? 26.443  -12.653 -45.866  1.00 133.75 ? 102  GLN   A HE22 1 
ATOM   1559  N  N    . ASP   A  1  103 ? 19.753  -11.829 -44.414  1.00 75.91  ? 103  ASP   A N    1 
ATOM   1560  C  CA   . ASP   A  1  103 ? 18.339  -11.644 -44.734  1.00 76.89  ? 103  ASP   A CA   1 
ATOM   1561  C  C    . ASP   A  1  103 ? 17.471  -12.669 -44.029  1.00 73.25  ? 103  ASP   A C    1 
ATOM   1562  O  O    . ASP   A  1  103 ? 16.318  -12.381 -43.685  1.00 76.25  ? 103  ASP   A O    1 
ATOM   1563  C  CB   . ASP   A  1  103 ? 18.090  -11.759 -46.242  1.00 82.97  ? 103  ASP   A CB   1 
ATOM   1564  C  CG   . ASP   A  1  103 ? 18.486  -10.510 -47.003  1.00 95.56  ? 103  ASP   A CG   1 
ATOM   1565  O  OD1  . ASP   A  1  103 ? 18.191  -9.393  -46.526  1.00 100.21 ? 103  ASP   A OD1  1 
ATOM   1566  O  OD2  . ASP   A  1  103 ? 19.083  -10.650 -48.090  1.00 101.39 ? 103  ASP   A OD2  1 
ATOM   1567  H  H    . ASP   A  1  103 ? 20.170  -12.388 -44.916  1.00 91.07  ? 103  ASP   A H    1 
ATOM   1568  H  HA   . ASP   A  1  103 ? 18.078  -10.750 -44.463  1.00 92.25  ? 103  ASP   A HA   1 
ATOM   1569  H  HB2  . ASP   A  1  103 ? 18.610  -12.499 -46.591  1.00 99.55  ? 103  ASP   A HB2  1 
ATOM   1570  H  HB3  . ASP   A  1  103 ? 17.145  -11.916 -46.394  1.00 99.55  ? 103  ASP   A HB3  1 
ATOM   1571  N  N    . LYS   A  1  104 ? 18.024  -13.854 -43.809  1.00 65.70  ? 104  LYS   A N    1 
ATOM   1572  C  CA   . LYS   A  1  104 ? 17.272  -14.971 -43.266  1.00 64.01  ? 104  LYS   A CA   1 
ATOM   1573  C  C    . LYS   A  1  104 ? 16.866  -14.708 -41.822  1.00 59.07  ? 104  LYS   A C    1 
ATOM   1574  O  O    . LYS   A  1  104 ? 17.613  -14.112 -41.043  1.00 54.93  ? 104  LYS   A O    1 
ATOM   1575  C  CB   . LYS   A  1  104 ? 18.124  -16.236 -43.366  1.00 68.26  ? 104  LYS   A CB   1 
ATOM   1576  C  CG   . LYS   A  1  104 ? 18.567  -16.555 -44.794  1.00 73.90  ? 104  LYS   A CG   1 
ATOM   1577  C  CD   . LYS   A  1  104 ? 19.747  -17.511 -44.814  1.00 74.90  ? 104  LYS   A CD   1 
ATOM   1578  C  CE   . LYS   A  1  104 ? 21.073  -16.773 -44.699  1.00 76.11  ? 104  LYS   A CE   1 
ATOM   1579  N  NZ   . LYS   A  1  104 ? 21.546  -16.253 -46.017  1.00 77.49  ? 104  LYS   A NZ   1 
ATOM   1580  H  H    . LYS   A  1  104 ? 18.848  -14.040 -43.968  1.00 78.82  ? 104  LYS   A H    1 
ATOM   1581  H  HA   . LYS   A  1  104 ? 16.455  -15.101 -43.772  1.00 76.79  ? 104  LYS   A HA   1 
ATOM   1582  H  HB2  . LYS   A  1  104 ? 18.921  -16.121 -42.825  1.00 81.89  ? 104  LYS   A HB2  1 
ATOM   1583  H  HB3  . LYS   A  1  104 ? 17.607  -16.989 -43.039  1.00 81.89  ? 104  LYS   A HB3  1 
ATOM   1584  H  HG2  . LYS   A  1  104 ? 17.832  -16.969 -45.273  1.00 88.66  ? 104  LYS   A HG2  1 
ATOM   1585  H  HG3  . LYS   A  1  104 ? 18.832  -15.735 -45.238  1.00 88.66  ? 104  LYS   A HG3  1 
ATOM   1586  H  HD2  . LYS   A  1  104 ? 19.675  -18.125 -44.067  1.00 89.86  ? 104  LYS   A HD2  1 
ATOM   1587  H  HD3  . LYS   A  1  104 ? 19.745  -18.004 -45.650  1.00 89.86  ? 104  LYS   A HD3  1 
ATOM   1588  H  HE2  . LYS   A  1  104 ? 20.967  -16.019 -44.097  1.00 91.31  ? 104  LYS   A HE2  1 
ATOM   1589  H  HE3  . LYS   A  1  104 ? 21.747  -17.380 -44.354  1.00 91.31  ? 104  LYS   A HE3  1 
ATOM   1590  H  HZ1  . LYS   A  1  104 ? 22.340  -15.863 -45.923  1.00 92.97  ? 104  LYS   A HZ1  1 
ATOM   1591  H  HZ2  . LYS   A  1  104 ? 21.619  -16.922 -46.599  1.00 92.97  ? 104  LYS   A HZ2  1 
ATOM   1592  H  HZ3  . LYS   A  1  104 ? 20.967  -15.656 -46.334  1.00 92.97  ? 104  LYS   A HZ3  1 
ATOM   1593  N  N    . ILE   A  1  105 ? 15.661  -15.151 -41.473  1.00 61.04  ? 105  ILE   A N    1 
ATOM   1594  C  CA   . ILE   A  1  105 ? 15.162  -15.113 -40.104  1.00 61.29  ? 105  ILE   A CA   1 
ATOM   1595  C  C    . ILE   A  1  105 ? 14.599  -16.489 -39.783  1.00 62.45  ? 105  ILE   A C    1 
ATOM   1596  O  O    . ILE   A  1  105 ? 13.755  -17.005 -40.524  1.00 64.53  ? 105  ILE   A O    1 
ATOM   1597  C  CB   . ILE   A  1  105 ? 14.080  -14.033 -39.903  1.00 63.80  ? 105  ILE   A CB   1 
ATOM   1598  C  CG1  . ILE   A  1  105 ? 14.613  -12.652 -40.294  1.00 68.99  ? 105  ILE   A CG1  1 
ATOM   1599  C  CG2  . ILE   A  1  105 ? 13.596  -14.042 -38.449  1.00 60.08  ? 105  ILE   A CG2  1 
ATOM   1600  C  CD1  . ILE   A  1  105 ? 13.602  -11.531 -40.112  1.00 71.18  ? 105  ILE   A CD1  1 
ATOM   1601  H  H    . ILE   A  1  105 ? 15.098  -15.488 -42.029  1.00 73.23  ? 105  ILE   A H    1 
ATOM   1602  H  HA   . ILE   A  1  105 ? 15.894  -14.916 -39.500  1.00 73.53  ? 105  ILE   A HA   1 
ATOM   1603  H  HB   . ILE   A  1  105 ? 13.329  -14.237 -40.482  1.00 76.54  ? 105  ILE   A HB   1 
ATOM   1604  H  HG12 . ILE   A  1  105 ? 15.384  -12.447 -39.743  1.00 82.76  ? 105  ILE   A HG12 1 
ATOM   1605  H  HG13 . ILE   A  1  105 ? 14.869  -12.670 -41.230  1.00 82.76  ? 105  ILE   A HG13 1 
ATOM   1606  H  HG21 . ILE   A  1  105 ? 12.907  -13.367 -38.342  1.00 72.08  ? 105  ILE   A HG21 1 
ATOM   1607  H  HG22 . ILE   A  1  105 ? 13.235  -14.918 -38.242  1.00 72.08  ? 105  ILE   A HG22 1 
ATOM   1608  H  HG23 . ILE   A  1  105 ? 14.345  -13.845 -37.866  1.00 72.08  ? 105  ILE   A HG23 1 
ATOM   1609  H  HD11 . ILE   A  1  105 ? 13.969  -10.711 -40.477  1.00 85.40  ? 105  ILE   A HD11 1 
ATOM   1610  H  HD12 . ILE   A  1  105 ? 12.784  -11.764 -40.579  1.00 85.40  ? 105  ILE   A HD12 1 
ATOM   1611  H  HD13 . ILE   A  1  105 ? 13.421  -11.419 -39.165  1.00 85.40  ? 105  ILE   A HD13 1 
ATOM   1612  N  N    . LEU   A  1  106 ? 15.060  -17.078 -38.683  1.00 59.44  ? 106  LEU   A N    1 
ATOM   1613  C  CA   . LEU   A  1  106 ? 14.629  -18.406 -38.265  1.00 53.96  ? 106  LEU   A CA   1 
ATOM   1614  C  C    . LEU   A  1  106 ? 13.956  -18.304 -36.905  1.00 59.23  ? 106  LEU   A C    1 
ATOM   1615  O  O    . LEU   A  1  106 ? 14.585  -17.888 -35.926  1.00 63.84  ? 106  LEU   A O    1 
ATOM   1616  C  CB   . LEU   A  1  106 ? 15.811  -19.376 -38.211  1.00 53.50  ? 106  LEU   A CB   1 
ATOM   1617  C  CG   . LEU   A  1  106 ? 15.457  -20.810 -37.811  1.00 50.09  ? 106  LEU   A CG   1 
ATOM   1618  C  CD1  . LEU   A  1  106 ? 14.453  -21.401 -38.790  1.00 50.31  ? 106  LEU   A CD1  1 
ATOM   1619  C  CD2  . LEU   A  1  106 ? 16.702  -21.676 -37.730  1.00 49.18  ? 106  LEU   A CD2  1 
ATOM   1620  H  H    . LEU   A  1  106 ? 15.636  -16.720 -38.154  1.00 71.31  ? 106  LEU   A H    1 
ATOM   1621  H  HA   . LEU   A  1  106 ? 13.979  -18.747 -38.900  1.00 64.74  ? 106  LEU   A HA   1 
ATOM   1622  H  HB2  . LEU   A  1  106 ? 16.217  -19.412 -39.091  1.00 64.18  ? 106  LEU   A HB2  1 
ATOM   1623  H  HB3  . LEU   A  1  106 ? 16.451  -19.042 -37.563  1.00 64.18  ? 106  LEU   A HB3  1 
ATOM   1624  H  HG   . LEU   A  1  106 ? 15.052  -20.799 -36.930  1.00 60.09  ? 106  LEU   A HG   1 
ATOM   1625  H  HD11 . LEU   A  1  106 ? 14.343  -22.345 -38.599  1.00 60.36  ? 106  LEU   A HD11 1 
ATOM   1626  H  HD12 . LEU   A  1  106 ? 13.604  -20.942 -38.687  1.00 60.36  ? 106  LEU   A HD12 1 
ATOM   1627  H  HD13 . LEU   A  1  106 ? 14.785  -21.282 -39.693  1.00 60.36  ? 106  LEU   A HD13 1 
ATOM   1628  H  HD21 . LEU   A  1  106 ? 16.450  -22.565 -37.434  1.00 59.00  ? 106  LEU   A HD21 1 
ATOM   1629  H  HD22 . LEU   A  1  106 ? 17.112  -21.722 -38.607  1.00 59.00  ? 106  LEU   A HD22 1 
ATOM   1630  H  HD23 . LEU   A  1  106 ? 17.321  -21.280 -37.096  1.00 59.00  ? 106  LEU   A HD23 1 
ATOM   1631  N  N    . ALA   A  1  107 ? 12.679  -18.680 -36.850  1.00 60.06  ? 107  ALA   A N    1 
ATOM   1632  C  CA   . ALA   A  1  107 ? 11.913  -18.731 -35.614  1.00 58.10  ? 107  ALA   A CA   1 
ATOM   1633  C  C    . ALA   A  1  107 ? 11.262  -20.101 -35.498  1.00 55.48  ? 107  ALA   A C    1 
ATOM   1634  O  O    . ALA   A  1  107 ? 10.883  -20.709 -36.503  1.00 56.40  ? 107  ALA   A O    1 
ATOM   1635  C  CB   . ALA   A  1  107 ? 10.847  -17.630 -35.567  1.00 58.73  ? 107  ALA   A CB   1 
ATOM   1636  H  H    . ALA   A  1  107 ? 12.223  -18.917 -37.540  1.00 72.05  ? 107  ALA   A H    1 
ATOM   1637  H  HA   . ALA   A  1  107 ? 12.499  -18.604 -34.851  1.00 69.71  ? 107  ALA   A HA   1 
ATOM   1638  H  HB1  . ALA   A  1  107 ? 10.362  -17.695 -34.730  1.00 70.46  ? 107  ALA   A HB1  1 
ATOM   1639  H  HB2  . ALA   A  1  107 ? 11.282  -16.766 -35.631  1.00 70.46  ? 107  ALA   A HB2  1 
ATOM   1640  H  HB3  . ALA   A  1  107 ? 10.237  -17.749 -36.312  1.00 70.46  ? 107  ALA   A HB3  1 
ATOM   1641  N  N    . CYS   A  1  108 ? 11.132  -20.588 -34.265  1.00 55.89  ? 108  CYS   A N    1 
ATOM   1642  C  CA   . CYS   A  1  108 ? 10.683  -21.952 -34.029  1.00 59.50  ? 108  CYS   A CA   1 
ATOM   1643  C  C    . CYS   A  1  108 ? 9.600   -21.994 -32.958  1.00 57.23  ? 108  CYS   A C    1 
ATOM   1644  O  O    . CYS   A  1  108 ? 9.491   -21.106 -32.109  1.00 56.30  ? 108  CYS   A O    1 
ATOM   1645  C  CB   . CYS   A  1  108 ? 11.852  -22.857 -33.612  1.00 60.13  ? 108  CYS   A CB   1 
ATOM   1646  S  SG   . CYS   A  1  108 ? 13.148  -23.046 -34.858  1.00 59.71  ? 108  CYS   A SG   1 
ATOM   1647  H  H    . CYS   A  1  108 ? 11.299  -20.143 -33.548  1.00 67.05  ? 108  CYS   A H    1 
ATOM   1648  H  HA   . CYS   A  1  108 ? 10.290  -22.291 -34.848  1.00 71.39  ? 108  CYS   A HA   1 
ATOM   1649  H  HB2  . CYS   A  1  108 ? 12.263  -22.482 -32.818  1.00 72.14  ? 108  CYS   A HB2  1 
ATOM   1650  H  HB3  . CYS   A  1  108 ? 11.502  -23.741 -33.419  1.00 72.14  ? 108  CYS   A HB3  1 
ATOM   1651  N  N    . ALA   A  1  109 ? 8.800   -23.060 -33.018  1.00 55.31  ? 109  ALA   A N    1 
ATOM   1652  C  CA   . ALA   A  1  109 ? 7.733   -23.342 -32.059  1.00 54.64  ? 109  ALA   A CA   1 
ATOM   1653  C  C    . ALA   A  1  109 ? 8.031   -24.693 -31.421  1.00 53.60  ? 109  ALA   A C    1 
ATOM   1654  O  O    . ALA   A  1  109 ? 7.615   -25.740 -31.942  1.00 49.31  ? 109  ALA   A O    1 
ATOM   1655  C  CB   . ALA   A  1  109 ? 6.366   -23.342 -32.741  1.00 54.26  ? 109  ALA   A CB   1 
ATOM   1656  H  H    . ALA   A  1  109 ? 8.860   -23.659 -33.632  1.00 66.36  ? 109  ALA   A H    1 
ATOM   1657  H  HA   . ALA   A  1  109 ? 7.722   -22.663 -31.366  1.00 65.55  ? 109  ALA   A HA   1 
ATOM   1658  H  HB1  . ALA   A  1  109 ? 5.684   -23.546 -32.082  1.00 65.09  ? 109  ALA   A HB1  1 
ATOM   1659  H  HB2  . ALA   A  1  109 ? 6.204   -22.465 -33.123  1.00 65.09  ? 109  ALA   A HB2  1 
ATOM   1660  H  HB3  . ALA   A  1  109 ? 6.362   -24.013 -33.440  1.00 65.09  ? 109  ALA   A HB3  1 
ATOM   1661  N  N    . PRO   A  1  110 ? 8.753   -24.724 -30.296  1.00 55.50  ? 110  PRO   A N    1 
ATOM   1662  C  CA   . PRO   A  1  110 ? 9.173   -26.017 -29.729  1.00 54.95  ? 110  PRO   A CA   1 
ATOM   1663  C  C    . PRO   A  1  110 ? 8.042   -26.835 -29.127  1.00 56.25  ? 110  PRO   A C    1 
ATOM   1664  O  O    . PRO   A  1  110 ? 8.282   -27.991 -28.754  1.00 60.66  ? 110  PRO   A O    1 
ATOM   1665  C  CB   . PRO   A  1  110 ? 10.194  -25.619 -28.651  1.00 52.73  ? 110  PRO   A CB   1 
ATOM   1666  C  CG   . PRO   A  1  110 ? 10.532  -24.180 -28.921  1.00 54.13  ? 110  PRO   A CG   1 
ATOM   1667  C  CD   . PRO   A  1  110 ? 9.310   -23.591 -29.540  1.00 54.36  ? 110  PRO   A CD   1 
ATOM   1668  H  HA   . PRO   A  1  110 ? 9.615   -26.543 -30.415  1.00 65.93  ? 110  PRO   A HA   1 
ATOM   1669  H  HB2  . PRO   A  1  110 ? 9.798   -25.721 -27.772  1.00 63.26  ? 110  PRO   A HB2  1 
ATOM   1670  H  HB3  . PRO   A  1  110 ? 10.984  -26.178 -28.726  1.00 63.26  ? 110  PRO   A HB3  1 
ATOM   1671  H  HG2  . PRO   A  1  110 ? 10.746  -23.731 -28.089  1.00 64.93  ? 110  PRO   A HG2  1 
ATOM   1672  H  HG3  . PRO   A  1  110 ? 11.285  -24.128 -29.530  1.00 64.93  ? 110  PRO   A HG3  1 
ATOM   1673  H  HD2  . PRO   A  1  110 ? 8.688   -23.287 -28.861  1.00 65.21  ? 110  PRO   A HD2  1 
ATOM   1674  H  HD3  . PRO   A  1  110 ? 9.539   -22.857 -30.132  1.00 65.21  ? 110  PRO   A HD3  1 
ATOM   1675  N  N    . LEU   A  1  111 ? 6.832   -26.286 -29.011  1.00 51.32  ? 111  LEU   A N    1 
ATOM   1676  C  CA   . LEU   A  1  111 ? 5.687   -27.019 -28.482  1.00 50.32  ? 111  LEU   A CA   1 
ATOM   1677  C  C    . LEU   A  1  111 ? 4.584   -27.153 -29.527  1.00 50.69  ? 111  LEU   A C    1 
ATOM   1678  O  O    . LEU   A  1  111 ? 3.401   -27.241 -29.193  1.00 51.11  ? 111  LEU   A O    1 
ATOM   1679  C  CB   . LEU   A  1  111 ? 5.157   -26.356 -27.212  1.00 50.49  ? 111  LEU   A CB   1 
ATOM   1680  C  CG   . LEU   A  1  111 ? 5.906   -26.749 -25.936  1.00 52.42  ? 111  LEU   A CG   1 
ATOM   1681  C  CD1  . LEU   A  1  111 ? 5.465   -25.890 -24.769  1.00 54.04  ? 111  LEU   A CD1  1 
ATOM   1682  C  CD2  . LEU   A  1  111 ? 5.695   -28.223 -25.612  1.00 54.29  ? 111  LEU   A CD2  1 
ATOM   1683  H  H    . LEU   A  1  111 ? 6.650   -25.476 -29.236  1.00 61.57  ? 111  LEU   A H    1 
ATOM   1684  H  HA   . LEU   A  1  111 ? 5.976   -27.914 -28.246  1.00 60.36  ? 111  LEU   A HA   1 
ATOM   1685  H  HB2  . LEU   A  1  111 ? 5.230   -25.394 -27.312  1.00 60.57  ? 111  LEU   A HB2  1 
ATOM   1686  H  HB3  . LEU   A  1  111 ? 4.227   -26.608 -27.097  1.00 60.57  ? 111  LEU   A HB3  1 
ATOM   1687  H  HG   . LEU   A  1  111 ? 6.854   -26.604 -26.081  1.00 62.88  ? 111  LEU   A HG   1 
ATOM   1688  H  HD11 . LEU   A  1  111 ? 5.950   -26.163 -23.975  1.00 64.83  ? 111  LEU   A HD11 1 
ATOM   1689  H  HD12 . LEU   A  1  111 ? 5.658   -24.961 -24.971  1.00 64.83  ? 111  LEU   A HD12 1 
ATOM   1690  H  HD13 . LEU   A  1  111 ? 4.512   -26.008 -24.633  1.00 64.83  ? 111  LEU   A HD13 1 
ATOM   1691  H  HD21 . LEU   A  1  111 ? 6.085   -28.415 -24.745  1.00 65.13  ? 111  LEU   A HD21 1 
ATOM   1692  H  HD22 . LEU   A  1  111 ? 4.743   -28.409 -25.595  1.00 65.13  ? 111  LEU   A HD22 1 
ATOM   1693  H  HD23 . LEU   A  1  111 ? 6.124   -28.761 -26.295  1.00 65.13  ? 111  LEU   A HD23 1 
ATOM   1694  N  N    . TYR   A  1  112 ? 4.966   -27.161 -30.799  1.00 47.72  ? 112  TYR   A N    1 
ATOM   1695  C  CA   . TYR   A  1  112 ? 4.058   -27.513 -31.882  1.00 52.82  ? 112  TYR   A CA   1 
ATOM   1696  C  C    . TYR   A  1  112 ? 3.891   -29.028 -31.910  1.00 57.70  ? 112  TYR   A C    1 
ATOM   1697  O  O    . TYR   A  1  112 ? 4.878   -29.763 -32.023  1.00 61.01  ? 112  TYR   A O    1 
ATOM   1698  C  CB   . TYR   A  1  112 ? 4.611   -26.983 -33.205  1.00 54.53  ? 112  TYR   A CB   1 
ATOM   1699  C  CG   . TYR   A  1  112 ? 4.083   -27.652 -34.456  1.00 51.64  ? 112  TYR   A CG   1 
ATOM   1700  C  CD1  . TYR   A  1  112 ? 2.999   -27.126 -35.145  1.00 49.09  ? 112  TYR   A CD1  1 
ATOM   1701  C  CD2  . TYR   A  1  112 ? 4.690   -28.796 -34.964  1.00 49.87  ? 112  TYR   A CD2  1 
ATOM   1702  C  CE1  . TYR   A  1  112 ? 2.523   -27.727 -36.294  1.00 48.55  ? 112  TYR   A CE1  1 
ATOM   1703  C  CE2  . TYR   A  1  112 ? 4.219   -29.406 -36.112  1.00 50.05  ? 112  TYR   A CE2  1 
ATOM   1704  C  CZ   . TYR   A  1  112 ? 3.135   -28.869 -36.773  1.00 51.38  ? 112  TYR   A CZ   1 
ATOM   1705  O  OH   . TYR   A  1  112 ? 2.665   -29.471 -37.918  1.00 50.93  ? 112  TYR   A OH   1 
ATOM   1706  H  H    . TYR   A  1  112 ? 5.760   -26.964 -31.065  1.00 57.24  ? 112  TYR   A H    1 
ATOM   1707  H  HA   . TYR   A  1  112 ? 3.184   -27.115 -31.742  1.00 63.37  ? 112  TYR   A HA   1 
ATOM   1708  H  HB2  . TYR   A  1  112 ? 4.392   -26.040 -33.270  1.00 65.42  ? 112  TYR   A HB2  1 
ATOM   1709  H  HB3  . TYR   A  1  112 ? 5.574   -27.100 -33.201  1.00 65.42  ? 112  TYR   A HB3  1 
ATOM   1710  H  HD1  . TYR   A  1  112 ? 2.585   -26.356 -34.827  1.00 58.88  ? 112  TYR   A HD1  1 
ATOM   1711  H  HD2  . TYR   A  1  112 ? 5.425   -29.156 -34.524  1.00 59.82  ? 112  TYR   A HD2  1 
ATOM   1712  H  HE1  . TYR   A  1  112 ? 1.795   -27.364 -36.744  1.00 58.24  ? 112  TYR   A HE1  1 
ATOM   1713  H  HE2  . TYR   A  1  112 ? 4.631   -30.175 -36.436  1.00 60.04  ? 112  TYR   A HE2  1 
ATOM   1714  H  HH   . TYR   A  1  112 ? 2.174   -28.937 -38.342  1.00 61.09  ? 112  TYR   A HH   1 
ATOM   1715  N  N    . HIS   A  1  113 ? 2.652   -29.494 -31.782  1.00 57.09  ? 113  HIS   A N    1 
ATOM   1716  C  CA   . HIS   A  1  113 ? 2.337   -30.914 -31.830  1.00 56.84  ? 113  HIS   A CA   1 
ATOM   1717  C  C    . HIS   A  1  113 ? 1.708   -31.243 -33.177  1.00 56.02  ? 113  HIS   A C    1 
ATOM   1718  O  O    . HIS   A  1  113 ? 1.026   -30.411 -33.782  1.00 60.31  ? 113  HIS   A O    1 
ATOM   1719  C  CB   . HIS   A  1  113 ? 1.377   -31.320 -30.707  1.00 60.39  ? 113  HIS   A CB   1 
ATOM   1720  C  CG   . HIS   A  1  113 ? 1.796   -30.856 -29.346  1.00 60.92  ? 113  HIS   A CG   1 
ATOM   1721  N  ND1  . HIS   A  1  113 ? 1.859   -29.523 -29.001  1.00 62.96  ? 113  HIS   A ND1  1 
ATOM   1722  C  CD2  . HIS   A  1  113 ? 2.159   -31.548 -28.240  1.00 59.85  ? 113  HIS   A CD2  1 
ATOM   1723  C  CE1  . HIS   A  1  113 ? 2.249   -29.414 -27.744  1.00 62.65  ? 113  HIS   A CE1  1 
ATOM   1724  N  NE2  . HIS   A  1  113 ? 2.438   -30.628 -27.259  1.00 60.53  ? 113  HIS   A NE2  1 
ATOM   1725  H  H    . HIS   A  1  113 ? 1.962   -28.993 -31.664  1.00 68.49  ? 113  HIS   A H    1 
ATOM   1726  H  HA   . HIS   A  1  113 ? 3.152   -31.428 -31.718  1.00 68.19  ? 113  HIS   A HA   1 
ATOM   1727  H  HB2  . HIS   A  1  113 ? 0.504   -30.941 -30.891  1.00 72.44  ? 113  HIS   A HB2  1 
ATOM   1728  H  HB3  . HIS   A  1  113 ? 1.320   -32.288 -30.683  1.00 72.44  ? 113  HIS   A HB3  1 
ATOM   1729  H  HD1  . HIS   A  1  113 ? 1.673   -28.866 -29.523  1.00 75.53  ? 113  HIS   A HD1  1 
ATOM   1730  H  HD2  . HIS   A  1  113 ? 2.210   -32.473 -28.160  1.00 71.80  ? 113  HIS   A HD2  1 
ATOM   1731  H  HE1  . HIS   A  1  113 ? 2.369   -28.618 -27.279  1.00 75.16  ? 113  HIS   A HE1  1 
ATOM   1732  N  N    . TRP   A  1  114 ? 1.940   -32.467 -33.642  1.00 55.09  ? 114  TRP   A N    1 
ATOM   1733  C  CA   . TRP   A  1  114 ? 1.416   -32.910 -34.925  1.00 57.66  ? 114  TRP   A CA   1 
ATOM   1734  C  C    . TRP   A  1  114 ? 0.818   -34.297 -34.770  1.00 57.46  ? 114  TRP   A C    1 
ATOM   1735  O  O    . TRP   A  1  114 ? 1.271   -35.101 -33.952  1.00 56.31  ? 114  TRP   A O    1 
ATOM   1736  C  CB   . TRP   A  1  114 ? 2.507   -32.870 -36.005  1.00 61.94  ? 114  TRP   A CB   1 
ATOM   1737  C  CG   . TRP   A  1  114 ? 3.156   -34.173 -36.381  1.00 61.82  ? 114  TRP   A CG   1 
ATOM   1738  C  CD1  . TRP   A  1  114 ? 3.913   -34.986 -35.584  1.00 64.16  ? 114  TRP   A CD1  1 
ATOM   1739  C  CD2  . TRP   A  1  114 ? 3.142   -34.782 -37.677  1.00 60.72  ? 114  TRP   A CD2  1 
ATOM   1740  N  NE1  . TRP   A  1  114 ? 4.355   -36.073 -36.304  1.00 67.06  ? 114  TRP   A NE1  1 
ATOM   1741  C  CE2  . TRP   A  1  114 ? 3.895   -35.969 -37.592  1.00 66.15  ? 114  TRP   A CE2  1 
ATOM   1742  C  CE3  . TRP   A  1  114 ? 2.557   -34.441 -38.901  1.00 58.30  ? 114  TRP   A CE3  1 
ATOM   1743  C  CZ2  . TRP   A  1  114 ? 4.076   -36.818 -38.684  1.00 71.01  ? 114  TRP   A CZ2  1 
ATOM   1744  C  CZ3  . TRP   A  1  114 ? 2.737   -35.284 -39.982  1.00 64.19  ? 114  TRP   A CZ3  1 
ATOM   1745  C  CH2  . TRP   A  1  114 ? 3.490   -36.457 -39.867  1.00 70.74  ? 114  TRP   A CH2  1 
ATOM   1746  H  H    . TRP   A  1  114 ? 2.402   -33.062 -33.228  1.00 66.09  ? 114  TRP   A H    1 
ATOM   1747  H  HA   . TRP   A  1  114 ? 0.698   -32.330 -35.226  1.00 69.17  ? 114  TRP   A HA   1 
ATOM   1748  H  HB2  . TRP   A  1  114 ? 2.112   -32.510 -36.814  1.00 74.31  ? 114  TRP   A HB2  1 
ATOM   1749  H  HB3  . TRP   A  1  114 ? 3.215   -32.285 -35.692  1.00 74.31  ? 114  TRP   A HB3  1 
ATOM   1750  H  HD1  . TRP   A  1  114 ? 4.101   -34.828 -34.687  1.00 76.98  ? 114  TRP   A HD1  1 
ATOM   1751  H  HE1  . TRP   A  1  114 ? 4.840   -36.712 -35.997  1.00 80.45  ? 114  TRP   A HE1  1 
ATOM   1752  H  HE3  . TRP   A  1  114 ? 2.056   -33.662 -38.985  1.00 69.94  ? 114  TRP   A HE3  1 
ATOM   1753  H  HZ2  . TRP   A  1  114 ? 4.576   -37.599 -38.611  1.00 85.19  ? 114  TRP   A HZ2  1 
ATOM   1754  H  HZ3  . TRP   A  1  114 ? 2.352   -35.066 -40.800  1.00 77.01  ? 114  TRP   A HZ3  1 
ATOM   1755  H  HH2  . TRP   A  1  114 ? 3.595   -37.005 -40.612  1.00 84.87  ? 114  TRP   A HH2  1 
ATOM   1756  N  N    . ARG   A  1  115 ? -0.230  -34.558 -35.547  1.00 60.25  ? 115  ARG   A N    1 
ATOM   1757  C  CA   . ARG   A  1  115 ? -1.044  -35.734 -35.287  1.00 62.94  ? 115  ARG   A CA   1 
ATOM   1758  C  C    . ARG   A  1  115 ? -0.308  -36.996 -35.699  1.00 65.11  ? 115  ARG   A C    1 
ATOM   1759  O  O    . ARG   A  1  115 ? 0.221   -37.718 -34.850  1.00 69.58  ? 115  ARG   A O    1 
ATOM   1760  C  CB   . ARG   A  1  115 ? -2.359  -35.585 -36.068  1.00 63.69  ? 115  ARG   A CB   1 
ATOM   1761  C  CG   . ARG   A  1  115 ? -3.305  -36.782 -36.099  1.00 64.73  ? 115  ARG   A CG   1 
ATOM   1762  C  CD   . ARG   A  1  115 ? -4.109  -36.775 -37.404  1.00 65.82  ? 115  ARG   A CD   1 
ATOM   1763  N  NE   . ARG   A  1  115 ? -5.206  -37.742 -37.409  1.00 68.15  ? 115  ARG   A NE   1 
ATOM   1764  C  CZ   . ARG   A  1  115 ? -5.174  -38.931 -38.008  1.00 69.17  ? 115  ARG   A CZ   1 
ATOM   1765  N  NH1  . ARG   A  1  115 ? -4.096  -39.338 -38.668  1.00 69.29  ? 115  ARG   A NH1  1 
ATOM   1766  N  NH2  . ARG   A  1  115 ? -6.236  -39.721 -37.946  1.00 69.16  ? 115  ARG   A NH2  1 
ATOM   1767  H  H    . ARG   A  1  115 ? -0.482  -34.079 -36.216  1.00 72.29  ? 115  ARG   A H    1 
ATOM   1768  H  HA   . ARG   A  1  115 ? -1.240  -35.816 -34.340  1.00 75.51  ? 115  ARG   A HA   1 
ATOM   1769  H  HB2  . ARG   A  1  115 ? -2.854  -34.848 -35.678  1.00 76.41  ? 115  ARG   A HB2  1 
ATOM   1770  H  HB3  . ARG   A  1  115 ? -2.135  -35.382 -36.990  1.00 76.41  ? 115  ARG   A HB3  1 
ATOM   1771  H  HG2  . ARG   A  1  115 ? -2.794  -37.605 -36.051  1.00 77.66  ? 115  ARG   A HG2  1 
ATOM   1772  H  HG3  . ARG   A  1  115 ? -3.922  -36.731 -35.352  1.00 77.66  ? 115  ARG   A HG3  1 
ATOM   1773  H  HD2  . ARG   A  1  115 ? -4.490  -35.893 -37.534  1.00 78.97  ? 115  ARG   A HD2  1 
ATOM   1774  H  HD3  . ARG   A  1  115 ? -3.516  -36.993 -38.140  1.00 78.97  ? 115  ARG   A HD3  1 
ATOM   1775  H  HE   . ARG   A  1  115 ? -5.927  -37.526 -36.994  1.00 81.76  ? 115  ARG   A HE   1 
ATOM   1776  H  HH11 . ARG   A  1  115 ? -3.404  -38.831 -38.714  1.00 83.13  ? 115  ARG   A HH11 1 
ATOM   1777  H  HH12 . ARG   A  1  115 ? -4.091  -40.109 -39.049  1.00 83.13  ? 115  ARG   A HH12 1 
ATOM   1778  H  HH21 . ARG   A  1  115 ? -6.939  -39.464 -37.522  1.00 82.97  ? 115  ARG   A HH21 1 
ATOM   1779  H  HH22 . ARG   A  1  115 ? -6.223  -40.490 -38.330  1.00 82.97  ? 115  ARG   A HH22 1 
ATOM   1780  N  N    . THR   A  1  116 ? -0.337  -37.300 -36.989  1.00 66.90  ? 116  THR   A N    1 
ATOM   1781  C  CA   . THR   A  1  116 ? 0.603   -38.133 -37.732  1.00 65.19  ? 116  THR   A CA   1 
ATOM   1782  C  C    . THR   A  1  116 ? -0.312  -38.518 -38.889  1.00 70.57  ? 116  THR   A C    1 
ATOM   1783  O  O    . THR   A  1  116 ? -1.449  -38.034 -38.930  1.00 75.33  ? 116  THR   A O    1 
ATOM   1784  C  CB   . THR   A  1  116 ? 1.203   -39.293 -36.950  1.00 64.11  ? 116  THR   A CB   1 
ATOM   1785  O  OG1  . THR   A  1  116 ? 0.199   -39.937 -36.169  1.00 67.48  ? 116  THR   A OG1  1 
ATOM   1786  C  CG2  . THR   A  1  116 ? 2.358   -38.792 -36.048  1.00 62.69  ? 116  THR   A CG2  1 
ATOM   1787  H  H    . THR   A  1  116 ? -0.954  -37.006 -37.513  1.00 80.26  ? 116  THR   A H    1 
ATOM   1788  H  HA   . THR   A  1  116 ? 1.437   -37.711 -37.991  1.00 78.21  ? 116  THR   A HA   1 
ATOM   1789  H  HB   . THR   A  1  116 ? 1.566   -39.948 -37.567  1.00 76.91  ? 116  THR   A HB   1 
ATOM   1790  H  HG1  . THR   A  1  116 ? 0.482   -40.067 -35.389  1.00 80.95  ? 116  THR   A HG1  1 
ATOM   1791  H  HG21 . THR   A  1  116 ? 2.351   -39.270 -35.204  1.00 75.21  ? 116  THR   A HG21 1 
ATOM   1792  H  HG22 . THR   A  1  116 ? 3.210   -38.940 -36.488  1.00 75.21  ? 116  THR   A HG22 1 
ATOM   1793  H  HG23 . THR   A  1  116 ? 2.254   -37.843 -35.874  1.00 75.21  ? 116  THR   A HG23 1 
ATOM   1794  N  N    . GLU   A  1  117 ? 0.117   -39.353 -39.824  1.00 73.21  ? 117  GLU   A N    1 
ATOM   1795  C  CA   . GLU   A  1  117 ? -0.862  -39.864 -40.778  1.00 75.73  ? 117  GLU   A CA   1 
ATOM   1796  C  C    . GLU   A  1  117 ? -1.450  -41.215 -40.389  1.00 75.74  ? 117  GLU   A C    1 
ATOM   1797  O  O    . GLU   A  1  117 ? -2.571  -41.521 -40.809  1.00 78.70  ? 117  GLU   A O    1 
ATOM   1798  C  CB   . GLU   A  1  117 ? -0.252  -39.951 -42.175  1.00 78.56  ? 117  GLU   A CB   1 
ATOM   1799  C  CG   . GLU   A  1  117 ? 0.264   -38.611 -42.648  1.00 78.66  ? 117  GLU   A CG   1 
ATOM   1800  C  CD   . GLU   A  1  117 ? 0.362   -38.520 -44.152  1.00 81.65  ? 117  GLU   A CD   1 
ATOM   1801  O  OE1  . GLU   A  1  117 ? 1.424   -38.877 -44.701  1.00 82.75  ? 117  GLU   A OE1  1 
ATOM   1802  O  OE2  . GLU   A  1  117 ? -0.628  -38.098 -44.787  1.00 82.57  ? 117  GLU   A OE2  1 
ATOM   1803  H  H    . GLU   A  1  117 ? 0.926   -39.626 -39.924  1.00 87.83  ? 117  GLU   A H    1 
ATOM   1804  H  HA   . GLU   A  1  117 ? -1.599  -39.234 -40.819  1.00 90.86  ? 117  GLU   A HA   1 
ATOM   1805  H  HB2  . GLU   A  1  117 ? 0.491   -40.576 -42.161  1.00 94.25  ? 117  GLU   A HB2  1 
ATOM   1806  H  HB3  . GLU   A  1  117 ? -0.928  -40.255 -42.801  1.00 94.25  ? 117  GLU   A HB3  1 
ATOM   1807  H  HG2  . GLU   A  1  117 ? -0.339  -37.915 -42.344  1.00 94.37  ? 117  GLU   A HG2  1 
ATOM   1808  H  HG3  . GLU   A  1  117 ? 1.150   -38.466 -42.281  1.00 94.37  ? 117  GLU   A HG3  1 
ATOM   1809  N  N    . MET   A  1  118 ? -0.753  -42.018 -39.581  1.00 76.60  ? 118  MET   A N    1 
ATOM   1810  C  CA   . MET   A  1  118 ? -1.258  -43.355 -39.281  1.00 78.58  ? 118  MET   A CA   1 
ATOM   1811  C  C    . MET   A  1  118 ? -2.332  -43.339 -38.195  1.00 77.23  ? 118  MET   A C    1 
ATOM   1812  O  O    . MET   A  1  118 ? -3.346  -44.034 -38.322  1.00 82.86  ? 118  MET   A O    1 
ATOM   1813  C  CB   . MET   A  1  118 ? -0.109  -44.278 -38.869  1.00 79.54  ? 118  MET   A CB   1 
ATOM   1814  C  CG   . MET   A  1  118 ? 0.853   -44.645 -40.000  1.00 82.48  ? 118  MET   A CG   1 
ATOM   1815  S  SD   . MET   A  1  118 ? 0.056   -44.993 -41.582  1.00 84.99  ? 118  MET   A SD   1 
ATOM   1816  C  CE   . MET   A  1  118 ? 1.253   -44.305 -42.723  1.00 84.98  ? 118  MET   A CE   1 
ATOM   1817  H  H    . MET   A  1  118 ? -0.006  -41.817 -39.205  1.00 91.90  ? 118  MET   A H    1 
ATOM   1818  H  HA   . MET   A  1  118 ? -1.651  -43.709 -40.094  1.00 94.28  ? 118  MET   A HA   1 
ATOM   1819  H  HB2  . MET   A  1  118 ? 0.408   -43.837 -38.177  1.00 95.43  ? 118  MET   A HB2  1 
ATOM   1820  H  HB3  . MET   A  1  118 ? -0.485  -45.104 -38.526  1.00 95.43  ? 118  MET   A HB3  1 
ATOM   1821  H  HG2  . MET   A  1  118 ? 1.464   -43.905 -40.137  1.00 98.96  ? 118  MET   A HG2  1 
ATOM   1822  H  HG3  . MET   A  1  118 ? 1.346   -45.439 -39.740  1.00 98.96  ? 118  MET   A HG3  1 
ATOM   1823  H  HE1  . MET   A  1  118 ? 0.995   -44.535 -43.629  1.00 101.95 ? 118  MET   A HE1  1 
ATOM   1824  H  HE2  . MET   A  1  118 ? 1.271   -43.341 -42.618  1.00 101.95 ? 118  MET   A HE2  1 
ATOM   1825  H  HE3  . MET   A  1  118 ? 2.128   -44.675 -42.524  1.00 101.95 ? 118  MET   A HE3  1 
ATOM   1826  N  N    . LYS   A  1  119 ? -2.138  -42.569 -37.124  1.00 74.25  ? 119  LYS   A N    1 
ATOM   1827  C  CA   . LYS   A  1  119 ? -3.055  -42.600 -35.992  1.00 77.07  ? 119  LYS   A CA   1 
ATOM   1828  C  C    . LYS   A  1  119 ? -3.226  -41.206 -35.405  1.00 73.56  ? 119  LYS   A C    1 
ATOM   1829  O  O    . LYS   A  1  119 ? -2.403  -40.311 -35.613  1.00 74.83  ? 119  LYS   A O    1 
ATOM   1830  C  CB   . LYS   A  1  119 ? -2.567  -43.568 -34.902  1.00 84.72  ? 119  LYS   A CB   1 
ATOM   1831  C  CG   . LYS   A  1  119 ? -3.002  -45.008 -35.127  1.00 96.81  ? 119  LYS   A CG   1 
ATOM   1832  C  CD   . LYS   A  1  119 ? -2.339  -45.969 -34.150  1.00 103.37 ? 119  LYS   A CD   1 
ATOM   1833  C  CE   . LYS   A  1  119 ? -2.372  -47.394 -34.683  1.00 105.91 ? 119  LYS   A CE   1 
ATOM   1834  N  NZ   . LYS   A  1  119 ? -2.141  -48.418 -33.626  1.00 105.65 ? 119  LYS   A NZ   1 
ATOM   1835  H  H    . LYS   A  1  119 ? -1.481  -42.022 -37.032  1.00 89.08  ? 119  LYS   A H    1 
ATOM   1836  H  HA   . LYS   A  1  119 ? -3.925  -42.890 -36.308  1.00 92.46  ? 119  LYS   A HA   1 
ATOM   1837  H  HB2  . LYS   A  1  119 ? -1.598  -43.551 -34.880  1.00 101.64 ? 119  LYS   A HB2  1 
ATOM   1838  H  HB3  . LYS   A  1  119 ? -2.924  -43.281 -34.047  1.00 101.64 ? 119  LYS   A HB3  1 
ATOM   1839  H  HG2  . LYS   A  1  119 ? -3.962  -45.073 -35.010  1.00 116.15 ? 119  LYS   A HG2  1 
ATOM   1840  H  HG3  . LYS   A  1  119 ? -2.758  -45.278 -36.027  1.00 116.15 ? 119  LYS   A HG3  1 
ATOM   1841  H  HD2  . LYS   A  1  119 ? -1.414  -45.711 -34.020  1.00 124.02 ? 119  LYS   A HD2  1 
ATOM   1842  H  HD3  . LYS   A  1  119 ? -2.813  -45.946 -33.303  1.00 124.02 ? 119  LYS   A HD3  1 
ATOM   1843  H  HE2  . LYS   A  1  119 ? -3.242  -47.563 -35.077  1.00 127.07 ? 119  LYS   A HE2  1 
ATOM   1844  H  HE3  . LYS   A  1  119 ? -1.679  -47.495 -35.354  1.00 127.07 ? 119  LYS   A HE3  1 
ATOM   1845  H  HZ1  . LYS   A  1  119 ? -2.094  -49.228 -33.992  1.00 126.76 ? 119  LYS   A HZ1  1 
ATOM   1846  H  HZ2  . LYS   A  1  119 ? -1.378  -48.248 -33.200  1.00 126.76 ? 119  LYS   A HZ2  1 
ATOM   1847  H  HZ3  . LYS   A  1  119 ? -2.809  -48.404 -33.038  1.00 126.76 ? 119  LYS   A HZ3  1 
ATOM   1848  N  N    . GLN   A  1  120 ? -4.321  -41.038 -34.663  1.00 67.84  ? 120  GLN   A N    1 
ATOM   1849  C  CA   . GLN   A  1  120 ? -4.594  -39.790 -33.958  1.00 63.74  ? 120  GLN   A CA   1 
ATOM   1850  C  C    . GLN   A  1  120 ? -3.662  -39.678 -32.759  1.00 65.47  ? 120  GLN   A C    1 
ATOM   1851  O  O    . GLN   A  1  120 ? -3.853  -40.360 -31.748  1.00 71.02  ? 120  GLN   A O    1 
ATOM   1852  C  CB   . GLN   A  1  120 ? -6.051  -39.738 -33.510  1.00 66.83  ? 120  GLN   A CB   1 
ATOM   1853  C  CG   . GLN   A  1  120 ? -6.977  -39.005 -34.461  1.00 70.02  ? 120  GLN   A CG   1 
ATOM   1854  C  CD   . GLN   A  1  120 ? -8.391  -38.916 -33.925  1.00 74.27  ? 120  GLN   A CD   1 
ATOM   1855  O  OE1  . GLN   A  1  120 ? -8.625  -38.362 -32.850  1.00 73.39  ? 120  GLN   A OE1  1 
ATOM   1856  N  NE2  . GLN   A  1  120 ? -9.342  -39.472 -34.666  1.00 78.79  ? 120  GLN   A NE2  1 
ATOM   1857  H  H    . GLN   A  1  120 ? -4.926  -41.638 -34.553  1.00 81.39  ? 120  GLN   A H    1 
ATOM   1858  H  HA   . GLN   A  1  120 ? -4.432  -39.045 -34.557  1.00 76.47  ? 120  GLN   A HA   1 
ATOM   1859  H  HB2  . GLN   A  1  120 ? -6.379  -40.647 -33.423  1.00 80.17  ? 120  GLN   A HB2  1 
ATOM   1860  H  HB3  . GLN   A  1  120 ? -6.094  -39.286 -32.653  1.00 80.17  ? 120  GLN   A HB3  1 
ATOM   1861  H  HG2  . GLN   A  1  120 ? -6.647  -38.103 -34.595  1.00 84.00  ? 120  GLN   A HG2  1 
ATOM   1862  H  HG3  . GLN   A  1  120 ? -7.004  -39.478 -35.307  1.00 84.00  ? 120  GLN   A HG3  1 
ATOM   1863  H  HE21 . GLN   A  1  120 ? -9.139  -39.856 -35.408  1.00 94.53  ? 120  GLN   A HE21 1 
ATOM   1864  H  HE22 . GLN   A  1  120 ? -10.160 -39.447 -34.404  1.00 94.53  ? 120  GLN   A HE22 1 
ATOM   1865  N  N    . GLU   A  1  121 ? -2.656  -38.818 -32.867  1.00 64.72  ? 121  GLU   A N    1 
ATOM   1866  C  CA   . GLU   A  1  121 ? -1.705  -38.577 -31.795  1.00 62.83  ? 121  GLU   A CA   1 
ATOM   1867  C  C    . GLU   A  1  121 ? -1.552  -37.071 -31.618  1.00 58.99  ? 121  GLU   A C    1 
ATOM   1868  O  O    . GLU   A  1  121 ? -2.141  -36.273 -32.352  1.00 59.28  ? 121  GLU   A O    1 
ATOM   1869  C  CB   . GLU   A  1  121 ? -0.354  -39.241 -32.093  1.00 62.62  ? 121  GLU   A CB   1 
ATOM   1870  C  CG   . GLU   A  1  121 ? -0.432  -40.735 -32.394  1.00 63.26  ? 121  GLU   A CG   1 
ATOM   1871  C  CD   . GLU   A  1  121 ? -0.674  -41.573 -31.156  1.00 68.37  ? 121  GLU   A CD   1 
ATOM   1872  O  OE1  . GLU   A  1  121 ? -0.656  -41.012 -30.040  1.00 71.75  ? 121  GLU   A OE1  1 
ATOM   1873  O  OE2  . GLU   A  1  121 ? -0.880  -42.796 -31.299  1.00 72.62  ? 121  GLU   A OE2  1 
ATOM   1874  H  H    . GLU   A  1  121 ? -2.502  -38.351 -33.573  1.00 77.65  ? 121  GLU   A H    1 
ATOM   1875  H  HA   . GLU   A  1  121 ? -2.045  -38.952 -30.967  1.00 75.37  ? 121  GLU   A HA   1 
ATOM   1876  H  HB2  . GLU   A  1  121 ? 0.039   -38.808 -32.867  1.00 75.12  ? 121  GLU   A HB2  1 
ATOM   1877  H  HB3  . GLU   A  1  121 ? 0.222   -39.128 -31.321  1.00 75.12  ? 121  GLU   A HB3  1 
ATOM   1878  H  HG2  . GLU   A  1  121 ? -1.164  -40.895 -33.011  1.00 75.89  ? 121  GLU   A HG2  1 
ATOM   1879  H  HG3  . GLU   A  1  121 ? 0.405   -41.022 -32.791  1.00 75.89  ? 121  GLU   A HG3  1 
ATOM   1880  N  N    . ARG   A  1  122 ? -0.777  -36.680 -30.608  1.00 55.22  ? 122  ARG   A N    1 
ATOM   1881  C  CA   . ARG   A  1  122 ? -0.405  -35.279 -30.386  1.00 55.18  ? 122  ARG   A CA   1 
ATOM   1882  C  C    . ARG   A  1  122 ? 1.058   -35.309 -29.948  1.00 49.68  ? 122  ARG   A C    1 
ATOM   1883  O  O    . ARG   A  1  122 ? 1.354   -35.356 -28.751  1.00 48.33  ? 122  ARG   A O    1 
ATOM   1884  C  CB   . ARG   A  1  122 ? -1.308  -34.620 -29.351  1.00 62.46  ? 122  ARG   A CB   1 
ATOM   1885  C  CG   . ARG   A  1  122 ? -1.027  -33.138 -29.088  1.00 67.59  ? 122  ARG   A CG   1 
ATOM   1886  C  CD   . ARG   A  1  122 ? -2.014  -32.564 -28.070  1.00 68.86  ? 122  ARG   A CD   1 
ATOM   1887  N  NE   . ARG   A  1  122 ? -1.750  -31.164 -27.740  1.00 71.62  ? 122  ARG   A NE   1 
ATOM   1888  C  CZ   . ARG   A  1  122 ? -0.886  -30.754 -26.815  1.00 83.40  ? 122  ARG   A CZ   1 
ATOM   1889  N  NH1  . ARG   A  1  122 ? -0.177  -31.632 -26.119  1.00 93.16  ? 122  ARG   A NH1  1 
ATOM   1890  N  NH2  . ARG   A  1  122 ? -0.727  -29.457 -26.588  1.00 85.47  ? 122  ARG   A NH2  1 
ATOM   1891  H  H    . ARG   A  1  122 ? -0.447  -37.218 -30.024  1.00 66.24  ? 122  ARG   A H    1 
ATOM   1892  H  HA   . ARG   A  1  122 ? -0.486  -34.769 -31.207  1.00 66.19  ? 122  ARG   A HA   1 
ATOM   1893  H  HB2  . ARG   A  1  122 ? -2.226  -34.691 -29.656  1.00 74.93  ? 122  ARG   A HB2  1 
ATOM   1894  H  HB3  . ARG   A  1  122 ? -1.201  -35.089 -28.508  1.00 74.93  ? 122  ARG   A HB3  1 
ATOM   1895  H  HG2  . ARG   A  1  122 ? -0.129  -33.037 -28.736  1.00 81.09  ? 122  ARG   A HG2  1 
ATOM   1896  H  HG3  . ARG   A  1  122 ? -1.117  -32.641 -29.916  1.00 81.09  ? 122  ARG   A HG3  1 
ATOM   1897  H  HD2  . ARG   A  1  122 ? -2.911  -32.621 -28.435  1.00 82.61  ? 122  ARG   A HD2  1 
ATOM   1898  H  HD3  . ARG   A  1  122 ? -1.956  -33.080 -27.250  1.00 82.61  ? 122  ARG   A HD3  1 
ATOM   1899  H  HE   . ARG   A  1  122 ? -2.185  -30.563 -28.176  1.00 85.92  ? 122  ARG   A HE   1 
ATOM   1900  H  HH11 . ARG   A  1  122 ? -0.273  -32.474 -26.263  1.00 111.78 ? 122  ARG   A HH11 1 
ATOM   1901  H  HH12 . ARG   A  1  122 ? 0.380   -31.358 -25.522  1.00 111.78 ? 122  ARG   A HH12 1 
ATOM   1902  H  HH21 . ARG   A  1  122 ? -1.182  -28.883 -27.039  1.00 102.54 ? 122  ARG   A HH21 1 
ATOM   1903  H  HH22 . ARG   A  1  122 ? -0.169  -29.191 -25.990  1.00 102.54 ? 122  ARG   A HH22 1 
ATOM   1904  N  N    . GLU   A  1  123 ? 1.966   -35.272 -30.922  1.00 50.66  ? 123  GLU   A N    1 
ATOM   1905  C  CA   . GLU   A  1  123 ? 3.384   -35.481 -30.661  1.00 51.67  ? 123  GLU   A CA   1 
ATOM   1906  C  C    . GLU   A  1  123 ? 4.147   -34.180 -30.854  1.00 52.61  ? 123  GLU   A C    1 
ATOM   1907  O  O    . GLU   A  1  123 ? 4.134   -33.622 -31.962  1.00 54.35  ? 123  GLU   A O    1 
ATOM   1908  C  CB   . GLU   A  1  123 ? 3.941   -36.575 -31.574  1.00 52.95  ? 123  GLU   A CB   1 
ATOM   1909  C  CG   . GLU   A  1  123 ? 3.336   -37.943 -31.294  1.00 58.89  ? 123  GLU   A CG   1 
ATOM   1910  C  CD   . GLU   A  1  123 ? 4.130   -39.086 -31.900  1.00 61.77  ? 123  GLU   A CD   1 
ATOM   1911  O  OE1  . GLU   A  1  123 ? 5.009   -38.825 -32.749  1.00 61.98  ? 123  GLU   A OE1  1 
ATOM   1912  O  OE2  . GLU   A  1  123 ? 3.876   -40.249 -31.522  1.00 61.12  ? 123  GLU   A OE2  1 
ATOM   1913  H  H    . GLU   A  1  123 ? 1.781   -35.126 -31.749  1.00 60.77  ? 123  GLU   A H    1 
ATOM   1914  H  HA   . GLU   A  1  123 ? 3.499   -35.761 -29.739  1.00 61.99  ? 123  GLU   A HA   1 
ATOM   1915  H  HB2  . GLU   A  1  123 ? 3.748   -36.344 -32.496  1.00 63.52  ? 123  GLU   A HB2  1 
ATOM   1916  H  HB3  . GLU   A  1  123 ? 4.900   -36.638 -31.442  1.00 63.52  ? 123  GLU   A HB3  1 
ATOM   1917  H  HG2  . GLU   A  1  123 ? 3.301   -38.080 -30.335  1.00 70.64  ? 123  GLU   A HG2  1 
ATOM   1918  H  HG3  . GLU   A  1  123 ? 2.440   -37.972 -31.667  1.00 70.64  ? 123  GLU   A HG3  1 
ATOM   1919  N  N    . PRO   A  1  124 ? 4.822   -33.659 -29.818  1.00 50.68  ? 124  PRO   A N    1 
ATOM   1920  C  CA   . PRO   A  1  124 ? 5.523   -32.363 -29.944  1.00 47.27  ? 124  PRO   A CA   1 
ATOM   1921  C  C    . PRO   A  1  124 ? 6.843   -32.479 -30.698  1.00 44.37  ? 124  PRO   A C    1 
ATOM   1922  O  O    . PRO   A  1  124 ? 7.942   -32.400 -30.139  1.00 39.29  ? 124  PRO   A O    1 
ATOM   1923  C  CB   . PRO   A  1  124 ? 5.711   -31.951 -28.480  1.00 49.99  ? 124  PRO   A CB   1 
ATOM   1924  C  CG   . PRO   A  1  124 ? 5.848   -33.241 -27.751  1.00 49.18  ? 124  PRO   A CG   1 
ATOM   1925  C  CD   . PRO   A  1  124 ? 4.940   -34.215 -28.456  1.00 51.36  ? 124  PRO   A CD   1 
ATOM   1926  H  HA   . PRO   A  1  124 ? 4.953   -31.719 -30.395  1.00 56.70  ? 124  PRO   A HA   1 
ATOM   1927  H  HB2  . PRO   A  1  124 ? 6.510   -31.410 -28.386  1.00 59.97  ? 124  PRO   A HB2  1 
ATOM   1928  H  HB3  . PRO   A  1  124 ? 4.936   -31.455 -28.171  1.00 59.97  ? 124  PRO   A HB3  1 
ATOM   1929  H  HG2  . PRO   A  1  124 ? 6.769   -33.542 -27.789  1.00 58.99  ? 124  PRO   A HG2  1 
ATOM   1930  H  HG3  . PRO   A  1  124 ? 5.575   -33.125 -26.828  1.00 58.99  ? 124  PRO   A HG3  1 
ATOM   1931  H  HD2  . PRO   A  1  124 ? 5.337   -35.100 -28.480  1.00 61.62  ? 124  PRO   A HD2  1 
ATOM   1932  H  HD3  . PRO   A  1  124 ? 4.072   -34.252 -28.024  1.00 61.62  ? 124  PRO   A HD3  1 
ATOM   1933  N  N    . VAL   A  1  125 ? 6.743   -32.676 -32.015  1.00 43.91  ? 125  VAL   A N    1 
ATOM   1934  C  CA   . VAL   A  1  125 ? 7.938   -32.714 -32.845  1.00 48.82  ? 125  VAL   A CA   1 
ATOM   1935  C  C    . VAL   A  1  125 ? 8.554   -31.331 -32.998  1.00 49.02  ? 125  VAL   A C    1 
ATOM   1936  O  O    . VAL   A  1  125 ? 9.736   -31.217 -33.346  1.00 50.10  ? 125  VAL   A O    1 
ATOM   1937  C  CB   . VAL   A  1  125 ? 7.620   -33.310 -34.231  1.00 55.55  ? 125  VAL   A CB   1 
ATOM   1938  C  CG1  . VAL   A  1  125 ? 7.104   -34.735 -34.092  1.00 61.14  ? 125  VAL   A CG1  1 
ATOM   1939  C  CG2  . VAL   A  1  125 ? 6.613   -32.439 -34.976  1.00 53.17  ? 125  VAL   A CG2  1 
ATOM   1940  H  H    . VAL   A  1  125 ? 6.004   -32.787 -32.441  1.00 52.68  ? 125  VAL   A H    1 
ATOM   1941  H  HA   . VAL   A  1  125 ? 8.585   -33.290 -32.410  1.00 58.56  ? 125  VAL   A HA   1 
ATOM   1942  H  HB   . VAL   A  1  125 ? 8.436   -33.334 -34.755  1.00 66.64  ? 125  VAL   A HB   1 
ATOM   1943  H  HG11 . VAL   A  1  125 ? 6.925   -35.093 -34.975  1.00 73.35  ? 125  VAL   A HG11 1 
ATOM   1944  H  HG12 . VAL   A  1  125 ? 7.778   -35.272 -33.647  1.00 73.35  ? 125  VAL   A HG12 1 
ATOM   1945  H  HG13 . VAL   A  1  125 ? 6.288   -34.726 -33.567  1.00 73.35  ? 125  VAL   A HG13 1 
ATOM   1946  H  HG21 . VAL   A  1  125 ? 6.414   -32.849 -35.832  1.00 63.78  ? 125  VAL   A HG21 1 
ATOM   1947  H  HG22 . VAL   A  1  125 ? 5.803   -32.369 -34.446  1.00 63.78  ? 125  VAL   A HG22 1 
ATOM   1948  H  HG23 . VAL   A  1  125 ? 6.997   -31.559 -35.111  1.00 63.78  ? 125  VAL   A HG23 1 
ATOM   1949  N  N    . GLY   A  1  126 ? 7.786   -30.274 -32.745  1.00 48.79  ? 126  GLY   A N    1 
ATOM   1950  C  CA   . GLY   A  1  126 ? 8.267   -28.923 -32.947  1.00 52.28  ? 126  GLY   A CA   1 
ATOM   1951  C  C    . GLY   A  1  126 ? 8.351   -28.563 -34.415  1.00 55.68  ? 126  GLY   A C    1 
ATOM   1952  O  O    . GLY   A  1  126 ? 8.453   -29.446 -35.271  1.00 60.25  ? 126  GLY   A O    1 
ATOM   1953  H  H    . GLY   A  1  126 ? 6.978   -30.319 -32.453  1.00 58.52  ? 126  GLY   A H    1 
ATOM   1954  H  HA2  . GLY   A  1  126 ? 7.667   -28.299 -32.511  1.00 62.71  ? 126  GLY   A HA2  1 
ATOM   1955  H  HA3  . GLY   A  1  126 ? 9.152   -28.835 -32.558  1.00 62.71  ? 126  GLY   A HA3  1 
ATOM   1956  N  N    . THR   A  1  127 ? 8.300   -27.269 -34.721  1.00 56.65  ? 127  THR   A N    1 
ATOM   1957  C  CA   . THR   A  1  127 ? 8.420   -26.809 -36.096  1.00 54.37  ? 127  THR   A CA   1 
ATOM   1958  C  C    . THR   A  1  127 ? 9.104   -25.451 -36.104  1.00 53.08  ? 127  THR   A C    1 
ATOM   1959  O  O    . THR   A  1  127 ? 9.158   -24.754 -35.088  1.00 51.72  ? 127  THR   A O    1 
ATOM   1960  C  CB   . THR   A  1  127 ? 7.053   -26.724 -36.791  1.00 54.79  ? 127  THR   A CB   1 
ATOM   1961  O  OG1  . THR   A  1  127 ? 7.240   -26.488 -38.192  1.00 56.23  ? 127  THR   A OG1  1 
ATOM   1962  C  CG2  . THR   A  1  127 ? 6.205   -25.601 -36.198  1.00 52.75  ? 127  THR   A CG2  1 
ATOM   1963  H  H    . THR   A  1  127 ? 8.196   -26.638 -34.147  1.00 67.97  ? 127  THR   A H    1 
ATOM   1964  H  HA   . THR   A  1  127 ? 8.971   -27.433 -36.593  1.00 65.23  ? 127  THR   A HA   1 
ATOM   1965  H  HB   . THR   A  1  127 ? 6.578   -27.560 -36.661  1.00 65.73  ? 127  THR   A HB   1 
ATOM   1966  H  HG1  . THR   A  1  127 ? 6.500   -26.518 -38.590  1.00 67.46  ? 127  THR   A HG1  1 
ATOM   1967  H  HG21 . THR   A  1  127 ? 5.306   -25.636 -36.562  1.00 63.28  ? 127  THR   A HG21 1 
ATOM   1968  H  HG22 . THR   A  1  127 ? 6.157   -25.695 -35.233  1.00 63.28  ? 127  THR   A HG22 1 
ATOM   1969  H  HG23 . THR   A  1  127 ? 6.598   -24.741 -36.411  1.00 63.28  ? 127  THR   A HG23 1 
ATOM   1970  N  N    . CYS   A  1  128 ? 9.630   -25.086 -37.269  1.00 53.03  ? 128  CYS   A N    1 
ATOM   1971  C  CA   . CYS   A  1  128 ? 10.276  -23.797 -37.452  1.00 51.82  ? 128  CYS   A CA   1 
ATOM   1972  C  C    . CYS   A  1  128 ? 9.803   -23.187 -38.763  1.00 52.25  ? 128  CYS   A C    1 
ATOM   1973  O  O    . CYS   A  1  128 ? 9.269   -23.875 -39.638  1.00 53.52  ? 128  CYS   A O    1 
ATOM   1974  C  CB   . CYS   A  1  128 ? 11.808  -23.915 -37.458  1.00 51.12  ? 128  CYS   A CB   1 
ATOM   1975  S  SG   . CYS   A  1  128 ? 12.556  -24.640 -35.974  1.00 59.24  ? 128  CYS   A SG   1 
ATOM   1976  H  H    . CYS   A  1  128 ? 9.625   -25.575 -37.976  1.00 63.61  ? 128  CYS   A H    1 
ATOM   1977  H  HA   . CYS   A  1  128 ? 10.020  -23.209 -36.724  1.00 62.17  ? 128  CYS   A HA   1 
ATOM   1978  H  HB2  . CYS   A  1  128 ? 12.066  -24.471 -38.210  1.00 61.32  ? 128  CYS   A HB2  1 
ATOM   1979  H  HB3  . CYS   A  1  128 ? 12.180  -23.025 -37.561  1.00 61.32  ? 128  CYS   A HB3  1 
ATOM   1980  N  N    . PHE   A  1  129 ? 10.001  -21.877 -38.884  1.00 53.95  ? 129  PHE   A N    1 
ATOM   1981  C  CA   . PHE   A  1  129 ? 9.727   -21.148 -40.114  1.00 53.87  ? 129  PHE   A CA   1 
ATOM   1982  C  C    . PHE   A  1  129 ? 10.955  -20.331 -40.476  1.00 57.16  ? 129  PHE   A C    1 
ATOM   1983  O  O    . PHE   A  1  129 ? 11.534  -19.658 -39.617  1.00 57.41  ? 129  PHE   A O    1 
ATOM   1984  C  CB   . PHE   A  1  129 ? 8.501   -20.245 -39.966  1.00 52.59  ? 129  PHE   A CB   1 
ATOM   1985  C  CG   . PHE   A  1  129 ? 7.203   -20.996 -39.930  1.00 53.20  ? 129  PHE   A CG   1 
ATOM   1986  C  CD1  . PHE   A  1  129 ? 6.559   -21.344 -41.106  1.00 54.90  ? 129  PHE   A CD1  1 
ATOM   1987  C  CD2  . PHE   A  1  129 ? 6.631   -21.362 -38.724  1.00 52.99  ? 129  PHE   A CD2  1 
ATOM   1988  C  CE1  . PHE   A  1  129 ? 5.366   -22.040 -41.079  1.00 57.21  ? 129  PHE   A CE1  1 
ATOM   1989  C  CE2  . PHE   A  1  129 ? 5.439   -22.057 -38.689  1.00 52.22  ? 129  PHE   A CE2  1 
ATOM   1990  C  CZ   . PHE   A  1  129 ? 4.805   -22.397 -39.868  1.00 54.97  ? 129  PHE   A CZ   1 
ATOM   1991  H  H    . PHE   A  1  129 ? 10.300  -21.379 -38.251  1.00 64.72  ? 129  PHE   A H    1 
ATOM   1992  H  HA   . PHE   A  1  129 ? 9.549   -21.772 -40.835  1.00 64.62  ? 129  PHE   A HA   1 
ATOM   1993  H  HB2  . PHE   A  1  129 ? 8.578   -19.746 -39.138  1.00 63.09  ? 129  PHE   A HB2  1 
ATOM   1994  H  HB3  . PHE   A  1  129 ? 8.470   -19.634 -40.720  1.00 63.09  ? 129  PHE   A HB3  1 
ATOM   1995  H  HD1  . PHE   A  1  129 ? 6.935   -21.107 -41.923  1.00 65.86  ? 129  PHE   A HD1  1 
ATOM   1996  H  HD2  . PHE   A  1  129 ? 7.054   -21.136 -37.927  1.00 63.57  ? 129  PHE   A HD2  1 
ATOM   1997  H  HE1  . PHE   A  1  129 ? 4.941   -22.268 -41.874  1.00 68.64  ? 129  PHE   A HE1  1 
ATOM   1998  H  HE2  . PHE   A  1  129 ? 5.063   -22.296 -37.873  1.00 62.65  ? 129  PHE   A HE2  1 
ATOM   1999  H  HZ   . PHE   A  1  129 ? 4.001   -22.865 -39.846  1.00 65.95  ? 129  PHE   A HZ   1 
ATOM   2000  N  N    . LEU   A  1  130 ? 11.355  -20.404 -41.742  1.00 59.39  ? 130  LEU   A N    1 
ATOM   2001  C  CA   . LEU   A  1  130 ? 12.518  -19.691 -42.254  1.00 59.89  ? 130  LEU   A CA   1 
ATOM   2002  C  C    . LEU   A  1  130 ? 12.049  -18.718 -43.323  1.00 60.01  ? 130  LEU   A C    1 
ATOM   2003  O  O    . LEU   A  1  130 ? 11.483  -19.134 -44.340  1.00 61.11  ? 130  LEU   A O    1 
ATOM   2004  C  CB   . LEU   A  1  130 ? 13.551  -20.665 -42.823  1.00 60.16  ? 130  LEU   A CB   1 
ATOM   2005  C  CG   . LEU   A  1  130 ? 14.790  -20.037 -43.463  1.00 61.95  ? 130  LEU   A CG   1 
ATOM   2006  C  CD1  . LEU   A  1  130 ? 15.611  -19.287 -42.427  1.00 60.21  ? 130  LEU   A CD1  1 
ATOM   2007  C  CD2  . LEU   A  1  130 ? 15.630  -21.100 -44.152  1.00 66.15  ? 130  LEU   A CD2  1 
ATOM   2008  H  H    . LEU   A  1  130 ? 10.956  -20.875 -42.340  1.00 71.25  ? 130  LEU   A H    1 
ATOM   2009  H  HA   . LEU   A  1  130 ? 12.937  -19.188 -41.539  1.00 71.85  ? 130  LEU   A HA   1 
ATOM   2010  H  HB2  . LEU   A  1  130 ? 13.859  -21.234 -42.100  1.00 72.17  ? 130  LEU   A HB2  1 
ATOM   2011  H  HB3  . LEU   A  1  130 ? 13.116  -21.201 -43.505  1.00 72.17  ? 130  LEU   A HB3  1 
ATOM   2012  H  HG   . LEU   A  1  130 ? 14.507  -19.396 -44.134  1.00 74.32  ? 130  LEU   A HG   1 
ATOM   2013  H  HD11 . LEU   A  1  130 ? 16.408  -18.932 -42.852  1.00 72.23  ? 130  LEU   A HD11 1 
ATOM   2014  H  HD12 . LEU   A  1  130 ? 15.078  -18.562 -42.066  1.00 72.23  ? 130  LEU   A HD12 1 
ATOM   2015  H  HD13 . LEU   A  1  130 ? 15.860  -19.900 -41.718  1.00 72.23  ? 130  LEU   A HD13 1 
ATOM   2016  H  HD21 . LEU   A  1  130 ? 16.405  -20.678 -44.555  1.00 79.36  ? 130  LEU   A HD21 1 
ATOM   2017  H  HD22 . LEU   A  1  130 ? 15.914  -21.754 -43.494  1.00 79.36  ? 130  LEU   A HD22 1 
ATOM   2018  H  HD23 . LEU   A  1  130 ? 15.094  -21.531 -44.836  1.00 79.36  ? 130  LEU   A HD23 1 
ATOM   2019  N  N    . GLN   A  1  131 ? 12.278  -17.429 -43.089  1.00 56.68  ? 131  GLN   A N    1 
ATOM   2020  C  CA   . GLN   A  1  131 ? 11.901  -16.369 -44.016  1.00 62.45  ? 131  GLN   A CA   1 
ATOM   2021  C  C    . GLN   A  1  131 ? 13.166  -15.694 -44.518  1.00 67.18  ? 131  GLN   A C    1 
ATOM   2022  O  O    . GLN   A  1  131 ? 13.936  -15.144 -43.723  1.00 66.80  ? 131  GLN   A O    1 
ATOM   2023  C  CB   . GLN   A  1  131 ? 10.979  -15.353 -43.336  1.00 65.57  ? 131  GLN   A CB   1 
ATOM   2024  C  CG   . GLN   A  1  131 ? 10.657  -14.130 -44.182  1.00 72.71  ? 131  GLN   A CG   1 
ATOM   2025  C  CD   . GLN   A  1  131 ? 9.626   -13.231 -43.528  1.00 79.91  ? 131  GLN   A CD   1 
ATOM   2026  O  OE1  . GLN   A  1  131 ? 9.873   -12.046 -43.299  1.00 81.82  ? 131  GLN   A OE1  1 
ATOM   2027  N  NE2  . GLN   A  1  131 ? 8.460   -13.790 -43.226  1.00 82.66  ? 131  GLN   A NE2  1 
ATOM   2028  H  H    . GLN   A  1  131 ? 12.664  -17.136 -42.378  1.00 67.99  ? 131  GLN   A H    1 
ATOM   2029  H  HA   . GLN   A  1  131 ? 11.432  -16.748 -44.775  1.00 74.92  ? 131  GLN   A HA   1 
ATOM   2030  H  HB2  . GLN   A  1  131 ? 10.140  -15.791 -43.124  1.00 78.67  ? 131  GLN   A HB2  1 
ATOM   2031  H  HB3  . GLN   A  1  131 ? 11.407  -15.043 -42.523  1.00 78.67  ? 131  GLN   A HB3  1 
ATOM   2032  H  HG2  . GLN   A  1  131 ? 11.467  -13.613 -44.314  1.00 87.24  ? 131  GLN   A HG2  1 
ATOM   2033  H  HG3  . GLN   A  1  131 ? 10.305  -14.419 -45.038  1.00 87.24  ? 131  GLN   A HG3  1 
ATOM   2034  H  HE21 . GLN   A  1  131 ? 8.323   -14.621 -43.403  1.00 99.18  ? 131  GLN   A HE21 1 
ATOM   2035  H  HE22 . GLN   A  1  131 ? 7.842   -13.323 -42.854  1.00 99.18  ? 131  GLN   A HE22 1 
ATOM   2036  N  N    . ASP   A  1  132 ? 13.394  -15.749 -45.830  1.00 74.60  ? 132  ASP   A N    1 
ATOM   2037  C  CA   . ASP   A  1  132 ? 14.548  -15.080 -46.417  1.00 83.45  ? 132  ASP   A CA   1 
ATOM   2038  C  C    . ASP   A  1  132 ? 14.170  -13.702 -46.940  1.00 90.34  ? 132  ASP   A C    1 
ATOM   2039  O  O    . ASP   A  1  132 ? 14.646  -12.682 -46.432  1.00 98.50  ? 132  ASP   A O    1 
ATOM   2040  C  CB   . ASP   A  1  132 ? 15.134  -15.939 -47.544  1.00 88.03  ? 132  ASP   A CB   1 
ATOM   2041  C  CG   . ASP   A  1  132 ? 16.484  -15.437 -48.020  1.00 95.79  ? 132  ASP   A CG   1 
ATOM   2042  O  OD1  . ASP   A  1  132 ? 16.632  -14.214 -48.226  1.00 99.76  ? 132  ASP   A OD1  1 
ATOM   2043  O  OD2  . ASP   A  1  132 ? 17.400  -16.269 -48.185  1.00 98.14  ? 132  ASP   A OD2  1 
ATOM   2044  H  H    . ASP   A  1  132 ? 12.897  -16.165 -46.395  1.00 89.50  ? 132  ASP   A H    1 
ATOM   2045  H  HA   . ASP   A  1  132 ? 15.235  -14.975 -45.739  1.00 100.12 ? 132  ASP   A HA   1 
ATOM   2046  H  HB2  . ASP   A  1  132 ? 15.248  -16.847 -47.224  1.00 105.62 ? 132  ASP   A HB2  1 
ATOM   2047  H  HB3  . ASP   A  1  132 ? 14.526  -15.927 -48.299  1.00 105.62 ? 132  ASP   A HB3  1 
ATOM   2048  N  N    . GLY   A  1  133 ? 13.305  -13.663 -47.951  1.00 88.26  ? 133  GLY   A N    1 
ATOM   2049  C  CA   . GLY   A  1  133 ? 12.733  -12.430 -48.448  1.00 92.55  ? 133  GLY   A CA   1 
ATOM   2050  C  C    . GLY   A  1  133 ? 11.223  -12.503 -48.408  1.00 97.59  ? 133  GLY   A C    1 
ATOM   2051  O  O    . GLY   A  1  133 ? 10.618  -12.556 -47.333  1.00 97.31  ? 133  GLY   A O    1 
ATOM   2052  H  H    . GLY   A  1  133 ? 13.030  -14.360 -48.373  1.00 105.89 ? 133  GLY   A H    1 
ATOM   2053  H  HA2  . GLY   A  1  133 ? 13.028  -11.686 -47.900  1.00 111.04 ? 133  GLY   A HA2  1 
ATOM   2054  H  HA3  . GLY   A  1  133 ? 13.017  -12.281 -49.363  1.00 111.04 ? 133  GLY   A HA3  1 
ATOM   2055  N  N    . THR   A  1  134 ? 10.604  -12.502 -49.589  1.00 102.62 ? 134  THR   A N    1 
ATOM   2056  C  CA   . THR   A  1  134 ? 9.217   -12.937 -49.687  1.00 102.50 ? 134  THR   A CA   1 
ATOM   2057  C  C    . THR   A  1  134 ? 9.094   -14.424 -49.384  1.00 97.22  ? 134  THR   A C    1 
ATOM   2058  O  O    . THR   A  1  134 ? 8.045   -14.880 -48.913  1.00 97.09  ? 134  THR   A O    1 
ATOM   2059  C  CB   . THR   A  1  134 ? 8.670   -12.644 -51.084  1.00 104.04 ? 134  THR   A CB   1 
ATOM   2060  O  OG1  . THR   A  1  134 ? 9.425   -13.379 -52.055  1.00 108.28 ? 134  THR   A OG1  1 
ATOM   2061  C  CG2  . THR   A  1  134 ? 8.758   -11.154 -51.394  1.00 100.21 ? 134  THR   A CG2  1 
ATOM   2062  H  H    . THR   A  1  134 ? 10.959  -12.258 -50.333  1.00 123.13 ? 134  THR   A H    1 
ATOM   2063  H  HA   . THR   A  1  134 ? 8.683   -12.441 -49.047  1.00 122.98 ? 134  THR   A HA   1 
ATOM   2064  H  HB   . THR   A  1  134 ? 7.738   -12.908 -51.130  1.00 124.83 ? 134  THR   A HB   1 
ATOM   2065  H  HG1  . THR   A  1  134 ? 9.135   -13.218 -52.827  1.00 129.91 ? 134  THR   A HG1  1 
ATOM   2066  H  HG21 . THR   A  1  134 ? 8.396   -10.977 -52.276  1.00 120.23 ? 134  THR   A HG21 1 
ATOM   2067  H  HG22 . THR   A  1  134 ? 8.252   -10.649 -50.739  1.00 120.23 ? 134  THR   A HG22 1 
ATOM   2068  H  HG23 . THR   A  1  134 ? 9.683   -10.864 -51.369  1.00 120.23 ? 134  THR   A HG23 1 
ATOM   2069  N  N    . LYS   A  1  135 ? 10.156  -15.186 -49.638  1.00 90.80  ? 135  LYS   A N    1 
ATOM   2070  C  CA   . LYS   A  1  135 ? 10.128  -16.629 -49.440  1.00 81.61  ? 135  LYS   A CA   1 
ATOM   2071  C  C    . LYS   A  1  135 ? 10.063  -16.971 -47.957  1.00 73.10  ? 135  LYS   A C    1 
ATOM   2072  O  O    . LYS   A  1  135 ? 10.878  -16.496 -47.160  1.00 73.31  ? 135  LYS   A O    1 
ATOM   2073  C  CB   . LYS   A  1  135 ? 11.367  -17.267 -50.069  1.00 80.51  ? 135  LYS   A CB   1 
ATOM   2074  C  CG   . LYS   A  1  135 ? 11.103  -18.045 -51.349  1.00 82.01  ? 135  LYS   A CG   1 
ATOM   2075  C  CD   . LYS   A  1  135 ? 10.571  -19.440 -51.055  1.00 80.59  ? 135  LYS   A CD   1 
ATOM   2076  C  CE   . LYS   A  1  135 ? 10.651  -20.335 -52.282  1.00 82.27  ? 135  LYS   A CE   1 
ATOM   2077  N  NZ   . LYS   A  1  135 ? 10.383  -21.763 -51.952  1.00 82.82  ? 135  LYS   A NZ   1 
ATOM   2078  H  H    . LYS   A  1  135 ? 10.909  -14.889 -49.929  1.00 108.95 ? 135  LYS   A H    1 
ATOM   2079  H  HA   . LYS   A  1  135 ? 9.337   -16.992 -49.868  1.00 97.91  ? 135  LYS   A HA   1 
ATOM   2080  H  HB2  . LYS   A  1  135 ? 12.001  -16.564 -50.281  1.00 96.59  ? 135  LYS   A HB2  1 
ATOM   2081  H  HB3  . LYS   A  1  135 ? 11.755  -17.883 -49.428  1.00 96.59  ? 135  LYS   A HB3  1 
ATOM   2082  H  HG2  . LYS   A  1  135 ? 10.444  -17.573 -51.882  1.00 98.39  ? 135  LYS   A HG2  1 
ATOM   2083  H  HG3  . LYS   A  1  135 ? 11.930  -18.133 -51.848  1.00 98.39  ? 135  LYS   A HG3  1 
ATOM   2084  H  HD2  . LYS   A  1  135 ? 11.099  -19.843 -50.348  1.00 96.68  ? 135  LYS   A HD2  1 
ATOM   2085  H  HD3  . LYS   A  1  135 ? 9.642   -19.379 -50.781  1.00 96.68  ? 135  LYS   A HD3  1 
ATOM   2086  H  HE2  . LYS   A  1  135 ? 9.991   -20.046 -52.932  1.00 98.70  ? 135  LYS   A HE2  1 
ATOM   2087  H  HE3  . LYS   A  1  135 ? 11.540  -20.274 -52.664  1.00 98.70  ? 135  LYS   A HE3  1 
ATOM   2088  H  HZ1  . LYS   A  1  135 ? 10.459  -22.264 -52.683  1.00 99.36  ? 135  LYS   A HZ1  1 
ATOM   2089  H  HZ2  . LYS   A  1  135 ? 10.966  -22.049 -51.343  1.00 99.36  ? 135  LYS   A HZ2  1 
ATOM   2090  H  HZ3  . LYS   A  1  135 ? 9.560   -21.850 -51.626  1.00 99.36  ? 135  LYS   A HZ3  1 
ATOM   2091  N  N    . THR   A  1  136 ? 9.088   -17.800 -47.592  1.00 67.77  ? 136  THR   A N    1 
ATOM   2092  C  CA   . THR   A  1  136 ? 8.977   -18.358 -46.251  1.00 64.80  ? 136  THR   A CA   1 
ATOM   2093  C  C    . THR   A  1  136 ? 8.662   -19.840 -46.385  1.00 59.62  ? 136  THR   A C    1 
ATOM   2094  O  O    . THR   A  1  136 ? 7.760   -20.217 -47.139  1.00 61.51  ? 136  THR   A O    1 
ATOM   2095  C  CB   . THR   A  1  136 ? 7.888   -17.652 -45.436  1.00 67.10  ? 136  THR   A CB   1 
ATOM   2096  O  OG1  . THR   A  1  136 ? 8.198   -16.256 -45.333  1.00 69.69  ? 136  THR   A OG1  1 
ATOM   2097  C  CG2  . THR   A  1  136 ? 7.785   -18.249 -44.037  1.00 65.93  ? 136  THR   A CG2  1 
ATOM   2098  H  H    . THR   A  1  136 ? 8.461   -18.061 -48.121  1.00 81.31  ? 136  THR   A H    1 
ATOM   2099  H  HA   . THR   A  1  136 ? 9.815   -18.254 -45.775  1.00 77.74  ? 136  THR   A HA   1 
ATOM   2100  H  HB   . THR   A  1  136 ? 7.032   -17.765 -45.877  1.00 80.50  ? 136  THR   A HB   1 
ATOM   2101  H  HG1  . THR   A  1  136 ? 7.564   -15.848 -44.963  1.00 83.61  ? 136  THR   A HG1  1 
ATOM   2102  H  HG21 . THR   A  1  136 ? 7.134   -17.756 -43.513  1.00 79.10  ? 136  THR   A HG21 1 
ATOM   2103  H  HG22 . THR   A  1  136 ? 7.508   -19.177 -44.091  1.00 79.10  ? 136  THR   A HG22 1 
ATOM   2104  H  HG23 . THR   A  1  136 ? 8.646   -18.203 -43.592  1.00 79.10  ? 136  THR   A HG23 1 
ATOM   2105  N  N    . VAL   A  1  137 ? 9.407   -20.676 -45.665  1.00 55.68  ? 137  VAL   A N    1 
ATOM   2106  C  CA   . VAL   A  1  137 ? 9.234   -22.120 -45.725  1.00 56.63  ? 137  VAL   A CA   1 
ATOM   2107  C  C    . VAL   A  1  137 ? 9.206   -22.677 -44.310  1.00 57.64  ? 137  VAL   A C    1 
ATOM   2108  O  O    . VAL   A  1  137 ? 9.828   -22.132 -43.393  1.00 60.47  ? 137  VAL   A O    1 
ATOM   2109  C  CB   . VAL   A  1  137 ? 10.350  -22.807 -46.548  1.00 55.56  ? 137  VAL   A CB   1 
ATOM   2110  C  CG1  . VAL   A  1  137 ? 10.387  -22.255 -47.964  1.00 56.01  ? 137  VAL   A CG1  1 
ATOM   2111  C  CG2  . VAL   A  1  137 ? 11.707  -22.645 -45.865  1.00 52.68  ? 137  VAL   A CG2  1 
ATOM   2112  H  H    . VAL   A  1  137 ? 10.029  -20.423 -45.126  1.00 66.80  ? 137  VAL   A H    1 
ATOM   2113  H  HA   . VAL   A  1  137 ? 8.382   -22.313 -46.145  1.00 67.94  ? 137  VAL   A HA   1 
ATOM   2114  H  HB   . VAL   A  1  137 ? 10.158  -23.756 -46.600  1.00 66.65  ? 137  VAL   A HB   1 
ATOM   2115  H  HG11 . VAL   A  1  137 ? 11.093  -22.699 -48.458  1.00 67.19  ? 137  VAL   A HG11 1 
ATOM   2116  H  HG12 . VAL   A  1  137 ? 9.531   -22.421 -48.390  1.00 67.19  ? 137  VAL   A HG12 1 
ATOM   2117  H  HG13 . VAL   A  1  137 ? 10.558  -21.301 -47.927  1.00 67.19  ? 137  VAL   A HG13 1 
ATOM   2118  H  HG21 . VAL   A  1  137 ? 12.395  -23.018 -46.438  1.00 63.19  ? 137  VAL   A HG21 1 
ATOM   2119  H  HG22 . VAL   A  1  137 ? 11.876  -21.701 -45.717  1.00 63.19  ? 137  VAL   A HG22 1 
ATOM   2120  H  HG23 . VAL   A  1  137 ? 11.692  -23.115 -45.017  1.00 63.19  ? 137  VAL   A HG23 1 
ATOM   2121  N  N    . GLU   A  1  138 ? 8.479   -23.778 -44.139  1.00 55.84  ? 138  GLU   A N    1 
ATOM   2122  C  CA   . GLU   A  1  138 ? 8.450   -24.492 -42.872  1.00 56.75  ? 138  GLU   A CA   1 
ATOM   2123  C  C    . GLU   A  1  138 ? 9.623   -25.461 -42.807  1.00 54.94  ? 138  GLU   A C    1 
ATOM   2124  O  O    . GLU   A  1  138 ? 9.968   -26.105 -43.802  1.00 57.05  ? 138  GLU   A O    1 
ATOM   2125  C  CB   . GLU   A  1  138 ? 7.133   -25.250 -42.700  1.00 55.85  ? 138  GLU   A CB   1 
ATOM   2126  C  CG   . GLU   A  1  138 ? 6.937   -25.821 -41.302  1.00 53.92  ? 138  GLU   A CG   1 
ATOM   2127  C  CD   . GLU   A  1  138 ? 5.616   -26.553 -41.143  1.00 53.44  ? 138  GLU   A CD   1 
ATOM   2128  O  OE1  . GLU   A  1  138 ? 5.001   -26.906 -42.171  1.00 54.18  ? 138  GLU   A OE1  1 
ATOM   2129  O  OE2  . GLU   A  1  138 ? 5.192   -26.774 -39.989  1.00 52.45  ? 138  GLU   A OE2  1 
ATOM   2130  H  H    . GLU   A  1  138 ? 7.990   -24.133 -44.751  1.00 66.99  ? 138  GLU   A H    1 
ATOM   2131  H  HA   . GLU   A  1  138 ? 8.523   -23.859 -42.140  1.00 68.07  ? 138  GLU   A HA   1 
ATOM   2132  H  HB2  . GLU   A  1  138 ? 6.397   -24.643 -42.878  1.00 67.00  ? 138  GLU   A HB2  1 
ATOM   2133  H  HB3  . GLU   A  1  138 ? 7.113   -25.988 -43.328  1.00 67.00  ? 138  GLU   A HB3  1 
ATOM   2134  H  HG2  . GLU   A  1  138 ? 7.652   -26.450 -41.115  1.00 64.69  ? 138  GLU   A HG2  1 
ATOM   2135  H  HG3  . GLU   A  1  138 ? 6.956   -25.095 -40.659  1.00 64.69  ? 138  GLU   A HG3  1 
ATOM   2136  N  N    . TYR   A  1  139 ? 10.234  -25.556 -41.628  1.00 51.91  ? 139  TYR   A N    1 
ATOM   2137  C  CA   . TYR   A  1  139 ? 11.388  -26.424 -41.399  1.00 52.09  ? 139  TYR   A CA   1 
ATOM   2138  C  C    . TYR   A  1  139 ? 11.139  -27.197 -40.108  1.00 51.92  ? 139  TYR   A C    1 
ATOM   2139  O  O    . TYR   A  1  139 ? 11.393  -26.688 -39.012  1.00 48.16  ? 139  TYR   A O    1 
ATOM   2140  C  CB   . TYR   A  1  139 ? 12.681  -25.615 -41.329  1.00 53.00  ? 139  TYR   A CB   1 
ATOM   2141  C  CG   . TYR   A  1  139 ? 13.904  -26.435 -40.977  1.00 57.68  ? 139  TYR   A CG   1 
ATOM   2142  C  CD1  . TYR   A  1  139 ? 14.307  -27.498 -41.776  1.00 60.30  ? 139  TYR   A CD1  1 
ATOM   2143  C  CD2  . TYR   A  1  139 ? 14.659  -26.142 -39.849  1.00 60.51  ? 139  TYR   A CD2  1 
ATOM   2144  C  CE1  . TYR   A  1  139 ? 15.423  -28.249 -41.457  1.00 61.45  ? 139  TYR   A CE1  1 
ATOM   2145  C  CE2  . TYR   A  1  139 ? 15.776  -26.886 -39.524  1.00 61.48  ? 139  TYR   A CE2  1 
ATOM   2146  C  CZ   . TYR   A  1  139 ? 16.154  -27.937 -40.331  1.00 59.96  ? 139  TYR   A CZ   1 
ATOM   2147  O  OH   . TYR   A  1  139 ? 17.265  -28.680 -40.007  1.00 57.72  ? 139  TYR   A OH   1 
ATOM   2148  H  H    . TYR   A  1  139 ? 9.992   -25.118 -40.929  1.00 62.28  ? 139  TYR   A H    1 
ATOM   2149  H  HA   . TYR   A  1  139 ? 11.467  -27.060 -42.127  1.00 62.49  ? 139  TYR   A HA   1 
ATOM   2150  H  HB2  . TYR   A  1  139 ? 12.839  -25.206 -42.195  1.00 63.59  ? 139  TYR   A HB2  1 
ATOM   2151  H  HB3  . TYR   A  1  139 ? 12.582  -24.928 -40.651  1.00 63.59  ? 139  TYR   A HB3  1 
ATOM   2152  H  HD1  . TYR   A  1  139 ? 13.818  -27.707 -42.539  1.00 72.34  ? 139  TYR   A HD1  1 
ATOM   2153  H  HD2  . TYR   A  1  139 ? 14.408  -25.432 -39.303  1.00 72.59  ? 139  TYR   A HD2  1 
ATOM   2154  H  HE1  . TYR   A  1  139 ? 15.678  -28.961 -41.998  1.00 73.72  ? 139  TYR   A HE1  1 
ATOM   2155  H  HE2  . TYR   A  1  139 ? 16.271  -26.678 -38.764  1.00 73.75  ? 139  TYR   A HE2  1 
ATOM   2156  H  HH   . TYR   A  1  139 ? 17.329  -29.341 -40.521  1.00 69.25  ? 139  TYR   A HH   1 
ATOM   2157  N  N    . ALA   A  1  140 ? 10.634  -28.425 -40.242  1.00 54.69  ? 140  ALA   A N    1 
ATOM   2158  C  CA   . ALA   A  1  140 ? 10.353  -29.314 -39.117  1.00 52.75  ? 140  ALA   A CA   1 
ATOM   2159  C  C    . ALA   A  1  140 ? 11.177  -30.581 -39.320  1.00 50.84  ? 140  ALA   A C    1 
ATOM   2160  O  O    . ALA   A  1  140 ? 10.641  -31.628 -39.713  1.00 48.53  ? 140  ALA   A O    1 
ATOM   2161  C  CB   . ALA   A  1  140 ? 8.861   -29.625 -39.010  1.00 53.45  ? 140  ALA   A CB   1 
ATOM   2162  H  H    . ALA   A  1  140 ? 10.439  -28.775 -41.003  1.00 65.61  ? 140  ALA   A H    1 
ATOM   2163  H  HA   . ALA   A  1  140 ? 10.628  -28.895 -38.287  1.00 63.28  ? 140  ALA   A HA   1 
ATOM   2164  H  HB1  . ALA   A  1  140 ? 8.713   -30.206 -38.248  1.00 64.13  ? 140  ALA   A HB1  1 
ATOM   2165  H  HB2  . ALA   A  1  140 ? 8.373   -28.795 -38.893  1.00 64.13  ? 140  ALA   A HB2  1 
ATOM   2166  H  HB3  . ALA   A  1  140 ? 8.571   -30.066 -39.824  1.00 64.13  ? 140  ALA   A HB3  1 
ATOM   2167  N  N    . PRO   A  1  141 ? 12.487  -30.525 -39.067  1.00 51.64  ? 141  PRO   A N    1 
ATOM   2168  C  CA   . PRO   A  1  141 ? 13.329  -31.707 -39.311  1.00 52.46  ? 141  PRO   A CA   1 
ATOM   2169  C  C    . PRO   A  1  141 ? 12.963  -32.897 -38.448  1.00 52.56  ? 141  PRO   A C    1 
ATOM   2170  O  O    . PRO   A  1  141 ? 13.249  -34.036 -38.838  1.00 53.81  ? 141  PRO   A O    1 
ATOM   2171  C  CB   . PRO   A  1  141 ? 14.745  -31.202 -39.000  1.00 50.67  ? 141  PRO   A CB   1 
ATOM   2172  C  CG   . PRO   A  1  141 ? 14.540  -30.063 -38.057  1.00 49.90  ? 141  PRO   A CG   1 
ATOM   2173  C  CD   . PRO   A  1  141 ? 13.254  -29.411 -38.481  1.00 51.72  ? 141  PRO   A CD   1 
ATOM   2174  H  HA   . PRO   A  1  141 ? 13.281  -31.963 -40.246  1.00 62.93  ? 141  PRO   A HA   1 
ATOM   2175  H  HB2  . PRO   A  1  141 ? 15.265  -31.908 -38.586  1.00 60.78  ? 141  PRO   A HB2  1 
ATOM   2176  H  HB3  . PRO   A  1  141 ? 15.178  -30.905 -39.816  1.00 60.78  ? 141  PRO   A HB3  1 
ATOM   2177  H  HG2  . PRO   A  1  141 ? 14.473  -30.397 -37.149  1.00 59.86  ? 141  PRO   A HG2  1 
ATOM   2178  H  HG3  . PRO   A  1  141 ? 15.281  -29.441 -38.128  1.00 59.86  ? 141  PRO   A HG3  1 
ATOM   2179  H  HD2  . PRO   A  1  141 ? 12.789  -29.035 -37.717  1.00 62.04  ? 141  PRO   A HD2  1 
ATOM   2180  H  HD3  . PRO   A  1  141 ? 13.418  -28.720 -39.142  1.00 62.04  ? 141  PRO   A HD3  1 
ATOM   2181  N  N    . CYS   A  1  142 ? 12.340  -32.677 -37.295  1.00 52.38  ? 142  CYS   A N    1 
ATOM   2182  C  CA   . CYS   A  1  142 ? 11.939  -33.763 -36.413  1.00 51.38  ? 142  CYS   A CA   1 
ATOM   2183  C  C    . CYS   A  1  142 ? 10.541  -34.287 -36.712  1.00 51.62  ? 142  CYS   A C    1 
ATOM   2184  O  O    . CYS   A  1  142 ? 10.119  -35.269 -36.092  1.00 52.71  ? 142  CYS   A O    1 
ATOM   2185  C  CB   . CYS   A  1  142 ? 12.021  -33.307 -34.955  1.00 52.09  ? 142  CYS   A CB   1 
ATOM   2186  S  SG   . CYS   A  1  142 ? 13.638  -33.591 -34.202  1.00 57.24  ? 142  CYS   A SG   1 
ATOM   2187  H  H    . CYS   A  1  142 ? 12.137  -31.896 -36.998  1.00 62.84  ? 142  CYS   A H    1 
ATOM   2188  H  HA   . CYS   A  1  142 ? 12.556  -34.502 -36.529  1.00 61.64  ? 142  CYS   A HA   1 
ATOM   2189  H  HB2  . CYS   A  1  142 ? 11.837  -32.355 -34.914  1.00 62.48  ? 142  CYS   A HB2  1 
ATOM   2190  H  HB3  . CYS   A  1  142 ? 11.361  -33.795 -34.437  1.00 62.48  ? 142  CYS   A HB3  1 
ATOM   2191  N  N    . ARG   A  1  143 ? 9.814   -33.663 -37.641  1.00 52.42  ? 143  ARG   A N    1 
ATOM   2192  C  CA   . ARG   A  1  143 ? 8.521   -34.176 -38.094  1.00 53.42  ? 143  ARG   A CA   1 
ATOM   2193  C  C    . ARG   A  1  143 ? 8.771   -35.242 -39.162  1.00 55.83  ? 143  ARG   A C    1 
ATOM   2194  O  O    . ARG   A  1  143 ? 8.454   -35.089 -40.344  1.00 53.93  ? 143  ARG   A O    1 
ATOM   2195  C  CB   . ARG   A  1  143 ? 7.646   -33.047 -38.616  1.00 52.53  ? 143  ARG   A CB   1 
ATOM   2196  C  CG   . ARG   A  1  143 ? 6.216   -33.459 -38.919  1.00 52.17  ? 143  ARG   A CG   1 
ATOM   2197  C  CD   . ARG   A  1  143 ? 5.359   -32.242 -39.216  1.00 48.75  ? 143  ARG   A CD   1 
ATOM   2198  N  NE   . ARG   A  1  143 ? 5.792   -31.550 -40.427  1.00 51.71  ? 143  ARG   A NE   1 
ATOM   2199  C  CZ   . ARG   A  1  143 ? 5.528   -30.275 -40.700  1.00 53.02  ? 143  ARG   A CZ   1 
ATOM   2200  N  NH1  . ARG   A  1  143 ? 4.841   -29.534 -39.841  1.00 52.15  ? 143  ARG   A NH1  1 
ATOM   2201  N  NH2  . ARG   A  1  143 ? 5.963   -29.738 -41.832  1.00 55.01  ? 143  ARG   A NH2  1 
ATOM   2202  H  H    . ARG   A  1  143 ? 10.051  -32.932 -38.027  1.00 62.89  ? 143  ARG   A H    1 
ATOM   2203  H  HA   . ARG   A  1  143 ? 8.058   -34.586 -37.346  1.00 64.09  ? 143  ARG   A HA   1 
ATOM   2204  H  HB2  . ARG   A  1  143 ? 7.615   -32.344 -37.948  1.00 63.02  ? 143  ARG   A HB2  1 
ATOM   2205  H  HB3  . ARG   A  1  143 ? 8.035   -32.707 -39.437  1.00 63.02  ? 143  ARG   A HB3  1 
ATOM   2206  H  HG2  . ARG   A  1  143 ? 6.204   -34.041 -39.694  1.00 62.58  ? 143  ARG   A HG2  1 
ATOM   2207  H  HG3  . ARG   A  1  143 ? 5.842   -33.919 -38.152  1.00 62.58  ? 143  ARG   A HG3  1 
ATOM   2208  H  HD2  . ARG   A  1  143 ? 4.439   -32.522 -39.339  1.00 58.48  ? 143  ARG   A HD2  1 
ATOM   2209  H  HD3  . ARG   A  1  143 ? 5.420   -31.620 -38.474  1.00 58.48  ? 143  ARG   A HD3  1 
ATOM   2210  H  HE   . ARG   A  1  143 ? 6.248   -31.997 -41.003  1.00 62.04  ? 143  ARG   A HE   1 
ATOM   2211  H  HH11 . ARG   A  1  143 ? 4.563   -29.876 -39.103  1.00 62.56  ? 143  ARG   A HH11 1 
ATOM   2212  H  HH12 . ARG   A  1  143 ? 4.673   -28.710 -40.023  1.00 62.56  ? 143  ARG   A HH12 1 
ATOM   2213  H  HH21 . ARG   A  1  143 ? 6.414   -30.213 -42.388  1.00 65.99  ? 143  ARG   A HH21 1 
ATOM   2214  H  HH22 . ARG   A  1  143 ? 5.793   -28.914 -42.009  1.00 65.99  ? 143  ARG   A HH22 1 
ATOM   2215  N  N    . SER   A  1  144 ? 9.368   -36.340 -38.716  1.00 59.01  ? 144  SER   A N    1 
ATOM   2216  C  CA   . SER   A  1  144 ? 9.710   -37.464 -39.566  1.00 61.18  ? 144  SER   A CA   1 
ATOM   2217  C  C    . SER   A  1  144 ? 8.681   -38.575 -39.376  1.00 62.38  ? 144  SER   A C    1 
ATOM   2218  O  O    . SER   A  1  144 ? 7.649   -38.396 -38.721  1.00 64.51  ? 144  SER   A O    1 
ATOM   2219  C  CB   . SER   A  1  144 ? 11.125  -37.947 -39.243  1.00 57.27  ? 144  SER   A CB   1 
ATOM   2220  O  OG   . SER   A  1  144 ? 11.193  -38.456 -37.922  1.00 54.32  ? 144  SER   A OG   1 
ATOM   2221  H  H    . SER   A  1  144 ? 9.592   -36.458 -37.894  1.00 70.79  ? 144  SER   A H    1 
ATOM   2222  H  HA   . SER   A  1  144 ? 9.689   -37.174 -40.491  1.00 73.40  ? 144  SER   A HA   1 
ATOM   2223  H  HB2  . SER   A  1  144 ? 11.369  -38.649 -39.865  1.00 68.71  ? 144  SER   A HB2  1 
ATOM   2224  H  HB3  . SER   A  1  144 ? 11.741  -37.201 -39.326  1.00 68.71  ? 144  SER   A HB3  1 
ATOM   2225  H  HG   . SER   A  1  144 ? 11.994  -38.574 -37.700  1.00 65.17  ? 144  SER   A HG   1 
ATOM   2226  N  N    . GLN   A  1  145 ? 8.956   -39.736 -39.962  1.00 60.96  ? 145  GLN   A N    1 
ATOM   2227  C  CA   . GLN   A  1  145 ? 8.169   -40.938 -39.728  1.00 60.60  ? 145  GLN   A CA   1 
ATOM   2228  C  C    . GLN   A  1  145 ? 8.678   -41.731 -38.529  1.00 58.46  ? 145  GLN   A C    1 
ATOM   2229  O  O    . GLN   A  1  145 ? 8.180   -42.832 -38.269  1.00 55.63  ? 145  GLN   A O    1 
ATOM   2230  C  CB   . GLN   A  1  145 ? 8.164   -41.806 -40.990  1.00 60.54  ? 145  GLN   A CB   1 
ATOM   2231  C  CG   . GLN   A  1  145 ? 7.372   -41.184 -42.137  1.00 61.73  ? 145  GLN   A CG   1 
ATOM   2232  C  CD   . GLN   A  1  145 ? 8.036   -41.357 -43.491  1.00 60.72  ? 145  GLN   A CD   1 
ATOM   2233  O  OE1  . GLN   A  1  145 ? 8.872   -42.239 -43.680  1.00 58.40  ? 145  GLN   A OE1  1 
ATOM   2234  N  NE2  . GLN   A  1  145 ? 7.665   -40.505 -44.442  1.00 60.09  ? 145  GLN   A NE2  1 
ATOM   2235  H  H    . GLN   A  1  145 ? 9.608   -39.853 -40.511  1.00 73.14  ? 145  GLN   A H    1 
ATOM   2236  H  HA   . GLN   A  1  145 ? 7.249   -40.691 -39.544  1.00 72.70  ? 145  GLN   A HA   1 
ATOM   2237  H  HB2  . GLN   A  1  145 ? 9.078   -41.931 -41.290  1.00 72.62  ? 145  GLN   A HB2  1 
ATOM   2238  H  HB3  . GLN   A  1  145 ? 7.764   -42.664 -40.780  1.00 72.62  ? 145  GLN   A HB3  1 
ATOM   2239  H  HG2  . GLN   A  1  145 ? 6.498   -41.604 -42.179  1.00 74.06  ? 145  GLN   A HG2  1 
ATOM   2240  H  HG3  . GLN   A  1  145 ? 7.275   -40.233 -41.972  1.00 74.06  ? 145  GLN   A HG3  1 
ATOM   2241  H  HE21 . GLN   A  1  145 ? 7.078   -39.900 -44.273  1.00 72.09  ? 145  GLN   A HE21 1 
ATOM   2242  H  HE22 . GLN   A  1  145 ? 8.012   -40.561 -45.228  1.00 72.09  ? 145  GLN   A HE22 1 
ATOM   2243  N  N    . ASP   A  1  146 ? 9.657   -41.191 -37.798  1.00 59.12  ? 146  ASP   A N    1 
ATOM   2244  C  CA   . ASP   A  1  146 ? 10.196  -41.822 -36.592  1.00 58.05  ? 146  ASP   A CA   1 
ATOM   2245  C  C    . ASP   A  1  146 ? 9.366   -41.341 -35.400  1.00 58.03  ? 146  ASP   A C    1 
ATOM   2246  O  O    . ASP   A  1  146 ? 9.735   -40.423 -34.663  1.00 61.04  ? 146  ASP   A O    1 
ATOM   2247  C  CB   . ASP   A  1  146 ? 11.678  -41.493 -36.444  1.00 59.81  ? 146  ASP   A CB   1 
ATOM   2248  C  CG   . ASP   A  1  146 ? 12.434  -42.518 -35.613  1.00 63.39  ? 146  ASP   A CG   1 
ATOM   2249  O  OD1  . ASP   A  1  146 ? 11.835  -43.542 -35.223  1.00 65.23  ? 146  ASP   A OD1  1 
ATOM   2250  O  OD2  . ASP   A  1  146 ? 13.637  -42.298 -35.352  1.00 64.09  ? 146  ASP   A OD2  1 
ATOM   2251  H  H    . ASP   A  1  146 ? 10.033  -40.441 -37.985  1.00 70.92  ? 146  ASP   A H    1 
ATOM   2252  H  HA   . ASP   A  1  146 ? 10.110  -42.787 -36.651  1.00 69.65  ? 146  ASP   A HA   1 
ATOM   2253  H  HB2  . ASP   A  1  146 ? 12.084  -41.463 -37.325  1.00 71.76  ? 146  ASP   A HB2  1 
ATOM   2254  H  HB3  . ASP   A  1  146 ? 11.767  -40.630 -36.009  1.00 71.76  ? 146  ASP   A HB3  1 
ATOM   2255  N  N    . ILE   A  1  147 ? 8.225   -42.001 -35.213  1.00 57.74  ? 147  ILE   A N    1 
ATOM   2256  C  CA   . ILE   A  1  147 ? 7.181   -41.569 -34.286  1.00 63.19  ? 147  ILE   A CA   1 
ATOM   2257  C  C    . ILE   A  1  147 ? 7.404   -42.211 -32.924  1.00 65.50  ? 147  ILE   A C    1 
ATOM   2258  O  O    . ILE   A  1  147 ? 7.468   -43.438 -32.828  1.00 76.54  ? 147  ILE   A O    1 
ATOM   2259  C  CB   . ILE   A  1  147 ? 5.794   -41.960 -34.809  1.00 70.36  ? 147  ILE   A CB   1 
ATOM   2260  C  CG1  . ILE   A  1  147 ? 5.741   -43.482 -35.038  1.00 72.50  ? 147  ILE   A CG1  1 
ATOM   2261  C  CG2  . ILE   A  1  147 ? 5.479   -41.240 -36.097  1.00 73.43  ? 147  ILE   A CG2  1 
ATOM   2262  C  CD1  . ILE   A  1  147 ? 4.371   -44.074 -35.045  1.00 78.66  ? 147  ILE   A CD1  1 
ATOM   2263  H  H    . ILE   A  1  147 ? 8.025   -42.728 -35.626  1.00 69.27  ? 147  ILE   A H    1 
ATOM   2264  H  HA   . ILE   A  1  147 ? 7.254   -40.607 -34.185  1.00 75.81  ? 147  ILE   A HA   1 
ATOM   2265  H  HB   . ILE   A  1  147 ? 5.135   -41.703 -34.146  1.00 84.41  ? 147  ILE   A HB   1 
ATOM   2266  H  HG12 . ILE   A  1  147 ? 6.145   -43.678 -35.898  1.00 86.98  ? 147  ILE   A HG12 1 
ATOM   2267  H  HG13 . ILE   A  1  147 ? 6.241   -43.917 -34.330  1.00 86.98  ? 147  ILE   A HG13 1 
ATOM   2268  H  HG21 . ILE   A  1  147 ? 4.575   -41.464 -36.371  1.00 88.10  ? 147  ILE   A HG21 1 
ATOM   2269  H  HG22 . ILE   A  1  147 ? 5.553   -40.284 -35.951  1.00 88.10  ? 147  ILE   A HG22 1 
ATOM   2270  H  HG23 . ILE   A  1  147 ? 6.109   -41.521 -36.778  1.00 88.10  ? 147  ILE   A HG23 1 
ATOM   2271  H  HD11 . ILE   A  1  147 ? 4.445   -45.041 -35.061  1.00 94.38  ? 147  ILE   A HD11 1 
ATOM   2272  H  HD12 . ILE   A  1  147 ? 3.901   -43.792 -34.245  1.00 94.38  ? 147  ILE   A HD12 1 
ATOM   2273  H  HD13 . ILE   A  1  147 ? 3.897   -43.765 -35.833  1.00 94.38  ? 147  ILE   A HD13 1 
ATOM   2274  N  N    . ASP   A  1  148 ? 7.708   -41.416 -31.904  1.00 62.64  ? 148  ASP   A N    1 
ATOM   2275  C  CA   . ASP   A  1  148 ? 7.163   -41.628 -30.560  1.00 62.16  ? 148  ASP   A CA   1 
ATOM   2276  C  C    . ASP   A  1  148 ? 8.247   -41.073 -29.643  1.00 59.79  ? 148  ASP   A C    1 
ATOM   2277  O  O    . ASP   A  1  148 ? 9.168   -40.406 -30.125  1.00 59.56  ? 148  ASP   A O    1 
ATOM   2278  C  CB   . ASP   A  1  148 ? 6.753   -43.067 -30.254  1.00 63.52  ? 148  ASP   A CB   1 
ATOM   2279  C  CG   . ASP   A  1  148 ? 5.648   -43.137 -29.205  1.00 63.74  ? 148  ASP   A CG   1 
ATOM   2280  O  OD1  . ASP   A  1  148 ? 5.550   -42.202 -28.379  1.00 63.47  ? 148  ASP   A OD1  1 
ATOM   2281  O  OD2  . ASP   A  1  148 ? 4.865   -44.113 -29.217  1.00 65.79  ? 148  ASP   A OD2  1 
ATOM   2282  H  H    . ASP   A  1  148 ? 8.234   -40.738 -31.961  1.00 75.15  ? 148  ASP   A H    1 
ATOM   2283  H  HA   . ASP   A  1  148 ? 6.311   -41.183 -30.428  1.00 74.57  ? 148  ASP   A HA   1 
ATOM   2284  H  HB2  . ASP   A  1  148 ? 6.426   -43.485 -31.067  1.00 76.21  ? 148  ASP   A HB2  1 
ATOM   2285  H  HB3  . ASP   A  1  148 ? 7.522   -43.553 -29.917  1.00 76.21  ? 148  ASP   A HB3  1 
ATOM   2286  N  N    . ALA   A  1  149 ? 8.152   -41.297 -28.333  1.00 57.99  ? 149  ALA   A N    1 
ATOM   2287  C  CA   . ALA   A  1  149 ? 9.327   -41.075 -27.495  1.00 58.26  ? 149  ALA   A CA   1 
ATOM   2288  C  C    . ALA   A  1  149 ? 10.546  -41.813 -28.052  1.00 59.14  ? 149  ALA   A C    1 
ATOM   2289  O  O    . ALA   A  1  149 ? 11.634  -41.236 -28.158  1.00 63.37  ? 149  ALA   A O    1 
ATOM   2290  C  CB   . ALA   A  1  149 ? 9.055   -41.507 -26.055  1.00 57.29  ? 149  ALA   A CB   1 
ATOM   2291  H  H    . ALA   A  1  149 ? 7.447   -41.567 -27.921  1.00 69.57  ? 149  ALA   A H    1 
ATOM   2292  H  HA   . ALA   A  1  149 ? 9.519   -40.125 -27.486  1.00 69.90  ? 149  ALA   A HA   1 
ATOM   2293  H  HB1  . ALA   A  1  149 ? 9.835   -41.310 -25.513  1.00 68.73  ? 149  ALA   A HB1  1 
ATOM   2294  H  HB2  . ALA   A  1  149 ? 8.287   -41.019 -25.719  1.00 68.73  ? 149  ALA   A HB2  1 
ATOM   2295  H  HB3  . ALA   A  1  149 ? 8.875   -42.460 -26.040  1.00 68.73  ? 149  ALA   A HB3  1 
ATOM   2296  N  N    . ASP   A  1  150 ? 10.386  -43.091 -28.427  1.00 59.11  ? 150  ASP   A N    1 
ATOM   2297  C  CA   . ASP   A  1  150 ? 11.539  -43.848 -28.915  1.00 60.37  ? 150  ASP   A CA   1 
ATOM   2298  C  C    . ASP   A  1  150 ? 12.115  -43.233 -30.186  1.00 55.65  ? 150  ASP   A C    1 
ATOM   2299  O  O    . ASP   A  1  150 ? 13.333  -43.269 -30.394  1.00 50.79  ? 150  ASP   A O    1 
ATOM   2300  C  CB   . ASP   A  1  150 ? 11.187  -45.323 -29.160  1.00 69.04  ? 150  ASP   A CB   1 
ATOM   2301  C  CG   . ASP   A  1  150 ? 9.849   -45.510 -29.845  1.00 80.43  ? 150  ASP   A CG   1 
ATOM   2302  O  OD1  . ASP   A  1  150 ? 8.823   -45.161 -29.232  1.00 85.61  ? 150  ASP   A OD1  1 
ATOM   2303  O  OD2  . ASP   A  1  150 ? 9.822   -46.022 -30.985  1.00 86.31  ? 150  ASP   A OD2  1 
ATOM   2304  H  H    . ASP   A  1  150 ? 9.644   -43.526 -28.408  1.00 70.91  ? 150  ASP   A H    1 
ATOM   2305  H  HA   . ASP   A  1  150 ? 12.217  -43.828 -28.222  1.00 72.43  ? 150  ASP   A HA   1 
ATOM   2306  H  HB2  . ASP   A  1  150 ? 11.868  -45.719 -29.725  1.00 82.83  ? 150  ASP   A HB2  1 
ATOM   2307  H  HB3  . ASP   A  1  150 ? 11.152  -45.784 -28.308  1.00 82.83  ? 150  ASP   A HB3  1 
ATOM   2308  N  N    . GLY   A  1  151 ? 11.266  -42.676 -31.047  1.00 57.73  ? 151  GLY   A N    1 
ATOM   2309  C  CA   . GLY   A  1  151 ? 11.736  -41.936 -32.203  1.00 57.65  ? 151  GLY   A CA   1 
ATOM   2310  C  C    . GLY   A  1  151 ? 11.921  -40.463 -31.892  1.00 55.93  ? 151  GLY   A C    1 
ATOM   2311  O  O    . GLY   A  1  151 ? 12.352  -40.109 -30.790  1.00 56.29  ? 151  GLY   A O    1 
ATOM   2312  H  H    . GLY   A  1  151 ? 10.410  -42.715 -30.979  1.00 69.26  ? 151  GLY   A H    1 
ATOM   2313  H  HA2  . GLY   A  1  151 ? 12.587  -42.298 -32.495  1.00 69.16  ? 151  GLY   A HA2  1 
ATOM   2314  H  HA3  . GLY   A  1  151 ? 11.092  -42.020 -32.924  1.00 69.16  ? 151  GLY   A HA3  1 
ATOM   2315  N  N    . GLN   A  1  152 ? 11.594  -39.593 -32.851  1.00 55.62  ? 152  GLN   A N    1 
ATOM   2316  C  CA   . GLN   A  1  152 ? 11.677  -38.150 -32.664  1.00 57.46  ? 152  GLN   A CA   1 
ATOM   2317  C  C    . GLN   A  1  152 ? 10.308  -37.514 -32.435  1.00 56.62  ? 152  GLN   A C    1 
ATOM   2318  O  O    . GLN   A  1  152 ? 10.161  -36.299 -32.608  1.00 55.42  ? 152  GLN   A O    1 
ATOM   2319  C  CB   . GLN   A  1  152 ? 12.344  -37.487 -33.872  1.00 58.26  ? 152  GLN   A CB   1 
ATOM   2320  C  CG   . GLN   A  1  152 ? 13.520  -38.239 -34.471  1.00 62.27  ? 152  GLN   A CG   1 
ATOM   2321  C  CD   . GLN   A  1  152 ? 13.960  -37.637 -35.791  1.00 61.11  ? 152  GLN   A CD   1 
ATOM   2322  O  OE1  . GLN   A  1  152 ? 13.457  -38.005 -36.853  1.00 59.43  ? 152  GLN   A OE1  1 
ATOM   2323  N  NE2  . GLN   A  1  152 ? 14.896  -36.696 -35.731  1.00 58.12  ? 152  GLN   A NE2  1 
ATOM   2324  H  H    . GLN   A  1  152 ? 11.317  -39.823 -33.631  1.00 66.72  ? 152  GLN   A H    1 
ATOM   2325  H  HA   . GLN   A  1  152 ? 12.229  -37.986 -31.883  1.00 68.93  ? 152  GLN   A HA   1 
ATOM   2326  H  HB2  . GLN   A  1  152 ? 11.679  -37.389 -34.571  1.00 69.89  ? 152  GLN   A HB2  1 
ATOM   2327  H  HB3  . GLN   A  1  152 ? 12.670  -36.615 -33.598  1.00 69.89  ? 152  GLN   A HB3  1 
ATOM   2328  H  HG2  . GLN   A  1  152 ? 14.269  -38.204 -33.856  1.00 74.70  ? 152  GLN   A HG2  1 
ATOM   2329  H  HG3  . GLN   A  1  152 ? 13.263  -39.161 -34.628  1.00 74.70  ? 152  GLN   A HG3  1 
ATOM   2330  H  HE21 . GLN   A  1  152 ? 15.218  -36.459 -34.970  1.00 69.73  ? 152  GLN   A HE21 1 
ATOM   2331  H  HE22 . GLN   A  1  152 ? 15.179  -36.324 -36.453  1.00 69.73  ? 152  GLN   A HE22 1 
ATOM   2332  N  N    . GLY   A  1  153 ? 9.303   -38.308 -32.062  1.00 53.20  ? 153  GLY   A N    1 
ATOM   2333  C  CA   . GLY   A  1  153 ? 7.964   -37.765 -31.899  1.00 51.55  ? 153  GLY   A CA   1 
ATOM   2334  C  C    . GLY   A  1  153 ? 7.884   -36.657 -30.869  1.00 51.12  ? 153  GLY   A C    1 
ATOM   2335  O  O    . GLY   A  1  153 ? 7.071   -35.737 -31.002  1.00 51.16  ? 153  GLY   A O    1 
ATOM   2336  H  H    . GLY   A  1  153 ? 9.372   -39.150 -31.900  1.00 63.82  ? 153  GLY   A H    1 
ATOM   2337  H  HA2  . GLY   A  1  153 ? 7.662   -37.409 -32.749  1.00 61.84  ? 153  GLY   A HA2  1 
ATOM   2338  H  HA3  . GLY   A  1  153 ? 7.365   -38.476 -31.624  1.00 61.84  ? 153  GLY   A HA3  1 
ATOM   2339  N  N    . PHE   A  1  154 ? 8.722   -36.720 -29.835  1.00 48.12  ? 154  PHE   A N    1 
ATOM   2340  C  CA   . PHE   A  1  154 ? 8.738   -35.728 -28.767  1.00 49.81  ? 154  PHE   A CA   1 
ATOM   2341  C  C    . PHE   A  1  154 ? 10.000  -34.876 -28.821  1.00 52.20  ? 154  PHE   A C    1 
ATOM   2342  O  O    . PHE   A  1  154 ? 10.447  -34.340 -27.805  1.00 52.34  ? 154  PHE   A O    1 
ATOM   2343  C  CB   . PHE   A  1  154 ? 8.601   -36.416 -27.412  1.00 50.65  ? 154  PHE   A CB   1 
ATOM   2344  C  CG   . PHE   A  1  154 ? 7.249   -37.015 -27.186  1.00 53.11  ? 154  PHE   A CG   1 
ATOM   2345  C  CD1  . PHE   A  1  154 ? 6.842   -38.121 -27.912  1.00 54.29  ? 154  PHE   A CD1  1 
ATOM   2346  C  CD2  . PHE   A  1  154 ? 6.377   -36.466 -26.263  1.00 55.73  ? 154  PHE   A CD2  1 
ATOM   2347  C  CE1  . PHE   A  1  154 ? 5.595   -38.672 -27.719  1.00 59.23  ? 154  PHE   A CE1  1 
ATOM   2348  C  CE2  . PHE   A  1  154 ? 5.126   -37.014 -26.064  1.00 57.45  ? 154  PHE   A CE2  1 
ATOM   2349  C  CZ   . PHE   A  1  154 ? 4.735   -38.119 -26.792  1.00 59.04  ? 154  PHE   A CZ   1 
ATOM   2350  H  H    . PHE   A  1  154 ? 9.303   -37.345 -29.730  1.00 57.73  ? 154  PHE   A H    1 
ATOM   2351  H  HA   . PHE   A  1  154 ? 7.980   -35.132 -28.873  1.00 59.75  ? 154  PHE   A HA   1 
ATOM   2352  H  HB2  . PHE   A  1  154 ? 9.257   -37.128 -27.354  1.00 60.76  ? 154  PHE   A HB2  1 
ATOM   2353  H  HB3  . PHE   A  1  154 ? 8.759   -35.763 -26.712  1.00 60.76  ? 154  PHE   A HB3  1 
ATOM   2354  H  HD1  . PHE   A  1  154 ? 7.418   -38.497 -28.537  1.00 65.13  ? 154  PHE   A HD1  1 
ATOM   2355  H  HD2  . PHE   A  1  154 ? 6.637   -35.720 -25.772  1.00 66.85  ? 154  PHE   A HD2  1 
ATOM   2356  H  HE1  . PHE   A  1  154 ? 5.332   -39.416 -28.212  1.00 71.05  ? 154  PHE   A HE1  1 
ATOM   2357  H  HE2  . PHE   A  1  154 ? 4.548   -36.638 -25.440  1.00 68.92  ? 154  PHE   A HE2  1 
ATOM   2358  H  HZ   . PHE   A  1  154 ? 3.893   -38.491 -26.659  1.00 70.83  ? 154  PHE   A HZ   1 
ATOM   2359  N  N    . CYS   A  1  155 ? 10.558  -34.727 -30.021  1.00 52.38  ? 155  CYS   A N    1 
ATOM   2360  C  CA   . CYS   A  1  155 ? 11.859  -34.089 -30.185  1.00 49.83  ? 155  CYS   A CA   1 
ATOM   2361  C  C    . CYS   A  1  155 ? 11.830  -32.617 -29.794  1.00 48.16  ? 155  CYS   A C    1 
ATOM   2362  O  O    . CYS   A  1  155 ? 12.811  -32.099 -29.248  1.00 46.82  ? 155  CYS   A O    1 
ATOM   2363  C  CB   . CYS   A  1  155 ? 12.303  -34.258 -31.635  1.00 51.36  ? 155  CYS   A CB   1 
ATOM   2364  S  SG   . CYS   A  1  155 ? 13.384  -32.982 -32.286  1.00 54.63  ? 155  CYS   A SG   1 
ATOM   2365  H  H    . CYS   A  1  155 ? 10.203  -34.987 -30.759  1.00 62.84  ? 155  CYS   A H    1 
ATOM   2366  H  HA   . CYS   A  1  155 ? 12.503  -34.521 -29.602  1.00 59.78  ? 155  CYS   A HA   1 
ATOM   2367  H  HB2  . CYS   A  1  155 ? 12.778  -35.100 -31.709  1.00 61.62  ? 155  CYS   A HB2  1 
ATOM   2368  H  HB3  . CYS   A  1  155 ? 11.511  -34.274 -32.194  1.00 61.62  ? 155  CYS   A HB3  1 
ATOM   2369  N  N    . GLN   A  1  156 ? 10.724  -31.927 -30.064  1.00 45.92  ? 156  GLN   A N    1 
ATOM   2370  C  CA   . GLN   A  1  156 ? 10.626  -30.485 -29.833  1.00 48.87  ? 156  GLN   A CA   1 
ATOM   2371  C  C    . GLN   A  1  156 ? 11.717  -29.742 -30.605  1.00 50.58  ? 156  GLN   A C    1 
ATOM   2372  O  O    . GLN   A  1  156 ? 12.455  -28.921 -30.056  1.00 49.31  ? 156  GLN   A O    1 
ATOM   2373  C  CB   . GLN   A  1  156 ? 10.692  -30.161 -28.338  1.00 49.43  ? 156  GLN   A CB   1 
ATOM   2374  C  CG   . GLN   A  1  156 ? 9.537   -30.723 -27.529  1.00 51.84  ? 156  GLN   A CG   1 
ATOM   2375  C  CD   . GLN   A  1  156 ? 9.572   -30.273 -26.085  1.00 55.93  ? 156  GLN   A CD   1 
ATOM   2376  O  OE1  . GLN   A  1  156 ? 10.127  -30.956 -25.226  1.00 58.00  ? 156  GLN   A OE1  1 
ATOM   2377  N  NE2  . GLN   A  1  156 ? 8.985   -29.113 -25.810  1.00 59.44  ? 156  GLN   A NE2  1 
ATOM   2378  H  H    . GLN   A  1  156 ? 10.007  -32.275 -30.387  1.00 55.08  ? 156  GLN   A H    1 
ATOM   2379  H  HA   . GLN   A  1  156 ? 9.768   -30.177 -30.163  1.00 58.63  ? 156  GLN   A HA   1 
ATOM   2380  H  HB2  . GLN   A  1  156 ? 11.513  -30.531 -27.976  1.00 59.29  ? 156  GLN   A HB2  1 
ATOM   2381  H  HB3  . GLN   A  1  156 ? 10.687  -29.197 -28.229  1.00 59.29  ? 156  GLN   A HB3  1 
ATOM   2382  H  HG2  . GLN   A  1  156 ? 8.701   -30.421 -27.918  1.00 62.19  ? 156  GLN   A HG2  1 
ATOM   2383  H  HG3  . GLN   A  1  156 ? 9.580   -31.692 -27.544  1.00 62.19  ? 156  GLN   A HG3  1 
ATOM   2384  H  HE21 . GLN   A  1  156 ? 8.611   -28.661 -26.439  1.00 71.31  ? 156  GLN   A HE21 1 
ATOM   2385  H  HE22 . GLN   A  1  156 ? 8.979   -28.815 -25.003  1.00 71.31  ? 156  GLN   A HE22 1 
ATOM   2386  N  N    . GLY   A  1  157 ? 11.811  -30.039 -31.899  1.00 51.18  ? 157  GLY   A N    1 
ATOM   2387  C  CA   . GLY   A  1  157 ? 12.854  -29.435 -32.710  1.00 52.04  ? 157  GLY   A CA   1 
ATOM   2388  C  C    . GLY   A  1  157 ? 12.682  -27.929 -32.801  1.00 55.86  ? 157  GLY   A C    1 
ATOM   2389  O  O    . GLY   A  1  157 ? 11.574  -27.417 -32.979  1.00 55.04  ? 157  GLY   A O    1 
ATOM   2390  H  H    . GLY   A  1  157 ? 11.291  -30.577 -32.322  1.00 61.40  ? 157  GLY   A H    1 
ATOM   2391  H  HA2  . GLY   A  1  157 ? 13.721  -29.625 -32.319  1.00 62.42  ? 157  GLY   A HA2  1 
ATOM   2392  H  HA3  . GLY   A  1  157 ? 12.823  -29.804 -33.607  1.00 62.42  ? 157  GLY   A HA3  1 
ATOM   2393  N  N    . GLY   A  1  158 ? 13.800  -27.214 -32.684  1.00 59.18  ? 158  GLY   A N    1 
ATOM   2394  C  CA   . GLY   A  1  158 ? 13.793  -25.770 -32.600  1.00 56.14  ? 158  GLY   A CA   1 
ATOM   2395  C  C    . GLY   A  1  158 ? 13.944  -25.230 -31.196  1.00 50.13  ? 158  GLY   A C    1 
ATOM   2396  O  O    . GLY   A  1  158 ? 14.021  -24.007 -31.026  1.00 49.76  ? 158  GLY   A O    1 
ATOM   2397  H  H    . GLY   A  1  158 ? 14.588  -27.557 -32.652  1.00 71.00  ? 158  GLY   A H    1 
ATOM   2398  H  HA2  . GLY   A  1  158 ? 14.524  -25.421 -33.134  1.00 67.35  ? 158  GLY   A HA2  1 
ATOM   2399  H  HA3  . GLY   A  1  158 ? 12.954  -25.440 -32.959  1.00 67.35  ? 158  GLY   A HA3  1 
ATOM   2400  N  N    . PHE   A  1  159 ? 13.979  -26.106 -30.188  1.00 47.86  ? 159  PHE   A N    1 
ATOM   2401  C  CA   . PHE   A  1  159 ? 14.187  -25.673 -28.809  1.00 50.67  ? 159  PHE   A CA   1 
ATOM   2402  C  C    . PHE   A  1  159 ? 15.370  -24.719 -28.707  1.00 55.00  ? 159  PHE   A C    1 
ATOM   2403  O  O    . PHE   A  1  159 ? 15.353  -23.774 -27.910  1.00 56.20  ? 159  PHE   A O    1 
ATOM   2404  C  CB   . PHE   A  1  159 ? 14.396  -26.905 -27.924  1.00 50.37  ? 159  PHE   A CB   1 
ATOM   2405  C  CG   . PHE   A  1  159 ? 14.337  -26.623 -26.452  1.00 51.00  ? 159  PHE   A CG   1 
ATOM   2406  C  CD1  . PHE   A  1  159 ? 13.119  -26.558 -25.795  1.00 51.92  ? 159  PHE   A CD1  1 
ATOM   2407  C  CD2  . PHE   A  1  159 ? 15.498  -26.446 -25.720  1.00 50.86  ? 159  PHE   A CD2  1 
ATOM   2408  C  CE1  . PHE   A  1  159 ? 13.061  -26.309 -24.439  1.00 50.81  ? 159  PHE   A CE1  1 
ATOM   2409  C  CE2  . PHE   A  1  159 ? 15.446  -26.196 -24.364  1.00 50.23  ? 159  PHE   A CE2  1 
ATOM   2410  C  CZ   . PHE   A  1  159 ? 14.225  -26.128 -23.724  1.00 52.02  ? 159  PHE   A CZ   1 
ATOM   2411  H  H    . PHE   A  1  159 ? 13.886  -26.956 -30.278  1.00 57.41  ? 159  PHE   A H    1 
ATOM   2412  H  HA   . PHE   A  1  159 ? 13.402  -25.199 -28.492  1.00 60.79  ? 159  PHE   A HA   1 
ATOM   2413  H  HB2  . PHE   A  1  159 ? 13.704  -27.554 -28.128  1.00 60.42  ? 159  PHE   A HB2  1 
ATOM   2414  H  HB3  . PHE   A  1  159 ? 15.270  -27.280 -28.117  1.00 60.42  ? 159  PHE   A HB3  1 
ATOM   2415  H  HD1  . PHE   A  1  159 ? 12.331  -26.685 -26.273  1.00 62.29  ? 159  PHE   A HD1  1 
ATOM   2416  H  HD2  . PHE   A  1  159 ? 16.323  -26.496 -26.147  1.00 61.01  ? 159  PHE   A HD2  1 
ATOM   2417  H  HE1  . PHE   A  1  159 ? 12.238  -26.263 -24.009  1.00 60.95  ? 159  PHE   A HE1  1 
ATOM   2418  H  HE2  . PHE   A  1  159 ? 16.231  -26.073 -23.882  1.00 60.26  ? 159  PHE   A HE2  1 
ATOM   2419  H  HZ   . PHE   A  1  159 ? 14.187  -25.960 -22.810  1.00 62.41  ? 159  PHE   A HZ   1 
ATOM   2420  N  N    . SER   A  1  160 ? 16.405  -24.953 -29.511  1.00 54.53  ? 160  SER   A N    1 
ATOM   2421  C  CA   . SER   A  1  160 ? 17.544  -24.052 -29.615  1.00 55.62  ? 160  SER   A CA   1 
ATOM   2422  C  C    . SER   A  1  160 ? 18.041  -24.090 -31.052  1.00 55.68  ? 160  SER   A C    1 
ATOM   2423  O  O    . SER   A  1  160 ? 18.016  -25.145 -31.692  1.00 55.18  ? 160  SER   A O    1 
ATOM   2424  C  CB   . SER   A  1  160 ? 18.666  -24.445 -28.648  1.00 56.72  ? 160  SER   A CB   1 
ATOM   2425  O  OG   . SER   A  1  160 ? 19.165  -25.737 -28.940  1.00 58.17  ? 160  SER   A OG   1 
ATOM   2426  H  H    . SER   A  1  160 ? 16.471  -25.644 -30.018  1.00 65.42  ? 160  SER   A H    1 
ATOM   2427  H  HA   . SER   A  1  160 ? 17.275  -23.146 -29.398  1.00 66.73  ? 160  SER   A HA   1 
ATOM   2428  H  HB2  . SER   A  1  160 ? 19.388  -23.803 -28.729  1.00 68.04  ? 160  SER   A HB2  1 
ATOM   2429  H  HB3  . SER   A  1  160 ? 18.317  -24.440 -27.743  1.00 68.04  ? 160  SER   A HB3  1 
ATOM   2430  H  HG   . SER   A  1  160 ? 18.782  -26.309 -28.459  1.00 69.79  ? 160  SER   A HG   1 
ATOM   2431  N  N    . ILE   A  1  161 ? 18.485  -22.937 -31.559  1.00 54.49  ? 161  ILE   A N    1 
ATOM   2432  C  CA   . ILE   A  1  161 ? 18.925  -22.818 -32.943  1.00 54.80  ? 161  ILE   A CA   1 
ATOM   2433  C  C    . ILE   A  1  161 ? 20.088  -21.842 -33.034  1.00 55.28  ? 161  ILE   A C    1 
ATOM   2434  O  O    . ILE   A  1  161 ? 20.316  -21.020 -32.143  1.00 58.07  ? 161  ILE   A O    1 
ATOM   2435  C  CB   . ILE   A  1  161 ? 17.785  -22.357 -33.881  1.00 56.34  ? 161  ILE   A CB   1 
ATOM   2436  C  CG1  . ILE   A  1  161 ? 17.024  -21.189 -33.248  1.00 58.99  ? 161  ILE   A CG1  1 
ATOM   2437  C  CG2  . ILE   A  1  161 ? 16.856  -23.518 -34.198  1.00 55.35  ? 161  ILE   A CG2  1 
ATOM   2438  C  CD1  . ILE   A  1  161 ? 16.166  -20.410 -34.224  1.00 58.95  ? 161  ILE   A CD1  1 
ATOM   2439  H  H    . ILE   A  1  161 ? 18.540  -22.204 -31.112  1.00 65.36  ? 161  ILE   A H    1 
ATOM   2440  H  HA   . ILE   A  1  161 ? 19.242  -23.687 -33.236  1.00 65.74  ? 161  ILE   A HA   1 
ATOM   2441  H  HB   . ILE   A  1  161 ? 18.171  -22.048 -34.715  1.00 67.59  ? 161  ILE   A HB   1 
ATOM   2442  H  HG12 . ILE   A  1  161 ? 16.440  -21.537 -32.555  1.00 70.77  ? 161  ILE   A HG12 1 
ATOM   2443  H  HG13 . ILE   A  1  161 ? 17.665  -20.572 -32.862  1.00 70.77  ? 161  ILE   A HG13 1 
ATOM   2444  H  HG21 . ILE   A  1  161 ? 16.265  -23.260 -34.923  1.00 66.40  ? 161  ILE   A HG21 1 
ATOM   2445  H  HG22 . ILE   A  1  161 ? 17.388  -24.285 -34.462  1.00 66.40  ? 161  ILE   A HG22 1 
ATOM   2446  H  HG23 . ILE   A  1  161 ? 16.337  -23.732 -33.407  1.00 66.40  ? 161  ILE   A HG23 1 
ATOM   2447  H  HD11 . ILE   A  1  161 ? 15.850  -19.601 -33.792  1.00 70.72  ? 161  ILE   A HD11 1 
ATOM   2448  H  HD12 . ILE   A  1  161 ? 16.700  -20.183 -35.002  1.00 70.72  ? 161  ILE   A HD12 1 
ATOM   2449  H  HD13 . ILE   A  1  161 ? 15.412  -20.960 -34.490  1.00 70.72  ? 161  ILE   A HD13 1 
ATOM   2450  N  N    . ASP   A  1  162 ? 20.827  -21.948 -34.135  1.00 51.50  ? 162  ASP   A N    1 
ATOM   2451  C  CA   . ASP   A  1  162 ? 21.886  -21.002 -34.457  1.00 52.43  ? 162  ASP   A CA   1 
ATOM   2452  C  C    . ASP   A  1  162 ? 22.204  -21.129 -35.940  1.00 52.00  ? 162  ASP   A C    1 
ATOM   2453  O  O    . ASP   A  1  162 ? 21.812  -22.094 -36.601  1.00 49.21  ? 162  ASP   A O    1 
ATOM   2454  C  CB   . ASP   A  1  162 ? 23.138  -21.243 -33.607  1.00 55.32  ? 162  ASP   A CB   1 
ATOM   2455  C  CG   . ASP   A  1  162 ? 23.945  -19.981 -33.392  1.00 63.59  ? 162  ASP   A CG   1 
ATOM   2456  O  OD1  . ASP   A  1  162 ? 23.798  -19.038 -34.198  1.00 66.78  ? 162  ASP   A OD1  1 
ATOM   2457  O  OD2  . ASP   A  1  162 ? 24.724  -19.931 -32.418  1.00 68.13  ? 162  ASP   A OD2  1 
ATOM   2458  H  H    . ASP   A  1  162 ? 20.732  -22.570 -34.721  1.00 61.78  ? 162  ASP   A H    1 
ATOM   2459  H  HA   . ASP   A  1  162 ? 21.572  -20.101 -34.282  1.00 62.90  ? 162  ASP   A HA   1 
ATOM   2460  H  HB2  . ASP   A  1  162 ? 22.871  -21.582 -32.738  1.00 66.36  ? 162  ASP   A HB2  1 
ATOM   2461  H  HB3  . ASP   A  1  162 ? 23.705  -21.890 -34.055  1.00 66.36  ? 162  ASP   A HB3  1 
ATOM   2462  N  N    . PHE   A  1  163 ? 22.919  -20.134 -36.456  1.00 54.11  ? 163  PHE   A N    1 
ATOM   2463  C  CA   . PHE   A  1  163 ? 23.398  -20.119 -37.830  1.00 56.43  ? 163  PHE   A CA   1 
ATOM   2464  C  C    . PHE   A  1  163 ? 24.912  -20.284 -37.841  1.00 59.69  ? 163  PHE   A C    1 
ATOM   2465  O  O    . PHE   A  1  163 ? 25.615  -19.672 -37.031  1.00 64.75  ? 163  PHE   A O    1 
ATOM   2466  C  CB   . PHE   A  1  163 ? 23.029  -18.808 -38.534  1.00 61.18  ? 163  PHE   A CB   1 
ATOM   2467  C  CG   . PHE   A  1  163 ? 21.642  -18.788 -39.112  1.00 64.20  ? 163  PHE   A CG   1 
ATOM   2468  C  CD1  . PHE   A  1  163 ? 21.354  -19.474 -40.281  1.00 66.32  ? 163  PHE   A CD1  1 
ATOM   2469  C  CD2  . PHE   A  1  163 ? 20.633  -18.061 -38.502  1.00 67.45  ? 163  PHE   A CD2  1 
ATOM   2470  C  CE1  . PHE   A  1  163 ? 20.080  -19.449 -40.822  1.00 67.93  ? 163  PHE   A CE1  1 
ATOM   2471  C  CE2  . PHE   A  1  163 ? 19.359  -18.032 -39.038  1.00 69.24  ? 163  PHE   A CE2  1 
ATOM   2472  C  CZ   . PHE   A  1  163 ? 19.083  -18.727 -40.201  1.00 68.66  ? 163  PHE   A CZ   1 
ATOM   2473  H  H    . PHE   A  1  163 ? 23.146  -19.433 -36.012  1.00 64.91  ? 163  PHE   A H    1 
ATOM   2474  H  HA   . PHE   A  1  163 ? 22.994  -20.854 -38.318  1.00 67.69  ? 163  PHE   A HA   1 
ATOM   2475  H  HB2  . PHE   A  1  163 ? 23.091  -18.083 -37.893  1.00 73.39  ? 163  PHE   A HB2  1 
ATOM   2476  H  HB3  . PHE   A  1  163 ? 23.653  -18.661 -39.262  1.00 73.39  ? 163  PHE   A HB3  1 
ATOM   2477  H  HD1  . PHE   A  1  163 ? 22.024  -19.956 -40.708  1.00 79.56  ? 163  PHE   A HD1  1 
ATOM   2478  H  HD2  . PHE   A  1  163 ? 20.815  -17.587 -37.723  1.00 80.92  ? 163  PHE   A HD2  1 
ATOM   2479  H  HE1  . PHE   A  1  163 ? 19.897  -19.920 -41.603  1.00 81.50  ? 163  PHE   A HE1  1 
ATOM   2480  H  HE2  . PHE   A  1  163 ? 18.688  -17.545 -38.617  1.00 83.07  ? 163  PHE   A HE2  1 
ATOM   2481  H  HZ   . PHE   A  1  163 ? 18.226  -18.708 -40.563  1.00 82.38  ? 163  PHE   A HZ   1 
ATOM   2482  N  N    . THR   A  1  164 ? 25.414  -21.106 -38.756  1.00 59.48  ? 164  THR   A N    1 
ATOM   2483  C  CA   . THR   A  1  164 ? 26.850  -21.182 -38.973  1.00 63.22  ? 164  THR   A CA   1 
ATOM   2484  C  C    . THR   A  1  164 ? 27.273  -20.092 -39.953  1.00 64.46  ? 164  THR   A C    1 
ATOM   2485  O  O    . THR   A  1  164 ? 26.450  -19.506 -40.661  1.00 62.39  ? 164  THR   A O    1 
ATOM   2486  C  CB   . THR   A  1  164 ? 27.269  -22.552 -39.508  1.00 67.46  ? 164  THR   A CB   1 
ATOM   2487  O  OG1  . THR   A  1  164 ? 26.964  -22.640 -40.905  1.00 70.98  ? 164  THR   A OG1  1 
ATOM   2488  C  CG2  . THR   A  1  164 ? 26.559  -23.673 -38.760  1.00 65.85  ? 164  THR   A CG2  1 
ATOM   2489  H  H    . THR   A  1  164 ? 24.946  -21.625 -39.258  1.00 71.35  ? 164  THR   A H    1 
ATOM   2490  H  HA   . THR   A  1  164 ? 27.307  -21.053 -38.127  1.00 75.84  ? 164  THR   A HA   1 
ATOM   2491  H  HB   . THR   A  1  164 ? 28.224  -22.664 -39.380  1.00 80.93  ? 164  THR   A HB   1 
ATOM   2492  H  HG1  . THR   A  1  164 ? 27.529  -23.126 -41.293  1.00 85.16  ? 164  THR   A HG1  1 
ATOM   2493  H  HG21 . THR   A  1  164 ? 26.891  -24.534 -39.059  1.00 79.00  ? 164  THR   A HG21 1 
ATOM   2494  H  HG22 . THR   A  1  164 ? 26.718  -23.588 -37.807  1.00 79.00  ? 164  THR   A HG22 1 
ATOM   2495  H  HG23 . THR   A  1  164 ? 25.604  -23.629 -38.925  1.00 79.00  ? 164  THR   A HG23 1 
ATOM   2496  N  N    . LYS   A  1  165 ? 28.579  -19.825 -39.992  1.00 65.96  ? 165  LYS   A N    1 
ATOM   2497  C  CA   . LYS   A  1  165 ? 29.075  -18.781 -40.879  1.00 66.58  ? 165  LYS   A CA   1 
ATOM   2498  C  C    . LYS   A  1  165 ? 28.888  -19.145 -42.347  1.00 69.72  ? 165  LYS   A C    1 
ATOM   2499  O  O    . LYS   A  1  165 ? 28.911  -18.252 -43.201  1.00 71.76  ? 165  LYS   A O    1 
ATOM   2500  C  CB   . LYS   A  1  165 ? 30.551  -18.491 -40.583  1.00 68.10  ? 165  LYS   A CB   1 
ATOM   2501  C  CG   . LYS   A  1  165 ? 31.562  -19.300 -41.391  1.00 72.35  ? 165  LYS   A CG   1 
ATOM   2502  C  CD   . LYS   A  1  165 ? 32.981  -18.810 -41.131  1.00 80.57  ? 165  LYS   A CD   1 
ATOM   2503  C  CE   . LYS   A  1  165 ? 33.967  -19.409 -42.119  1.00 88.33  ? 165  LYS   A CE   1 
ATOM   2504  N  NZ   . LYS   A  1  165 ? 35.343  -18.866 -41.947  1.00 91.58  ? 165  LYS   A NZ   1 
ATOM   2505  H  H    . LYS   A  1  165 ? 29.181  -20.225 -39.526  1.00 79.13  ? 165  LYS   A H    1 
ATOM   2506  H  HA   . LYS   A  1  165 ? 28.582  -17.963 -40.712  1.00 79.88  ? 165  LYS   A HA   1 
ATOM   2507  H  HB2  . LYS   A  1  165 ? 30.720  -17.554 -40.767  1.00 81.70  ? 165  LYS   A HB2  1 
ATOM   2508  H  HB3  . LYS   A  1  165 ? 30.716  -18.680 -39.645  1.00 81.70  ? 165  LYS   A HB3  1 
ATOM   2509  H  HG2  . LYS   A  1  165 ? 31.507  -20.234 -41.136  1.00 86.80  ? 165  LYS   A HG2  1 
ATOM   2510  H  HG3  . LYS   A  1  165 ? 31.372  -19.203 -42.337  1.00 86.80  ? 165  LYS   A HG3  1 
ATOM   2511  H  HD2  . LYS   A  1  165 ? 33.009  -17.845 -41.219  1.00 96.66  ? 165  LYS   A HD2  1 
ATOM   2512  H  HD3  . LYS   A  1  165 ? 33.251  -19.069 -40.236  1.00 96.66  ? 165  LYS   A HD3  1 
ATOM   2513  H  HE2  . LYS   A  1  165 ? 34.004  -20.370 -41.989  1.00 105.97 ? 165  LYS   A HE2  1 
ATOM   2514  H  HE3  . LYS   A  1  165 ? 33.674  -19.208 -43.022  1.00 105.97 ? 165  LYS   A HE3  1 
ATOM   2515  H  HZ1  . LYS   A  1  165 ? 35.923  -19.350 -42.417  1.00 109.88 ? 165  LYS   A HZ1  1 
ATOM   2516  H  HZ2  . LYS   A  1  165 ? 35.375  -18.023 -42.229  1.00 109.88 ? 165  LYS   A HZ2  1 
ATOM   2517  H  HZ3  . LYS   A  1  165 ? 35.575  -18.892 -41.088  1.00 109.88 ? 165  LYS   A HZ3  1 
ATOM   2518  N  N    . ALA   A  1  166 ? 28.698  -20.429 -42.656  1.00 71.12  ? 166  ALA   A N    1 
ATOM   2519  C  CA   . ALA   A  1  166 ? 28.553  -20.903 -44.027  1.00 74.08  ? 166  ALA   A CA   1 
ATOM   2520  C  C    . ALA   A  1  166 ? 27.103  -21.210 -44.387  1.00 75.00  ? 166  ALA   A C    1 
ATOM   2521  O  O    . ALA   A  1  166 ? 26.840  -22.097 -45.206  1.00 75.06  ? 166  ALA   A O    1 
ATOM   2522  C  CB   . ALA   A  1  166 ? 29.425  -22.138 -44.248  1.00 73.69  ? 166  ALA   A CB   1 
ATOM   2523  H  H    . ALA   A  1  166 ? 28.649  -21.058 -42.071  1.00 85.32  ? 166  ALA   A H    1 
ATOM   2524  H  HA   . ALA   A  1  166 ? 28.859  -20.203 -44.625  1.00 88.87  ? 166  ALA   A HA   1 
ATOM   2525  H  HB1  . ALA   A  1  166 ? 29.325  -22.435 -45.166  1.00 88.41  ? 166  ALA   A HB1  1 
ATOM   2526  H  HB2  . ALA   A  1  166 ? 30.351  -21.906 -44.075  1.00 88.41  ? 166  ALA   A HB2  1 
ATOM   2527  H  HB3  . ALA   A  1  166 ? 29.141  -22.838 -43.640  1.00 88.41  ? 166  ALA   A HB3  1 
ATOM   2528  N  N    . ASP   A  1  167 ? 26.154  -20.493 -43.786  1.00 77.14  ? 167  ASP   A N    1 
ATOM   2529  C  CA   . ASP   A  1  167 ? 24.735  -20.631 -44.117  1.00 79.61  ? 167  ASP   A CA   1 
ATOM   2530  C  C    . ASP   A  1  167 ? 24.247  -22.062 -43.898  1.00 72.87  ? 167  ASP   A C    1 
ATOM   2531  O  O    . ASP   A  1  167 ? 23.540  -22.638 -44.729  1.00 70.09  ? 167  ASP   A O    1 
ATOM   2532  C  CB   . ASP   A  1  167 ? 24.463  -20.169 -45.549  1.00 91.74  ? 167  ASP   A CB   1 
ATOM   2533  C  CG   . ASP   A  1  167 ? 24.515  -18.663 -45.694  1.00 102.82 ? 167  ASP   A CG   1 
ATOM   2534  O  OD1  . ASP   A  1  167 ? 23.984  -17.963 -44.808  1.00 104.98 ? 167  ASP   A OD1  1 
ATOM   2535  O  OD2  . ASP   A  1  167 ? 25.086  -18.178 -46.693  1.00 108.04 ? 167  ASP   A OD2  1 
ATOM   2536  H  H    . ASP   A  1  167 ? 26.309  -19.911 -43.172  1.00 92.55  ? 167  ASP   A H    1 
ATOM   2537  H  HA   . ASP   A  1  167 ? 24.225  -20.064 -43.518  1.00 95.51  ? 167  ASP   A HA   1 
ATOM   2538  H  HB2  . ASP   A  1  167 ? 25.132  -20.551 -46.138  1.00 110.07 ? 167  ASP   A HB2  1 
ATOM   2539  H  HB3  . ASP   A  1  167 ? 23.578  -20.466 -45.815  1.00 110.07 ? 167  ASP   A HB3  1 
ATOM   2540  N  N    . ARG   A  1  168 ? 24.633  -22.639 -42.767  1.00 70.34  ? 168  ARG   A N    1 
ATOM   2541  C  CA   . ARG   A  1  168 ? 24.038  -23.865 -42.261  1.00 64.57  ? 168  ARG   A CA   1 
ATOM   2542  C  C    . ARG   A  1  168 ? 23.259  -23.544 -40.993  1.00 64.00  ? 168  ARG   A C    1 
ATOM   2543  O  O    . ARG   A  1  168 ? 23.643  -22.665 -40.217  1.00 64.91  ? 168  ARG   A O    1 
ATOM   2544  C  CB   . ARG   A  1  168 ? 25.098  -24.931 -41.964  1.00 62.19  ? 168  ARG   A CB   1 
ATOM   2545  C  CG   . ARG   A  1  168 ? 24.978  -26.185 -42.825  1.00 61.03  ? 168  ARG   A CG   1 
ATOM   2546  C  CD   . ARG   A  1  168 ? 26.051  -27.214 -42.489  1.00 61.36  ? 168  ARG   A CD   1 
ATOM   2547  N  NE   . ARG   A  1  168 ? 26.083  -28.303 -43.463  1.00 62.35  ? 168  ARG   A NE   1 
ATOM   2548  C  CZ   . ARG   A  1  168 ? 25.273  -29.358 -43.443  1.00 61.09  ? 168  ARG   A CZ   1 
ATOM   2549  N  NH1  . ARG   A  1  168 ? 24.351  -29.483 -42.497  1.00 59.08  ? 168  ARG   A NH1  1 
ATOM   2550  N  NH2  . ARG   A  1  168 ? 25.384  -30.293 -44.377  1.00 62.44  ? 168  ARG   A NH2  1 
ATOM   2551  H  H    . ARG   A  1  168 ? 25.256  -22.329 -42.261  1.00 84.39  ? 168  ARG   A H    1 
ATOM   2552  H  HA   . ARG   A  1  168 ? 23.436  -24.237 -42.924  1.00 77.47  ? 168  ARG   A HA   1 
ATOM   2553  H  HB2  . ARG   A  1  168 ? 25.976  -24.548 -42.122  1.00 74.61  ? 168  ARG   A HB2  1 
ATOM   2554  H  HB3  . ARG   A  1  168 ? 25.016  -25.201 -41.037  1.00 74.61  ? 168  ARG   A HB3  1 
ATOM   2555  H  HG2  . ARG   A  1  168 ? 24.111  -26.593 -42.676  1.00 73.22  ? 168  ARG   A HG2  1 
ATOM   2556  H  HG3  . ARG   A  1  168 ? 25.075  -25.942 -43.759  1.00 73.22  ? 168  ARG   A HG3  1 
ATOM   2557  H  HD2  . ARG   A  1  168 ? 26.920  -26.782 -42.488  1.00 73.61  ? 168  ARG   A HD2  1 
ATOM   2558  H  HD3  . ARG   A  1  168 ? 25.868  -27.593 -41.615  1.00 73.61  ? 168  ARG   A HD3  1 
ATOM   2559  H  HE   . ARG   A  1  168 ? 26.667  -28.259 -44.093  1.00 74.80  ? 168  ARG   A HE   1 
ATOM   2560  H  HH11 . ARG   A  1  168 ? 24.273  -28.879 -41.890  1.00 70.88  ? 168  ARG   A HH11 1 
ATOM   2561  H  HH12 . ARG   A  1  168 ? 23.831  -30.168 -42.491  1.00 70.88  ? 168  ARG   A HH12 1 
ATOM   2562  H  HH21 . ARG   A  1  168 ? 25.978  -30.216 -44.994  1.00 74.91  ? 168  ARG   A HH21 1 
ATOM   2563  H  HH22 . ARG   A  1  168 ? 24.861  -30.976 -44.366  1.00 74.91  ? 168  ARG   A HH22 1 
ATOM   2564  N  N    . VAL   A  1  169 ? 22.156  -24.256 -40.793  1.00 63.45  ? 169  VAL   A N    1 
ATOM   2565  C  CA   . VAL   A  1  169 ? 21.321  -24.093 -39.609  1.00 59.84  ? 169  VAL   A CA   1 
ATOM   2566  C  C    . VAL   A  1  169 ? 21.697  -25.173 -38.608  1.00 57.73  ? 169  VAL   A C    1 
ATOM   2567  O  O    . VAL   A  1  169 ? 21.744  -26.358 -38.953  1.00 61.27  ? 169  VAL   A O    1 
ATOM   2568  C  CB   . VAL   A  1  169 ? 19.825  -24.170 -39.962  1.00 56.90  ? 169  VAL   A CB   1 
ATOM   2569  C  CG1  . VAL   A  1  169 ? 18.995  -24.418 -38.708  1.00 50.56  ? 169  VAL   A CG1  1 
ATOM   2570  C  CG2  . VAL   A  1  169 ? 19.380  -22.889 -40.645  1.00 60.06  ? 169  VAL   A CG2  1 
ATOM   2571  H  H    . VAL   A  1  169 ? 21.864  -24.851 -41.341  1.00 76.12  ? 169  VAL   A H    1 
ATOM   2572  H  HA   . VAL   A  1  169 ? 21.494  -23.226 -39.211  1.00 71.79  ? 169  VAL   A HA   1 
ATOM   2573  H  HB   . VAL   A  1  169 ? 19.683  -24.909 -40.573  1.00 68.26  ? 169  VAL   A HB   1 
ATOM   2574  H  HG11 . VAL   A  1  169 ? 18.072  -24.177 -38.888  1.00 60.66  ? 169  VAL   A HG11 1 
ATOM   2575  H  HG12 . VAL   A  1  169 ? 19.051  -25.357 -38.473  1.00 60.66  ? 169  VAL   A HG12 1 
ATOM   2576  H  HG13 . VAL   A  1  169 ? 19.344  -23.874 -37.985  1.00 60.66  ? 169  VAL   A HG13 1 
ATOM   2577  H  HG21 . VAL   A  1  169 ? 18.564  -23.063 -41.140  1.00 72.06  ? 169  VAL   A HG21 1 
ATOM   2578  H  HG22 . VAL   A  1  169 ? 19.220  -22.211 -39.970  1.00 72.06  ? 169  VAL   A HG22 1 
ATOM   2579  H  HG23 . VAL   A  1  169 ? 20.078  -22.595 -41.250  1.00 72.06  ? 169  VAL   A HG23 1 
ATOM   2580  N  N    . LEU   A  1  170 ? 21.978  -24.764 -37.375  1.00 55.65  ? 170  LEU   A N    1 
ATOM   2581  C  CA   . LEU   A  1  170 ? 22.189  -25.685 -36.266  1.00 55.35  ? 170  LEU   A CA   1 
ATOM   2582  C  C    . LEU   A  1  170 ? 20.947  -25.652 -35.389  1.00 57.05  ? 170  LEU   A C    1 
ATOM   2583  O  O    . LEU   A  1  170 ? 20.584  -24.595 -34.863  1.00 58.85  ? 170  LEU   A O    1 
ATOM   2584  C  CB   . LEU   A  1  170 ? 23.430  -25.314 -35.456  1.00 52.97  ? 170  LEU   A CB   1 
ATOM   2585  C  CG   . LEU   A  1  170 ? 23.641  -26.147 -34.188  1.00 52.26  ? 170  LEU   A CG   1 
ATOM   2586  C  CD1  . LEU   A  1  170 ? 23.724  -27.632 -34.520  1.00 51.34  ? 170  LEU   A CD1  1 
ATOM   2587  C  CD2  . LEU   A  1  170 ? 24.888  -25.698 -33.446  1.00 56.44  ? 170  LEU   A CD2  1 
ATOM   2588  H  H    . LEU   A  1  170 ? 22.054  -23.937 -37.151  1.00 66.76  ? 170  LEU   A H    1 
ATOM   2589  H  HA   . LEU   A  1  170 ? 22.321  -26.584 -36.607  1.00 66.40  ? 170  LEU   A HA   1 
ATOM   2590  H  HB2  . LEU   A  1  170 ? 24.212  -25.434 -36.019  1.00 63.55  ? 170  LEU   A HB2  1 
ATOM   2591  H  HB3  . LEU   A  1  170 ? 23.355  -24.385 -35.187  1.00 63.55  ? 170  LEU   A HB3  1 
ATOM   2592  H  HG   . LEU   A  1  170 ? 22.880  -26.013 -33.603  1.00 62.69  ? 170  LEU   A HG   1 
ATOM   2593  H  HD11 . LEU   A  1  170 ? 23.918  -28.127 -33.709  1.00 61.59  ? 170  LEU   A HD11 1 
ATOM   2594  H  HD12 . LEU   A  1  170 ? 22.874  -27.921 -34.888  1.00 61.59  ? 170  LEU   A HD12 1 
ATOM   2595  H  HD13 . LEU   A  1  170 ? 24.430  -27.772 -35.170  1.00 61.59  ? 170  LEU   A HD13 1 
ATOM   2596  H  HD21 . LEU   A  1  170 ? 25.020  -26.272 -32.675  1.00 67.71  ? 170  LEU   A HD21 1 
ATOM   2597  H  HD22 . LEU   A  1  170 ? 25.651  -25.764 -34.041  1.00 67.71  ? 170  LEU   A HD22 1 
ATOM   2598  H  HD23 . LEU   A  1  170 ? 24.771  -24.779 -33.159  1.00 67.71  ? 170  LEU   A HD23 1 
ATOM   2599  N  N    . LEU   A  1  171 ? 20.300  -26.804 -35.238  1.00 54.51  ? 171  LEU   A N    1 
ATOM   2600  C  CA   . LEU   A  1  171 ? 19.059  -26.914 -34.490  1.00 51.87  ? 171  LEU   A CA   1 
ATOM   2601  C  C    . LEU   A  1  171 ? 19.163  -28.068 -33.506  1.00 54.17  ? 171  LEU   A C    1 
ATOM   2602  O  O    . LEU   A  1  171 ? 19.798  -29.089 -33.784  1.00 57.65  ? 171  LEU   A O    1 
ATOM   2603  C  CB   . LEU   A  1  171 ? 17.866  -27.117 -35.435  1.00 50.88  ? 171  LEU   A CB   1 
ATOM   2604  C  CG   . LEU   A  1  171 ? 16.505  -27.406 -34.800  1.00 50.47  ? 171  LEU   A CG   1 
ATOM   2605  C  CD1  . LEU   A  1  171 ? 15.395  -26.900 -35.707  1.00 50.61  ? 171  LEU   A CD1  1 
ATOM   2606  C  CD2  . LEU   A  1  171 ? 16.322  -28.894 -34.517  1.00 48.09  ? 171  LEU   A CD2  1 
ATOM   2607  H  H    . LEU   A  1  171 ? 20.569  -27.551 -35.569  1.00 65.40  ? 171  LEU   A H    1 
ATOM   2608  H  HA   . LEU   A  1  171 ? 18.901  -26.106 -33.978  1.00 62.22  ? 171  LEU   A HA   1 
ATOM   2609  H  HB2  . LEU   A  1  171 ? 17.764  -26.309 -35.962  1.00 61.04  ? 171  LEU   A HB2  1 
ATOM   2610  H  HB3  . LEU   A  1  171 ? 18.071  -27.868 -36.014  1.00 61.04  ? 171  LEU   A HB3  1 
ATOM   2611  H  HG   . LEU   A  1  171 ? 16.454  -26.943 -33.949  1.00 60.55  ? 171  LEU   A HG   1 
ATOM   2612  H  HD11 . LEU   A  1  171 ? 14.539  -27.159 -35.332  1.00 60.71  ? 171  LEU   A HD11 1 
ATOM   2613  H  HD12 . LEU   A  1  171 ? 15.452  -25.933 -35.766  1.00 60.71  ? 171  LEU   A HD12 1 
ATOM   2614  H  HD13 . LEU   A  1  171 ? 15.504  -27.292 -36.587  1.00 60.71  ? 171  LEU   A HD13 1 
ATOM   2615  H  HD21 . LEU   A  1  171 ? 15.442  -29.167 -34.818  1.00 57.68  ? 171  LEU   A HD21 1 
ATOM   2616  H  HD22 . LEU   A  1  171 ? 17.004  -29.392 -34.995  1.00 57.68  ? 171  LEU   A HD22 1 
ATOM   2617  H  HD23 . LEU   A  1  171 ? 16.409  -29.047 -33.563  1.00 57.68  ? 171  LEU   A HD23 1 
ATOM   2618  N  N    . GLY   A  1  172 ? 18.542  -27.890 -32.353  1.00 52.21  ? 172  GLY   A N    1 
ATOM   2619  C  CA   . GLY   A  1  172 ? 18.581  -28.894 -31.303  1.00 51.92  ? 172  GLY   A CA   1 
ATOM   2620  C  C    . GLY   A  1  172 ? 17.202  -29.187 -30.758  1.00 54.68  ? 172  GLY   A C    1 
ATOM   2621  O  O    . GLY   A  1  172 ? 16.397  -28.280 -30.549  1.00 56.38  ? 172  GLY   A O    1 
ATOM   2622  H  H    . GLY   A  1  172 ? 18.085  -27.190 -32.151  1.00 62.63  ? 172  GLY   A H    1 
ATOM   2623  H  HA2  . GLY   A  1  172 ? 18.955  -29.717 -31.655  1.00 62.28  ? 172  GLY   A HA2  1 
ATOM   2624  H  HA3  . GLY   A  1  172 ? 19.139  -28.580 -30.575  1.00 62.28  ? 172  GLY   A HA3  1 
ATOM   2625  N  N    . GLY   A  1  173 ? 16.935  -30.472 -30.537  1.00 53.91  ? 173  GLY   A N    1 
ATOM   2626  C  CA   . GLY   A  1  173 ? 15.702  -30.903 -29.923  1.00 54.02  ? 173  GLY   A CA   1 
ATOM   2627  C  C    . GLY   A  1  173 ? 15.975  -31.852 -28.771  1.00 52.35  ? 173  GLY   A C    1 
ATOM   2628  O  O    . GLY   A  1  173 ? 16.458  -32.972 -28.969  1.00 52.79  ? 173  GLY   A O    1 
ATOM   2629  H  H    . GLY   A  1  173 ? 17.466  -31.117 -30.740  1.00 64.67  ? 173  GLY   A H    1 
ATOM   2630  H  HA2  . GLY   A  1  173 ? 15.218  -30.134 -29.585  1.00 64.80  ? 173  GLY   A HA2  1 
ATOM   2631  H  HA3  . GLY   A  1  173 ? 15.152  -31.359 -30.578  1.00 64.80  ? 173  GLY   A HA3  1 
ATOM   2632  N  N    . PRO   A  1  174 ? 15.658  -31.436 -27.541  1.00 51.29  ? 174  PRO   A N    1 
ATOM   2633  C  CA   . PRO   A  1  174 ? 16.074  -32.220 -26.371  1.00 51.62  ? 174  PRO   A CA   1 
ATOM   2634  C  C    . PRO   A  1  174 ? 15.255  -33.476 -26.123  1.00 51.51  ? 174  PRO   A C    1 
ATOM   2635  O  O    . PRO   A  1  174 ? 15.552  -34.200 -25.167  1.00 54.70  ? 174  PRO   A O    1 
ATOM   2636  C  CB   . PRO   A  1  174 ? 15.904  -31.224 -25.212  1.00 52.12  ? 174  PRO   A CB   1 
ATOM   2637  C  CG   . PRO   A  1  174 ? 14.814  -30.318 -25.662  1.00 53.69  ? 174  PRO   A CG   1 
ATOM   2638  C  CD   . PRO   A  1  174 ? 14.967  -30.190 -27.152  1.00 52.56  ? 174  PRO   A CD   1 
ATOM   2639  H  HA   . PRO   A  1  174 ? 17.009  -32.462 -26.453  1.00 61.93  ? 174  PRO   A HA   1 
ATOM   2640  H  HB2  . PRO   A  1  174 ? 15.654  -31.696 -24.402  1.00 62.53  ? 174  PRO   A HB2  1 
ATOM   2641  H  HB3  . PRO   A  1  174 ? 16.729  -30.735 -25.070  1.00 62.53  ? 174  PRO   A HB3  1 
ATOM   2642  H  HG2  . PRO   A  1  174 ? 13.954  -30.705 -25.438  1.00 64.41  ? 174  PRO   A HG2  1 
ATOM   2643  H  HG3  . PRO   A  1  174 ? 14.911  -29.453 -25.232  1.00 64.41  ? 174  PRO   A HG3  1 
ATOM   2644  H  HD2  . PRO   A  1  174 ? 14.100  -30.129 -27.582  1.00 63.05  ? 174  PRO   A HD2  1 
ATOM   2645  H  HD3  . PRO   A  1  174 ? 15.505  -29.414 -27.377  1.00 63.05  ? 174  PRO   A HD3  1 
ATOM   2646  N  N    . GLY   A  1  175 ? 14.252  -33.769 -26.945  1.00 50.91  ? 175  GLY   A N    1 
ATOM   2647  C  CA   . GLY   A  1  175 ? 13.346  -34.860 -26.645  1.00 52.47  ? 175  GLY   A CA   1 
ATOM   2648  C  C    . GLY   A  1  175 ? 13.526  -36.116 -27.475  1.00 52.01  ? 175  GLY   A C    1 
ATOM   2649  O  O    . GLY   A  1  175 ? 12.896  -37.140 -27.195  1.00 55.75  ? 175  GLY   A O    1 
ATOM   2650  H  H    . GLY   A  1  175 ? 14.080  -33.351 -27.676  1.00 61.07  ? 175  GLY   A H    1 
ATOM   2651  H  HA2  . GLY   A  1  175 ? 13.460  -35.108 -25.714  1.00 62.95  ? 175  GLY   A HA2  1 
ATOM   2652  H  HA3  . GLY   A  1  175 ? 12.436  -34.551 -26.780  1.00 62.95  ? 175  GLY   A HA3  1 
ATOM   2653  N  N    . SER   A  1  176 ? 14.381  -36.060 -28.493  1.00 47.62  ? 176  SER   A N    1 
ATOM   2654  C  CA   . SER   A  1  176 ? 14.544  -37.201 -29.384  1.00 52.16  ? 176  SER   A CA   1 
ATOM   2655  C  C    . SER   A  1  176 ? 15.096  -38.410 -28.636  1.00 52.72  ? 176  SER   A C    1 
ATOM   2656  O  O    . SER   A  1  176 ? 15.964  -38.285 -27.767  1.00 51.92  ? 176  SER   A O    1 
ATOM   2657  C  CB   . SER   A  1  176 ? 15.473  -36.840 -30.544  1.00 53.84  ? 176  SER   A CB   1 
ATOM   2658  O  OG   . SER   A  1  176 ? 14.896  -35.852 -31.379  1.00 52.23  ? 176  SER   A OG   1 
ATOM   2659  H  H    . SER   A  1  176 ? 14.873  -35.382 -28.686  1.00 57.12  ? 176  SER   A H    1 
ATOM   2660  H  HA   . SER   A  1  176 ? 13.676  -37.441 -29.745  1.00 62.57  ? 176  SER   A HA   1 
ATOM   2661  H  HB2  . SER   A  1  176 ? 16.306  -36.497 -30.183  1.00 64.59  ? 176  SER   A HB2  1 
ATOM   2662  H  HB3  . SER   A  1  176 ? 15.642  -37.636 -31.070  1.00 64.59  ? 176  SER   A HB3  1 
ATOM   2663  H  HG   . SER   A  1  176 ? 15.375  -35.736 -32.059  1.00 62.66  ? 176  SER   A HG   1 
ATOM   2664  N  N    . PHE   A  1  177 ? 14.579  -39.589 -28.984  1.00 53.23  ? 177  PHE   A N    1 
ATOM   2665  C  CA   . PHE   A  1  177 ? 15.110  -40.866 -28.510  1.00 55.57  ? 177  PHE   A CA   1 
ATOM   2666  C  C    . PHE   A  1  177 ? 15.062  -40.954 -26.983  1.00 56.78  ? 177  PHE   A C    1 
ATOM   2667  O  O    . PHE   A  1  177 ? 16.083  -41.071 -26.303  1.00 56.38  ? 177  PHE   A O    1 
ATOM   2668  C  CB   . PHE   A  1  177 ? 16.535  -41.072 -29.032  1.00 55.69  ? 177  PHE   A CB   1 
ATOM   2669  C  CG   . PHE   A  1  177 ? 16.716  -40.661 -30.465  1.00 56.07  ? 177  PHE   A CG   1 
ATOM   2670  C  CD1  . PHE   A  1  177 ? 15.776  -41.004 -31.423  1.00 56.34  ? 177  PHE   A CD1  1 
ATOM   2671  C  CD2  . PHE   A  1  177 ? 17.818  -39.917 -30.852  1.00 55.20  ? 177  PHE   A CD2  1 
ATOM   2672  C  CE1  . PHE   A  1  177 ? 15.939  -40.624 -32.742  1.00 56.38  ? 177  PHE   A CE1  1 
ATOM   2673  C  CE2  . PHE   A  1  177 ? 17.985  -39.532 -32.170  1.00 53.78  ? 177  PHE   A CE2  1 
ATOM   2674  C  CZ   . PHE   A  1  177 ? 17.044  -39.885 -33.115  1.00 55.46  ? 177  PHE   A CZ   1 
ATOM   2675  H  H    . PHE   A  1  177 ? 13.903  -39.676 -29.509  1.00 63.86  ? 177  PHE   A H    1 
ATOM   2676  H  HA   . PHE   A  1  177 ? 14.549  -41.579 -28.853  1.00 66.66  ? 177  PHE   A HA   1 
ATOM   2677  H  HB2  . PHE   A  1  177 ? 17.144  -40.544 -28.493  1.00 66.81  ? 177  PHE   A HB2  1 
ATOM   2678  H  HB3  . PHE   A  1  177 ? 16.760  -42.013 -28.963  1.00 66.81  ? 177  PHE   A HB3  1 
ATOM   2679  H  HD1  . PHE   A  1  177 ? 15.027  -41.497 -31.176  1.00 67.59  ? 177  PHE   A HD1  1 
ATOM   2680  H  HD2  . PHE   A  1  177 ? 18.454  -39.674 -30.219  1.00 66.22  ? 177  PHE   A HD2  1 
ATOM   2681  H  HE1  . PHE   A  1  177 ? 15.304  -40.864 -33.378  1.00 67.63  ? 177  PHE   A HE1  1 
ATOM   2682  H  HE2  . PHE   A  1  177 ? 18.731  -39.035 -32.418  1.00 64.52  ? 177  PHE   A HE2  1 
ATOM   2683  H  HZ   . PHE   A  1  177 ? 17.155  -39.627 -34.001  1.00 66.53  ? 177  PHE   A HZ   1 
ATOM   2684  N  N    . TYR   A  1  178 ? 13.841  -40.911 -26.455  1.00 53.34  ? 178  TYR   A N    1 
ATOM   2685  C  CA   . TYR   A  1  178 ? 13.605  -40.929 -25.013  1.00 54.33  ? 178  TYR   A CA   1 
ATOM   2686  C  C    . TYR   A  1  178 ? 14.446  -39.862 -24.316  1.00 49.85  ? 178  TYR   A C    1 
ATOM   2687  O  O    . TYR   A  1  178 ? 15.144  -40.114 -23.331  1.00 48.51  ? 178  TYR   A O    1 
ATOM   2688  C  CB   . TYR   A  1  178 ? 13.864  -42.319 -24.431  1.00 56.74  ? 178  TYR   A CB   1 
ATOM   2689  C  CG   . TYR   A  1  178 ? 12.644  -43.208 -24.497  1.00 63.34  ? 178  TYR   A CG   1 
ATOM   2690  C  CD1  . TYR   A  1  178 ? 11.538  -42.953 -23.699  1.00 67.71  ? 178  TYR   A CD1  1 
ATOM   2691  C  CD2  . TYR   A  1  178 ? 12.591  -44.294 -25.361  1.00 66.82  ? 178  TYR   A CD2  1 
ATOM   2692  C  CE1  . TYR   A  1  178 ? 10.416  -43.752 -23.754  1.00 71.61  ? 178  TYR   A CE1  1 
ATOM   2693  C  CE2  . TYR   A  1  178 ? 11.470  -45.104 -25.422  1.00 70.07  ? 178  TYR   A CE2  1 
ATOM   2694  C  CZ   . TYR   A  1  178 ? 10.386  -44.827 -24.616  1.00 73.53  ? 178  TYR   A CZ   1 
ATOM   2695  O  OH   . TYR   A  1  178 ? 9.265   -45.625 -24.669  1.00 77.97  ? 178  TYR   A OH   1 
ATOM   2696  H  H    . TYR   A  1  178 ? 13.118  -40.871 -26.921  1.00 63.99  ? 178  TYR   A H    1 
ATOM   2697  H  HA   . TYR   A  1  178 ? 12.673  -40.716 -24.849  1.00 65.17  ? 178  TYR   A HA   1 
ATOM   2698  H  HB2  . TYR   A  1  178 ? 14.576  -42.745 -24.933  1.00 68.07  ? 178  TYR   A HB2  1 
ATOM   2699  H  HB3  . TYR   A  1  178 ? 14.122  -42.230 -23.500  1.00 68.07  ? 178  TYR   A HB3  1 
ATOM   2700  H  HD1  . TYR   A  1  178 ? 11.554  -42.228 -23.115  1.00 81.23  ? 178  TYR   A HD1  1 
ATOM   2701  H  HD2  . TYR   A  1  178 ? 13.321  -44.481 -25.907  1.00 80.16  ? 178  TYR   A HD2  1 
ATOM   2702  H  HE1  . TYR   A  1  178 ? 9.683   -43.567 -23.212  1.00 85.91  ? 178  TYR   A HE1  1 
ATOM   2703  H  HE2  . TYR   A  1  178 ? 11.448  -45.829 -26.003  1.00 84.07  ? 178  TYR   A HE2  1 
ATOM   2704  H  HH   . TYR   A  1  178 ? 9.350   -46.199 -25.276  1.00 93.54  ? 178  TYR   A HH   1 
ATOM   2705  N  N    . TRP   A  1  179 ? 14.369  -38.646 -24.854  1.00 48.65  ? 179  TRP   A N    1 
ATOM   2706  C  CA   . TRP   A  1  179 ? 15.000  -37.461 -24.282  1.00 50.66  ? 179  TRP   A CA   1 
ATOM   2707  C  C    . TRP   A  1  179 ? 16.514  -37.598 -24.178  1.00 50.98  ? 179  TRP   A C    1 
ATOM   2708  O  O    . TRP   A  1  179 ? 17.146  -36.941 -23.344  1.00 47.88  ? 179  TRP   A O    1 
ATOM   2709  C  CB   . TRP   A  1  179 ? 14.387  -37.124 -22.919  1.00 49.78  ? 179  TRP   A CB   1 
ATOM   2710  C  CG   . TRP   A  1  179 ? 12.965  -36.676 -23.054  1.00 48.93  ? 179  TRP   A CG   1 
ATOM   2711  C  CD1  . TRP   A  1  179 ? 12.522  -35.397 -23.211  1.00 49.60  ? 179  TRP   A CD1  1 
ATOM   2712  C  CD2  . TRP   A  1  179 ? 11.800  -37.510 -23.072  1.00 50.22  ? 179  TRP   A CD2  1 
ATOM   2713  N  NE1  . TRP   A  1  179 ? 11.152  -35.380 -23.320  1.00 50.92  ? 179  TRP   A NE1  1 
ATOM   2714  C  CE2  . TRP   A  1  179 ? 10.685  -36.666 -23.236  1.00 50.52  ? 179  TRP   A CE2  1 
ATOM   2715  C  CE3  . TRP   A  1  179 ? 11.592  -38.889 -22.961  1.00 51.30  ? 179  TRP   A CE3  1 
ATOM   2716  C  CZ2  . TRP   A  1  179 ? 9.380   -37.153 -23.289  1.00 53.39  ? 179  TRP   A CZ2  1 
ATOM   2717  C  CZ3  . TRP   A  1  179 ? 10.295  -39.372 -23.014  1.00 55.05  ? 179  TRP   A CZ3  1 
ATOM   2718  C  CH2  . TRP   A  1  179 ? 9.206   -38.506 -23.178  1.00 55.03  ? 179  TRP   A CH2  1 
ATOM   2719  H  H    . TRP   A  1  179 ? 13.939  -38.477 -25.579  1.00 58.36  ? 179  TRP   A H    1 
ATOM   2720  H  HA   . TRP   A  1  179 ? 14.835  -36.711 -24.874  1.00 60.77  ? 179  TRP   A HA   1 
ATOM   2721  H  HB2  . TRP   A  1  179 ? 14.407  -37.912 -22.354  1.00 59.71  ? 179  TRP   A HB2  1 
ATOM   2722  H  HB3  . TRP   A  1  179 ? 14.895  -36.408 -22.506  1.00 59.71  ? 179  TRP   A HB3  1 
ATOM   2723  H  HD1  . TRP   A  1  179 ? 13.067  -34.644 -23.240  1.00 59.50  ? 179  TRP   A HD1  1 
ATOM   2724  H  HE1  . TRP   A  1  179 ? 10.667  -34.678 -23.424  1.00 61.09  ? 179  TRP   A HE1  1 
ATOM   2725  H  HE3  . TRP   A  1  179 ? 12.311  -39.470 -22.854  1.00 61.54  ? 179  TRP   A HE3  1 
ATOM   2726  H  HZ2  . TRP   A  1  179 ? 8.655   -36.580 -23.396  1.00 64.05  ? 179  TRP   A HZ2  1 
ATOM   2727  H  HZ3  . TRP   A  1  179 ? 10.144  -40.286 -22.940  1.00 66.04  ? 179  TRP   A HZ3  1 
ATOM   2728  H  HH2  . TRP   A  1  179 ? 8.346   -38.858 -23.213  1.00 66.02  ? 179  TRP   A HH2  1 
ATOM   2729  N  N    . GLN   A  1  180 ? 17.111  -38.445 -25.018  1.00 52.81  ? 180  GLN   A N    1 
ATOM   2730  C  CA   . GLN   A  1  180 ? 18.546  -38.349 -25.246  1.00 52.44  ? 180  GLN   A CA   1 
ATOM   2731  C  C    . GLN   A  1  180 ? 18.905  -36.996 -25.837  1.00 51.75  ? 180  GLN   A C    1 
ATOM   2732  O  O    . GLN   A  1  180 ? 19.994  -36.471 -25.581  1.00 55.63  ? 180  GLN   A O    1 
ATOM   2733  C  CB   . GLN   A  1  180 ? 19.017  -39.465 -26.181  1.00 54.05  ? 180  GLN   A CB   1 
ATOM   2734  C  CG   . GLN   A  1  180 ? 19.026  -40.852 -25.564  1.00 55.75  ? 180  GLN   A CG   1 
ATOM   2735  C  CD   . GLN   A  1  180 ? 19.498  -41.917 -26.538  1.00 55.95  ? 180  GLN   A CD   1 
ATOM   2736  O  OE1  . GLN   A  1  180 ? 20.079  -41.609 -27.580  1.00 57.07  ? 180  GLN   A OE1  1 
ATOM   2737  N  NE2  . GLN   A  1  180 ? 19.248  -43.178 -26.204  1.00 58.27  ? 180  GLN   A NE2  1 
ATOM   2738  H  H    . GLN   A  1  180 ? 16.715  -39.069 -25.458  1.00 63.35  ? 180  GLN   A H    1 
ATOM   2739  H  HA   . GLN   A  1  180 ? 19.007  -38.460 -24.399  1.00 62.91  ? 180  GLN   A HA   1 
ATOM   2740  H  HB2  . GLN   A  1  180 ? 18.426  -39.492 -26.950  1.00 64.84  ? 180  GLN   A HB2  1 
ATOM   2741  H  HB3  . GLN   A  1  180 ? 19.923  -39.266 -26.465  1.00 64.84  ? 180  GLN   A HB3  1 
ATOM   2742  H  HG2  . GLN   A  1  180 ? 19.625  -40.856 -24.800  1.00 66.88  ? 180  GLN   A HG2  1 
ATOM   2743  H  HG3  . GLN   A  1  180 ? 18.127  -41.080 -25.281  1.00 66.88  ? 180  GLN   A HG3  1 
ATOM   2744  H  HE21 . GLN   A  1  180 ? 18.839  -43.355 -25.469  1.00 69.90  ? 180  GLN   A HE21 1 
ATOM   2745  H  HE22 . GLN   A  1  180 ? 19.496  -43.817 -26.724  1.00 69.90  ? 180  GLN   A HE22 1 
ATOM   2746  N  N    . GLY   A  1  181 ? 17.999  -36.417 -26.620  1.00 53.86  ? 181  GLY   A N    1 
ATOM   2747  C  CA   . GLY   A  1  181 ? 18.270  -35.193 -27.340  1.00 56.26  ? 181  GLY   A CA   1 
ATOM   2748  C  C    . GLY   A  1  181 ? 18.931  -35.467 -28.677  1.00 56.38  ? 181  GLY   A C    1 
ATOM   2749  O  O    . GLY   A  1  181 ? 19.404  -36.568 -28.968  1.00 60.17  ? 181  GLY   A O    1 
ATOM   2750  H  H    . GLY   A  1  181 ? 17.207  -36.725 -26.749  1.00 64.61  ? 181  GLY   A H    1 
ATOM   2751  H  HA2  . GLY   A  1  181 ? 17.439  -34.719 -27.497  1.00 67.50  ? 181  GLY   A HA2  1 
ATOM   2752  H  HA3  . GLY   A  1  181 ? 18.860  -34.632 -26.813  1.00 67.50  ? 181  GLY   A HA3  1 
ATOM   2753  N  N    . GLN   A  1  182 ? 18.964  -34.431 -29.508  1.00 53.32  ? 182  GLN   A N    1 
ATOM   2754  C  CA   . GLN   A  1  182 ? 19.454  -34.587 -30.868  1.00 52.12  ? 182  GLN   A CA   1 
ATOM   2755  C  C    . GLN   A  1  182 ? 19.893  -33.234 -31.403  1.00 54.04  ? 182  GLN   A C    1 
ATOM   2756  O  O    . GLN   A  1  182 ? 19.311  -32.199 -31.069  1.00 54.13  ? 182  GLN   A O    1 
ATOM   2757  C  CB   . GLN   A  1  182 ? 18.373  -35.196 -31.770  1.00 48.57  ? 182  GLN   A CB   1 
ATOM   2758  C  CG   . GLN   A  1  182 ? 18.820  -35.508 -33.186  1.00 49.37  ? 182  GLN   A CG   1 
ATOM   2759  C  CD   . GLN   A  1  182 ? 17.726  -36.172 -34.002  1.00 50.48  ? 182  GLN   A CD   1 
ATOM   2760  O  OE1  . GLN   A  1  182 ? 16.538  -35.960 -33.757  1.00 47.94  ? 182  GLN   A OE1  1 
ATOM   2761  N  NE2  . GLN   A  1  182 ? 18.122  -36.987 -34.973  1.00 54.00  ? 182  GLN   A NE2  1 
ATOM   2762  H  H    . GLN   A  1  182 ? 18.710  -33.634 -29.308  1.00 63.96  ? 182  GLN   A H    1 
ATOM   2763  H  HA   . GLN   A  1  182 ? 20.230  -35.170 -30.870  1.00 62.52  ? 182  GLN   A HA   1 
ATOM   2764  H  HB2  . GLN   A  1  182 ? 18.072  -36.026 -31.370  1.00 58.26  ? 182  GLN   A HB2  1 
ATOM   2765  H  HB3  . GLN   A  1  182 ? 17.635  -34.569 -31.829  1.00 58.26  ? 182  GLN   A HB3  1 
ATOM   2766  H  HG2  . GLN   A  1  182 ? 19.069  -34.683 -33.630  1.00 59.23  ? 182  GLN   A HG2  1 
ATOM   2767  H  HG3  . GLN   A  1  182 ? 19.580  -36.110 -33.154  1.00 59.23  ? 182  GLN   A HG3  1 
ATOM   2768  H  HE21 . GLN   A  1  182 ? 18.962  -37.114 -35.111  1.00 64.78  ? 182  GLN   A HE21 1 
ATOM   2769  H  HE22 . GLN   A  1  182 ? 17.540  -37.387 -35.463  1.00 64.78  ? 182  GLN   A HE22 1 
ATOM   2770  N  N    . LEU   A  1  183 ? 20.937  -33.259 -32.225  1.00 52.68  ? 183  LEU   A N    1 
ATOM   2771  C  CA   . LEU   A  1  183 ? 21.350  -32.111 -33.014  1.00 51.79  ? 183  LEU   A CA   1 
ATOM   2772  C  C    . LEU   A  1  183 ? 21.121  -32.425 -34.485  1.00 52.86  ? 183  LEU   A C    1 
ATOM   2773  O  O    . LEU   A  1  183 ? 21.412  -33.534 -34.943  1.00 54.50  ? 183  LEU   A O    1 
ATOM   2774  C  CB   . LEU   A  1  183 ? 22.823  -31.766 -32.778  1.00 52.78  ? 183  LEU   A CB   1 
ATOM   2775  C  CG   . LEU   A  1  183 ? 23.231  -31.373 -31.357  1.00 53.38  ? 183  LEU   A CG   1 
ATOM   2776  C  CD1  . LEU   A  1  183 ? 24.692  -30.942 -31.337  1.00 55.38  ? 183  LEU   A CD1  1 
ATOM   2777  C  CD2  . LEU   A  1  183 ? 22.341  -30.271 -30.805  1.00 50.87  ? 183  LEU   A CD2  1 
ATOM   2778  H  H    . LEU   A  1  183 ? 21.433  -33.951 -32.344  1.00 63.20  ? 183  LEU   A H    1 
ATOM   2779  H  HA   . LEU   A  1  183 ? 20.827  -31.333 -32.767  1.00 62.13  ? 183  LEU   A HA   1 
ATOM   2780  H  HB2  . LEU   A  1  183 ? 23.353  -32.542 -33.019  1.00 63.31  ? 183  LEU   A HB2  1 
ATOM   2781  H  HB3  . LEU   A  1  183 ? 23.049  -31.018 -33.353  1.00 63.31  ? 183  LEU   A HB3  1 
ATOM   2782  H  HG   . LEU   A  1  183 ? 23.124  -32.143 -30.778  1.00 64.04  ? 183  LEU   A HG   1 
ATOM   2783  H  HD11 . LEU   A  1  183 ? 24.952  -30.751 -30.422  1.00 66.43  ? 183  LEU   A HD11 1 
ATOM   2784  H  HD12 . LEU   A  1  183 ? 25.238  -31.661 -31.693  1.00 66.43  ? 183  LEU   A HD12 1 
ATOM   2785  H  HD13 . LEU   A  1  183 ? 24.795  -30.147 -31.883  1.00 66.43  ? 183  LEU   A HD13 1 
ATOM   2786  H  HD21 . LEU   A  1  183 ? 22.662  -30.017 -29.925  1.00 61.03  ? 183  LEU   A HD21 1 
ATOM   2787  H  HD22 . LEU   A  1  183 ? 22.376  -29.508 -31.402  1.00 61.03  ? 183  LEU   A HD22 1 
ATOM   2788  H  HD23 . LEU   A  1  183 ? 21.431  -30.601 -30.742  1.00 61.03  ? 183  LEU   A HD23 1 
ATOM   2789  N  N    . ILE   A  1  184 ? 20.583  -31.454 -35.218  1.00 50.85  ? 184  ILE   A N    1 
ATOM   2790  C  CA   . ILE   A  1  184 ? 20.352  -31.586 -36.651  1.00 49.30  ? 184  ILE   A CA   1 
ATOM   2791  C  C    . ILE   A  1  184 ? 20.859  -30.323 -37.329  1.00 50.08  ? 184  ILE   A C    1 
ATOM   2792  O  O    . ILE   A  1  184 ? 20.582  -29.211 -36.865  1.00 55.12  ? 184  ILE   A O    1 
ATOM   2793  C  CB   . ILE   A  1  184 ? 18.865  -31.819 -36.980  1.00 48.67  ? 184  ILE   A CB   1 
ATOM   2794  C  CG1  . ILE   A  1  184 ? 18.371  -33.104 -36.309  1.00 48.41  ? 184  ILE   A CG1  1 
ATOM   2795  C  CG2  . ILE   A  1  184 ? 18.658  -31.897 -38.492  1.00 47.99  ? 184  ILE   A CG2  1 
ATOM   2796  C  CD1  . ILE   A  1  184 ? 16.888  -33.356 -36.474  1.00 46.60  ? 184  ILE   A CD1  1 
ATOM   2797  H  H    . ILE   A  1  184 ? 20.339  -30.694 -34.900  1.00 61.00  ? 184  ILE   A H    1 
ATOM   2798  H  HA   . ILE   A  1  184 ? 20.856  -32.343 -36.990  1.00 59.14  ? 184  ILE   A HA   1 
ATOM   2799  H  HB   . ILE   A  1  184 ? 18.353  -31.070 -36.635  1.00 58.39  ? 184  ILE   A HB   1 
ATOM   2800  H  HG12 . ILE   A  1  184 ? 18.843  -33.857 -36.697  1.00 58.07  ? 184  ILE   A HG12 1 
ATOM   2801  H  HG13 . ILE   A  1  184 ? 18.557  -33.049 -35.359  1.00 58.07  ? 184  ILE   A HG13 1 
ATOM   2802  H  HG21 . ILE   A  1  184 ? 17.716  -32.034 -38.676  1.00 57.57  ? 184  ILE   A HG21 1 
ATOM   2803  H  HG22 . ILE   A  1  184 ? 18.955  -31.066 -38.895  1.00 57.57  ? 184  ILE   A HG22 1 
ATOM   2804  H  HG23 . ILE   A  1  184 ? 19.175  -32.638 -38.844  1.00 57.57  ? 184  ILE   A HG23 1 
ATOM   2805  H  HD11 . ILE   A  1  184 ? 16.638  -34.131 -35.946  1.00 55.90  ? 184  ILE   A HD11 1 
ATOM   2806  H  HD12 . ILE   A  1  184 ? 16.399  -32.576 -36.168  1.00 55.90  ? 184  ILE   A HD12 1 
ATOM   2807  H  HD13 . ILE   A  1  184 ? 16.697  -33.519 -37.411  1.00 55.90  ? 184  ILE   A HD13 1 
ATOM   2808  N  N    . SER   A  1  185 ? 21.600  -30.495 -38.421  1.00 50.35  ? 185  SER   A N    1 
ATOM   2809  C  CA   . SER   A  1  185 ? 22.122  -29.380 -39.198  1.00 53.83  ? 185  SER   A CA   1 
ATOM   2810  C  C    . SER   A  1  185 ? 21.726  -29.558 -40.656  1.00 56.38  ? 185  SER   A C    1 
ATOM   2811  O  O    . SER   A  1  185 ? 21.969  -30.616 -41.245  1.00 58.46  ? 185  SER   A O    1 
ATOM   2812  C  CB   . SER   A  1  185 ? 23.645  -29.272 -39.072  1.00 54.27  ? 185  SER   A CB   1 
ATOM   2813  O  OG   . SER   A  1  185 ? 24.146  -28.222 -39.882  1.00 55.99  ? 185  SER   A OG   1 
ATOM   2814  H  H    . SER   A  1  185 ? 21.817  -31.265 -38.736  1.00 60.40  ? 185  SER   A H    1 
ATOM   2815  H  HA   . SER   A  1  185 ? 21.731  -28.553 -38.875  1.00 64.58  ? 185  SER   A HA   1 
ATOM   2816  H  HB2  . SER   A  1  185 ? 23.873  -29.093 -38.146  1.00 65.10  ? 185  SER   A HB2  1 
ATOM   2817  H  HB3  . SER   A  1  185 ? 24.046  -30.109 -39.356  1.00 65.10  ? 185  SER   A HB3  1 
ATOM   2818  H  HG   . SER   A  1  185 ? 24.967  -28.115 -39.740  1.00 67.17  ? 185  SER   A HG   1 
ATOM   2819  N  N    . ASP   A  1  186 ? 21.124  -28.520 -41.233  1.00 55.98  ? 186  ASP   A N    1 
ATOM   2820  C  CA   . ASP   A  1  186 ? 20.679  -28.539 -42.617  1.00 59.81  ? 186  ASP   A CA   1 
ATOM   2821  C  C    . ASP   A  1  186 ? 21.131  -27.269 -43.321  1.00 60.56  ? 186  ASP   A C    1 
ATOM   2822  O  O    . ASP   A  1  186 ? 21.202  -26.194 -42.719  1.00 64.08  ? 186  ASP   A O    1 
ATOM   2823  C  CB   . ASP   A  1  186 ? 19.151  -28.672 -42.713  1.00 62.46  ? 186  ASP   A CB   1 
ATOM   2824  C  CG   . ASP   A  1  186 ? 18.686  -30.116 -42.651  1.00 61.88  ? 186  ASP   A CG   1 
ATOM   2825  O  OD1  . ASP   A  1  186 ? 19.142  -30.925 -43.486  1.00 62.87  ? 186  ASP   A OD1  1 
ATOM   2826  O  OD2  . ASP   A  1  186 ? 17.874  -30.444 -41.761  1.00 58.36  ? 186  ASP   A OD2  1 
ATOM   2827  H  H    . ASP   A  1  186 ? 20.959  -27.778 -40.831  1.00 67.16  ? 186  ASP   A H    1 
ATOM   2828  H  HA   . ASP   A  1  186 ? 21.080  -29.294 -43.075  1.00 71.75  ? 186  ASP   A HA   1 
ATOM   2829  H  HB2  . ASP   A  1  186 ? 18.745  -28.193 -41.974  1.00 74.93  ? 186  ASP   A HB2  1 
ATOM   2830  H  HB3  . ASP   A  1  186 ? 18.853  -28.296 -43.556  1.00 74.93  ? 186  ASP   A HB3  1 
ATOM   2831  N  N    . GLN   A  1  187 ? 21.442  -27.409 -44.607  1.00 56.51  ? 187  GLN   A N    1 
ATOM   2832  C  CA   . GLN   A  1  187 ? 21.808  -26.259 -45.420  1.00 55.59  ? 187  GLN   A CA   1 
ATOM   2833  C  C    . GLN   A  1  187 ? 20.561  -25.446 -45.742  1.00 56.81  ? 187  GLN   A C    1 
ATOM   2834  O  O    . GLN   A  1  187 ? 19.550  -25.999 -46.185  1.00 59.09  ? 187  GLN   A O    1 
ATOM   2835  C  CB   . GLN   A  1  187 ? 22.485  -26.719 -46.710  1.00 58.32  ? 187  GLN   A CB   1 
ATOM   2836  C  CG   . GLN   A  1  187 ? 23.698  -27.611 -46.500  1.00 64.63  ? 187  GLN   A CG   1 
ATOM   2837  C  CD   . GLN   A  1  187 ? 24.169  -28.263 -47.786  1.00 68.85  ? 187  GLN   A CD   1 
ATOM   2838  O  OE1  . GLN   A  1  187 ? 23.376  -28.530 -48.689  1.00 66.68  ? 187  GLN   A OE1  1 
ATOM   2839  N  NE2  . GLN   A  1  187 ? 25.468  -28.522 -47.875  1.00 75.49  ? 187  GLN   A NE2  1 
ATOM   2840  H  H    . GLN   A  1  187 ? 21.448  -28.158 -45.029  1.00 67.80  ? 187  GLN   A H    1 
ATOM   2841  H  HA   . GLN   A  1  187 ? 22.434  -25.698 -44.936  1.00 66.68  ? 187  GLN   A HA   1 
ATOM   2842  H  HB2  . GLN   A  1  187 ? 21.841  -27.219 -47.236  1.00 69.97  ? 187  GLN   A HB2  1 
ATOM   2843  H  HB3  . GLN   A  1  187 ? 22.778  -25.936 -47.202  1.00 69.97  ? 187  GLN   A HB3  1 
ATOM   2844  H  HG2  . GLN   A  1  187 ? 24.427  -27.076 -46.148  1.00 77.53  ? 187  GLN   A HG2  1 
ATOM   2845  H  HG3  . GLN   A  1  187 ? 23.469  -28.314 -45.872  1.00 77.53  ? 187  GLN   A HG3  1 
ATOM   2846  H  HE21 . GLN   A  1  187 ? 25.992  -28.320 -47.224  1.00 90.57  ? 187  GLN   A HE21 1 
ATOM   2847  H  HE22 . GLN   A  1  187 ? 25.785  -28.891 -48.584  1.00 90.57  ? 187  GLN   A HE22 1 
ATOM   2848  N  N    . VAL   A  1  188 ? 20.629  -24.130 -45.516  1.00 55.25  ? 188  VAL   A N    1 
ATOM   2849  C  CA   . VAL   A  1  188 ? 19.478  -23.280 -45.811  1.00 57.99  ? 188  VAL   A CA   1 
ATOM   2850  C  C    . VAL   A  1  188 ? 19.045  -23.460 -47.259  1.00 59.19  ? 188  VAL   A C    1 
ATOM   2851  O  O    . VAL   A  1  188 ? 17.851  -23.385 -47.574  1.00 62.50  ? 188  VAL   A O    1 
ATOM   2852  C  CB   . VAL   A  1  188 ? 19.791  -21.800 -45.499  1.00 63.89  ? 188  VAL   A CB   1 
ATOM   2853  C  CG1  . VAL   A  1  188 ? 20.141  -21.626 -44.026  1.00 63.68  ? 188  VAL   A CG1  1 
ATOM   2854  C  CG2  . VAL   A  1  188 ? 20.911  -21.279 -46.390  1.00 70.78  ? 188  VAL   A CG2  1 
ATOM   2855  H  H    . VAL   A  1  188 ? 21.313  -23.717 -45.200  1.00 66.28  ? 188  VAL   A H    1 
ATOM   2856  H  HA   . VAL   A  1  188 ? 18.746  -23.550 -45.235  1.00 69.57  ? 188  VAL   A HA   1 
ATOM   2857  H  HB   . VAL   A  1  188 ? 19.000  -21.272 -45.684  1.00 76.65  ? 188  VAL   A HB   1 
ATOM   2858  H  HG11 . VAL   A  1  188 ? 20.292  -20.685 -43.847  1.00 76.39  ? 188  VAL   A HG11 1 
ATOM   2859  H  HG12 . VAL   A  1  188 ? 19.404  -21.951 -43.486  1.00 76.39  ? 188  VAL   A HG12 1 
ATOM   2860  H  HG13 . VAL   A  1  188 ? 20.944  -22.134 -43.830  1.00 76.39  ? 188  VAL   A HG13 1 
ATOM   2861  H  HG21 . VAL   A  1  188 ? 21.122  -20.368 -46.132  1.00 84.92  ? 188  VAL   A HG21 1 
ATOM   2862  H  HG22 . VAL   A  1  188 ? 21.692  -21.843 -46.279  1.00 84.92  ? 188  VAL   A HG22 1 
ATOM   2863  H  HG23 . VAL   A  1  188 ? 20.616  -21.301 -47.314  1.00 84.92  ? 188  VAL   A HG23 1 
ATOM   2864  N  N    . ALA   A  1  189 ? 19.999  -23.708 -48.159  1.00 61.05  ? 189  ALA   A N    1 
ATOM   2865  C  CA   . ALA   A  1  189 ? 19.646  -23.957 -49.552  1.00 63.63  ? 189  ALA   A CA   1 
ATOM   2866  C  C    . ALA   A  1  189 ? 18.748  -25.181 -49.678  1.00 66.97  ? 189  ALA   A C    1 
ATOM   2867  O  O    . ALA   A  1  189 ? 17.756  -25.160 -50.416  1.00 71.44  ? 189  ALA   A O    1 
ATOM   2868  C  CB   . ALA   A  1  189 ? 20.911  -24.128 -50.393  1.00 60.39  ? 189  ALA   A CB   1 
ATOM   2869  H  H    . ALA   A  1  189 ? 20.842  -23.737 -47.991  1.00 73.23  ? 189  ALA   A H    1 
ATOM   2870  H  HA   . ALA   A  1  189 ? 19.162  -23.189 -49.896  1.00 76.34  ? 189  ALA   A HA   1 
ATOM   2871  H  HB1  . ALA   A  1  189 ? 20.658  -24.297 -51.314  1.00 72.45  ? 189  ALA   A HB1  1 
ATOM   2872  H  HB2  . ALA   A  1  189 ? 21.439  -23.316 -50.339  1.00 72.45  ? 189  ALA   A HB2  1 
ATOM   2873  H  HB3  . ALA   A  1  189 ? 21.421  -24.878 -50.048  1.00 72.45  ? 189  ALA   A HB3  1 
ATOM   2874  N  N    . GLU   A  1  190 ? 19.078  -26.258 -48.962  1.00 66.13  ? 190  GLU   A N    1 
ATOM   2875  C  CA   . GLU   A  1  190 ? 18.209  -27.431 -48.950  1.00 63.00  ? 190  GLU   A CA   1 
ATOM   2876  C  C    . GLU   A  1  190 ? 16.856  -27.099 -48.333  1.00 60.93  ? 190  GLU   A C    1 
ATOM   2877  O  O    . GLU   A  1  190 ? 15.806  -27.456 -48.879  1.00 60.02  ? 190  GLU   A O    1 
ATOM   2878  C  CB   . GLU   A  1  190 ? 18.876  -28.572 -48.180  1.00 62.71  ? 190  GLU   A CB   1 
ATOM   2879  C  CG   . GLU   A  1  190 ? 19.948  -29.322 -48.949  1.00 66.96  ? 190  GLU   A CG   1 
ATOM   2880  C  CD   . GLU   A  1  190 ? 19.380  -30.165 -50.065  1.00 70.44  ? 190  GLU   A CD   1 
ATOM   2881  O  OE1  . GLU   A  1  190 ? 19.351  -29.681 -51.215  1.00 73.93  ? 190  GLU   A OE1  1 
ATOM   2882  O  OE2  . GLU   A  1  190 ? 18.957  -31.308 -49.790  1.00 69.87  ? 190  GLU   A OE2  1 
ATOM   2883  H  H    . GLU   A  1  190 ? 19.788  -26.333 -48.483  1.00 79.34  ? 190  GLU   A H    1 
ATOM   2884  H  HA   . GLU   A  1  190 ? 18.069  -27.723 -49.864  1.00 75.58  ? 190  GLU   A HA   1 
ATOM   2885  H  HB2  . GLU   A  1  190 ? 19.291  -28.204 -47.384  1.00 75.24  ? 190  GLU   A HB2  1 
ATOM   2886  H  HB3  . GLU   A  1  190 ? 18.193  -29.214 -47.931  1.00 75.24  ? 190  GLU   A HB3  1 
ATOM   2887  H  HG2  . GLU   A  1  190 ? 20.564  -28.682 -49.339  1.00 80.33  ? 190  GLU   A HG2  1 
ATOM   2888  H  HG3  . GLU   A  1  190 ? 20.422  -29.909 -48.339  1.00 80.33  ? 190  GLU   A HG3  1 
ATOM   2889  N  N    . ILE   A  1  191 ? 16.866  -26.409 -47.189  1.00 57.54  ? 191  ILE   A N    1 
ATOM   2890  C  CA   . ILE   A  1  191 ? 15.630  -26.159 -46.452  1.00 55.69  ? 191  ILE   A CA   1 
ATOM   2891  C  C    . ILE   A  1  191 ? 14.606  -25.460 -47.337  1.00 59.75  ? 191  ILE   A C    1 
ATOM   2892  O  O    . ILE   A  1  191 ? 13.402  -25.731 -47.248  1.00 62.25  ? 191  ILE   A O    1 
ATOM   2893  C  CB   . ILE   A  1  191 ? 15.927  -25.347 -45.176  1.00 52.80  ? 191  ILE   A CB   1 
ATOM   2894  C  CG1  . ILE   A  1  191 ? 16.849  -26.145 -44.248  1.00 52.78  ? 191  ILE   A CG1  1 
ATOM   2895  C  CG2  . ILE   A  1  191 ? 14.629  -24.983 -44.459  1.00 52.70  ? 191  ILE   A CG2  1 
ATOM   2896  C  CD1  . ILE   A  1  191 ? 17.282  -25.401 -43.000  1.00 53.31  ? 191  ILE   A CD1  1 
ATOM   2897  H  H    . ILE   A  1  191 ? 17.570  -26.079 -46.823  1.00 69.03  ? 191  ILE   A H    1 
ATOM   2898  H  HA   . ILE   A  1  191 ? 15.255  -27.014 -46.186  1.00 66.81  ? 191  ILE   A HA   1 
ATOM   2899  H  HB   . ILE   A  1  191 ? 16.375  -24.525 -45.430  1.00 63.34  ? 191  ILE   A HB   1 
ATOM   2900  H  HG12 . ILE   A  1  191 ? 16.383  -26.947 -43.965  1.00 63.32  ? 191  ILE   A HG12 1 
ATOM   2901  H  HG13 . ILE   A  1  191 ? 17.650  -26.383 -44.740  1.00 63.32  ? 191  ILE   A HG13 1 
ATOM   2902  H  HG21 . ILE   A  1  191 ? 14.843  -24.506 -43.642  1.00 63.23  ? 191  ILE   A HG21 1 
ATOM   2903  H  HG22 . ILE   A  1  191 ? 14.094  -24.420 -45.040  1.00 63.23  ? 191  ILE   A HG22 1 
ATOM   2904  H  HG23 . ILE   A  1  191 ? 14.145  -25.797 -44.250  1.00 63.23  ? 191  ILE   A HG23 1 
ATOM   2905  H  HD11 . ILE   A  1  191 ? 17.935  -25.936 -42.524  1.00 63.95  ? 191  ILE   A HD11 1 
ATOM   2906  H  HD12 . ILE   A  1  191 ? 17.675  -24.552 -43.258  1.00 63.95  ? 191  ILE   A HD12 1 
ATOM   2907  H  HD13 . ILE   A  1  191 ? 16.506  -25.248 -42.438  1.00 63.95  ? 191  ILE   A HD13 1 
ATOM   2908  N  N    . VAL   A  1  192 ? 15.059  -24.556 -48.201  1.00 60.08  ? 192  VAL   A N    1 
ATOM   2909  C  CA   . VAL   A  1  192 ? 14.136  -23.793 -49.037  1.00 65.54  ? 192  VAL   A CA   1 
ATOM   2910  C  C    . VAL   A  1  192 ? 13.858  -24.506 -50.356  1.00 66.85  ? 192  VAL   A C    1 
ATOM   2911  O  O    . VAL   A  1  192 ? 12.718  -24.526 -50.825  1.00 70.47  ? 192  VAL   A O    1 
ATOM   2912  C  CB   . VAL   A  1  192 ? 14.682  -22.368 -49.273  1.00 69.47  ? 192  VAL   A CB   1 
ATOM   2913  C  CG1  . VAL   A  1  192 ? 15.031  -21.703 -47.948  1.00 64.03  ? 192  VAL   A CG1  1 
ATOM   2914  C  CG2  . VAL   A  1  192 ? 15.889  -22.387 -50.204  1.00 75.53  ? 192  VAL   A CG2  1 
ATOM   2915  H  H    . VAL   A  1  192 ? 15.889  -24.367 -48.322  1.00 72.08  ? 192  VAL   A H    1 
ATOM   2916  H  HA   . VAL   A  1  192 ? 13.294  -23.713 -48.562  1.00 78.62  ? 192  VAL   A HA   1 
ATOM   2917  H  HB   . VAL   A  1  192 ? 13.990  -21.842 -49.703  1.00 83.35  ? 192  VAL   A HB   1 
ATOM   2918  H  HG11 . VAL   A  1  192 ? 15.329  -20.796 -48.119  1.00 76.81  ? 192  VAL   A HG11 1 
ATOM   2919  H  HG12 . VAL   A  1  192 ? 14.242  -21.691 -47.384  1.00 76.81  ? 192  VAL   A HG12 1 
ATOM   2920  H  HG13 . VAL   A  1  192 ? 15.738  -22.208 -47.518  1.00 76.81  ? 192  VAL   A HG13 1 
ATOM   2921  H  HG21 . VAL   A  1  192 ? 16.275  -21.498 -50.240  1.00 90.62  ? 192  VAL   A HG21 1 
ATOM   2922  H  HG22 . VAL   A  1  192 ? 16.542  -23.018 -49.861  1.00 90.62  ? 192  VAL   A HG22 1 
ATOM   2923  H  HG23 . VAL   A  1  192 ? 15.600  -22.659 -51.089  1.00 90.62  ? 192  VAL   A HG23 1 
ATOM   2924  N  N    . SER   A  1  193 ? 14.879  -25.104 -50.974  1.00 65.74  ? 193  SER   A N    1 
ATOM   2925  C  CA   . SER   A  1  193 ? 14.678  -25.718 -52.282  1.00 67.62  ? 193  SER   A CA   1 
ATOM   2926  C  C    . SER   A  1  193 ? 13.840  -26.985 -52.176  1.00 64.02  ? 193  SER   A C    1 
ATOM   2927  O  O    . SER   A  1  193 ? 12.994  -27.249 -53.039  1.00 69.43  ? 193  SER   A O    1 
ATOM   2928  C  CB   . SER   A  1  193 ? 16.026  -26.025 -52.935  1.00 69.10  ? 193  SER   A CB   1 
ATOM   2929  O  OG   . SER   A  1  193 ? 16.669  -27.112 -52.293  1.00 71.98  ? 193  SER   A OG   1 
ATOM   2930  H  H    . SER   A  1  193 ? 15.678  -25.166 -50.663  1.00 78.87  ? 193  SER   A H    1 
ATOM   2931  H  HA   . SER   A  1  193 ? 14.206  -25.088 -52.849  1.00 81.13  ? 193  SER   A HA   1 
ATOM   2932  H  HB2  . SER   A  1  193 ? 15.879  -26.252 -53.867  1.00 82.90  ? 193  SER   A HB2  1 
ATOM   2933  H  HB3  . SER   A  1  193 ? 16.593  -25.241 -52.870  1.00 82.90  ? 193  SER   A HB3  1 
ATOM   2934  H  HG   . SER   A  1  193 ? 16.999  -26.860 -51.563  1.00 86.35  ? 193  SER   A HG   1 
ATOM   2935  N  N    . LYS   A  1  194 ? 14.058  -27.781 -51.130  1.00 60.25  ? 194  LYS   A N    1 
ATOM   2936  C  CA   . LYS   A  1  194 ? 13.334  -29.033 -50.958  1.00 61.58  ? 194  LYS   A CA   1 
ATOM   2937  C  C    . LYS   A  1  194 ? 11.959  -28.847 -50.329  1.00 61.85  ? 194  LYS   A C    1 
ATOM   2938  O  O    . LYS   A  1  194 ? 11.248  -29.840 -50.143  1.00 61.93  ? 194  LYS   A O    1 
ATOM   2939  C  CB   . LYS   A  1  194 ? 14.148  -30.002 -50.095  1.00 62.98  ? 194  LYS   A CB   1 
ATOM   2940  C  CG   . LYS   A  1  194 ? 15.562  -30.261 -50.587  1.00 70.01  ? 194  LYS   A CG   1 
ATOM   2941  C  CD   . LYS   A  1  194 ? 15.583  -31.048 -51.888  1.00 76.05  ? 194  LYS   A CD   1 
ATOM   2942  C  CE   . LYS   A  1  194 ? 17.008  -31.415 -52.272  1.00 82.86  ? 194  LYS   A CE   1 
ATOM   2943  N  NZ   . LYS   A  1  194 ? 17.082  -32.179 -53.546  1.00 89.81  ? 194  LYS   A NZ   1 
ATOM   2944  H  H    . LYS   A  1  194 ? 14.624  -27.614 -50.505  1.00 72.28  ? 194  LYS   A H    1 
ATOM   2945  H  HA   . LYS   A  1  194 ? 13.215  -29.433 -51.834  1.00 73.87  ? 194  LYS   A HA   1 
ATOM   2946  H  HB2  . LYS   A  1  194 ? 14.213  -29.635 -49.199  1.00 75.55  ? 194  LYS   A HB2  1 
ATOM   2947  H  HB3  . LYS   A  1  194 ? 13.686  -30.854 -50.070  1.00 75.55  ? 194  LYS   A HB3  1 
ATOM   2948  H  HG2  . LYS   A  1  194 ? 16.006  -29.412 -50.741  1.00 83.99  ? 194  LYS   A HG2  1 
ATOM   2949  H  HG3  . LYS   A  1  194 ? 16.044  -30.771 -49.918  1.00 83.99  ? 194  LYS   A HG3  1 
ATOM   2950  H  HD2  . LYS   A  1  194 ? 15.073  -31.866 -51.780  1.00 91.24  ? 194  LYS   A HD2  1 
ATOM   2951  H  HD3  . LYS   A  1  194 ? 15.201  -30.510 -52.599  1.00 91.24  ? 194  LYS   A HD3  1 
ATOM   2952  H  HE2  . LYS   A  1  194 ? 17.525  -30.602 -52.380  1.00 99.42  ? 194  LYS   A HE2  1 
ATOM   2953  H  HE3  . LYS   A  1  194 ? 17.393  -31.963 -51.571  1.00 99.42  ? 194  LYS   A HE3  1 
ATOM   2954  H  HZ1  . LYS   A  1  194 ? 17.928  -32.387 -53.727  1.00 107.75 ? 194  LYS   A HZ1  1 
ATOM   2955  H  HZ2  . LYS   A  1  194 ? 16.608  -32.930 -53.479  1.00 107.75 ? 194  LYS   A HZ2  1 
ATOM   2956  H  HZ3  . LYS   A  1  194 ? 16.756  -31.690 -54.214  1.00 107.75 ? 194  LYS   A HZ3  1 
ATOM   2957  N  N    . TYR   A  1  195 ? 11.567  -27.619 -49.994  1.00 60.70  ? 195  TYR   A N    1 
ATOM   2958  C  CA   . TYR   A  1  195 ? 10.282  -27.416 -49.341  1.00 61.38  ? 195  TYR   A CA   1 
ATOM   2959  C  C    . TYR   A  1  195 ? 9.142   -27.758 -50.292  1.00 61.04  ? 195  TYR   A C    1 
ATOM   2960  O  O    . TYR   A  1  195 ? 9.116   -27.308 -51.442  1.00 60.33  ? 195  TYR   A O    1 
ATOM   2961  C  CB   . TYR   A  1  195 ? 10.130  -25.977 -48.849  1.00 61.85  ? 195  TYR   A CB   1 
ATOM   2962  C  CG   . TYR   A  1  195 ? 8.802   -25.746 -48.161  1.00 60.44  ? 195  TYR   A CG   1 
ATOM   2963  C  CD1  . TYR   A  1  195 ? 8.499   -26.391 -46.969  1.00 61.94  ? 195  TYR   A CD1  1 
ATOM   2964  C  CD2  . TYR   A  1  195 ? 7.847   -24.896 -48.705  1.00 62.70  ? 195  TYR   A CD2  1 
ATOM   2965  C  CE1  . TYR   A  1  195 ? 7.288   -26.196 -46.337  1.00 61.63  ? 195  TYR   A CE1  1 
ATOM   2966  C  CE2  . TYR   A  1  195 ? 6.630   -24.692 -48.077  1.00 62.40  ? 195  TYR   A CE2  1 
ATOM   2967  C  CZ   . TYR   A  1  195 ? 6.357   -25.346 -46.893  1.00 63.12  ? 195  TYR   A CZ   1 
ATOM   2968  O  OH   . TYR   A  1  195 ? 5.151   -25.151 -46.260  1.00 61.33  ? 195  TYR   A OH   1 
ATOM   2969  H  H    . TYR   A  1  195 ? 12.019  -26.902 -50.133  1.00 72.82  ? 195  TYR   A H    1 
ATOM   2970  H  HA   . TYR   A  1  195 ? 10.236  -28.002 -48.569  1.00 73.64  ? 195  TYR   A HA   1 
ATOM   2971  H  HB2  . TYR   A  1  195 ? 10.838  -25.782 -48.215  1.00 74.20  ? 195  TYR   A HB2  1 
ATOM   2972  H  HB3  . TYR   A  1  195 ? 10.188  -25.375 -49.607  1.00 74.20  ? 195  TYR   A HB3  1 
ATOM   2973  H  HD1  . TYR   A  1  195 ? 9.125   -26.966 -46.591  1.00 74.31  ? 195  TYR   A HD1  1 
ATOM   2974  H  HD2  . TYR   A  1  195 ? 8.028   -24.458 -49.505  1.00 75.22  ? 195  TYR   A HD2  1 
ATOM   2975  H  HE1  . TYR   A  1  195 ? 7.102   -26.636 -45.539  1.00 73.94  ? 195  TYR   A HE1  1 
ATOM   2976  H  HE2  . TYR   A  1  195 ? 6.001   -24.118 -48.450  1.00 74.86  ? 195  TYR   A HE2  1 
ATOM   2977  H  HH   . TYR   A  1  195 ? 4.678   -24.615 -46.701  1.00 73.58  ? 195  TYR   A HH   1 
ATOM   2978  N  N    . ASP   A  1  196 ? 8.205   -28.561 -49.804  1.00 61.81  ? 196  ASP   A N    1 
ATOM   2979  C  CA   . ASP   A  1  196 ? 6.973   -28.879 -50.509  1.00 64.27  ? 196  ASP   A CA   1 
ATOM   2980  C  C    . ASP   A  1  196 ? 5.860   -28.958 -49.470  1.00 64.60  ? 196  ASP   A C    1 
ATOM   2981  O  O    . ASP   A  1  196 ? 5.894   -29.838 -48.600  1.00 63.56  ? 196  ASP   A O    1 
ATOM   2982  C  CB   . ASP   A  1  196 ? 7.098   -30.194 -51.278  1.00 64.46  ? 196  ASP   A CB   1 
ATOM   2983  C  CG   . ASP   A  1  196 ? 5.909   -30.456 -52.180  1.00 63.85  ? 196  ASP   A CG   1 
ATOM   2984  O  OD1  . ASP   A  1  196 ? 4.831   -29.875 -51.932  1.00 62.21  ? 196  ASP   A OD1  1 
ATOM   2985  O  OD2  . ASP   A  1  196 ? 6.050   -31.245 -53.139  1.00 63.02  ? 196  ASP   A OD2  1 
ATOM   2986  H  H    . ASP   A  1  196 ? 8.263   -28.948 -49.038  1.00 74.15  ? 196  ASP   A H    1 
ATOM   2987  H  HA   . ASP   A  1  196 ? 6.764   -28.194 -51.163  1.00 77.10  ? 196  ASP   A HA   1 
ATOM   2988  H  HB2  . ASP   A  1  196 ? 7.895   -30.163 -51.831  1.00 77.33  ? 196  ASP   A HB2  1 
ATOM   2989  H  HB3  . ASP   A  1  196 ? 7.163   -30.926 -50.645  1.00 77.33  ? 196  ASP   A HB3  1 
ATOM   2990  N  N    . PRO   A  1  197 ? 4.870   -28.062 -49.505  1.00 63.22  ? 197  PRO   A N    1 
ATOM   2991  C  CA   . PRO   A  1  197 ? 3.822   -28.102 -48.471  1.00 62.20  ? 197  PRO   A CA   1 
ATOM   2992  C  C    . PRO   A  1  197 ? 3.007   -29.382 -48.485  1.00 64.51  ? 197  PRO   A C    1 
ATOM   2993  O  O    . PRO   A  1  197 ? 2.367   -29.699 -47.475  1.00 67.21  ? 197  PRO   A O    1 
ATOM   2994  C  CB   . PRO   A  1  197 ? 2.957   -26.876 -48.796  1.00 59.12  ? 197  PRO   A CB   1 
ATOM   2995  C  CG   . PRO   A  1  197 ? 3.205   -26.605 -50.239  1.00 59.16  ? 197  PRO   A CG   1 
ATOM   2996  C  CD   . PRO   A  1  197 ? 4.632   -26.991 -50.490  1.00 58.52  ? 197  PRO   A CD   1 
ATOM   2997  H  HA   . PRO   A  1  197 ? 4.217   -27.986 -47.593  1.00 74.62  ? 197  PRO   A HA   1 
ATOM   2998  H  HB2  . PRO   A  1  197 ? 2.022   -27.080 -48.637  1.00 70.92  ? 197  PRO   A HB2  1 
ATOM   2999  H  HB3  . PRO   A  1  197 ? 3.231   -26.124 -48.249  1.00 70.92  ? 197  PRO   A HB3  1 
ATOM   3000  H  HG2  . PRO   A  1  197 ? 2.604   -27.140 -50.780  1.00 70.98  ? 197  PRO   A HG2  1 
ATOM   3001  H  HG3  . PRO   A  1  197 ? 3.068   -25.662 -50.423  1.00 70.98  ? 197  PRO   A HG3  1 
ATOM   3002  H  HD2  . PRO   A  1  197 ? 4.746   -27.323 -51.395  1.00 70.21  ? 197  PRO   A HD2  1 
ATOM   3003  H  HD3  . PRO   A  1  197 ? 5.226   -26.241 -50.334  1.00 70.21  ? 197  PRO   A HD3  1 
ATOM   3004  N  N    . ASN   A  1  198 ? 3.009   -30.128 -49.590  1.00 62.97  ? 198  ASN   A N    1 
ATOM   3005  C  CA   . ASN   A  1  198 ? 2.300   -31.399 -49.652  1.00 60.38  ? 198  ASN   A CA   1 
ATOM   3006  C  C    . ASN   A  1  198 ? 3.041   -32.527 -48.947  1.00 61.33  ? 198  ASN   A C    1 
ATOM   3007  O  O    . ASN   A  1  198 ? 2.457   -33.597 -48.747  1.00 64.21  ? 198  ASN   A O    1 
ATOM   3008  C  CB   . ASN   A  1  198 ? 2.056   -31.795 -51.111  1.00 58.08  ? 198  ASN   A CB   1 
ATOM   3009  C  CG   . ASN   A  1  198 ? 1.182   -30.799 -51.846  1.00 56.78  ? 198  ASN   A CG   1 
ATOM   3010  O  OD1  . ASN   A  1  198 ? 1.554   -30.290 -52.903  1.00 58.66  ? 198  ASN   A OD1  1 
ATOM   3011  N  ND2  . ASN   A  1  198 ? 0.012   -30.515 -51.288  1.00 56.61  ? 198  ASN   A ND2  1 
ATOM   3012  H  H    . ASN   A  1  198 ? 3.416   -29.918 -50.317  1.00 75.54  ? 198  ASN   A H    1 
ATOM   3013  H  HA   . ASN   A  1  198 ? 1.439   -31.290 -49.220  1.00 72.44  ? 198  ASN   A HA   1 
ATOM   3014  H  HB2  . ASN   A  1  198 ? 2.908   -31.844 -51.572  1.00 69.68  ? 198  ASN   A HB2  1 
ATOM   3015  H  HB3  . ASN   A  1  198 ? 1.615   -32.658 -51.135  1.00 69.68  ? 198  ASN   A HB3  1 
ATOM   3016  H  HD21 . ASN   A  1  198 ? -0.521  -29.956 -51.667  1.00 67.92  ? 198  ASN   A HD21 1 
ATOM   3017  H  HD22 . ASN   A  1  198 ? -0.214  -30.890 -50.548  1.00 67.92  ? 198  ASN   A HD22 1 
ATOM   3018  N  N    . VAL   A  1  199 ? 4.299   -32.318 -48.567  1.00 57.07  ? 199  VAL   A N    1 
ATOM   3019  C  CA   . VAL   A  1  199 ? 5.124   -33.342 -47.938  1.00 55.01  ? 199  VAL   A CA   1 
ATOM   3020  C  C    . VAL   A  1  199 ? 5.437   -32.882 -46.522  1.00 56.97  ? 199  VAL   A C    1 
ATOM   3021  O  O    . VAL   A  1  199 ? 6.029   -31.813 -46.327  1.00 58.40  ? 199  VAL   A O    1 
ATOM   3022  C  CB   . VAL   A  1  199 ? 6.413   -33.602 -48.733  1.00 55.17  ? 199  VAL   A CB   1 
ATOM   3023  C  CG1  . VAL   A  1  199 ? 7.204   -34.743 -48.111  1.00 55.15  ? 199  VAL   A CG1  1 
ATOM   3024  C  CG2  . VAL   A  1  199 ? 6.083   -33.901 -50.188  1.00 57.57  ? 199  VAL   A CG2  1 
ATOM   3025  H  H    . VAL   A  1  199 ? 4.707   -31.567 -48.667  1.00 68.46  ? 199  VAL   A H    1 
ATOM   3026  H  HA   . VAL   A  1  199 ? 4.626   -34.173 -47.886  1.00 66.00  ? 199  VAL   A HA   1 
ATOM   3027  H  HB   . VAL   A  1  199 ? 6.968   -32.807 -48.706  1.00 66.18  ? 199  VAL   A HB   1 
ATOM   3028  H  HG11 . VAL   A  1  199 ? 7.990   -34.916 -48.653  1.00 66.16  ? 199  VAL   A HG11 1 
ATOM   3029  H  HG12 . VAL   A  1  199 ? 7.472   -34.490 -47.213  1.00 66.16  ? 199  VAL   A HG12 1 
ATOM   3030  H  HG13 . VAL   A  1  199 ? 6.644   -35.535 -48.078  1.00 66.16  ? 199  VAL   A HG13 1 
ATOM   3031  H  HG21 . VAL   A  1  199 ? 6.905   -34.093 -50.665  1.00 69.06  ? 199  VAL   A HG21 1 
ATOM   3032  H  HG22 . VAL   A  1  199 ? 5.492   -34.669 -50.226  1.00 69.06  ? 199  VAL   A HG22 1 
ATOM   3033  H  HG23 . VAL   A  1  199 ? 5.646   -33.128 -50.578  1.00 69.06  ? 199  VAL   A HG23 1 
ATOM   3034  N  N    . TYR   A  1  200 ? 5.044   -33.691 -45.537  1.00 57.04  ? 200  TYR   A N    1 
ATOM   3035  C  CA   . TYR   A  1  200 ? 5.214   -33.336 -44.134  1.00 54.36  ? 200  TYR   A CA   1 
ATOM   3036  C  C    . TYR   A  1  200 ? 6.578   -33.733 -43.590  1.00 55.79  ? 200  TYR   A C    1 
ATOM   3037  O  O    . TYR   A  1  200 ? 7.056   -33.119 -42.628  1.00 56.23  ? 200  TYR   A O    1 
ATOM   3038  C  CB   . TYR   A  1  200 ? 4.117   -33.997 -43.292  1.00 53.96  ? 200  TYR   A CB   1 
ATOM   3039  C  CG   . TYR   A  1  200 ? 2.721   -33.758 -43.823  1.00 54.46  ? 200  TYR   A CG   1 
ATOM   3040  C  CD1  . TYR   A  1  200 ? 2.395   -32.568 -44.459  1.00 53.79  ? 200  TYR   A CD1  1 
ATOM   3041  C  CD2  . TYR   A  1  200 ? 1.732   -34.725 -43.699  1.00 55.70  ? 200  TYR   A CD2  1 
ATOM   3042  C  CE1  . TYR   A  1  200 ? 1.127   -32.346 -44.950  1.00 56.19  ? 200  TYR   A CE1  1 
ATOM   3043  C  CE2  . TYR   A  1  200 ? 0.459   -34.511 -44.188  1.00 54.36  ? 200  TYR   A CE2  1 
ATOM   3044  C  CZ   . TYR   A  1  200 ? 0.163   -33.319 -44.813  1.00 56.12  ? 200  TYR   A CZ   1 
ATOM   3045  O  OH   . TYR   A  1  200 ? -1.102  -33.096 -45.304  1.00 57.30  ? 200  TYR   A OH   1 
ATOM   3046  H  H    . TYR   A  1  200 ? 4.673   -34.457 -45.660  1.00 68.42  ? 200  TYR   A H    1 
ATOM   3047  H  HA   . TYR   A  1  200 ? 5.125   -32.375 -44.039  1.00 65.21  ? 200  TYR   A HA   1 
ATOM   3048  H  HB2  . TYR   A  1  200 ? 4.268   -34.955 -43.278  1.00 64.73  ? 200  TYR   A HB2  1 
ATOM   3049  H  HB3  . TYR   A  1  200 ? 4.157   -33.641 -42.391  1.00 64.73  ? 200  TYR   A HB3  1 
ATOM   3050  H  HD1  . TYR   A  1  200 ? 3.044   -31.910 -44.556  1.00 64.52  ? 200  TYR   A HD1  1 
ATOM   3051  H  HD2  . TYR   A  1  200 ? 1.931   -35.531 -43.279  1.00 66.82  ? 200  TYR   A HD2  1 
ATOM   3052  H  HE1  . TYR   A  1  200 ? 0.923   -31.542 -45.372  1.00 67.41  ? 200  TYR   A HE1  1 
ATOM   3053  H  HE2  . TYR   A  1  200 ? -0.194  -35.167 -44.096  1.00 65.22  ? 200  TYR   A HE2  1 
ATOM   3054  H  HH   . TYR   A  1  200 ? -1.588  -33.767 -45.161  1.00 68.75  ? 200  TYR   A HH   1 
ATOM   3055  N  N    . SER   A  1  201 ? 7.213   -34.742 -44.181  1.00 55.47  ? 201  SER   A N    1 
ATOM   3056  C  CA   . SER   A  1  201 ? 8.546   -35.199 -43.792  1.00 54.71  ? 201  SER   A CA   1 
ATOM   3057  C  C    . SER   A  1  201 ? 9.443   -35.046 -45.016  1.00 59.57  ? 201  SER   A C    1 
ATOM   3058  O  O    . SER   A  1  201 ? 9.436   -35.896 -45.912  1.00 62.20  ? 201  SER   A O    1 
ATOM   3059  C  CB   . SER   A  1  201 ? 8.509   -36.639 -43.292  1.00 57.48  ? 201  SER   A CB   1 
ATOM   3060  O  OG   . SER   A  1  201 ? 7.548   -36.792 -42.261  1.00 62.92  ? 201  SER   A OG   1 
ATOM   3061  H  H    . SER   A  1  201 ? 6.880   -35.194 -44.833  1.00 66.55  ? 201  SER   A H    1 
ATOM   3062  H  HA   . SER   A  1  201 ? 8.893   -34.645 -43.075  1.00 65.63  ? 201  SER   A HA   1 
ATOM   3063  H  HB2  . SER   A  1  201 ? 8.276   -37.223 -44.030  1.00 68.96  ? 201  SER   A HB2  1 
ATOM   3064  H  HB3  . SER   A  1  201 ? 9.384   -36.875 -42.945  1.00 68.96  ? 201  SER   A HB3  1 
ATOM   3065  H  HG   . SER   A  1  201 ? 7.724   -36.272 -41.625  1.00 75.48  ? 201  SER   A HG   1 
ATOM   3066  N  N    . ILE   A  1  202 ? 10.210  -33.963 -45.053  1.00 61.90  ? 202  ILE   A N    1 
ATOM   3067  C  CA   . ILE   A  1  202 ? 10.979  -33.588 -46.235  1.00 61.45  ? 202  ILE   A CA   1 
ATOM   3068  C  C    . ILE   A  1  202 ? 12.343  -34.260 -46.180  1.00 60.60  ? 202  ILE   A C    1 
ATOM   3069  O  O    . ILE   A  1  202 ? 13.038  -34.200 -45.158  1.00 59.92  ? 202  ILE   A O    1 
ATOM   3070  C  CB   . ILE   A  1  202 ? 11.113  -32.058 -46.332  1.00 59.37  ? 202  ILE   A CB   1 
ATOM   3071  C  CG1  . ILE   A  1  202 ? 9.724   -31.426 -46.477  1.00 62.18  ? 202  ILE   A CG1  1 
ATOM   3072  C  CG2  . ILE   A  1  202 ? 12.011  -31.670 -47.501  1.00 59.59  ? 202  ILE   A CG2  1 
ATOM   3073  C  CD1  . ILE   A  1  202 ? 9.709   -29.915 -46.381  1.00 68.29  ? 202  ILE   A CD1  1 
ATOM   3074  H  H    . ILE   A  1  202 ? 10.305  -33.418 -44.394  1.00 74.27  ? 202  ILE   A H    1 
ATOM   3075  H  HA   . ILE   A  1  202 ? 10.522  -33.908 -47.028  1.00 73.72  ? 202  ILE   A HA   1 
ATOM   3076  H  HB   . ILE   A  1  202 ? 11.524  -31.728 -45.518  1.00 71.22  ? 202  ILE   A HB   1 
ATOM   3077  H  HG12 . ILE   A  1  202 ? 9.364   -31.667 -47.345  1.00 74.59  ? 202  ILE   A HG12 1 
ATOM   3078  H  HG13 . ILE   A  1  202 ? 9.153   -31.770 -45.773  1.00 74.59  ? 202  ILE   A HG13 1 
ATOM   3079  H  HG21 . ILE   A  1  202 ? 12.041  -30.703 -47.569  1.00 71.49  ? 202  ILE   A HG21 1 
ATOM   3080  H  HG22 . ILE   A  1  202 ? 12.902  -32.019 -47.344  1.00 71.49  ? 202  ILE   A HG22 1 
ATOM   3081  H  HG23 . ILE   A  1  202 ? 11.647  -32.048 -48.317  1.00 71.49  ? 202  ILE   A HG23 1 
ATOM   3082  H  HD11 . ILE   A  1  202 ? 8.799   -29.600 -46.498  1.00 81.93  ? 202  ILE   A HD11 1 
ATOM   3083  H  HD12 . ILE   A  1  202 ? 10.041  -29.651 -45.509  1.00 81.93  ? 202  ILE   A HD12 1 
ATOM   3084  H  HD13 . ILE   A  1  202 ? 10.278  -29.548 -47.076  1.00 81.93  ? 202  ILE   A HD13 1 
ATOM   3085  N  N    . LYS   A  1  203 ? 12.727  -34.900 -47.284  1.00 58.52  ? 203  LYS   A N    1 
ATOM   3086  C  CA   . LYS   A  1  203 ? 14.013  -35.588 -47.393  1.00 55.36  ? 203  LYS   A CA   1 
ATOM   3087  C  C    . LYS   A  1  203 ? 15.077  -34.575 -47.795  1.00 56.82  ? 203  LYS   A C    1 
ATOM   3088  O  O    . LYS   A  1  203 ? 15.353  -34.364 -48.977  1.00 63.02  ? 203  LYS   A O    1 
ATOM   3089  C  CB   . LYS   A  1  203 ? 13.936  -36.725 -48.405  1.00 54.53  ? 203  LYS   A CB   1 
ATOM   3090  C  CG   . LYS   A  1  203 ? 13.176  -37.953 -47.928  1.00 58.51  ? 203  LYS   A CG   1 
ATOM   3091  C  CD   . LYS   A  1  203 ? 13.227  -39.073 -48.963  1.00 61.01  ? 203  LYS   A CD   1 
ATOM   3092  C  CE   . LYS   A  1  203 ? 12.552  -40.340 -48.455  1.00 65.53  ? 203  LYS   A CE   1 
ATOM   3093  N  NZ   . LYS   A  1  203 ? 11.101  -40.145 -48.179  1.00 66.90  ? 203  LYS   A NZ   1 
ATOM   3094  H  H    . LYS   A  1  203 ? 12.251  -34.952 -47.998  1.00 70.21  ? 203  LYS   A H    1 
ATOM   3095  H  HA   . LYS   A  1  203 ? 14.245  -35.954 -46.525  1.00 66.42  ? 203  LYS   A HA   1 
ATOM   3096  H  HB2  . LYS   A  1  203 ? 13.490  -36.398 -49.202  1.00 65.42  ? 203  LYS   A HB2  1 
ATOM   3097  H  HB3  . LYS   A  1  203 ? 14.838  -37.007 -48.621  1.00 65.42  ? 203  LYS   A HB3  1 
ATOM   3098  H  HG2  . LYS   A  1  203 ? 13.573  -38.279 -47.106  1.00 70.19  ? 203  LYS   A HG2  1 
ATOM   3099  H  HG3  . LYS   A  1  203 ? 12.247  -37.719 -47.778  1.00 70.19  ? 203  LYS   A HG3  1 
ATOM   3100  H  HD2  . LYS   A  1  203 ? 12.768  -38.787 -49.769  1.00 73.19  ? 203  LYS   A HD2  1 
ATOM   3101  H  HD3  . LYS   A  1  203 ? 14.153  -39.281 -49.165  1.00 73.19  ? 203  LYS   A HD3  1 
ATOM   3102  H  HE2  . LYS   A  1  203 ? 12.640  -41.037 -49.124  1.00 78.62  ? 203  LYS   A HE2  1 
ATOM   3103  H  HE3  . LYS   A  1  203 ? 12.980  -40.618 -47.630  1.00 78.62  ? 203  LYS   A HE3  1 
ATOM   3104  H  HZ1  . LYS   A  1  203 ? 10.762  -40.875 -47.800  1.00 80.26  ? 203  LYS   A HZ1  1 
ATOM   3105  H  HZ2  . LYS   A  1  203 ? 10.986  -39.454 -47.630  1.00 80.26  ? 203  LYS   A HZ2  1 
ATOM   3106  H  HZ3  . LYS   A  1  203 ? 10.666  -39.985 -48.939  1.00 80.26  ? 203  LYS   A HZ3  1 
ATOM   3107  N  N    . TYR   A  1  204 ? 15.690  -33.940 -46.798  1.00 53.27  ? 204  TYR   A N    1 
ATOM   3108  C  CA   . TYR   A  1  204 ? 16.797  -33.030 -47.054  1.00 57.03  ? 204  TYR   A CA   1 
ATOM   3109  C  C    . TYR   A  1  204 ? 18.072  -33.827 -47.293  1.00 62.16  ? 204  TYR   A C    1 
ATOM   3110  O  O    . TYR   A  1  204 ? 18.414  -34.719 -46.510  1.00 66.14  ? 204  TYR   A O    1 
ATOM   3111  C  CB   . TYR   A  1  204 ? 16.998  -32.073 -45.879  1.00 55.71  ? 204  TYR   A CB   1 
ATOM   3112  C  CG   . TYR   A  1  204 ? 15.762  -31.298 -45.489  1.00 57.01  ? 204  TYR   A CG   1 
ATOM   3113  C  CD1  . TYR   A  1  204 ? 15.275  -30.277 -46.294  1.00 56.98  ? 204  TYR   A CD1  1 
ATOM   3114  C  CD2  . TYR   A  1  204 ? 15.090  -31.579 -44.308  1.00 61.54  ? 204  TYR   A CD2  1 
ATOM   3115  C  CE1  . TYR   A  1  204 ? 14.148  -29.565 -45.938  1.00 59.13  ? 204  TYR   A CE1  1 
ATOM   3116  C  CE2  . TYR   A  1  204 ? 13.964  -30.872 -43.944  1.00 67.54  ? 204  TYR   A CE2  1 
ATOM   3117  C  CZ   . TYR   A  1  204 ? 13.498  -29.866 -44.763  1.00 66.08  ? 204  TYR   A CZ   1 
ATOM   3118  O  OH   . TYR   A  1  204 ? 12.376  -29.158 -44.405  1.00 67.97  ? 204  TYR   A OH   1 
ATOM   3119  H  H    . TYR   A  1  204 ? 15.481  -34.021 -45.968  1.00 63.91  ? 204  TYR   A H    1 
ATOM   3120  H  HA   . TYR   A  1  204 ? 16.598  -32.502 -47.843  1.00 68.42  ? 204  TYR   A HA   1 
ATOM   3121  H  HB2  . TYR   A  1  204 ? 17.278  -32.587 -45.106  1.00 66.83  ? 204  TYR   A HB2  1 
ATOM   3122  H  HB3  . TYR   A  1  204 ? 17.684  -31.430 -46.117  1.00 66.83  ? 204  TYR   A HB3  1 
ATOM   3123  H  HD1  . TYR   A  1  204 ? 15.716  -30.070 -47.086  1.00 68.36  ? 204  TYR   A HD1  1 
ATOM   3124  H  HD2  . TYR   A  1  204 ? 15.405  -32.255 -43.752  1.00 73.83  ? 204  TYR   A HD2  1 
ATOM   3125  H  HE1  . TYR   A  1  204 ? 13.830  -28.886 -46.488  1.00 70.94  ? 204  TYR   A HE1  1 
ATOM   3126  H  HE2  . TYR   A  1  204 ? 13.521  -31.073 -43.151  1.00 81.03  ? 204  TYR   A HE2  1 
ATOM   3127  H  HH   . TYR   A  1  204 ? 12.043  -29.481 -43.705  1.00 81.54  ? 204  TYR   A HH   1 
ATOM   3128  N  N    . ASN   A  1  205 ? 18.773  -33.507 -48.376  1.00 65.48  ? 205  ASN   A N    1 
ATOM   3129  C  CA   . ASN   A  1  205 ? 20.071  -34.108 -48.627  1.00 70.50  ? 205  ASN   A CA   1 
ATOM   3130  C  C    . ASN   A  1  205 ? 21.143  -33.387 -47.815  1.00 73.41  ? 205  ASN   A C    1 
ATOM   3131  O  O    . ASN   A  1  205 ? 20.960  -32.253 -47.362  1.00 76.86  ? 205  ASN   A O    1 
ATOM   3132  C  CB   . ASN   A  1  205 ? 20.409  -34.056 -50.117  1.00 75.58  ? 205  ASN   A CB   1 
ATOM   3133  C  CG   . ASN   A  1  205 ? 21.593  -34.931 -50.477  1.00 83.34  ? 205  ASN   A CG   1 
ATOM   3134  O  OD1  . ASN   A  1  205 ? 22.077  -35.709 -49.655  1.00 83.39  ? 205  ASN   A OD1  1 
ATOM   3135  N  ND2  . ASN   A  1  205 ? 22.060  -34.815 -51.714  1.00 89.77  ? 205  ASN   A ND2  1 
ATOM   3136  H  H    . ASN   A  1  205 ? 18.517  -32.947 -48.977  1.00 78.56  ? 205  ASN   A H    1 
ATOM   3137  H  HA   . ASN   A  1  205 ? 20.059  -35.041 -48.361  1.00 84.58  ? 205  ASN   A HA   1 
ATOM   3138  H  HB2  . ASN   A  1  205 ? 19.643  -34.364 -50.626  1.00 90.68  ? 205  ASN   A HB2  1 
ATOM   3139  H  HB3  . ASN   A  1  205 ? 20.625  -33.143 -50.361  1.00 90.68  ? 205  ASN   A HB3  1 
ATOM   3140  H  HD21 . ASN   A  1  205 ? 22.731  -35.290 -51.967  1.00 107.70 ? 205  ASN   A HD21 1 
ATOM   3141  H  HD22 . ASN   A  1  205 ? 21.691  -34.265 -52.263  1.00 107.70 ? 205  ASN   A HD22 1 
ATOM   3142  N  N    . ASN   A  1  206 ? 22.271  -34.067 -47.623  1.00 71.12  ? 206  ASN   A N    1 
ATOM   3143  C  CA   . ASN   A  1  206 ? 23.403  -33.508 -46.886  1.00 69.24  ? 206  ASN   A CA   1 
ATOM   3144  C  C    . ASN   A  1  206 ? 23.019  -33.115 -45.462  1.00 62.16  ? 206  ASN   A C    1 
ATOM   3145  O  O    . ASN   A  1  206 ? 23.647  -32.240 -44.860  1.00 58.50  ? 206  ASN   A O    1 
ATOM   3146  C  CB   . ASN   A  1  206 ? 23.997  -32.303 -47.622  1.00 72.19  ? 206  ASN   A CB   1 
ATOM   3147  C  CG   . ASN   A  1  206 ? 24.545  -32.666 -48.985  1.00 79.53  ? 206  ASN   A CG   1 
ATOM   3148  O  OD1  . ASN   A  1  206 ? 25.114  -33.741 -49.171  1.00 86.72  ? 206  ASN   A OD1  1 
ATOM   3149  N  ND2  . ASN   A  1  206 ? 24.373  -31.770 -49.950  1.00 80.66  ? 206  ASN   A ND2  1 
ATOM   3150  H  H    . ASN   A  1  206 ? 22.408  -34.864 -47.914  1.00 85.33  ? 206  ASN   A H    1 
ATOM   3151  H  HA   . ASN   A  1  206 ? 24.086  -34.194 -46.823  1.00 83.07  ? 206  ASN   A HA   1 
ATOM   3152  H  HB2  . ASN   A  1  206 ? 23.305  -31.634 -47.744  1.00 86.61  ? 206  ASN   A HB2  1 
ATOM   3153  H  HB3  . ASN   A  1  206 ? 24.723  -31.936 -47.094  1.00 86.61  ? 206  ASN   A HB3  1 
ATOM   3154  H  HD21 . ASN   A  1  206 ? 24.666  -31.930 -50.742  1.00 96.77  ? 206  ASN   A HD21 1 
ATOM   3155  H  HD22 . ASN   A  1  206 ? 23.968  -31.030 -49.783  1.00 96.77  ? 206  ASN   A HD22 1 
ATOM   3156  N  N    . GLN   A  1  207 ? 21.989  -33.749 -44.908  1.00 60.07  ? 207  GLN   A N    1 
ATOM   3157  C  CA   . GLN   A  1  207 ? 21.604  -33.483 -43.529  1.00 58.01  ? 207  GLN   A CA   1 
ATOM   3158  C  C    . GLN   A  1  207 ? 22.586  -34.146 -42.573  1.00 58.17  ? 207  GLN   A C    1 
ATOM   3159  O  O    . GLN   A  1  207 ? 23.040  -35.271 -42.804  1.00 60.32  ? 207  GLN   A O    1 
ATOM   3160  C  CB   . GLN   A  1  207 ? 20.187  -33.988 -43.246  1.00 57.44  ? 207  GLN   A CB   1 
ATOM   3161  C  CG   . GLN   A  1  207 ? 19.713  -33.691 -41.823  1.00 54.60  ? 207  GLN   A CG   1 
ATOM   3162  C  CD   . GLN   A  1  207 ? 18.318  -34.213 -41.537  1.00 54.92  ? 207  GLN   A CD   1 
ATOM   3163  O  OE1  . GLN   A  1  207 ? 18.101  -35.421 -41.448  1.00 59.34  ? 207  GLN   A OE1  1 
ATOM   3164  N  NE2  . GLN   A  1  207 ? 17.363  -33.301 -41.385  1.00 53.44  ? 207  GLN   A NE2  1 
ATOM   3165  H  H    . GLN   A  1  207 ? 21.501  -34.333 -45.308  1.00 72.06  ? 207  GLN   A H    1 
ATOM   3166  H  HA   . GLN   A  1  207 ? 21.613  -32.525 -43.377  1.00 69.59  ? 207  GLN   A HA   1 
ATOM   3167  H  HB2  . GLN   A  1  207 ? 19.572  -33.558 -43.860  1.00 68.91  ? 207  GLN   A HB2  1 
ATOM   3168  H  HB3  . GLN   A  1  207 ? 20.166  -34.949 -43.373  1.00 68.91  ? 207  GLN   A HB3  1 
ATOM   3169  H  HG2  . GLN   A  1  207 ? 20.323  -34.109 -41.195  1.00 65.51  ? 207  GLN   A HG2  1 
ATOM   3170  H  HG3  . GLN   A  1  207 ? 19.706  -32.730 -41.688  1.00 65.51  ? 207  GLN   A HG3  1 
ATOM   3171  H  HE21 . GLN   A  1  207 ? 17.553  -32.465 -41.450  1.00 64.10  ? 207  GLN   A HE21 1 
ATOM   3172  H  HE22 . GLN   A  1  207 ? 16.555  -33.547 -41.221  1.00 64.10  ? 207  GLN   A HE22 1 
ATOM   3173  N  N    . LEU   A  1  208 ? 22.913  -33.438 -41.497  1.00 57.19  ? 208  LEU   A N    1 
ATOM   3174  C  CA   . LEU   A  1  208 ? 23.749  -33.957 -40.424  1.00 55.93  ? 208  LEU   A CA   1 
ATOM   3175  C  C    . LEU   A  1  208 ? 22.903  -34.076 -39.167  1.00 53.64  ? 208  LEU   A C    1 
ATOM   3176  O  O    . LEU   A  1  208 ? 22.195  -33.132 -38.803  1.00 53.61  ? 208  LEU   A O    1 
ATOM   3177  C  CB   . LEU   A  1  208 ? 24.948  -33.043 -40.167  1.00 55.20  ? 208  LEU   A CB   1 
ATOM   3178  C  CG   . LEU   A  1  208 ? 25.895  -32.802 -41.342  1.00 56.41  ? 208  LEU   A CG   1 
ATOM   3179  C  CD1  . LEU   A  1  208 ? 26.962  -31.794 -40.948  1.00 58.02  ? 208  LEU   A CD1  1 
ATOM   3180  C  CD2  . LEU   A  1  208 ? 26.528  -34.104 -41.801  1.00 56.09  ? 208  LEU   A CD2  1 
ATOM   3181  H  H    . LEU   A  1  208 ? 22.653  -32.629 -41.363  1.00 68.60  ? 208  LEU   A H    1 
ATOM   3182  H  HA   . LEU   A  1  208 ? 24.088  -34.834 -40.664  1.00 67.10  ? 208  LEU   A HA   1 
ATOM   3183  H  HB2  . LEU   A  1  208 ? 24.610  -32.177 -39.892  1.00 66.23  ? 208  LEU   A HB2  1 
ATOM   3184  H  HB3  . LEU   A  1  208 ? 25.475  -33.435 -39.453  1.00 66.23  ? 208  LEU   A HB3  1 
ATOM   3185  H  HG   . LEU   A  1  208 ? 25.394  -32.443 -42.090  1.00 67.67  ? 208  LEU   A HG   1 
ATOM   3186  H  HD11 . LEU   A  1  208 ? 27.571  -31.671 -41.693  1.00 69.60  ? 208  LEU   A HD11 1 
ATOM   3187  H  HD12 . LEU   A  1  208 ? 26.534  -30.952 -40.728  1.00 69.60  ? 208  LEU   A HD12 1 
ATOM   3188  H  HD13 . LEU   A  1  208 ? 27.446  -32.131 -40.178  1.00 69.60  ? 208  LEU   A HD13 1 
ATOM   3189  H  HD21 . LEU   A  1  208 ? 27.150  -33.916 -42.522  1.00 67.28  ? 208  LEU   A HD21 1 
ATOM   3190  H  HD22 . LEU   A  1  208 ? 26.999  -34.506 -41.054  1.00 67.28  ? 208  LEU   A HD22 1 
ATOM   3191  H  HD23 . LEU   A  1  208 ? 25.831  -34.702 -42.112  1.00 67.28  ? 208  LEU   A HD23 1 
ATOM   3192  N  N    . ALA   A  1  209 ? 22.970  -35.231 -38.509  1.00 52.85  ? 209  ALA   A N    1 
ATOM   3193  C  CA   . ALA   A  1  209 ? 22.163  -35.458 -37.320  1.00 52.44  ? 209  ALA   A CA   1 
ATOM   3194  C  C    . ALA   A  1  209 ? 22.835  -36.482 -36.422  1.00 57.76  ? 209  ALA   A C    1 
ATOM   3195  O  O    . ALA   A  1  209 ? 23.378  -37.481 -36.902  1.00 58.85  ? 209  ALA   A O    1 
ATOM   3196  C  CB   . ALA   A  1  209 ? 20.755  -35.937 -37.691  1.00 53.44  ? 209  ALA   A CB   1 
ATOM   3197  H  H    . ALA   A  1  209 ? 23.474  -35.891 -38.731  1.00 63.40  ? 209  ALA   A H    1 
ATOM   3198  H  HA   . ALA   A  1  209 ? 22.096  -34.628 -36.823  1.00 62.91  ? 209  ALA   A HA   1 
ATOM   3199  H  HB1  . ALA   A  1  209 ? 20.249  -36.089 -36.878  1.00 64.11  ? 209  ALA   A HB1  1 
ATOM   3200  H  HB2  . ALA   A  1  209 ? 20.321  -35.256 -38.228  1.00 64.11  ? 209  ALA   A HB2  1 
ATOM   3201  H  HB3  . ALA   A  1  209 ? 20.825  -36.762 -38.196  1.00 64.11  ? 209  ALA   A HB3  1 
ATOM   3202  N  N    . THR   A  1  210 ? 22.793  -36.225 -35.117  1.00 60.06  ? 210  THR   A N    1 
ATOM   3203  C  CA   . THR   A  1  210 ? 23.217  -37.228 -34.154  1.00 57.63  ? 210  THR   A CA   1 
ATOM   3204  C  C    . THR   A  1  210 ? 22.282  -38.432 -34.219  1.00 57.70  ? 210  THR   A C    1 
ATOM   3205  O  O    . THR   A  1  210 ? 21.120  -38.329 -34.625  1.00 55.88  ? 210  THR   A O    1 
ATOM   3206  C  CB   . THR   A  1  210 ? 23.234  -36.649 -32.739  1.00 52.97  ? 210  THR   A CB   1 
ATOM   3207  O  OG1  . THR   A  1  210 ? 21.937  -36.141 -32.408  1.00 50.13  ? 210  THR   A OG1  1 
ATOM   3208  C  CG2  . THR   A  1  210 ? 24.263  -35.532 -32.627  1.00 53.67  ? 210  THR   A CG2  1 
ATOM   3209  H  H    . THR   A  1  210 ? 22.527  -35.485 -34.770  1.00 72.06  ? 210  THR   A H    1 
ATOM   3210  H  HA   . THR   A  1  210 ? 24.118  -37.520 -34.360  1.00 69.14  ? 210  THR   A HA   1 
ATOM   3211  H  HB   . THR   A  1  210 ? 23.476  -37.347 -32.109  1.00 63.55  ? 210  THR   A HB   1 
ATOM   3212  H  HG1  . THR   A  1  210 ? 21.431  -36.771 -32.178  1.00 60.14  ? 210  THR   A HG1  1 
ATOM   3213  H  HG21 . THR   A  1  210 ? 24.264  -35.170 -31.727  1.00 64.39  ? 210  THR   A HG21 1 
ATOM   3214  H  HG22 . THR   A  1  210 ? 25.148  -35.874 -32.829  1.00 64.39  ? 210  THR   A HG22 1 
ATOM   3215  H  HG23 . THR   A  1  210 ? 24.050  -34.821 -33.252  1.00 64.39  ? 210  THR   A HG23 1 
ATOM   3216  N  N    . ARG   A  1  211 ? 22.802  -39.584 -33.815  1.00 57.76  ? 211  ARG   A N    1 
ATOM   3217  C  CA   . ARG   A  1  211 ? 22.101  -40.850 -33.946  1.00 57.85  ? 211  ARG   A CA   1 
ATOM   3218  C  C    . ARG   A  1  211 ? 21.643  -41.357 -32.585  1.00 57.99  ? 211  ARG   A C    1 
ATOM   3219  O  O    . ARG   A  1  211 ? 22.175  -40.975 -31.538  1.00 57.57  ? 211  ARG   A O    1 
ATOM   3220  C  CB   . ARG   A  1  211 ? 22.997  -41.897 -34.617  1.00 64.47  ? 211  ARG   A CB   1 
ATOM   3221  C  CG   . ARG   A  1  211 ? 23.449  -41.521 -36.024  1.00 70.74  ? 211  ARG   A CG   1 
ATOM   3222  C  CD   . ARG   A  1  211 ? 24.480  -42.507 -36.558  1.00 84.30  ? 211  ARG   A CD   1 
ATOM   3223  N  NE   . ARG   A  1  211 ? 23.993  -43.252 -37.718  1.00 97.56  ? 211  ARG   A NE   1 
ATOM   3224  C  CZ   . ARG   A  1  211 ? 24.224  -42.920 -38.987  1.00 106.75 ? 211  ARG   A CZ   1 
ATOM   3225  N  NH1  . ARG   A  1  211 ? 24.942  -41.847 -39.289  1.00 112.82 ? 211  ARG   A NH1  1 
ATOM   3226  N  NH2  . ARG   A  1  211 ? 23.733  -43.672 -39.961  1.00 108.11 ? 211  ARG   A NH2  1 
ATOM   3227  H  H    . ARG   A  1  211 ? 23.578  -39.657 -33.453  1.00 69.29  ? 211  ARG   A H    1 
ATOM   3228  H  HA   . ARG   A  1  211 ? 21.311  -40.721 -34.494  1.00 69.40  ? 211  ARG   A HA   1 
ATOM   3229  H  HB2  . ARG   A  1  211 ? 23.792  -42.018 -34.075  1.00 77.34  ? 211  ARG   A HB2  1 
ATOM   3230  H  HB3  . ARG   A  1  211 ? 22.507  -42.732 -34.679  1.00 77.34  ? 211  ARG   A HB3  1 
ATOM   3231  H  HG2  . ARG   A  1  211 ? 22.684  -41.526 -36.620  1.00 84.87  ? 211  ARG   A HG2  1 
ATOM   3232  H  HG3  . ARG   A  1  211 ? 23.851  -40.638 -36.007  1.00 84.87  ? 211  ARG   A HG3  1 
ATOM   3233  H  HD2  . ARG   A  1  211 ? 25.275  -42.020 -36.826  1.00 101.15 ? 211  ARG   A HD2  1 
ATOM   3234  H  HD3  . ARG   A  1  211 ? 24.700  -43.145 -35.862  1.00 101.15 ? 211  ARG   A HD3  1 
ATOM   3235  H  HE   . ARG   A  1  211 ? 23.522  -43.956 -37.570  1.00 117.05 ? 211  ARG   A HE   1 
ATOM   3236  H  HH11 . ARG   A  1  211 ? 25.265  -41.355 -38.662  1.00 135.36 ? 211  ARG   A HH11 1 
ATOM   3237  H  HH12 . ARG   A  1  211 ? 25.085  -41.643 -40.113  1.00 135.36 ? 211  ARG   A HH12 1 
ATOM   3238  H  HH21 . ARG   A  1  211 ? 23.268  -44.371 -39.773  1.00 129.71 ? 211  ARG   A HH21 1 
ATOM   3239  H  HH22 . ARG   A  1  211 ? 23.880  -43.462 -40.782  1.00 129.71 ? 211  ARG   A HH22 1 
ATOM   3240  N  N    . THR   A  1  212 ? 20.634  -42.225 -32.616  1.00 59.07  ? 212  THR   A N    1 
ATOM   3241  C  CA   . THR   A  1  212 ? 20.164  -42.871 -31.398  1.00 58.44  ? 212  THR   A CA   1 
ATOM   3242  C  C    . THR   A  1  212 ? 21.281  -43.704 -30.782  1.00 58.18  ? 212  THR   A C    1 
ATOM   3243  O  O    . THR   A  1  212 ? 22.027  -44.390 -31.486  1.00 60.88  ? 212  THR   A O    1 
ATOM   3244  C  CB   . THR   A  1  212 ? 18.959  -43.762 -31.699  1.00 58.22  ? 212  THR   A CB   1 
ATOM   3245  O  OG1  . THR   A  1  212 ? 18.008  -43.038 -32.487  1.00 61.07  ? 212  THR   A OG1  1 
ATOM   3246  C  CG2  . THR   A  1  212 ? 18.300  -44.221 -30.408  1.00 56.36  ? 212  THR   A CG2  1 
ATOM   3247  H  H    . THR   A  1  212 ? 20.208  -42.455 -33.326  1.00 70.86  ? 212  THR   A H    1 
ATOM   3248  H  HA   . THR   A  1  212 ? 19.889  -42.194 -30.760  1.00 70.11  ? 212  THR   A HA   1 
ATOM   3249  H  HB   . THR   A  1  212 ? 19.252  -44.547 -32.188  1.00 69.84  ? 212  THR   A HB   1 
ATOM   3250  H  HG1  . THR   A  1  212 ? 17.826  -42.307 -32.117  1.00 73.26  ? 212  THR   A HG1  1 
ATOM   3251  H  HG21 . THR   A  1  212 ? 17.485  -44.708 -30.606  1.00 67.61  ? 212  THR   A HG21 1 
ATOM   3252  H  HG22 . THR   A  1  212 ? 18.902  -44.802 -29.916  1.00 67.61  ? 212  THR   A HG22 1 
ATOM   3253  H  HG23 . THR   A  1  212 ? 18.082  -43.454 -29.856  1.00 67.61  ? 212  THR   A HG23 1 
ATOM   3254  N  N    . ALA   A  1  213 ? 21.390  -43.645 -29.460  1.00 55.63  ? 213  ALA   A N    1 
ATOM   3255  C  CA   . ALA   A  1  213 ? 22.433  -44.343 -28.722  1.00 57.60  ? 213  ALA   A CA   1 
ATOM   3256  C  C    . ALA   A  1  213 ? 21.807  -45.263 -27.680  1.00 54.44  ? 213  ALA   A C    1 
ATOM   3257  O  O    . ALA   A  1  213 ? 20.585  -45.414 -27.600  1.00 53.15  ? 213  ALA   A O    1 
ATOM   3258  C  CB   . ALA   A  1  213 ? 23.391  -43.345 -28.065  1.00 58.72  ? 213  ALA   A CB   1 
ATOM   3259  H  H    . ALA   A  1  213 ? 20.857  -43.196 -28.957  1.00 66.74  ? 213  ALA   A H    1 
ATOM   3260  H  HA   . ALA   A  1  213 ? 22.940  -44.891 -29.341  1.00 69.11  ? 213  ALA   A HA   1 
ATOM   3261  H  HB1  . ALA   A  1  213 ? 24.088  -43.835 -27.601  1.00 70.45  ? 213  ALA   A HB1  1 
ATOM   3262  H  HB2  . ALA   A  1  213 ? 23.783  -42.784 -28.752  1.00 70.45  ? 213  ALA   A HB2  1 
ATOM   3263  H  HB3  . ALA   A  1  213 ? 22.895  -42.799 -27.435  1.00 70.45  ? 213  ALA   A HB3  1 
ATOM   3264  N  N    . GLN   A  1  214 ? 22.666  -45.881 -26.874  1.00 55.56  ? 214  GLN   A N    1 
ATOM   3265  C  CA   . GLN   A  1  214 ? 22.204  -46.814 -25.859  1.00 57.34  ? 214  GLN   A CA   1 
ATOM   3266  C  C    . GLN   A  1  214 ? 21.272  -46.112 -24.876  1.00 57.57  ? 214  GLN   A C    1 
ATOM   3267  O  O    . GLN   A  1  214 ? 21.327  -44.896 -24.686  1.00 55.90  ? 214  GLN   A O    1 
ATOM   3268  C  CB   . GLN   A  1  214 ? 23.392  -47.425 -25.117  1.00 54.95  ? 214  GLN   A CB   1 
ATOM   3269  C  CG   . GLN   A  1  214 ? 24.303  -48.279 -25.993  1.00 65.40  ? 214  GLN   A CG   1 
ATOM   3270  C  CD   . GLN   A  1  214 ? 25.333  -47.464 -26.754  1.00 69.80  ? 214  GLN   A CD   1 
ATOM   3271  O  OE1  . GLN   A  1  214 ? 25.311  -46.234 -26.728  1.00 68.75  ? 214  GLN   A OE1  1 
ATOM   3272  N  NE2  . GLN   A  1  214 ? 26.243  -48.150 -27.437  1.00 73.81  ? 214  GLN   A NE2  1 
ATOM   3273  H  H    . GLN   A  1  214 ? 23.520  -45.776 -26.896  1.00 66.66  ? 214  GLN   A H    1 
ATOM   3274  H  HA   . GLN   A  1  214 ? 21.710  -47.535 -26.280  1.00 68.78  ? 214  GLN   A HA   1 
ATOM   3275  H  HB2  . GLN   A  1  214 ? 23.928  -46.707 -24.747  1.00 65.92  ? 214  GLN   A HB2  1 
ATOM   3276  H  HB3  . GLN   A  1  214 ? 23.055  -47.990 -24.404  1.00 65.92  ? 214  GLN   A HB3  1 
ATOM   3277  H  HG2  . GLN   A  1  214 ? 24.779  -48.910 -25.430  1.00 78.46  ? 214  GLN   A HG2  1 
ATOM   3278  H  HG3  . GLN   A  1  214 ? 23.761  -48.756 -26.641  1.00 78.46  ? 214  GLN   A HG3  1 
ATOM   3279  H  HE21 . GLN   A  1  214 ? 26.227  -49.010 -27.431  1.00 88.56  ? 214  GLN   A HE21 1 
ATOM   3280  H  HE22 . GLN   A  1  214 ? 26.848  -47.734 -27.885  1.00 88.56  ? 214  GLN   A HE22 1 
ATOM   3281  N  N    . ALA   A  1  215 ? 20.404  -46.907 -24.242  1.00 57.45  ? 215  ALA   A N    1 
ATOM   3282  C  CA   . ALA   A  1  215 ? 19.406  -46.348 -23.339  1.00 58.53  ? 215  ALA   A CA   1 
ATOM   3283  C  C    . ALA   A  1  215 ? 20.029  -45.672 -22.126  1.00 56.79  ? 215  ALA   A C    1 
ATOM   3284  O  O    . ALA   A  1  215 ? 19.360  -44.867 -21.469  1.00 55.39  ? 215  ALA   A O    1 
ATOM   3285  C  CB   . ALA   A  1  215 ? 18.443  -47.444 -22.878  1.00 61.27  ? 215  ALA   A CB   1 
ATOM   3286  H  H    . ALA   A  1  215 ? 20.376  -47.763 -24.319  1.00 68.92  ? 215  ALA   A H    1 
ATOM   3287  H  HA   . ALA   A  1  215 ? 18.897  -45.679 -23.823  1.00 70.21  ? 215  ALA   A HA   1 
ATOM   3288  H  HB1  . ALA   A  1  215 ? 17.795  -47.059 -22.268  1.00 73.50  ? 215  ALA   A HB1  1 
ATOM   3289  H  HB2  . ALA   A  1  215 ? 17.991  -47.813 -23.652  1.00 73.50  ? 215  ALA   A HB2  1 
ATOM   3290  H  HB3  . ALA   A  1  215 ? 18.949  -48.139 -22.428  1.00 73.50  ? 215  ALA   A HB3  1 
ATOM   3291  N  N    . ILE   A  1  216 ? 21.289  -45.980 -21.808  1.00 55.94  ? 216  ILE   A N    1 
ATOM   3292  C  CA   . ILE   A  1  216 ? 21.939  -45.343 -20.671  1.00 56.67  ? 216  ILE   A CA   1 
ATOM   3293  C  C    . ILE   A  1  216 ? 21.989  -43.830 -20.839  1.00 53.22  ? 216  ILE   A C    1 
ATOM   3294  O  O    . ILE   A  1  216 ? 22.070  -43.100 -19.845  1.00 49.38  ? 216  ILE   A O    1 
ATOM   3295  C  CB   . ILE   A  1  216 ? 23.357  -45.922 -20.465  1.00 60.78  ? 216  ILE   A CB   1 
ATOM   3296  C  CG1  . ILE   A  1  216 ? 23.968  -45.384 -19.167  1.00 70.57  ? 216  ILE   A CG1  1 
ATOM   3297  C  CG2  . ILE   A  1  216 ? 24.253  -45.598 -21.658  1.00 58.41  ? 216  ILE   A CG2  1 
ATOM   3298  C  CD1  . ILE   A  1  216 ? 25.336  -45.955 -18.840  1.00 78.01  ? 216  ILE   A CD1  1 
ATOM   3299  H  H    . ILE   A  1  216 ? 21.779  -46.547 -22.231  1.00 67.11  ? 216  ILE   A H    1 
ATOM   3300  H  HA   . ILE   A  1  216 ? 21.422  -45.539 -19.874  1.00 67.98  ? 216  ILE   A HA   1 
ATOM   3301  H  HB   . ILE   A  1  216 ? 23.285  -46.887 -20.395  1.00 72.91  ? 216  ILE   A HB   1 
ATOM   3302  H  HG12 . ILE   A  1  216 ? 24.061  -44.421 -19.244  1.00 84.66  ? 216  ILE   A HG12 1 
ATOM   3303  H  HG13 . ILE   A  1  216 ? 23.374  -45.602 -18.431  1.00 84.66  ? 216  ILE   A HG13 1 
ATOM   3304  H  HG21 . ILE   A  1  216 ? 25.088  -46.083 -21.567  1.00 70.08  ? 216  ILE   A HG21 1 
ATOM   3305  H  HG22 . ILE   A  1  216 ? 23.802  -45.867 -22.474  1.00 70.08  ? 216  ILE   A HG22 1 
ATOM   3306  H  HG23 . ILE   A  1  216 ? 24.424  -44.643 -21.674  1.00 70.08  ? 216  ILE   A HG23 1 
ATOM   3307  H  HD11 . ILE   A  1  216 ? 25.619  -45.621 -17.975  1.00 93.59  ? 216  ILE   A HD11 1 
ATOM   3308  H  HD12 . ILE   A  1  216 ? 25.278  -46.923 -18.819  1.00 93.59  ? 216  ILE   A HD12 1 
ATOM   3309  H  HD13 . ILE   A  1  216 ? 25.966  -45.677 -19.524  1.00 93.59  ? 216  ILE   A HD13 1 
ATOM   3310  N  N    . PHE   A  1  217 ? 21.937  -43.338 -22.075  1.00 53.28  ? 217  PHE   A N    1 
ATOM   3311  C  CA   . PHE   A  1  217 ? 22.001  -41.911 -22.354  1.00 56.99  ? 217  PHE   A CA   1 
ATOM   3312  C  C    . PHE   A  1  217 ? 20.630  -41.244 -22.367  1.00 58.17  ? 217  PHE   A C    1 
ATOM   3313  O  O    . PHE   A  1  217 ? 20.538  -40.055 -22.691  1.00 56.48  ? 217  PHE   A O    1 
ATOM   3314  C  CB   . PHE   A  1  217 ? 22.704  -41.673 -23.695  1.00 56.30  ? 217  PHE   A CB   1 
ATOM   3315  C  CG   . PHE   A  1  217 ? 24.092  -42.244 -23.757  1.00 54.70  ? 217  PHE   A CG   1 
ATOM   3316  C  CD1  . PHE   A  1  217 ? 25.165  -41.548 -23.226  1.00 53.35  ? 217  PHE   A CD1  1 
ATOM   3317  C  CD2  . PHE   A  1  217 ? 24.322  -43.480 -24.343  1.00 54.82  ? 217  PHE   A CD2  1 
ATOM   3318  C  CE1  . PHE   A  1  217 ? 26.445  -42.070 -23.277  1.00 53.79  ? 217  PHE   A CE1  1 
ATOM   3319  C  CE2  . PHE   A  1  217 ? 25.600  -44.010 -24.399  1.00 55.67  ? 217  PHE   A CE2  1 
ATOM   3320  C  CZ   . PHE   A  1  217 ? 26.664  -43.304 -23.865  1.00 54.94  ? 217  PHE   A CZ   1 
ATOM   3321  H  H    . PHE   A  1  217 ? 21.863  -43.824 -22.781  1.00 63.92  ? 217  PHE   A H    1 
ATOM   3322  H  HA   . PHE   A  1  217 ? 22.526  -41.486 -21.658  1.00 68.37  ? 217  PHE   A HA   1 
ATOM   3323  H  HB2  . PHE   A  1  217 ? 22.181  -42.087 -24.399  1.00 67.54  ? 217  PHE   A HB2  1 
ATOM   3324  H  HB3  . PHE   A  1  217 ? 22.769  -40.717 -23.848  1.00 67.54  ? 217  PHE   A HB3  1 
ATOM   3325  H  HD1  . PHE   A  1  217 ? 25.022  -40.719 -22.829  1.00 64.00  ? 217  PHE   A HD1  1 
ATOM   3326  H  HD2  . PHE   A  1  217 ? 23.610  -43.958 -24.702  1.00 65.76  ? 217  PHE   A HD2  1 
ATOM   3327  H  HE1  . PHE   A  1  217 ? 27.157  -41.593 -22.917  1.00 64.53  ? 217  PHE   A HE1  1 
ATOM   3328  H  HE2  . PHE   A  1  217 ? 25.743  -44.839 -24.794  1.00 66.79  ? 217  PHE   A HE2  1 
ATOM   3329  H  HZ   . PHE   A  1  217 ? 27.523  -43.658 -23.901  1.00 65.91  ? 217  PHE   A HZ   1 
ATOM   3330  N  N    . ASP   A  1  218 ? 19.568  -41.972 -22.028  1.00 57.63  ? 218  ASP   A N    1 
ATOM   3331  C  CA   . ASP   A  1  218 ? 18.236  -41.383 -22.025  1.00 58.26  ? 218  ASP   A CA   1 
ATOM   3332  C  C    . ASP   A  1  218 ? 18.170  -40.193 -21.073  1.00 54.57  ? 218  ASP   A C    1 
ATOM   3333  O  O    . ASP   A  1  218 ? 18.932  -40.093 -20.108  1.00 49.56  ? 218  ASP   A O    1 
ATOM   3334  C  CB   . ASP   A  1  218 ? 17.188  -42.419 -21.616  1.00 59.81  ? 218  ASP   A CB   1 
ATOM   3335  C  CG   . ASP   A  1  218 ? 17.031  -43.530 -22.636  1.00 58.57  ? 218  ASP   A CG   1 
ATOM   3336  O  OD1  . ASP   A  1  218 ? 17.482  -43.358 -23.788  1.00 58.16  ? 218  ASP   A OD1  1 
ATOM   3337  O  OD2  . ASP   A  1  218 ? 16.446  -44.575 -22.283  1.00 59.27  ? 218  ASP   A OD2  1 
ATOM   3338  H  H    . ASP   A  1  218 ? 19.593  -42.800 -21.798  1.00 69.14  ? 218  ASP   A H    1 
ATOM   3339  H  HA   . ASP   A  1  218 ? 18.031  -41.074 -22.921  1.00 69.89  ? 218  ASP   A HA   1 
ATOM   3340  H  HB2  . ASP   A  1  218 ? 17.452  -42.821 -20.774  1.00 71.75  ? 218  ASP   A HB2  1 
ATOM   3341  H  HB3  . ASP   A  1  218 ? 16.329  -41.979 -21.518  1.00 71.75  ? 218  ASP   A HB3  1 
ATOM   3342  N  N    . ASP   A  1  219 ? 17.240  -39.282 -21.360  1.00 55.92  ? 219  ASP   A N    1 
ATOM   3343  C  CA   . ASP   A  1  219 ? 16.938  -38.164 -20.468  1.00 53.80  ? 219  ASP   A CA   1 
ATOM   3344  C  C    . ASP   A  1  219 ? 18.166  -37.287 -20.235  1.00 54.98  ? 219  ASP   A C    1 
ATOM   3345  O  O    . ASP   A  1  219 ? 18.415  -36.816 -19.123  1.00 54.11  ? 219  ASP   A O    1 
ATOM   3346  C  CB   . ASP   A  1  219 ? 16.373  -38.676 -19.141  1.00 53.39  ? 219  ASP   A CB   1 
ATOM   3347  C  CG   . ASP   A  1  219 ? 15.209  -39.630 -19.337  1.00 58.54  ? 219  ASP   A CG   1 
ATOM   3348  O  OD1  . ASP   A  1  219 ? 14.275  -39.282 -20.089  1.00 58.52  ? 219  ASP   A OD1  1 
ATOM   3349  O  OD2  . ASP   A  1  219 ? 15.235  -40.733 -18.752  1.00 60.68  ? 219  ASP   A OD2  1 
ATOM   3350  H  H    . ASP   A  1  219 ? 16.763  -39.291 -22.075  1.00 67.09  ? 219  ASP   A H    1 
ATOM   3351  H  HA   . ASP   A  1  219 ? 16.268  -37.604 -20.890  1.00 64.54  ? 219  ASP   A HA   1 
ATOM   3352  H  HB2  . ASP   A  1  219 ? 17.071  -39.147 -18.660  1.00 64.05  ? 219  ASP   A HB2  1 
ATOM   3353  H  HB3  . ASP   A  1  219 ? 16.060  -37.922 -18.617  1.00 64.05  ? 219  ASP   A HB3  1 
ATOM   3354  N  N    . SER   A  1  220 ? 18.938  -37.056 -21.296  1.00 54.13  ? 220  SER   A N    1 
ATOM   3355  C  CA   . SER   A  1  220 ? 20.123  -36.211 -21.219  1.00 54.93  ? 220  SER   A CA   1 
ATOM   3356  C  C    . SER   A  1  220 ? 19.883  -34.793 -21.718  1.00 52.20  ? 220  SER   A C    1 
ATOM   3357  O  O    . SER   A  1  220 ? 20.578  -33.870 -21.282  1.00 50.32  ? 220  SER   A O    1 
ATOM   3358  C  CB   . SER   A  1  220 ? 21.267  -36.836 -22.022  1.00 52.13  ? 220  SER   A CB   1 
ATOM   3359  O  OG   . SER   A  1  220 ? 21.653  -38.079 -21.466  1.00 56.69  ? 220  SER   A OG   1 
ATOM   3360  H  H    . SER   A  1  220 ? 18.793  -37.382 -22.078  1.00 64.93  ? 220  SER   A H    1 
ATOM   3361  H  HA   . SER   A  1  220 ? 20.405  -36.152 -20.293  1.00 65.90  ? 220  SER   A HA   1 
ATOM   3362  H  HB2  . SER   A  1  220 ? 20.972  -36.976 -22.935  1.00 62.54  ? 220  SER   A HB2  1 
ATOM   3363  H  HB3  . SER   A  1  220 ? 22.028  -36.234 -22.008  1.00 62.54  ? 220  SER   A HB3  1 
ATOM   3364  H  HG   . SER   A  1  220 ? 21.506  -38.697 -22.015  1.00 68.01  ? 220  SER   A HG   1 
ATOM   3365  N  N    . TYR   A  1  221 ? 18.920  -34.605 -22.622  1.00 49.35  ? 221  TYR   A N    1 
ATOM   3366  C  CA   . TYR   A  1  221 ? 18.548  -33.288 -23.141  1.00 51.06  ? 221  TYR   A CA   1 
ATOM   3367  C  C    . TYR   A  1  221 ? 19.646  -32.687 -24.023  1.00 51.31  ? 221  TYR   A C    1 
ATOM   3368  O  O    . TYR   A  1  221 ? 19.950  -31.498 -23.925  1.00 48.73  ? 221  TYR   A O    1 
ATOM   3369  C  CB   . TYR   A  1  221 ? 18.189  -32.315 -22.009  1.00 53.52  ? 221  TYR   A CB   1 
ATOM   3370  C  CG   . TYR   A  1  221 ? 16.903  -32.624 -21.265  1.00 57.53  ? 221  TYR   A CG   1 
ATOM   3371  C  CD1  . TYR   A  1  221 ? 16.105  -33.707 -21.616  1.00 60.79  ? 221  TYR   A CD1  1 
ATOM   3372  C  CD2  . TYR   A  1  221 ? 16.483  -31.818 -20.213  1.00 56.64  ? 221  TYR   A CD2  1 
ATOM   3373  C  CE1  . TYR   A  1  221 ? 14.932  -33.981 -20.934  1.00 61.50  ? 221  TYR   A CE1  1 
ATOM   3374  C  CE2  . TYR   A  1  221 ? 15.314  -32.084 -19.528  1.00 57.70  ? 221  TYR   A CE2  1 
ATOM   3375  C  CZ   . TYR   A  1  221 ? 14.541  -33.166 -19.892  1.00 59.96  ? 221  TYR   A CZ   1 
ATOM   3376  O  OH   . TYR   A  1  221 ? 13.375  -33.431 -19.209  1.00 58.59  ? 221  TYR   A OH   1 
ATOM   3377  H  H    . TYR   A  1  221 ? 18.454  -35.244 -22.961  1.00 59.20  ? 221  TYR   A H    1 
ATOM   3378  H  HA   . TYR   A  1  221 ? 17.764  -33.407 -23.699  1.00 61.25  ? 221  TYR   A HA   1 
ATOM   3379  H  HB2  . TYR   A  1  221 ? 18.908  -32.326 -21.359  1.00 64.21  ? 221  TYR   A HB2  1 
ATOM   3380  H  HB3  . TYR   A  1  221 ? 18.097  -31.427 -22.388  1.00 64.21  ? 221  TYR   A HB3  1 
ATOM   3381  H  HD1  . TYR   A  1  221 ? 16.364  -34.257 -22.320  1.00 72.93  ? 221  TYR   A HD1  1 
ATOM   3382  H  HD2  . TYR   A  1  221 ? 16.999  -31.086 -19.966  1.00 67.94  ? 221  TYR   A HD2  1 
ATOM   3383  H  HE1  . TYR   A  1  221 ? 14.410  -34.711 -21.177  1.00 73.78  ? 221  TYR   A HE1  1 
ATOM   3384  H  HE2  . TYR   A  1  221 ? 15.049  -31.536 -18.824  1.00 69.23  ? 221  TYR   A HE2  1 
ATOM   3385  H  HH   . TYR   A  1  221 ? 13.260  -32.860 -18.604  1.00 70.29  ? 221  TYR   A HH   1 
ATOM   3386  N  N    . LEU   A  1  222 ? 20.246  -33.503 -24.892  1.00 52.72  ? 222  LEU   A N    1 
ATOM   3387  C  CA   . LEU   A  1  222 ? 21.125  -32.955 -25.919  1.00 53.38  ? 222  LEU   A CA   1 
ATOM   3388  C  C    . LEU   A  1  222 ? 20.340  -31.982 -26.790  1.00 51.58  ? 222  LEU   A C    1 
ATOM   3389  O  O    . LEU   A  1  222 ? 19.205  -32.257 -27.189  1.00 51.14  ? 222  LEU   A O    1 
ATOM   3390  C  CB   . LEU   A  1  222 ? 21.723  -34.068 -26.783  1.00 54.08  ? 222  LEU   A CB   1 
ATOM   3391  C  CG   . LEU   A  1  222 ? 22.442  -33.625 -28.066  1.00 52.69  ? 222  LEU   A CG   1 
ATOM   3392  C  CD1  . LEU   A  1  222 ? 23.652  -32.750 -27.758  1.00 54.61  ? 222  LEU   A CD1  1 
ATOM   3393  C  CD2  . LEU   A  1  222 ? 22.861  -34.826 -28.906  1.00 48.09  ? 222  LEU   A CD2  1 
ATOM   3394  H  H    . LEU   A  1  222 ? 20.161  -34.358 -24.906  1.00 63.24  ? 222  LEU   A H    1 
ATOM   3395  H  HA   . LEU   A  1  222 ? 21.863  -32.487 -25.499  1.00 64.03  ? 222  LEU   A HA   1 
ATOM   3396  H  HB2  . LEU   A  1  222 ? 22.370  -34.551 -26.246  1.00 64.87  ? 222  LEU   A HB2  1 
ATOM   3397  H  HB3  . LEU   A  1  222 ? 21.004  -34.662 -27.050  1.00 64.87  ? 222  LEU   A HB3  1 
ATOM   3398  H  HG   . LEU   A  1  222 ? 21.817  -33.094 -28.584  1.00 63.21  ? 222  LEU   A HG   1 
ATOM   3399  H  HD11 . LEU   A  1  222 ? 24.090  -32.513 -28.591  1.00 65.52  ? 222  LEU   A HD11 1 
ATOM   3400  H  HD12 . LEU   A  1  222 ? 23.353  -31.948 -27.302  1.00 65.52  ? 222  LEU   A HD12 1 
ATOM   3401  H  HD13 . LEU   A  1  222 ? 24.264  -33.245 -27.192  1.00 65.52  ? 222  LEU   A HD13 1 
ATOM   3402  H  HD21 . LEU   A  1  222 ? 23.332  -34.512 -29.694  1.00 57.69  ? 222  LEU   A HD21 1 
ATOM   3403  H  HD22 . LEU   A  1  222 ? 23.443  -35.394 -28.378  1.00 57.69  ? 222  LEU   A HD22 1 
ATOM   3404  H  HD23 . LEU   A  1  222 ? 22.068  -35.319 -29.170  1.00 57.69  ? 222  LEU   A HD23 1 
ATOM   3405  N  N    . GLY   A  1  223 ? 20.949  -30.841 -27.089  1.00 51.17  ? 223  GLY   A N    1 
ATOM   3406  C  CA   . GLY   A  1  223 ? 20.269  -29.797 -27.825  1.00 52.48  ? 223  GLY   A CA   1 
ATOM   3407  C  C    . GLY   A  1  223 ? 19.467  -28.846 -26.969  1.00 50.48  ? 223  GLY   A C    1 
ATOM   3408  O  O    . GLY   A  1  223 ? 18.746  -28.003 -27.517  1.00 50.18  ? 223  GLY   A O    1 
ATOM   3409  H  H    . GLY   A  1  223 ? 21.759  -30.651 -26.874  1.00 61.38  ? 223  GLY   A H    1 
ATOM   3410  H  HA2  . GLY   A  1  223 ? 20.929  -29.277 -28.310  1.00 62.96  ? 223  GLY   A HA2  1 
ATOM   3411  H  HA3  . GLY   A  1  223 ? 19.663  -30.209 -28.461  1.00 62.96  ? 223  GLY   A HA3  1 
ATOM   3412  N  N    . TYR   A  1  224 ? 19.553  -28.967 -25.642  1.00 49.53  ? 224  TYR   A N    1 
ATOM   3413  C  CA   . TYR   A  1  224 ? 18.941  -27.981 -24.758  1.00 52.36  ? 224  TYR   A CA   1 
ATOM   3414  C  C    . TYR   A  1  224 ? 19.430  -26.580 -25.096  1.00 53.94  ? 224  TYR   A C    1 
ATOM   3415  O  O    . TYR   A  1  224 ? 18.673  -25.606 -25.013  1.00 53.96  ? 224  TYR   A O    1 
ATOM   3416  C  CB   . TYR   A  1  224 ? 19.270  -28.336 -23.306  1.00 54.21  ? 224  TYR   A CB   1 
ATOM   3417  C  CG   . TYR   A  1  224 ? 18.392  -27.691 -22.258  1.00 53.92  ? 224  TYR   A CG   1 
ATOM   3418  C  CD1  . TYR   A  1  224 ? 18.613  -26.386 -21.841  1.00 53.58  ? 224  TYR   A CD1  1 
ATOM   3419  C  CD2  . TYR   A  1  224 ? 17.361  -28.404 -21.659  1.00 50.94  ? 224  TYR   A CD2  1 
ATOM   3420  C  CE1  . TYR   A  1  224 ? 17.819  -25.801 -20.872  1.00 54.03  ? 224  TYR   A CE1  1 
ATOM   3421  C  CE2  . TYR   A  1  224 ? 16.563  -27.829 -20.689  1.00 52.52  ? 224  TYR   A CE2  1 
ATOM   3422  C  CZ   . TYR   A  1  224 ? 16.796  -26.528 -20.299  1.00 52.67  ? 224  TYR   A CZ   1 
ATOM   3423  O  OH   . TYR   A  1  224 ? 16.004  -25.953 -19.332  1.00 50.38  ? 224  TYR   A OH   1 
ATOM   3424  H  H    . TYR   A  1  224 ? 19.958  -29.607 -25.234  1.00 59.42  ? 224  TYR   A H    1 
ATOM   3425  H  HA   . TYR   A  1  224 ? 17.977  -27.996 -24.863  1.00 62.81  ? 224  TYR   A HA   1 
ATOM   3426  H  HB2  . TYR   A  1  224 ? 19.186  -29.296 -23.201  1.00 65.03  ? 224  TYR   A HB2  1 
ATOM   3427  H  HB3  . TYR   A  1  224 ? 20.182  -28.061 -23.126  1.00 65.03  ? 224  TYR   A HB3  1 
ATOM   3428  H  HD1  . TYR   A  1  224 ? 19.307  -25.896 -22.220  1.00 64.28  ? 224  TYR   A HD1  1 
ATOM   3429  H  HD2  . TYR   A  1  224 ? 17.205  -29.284 -21.916  1.00 61.11  ? 224  TYR   A HD2  1 
ATOM   3430  H  HE1  . TYR   A  1  224 ? 17.973  -24.923 -20.608  1.00 64.82  ? 224  TYR   A HE1  1 
ATOM   3431  H  HE2  . TYR   A  1  224 ? 15.872  -28.317 -20.302  1.00 63.01  ? 224  TYR   A HE2  1 
ATOM   3432  H  HH   . TYR   A  1  224 ? 15.471  -26.522 -19.022  1.00 60.43  ? 224  TYR   A HH   1 
ATOM   3433  N  N    . SER   A  1  225 ? 20.697  -26.466 -25.491  1.00 52.68  ? 225  SER   A N    1 
ATOM   3434  C  CA   . SER   A  1  225 ? 21.304  -25.206 -25.889  1.00 51.04  ? 225  SER   A CA   1 
ATOM   3435  C  C    . SER   A  1  225 ? 22.356  -25.513 -26.944  1.00 49.68  ? 225  SER   A C    1 
ATOM   3436  O  O    . SER   A  1  225 ? 22.938  -26.600 -26.951  1.00 49.90  ? 225  SER   A O    1 
ATOM   3437  C  CB   . SER   A  1  225 ? 21.934  -24.484 -24.694  1.00 50.66  ? 225  SER   A CB   1 
ATOM   3438  O  OG   . SER   A  1  225 ? 22.858  -25.325 -24.024  1.00 54.04  ? 225  SER   A OG   1 
ATOM   3439  H  H    . SER   A  1  225 ? 21.242  -27.130 -25.537  1.00 63.20  ? 225  SER   A H    1 
ATOM   3440  H  HA   . SER   A  1  225 ? 20.639  -24.614 -26.272  1.00 61.23  ? 225  SER   A HA   1 
ATOM   3441  H  HB2  . SER   A  1  225 ? 22.399  -23.694 -25.012  1.00 60.78  ? 225  SER   A HB2  1 
ATOM   3442  H  HB3  . SER   A  1  225 ? 21.233  -24.229 -24.074  1.00 60.78  ? 225  SER   A HB3  1 
ATOM   3443  H  HG   . SER   A  1  225 ? 22.676  -25.358 -23.205  1.00 64.82  ? 225  SER   A HG   1 
ATOM   3444  N  N    . VAL   A  1  226 ? 22.588  -24.557 -27.844  1.00 49.61  ? 226  VAL   A N    1 
ATOM   3445  C  CA   . VAL   A  1  226 ? 23.540  -24.749 -28.930  1.00 50.76  ? 226  VAL   A CA   1 
ATOM   3446  C  C    . VAL   A  1  226 ? 24.306  -23.460 -29.185  1.00 52.88  ? 226  VAL   A C    1 
ATOM   3447  O  O    . VAL   A  1  226 ? 23.792  -22.353 -28.994  1.00 56.11  ? 226  VAL   A O    1 
ATOM   3448  C  CB   . VAL   A  1  226 ? 22.854  -25.220 -30.234  1.00 53.20  ? 226  VAL   A CB   1 
ATOM   3449  C  CG1  . VAL   A  1  226 ? 22.170  -26.563 -30.023  1.00 53.88  ? 226  VAL   A CG1  1 
ATOM   3450  C  CG2  . VAL   A  1  226 ? 21.864  -24.174 -30.734  1.00 54.11  ? 226  VAL   A CG2  1 
ATOM   3451  H  H    . VAL   A  1  226 ? 22.204  -23.788 -27.843  1.00 59.52  ? 226  VAL   A H    1 
ATOM   3452  H  HA   . VAL   A  1  226 ? 24.177  -25.424 -28.648  1.00 60.89  ? 226  VAL   A HA   1 
ATOM   3453  H  HB   . VAL   A  1  226 ? 23.531  -25.335 -30.920  1.00 63.82  ? 226  VAL   A HB   1 
ATOM   3454  H  HG11 . VAL   A  1  226 ? 21.774  -26.851 -30.860  1.00 64.63  ? 226  VAL   A HG11 1 
ATOM   3455  H  HG12 . VAL   A  1  226 ? 22.830  -27.211 -29.730  1.00 64.63  ? 226  VAL   A HG12 1 
ATOM   3456  H  HG13 . VAL   A  1  226 ? 21.481  -26.464 -29.348  1.00 64.63  ? 226  VAL   A HG13 1 
ATOM   3457  H  HG21 . VAL   A  1  226 ? 21.428  -24.508 -31.533  1.00 64.91  ? 226  VAL   A HG21 1 
ATOM   3458  H  HG22 . VAL   A  1  226 ? 21.204  -24.007 -30.043  1.00 64.91  ? 226  VAL   A HG22 1 
ATOM   3459  H  HG23 . VAL   A  1  226 ? 22.344  -23.356 -30.937  1.00 64.91  ? 226  VAL   A HG23 1 
ATOM   3460  N  N    . ALA   A  1  227 ? 25.551  -23.622 -29.624  1.00 54.41  ? 227  ALA   A N    1 
ATOM   3461  C  CA   . ALA   A  1  227 ? 26.381  -22.524 -30.094  1.00 55.70  ? 227  ALA   A CA   1 
ATOM   3462  C  C    . ALA   A  1  227 ? 27.276  -23.072 -31.196  1.00 54.74  ? 227  ALA   A C    1 
ATOM   3463  O  O    . ALA   A  1  227 ? 27.387  -24.286 -31.383  1.00 52.39  ? 227  ALA   A O    1 
ATOM   3464  C  CB   . ALA   A  1  227 ? 27.205  -21.909 -28.961  1.00 57.97  ? 227  ALA   A CB   1 
ATOM   3465  H  H    . ALA   A  1  227 ? 25.949  -24.384 -29.659  1.00 65.27  ? 227  ALA   A H    1 
ATOM   3466  H  HA   . ALA   A  1  227 ? 25.824  -21.819 -30.459  1.00 66.82  ? 227  ALA   A HA   1 
ATOM   3467  H  HB1  . ALA   A  1  227 ? 27.745  -21.187 -29.319  1.00 69.55  ? 227  ALA   A HB1  1 
ATOM   3468  H  HB2  . ALA   A  1  227 ? 26.603  -21.566 -28.282  1.00 69.55  ? 227  ALA   A HB2  1 
ATOM   3469  H  HB3  . ALA   A  1  227 ? 27.778  -22.593 -28.580  1.00 69.55  ? 227  ALA   A HB3  1 
ATOM   3470  N  N    . VAL   A  1  228 ? 27.916  -22.166 -31.932  1.00 53.15  ? 228  VAL   A N    1 
ATOM   3471  C  CA   . VAL   A  1  228 ? 28.737  -22.548 -33.071  1.00 53.01  ? 228  VAL   A CA   1 
ATOM   3472  C  C    . VAL   A  1  228 ? 30.095  -21.869 -32.982  1.00 59.02  ? 228  VAL   A C    1 
ATOM   3473  O  O    . VAL   A  1  228 ? 30.228  -20.754 -32.468  1.00 65.23  ? 228  VAL   A O    1 
ATOM   3474  C  CB   . VAL   A  1  228 ? 28.050  -22.209 -34.413  1.00 54.99  ? 228  VAL   A CB   1 
ATOM   3475  C  CG1  . VAL   A  1  228 ? 26.858  -23.126 -34.638  1.00 49.09  ? 228  VAL   A CG1  1 
ATOM   3476  C  CG2  . VAL   A  1  228 ? 27.620  -20.750 -34.444  1.00 59.55  ? 228  VAL   A CG2  1 
ATOM   3477  H  H    . VAL   A  1  228 ? 27.888  -21.319 -31.787  1.00 63.76  ? 228  VAL   A H    1 
ATOM   3478  H  HA   . VAL   A  1  228 ? 28.888  -23.505 -33.032  1.00 63.59  ? 228  VAL   A HA   1 
ATOM   3479  H  HB   . VAL   A  1  228 ? 28.683  -22.347 -35.135  1.00 65.97  ? 228  VAL   A HB   1 
ATOM   3480  H  HG11 . VAL   A  1  228 ? 26.452  -22.912 -35.492  1.00 58.89  ? 228  VAL   A HG11 1 
ATOM   3481  H  HG12 . VAL   A  1  228 ? 27.164  -24.047 -34.638  1.00 58.89  ? 228  VAL   A HG12 1 
ATOM   3482  H  HG13 . VAL   A  1  228 ? 26.216  -22.991 -33.923  1.00 58.89  ? 228  VAL   A HG13 1 
ATOM   3483  H  HG21 . VAL   A  1  228 ? 27.203  -20.562 -35.300  1.00 71.44  ? 228  VAL   A HG21 1 
ATOM   3484  H  HG22 . VAL   A  1  228 ? 26.988  -20.592 -33.726  1.00 71.44  ? 228  VAL   A HG22 1 
ATOM   3485  H  HG23 . VAL   A  1  228 ? 28.402  -20.188 -34.327  1.00 71.44  ? 228  VAL   A HG23 1 
ATOM   3486  N  N    . GLY   A  1  229 ? 31.107  -22.560 -33.497  1.00 58.93  ? 229  GLY   A N    1 
ATOM   3487  C  CA   . GLY   A  1  229 ? 32.467  -22.066 -33.514  1.00 60.42  ? 229  GLY   A CA   1 
ATOM   3488  C  C    . GLY   A  1  229 ? 33.398  -23.147 -34.019  1.00 61.10  ? 229  GLY   A C    1 
ATOM   3489  O  O    . GLY   A  1  229 ? 33.083  -24.335 -33.903  1.00 63.51  ? 229  GLY   A O    1 
ATOM   3490  H  H    . GLY   A  1  229 ? 31.024  -23.338 -33.852  1.00 70.69  ? 229  GLY   A H    1 
ATOM   3491  H  HA2  . GLY   A  1  229 ? 32.532  -21.294 -34.098  1.00 72.48  ? 229  GLY   A HA2  1 
ATOM   3492  H  HA3  . GLY   A  1  229 ? 32.737  -21.809 -32.619  1.00 72.48  ? 229  GLY   A HA3  1 
ATOM   3493  N  N    . ASP   A  1  230 ? 34.537  -22.761 -34.588  1.00 58.50  ? 230  ASP   A N    1 
ATOM   3494  C  CA   . ASP   A  1  230 ? 35.486  -23.721 -35.137  1.00 61.16  ? 230  ASP   A CA   1 
ATOM   3495  C  C    . ASP   A  1  230 ? 36.421  -24.202 -34.034  1.00 63.70  ? 230  ASP   A C    1 
ATOM   3496  O  O    . ASP   A  1  230 ? 36.982  -23.391 -33.290  1.00 66.31  ? 230  ASP   A O    1 
ATOM   3497  C  CB   . ASP   A  1  230 ? 36.294  -23.100 -36.278  1.00 59.34  ? 230  ASP   A CB   1 
ATOM   3498  C  CG   . ASP   A  1  230 ? 37.010  -24.143 -37.120  1.00 60.74  ? 230  ASP   A CG   1 
ATOM   3499  O  OD1  . ASP   A  1  230 ? 36.622  -25.328 -37.059  1.00 59.67  ? 230  ASP   A OD1  1 
ATOM   3500  O  OD2  . ASP   A  1  230 ? 37.964  -23.779 -37.841  1.00 63.47  ? 230  ASP   A OD2  1 
ATOM   3501  H  H    . ASP   A  1  230 ? 34.783  -21.941 -34.669  1.00 70.18  ? 230  ASP   A H    1 
ATOM   3502  H  HA   . ASP   A  1  230 ? 35.003  -24.484 -35.490  1.00 73.37  ? 230  ASP   A HA   1 
ATOM   3503  H  HB2  . ASP   A  1  230 ? 35.693  -22.606 -36.858  1.00 71.18  ? 230  ASP   A HB2  1 
ATOM   3504  H  HB3  . ASP   A  1  230 ? 36.962  -22.504 -35.906  1.00 71.18  ? 230  ASP   A HB3  1 
ATOM   3505  N  N    . PHE   A  1  231 ? 36.588  -25.523 -33.934  1.00 63.76  ? 231  PHE   A N    1 
ATOM   3506  C  CA   . PHE   A  1  231 ? 37.419  -26.110 -32.894  1.00 66.95  ? 231  PHE   A CA   1 
ATOM   3507  C  C    . PHE   A  1  231 ? 38.377  -27.179 -33.400  1.00 68.37  ? 231  PHE   A C    1 
ATOM   3508  O  O    . PHE   A  1  231 ? 39.070  -27.798 -32.585  1.00 71.35  ? 231  PHE   A O    1 
ATOM   3509  C  CB   . PHE   A  1  231 ? 36.536  -26.694 -31.782  1.00 64.70  ? 231  PHE   A CB   1 
ATOM   3510  C  CG   . PHE   A  1  231 ? 35.722  -25.658 -31.065  1.00 61.12  ? 231  PHE   A CG   1 
ATOM   3511  C  CD1  . PHE   A  1  231 ? 36.280  -24.908 -30.045  1.00 61.02  ? 231  PHE   A CD1  1 
ATOM   3512  C  CD2  . PHE   A  1  231 ? 34.406  -25.420 -31.424  1.00 57.90  ? 231  PHE   A CD2  1 
ATOM   3513  C  CE1  . PHE   A  1  231 ? 35.540  -23.946 -29.388  1.00 60.92  ? 231  PHE   A CE1  1 
ATOM   3514  C  CE2  . PHE   A  1  231 ? 33.659  -24.459 -30.771  1.00 57.41  ? 231  PHE   A CE2  1 
ATOM   3515  C  CZ   . PHE   A  1  231 ? 34.227  -23.721 -29.751  1.00 58.07  ? 231  PHE   A CZ   1 
ATOM   3516  H  H    . PHE   A  1  231 ? 36.226  -26.099 -34.460  1.00 76.50  ? 231  PHE   A H    1 
ATOM   3517  H  HA   . PHE   A  1  231 ? 37.964  -25.409 -32.503  1.00 80.32  ? 231  PHE   A HA   1 
ATOM   3518  H  HB2  . PHE   A  1  231 ? 35.923  -27.336 -32.173  1.00 77.61  ? 231  PHE   A HB2  1 
ATOM   3519  H  HB3  . PHE   A  1  231 ? 37.103  -27.132 -31.129  1.00 77.61  ? 231  PHE   A HB3  1 
ATOM   3520  H  HD1  . PHE   A  1  231 ? 37.166  -25.053 -29.799  1.00 73.20  ? 231  PHE   A HD1  1 
ATOM   3521  H  HD2  . PHE   A  1  231 ? 34.021  -25.912 -32.113  1.00 69.46  ? 231  PHE   A HD2  1 
ATOM   3522  H  HE1  . PHE   A  1  231 ? 35.925  -23.450 -28.702  1.00 73.09  ? 231  PHE   A HE1  1 
ATOM   3523  H  HE2  . PHE   A  1  231 ? 32.775  -24.310 -31.017  1.00 68.87  ? 231  PHE   A HE2  1 
ATOM   3524  H  HZ   . PHE   A  1  231 ? 33.726  -23.073 -29.310  1.00 69.66  ? 231  PHE   A HZ   1 
ATOM   3525  N  N    . ASN   A  1  232 ? 38.438  -27.419 -34.711  1.00 66.41  ? 232  ASN   A N    1 
ATOM   3526  C  CA   . ASN   A  1  232 ? 39.506  -28.210 -35.311  1.00 66.59  ? 232  ASN   A CA   1 
ATOM   3527  C  C    . ASN   A  1  232 ? 40.235  -27.426 -36.398  1.00 68.77  ? 232  ASN   A C    1 
ATOM   3528  O  O    . ASN   A  1  232 ? 40.930  -28.018 -37.230  1.00 69.77  ? 232  ASN   A O    1 
ATOM   3529  C  CB   . ASN   A  1  232 ? 38.966  -29.529 -35.866  1.00 68.45  ? 232  ASN   A CB   1 
ATOM   3530  C  CG   . ASN   A  1  232 ? 37.760  -29.341 -36.757  1.00 73.97  ? 232  ASN   A CG   1 
ATOM   3531  O  OD1  . ASN   A  1  232 ? 37.335  -28.217 -37.016  1.00 78.58  ? 232  ASN   A OD1  1 
ATOM   3532  N  ND2  . ASN   A  1  232 ? 37.202  -30.446 -37.238  1.00 75.17  ? 232  ASN   A ND2  1 
ATOM   3533  H  H    . ASN   A  1  232 ? 37.862  -27.128 -35.280  1.00 79.67  ? 232  ASN   A H    1 
ATOM   3534  H  HA   . ASN   A  1  232 ? 40.150  -28.435 -34.621  1.00 79.89  ? 232  ASN   A HA   1 
ATOM   3535  H  HB2  . ASN   A  1  232 ? 39.660  -29.960 -36.388  1.00 82.12  ? 232  ASN   A HB2  1 
ATOM   3536  H  HB3  . ASN   A  1  232 ? 38.705  -30.100 -35.126  1.00 82.12  ? 232  ASN   A HB3  1 
ATOM   3537  H  HD21 . ASN   A  1  232 ? 36.513  -30.392 -37.750  1.00 90.18  ? 232  ASN   A HD21 1 
ATOM   3538  H  HD22 . ASN   A  1  232 ? 37.530  -31.216 -37.038  1.00 90.18  ? 232  ASN   A HD22 1 
ATOM   3539  N  N    . GLY   A  1  233 ? 40.075  -26.103 -36.411  1.00 68.71  ? 233  GLY   A N    1 
ATOM   3540  C  CA   . GLY   A  1  233 ? 40.896  -25.242 -37.240  1.00 67.59  ? 233  GLY   A CA   1 
ATOM   3541  C  C    . GLY   A  1  233 ? 40.759  -25.443 -38.731  1.00 69.96  ? 233  GLY   A C    1 
ATOM   3542  O  O    . GLY   A  1  233 ? 41.677  -25.090 -39.475  1.00 76.56  ? 233  GLY   A O    1 
ATOM   3543  H  H    . GLY   A  1  233 ? 39.492  -25.680 -35.942  1.00 82.43  ? 233  GLY   A H    1 
ATOM   3544  H  HA2  . GLY   A  1  233 ? 40.666  -24.320 -37.047  1.00 81.09  ? 233  GLY   A HA2  1 
ATOM   3545  H  HA3  . GLY   A  1  233 ? 41.827  -25.390 -37.010  1.00 81.09  ? 233  GLY   A HA3  1 
ATOM   3546  N  N    . ASP   A  1  234 ? 39.639  -25.991 -39.199  1.00 65.14  ? 234  ASP   A N    1 
ATOM   3547  C  CA   . ASP   A  1  234 ? 39.411  -26.170 -40.627  1.00 65.73  ? 234  ASP   A CA   1 
ATOM   3548  C  C    . ASP   A  1  234 ? 38.479  -25.116 -41.211  1.00 66.83  ? 234  ASP   A C    1 
ATOM   3549  O  O    . ASP   A  1  234 ? 38.004  -25.281 -42.339  1.00 71.40  ? 234  ASP   A O    1 
ATOM   3550  C  CB   . ASP   A  1  234 ? 38.858  -27.571 -40.907  1.00 67.03  ? 234  ASP   A CB   1 
ATOM   3551  C  CG   . ASP   A  1  234 ? 37.461  -27.780 -40.348  1.00 65.95  ? 234  ASP   A CG   1 
ATOM   3552  O  OD1  . ASP   A  1  234 ? 36.952  -26.897 -39.623  1.00 67.01  ? 234  ASP   A OD1  1 
ATOM   3553  O  OD2  . ASP   A  1  234 ? 36.868  -28.840 -40.638  1.00 67.69  ? 234  ASP   A OD2  1 
ATOM   3554  H  H    . ASP   A  1  234 ? 38.993  -26.268 -38.703  1.00 78.15  ? 234  ASP   A H    1 
ATOM   3555  H  HA   . ASP   A  1  234 ? 40.265  -26.094 -41.081  1.00 78.85  ? 234  ASP   A HA   1 
ATOM   3556  H  HB2  . ASP   A  1  234 ? 38.820  -27.709 -41.866  1.00 80.42  ? 234  ASP   A HB2  1 
ATOM   3557  H  HB3  . ASP   A  1  234 ? 39.444  -28.228 -40.500  1.00 80.42  ? 234  ASP   A HB3  1 
ATOM   3558  N  N    . GLY   A  1  235 ? 38.208  -24.039 -40.474  1.00 64.41  ? 235  GLY   A N    1 
ATOM   3559  C  CA   . GLY   A  1  235 ? 37.353  -22.974 -40.953  1.00 64.52  ? 235  GLY   A CA   1 
ATOM   3560  C  C    . GLY   A  1  235 ? 35.876  -23.291 -40.974  1.00 66.60  ? 235  GLY   A C    1 
ATOM   3561  O  O    . GLY   A  1  235 ? 35.071  -22.384 -41.218  1.00 70.14  ? 235  GLY   A O    1 
ATOM   3562  H  H    . GLY   A  1  235 ? 38.515  -23.907 -39.682  1.00 77.28  ? 235  GLY   A H    1 
ATOM   3563  H  HA2  . GLY   A  1  235 ? 37.479  -22.198 -40.385  1.00 77.40  ? 235  GLY   A HA2  1 
ATOM   3564  H  HA3  . GLY   A  1  235 ? 37.618  -22.750 -41.859  1.00 77.40  ? 235  GLY   A HA3  1 
ATOM   3565  N  N    . ILE   A  1  236 ? 35.487  -24.538 -40.732  1.00 61.80  ? 236  ILE   A N    1 
ATOM   3566  C  CA   . ILE   A  1  236 ? 34.083  -24.931 -40.716  1.00 60.42  ? 236  ILE   A CA   1 
ATOM   3567  C  C    . ILE   A  1  236 ? 33.580  -24.828 -39.282  1.00 62.63  ? 236  ILE   A C    1 
ATOM   3568  O  O    . ILE   A  1  236 ? 34.127  -25.466 -38.376  1.00 63.82  ? 236  ILE   A O    1 
ATOM   3569  C  CB   . ILE   A  1  236 ? 33.897  -26.351 -41.271  1.00 58.94  ? 236  ILE   A CB   1 
ATOM   3570  C  CG1  . ILE   A  1  236 ? 34.380  -26.412 -42.724  1.00 61.30  ? 236  ILE   A CG1  1 
ATOM   3571  C  CG2  . ILE   A  1  236 ? 32.435  -26.780 -41.178  1.00 54.31  ? 236  ILE   A CG2  1 
ATOM   3572  C  CD1  . ILE   A  1  236 ? 34.431  -27.804 -43.303  1.00 60.88  ? 236  ILE   A CD1  1 
ATOM   3573  H  H    . ILE   A  1  236 ? 36.028  -25.187 -40.572  1.00 74.14  ? 236  ILE   A H    1 
ATOM   3574  H  HA   . ILE   A  1  236 ? 33.569  -24.321 -41.267  1.00 72.48  ? 236  ILE   A HA   1 
ATOM   3575  H  HB   . ILE   A  1  236 ? 34.428  -26.962 -40.737  1.00 70.71  ? 236  ILE   A HB   1 
ATOM   3576  H  HG12 . ILE   A  1  236 ? 33.776  -25.887 -43.273  1.00 73.55  ? 236  ILE   A HG12 1 
ATOM   3577  H  HG13 . ILE   A  1  236 ? 35.275  -26.041 -42.768  1.00 73.55  ? 236  ILE   A HG13 1 
ATOM   3578  H  HG21 . ILE   A  1  236 ? 32.342  -27.669 -41.554  1.00 65.15  ? 236  ILE   A HG21 1 
ATOM   3579  H  HG22 . ILE   A  1  236 ? 32.166  -26.785 -40.246  1.00 65.15  ? 236  ILE   A HG22 1 
ATOM   3580  H  HG23 . ILE   A  1  236 ? 31.890  -26.151 -41.676  1.00 65.15  ? 236  ILE   A HG23 1 
ATOM   3581  H  HD11 . ILE   A  1  236 ? 34.803  -27.760 -44.197  1.00 73.04  ? 236  ILE   A HD11 1 
ATOM   3582  H  HD12 . ILE   A  1  236 ? 34.991  -28.360 -42.738  1.00 73.04  ? 236  ILE   A HD12 1 
ATOM   3583  H  HD13 . ILE   A  1  236 ? 33.532  -28.166 -43.336  1.00 73.04  ? 236  ILE   A HD13 1 
ATOM   3584  N  N    . ASP   A  1  237 ? 32.545  -24.018 -39.073  1.00 64.90  ? 237  ASP   A N    1 
ATOM   3585  C  CA   . ASP   A  1  237 ? 31.961  -23.888 -37.746  1.00 64.18  ? 237  ASP   A CA   1 
ATOM   3586  C  C    . ASP   A  1  237 ? 31.503  -25.247 -37.236  1.00 61.27  ? 237  ASP   A C    1 
ATOM   3587  O  O    . ASP   A  1  237 ? 30.884  -26.026 -37.965  1.00 57.25  ? 237  ASP   A O    1 
ATOM   3588  C  CB   . ASP   A  1  237 ? 30.783  -22.915 -37.775  1.00 64.15  ? 237  ASP   A CB   1 
ATOM   3589  C  CG   . ASP   A  1  237 ? 31.223  -21.466 -37.728  1.00 70.31  ? 237  ASP   A CG   1 
ATOM   3590  O  OD1  . ASP   A  1  237 ? 32.443  -21.218 -37.626  1.00 74.28  ? 237  ASP   A OD1  1 
ATOM   3591  O  OD2  . ASP   A  1  237 ? 30.349  -20.576 -37.791  1.00 70.36  ? 237  ASP   A OD2  1 
ATOM   3592  H  H    . ASP   A  1  237 ? 32.168  -23.537 -39.679  1.00 77.86  ? 237  ASP   A H    1 
ATOM   3593  H  HA   . ASP   A  1  237 ? 32.627  -23.536 -37.135  1.00 76.99  ? 237  ASP   A HA   1 
ATOM   3594  H  HB2  . ASP   A  1  237 ? 30.280  -23.050 -38.593  1.00 76.96  ? 237  ASP   A HB2  1 
ATOM   3595  H  HB3  . ASP   A  1  237 ? 30.216  -23.081 -37.006  1.00 76.96  ? 237  ASP   A HB3  1 
ATOM   3596  N  N    . ASP   A  1  238 ? 31.812  -25.527 -35.974  1.00 60.92  ? 238  ASP   A N    1 
ATOM   3597  C  CA   . ASP   A  1  238 ? 31.471  -26.783 -35.326  1.00 57.13  ? 238  ASP   A CA   1 
ATOM   3598  C  C    . ASP   A  1  238 ? 30.366  -26.555 -34.301  1.00 57.62  ? 238  ASP   A C    1 
ATOM   3599  O  O    . ASP   A  1  238 ? 30.100  -25.426 -33.880  1.00 54.78  ? 238  ASP   A O    1 
ATOM   3600  C  CB   . ASP   A  1  238 ? 32.709  -27.399 -34.666  1.00 55.50  ? 238  ASP   A CB   1 
ATOM   3601  C  CG   . ASP   A  1  238 ? 33.824  -27.676 -35.667  1.00 58.99  ? 238  ASP   A CG   1 
ATOM   3602  O  OD1  . ASP   A  1  238 ? 33.539  -28.274 -36.727  1.00 59.39  ? 238  ASP   A OD1  1 
ATOM   3603  O  OD2  . ASP   A  1  238 ? 34.983  -27.287 -35.405  1.00 59.18  ? 238  ASP   A OD2  1 
ATOM   3604  H  H    . ASP   A  1  238 ? 32.234  -24.984 -35.457  1.00 73.09  ? 238  ASP   A H    1 
ATOM   3605  H  HA   . ASP   A  1  238 ? 31.137  -27.417 -35.980  1.00 68.54  ? 238  ASP   A HA   1 
ATOM   3606  H  HB2  . ASP   A  1  238 ? 33.051  -26.785 -33.997  1.00 66.58  ? 238  ASP   A HB2  1 
ATOM   3607  H  HB3  . ASP   A  1  238 ? 32.462  -28.239 -34.250  1.00 66.58  ? 238  ASP   A HB3  1 
ATOM   3608  N  N    . PHE   A  1  239 ? 29.722  -27.649 -33.899  1.00 57.35  ? 239  PHE   A N    1 
ATOM   3609  C  CA   . PHE   A  1  239 ? 28.483  -27.592 -33.133  1.00 55.75  ? 239  PHE   A CA   1 
ATOM   3610  C  C    . PHE   A  1  239 ? 28.764  -27.823 -31.653  1.00 56.78  ? 239  PHE   A C    1 
ATOM   3611  O  O    . PHE   A  1  239 ? 29.217  -28.903 -31.264  1.00 60.32  ? 239  PHE   A O    1 
ATOM   3612  C  CB   . PHE   A  1  239 ? 27.487  -28.632 -33.649  1.00 52.18  ? 239  PHE   A CB   1 
ATOM   3613  C  CG   . PHE   A  1  239 ? 27.270  -28.578 -35.134  1.00 53.85  ? 239  PHE   A CG   1 
ATOM   3614  C  CD1  . PHE   A  1  239 ? 27.305  -27.369 -35.812  1.00 54.92  ? 239  PHE   A CD1  1 
ATOM   3615  C  CD2  . PHE   A  1  239 ? 27.038  -29.739 -35.855  1.00 52.33  ? 239  PHE   A CD2  1 
ATOM   3616  C  CE1  . PHE   A  1  239 ? 27.108  -27.317 -37.180  1.00 55.25  ? 239  PHE   A CE1  1 
ATOM   3617  C  CE2  . PHE   A  1  239 ? 26.840  -29.695 -37.223  1.00 53.42  ? 239  PHE   A CE2  1 
ATOM   3618  C  CZ   . PHE   A  1  239 ? 26.876  -28.481 -37.888  1.00 54.31  ? 239  PHE   A CZ   1 
ATOM   3619  H  H    . PHE   A  1  239 ? 29.990  -28.449 -34.062  1.00 68.80  ? 239  PHE   A H    1 
ATOM   3620  H  HA   . PHE   A  1  239 ? 28.099  -26.706 -33.226  1.00 66.89  ? 239  PHE   A HA   1 
ATOM   3621  H  HB2  . PHE   A  1  239 ? 27.819  -29.517 -33.430  1.00 62.59  ? 239  PHE   A HB2  1 
ATOM   3622  H  HB3  . PHE   A  1  239 ? 26.630  -28.483 -33.219  1.00 62.59  ? 239  PHE   A HB3  1 
ATOM   3623  H  HD1  . PHE   A  1  239 ? 27.463  -26.583 -35.340  1.00 65.89  ? 239  PHE   A HD1  1 
ATOM   3624  H  HD2  . PHE   A  1  239 ? 27.015  -30.557 -35.413  1.00 62.78  ? 239  PHE   A HD2  1 
ATOM   3625  H  HE1  . PHE   A  1  239 ? 27.132  -26.500 -37.623  1.00 66.28  ? 239  PHE   A HE1  1 
ATOM   3626  H  HE2  . PHE   A  1  239 ? 26.683  -30.481 -37.696  1.00 64.09  ? 239  PHE   A HE2  1 
ATOM   3627  H  HZ   . PHE   A  1  239 ? 26.744  -28.449 -38.808  1.00 65.16  ? 239  PHE   A HZ   1 
ATOM   3628  N  N    . VAL   A  1  240 ? 28.483  -26.809 -30.836  1.00 54.56  ? 240  VAL   A N    1 
ATOM   3629  C  CA   . VAL   A  1  240 ? 28.528  -26.912 -29.381  1.00 52.25  ? 240  VAL   A CA   1 
ATOM   3630  C  C    . VAL   A  1  240 ? 27.098  -27.040 -28.881  1.00 53.77  ? 240  VAL   A C    1 
ATOM   3631  O  O    . VAL   A  1  240 ? 26.196  -26.357 -29.381  1.00 55.73  ? 240  VAL   A O    1 
ATOM   3632  C  CB   . VAL   A  1  240 ? 29.221  -25.687 -28.754  1.00 54.63  ? 240  VAL   A CB   1 
ATOM   3633  C  CG1  . VAL   A  1  240 ? 29.352  -25.857 -27.244  1.00 55.72  ? 240  VAL   A CG1  1 
ATOM   3634  C  CG2  . VAL   A  1  240 ? 30.581  -25.449 -29.394  1.00 54.31  ? 240  VAL   A CG2  1 
ATOM   3635  H  H    . VAL   A  1  240 ? 28.256  -26.027 -31.111  1.00 65.45  ? 240  VAL   A H    1 
ATOM   3636  H  HA   . VAL   A  1  240 ? 29.031  -27.702 -29.125  1.00 62.68  ? 240  VAL   A HA   1 
ATOM   3637  H  HB   . VAL   A  1  240 ? 28.674  -24.903 -28.920  1.00 65.53  ? 240  VAL   A HB   1 
ATOM   3638  H  HG11 . VAL   A  1  240 ? 29.835  -25.098 -26.882  1.00 66.85  ? 240  VAL   A HG11 1 
ATOM   3639  H  HG12 . VAL   A  1  240 ? 28.465  -25.902 -26.854  1.00 66.85  ? 240  VAL   A HG12 1 
ATOM   3640  H  HG13 . VAL   A  1  240 ? 29.837  -26.676 -27.060  1.00 66.85  ? 240  VAL   A HG13 1 
ATOM   3641  H  HG21 . VAL   A  1  240 ? 31.009  -24.698 -28.955  1.00 65.15  ? 240  VAL   A HG21 1 
ATOM   3642  H  HG22 . VAL   A  1  240 ? 31.123  -26.246 -29.291  1.00 65.15  ? 240  VAL   A HG22 1 
ATOM   3643  H  HG23 . VAL   A  1  240 ? 30.456  -25.254 -30.337  1.00 65.15  ? 240  VAL   A HG23 1 
ATOM   3644  N  N    . SER   A  1  241 ? 26.879  -27.911 -27.897  1.00 52.81  ? 241  SER   A N    1 
ATOM   3645  C  CA   . SER   A  1  241 ? 25.532  -28.115 -27.384  1.00 54.78  ? 241  SER   A CA   1 
ATOM   3646  C  C    . SER   A  1  241 ? 25.574  -28.555 -25.929  1.00 53.61  ? 241  SER   A C    1 
ATOM   3647  O  O    . SER   A  1  241 ? 26.368  -29.422 -25.553  1.00 50.50  ? 241  SER   A O    1 
ATOM   3648  C  CB   . SER   A  1  241 ? 24.771  -29.155 -28.214  1.00 57.10  ? 241  SER   A CB   1 
ATOM   3649  O  OG   . SER   A  1  241 ? 23.473  -29.365 -27.687  1.00 57.19  ? 241  SER   A OG   1 
ATOM   3650  H  H    . SER   A  1  241 ? 27.487  -28.386 -27.517  1.00 63.36  ? 241  SER   A H    1 
ATOM   3651  H  HA   . SER   A  1  241 ? 25.060  -27.269 -27.419  1.00 65.72  ? 241  SER   A HA   1 
ATOM   3652  H  HB2  . SER   A  1  241 ? 24.693  -28.835 -29.127  1.00 68.51  ? 241  SER   A HB2  1 
ATOM   3653  H  HB3  . SER   A  1  241 ? 25.259  -29.993 -28.197  1.00 68.51  ? 241  SER   A HB3  1 
ATOM   3654  H  HG   . SER   A  1  241 ? 23.097  -28.628 -27.545  1.00 68.61  ? 241  SER   A HG   1 
ATOM   3655  N  N    . GLY   A  1  242 ? 24.702  -27.954 -25.121  1.00 54.00  ? 242  GLY   A N    1 
ATOM   3656  C  CA   . GLY   A  1  242 ? 24.592  -28.335 -23.725  1.00 51.49  ? 242  GLY   A CA   1 
ATOM   3657  C  C    . GLY   A  1  242 ? 23.730  -29.575 -23.548  1.00 52.74  ? 242  GLY   A C    1 
ATOM   3658  O  O    . GLY   A  1  242 ? 22.732  -29.775 -24.240  1.00 54.66  ? 242  GLY   A O    1 
ATOM   3659  H  H    . GLY   A  1  242 ? 24.166  -27.325 -25.361  1.00 64.78  ? 242  GLY   A H    1 
ATOM   3660  H  HA2  . GLY   A  1  242 ? 25.475  -28.519 -23.368  1.00 61.76  ? 242  GLY   A HA2  1 
ATOM   3661  H  HA3  . GLY   A  1  242 ? 24.194  -27.608 -23.221  1.00 61.76  ? 242  GLY   A HA3  1 
ATOM   3662  N  N    . VAL   A  1  243 ? 24.135  -30.415 -22.601  1.00 54.22  ? 243  VAL   A N    1 
ATOM   3663  C  CA   . VAL   A  1  243 ? 23.437  -31.660 -22.287  1.00 50.64  ? 243  VAL   A CA   1 
ATOM   3664  C  C    . VAL   A  1  243 ? 23.267  -31.695 -20.772  1.00 51.68  ? 243  VAL   A C    1 
ATOM   3665  O  O    . VAL   A  1  243 ? 24.017  -32.396 -20.078  1.00 52.67  ? 243  VAL   A O    1 
ATOM   3666  C  CB   . VAL   A  1  243 ? 24.210  -32.878 -22.812  1.00 49.11  ? 243  VAL   A CB   1 
ATOM   3667  C  CG1  . VAL   A  1  243 ? 23.315  -34.100 -22.842  1.00 49.23  ? 243  VAL   A CG1  1 
ATOM   3668  C  CG2  . VAL   A  1  243 ? 24.774  -32.594 -24.199  1.00 50.55  ? 243  VAL   A CG2  1 
ATOM   3669  H  H    . VAL   A  1  243 ? 24.831  -30.284 -22.113  1.00 65.04  ? 243  VAL   A H    1 
ATOM   3670  H  HA   . VAL   A  1  243 ? 22.563  -31.680 -22.706  1.00 60.74  ? 243  VAL   A HA   1 
ATOM   3671  H  HB   . VAL   A  1  243 ? 24.952  -33.061 -22.214  1.00 58.91  ? 243  VAL   A HB   1 
ATOM   3672  H  HG11 . VAL   A  1  243 ? 23.838  -34.867 -23.122  1.00 59.06  ? 243  VAL   A HG11 1 
ATOM   3673  H  HG12 . VAL   A  1  243 ? 22.957  -34.250 -21.954  1.00 59.06  ? 243  VAL   A HG12 1 
ATOM   3674  H  HG13 . VAL   A  1  243 ? 22.592  -33.946 -23.469  1.00 59.06  ? 243  VAL   A HG13 1 
ATOM   3675  H  HG21 . VAL   A  1  243 ? 25.189  -33.401 -24.543  1.00 60.64  ? 243  VAL   A HG21 1 
ATOM   3676  H  HG22 . VAL   A  1  243 ? 24.051  -32.319 -24.784  1.00 60.64  ? 243  VAL   A HG22 1 
ATOM   3677  H  HG23 . VAL   A  1  243 ? 25.434  -31.886 -24.133  1.00 60.64  ? 243  VAL   A HG23 1 
ATOM   3678  N  N    . PRO   A  1  244 ? 22.294  -30.964 -20.219  1.00 49.95  ? 244  PRO   A N    1 
ATOM   3679  C  CA   . PRO   A  1  244 ? 22.338  -30.647 -18.780  1.00 51.59  ? 244  PRO   A CA   1 
ATOM   3680  C  C    . PRO   A  1  244 ? 21.988  -31.794 -17.844  1.00 50.62  ? 244  PRO   A C    1 
ATOM   3681  O  O    . PRO   A  1  244 ? 22.295  -31.690 -16.649  1.00 54.76  ? 244  PRO   A O    1 
ATOM   3682  C  CB   . PRO   A  1  244 ? 21.324  -29.502 -18.643  1.00 53.54  ? 244  PRO   A CB   1 
ATOM   3683  C  CG   . PRO   A  1  244 ? 20.380  -29.691 -19.787  1.00 51.88  ? 244  PRO   A CG   1 
ATOM   3684  C  CD   . PRO   A  1  244 ? 21.199  -30.259 -20.912  1.00 49.10  ? 244  PRO   A CD   1 
ATOM   3685  H  HA   . PRO   A  1  244 ? 23.230  -30.337 -18.558  1.00 61.89  ? 244  PRO   A HA   1 
ATOM   3686  H  HB2  . PRO   A  1  244 ? 20.861  -29.570 -17.794  1.00 64.23  ? 244  PRO   A HB2  1 
ATOM   3687  H  HB3  . PRO   A  1  244 ? 21.780  -28.648 -18.706  1.00 64.23  ? 244  PRO   A HB3  1 
ATOM   3688  H  HG2  . PRO   A  1  244 ? 19.676  -30.308 -19.531  1.00 62.24  ? 244  PRO   A HG2  1 
ATOM   3689  H  HG3  . PRO   A  1  244 ? 19.997  -28.836 -20.039  1.00 62.24  ? 244  PRO   A HG3  1 
ATOM   3690  H  HD2  . PRO   A  1  244 ? 20.673  -30.877 -21.444  1.00 58.90  ? 244  PRO   A HD2  1 
ATOM   3691  H  HD3  . PRO   A  1  244 ? 21.548  -29.550 -21.476  1.00 58.90  ? 244  PRO   A HD3  1 
ATOM   3692  N  N    . ARG   A  1  245 ? 21.363  -32.869 -18.319  1.00 52.48  ? 245  ARG   A N    1 
ATOM   3693  C  CA   . ARG   A  1  245 ? 21.030  -33.999 -17.459  1.00 52.16  ? 245  ARG   A CA   1 
ATOM   3694  C  C    . ARG   A  1  245 ? 21.988  -35.173 -17.624  1.00 49.32  ? 245  ARG   A C    1 
ATOM   3695  O  O    . ARG   A  1  245 ? 21.858  -36.166 -16.901  1.00 50.61  ? 245  ARG   A O    1 
ATOM   3696  C  CB   . ARG   A  1  245 ? 19.593  -34.463 -17.725  1.00 55.41  ? 245  ARG   A CB   1 
ATOM   3697  C  CG   . ARG   A  1  245 ? 18.527  -33.551 -17.123  1.00 55.59  ? 245  ARG   A CG   1 
ATOM   3698  C  CD   . ARG   A  1  245 ? 17.135  -34.166 -17.204  1.00 54.22  ? 245  ARG   A CD   1 
ATOM   3699  N  NE   . ARG   A  1  245 ? 17.065  -35.471 -16.549  1.00 56.16  ? 245  ARG   A NE   1 
ATOM   3700  C  CZ   . ARG   A  1  245 ? 16.828  -35.657 -15.253  1.00 56.82  ? 245  ARG   A CZ   1 
ATOM   3701  N  NH1  . ARG   A  1  245 ? 16.635  -34.623 -14.445  1.00 57.36  ? 245  ARG   A NH1  1 
ATOM   3702  N  NH2  . ARG   A  1  245 ? 16.785  -36.887 -14.762  1.00 59.47  ? 245  ARG   A NH2  1 
ATOM   3703  H  H    . ARG   A  1  245 ? 21.121  -32.966 -19.138  1.00 62.96  ? 245  ARG   A H    1 
ATOM   3704  H  HA   . ARG   A  1  245 ? 21.080  -33.706 -16.536  1.00 62.57  ? 245  ARG   A HA   1 
ATOM   3705  H  HB2  . ARG   A  1  245 ? 19.447  -34.495 -18.683  1.00 66.47  ? 245  ARG   A HB2  1 
ATOM   3706  H  HB3  . ARG   A  1  245 ? 19.475  -35.347 -17.342  1.00 66.47  ? 245  ARG   A HB3  1 
ATOM   3707  H  HG2  . ARG   A  1  245 ? 18.734  -33.392 -16.188  1.00 66.69  ? 245  ARG   A HG2  1 
ATOM   3708  H  HG3  . ARG   A  1  245 ? 18.515  -32.711 -17.608  1.00 66.69  ? 245  ARG   A HG3  1 
ATOM   3709  H  HD2  . ARG   A  1  245 ? 16.501  -33.576 -16.768  1.00 65.05  ? 245  ARG   A HD2  1 
ATOM   3710  H  HD3  . ARG   A  1  245 ? 16.893  -34.283 -18.136  1.00 65.05  ? 245  ARG   A HD3  1 
ATOM   3711  H  HE   . ARG   A  1  245 ? 17.186  -36.169 -17.036  1.00 67.37  ? 245  ARG   A HE   1 
ATOM   3712  H  HH11 . ARG   A  1  245 ? 16.663  -33.822 -14.757  1.00 68.81  ? 245  ARG   A HH11 1 
ATOM   3713  H  HH12 . ARG   A  1  245 ? 16.483  -34.753 -13.608  1.00 68.81  ? 245  ARG   A HH12 1 
ATOM   3714  H  HH21 . ARG   A  1  245 ? 16.910  -37.561 -15.280  1.00 71.34  ? 245  ARG   A HH21 1 
ATOM   3715  H  HH22 . ARG   A  1  245 ? 16.632  -37.010 -13.924  1.00 71.34  ? 245  ARG   A HH22 1 
ATOM   3716  N  N    . ALA   A  1  246 ? 22.948  -35.080 -18.540  1.00 50.11  ? 246  ALA   A N    1 
ATOM   3717  C  CA   . ALA   A  1  246 ? 23.880  -36.171 -18.772  1.00 51.69  ? 246  ALA   A CA   1 
ATOM   3718  C  C    . ALA   A  1  246 ? 24.781  -36.382 -17.556  1.00 54.34  ? 246  ALA   A C    1 
ATOM   3719  O  O    . ALA   A  1  246 ? 24.831  -35.569 -16.628  1.00 55.67  ? 246  ALA   A O    1 
ATOM   3720  C  CB   . ALA   A  1  246 ? 24.730  -35.892 -20.009  1.00 51.87  ? 246  ALA   A CB   1 
ATOM   3721  H  H    . ALA   A  1  246 ? 23.079  -34.393 -19.040  1.00 60.11  ? 246  ALA   A H    1 
ATOM   3722  H  HA   . ALA   A  1  246 ? 23.377  -36.987 -18.921  1.00 62.01  ? 246  ALA   A HA   1 
ATOM   3723  H  HB1  . ALA   A  1  246 ? 25.353  -36.624 -20.136  1.00 62.22  ? 246  ALA   A HB1  1 
ATOM   3724  H  HB2  . ALA   A  1  246 ? 24.148  -35.816 -20.782  1.00 62.22  ? 246  ALA   A HB2  1 
ATOM   3725  H  HB3  . ALA   A  1  246 ? 25.215  -35.062 -19.878  1.00 62.22  ? 246  ALA   A HB3  1 
ATOM   3726  N  N    . ALA   A  1  247 ? 25.510  -37.499 -17.576  1.00 56.31  ? 247  ALA   A N    1 
ATOM   3727  C  CA   . ALA   A  1  247 ? 26.435  -37.850 -16.499  1.00 53.86  ? 247  ALA   A CA   1 
ATOM   3728  C  C    . ALA   A  1  247 ? 25.722  -37.857 -15.149  1.00 53.70  ? 247  ALA   A C    1 
ATOM   3729  O  O    . ALA   A  1  247 ? 26.240  -37.369 -14.143  1.00 54.81  ? 247  ALA   A O    1 
ATOM   3730  C  CB   . ALA   A  1  247 ? 27.634  -36.901 -16.476  1.00 54.91  ? 247  ALA   A CB   1 
ATOM   3731  H  H    . ALA   A  1  247 ? 25.486  -38.078 -18.212  1.00 67.55  ? 247  ALA   A H    1 
ATOM   3732  H  HA   . ALA   A  1  247 ? 26.768  -38.747 -16.660  1.00 64.61  ? 247  ALA   A HA   1 
ATOM   3733  H  HB1  . ALA   A  1  247 ? 28.227  -37.158 -15.753  1.00 65.87  ? 247  ALA   A HB1  1 
ATOM   3734  H  HB2  . ALA   A  1  247 ? 28.101  -36.961 -17.324  1.00 65.87  ? 247  ALA   A HB2  1 
ATOM   3735  H  HB3  . ALA   A  1  247 ? 27.317  -35.995 -16.337  1.00 65.87  ? 247  ALA   A HB3  1 
ATOM   3736  N  N    . ARG   A  1  248 ? 24.515  -38.419 -15.135  1.00 55.74  ? 248  ARG   A N    1 
ATOM   3737  C  CA   . ARG   A  1  248 ? 23.677  -38.479 -13.938  1.00 58.81  ? 248  ARG   A CA   1 
ATOM   3738  C  C    . ARG   A  1  248 ? 23.572  -37.106 -13.277  1.00 54.23  ? 248  ARG   A C    1 
ATOM   3739  O  O    . ARG   A  1  248 ? 23.862  -36.926 -12.092  1.00 56.27  ? 248  ARG   A O    1 
ATOM   3740  C  CB   . ARG   A  1  248 ? 24.198  -39.532 -12.957  1.00 68.31  ? 248  ARG   A CB   1 
ATOM   3741  C  CG   . ARG   A  1  248 ? 24.208  -40.960 -13.514  1.00 80.90  ? 248  ARG   A CG   1 
ATOM   3742  C  CD   . ARG   A  1  248 ? 22.823  -41.450 -13.945  1.00 89.63  ? 248  ARG   A CD   1 
ATOM   3743  N  NE   . ARG   A  1  248 ? 22.038  -41.995 -12.840  1.00 96.30  ? 248  ARG   A NE   1 
ATOM   3744  C  CZ   . ARG   A  1  248 ? 20.742  -42.287 -12.915  1.00 95.44  ? 248  ARG   A CZ   1 
ATOM   3745  N  NH1  . ARG   A  1  248 ? 20.071  -42.074 -14.040  1.00 97.89  ? 248  ARG   A NH1  1 
ATOM   3746  N  NH2  . ARG   A  1  248 ? 20.110  -42.785 -11.861  1.00 89.69  ? 248  ARG   A NH2  1 
ATOM   3747  H  H    . ARG   A  1  248 ? 24.149  -38.783 -15.823  1.00 66.86  ? 248  ARG   A H    1 
ATOM   3748  H  HA   . ARG   A  1  248 ? 22.782  -38.742 -14.204  1.00 70.55  ? 248  ARG   A HA   1 
ATOM   3749  H  HB2  . ARG   A  1  248 ? 25.109  -39.305 -12.713  1.00 81.96  ? 248  ARG   A HB2  1 
ATOM   3750  H  HB3  . ARG   A  1  248 ? 23.632  -39.528 -12.169  1.00 81.96  ? 248  ARG   A HB3  1 
ATOM   3751  H  HG2  . ARG   A  1  248 ? 24.790  -40.992 -14.289  1.00 97.06  ? 248  ARG   A HG2  1 
ATOM   3752  H  HG3  . ARG   A  1  248 ? 24.537  -41.563 -12.828  1.00 97.06  ? 248  ARG   A HG3  1 
ATOM   3753  H  HD2  . ARG   A  1  248 ? 22.329  -40.705 -14.322  1.00 107.53 ? 248  ARG   A HD2  1 
ATOM   3754  H  HD3  . ARG   A  1  248 ? 22.928  -42.148 -14.610  1.00 107.53 ? 248  ARG   A HD3  1 
ATOM   3755  H  HE   . ARG   A  1  248 ? 22.440  -42.137 -12.093  1.00 115.54 ? 248  ARG   A HE   1 
ATOM   3756  H  HH11 . ARG   A  1  248 ? 20.474  -41.746 -14.726  1.00 117.45 ? 248  ARG   A HH11 1 
ATOM   3757  H  HH12 . ARG   A  1  248 ? 19.233  -42.264 -14.084  1.00 117.45 ? 248  ARG   A HH12 1 
ATOM   3758  H  HH21 . ARG   A  1  248 ? 20.538  -42.921 -11.128  1.00 107.61 ? 248  ARG   A HH21 1 
ATOM   3759  H  HH22 . ARG   A  1  248 ? 19.272  -42.973 -11.911  1.00 107.61 ? 248  ARG   A HH22 1 
ATOM   3760  N  N    . THR   A  1  249 ? 23.145  -36.127 -14.070  1.00 52.99  ? 249  THR   A N    1 
ATOM   3761  C  CA   . THR   A  1  249 ? 22.799  -34.770 -13.664  1.00 57.60  ? 249  THR   A CA   1 
ATOM   3762  C  C    . THR   A  1  249 ? 24.022  -33.907 -13.377  1.00 54.86  ? 249  THR   A C    1 
ATOM   3763  O  O    . THR   A  1  249 ? 23.850  -32.756 -12.962  1.00 58.01  ? 249  THR   A O    1 
ATOM   3764  C  CB   . THR   A  1  249 ? 21.882  -34.736 -12.430  1.00 66.18  ? 249  THR   A CB   1 
ATOM   3765  O  OG1  . THR   A  1  249 ? 22.608  -35.162 -11.270  1.00 69.21  ? 249  THR   A OG1  1 
ATOM   3766  C  CG2  . THR   A  1  249 ? 20.681  -35.644 -12.641  1.00 70.55  ? 249  THR   A CG2  1 
ATOM   3767  H  H    . THR   A  1  249 ? 23.040  -36.239 -14.916  1.00 63.57  ? 249  THR   A H    1 
ATOM   3768  H  HA   . THR   A  1  249 ? 22.328  -34.358 -14.406  1.00 69.10  ? 249  THR   A HA   1 
ATOM   3769  H  HB   . THR   A  1  249 ? 21.563  -33.831 -12.288  1.00 79.39  ? 249  THR   A HB   1 
ATOM   3770  H  HG1  . THR   A  1  249 ? 22.650  -36.001 -11.249  1.00 83.04  ? 249  THR   A HG1  1 
ATOM   3771  H  HG21 . THR   A  1  249 ? 20.060  -35.549 -11.902  1.00 84.64  ? 249  THR   A HG21 1 
ATOM   3772  H  HG22 . THR   A  1  249 ? 20.227  -35.407 -13.466  1.00 84.64  ? 249  THR   A HG22 1 
ATOM   3773  H  HG23 . THR   A  1  249 ? 20.969  -36.568 -12.694  1.00 84.64  ? 249  THR   A HG23 1 
ATOM   3774  N  N    . LEU   A  1  250 ? 25.244  -34.410 -13.567  1.00 55.79  ? 250  LEU   A N    1 
ATOM   3775  C  CA   . LEU   A  1  250 ? 26.398  -33.519 -13.532  1.00 56.81  ? 250  LEU   A CA   1 
ATOM   3776  C  C    . LEU   A  1  250 ? 26.363  -32.542 -14.697  1.00 57.08  ? 250  LEU   A C    1 
ATOM   3777  O  O    . LEU   A  1  250 ? 26.894  -31.431 -14.596  1.00 54.29  ? 250  LEU   A O    1 
ATOM   3778  C  CB   . LEU   A  1  250 ? 27.700  -34.319 -13.563  1.00 55.91  ? 250  LEU   A CB   1 
ATOM   3779  C  CG   . LEU   A  1  250 ? 28.143  -34.985 -12.262  1.00 56.42  ? 250  LEU   A CG   1 
ATOM   3780  C  CD1  . LEU   A  1  250 ? 29.369  -35.845 -12.518  1.00 52.99  ? 250  LEU   A CD1  1 
ATOM   3781  C  CD2  . LEU   A  1  250 ? 28.436  -33.952 -11.189  1.00 59.84  ? 250  LEU   A CD2  1 
ATOM   3782  H  H    . LEU   A  1  250 ? 25.424  -35.238 -13.714  1.00 66.93  ? 250  LEU   A H    1 
ATOM   3783  H  HA   . LEU   A  1  250 ? 26.380  -33.021 -12.700  1.00 68.16  ? 250  LEU   A HA   1 
ATOM   3784  H  HB2  . LEU   A  1  250 ? 27.599  -35.025 -14.221  1.00 67.08  ? 250  LEU   A HB2  1 
ATOM   3785  H  HB3  . LEU   A  1  250 ? 28.412  -33.717 -13.829  1.00 67.08  ? 250  LEU   A HB3  1 
ATOM   3786  H  HG   . LEU   A  1  250 ? 27.424  -35.549 -11.935  1.00 67.68  ? 250  LEU   A HG   1 
ATOM   3787  H  HD11 . LEU   A  1  250 ? 29.655  -36.243 -11.681  1.00 63.57  ? 250  LEU   A HD11 1 
ATOM   3788  H  HD12 . LEU   A  1  250 ? 29.139  -36.541 -13.154  1.00 63.57  ? 250  LEU   A HD12 1 
ATOM   3789  H  HD13 . LEU   A  1  250 ? 30.076  -35.288 -12.879  1.00 63.57  ? 250  LEU   A HD13 1 
ATOM   3790  H  HD21 . LEU   A  1  250 ? 28.787  -34.402 -10.404  1.00 71.79  ? 250  LEU   A HD21 1 
ATOM   3791  H  HD22 . LEU   A  1  250 ? 29.090  -33.321 -11.528  1.00 71.79  ? 250  LEU   A HD22 1 
ATOM   3792  H  HD23 . LEU   A  1  250 ? 27.614  -33.489 -10.964  1.00 71.79  ? 250  LEU   A HD23 1 
ATOM   3793  N  N    . GLY   A  1  251 ? 25.732  -32.932 -15.799  1.00 57.07  ? 251  GLY   A N    1 
ATOM   3794  C  CA   . GLY   A  1  251 ? 25.702  -32.108 -16.987  1.00 54.70  ? 251  GLY   A CA   1 
ATOM   3795  C  C    . GLY   A  1  251 ? 26.926  -32.302 -17.856  1.00 53.23  ? 251  GLY   A C    1 
ATOM   3796  O  O    . GLY   A  1  251 ? 28.025  -32.601 -17.376  1.00 52.13  ? 251  GLY   A O    1 
ATOM   3797  H  H    . GLY   A  1  251 ? 25.311  -33.677 -15.879  1.00 68.47  ? 251  GLY   A H    1 
ATOM   3798  H  HA2  . GLY   A  1  251 ? 24.916  -32.331 -17.512  1.00 65.62  ? 251  GLY   A HA2  1 
ATOM   3799  H  HA3  . GLY   A  1  251 ? 25.655  -31.174 -16.729  1.00 65.62  ? 251  GLY   A HA3  1 
ATOM   3800  N  N    . MET   A  1  252 ? 26.734  -32.139 -19.157  1.00 51.03  ? 252  MET   A N    1 
ATOM   3801  C  CA   . MET   A  1  252 ? 27.831  -32.210 -20.105  1.00 50.44  ? 252  MET   A CA   1 
ATOM   3802  C  C    . MET   A  1  252 ? 27.577  -31.216 -21.227  1.00 49.37  ? 252  MET   A C    1 
ATOM   3803  O  O    . MET   A  1  252 ? 26.463  -30.718 -21.406  1.00 46.38  ? 252  MET   A O    1 
ATOM   3804  C  CB   . MET   A  1  252 ? 27.999  -33.623 -20.681  1.00 49.43  ? 252  MET   A CB   1 
ATOM   3805  C  CG   . MET   A  1  252 ? 28.444  -34.666 -19.667  1.00 56.94  ? 252  MET   A CG   1 
ATOM   3806  S  SD   . MET   A  1  252 ? 28.750  -36.285 -20.408  1.00 54.08  ? 252  MET   A SD   1 
ATOM   3807  C  CE   . MET   A  1  252 ? 30.242  -35.968 -21.349  1.00 54.69  ? 252  MET   A CE   1 
ATOM   3808  H  H    . MET   A  1  252 ? 25.969  -31.986 -19.518  1.00 61.21  ? 252  MET   A H    1 
ATOM   3809  H  HA   . MET   A  1  252 ? 28.655  -31.975 -19.652  1.00 60.51  ? 252  MET   A HA   1 
ATOM   3810  H  HB2  . MET   A  1  252 ? 27.148  -33.912 -21.045  1.00 59.30  ? 252  MET   A HB2  1 
ATOM   3811  H  HB3  . MET   A  1  252 ? 28.668  -33.593 -21.383  1.00 59.30  ? 252  MET   A HB3  1 
ATOM   3812  H  HG2  . MET   A  1  252 ? 29.267  -34.369 -19.248  1.00 68.30  ? 252  MET   A HG2  1 
ATOM   3813  H  HG3  . MET   A  1  252 ? 27.750  -34.771 -18.997  1.00 68.30  ? 252  MET   A HG3  1 
ATOM   3814  H  HE1  . MET   A  1  252 ? 30.502  -36.780 -21.812  1.00 65.61  ? 252  MET   A HE1  1 
ATOM   3815  H  HE2  . MET   A  1  252 ? 30.066  -35.263 -21.992  1.00 65.61  ? 252  MET   A HE2  1 
ATOM   3816  H  HE3  . MET   A  1  252 ? 30.947  -35.693 -20.742  1.00 65.61  ? 252  MET   A HE3  1 
ATOM   3817  N  N    . VAL   A  1  253 ? 28.637  -30.927 -21.976  1.00 51.10  ? 253  VAL   A N    1 
ATOM   3818  C  CA   . VAL   A  1  253 ? 28.559  -30.129 -23.193  1.00 51.48  ? 253  VAL   A CA   1 
ATOM   3819  C  C    . VAL   A  1  253 ? 29.296  -30.894 -24.280  1.00 51.41  ? 253  VAL   A C    1 
ATOM   3820  O  O    . VAL   A  1  253 ? 30.500  -31.149 -24.157  1.00 56.44  ? 253  VAL   A O    1 
ATOM   3821  C  CB   . VAL   A  1  253 ? 29.158  -28.724 -23.009  1.00 55.57  ? 253  VAL   A CB   1 
ATOM   3822  C  CG1  . VAL   A  1  253 ? 29.370  -28.043 -24.358  1.00 54.00  ? 253  VAL   A CG1  1 
ATOM   3823  C  CG2  . VAL   A  1  253 ? 28.256  -27.876 -22.121  1.00 53.93  ? 253  VAL   A CG2  1 
ATOM   3824  H  H    . VAL   A  1  253 ? 29.435  -31.191 -21.794  1.00 61.30  ? 253  VAL   A H    1 
ATOM   3825  H  HA   . VAL   A  1  253 ? 27.632  -30.022 -23.458  1.00 61.76  ? 253  VAL   A HA   1 
ATOM   3826  H  HB   . VAL   A  1  253 ? 30.023  -28.809 -22.577  1.00 66.66  ? 253  VAL   A HB   1 
ATOM   3827  H  HG11 . VAL   A  1  253 ? 29.589  -27.109 -24.210  1.00 64.78  ? 253  VAL   A HG11 1 
ATOM   3828  H  HG12 . VAL   A  1  253 ? 30.099  -28.483 -24.823  1.00 64.78  ? 253  VAL   A HG12 1 
ATOM   3829  H  HG13 . VAL   A  1  253 ? 28.555  -28.113 -24.879  1.00 64.78  ? 253  VAL   A HG13 1 
ATOM   3830  H  HG21 . VAL   A  1  253 ? 28.658  -27.000 -22.007  1.00 64.70  ? 253  VAL   A HG21 1 
ATOM   3831  H  HG22 . VAL   A  1  253 ? 27.388  -27.789 -22.545  1.00 64.70  ? 253  VAL   A HG22 1 
ATOM   3832  H  HG23 . VAL   A  1  253 ? 28.161  -28.311 -21.260  1.00 64.70  ? 253  VAL   A HG23 1 
ATOM   3833  N  N    . TYR   A  1  254 ? 28.576  -31.272 -25.331  1.00 53.81  ? 254  TYR   A N    1 
ATOM   3834  C  CA   . TYR   A  1  254 ? 29.162  -31.996 -26.448  1.00 56.27  ? 254  TYR   A CA   1 
ATOM   3835  C  C    . TYR   A  1  254 ? 29.583  -31.015 -27.533  1.00 55.98  ? 254  TYR   A C    1 
ATOM   3836  O  O    . TYR   A  1  254 ? 28.910  -30.008 -27.771  1.00 52.81  ? 254  TYR   A O    1 
ATOM   3837  C  CB   . TYR   A  1  254 ? 28.170  -33.000 -27.037  1.00 62.51  ? 254  TYR   A CB   1 
ATOM   3838  C  CG   . TYR   A  1  254 ? 27.704  -34.093 -26.098  1.00 63.14  ? 254  TYR   A CG   1 
ATOM   3839  C  CD1  . TYR   A  1  254 ? 28.397  -34.394 -24.932  1.00 62.44  ? 254  TYR   A CD1  1 
ATOM   3840  C  CD2  . TYR   A  1  254 ? 26.566  -34.833 -26.391  1.00 61.11  ? 254  TYR   A CD2  1 
ATOM   3841  C  CE1  . TYR   A  1  254 ? 27.962  -35.400 -24.083  1.00 62.83  ? 254  TYR   A CE1  1 
ATOM   3842  C  CE2  . TYR   A  1  254 ? 26.126  -35.835 -25.553  1.00 59.85  ? 254  TYR   A CE2  1 
ATOM   3843  C  CZ   . TYR   A  1  254 ? 26.826  -36.116 -24.401  1.00 62.91  ? 254  TYR   A CZ   1 
ATOM   3844  O  OH   . TYR   A  1  254 ? 26.384  -37.117 -23.568  1.00 65.87  ? 254  TYR   A OH   1 
ATOM   3845  H  H    . TYR   A  1  254 ? 27.735  -31.118 -25.420  1.00 64.56  ? 254  TYR   A H    1 
ATOM   3846  H  HA   . TYR   A  1  254 ? 29.940  -32.484 -26.136  1.00 67.50  ? 254  TYR   A HA   1 
ATOM   3847  H  HB2  . TYR   A  1  254 ? 27.382  -32.515 -27.328  1.00 74.99  ? 254  TYR   A HB2  1 
ATOM   3848  H  HB3  . TYR   A  1  254 ? 28.591  -33.434 -27.796  1.00 74.99  ? 254  TYR   A HB3  1 
ATOM   3849  H  HD1  . TYR   A  1  254 ? 29.165  -33.915 -24.719  1.00 74.91  ? 254  TYR   A HD1  1 
ATOM   3850  H  HD2  . TYR   A  1  254 ? 26.091  -34.648 -27.169  1.00 73.31  ? 254  TYR   A HD2  1 
ATOM   3851  H  HE1  . TYR   A  1  254 ? 28.433  -35.591 -23.305  1.00 75.37  ? 254  TYR   A HE1  1 
ATOM   3852  H  HE2  . TYR   A  1  254 ? 25.361  -36.319 -25.765  1.00 71.80  ? 254  TYR   A HE2  1 
ATOM   3853  H  HH   . TYR   A  1  254 ? 25.715  -37.497 -23.905  1.00 79.02  ? 254  TYR   A HH   1 
ATOM   3854  N  N    . ILE   A  1  255 ? 30.699  -31.316 -28.190  1.00 57.19  ? 255  ILE   A N    1 
ATOM   3855  C  CA   . ILE   A  1  255 ? 31.127  -30.604 -29.389  1.00 56.98  ? 255  ILE   A CA   1 
ATOM   3856  C  C    . ILE   A  1  255 ? 31.236  -31.627 -30.510  1.00 57.11  ? 255  ILE   A C    1 
ATOM   3857  O  O    . ILE   A  1  255 ? 31.963  -32.620 -30.384  1.00 57.23  ? 255  ILE   A O    1 
ATOM   3858  C  CB   . ILE   A  1  255 ? 32.456  -29.859 -29.182  1.00 57.66  ? 255  ILE   A CB   1 
ATOM   3859  C  CG1  . ILE   A  1  255 ? 32.293  -28.801 -28.085  1.00 57.63  ? 255  ILE   A CG1  1 
ATOM   3860  C  CG2  . ILE   A  1  255 ? 32.913  -29.209 -30.489  1.00 56.97  ? 255  ILE   A CG2  1 
ATOM   3861  C  CD1  . ILE   A  1  255 ? 33.494  -27.891 -27.900  1.00 59.03  ? 255  ILE   A CD1  1 
ATOM   3862  H  H    . ILE   A  1  255 ? 31.238  -31.943 -27.954  1.00 68.61  ? 255  ILE   A H    1 
ATOM   3863  H  HA   . ILE   A  1  255 ? 30.456  -29.947 -29.632  1.00 68.36  ? 255  ILE   A HA   1 
ATOM   3864  H  HB   . ILE   A  1  255 ? 33.131  -30.498 -28.905  1.00 69.17  ? 255  ILE   A HB   1 
ATOM   3865  H  HG12 . ILE   A  1  255 ? 31.533  -28.240 -28.308  1.00 69.14  ? 255  ILE   A HG12 1 
ATOM   3866  H  HG13 . ILE   A  1  255 ? 32.135  -29.253 -27.242  1.00 69.14  ? 255  ILE   A HG13 1 
ATOM   3867  H  HG21 . ILE   A  1  255 ? 33.778  -28.794 -30.350  1.00 68.35  ? 255  ILE   A HG21 1 
ATOM   3868  H  HG22 . ILE   A  1  255 ? 32.980  -29.891 -31.175  1.00 68.35  ? 255  ILE   A HG22 1 
ATOM   3869  H  HG23 . ILE   A  1  255 ? 32.263  -28.539 -30.753  1.00 68.35  ? 255  ILE   A HG23 1 
ATOM   3870  H  HD11 . ILE   A  1  255 ? 33.343  -27.320 -27.130  1.00 70.81  ? 255  ILE   A HD11 1 
ATOM   3871  H  HD12 . ILE   A  1  255 ? 34.284  -28.436 -27.758  1.00 70.81  ? 255  ILE   A HD12 1 
ATOM   3872  H  HD13 . ILE   A  1  255 ? 33.606  -27.349 -28.697  1.00 70.81  ? 255  ILE   A HD13 1 
ATOM   3873  N  N    . TYR   A  1  256 ? 30.505  -31.391 -31.596  1.00 57.89  ? 256  TYR   A N    1 
ATOM   3874  C  CA   . TYR   A  1  256 ? 30.529  -32.244 -32.772  1.00 58.11  ? 256  TYR   A CA   1 
ATOM   3875  C  C    . TYR   A  1  256 ? 31.163  -31.494 -33.936  1.00 58.52  ? 256  TYR   A C    1 
ATOM   3876  O  O    . TYR   A  1  256 ? 31.073  -30.266 -34.028  1.00 58.66  ? 256  TYR   A O    1 
ATOM   3877  C  CB   . TYR   A  1  256 ? 29.117  -32.693 -33.167  1.00 59.01  ? 256  TYR   A CB   1 
ATOM   3878  C  CG   . TYR   A  1  256 ? 28.422  -33.596 -32.169  1.00 59.76  ? 256  TYR   A CG   1 
ATOM   3879  C  CD1  . TYR   A  1  256 ? 27.647  -33.068 -31.143  1.00 57.48  ? 256  TYR   A CD1  1 
ATOM   3880  C  CD2  . TYR   A  1  256 ? 28.521  -34.977 -32.268  1.00 61.98  ? 256  TYR   A CD2  1 
ATOM   3881  C  CE1  . TYR   A  1  256 ? 27.002  -33.894 -30.235  1.00 56.23  ? 256  TYR   A CE1  1 
ATOM   3882  C  CE2  . TYR   A  1  256 ? 27.881  -35.808 -31.367  1.00 63.97  ? 256  TYR   A CE2  1 
ATOM   3883  C  CZ   . TYR   A  1  256 ? 27.122  -35.263 -30.354  1.00 61.67  ? 256  TYR   A CZ   1 
ATOM   3884  O  OH   . TYR   A  1  256 ? 26.489  -36.097 -29.461  1.00 61.08  ? 256  TYR   A OH   1 
ATOM   3885  H  H    . TYR   A  1  256 ? 29.972  -30.721 -31.674  1.00 69.45  ? 256  TYR   A H    1 
ATOM   3886  H  HA   . TYR   A  1  256 ? 31.055  -33.037 -32.584  1.00 69.71  ? 256  TYR   A HA   1 
ATOM   3887  H  HB2  . TYR   A  1  256 ? 28.564  -31.903 -33.277  1.00 70.80  ? 256  TYR   A HB2  1 
ATOM   3888  H  HB3  . TYR   A  1  256 ? 29.173  -33.177 -34.006  1.00 70.80  ? 256  TYR   A HB3  1 
ATOM   3889  H  HD1  . TYR   A  1  256 ? 27.560  -32.146 -31.064  1.00 68.96  ? 256  TYR   A HD1  1 
ATOM   3890  H  HD2  . TYR   A  1  256 ? 29.027  -35.350 -32.953  1.00 74.36  ? 256  TYR   A HD2  1 
ATOM   3891  H  HE1  . TYR   A  1  256 ? 26.492  -33.527 -29.549  1.00 67.45  ? 256  TYR   A HE1  1 
ATOM   3892  H  HE2  . TYR   A  1  256 ? 27.962  -36.731 -31.444  1.00 76.75  ? 256  TYR   A HE2  1 
ATOM   3893  H  HH   . TYR   A  1  256 ? 26.348  -35.691 -28.739  1.00 73.28  ? 256  TYR   A HH   1 
ATOM   3894  N  N    . ASP   A  1  257 ? 31.803  -32.244 -34.829  1.00 59.55  ? 257  ASP   A N    1 
ATOM   3895  C  CA   . ASP   A  1  257 ? 32.395  -31.649 -36.018  1.00 60.47  ? 257  ASP   A CA   1 
ATOM   3896  C  C    . ASP   A  1  257 ? 31.296  -31.120 -36.931  1.00 63.66  ? 257  ASP   A C    1 
ATOM   3897  O  O    . ASP   A  1  257 ? 30.341  -31.835 -37.249  1.00 64.71  ? 257  ASP   A O    1 
ATOM   3898  C  CB   . ASP   A  1  257 ? 33.249  -32.681 -36.751  1.00 65.90  ? 257  ASP   A CB   1 
ATOM   3899  C  CG   . ASP   A  1  257 ? 34.058  -32.078 -37.882  1.00 75.00  ? 257  ASP   A CG   1 
ATOM   3900  O  OD1  . ASP   A  1  257 ? 33.539  -31.192 -38.593  1.00 78.88  ? 257  ASP   A OD1  1 
ATOM   3901  O  OD2  . ASP   A  1  257 ? 35.220  -32.497 -38.059  1.00 81.02  ? 257  ASP   A OD2  1 
ATOM   3902  H  H    . ASP   A  1  257 ? 31.907  -33.095 -34.768  1.00 71.44  ? 257  ASP   A H    1 
ATOM   3903  H  HA   . ASP   A  1  257 ? 32.969  -30.908 -35.767  1.00 72.55  ? 257  ASP   A HA   1 
ATOM   3904  H  HB2  . ASP   A  1  257 ? 33.868  -33.083 -36.121  1.00 79.06  ? 257  ASP   A HB2  1 
ATOM   3905  H  HB3  . ASP   A  1  257 ? 32.669  -33.361 -37.127  1.00 79.06  ? 257  ASP   A HB3  1 
ATOM   3906  N  N    . GLY   A  1  258 ? 31.435  -29.866 -37.356  1.00 65.86  ? 258  GLY   A N    1 
ATOM   3907  C  CA   . GLY   A  1  258 ? 30.430  -29.234 -38.188  1.00 63.50  ? 258  GLY   A CA   1 
ATOM   3908  C  C    . GLY   A  1  258 ? 30.372  -29.725 -39.616  1.00 61.08  ? 258  GLY   A C    1 
ATOM   3909  O  O    . GLY   A  1  258 ? 29.582  -29.194 -40.402  1.00 60.84  ? 258  GLY   A O    1 
ATOM   3910  H  H    . GLY   A  1  258 ? 32.107  -29.362 -37.172  1.00 79.01  ? 258  GLY   A H    1 
ATOM   3911  H  HA2  . GLY   A  1  258 ? 29.559  -29.385 -37.789  1.00 76.18  ? 258  GLY   A HA2  1 
ATOM   3912  H  HA3  . GLY   A  1  258 ? 30.605  -28.280 -38.212  1.00 76.18  ? 258  GLY   A HA3  1 
ATOM   3913  N  N    . LYS   A  1  259 ? 31.182  -30.717 -39.977  1.00 61.82  ? 259  LYS   A N    1 
ATOM   3914  C  CA   . LYS   A  1  259 ? 31.188  -31.284 -41.320  1.00 65.91  ? 259  LYS   A CA   1 
ATOM   3915  C  C    . LYS   A  1  259 ? 30.549  -32.662 -41.398  1.00 63.35  ? 259  LYS   A C    1 
ATOM   3916  O  O    . LYS   A  1  259 ? 29.890  -32.970 -42.393  1.00 64.92  ? 259  LYS   A O    1 
ATOM   3917  C  CB   . LYS   A  1  259 ? 32.627  -31.359 -41.849  1.00 75.15  ? 259  LYS   A CB   1 
ATOM   3918  C  CG   . LYS   A  1  259 ? 32.804  -32.238 -43.082  1.00 81.88  ? 259  LYS   A CG   1 
ATOM   3919  C  CD   . LYS   A  1  259 ? 34.183  -32.064 -43.711  1.00 88.29  ? 259  LYS   A CD   1 
ATOM   3920  C  CE   . LYS   A  1  259 ? 34.173  -31.000 -44.798  1.00 94.44  ? 259  LYS   A CE   1 
ATOM   3921  N  NZ   . LYS   A  1  259 ? 35.520  -30.793 -45.402  1.00 99.67  ? 259  LYS   A NZ   1 
ATOM   3922  H  H    . LYS   A  1  259 ? 31.751  -31.086 -39.448  1.00 74.17  ? 259  LYS   A H    1 
ATOM   3923  H  HA   . LYS   A  1  259 ? 30.687  -30.698 -41.909  1.00 79.08  ? 259  LYS   A HA   1 
ATOM   3924  H  HB2  . LYS   A  1  259 ? 32.917  -30.464 -42.084  1.00 90.17  ? 259  LYS   A HB2  1 
ATOM   3925  H  HB3  . LYS   A  1  259 ? 33.195  -31.719 -41.150  1.00 90.17  ? 259  LYS   A HB3  1 
ATOM   3926  H  HG2  . LYS   A  1  259 ? 32.702  -33.169 -42.829  1.00 98.24  ? 259  LYS   A HG2  1 
ATOM   3927  H  HG3  . LYS   A  1  259 ? 32.137  -31.999 -43.744  1.00 98.24  ? 259  LYS   A HG3  1 
ATOM   3928  H  HD2  . LYS   A  1  259 ? 34.816  -31.794 -43.027  1.00 105.93 ? 259  LYS   A HD2  1 
ATOM   3929  H  HD3  . LYS   A  1  259 ? 34.462  -32.903 -44.109  1.00 105.93 ? 259  LYS   A HD3  1 
ATOM   3930  H  HE2  . LYS   A  1  259 ? 33.565  -31.272 -45.504  1.00 113.31 ? 259  LYS   A HE2  1 
ATOM   3931  H  HE3  . LYS   A  1  259 ? 33.881  -30.157 -44.416  1.00 113.31 ? 259  LYS   A HE3  1 
ATOM   3932  H  HZ1  . LYS   A  1  259 ? 35.479  -30.166 -46.032  1.00 119.59 ? 259  LYS   A HZ1  1 
ATOM   3933  H  HZ2  . LYS   A  1  259 ? 36.098  -30.536 -44.776  1.00 119.59 ? 259  LYS   A HZ2  1 
ATOM   3934  H  HZ3  . LYS   A  1  259 ? 35.809  -31.551 -45.768  1.00 119.59 ? 259  LYS   A HZ3  1 
ATOM   3935  N  N    . ASN   A  1  260 ? 30.722  -33.503 -40.370  1.00 63.51  ? 260  ASN   A N    1 
ATOM   3936  C  CA   . ASN   A  1  260 ? 30.175  -34.856 -40.390  1.00 64.61  ? 260  ASN   A CA   1 
ATOM   3937  C  C    . ASN   A  1  260 ? 29.498  -35.251 -39.080  1.00 59.30  ? 260  ASN   A C    1 
ATOM   3938  O  O    . ASN   A  1  260 ? 29.111  -36.418 -38.930  1.00 57.56  ? 260  ASN   A O    1 
ATOM   3939  C  CB   . ASN   A  1  260 ? 31.280  -35.868 -40.720  1.00 75.46  ? 260  ASN   A CB   1 
ATOM   3940  C  CG   . ASN   A  1  260 ? 32.593  -35.543 -40.036  1.00 90.54  ? 260  ASN   A CG   1 
ATOM   3941  O  OD1  . ASN   A  1  260 ? 32.631  -34.797 -39.058  1.00 89.33  ? 260  ASN   A OD1  1 
ATOM   3942  N  ND2  . ASN   A  1  260 ? 33.679  -36.104 -40.553  1.00 108.50 ? 260  ASN   A ND2  1 
ATOM   3943  H  H    . ASN   A  1  260 ? 31.152  -33.310 -39.651  1.00 76.20  ? 260  ASN   A H    1 
ATOM   3944  H  HA   . ASN   A  1  260 ? 29.498  -34.902 -41.083  1.00 77.51  ? 260  ASN   A HA   1 
ATOM   3945  H  HB2  . ASN   A  1  260 ? 31.000  -36.750 -40.429  1.00 90.53  ? 260  ASN   A HB2  1 
ATOM   3946  H  HB3  . ASN   A  1  260 ? 31.433  -35.868 -41.678  1.00 90.53  ? 260  ASN   A HB3  1 
ATOM   3947  H  HD21 . ASN   A  1  260 ? 33.606  -36.621 -41.237  1.00 130.18 ? 260  ASN   A HD21 1 
ATOM   3948  N  N    . MET   A  1  261 ? 29.335  -34.328 -38.135  1.00 59.73  ? 261  MET   A N    1 
ATOM   3949  C  CA   . MET   A  1  261 ? 28.707  -34.605 -36.845  1.00 60.76  ? 261  MET   A CA   1 
ATOM   3950  C  C    . MET   A  1  261 ? 29.474  -35.656 -36.045  1.00 61.02  ? 261  MET   A C    1 
ATOM   3951  O  O    . MET   A  1  261 ? 28.908  -36.303 -35.158  1.00 61.80  ? 261  MET   A O    1 
ATOM   3952  C  CB   . MET   A  1  261 ? 27.244  -35.041 -37.021  1.00 59.58  ? 261  MET   A CB   1 
ATOM   3953  C  CG   . MET   A  1  261 ? 26.379  -34.899 -35.765  1.00 58.96  ? 261  MET   A CG   1 
ATOM   3954  S  SD   . MET   A  1  261 ? 26.090  -33.184 -35.272  1.00 58.82  ? 261  MET   A SD   1 
ATOM   3955  C  CE   . MET   A  1  261 ? 24.747  -32.716 -36.366  1.00 56.38  ? 261  MET   A CE   1 
ATOM   3956  H  H    . MET   A  1  261 ? 29.587  -33.510 -38.221  1.00 71.66  ? 261  MET   A H    1 
ATOM   3957  H  HA   . MET   A  1  261 ? 28.708  -33.781 -36.332  1.00 72.89  ? 261  MET   A HA   1 
ATOM   3958  H  HB2  . MET   A  1  261 ? 26.842  -34.498 -37.716  1.00 71.47  ? 261  MET   A HB2  1 
ATOM   3959  H  HB3  . MET   A  1  261 ? 27.231  -35.976 -37.281  1.00 71.47  ? 261  MET   A HB3  1 
ATOM   3960  H  HG2  . MET   A  1  261 ? 25.516  -35.308 -35.932  1.00 70.73  ? 261  MET   A HG2  1 
ATOM   3961  H  HG3  . MET   A  1  261 ? 26.822  -35.348 -35.028  1.00 70.73  ? 261  MET   A HG3  1 
ATOM   3962  H  HE1  . MET   A  1  261 ? 24.507  -31.792 -36.195  1.00 67.63  ? 261  MET   A HE1  1 
ATOM   3963  H  HE2  . MET   A  1  261 ? 25.040  -32.817 -37.286  1.00 67.63  ? 261  MET   A HE2  1 
ATOM   3964  H  HE3  . MET   A  1  261 ? 23.986  -33.293 -36.196  1.00 67.63  ? 261  MET   A HE3  1 
ATOM   3965  N  N    . SER   A  1  262 ? 30.755  -35.848 -36.347  1.00 61.45  ? 262  SER   A N    1 
ATOM   3966  C  CA   . SER   A  1  262 ? 31.601  -36.697 -35.521  1.00 60.58  ? 262  SER   A CA   1 
ATOM   3967  C  C    . SER   A  1  262 ? 31.935  -35.985 -34.214  1.00 61.71  ? 262  SER   A C    1 
ATOM   3968  O  O    . SER   A  1  262 ? 32.081  -34.760 -34.168  1.00 63.59  ? 262  SER   A O    1 
ATOM   3969  C  CB   . SER   A  1  262 ? 32.885  -37.059 -36.268  1.00 61.22  ? 262  SER   A CB   1 
ATOM   3970  O  OG   . SER   A  1  262 ? 33.765  -37.807 -35.447  1.00 66.59  ? 262  SER   A OG   1 
ATOM   3971  H  H    . SER   A  1  262 ? 31.156  -35.499 -37.024  1.00 73.72  ? 262  SER   A H    1 
ATOM   3972  H  HA   . SER   A  1  262 ? 31.138  -37.523 -35.313  1.00 72.67  ? 262  SER   A HA   1 
ATOM   3973  H  HB2  . SER   A  1  262 ? 32.656  -37.590 -37.047  1.00 73.45  ? 262  SER   A HB2  1 
ATOM   3974  H  HB3  . SER   A  1  262 ? 33.330  -36.242 -36.542  1.00 73.45  ? 262  SER   A HB3  1 
ATOM   3975  H  HG   . SER   A  1  262 ? 34.461  -38.002 -35.875  1.00 79.89  ? 262  SER   A HG   1 
ATOM   3976  N  N    . SER   A  1  263 ? 32.056  -36.766 -33.142  1.00 61.27  ? 263  SER   A N    1 
ATOM   3977  C  CA   . SER   A  1  263 ? 32.292  -36.203 -31.818  1.00 59.78  ? 263  SER   A CA   1 
ATOM   3978  C  C    . SER   A  1  263 ? 33.738  -35.738 -31.694  1.00 60.89  ? 263  SER   A C    1 
ATOM   3979  O  O    . SER   A  1  263 ? 34.671  -36.483 -32.013  1.00 58.16  ? 263  SER   A O    1 
ATOM   3980  C  CB   . SER   A  1  263 ? 31.968  -37.232 -30.734  1.00 60.78  ? 263  SER   A CB   1 
ATOM   3981  O  OG   . SER   A  1  263 ? 32.074  -36.662 -29.440  1.00 62.44  ? 263  SER   A OG   1 
ATOM   3982  H  H    . SER   A  1  263 ? 32.005  -37.624 -33.157  1.00 73.51  ? 263  SER   A H    1 
ATOM   3983  H  HA   . SER   A  1  263 ? 31.714  -35.436 -31.688  1.00 71.72  ? 263  SER   A HA   1 
ATOM   3984  H  HB2  . SER   A  1  263 ? 31.061  -37.552 -30.864  1.00 72.92  ? 263  SER   A HB2  1 
ATOM   3985  H  HB3  . SER   A  1  263 ? 32.593  -37.971 -30.804  1.00 72.92  ? 263  SER   A HB3  1 
ATOM   3986  H  HG   . SER   A  1  263 ? 31.731  -37.175 -28.871  1.00 74.90  ? 263  SER   A HG   1 
ATOM   3987  N  N    . LEU   A  1  264 ? 33.921  -34.505 -31.221  1.00 61.18  ? 264  LEU   A N    1 
ATOM   3988  C  CA   . LEU   A  1  264 ? 35.235  -33.883 -31.128  1.00 63.80  ? 264  LEU   A CA   1 
ATOM   3989  C  C    . LEU   A  1  264 ? 35.711  -33.691 -29.696  1.00 60.72  ? 264  LEU   A C    1 
ATOM   3990  O  O    . LEU   A  1  264 ? 36.810  -34.134 -29.347  1.00 62.06  ? 264  LEU   A O    1 
ATOM   3991  C  CB   . LEU   A  1  264 ? 35.223  -32.523 -31.842  1.00 67.09  ? 264  LEU   A CB   1 
ATOM   3992  C  CG   . LEU   A  1  264 ? 35.311  -32.509 -33.369  1.00 72.65  ? 264  LEU   A CG   1 
ATOM   3993  C  CD1  . LEU   A  1  264 ? 35.327  -31.068 -33.860  1.00 74.88  ? 264  LEU   A CD1  1 
ATOM   3994  C  CD2  . LEU   A  1  264 ? 36.538  -33.256 -33.871  1.00 74.06  ? 264  LEU   A CD2  1 
ATOM   3995  H  H    . LEU   A  1  264 ? 33.282  -34.001 -30.943  1.00 73.40  ? 264  LEU   A H    1 
ATOM   3996  H  HA   . LEU   A  1  264 ? 35.873  -34.461 -31.574  1.00 76.54  ? 264  LEU   A HA   1 
ATOM   3997  H  HB2  . LEU   A  1  264 ? 34.395  -32.075 -31.608  1.00 80.49  ? 264  LEU   A HB2  1 
ATOM   3998  H  HB3  . LEU   A  1  264 ? 35.981  -32.013 -31.516  1.00 80.49  ? 264  LEU   A HB3  1 
ATOM   3999  H  HG   . LEU   A  1  264 ? 34.536  -32.965 -33.734  1.00 87.16  ? 264  LEU   A HG   1 
ATOM   4000  H  HD11 . LEU   A  1  264 ? 35.416  -31.064 -34.825  1.00 89.84  ? 264  LEU   A HD11 1 
ATOM   4001  H  HD12 . LEU   A  1  264 ? 34.496  -30.638 -33.603  1.00 89.84  ? 264  LEU   A HD12 1 
ATOM   4002  H  HD13 . LEU   A  1  264 ? 36.078  -30.605 -33.456  1.00 89.84  ? 264  LEU   A HD13 1 
ATOM   4003  H  HD21 . LEU   A  1  264 ? 36.611  -33.135 -34.831  1.00 88.85  ? 264  LEU   A HD21 1 
ATOM   4004  H  HD22 . LEU   A  1  264 ? 37.326  -32.900 -33.432  1.00 88.85  ? 264  LEU   A HD22 1 
ATOM   4005  H  HD23 . LEU   A  1  264 ? 36.441  -34.199 -33.663  1.00 88.85  ? 264  LEU   A HD23 1 
ATOM   4006  N  N    A TYR   A  1  265 ? 34.917  -33.041 -28.847  0.51 62.17  ? 265  TYR   A N    1 
ATOM   4007  N  N    B TYR   A  1  265 ? 34.914  -33.030 -28.857  0.49 62.20  ? 265  TYR   A N    1 
ATOM   4008  C  CA   A TYR   A  1  265 ? 35.340  -32.784 -27.479  0.51 57.97  ? 265  TYR   A CA   1 
ATOM   4009  C  CA   B TYR   A  1  265 ? 35.308  -32.717 -27.492  0.49 57.94  ? 265  TYR   A CA   1 
ATOM   4010  C  C    A TYR   A  1  265 ? 34.130  -32.814 -26.559  0.51 62.54  ? 265  TYR   A C    1 
ATOM   4011  C  C    B TYR   A  1  265 ? 34.110  -32.880 -26.567  0.49 62.52  ? 265  TYR   A C    1 
ATOM   4012  O  O    A TYR   A  1  265 ? 32.988  -32.631 -26.989  0.51 57.90  ? 265  TYR   A O    1 
ATOM   4013  O  O    B TYR   A  1  265 ? 32.955  -32.852 -26.999  0.49 57.98  ? 265  TYR   A O    1 
ATOM   4014  C  CB   A TYR   A  1  265 ? 36.075  -31.442 -27.362  0.51 60.09  ? 265  TYR   A CB   1 
ATOM   4015  C  CB   B TYR   A  1  265 ? 35.864  -31.288 -27.374  0.49 59.71  ? 265  TYR   A CB   1 
ATOM   4016  C  CG   A TYR   A  1  265 ? 36.756  -31.235 -26.028  0.51 53.36  ? 265  TYR   A CG   1 
ATOM   4017  C  CG   B TYR   A  1  265 ? 37.117  -31.036 -28.186  0.49 54.23  ? 265  TYR   A CG   1 
ATOM   4018  C  CD1  A TYR   A  1  265 ? 37.965  -31.854 -25.738  0.51 52.12  ? 265  TYR   A CD1  1 
ATOM   4019  C  CD1  B TYR   A  1  265 ? 38.350  -31.512 -27.761  0.49 52.39  ? 265  TYR   A CD1  1 
ATOM   4020  C  CD2  A TYR   A  1  265 ? 36.192  -30.418 -25.059  0.51 51.27  ? 265  TYR   A CD2  1 
ATOM   4021  C  CD2  B TYR   A  1  265 ? 37.068  -30.311 -29.371  0.49 53.74  ? 265  TYR   A CD2  1 
ATOM   4022  C  CE1  A TYR   A  1  265 ? 38.591  -31.666 -24.519  0.51 51.03  ? 265  TYR   A CE1  1 
ATOM   4023  C  CE1  B TYR   A  1  265 ? 39.499  -31.281 -28.496  0.49 52.22  ? 265  TYR   A CE1  1 
ATOM   4024  C  CE2  A TYR   A  1  265 ? 36.810  -30.225 -23.839  0.51 49.98  ? 265  TYR   A CE2  1 
ATOM   4025  C  CE2  B TYR   A  1  265 ? 38.212  -30.074 -30.113  0.49 52.89  ? 265  TYR   A CE2  1 
ATOM   4026  C  CZ   A TYR   A  1  265 ? 38.007  -30.849 -23.574  0.51 49.14  ? 265  TYR   A CZ   1 
ATOM   4027  C  CZ   B TYR   A  1  265 ? 39.425  -30.561 -29.671  0.49 52.87  ? 265  TYR   A CZ   1 
ATOM   4028  O  OH   A TYR   A  1  265 ? 38.620  -30.653 -22.357  0.51 50.82  ? 265  TYR   A OH   1 
ATOM   4029  O  OH   B TYR   A  1  265 ? 40.566  -30.328 -30.406  0.49 53.50  ? 265  TYR   A OH   1 
ATOM   4030  H  H    A TYR   A  1  265 ? 34.134  -32.742 -29.041  0.51 74.58  ? 265  TYR   A H    1 
ATOM   4031  H  H    B TYR   A  1  265 ? 34.127  -32.750 -29.061  0.49 74.62  ? 265  TYR   A H    1 
ATOM   4032  H  HA   A TYR   A  1  265 ? 35.944  -33.489 -27.196  0.51 69.54  ? 265  TYR   A HA   1 
ATOM   4033  H  HA   B TYR   A  1  265 ? 35.997  -33.340 -27.212  0.49 69.51  ? 265  TYR   A HA   1 
ATOM   4034  H  HB2  A TYR   A  1  265 ? 36.756  -31.398 -28.052  0.51 72.09  ? 265  TYR   A HB2  1 
ATOM   4035  H  HB2  B TYR   A  1  265 ? 35.186  -30.666 -27.681  0.49 71.64  ? 265  TYR   A HB2  1 
ATOM   4036  H  HB3  A TYR   A  1  265 ? 35.434  -30.724 -27.482  0.51 72.09  ? 265  TYR   A HB3  1 
ATOM   4037  H  HB3  B TYR   A  1  265 ? 36.077  -31.115 -26.444  0.49 71.64  ? 265  TYR   A HB3  1 
ATOM   4038  H  HD1  A TYR   A  1  265 ? 38.361  -32.404 -26.375  0.51 62.53  ? 265  TYR   A HD1  1 
ATOM   4039  H  HD1  B TYR   A  1  265 ? 38.405  -31.995 -26.967  0.49 62.85  ? 265  TYR   A HD1  1 
ATOM   4040  H  HD2  A TYR   A  1  265 ? 35.383  -29.994 -25.234  0.51 61.51  ? 265  TYR   A HD2  1 
ATOM   4041  H  HD2  B TYR   A  1  265 ? 36.252  -29.979 -29.670  0.49 64.47  ? 265  TYR   A HD2  1 
ATOM   4042  H  HE1  A TYR   A  1  265 ? 39.400  -32.088 -24.338  0.51 61.22  ? 265  TYR   A HE1  1 
ATOM   4043  H  HE1  B TYR   A  1  265 ? 40.318  -31.610 -28.200  0.49 62.65  ? 265  TYR   A HE1  1 
ATOM   4044  H  HE2  A TYR   A  1  265 ? 36.418  -29.675 -23.200  0.51 59.96  ? 265  TYR   A HE2  1 
ATOM   4045  H  HE2  B TYR   A  1  265 ? 38.164  -29.590 -30.906  0.49 63.45  ? 265  TYR   A HE2  1 
ATOM   4046  H  HH   A TYR   A  1  265 ? 38.168  -30.121 -21.890  0.51 60.96  ? 265  TYR   A HH   1 
ATOM   4047  H  HH   B TYR   A  1  265 ? 40.374  -29.916 -31.113  0.49 64.19  ? 265  TYR   A HH   1 
ATOM   4048  N  N    . ASN   A  1  266 ? 34.405  -33.047 -25.278  1.00 60.32  ? 266  ASN   A N    1 
ATOM   4049  C  CA   . ASN   A  1  266 ? 33.385  -33.196 -24.252  1.00 57.74  ? 266  ASN   A CA   1 
ATOM   4050  C  C    . ASN   A  1  266 ? 33.754  -32.352 -23.041  1.00 60.58  ? 266  ASN   A C    1 
ATOM   4051  O  O    . ASN   A  1  266 ? 34.926  -32.278 -22.663  1.00 67.98  ? 266  ASN   A O    1 
ATOM   4052  C  CB   . ASN   A  1  266 ? 33.252  -34.660 -23.815  1.00 56.92  ? 266  ASN   A CB   1 
ATOM   4053  C  CG   . ASN   A  1  266 ? 32.335  -35.467 -24.706  1.00 58.04  ? 266  ASN   A CG   1 
ATOM   4054  O  OD1  . ASN   A  1  266 ? 31.396  -34.937 -25.298  1.00 55.27  ? 266  ASN   A OD1  1 
ATOM   4055  N  ND2  . ASN   A  1  266 ? 32.600  -36.768 -24.798  1.00 69.19  ? 266  ASN   A ND2  1 
ATOM   4056  H  H    A ASN   A  1  266 ? 35.204  -33.124 -24.971  0.51 72.36  ? 266  ASN   A H    1 
ATOM   4057  H  H    B ASN   A  1  266 ? 35.207  -33.076 -24.970  0.49 72.36  ? 266  ASN   A H    1 
ATOM   4058  H  HA   . ASN   A  1  266 ? 32.533  -32.889 -24.600  1.00 69.26  ? 266  ASN   A HA   1 
ATOM   4059  H  HB2  . ASN   A  1  266 ? 34.129  -35.076 -23.836  1.00 68.29  ? 266  ASN   A HB2  1 
ATOM   4060  H  HB3  . ASN   A  1  266 ? 32.893  -34.688 -22.914  1.00 68.29  ? 266  ASN   A HB3  1 
ATOM   4061  H  HD21 . ASN   A  1  266 ? 33.275  -37.100 -24.381  1.00 83.01  ? 266  ASN   A HD21 1 
ATOM   4062  N  N    . PHE   A  1  267 ? 32.751  -31.720 -22.437  1.00 58.57  ? 267  PHE   A N    1 
ATOM   4063  C  CA   . PHE   A  1  267 ? 32.889  -31.083 -21.135  1.00 58.20  ? 267  PHE   A CA   1 
ATOM   4064  C  C    . PHE   A  1  267 ? 31.919  -31.746 -20.165  1.00 59.60  ? 267  PHE   A C    1 
ATOM   4065  O  O    . PHE   A  1  267 ? 30.866  -32.248 -20.568  1.00 60.57  ? 267  PHE   A O    1 
ATOM   4066  C  CB   . PHE   A  1  267 ? 32.604  -29.575 -21.191  1.00 57.08  ? 267  PHE   A CB   1 
ATOM   4067  C  CG   . PHE   A  1  267 ? 33.514  -28.809 -22.110  1.00 55.74  ? 267  PHE   A CG   1 
ATOM   4068  C  CD1  . PHE   A  1  267 ? 33.226  -28.700 -23.461  1.00 57.01  ? 267  PHE   A CD1  1 
ATOM   4069  C  CD2  . PHE   A  1  267 ? 34.647  -28.180 -21.620  1.00 52.97  ? 267  PHE   A CD2  1 
ATOM   4070  C  CE1  . PHE   A  1  267 ? 34.056  -27.988 -24.308  1.00 58.64  ? 267  PHE   A CE1  1 
ATOM   4071  C  CE2  . PHE   A  1  267 ? 35.481  -27.465 -22.461  1.00 54.71  ? 267  PHE   A CE2  1 
ATOM   4072  C  CZ   . PHE   A  1  267 ? 35.185  -27.371 -23.807  1.00 58.85  ? 267  PHE   A CZ   1 
ATOM   4073  H  H    . PHE   A  1  267 ? 31.962  -31.646 -22.772  1.00 70.26  ? 267  PHE   A H    1 
ATOM   4074  H  HA   . PHE   A  1  267 ? 33.798  -31.194 -20.816  1.00 69.82  ? 267  PHE   A HA   1 
ATOM   4075  H  HB2  . PHE   A  1  267 ? 31.694  -29.443 -21.500  1.00 68.48  ? 267  PHE   A HB2  1 
ATOM   4076  H  HB3  . PHE   A  1  267 ? 32.708  -29.207 -20.300  1.00 68.48  ? 267  PHE   A HB3  1 
ATOM   4077  H  HD1  . PHE   A  1  267 ? 32.464  -29.111 -23.803  1.00 68.39  ? 267  PHE   A HD1  1 
ATOM   4078  H  HD2  . PHE   A  1  267 ? 34.849  -28.239 -20.714  1.00 63.55  ? 267  PHE   A HD2  1 
ATOM   4079  H  HE1  . PHE   A  1  267 ? 33.854  -27.925 -25.213  1.00 70.35  ? 267  PHE   A HE1  1 
ATOM   4080  H  HE2  . PHE   A  1  267 ? 36.239  -27.049 -22.120  1.00 65.63  ? 267  PHE   A HE2  1 
ATOM   4081  H  HZ   . PHE   A  1  267 ? 35.745  -26.893 -24.375  1.00 70.61  ? 267  PHE   A HZ   1 
ATOM   4082  N  N    . THR   A  1  268 ? 32.279  -31.746 -18.884  1.00 59.66  ? 268  THR   A N    1 
ATOM   4083  C  CA   . THR   A  1  268 ? 31.458  -32.372 -17.857  1.00 58.89  ? 268  THR   A CA   1 
ATOM   4084  C  C    . THR   A  1  268 ? 31.401  -31.479 -16.628  1.00 58.85  ? 268  THR   A C    1 
ATOM   4085  O  O    . THR   A  1  268 ? 32.413  -30.899 -16.224  1.00 58.83  ? 268  THR   A O    1 
ATOM   4086  C  CB   . THR   A  1  268 ? 32.002  -33.755 -17.471  1.00 59.12  ? 268  THR   A CB   1 
ATOM   4087  O  OG1  . THR   A  1  268 ? 32.122  -34.571 -18.644  1.00 62.45  ? 268  THR   A OG1  1 
ATOM   4088  C  CG2  . THR   A  1  268 ? 31.075  -34.437 -16.473  1.00 56.00  ? 268  THR   A CG2  1 
ATOM   4089  H  H    . THR   A  1  268 ? 33.000  -31.386 -18.584  1.00 71.57  ? 268  THR   A H    1 
ATOM   4090  H  HA   . THR   A  1  268 ? 30.554  -32.480 -18.192  1.00 70.65  ? 268  THR   A HA   1 
ATOM   4091  H  HB   . THR   A  1  268 ? 32.874  -33.654 -17.058  1.00 70.92  ? 268  THR   A HB   1 
ATOM   4092  H  HG1  . THR   A  1  268 ? 32.457  -35.314 -18.444  1.00 74.92  ? 268  THR   A HG1  1 
ATOM   4093  H  HG21 . THR   A  1  268 ? 31.397  -35.331 -16.277  1.00 67.18  ? 268  THR   A HG21 1 
ATOM   4094  H  HG22 . THR   A  1  268 ? 31.043  -33.927 -15.648  1.00 67.18  ? 268  THR   A HG22 1 
ATOM   4095  H  HG23 . THR   A  1  268 ? 30.179  -34.498 -16.840  1.00 67.18  ? 268  THR   A HG23 1 
ATOM   4096  N  N    . GLY   A  1  269 ? 30.213  -31.379 -16.037  1.00 57.62  ? 269  GLY   A N    1 
ATOM   4097  C  CA   . GLY   A  1  269 ? 30.034  -30.579 -14.845  1.00 58.91  ? 269  GLY   A CA   1 
ATOM   4098  C  C    . GLY   A  1  269 ? 30.683  -31.204 -13.624  1.00 63.41  ? 269  GLY   A C    1 
ATOM   4099  O  O    . GLY   A  1  269 ? 31.115  -32.357 -13.618  1.00 68.64  ? 269  GLY   A O    1 
ATOM   4100  H  H    . GLY   A  1  269 ? 29.497  -31.769 -16.311  1.00 69.12  ? 269  GLY   A H    1 
ATOM   4101  H  HA2  . GLY   A  1  269 ? 30.426  -29.703 -14.985  1.00 70.67  ? 269  GLY   A HA2  1 
ATOM   4102  H  HA3  . GLY   A  1  269 ? 29.086  -30.476 -14.667  1.00 70.67  ? 269  GLY   A HA3  1 
ATOM   4103  N  N    . GLU   A  1  270 ? 30.739  -30.407 -12.556  1.00 65.62  ? 270  GLU   A N    1 
ATOM   4104  C  CA   . GLU   A  1  270 ? 31.402  -30.796 -11.321  1.00 70.37  ? 270  GLU   A CA   1 
ATOM   4105  C  C    . GLU   A  1  270 ? 30.443  -31.049 -10.167  1.00 65.70  ? 270  GLU   A C    1 
ATOM   4106  O  O    . GLU   A  1  270 ? 30.865  -31.615 -9.152   1.00 67.33  ? 270  GLU   A O    1 
ATOM   4107  C  CB   . GLU   A  1  270 ? 32.399  -29.708 -10.892  1.00 81.32  ? 270  GLU   A CB   1 
ATOM   4108  C  CG   . GLU   A  1  270 ? 33.552  -29.479 -11.854  1.00 94.77  ? 270  GLU   A CG   1 
ATOM   4109  C  CD   . GLU   A  1  270 ? 34.667  -30.492 -11.685  1.00 106.65 ? 270  GLU   A CD   1 
ATOM   4110  O  OE1  . GLU   A  1  270 ? 34.408  -31.702 -11.855  1.00 110.16 ? 270  GLU   A OE1  1 
ATOM   4111  O  OE2  . GLU   A  1  270 ? 35.802  -30.077 -11.370  1.00 111.49 ? 270  GLU   A OE2  1 
ATOM   4112  H  H    . GLU   A  1  270 ? 30.392  -29.621 -12.526  1.00 78.73  ? 270  GLU   A H    1 
ATOM   4113  H  HA   . GLU   A  1  270 ? 31.892  -31.616 -11.487  1.00 84.43  ? 270  GLU   A HA   1 
ATOM   4114  H  HB2  . GLU   A  1  270 ? 31.920  -28.869 -10.806  1.00 97.56  ? 270  GLU   A HB2  1 
ATOM   4115  H  HB3  . GLU   A  1  270 ? 32.780  -29.962 -10.037  1.00 97.56  ? 270  GLU   A HB3  1 
ATOM   4116  H  HG2  . GLU   A  1  270 ? 33.222  -29.546 -12.764  1.00 113.70 ? 270  GLU   A HG2  1 
ATOM   4117  H  HG3  . GLU   A  1  270 ? 33.922  -28.596 -11.700  1.00 113.70 ? 270  GLU   A HG3  1 
ATOM   4118  N  N    . GLN   A  1  271 ? 29.179  -30.648 -10.285  1.00 61.88  ? 271  GLN   A N    1 
ATOM   4119  C  CA   . GLN   A  1  271 ? 28.235  -30.733 -9.182   1.00 62.67  ? 271  GLN   A CA   1 
ATOM   4120  C  C    . GLN   A  1  271 ? 26.903  -31.266 -9.682   1.00 63.67  ? 271  GLN   A C    1 
ATOM   4121  O  O    . GLN   A  1  271 ? 26.433  -30.882 -10.757  1.00 64.24  ? 271  GLN   A O    1 
ATOM   4122  C  CB   . GLN   A  1  271 ? 28.034  -29.364 -8.520   1.00 62.57  ? 271  GLN   A CB   1 
ATOM   4123  C  CG   . GLN   A  1  271 ? 27.034  -29.369 -7.377   1.00 65.56  ? 271  GLN   A CG   1 
ATOM   4124  C  CD   . GLN   A  1  271 ? 26.900  -28.008 -6.718   1.00 67.59  ? 271  GLN   A CD   1 
ATOM   4125  O  OE1  . GLN   A  1  271 ? 25.916  -27.297 -6.926   1.00 72.06  ? 271  GLN   A OE1  1 
ATOM   4126  N  NE2  . GLN   A  1  271 ? 27.893  -27.640 -5.918   1.00 62.71  ? 271  GLN   A NE2  1 
ATOM   4127  H  H    . GLN   A  1  271 ? 28.844  -30.319 -11.006  1.00 74.24  ? 271  GLN   A H    1 
ATOM   4128  H  HA   . GLN   A  1  271 ? 28.573  -31.353 -8.516   1.00 75.18  ? 271  GLN   A HA   1 
ATOM   4129  H  HB2  . GLN   A  1  271 ? 28.885  -29.063 -8.165   1.00 75.07  ? 271  GLN   A HB2  1 
ATOM   4130  H  HB3  . GLN   A  1  271 ? 27.714  -28.740 -9.189   1.00 75.07  ? 271  GLN   A HB3  1 
ATOM   4131  H  HG2  . GLN   A  1  271 ? 26.163  -29.625 -7.719   1.00 78.65  ? 271  GLN   A HG2  1 
ATOM   4132  H  HG3  . GLN   A  1  271 ? 27.325  -30.002 -6.703   1.00 78.65  ? 271  GLN   A HG3  1 
ATOM   4133  H  HE21 . GLN   A  1  271 ? 28.564  -28.164 -5.797   1.00 75.24  ? 271  GLN   A HE21 1 
ATOM   4134  H  HE22 . GLN   A  1  271 ? 27.864  -26.878 -5.520   1.00 75.24  ? 271  GLN   A HE22 1 
ATOM   4135  N  N    . MET   A  1  272 ? 26.302  -32.150 -8.890   1.00 63.94  ? 272  MET   A N    1 
ATOM   4136  C  CA   . MET   A  1  272 ? 25.019  -32.734 -9.251   1.00 65.85  ? 272  MET   A CA   1 
ATOM   4137  C  C    . MET   A  1  272 ? 23.947  -31.659 -9.378   1.00 63.49  ? 272  MET   A C    1 
ATOM   4138  O  O    . MET   A  1  272 ? 23.817  -30.784 -8.518   1.00 64.48  ? 272  MET   A O    1 
ATOM   4139  C  CB   . MET   A  1  272 ? 24.605  -33.766 -8.201   1.00 73.87  ? 272  MET   A CB   1 
ATOM   4140  C  CG   . MET   A  1  272 ? 25.451  -35.028 -8.212   1.00 81.16  ? 272  MET   A CG   1 
ATOM   4141  S  SD   . MET   A  1  272 ? 24.624  -36.404 -9.034   1.00 88.47  ? 272  MET   A SD   1 
ATOM   4142  C  CE   . MET   A  1  272 ? 26.021  -37.451 -9.438   1.00 92.38  ? 272  MET   A CE   1 
ATOM   4143  H  H    . MET   A  1  272 ? 26.617  -32.426 -8.139   1.00 76.71  ? 272  MET   A H    1 
ATOM   4144  H  HA   . MET   A  1  272 ? 25.110  -33.185 -10.105  1.00 79.01  ? 272  MET   A HA   1 
ATOM   4145  H  HB2  . MET   A  1  272 ? 24.684  -33.364 -7.322   1.00 88.63  ? 272  MET   A HB2  1 
ATOM   4146  H  HB3  . MET   A  1  272 ? 23.684  -34.025 -8.366   1.00 88.63  ? 272  MET   A HB3  1 
ATOM   4147  H  HG2  . MET   A  1  272 ? 26.280  -34.850 -8.682   1.00 97.37  ? 272  MET   A HG2  1 
ATOM   4148  H  HG3  . MET   A  1  272 ? 25.638  -35.292 -7.297   1.00 97.37  ? 272  MET   A HG3  1 
ATOM   4149  H  HE1  . MET   A  1  272 ? 25.703  -38.230 -9.920   1.00 110.84 ? 272  MET   A HE1  1 
ATOM   4150  H  HE2  . MET   A  1  272 ? 26.642  -36.950 -9.990   1.00 110.84 ? 272  MET   A HE2  1 
ATOM   4151  H  HE3  . MET   A  1  272 ? 26.457  -37.726 -8.616   1.00 110.84 ? 272  MET   A HE3  1 
ATOM   4152  N  N    . ALA   A  1  273 ? 23.182  -31.728 -10.467  1.00 61.50  ? 273  ALA   A N    1 
ATOM   4153  C  CA   . ALA   A  1  273 ? 21.986  -30.907 -10.648  1.00 62.42  ? 273  ALA   A CA   1 
ATOM   4154  C  C    . ALA   A  1  273 ? 22.299  -29.413 -10.661  1.00 60.15  ? 273  ALA   A C    1 
ATOM   4155  O  O    . ALA   A  1  273 ? 21.446  -28.589 -10.321  1.00 60.45  ? 273  ALA   A O    1 
ATOM   4156  C  CB   . ALA   A  1  273 ? 20.944  -31.216 -9.569   1.00 62.41  ? 273  ALA   A CB   1 
ATOM   4157  H  H    . ALA   A  1  273 ? 23.338  -32.254 -11.129  1.00 73.79  ? 273  ALA   A H    1 
ATOM   4158  H  HA   . ALA   A  1  273 ? 21.609  -31.123 -11.515  1.00 74.89  ? 273  ALA   A HA   1 
ATOM   4159  H  HB1  . ALA   A  1  273 ? 20.162  -30.662 -9.717   1.00 74.88  ? 273  ALA   A HB1  1 
ATOM   4160  H  HB2  . ALA   A  1  273 ? 20.700  -32.154 -9.624   1.00 74.88  ? 273  ALA   A HB2  1 
ATOM   4161  H  HB3  . ALA   A  1  273 ? 21.325  -31.025 -8.697   1.00 74.88  ? 273  ALA   A HB3  1 
ATOM   4162  N  N    . ALA   A  1  274 ? 23.516  -29.042 -11.053  1.00 58.36  ? 274  ALA   A N    1 
ATOM   4163  C  CA   . ALA   A  1  274 ? 23.841  -27.638 -11.270  1.00 60.03  ? 274  ALA   A CA   1 
ATOM   4164  C  C    . ALA   A  1  274 ? 23.302  -27.116 -12.595  1.00 56.09  ? 274  ALA   A C    1 
ATOM   4165  O  O    . ALA   A  1  274 ? 23.483  -25.932 -12.899  1.00 57.37  ? 274  ALA   A O    1 
ATOM   4166  C  CB   . ALA   A  1  274 ? 25.356  -27.430 -11.215  1.00 61.03  ? 274  ALA   A CB   1 
ATOM   4167  H  H    . ALA   A  1  274 ? 24.167  -29.584 -11.200  1.00 70.01  ? 274  ALA   A H    1 
ATOM   4168  H  HA   . ALA   A  1  274 ? 23.447  -27.113 -10.555  1.00 72.01  ? 274  ALA   A HA   1 
ATOM   4169  H  HB1  . ALA   A  1  274 ? 25.551  -26.489 -11.345  1.00 73.22  ? 274  ALA   A HB1  1 
ATOM   4170  H  HB2  . ALA   A  1  274 ? 25.684  -27.719 -10.349  1.00 73.22  ? 274  ALA   A HB2  1 
ATOM   4171  H  HB3  . ALA   A  1  274 ? 25.773  -27.954 -11.917  1.00 73.22  ? 274  ALA   A HB3  1 
ATOM   4172  N  N    . TYR   A  1  275 ? 22.638  -27.967 -13.376  1.00 49.40  ? 275  TYR   A N    1 
ATOM   4173  C  CA   . TYR   A  1  275 ? 22.192  -27.629 -14.726  1.00 49.76  ? 275  TYR   A CA   1 
ATOM   4174  C  C    . TYR   A  1  275 ? 23.352  -27.102 -15.566  1.00 50.70  ? 275  TYR   A C    1 
ATOM   4175  O  O    . TYR   A  1  275 ? 23.235  -26.115 -16.296  1.00 46.47  ? 275  TYR   A O    1 
ATOM   4176  C  CB   . TYR   A  1  275 ? 21.022  -26.646 -14.695  1.00 51.31  ? 275  TYR   A CB   1 
ATOM   4177  C  CG   . TYR   A  1  275 ? 19.839  -27.185 -15.464  1.00 52.46  ? 275  TYR   A CG   1 
ATOM   4178  C  CD1  . TYR   A  1  275 ? 19.777  -27.065 -16.844  1.00 50.76  ? 275  TYR   A CD1  1 
ATOM   4179  C  CD2  . TYR   A  1  275 ? 18.805  -27.847 -14.816  1.00 52.58  ? 275  TYR   A CD2  1 
ATOM   4180  C  CE1  . TYR   A  1  275 ? 18.710  -27.570 -17.557  1.00 51.72  ? 275  TYR   A CE1  1 
ATOM   4181  C  CE2  . TYR   A  1  275 ? 17.731  -28.357 -15.521  1.00 52.66  ? 275  TYR   A CE2  1 
ATOM   4182  C  CZ   . TYR   A  1  275 ? 17.690  -28.217 -16.892  1.00 52.94  ? 275  TYR   A CZ   1 
ATOM   4183  O  OH   . TYR   A  1  275 ? 16.626  -28.721 -17.603  1.00 55.90  ? 275  TYR   A OH   1 
ATOM   4184  H  H    . TYR   A  1  275 ? 22.430  -28.768 -13.140  1.00 59.26  ? 275  TYR   A H    1 
ATOM   4185  H  HA   . TYR   A  1  275 ? 21.871  -28.438 -15.155  1.00 59.69  ? 275  TYR   A HA   1 
ATOM   4186  H  HB2  . TYR   A  1  275 ? 20.750  -26.497 -13.776  1.00 61.55  ? 275  TYR   A HB2  1 
ATOM   4187  H  HB3  . TYR   A  1  275 ? 21.296  -25.808 -15.099  1.00 61.55  ? 275  TYR   A HB3  1 
ATOM   4188  H  HD1  . TYR   A  1  275 ? 20.467  -26.637 -17.297  1.00 60.89  ? 275  TYR   A HD1  1 
ATOM   4189  H  HD2  . TYR   A  1  275 ? 18.835  -27.950 -13.892  1.00 63.07  ? 275  TYR   A HD2  1 
ATOM   4190  H  HE1  . TYR   A  1  275 ? 18.678  -27.475 -18.482  1.00 62.04  ? 275  TYR   A HE1  1 
ATOM   4191  H  HE2  . TYR   A  1  275 ? 17.041  -28.792 -15.074  1.00 63.17  ? 275  TYR   A HE2  1 
ATOM   4192  H  HH   . TYR   A  1  275 ? 16.219  -29.295 -17.143  1.00 67.06  ? 275  TYR   A HH   1 
ATOM   4193  N  N    . PHE   A  1  276 ? 24.488  -27.784 -15.458  1.00 51.50  ? 276  PHE   A N    1 
ATOM   4194  C  CA   . PHE   A  1  276 ? 25.636  -27.514 -16.311  1.00 52.53  ? 276  PHE   A CA   1 
ATOM   4195  C  C    . PHE   A  1  276 ? 25.267  -27.751 -17.769  1.00 52.70  ? 276  PHE   A C    1 
ATOM   4196  O  O    . PHE   A  1  276 ? 24.975  -28.882 -18.167  1.00 50.05  ? 276  PHE   A O    1 
ATOM   4197  C  CB   . PHE   A  1  276 ? 26.791  -28.418 -15.886  1.00 56.32  ? 276  PHE   A CB   1 
ATOM   4198  C  CG   . PHE   A  1  276 ? 28.025  -28.293 -16.731  1.00 56.37  ? 276  PHE   A CG   1 
ATOM   4199  C  CD1  . PHE   A  1  276 ? 28.207  -29.101 -17.843  1.00 57.92  ? 276  PHE   A CD1  1 
ATOM   4200  C  CD2  . PHE   A  1  276 ? 29.025  -27.397 -16.389  1.00 53.37  ? 276  PHE   A CD2  1 
ATOM   4201  C  CE1  . PHE   A  1  276 ? 29.354  -29.001 -18.611  1.00 58.50  ? 276  PHE   A CE1  1 
ATOM   4202  C  CE2  . PHE   A  1  276 ? 30.175  -27.291 -17.153  1.00 54.28  ? 276  PHE   A CE2  1 
ATOM   4203  C  CZ   . PHE   A  1  276 ? 30.341  -28.095 -18.263  1.00 56.51  ? 276  PHE   A CZ   1 
ATOM   4204  H  H    . PHE   A  1  276 ? 24.620  -28.417 -14.891  1.00 61.78  ? 276  PHE   A H    1 
ATOM   4205  H  HA   . PHE   A  1  276 ? 25.917  -26.590 -16.220  1.00 63.02  ? 276  PHE   A HA   1 
ATOM   4206  H  HB2  . PHE   A  1  276 ? 27.036  -28.197 -14.974  1.00 67.57  ? 276  PHE   A HB2  1 
ATOM   4207  H  HB3  . PHE   A  1  276 ? 26.494  -29.341 -15.934  1.00 67.57  ? 276  PHE   A HB3  1 
ATOM   4208  H  HD1  . PHE   A  1  276 ? 27.550  -29.718 -18.075  1.00 69.49  ? 276  PHE   A HD1  1 
ATOM   4209  H  HD2  . PHE   A  1  276 ? 28.922  -26.859 -15.638  1.00 64.03  ? 276  PHE   A HD2  1 
ATOM   4210  H  HE1  . PHE   A  1  276 ? 29.461  -29.542 -19.360  1.00 70.18  ? 276  PHE   A HE1  1 
ATOM   4211  H  HE2  . PHE   A  1  276 ? 30.835  -26.680 -16.918  1.00 65.12  ? 276  PHE   A HE2  1 
ATOM   4212  H  HZ   . PHE   A  1  276 ? 31.113  -28.027 -18.776  1.00 67.80  ? 276  PHE   A HZ   1 
ATOM   4213  N  N    . GLY   A  1  277 ? 25.284  -26.684 -18.565  1.00 53.75  ? 277  GLY   A N    1 
ATOM   4214  C  CA   . GLY   A  1  277 ? 24.880  -26.746 -19.956  1.00 54.19  ? 277  GLY   A CA   1 
ATOM   4215  C  C    . GLY   A  1  277 ? 23.551  -26.088 -20.255  1.00 55.74  ? 277  GLY   A C    1 
ATOM   4216  O  O    . GLY   A  1  277 ? 23.097  -26.148 -21.403  1.00 52.76  ? 277  GLY   A O    1 
ATOM   4217  H  H    . GLY   A  1  277 ? 25.531  -25.900 -18.313  1.00 64.48  ? 277  GLY   A H    1 
ATOM   4218  H  HA2  . GLY   A  1  277 ? 25.556  -26.309 -20.497  1.00 65.01  ? 277  GLY   A HA2  1 
ATOM   4219  H  HA3  . GLY   A  1  277 ? 24.816  -27.677 -20.221  1.00 65.01  ? 277  GLY   A HA3  1 
ATOM   4220  N  N    . PHE   A  1  278 ? 22.905  -25.471 -19.261  1.00 55.03  ? 278  PHE   A N    1 
ATOM   4221  C  CA   . PHE   A  1  278 ? 21.685  -24.715 -19.521  1.00 54.98  ? 278  PHE   A CA   1 
ATOM   4222  C  C    . PHE   A  1  278 ? 21.895  -23.697 -20.632  1.00 52.12  ? 278  PHE   A C    1 
ATOM   4223  O  O    . PHE   A  1  278 ? 20.969  -23.409 -21.398  1.00 48.48  ? 278  PHE   A O    1 
ATOM   4224  C  CB   . PHE   A  1  278 ? 21.228  -24.016 -18.239  1.00 56.61  ? 278  PHE   A CB   1 
ATOM   4225  C  CG   . PHE   A  1  278 ? 19.949  -23.243 -18.387  1.00 56.56  ? 278  PHE   A CG   1 
ATOM   4226  C  CD1  . PHE   A  1  278 ? 18.724  -23.876 -18.259  1.00 55.69  ? 278  PHE   A CD1  1 
ATOM   4227  C  CD2  . PHE   A  1  278 ? 19.971  -21.882 -18.643  1.00 55.55  ? 278  PHE   A CD2  1 
ATOM   4228  C  CE1  . PHE   A  1  278 ? 17.545  -23.167 -18.391  1.00 55.05  ? 278  PHE   A CE1  1 
ATOM   4229  C  CE2  . PHE   A  1  278 ? 18.795  -21.168 -18.776  1.00 55.65  ? 278  PHE   A CE2  1 
ATOM   4230  C  CZ   . PHE   A  1  278 ? 17.581  -21.812 -18.649  1.00 55.30  ? 278  PHE   A CZ   1 
ATOM   4231  H  H    . PHE   A  1  278 ? 23.151  -25.477 -18.437  1.00 66.02  ? 278  PHE   A H    1 
ATOM   4232  H  HA   . PHE   A  1  278 ? 20.983  -25.324 -19.799  1.00 65.96  ? 278  PHE   A HA   1 
ATOM   4233  H  HB2  . PHE   A  1  278 ? 21.090  -24.687 -17.552  1.00 67.91  ? 278  PHE   A HB2  1 
ATOM   4234  H  HB3  . PHE   A  1  278 ? 21.919  -23.394 -17.961  1.00 67.91  ? 278  PHE   A HB3  1 
ATOM   4235  H  HD1  . PHE   A  1  278 ? 18.694  -24.788 -18.081  1.00 66.80  ? 278  PHE   A HD1  1 
ATOM   4236  H  HD2  . PHE   A  1  278 ? 20.787  -21.443 -18.727  1.00 66.64  ? 278  PHE   A HD2  1 
ATOM   4237  H  HE1  . PHE   A  1  278 ? 16.728  -23.603 -18.306  1.00 66.04  ? 278  PHE   A HE1  1 
ATOM   4238  H  HE2  . PHE   A  1  278 ? 18.821  -20.255 -18.950  1.00 66.76  ? 278  PHE   A HE2  1 
ATOM   4239  H  HZ   . PHE   A  1  278 ? 16.788  -21.334 -18.737  1.00 66.34  ? 278  PHE   A HZ   1 
ATOM   4240  N  N    . SER   A  1  279 ? 23.103  -23.149 -20.735  1.00 53.01  ? 279  SER   A N    1 
ATOM   4241  C  CA   . SER   A  1  279 ? 23.444  -22.182 -21.767  1.00 55.55  ? 279  SER   A CA   1 
ATOM   4242  C  C    . SER   A  1  279 ? 24.891  -22.393 -22.184  1.00 54.03  ? 279  SER   A C    1 
ATOM   4243  O  O    . SER   A  1  279 ? 25.734  -22.793 -21.377  1.00 51.09  ? 279  SER   A O    1 
ATOM   4244  C  CB   . SER   A  1  279 ? 23.238  -20.745 -21.275  1.00 59.95  ? 279  SER   A CB   1 
ATOM   4245  O  OG   . SER   A  1  279 ? 23.919  -20.524 -20.052  1.00 65.42  ? 279  SER   A OG   1 
ATOM   4246  H  H    . SER   A  1  279 ? 23.757  -23.326 -20.205  1.00 63.59  ? 279  SER   A H    1 
ATOM   4247  H  HA   . SER   A  1  279 ? 22.880  -22.324 -22.543  1.00 66.64  ? 279  SER   A HA   1 
ATOM   4248  H  HB2  . SER   A  1  279 ? 23.582  -20.131 -21.943  1.00 71.92  ? 279  SER   A HB2  1 
ATOM   4249  H  HB3  . SER   A  1  279 ? 22.290  -20.590 -21.140  1.00 71.92  ? 279  SER   A HB3  1 
ATOM   4250  H  HG   . SER   A  1  279 ? 23.535  -19.919 -19.614  1.00 78.49  ? 279  SER   A HG   1 
ATOM   4251  N  N    . VAL   A  1  280 ? 25.169  -22.125 -23.459  1.00 55.36  ? 280  VAL   A N    1 
ATOM   4252  C  CA   . VAL   A  1  280 ? 26.516  -22.222 -24.002  1.00 58.33  ? 280  VAL   A CA   1 
ATOM   4253  C  C    . VAL   A  1  280 ? 26.726  -21.082 -24.988  1.00 59.04  ? 280  VAL   A C    1 
ATOM   4254  O  O    . VAL   A  1  280 ? 25.780  -20.592 -25.613  1.00 57.45  ? 280  VAL   A O    1 
ATOM   4255  C  CB   . VAL   A  1  280 ? 26.777  -23.584 -24.686  1.00 60.46  ? 280  VAL   A CB   1 
ATOM   4256  C  CG1  . VAL   A  1  280 ? 26.651  -24.723 -23.682  1.00 62.91  ? 280  VAL   A CG1  1 
ATOM   4257  C  CG2  . VAL   A  1  280 ? 25.828  -23.790 -25.858  1.00 59.30  ? 280  VAL   A CG2  1 
ATOM   4258  H  H    . VAL   A  1  280 ? 24.580  -21.881 -24.037  1.00 66.41  ? 280  VAL   A H    1 
ATOM   4259  H  HA   . VAL   A  1  280 ? 27.154  -22.125 -23.278  1.00 69.98  ? 280  VAL   A HA   1 
ATOM   4260  H  HB   . VAL   A  1  280 ? 27.683  -23.589 -25.033  1.00 72.54  ? 280  VAL   A HB   1 
ATOM   4261  H  HG11 . VAL   A  1  280 ? 26.837  -25.562 -24.131  1.00 75.48  ? 280  VAL   A HG11 1 
ATOM   4262  H  HG12 . VAL   A  1  280 ? 27.288  -24.583 -22.965  1.00 75.48  ? 280  VAL   A HG12 1 
ATOM   4263  H  HG13 . VAL   A  1  280 ? 25.748  -24.731 -23.327  1.00 75.48  ? 280  VAL   A HG13 1 
ATOM   4264  H  HG21 . VAL   A  1  280 ? 25.985  -24.667 -26.242  1.00 71.14  ? 280  VAL   A HG21 1 
ATOM   4265  H  HG22 . VAL   A  1  280 ? 24.914  -23.728 -25.538  1.00 71.14  ? 280  VAL   A HG22 1 
ATOM   4266  H  HG23 . VAL   A  1  280 ? 25.993  -23.104 -26.523  1.00 71.14  ? 280  VAL   A HG23 1 
ATOM   4267  N  N    . ALA   A  1  281 ? 27.980  -20.659 -25.122  1.00 57.46  ? 281  ALA   A N    1 
ATOM   4268  C  CA   . ALA   A  1  281 ? 28.343  -19.615 -26.066  1.00 56.75  ? 281  ALA   A CA   1 
ATOM   4269  C  C    . ALA   A  1  281 ? 29.757  -19.874 -26.563  1.00 54.41  ? 281  ALA   A C    1 
ATOM   4270  O  O    . ALA   A  1  281 ? 30.564  -20.517 -25.885  1.00 52.34  ? 281  ALA   A O    1 
ATOM   4271  C  CB   . ALA   A  1  281 ? 28.243  -18.220 -25.436  1.00 57.94  ? 281  ALA   A CB   1 
ATOM   4272  H  H    . ALA   A  1  281 ? 28.645  -20.967 -24.670  1.00 68.94  ? 281  ALA   A H    1 
ATOM   4273  H  HA   . ALA   A  1  281 ? 27.743  -19.641 -26.827  1.00 68.08  ? 281  ALA   A HA   1 
ATOM   4274  H  HB1  . ALA   A  1  281 ? 28.492  -17.556 -26.098  1.00 69.51  ? 281  ALA   A HB1  1 
ATOM   4275  H  HB2  . ALA   A  1  281 ? 27.330  -18.070 -25.145  1.00 69.51  ? 281  ALA   A HB2  1 
ATOM   4276  H  HB3  . ALA   A  1  281 ? 28.844  -18.173 -24.676  1.00 69.51  ? 281  ALA   A HB3  1 
ATOM   4277  N  N    . ALA   A  1  282 ? 30.048  -19.369 -27.759  1.00 53.90  ? 282  ALA   A N    1 
ATOM   4278  C  CA   . ALA   A  1  282 ? 31.358  -19.524 -28.377  1.00 53.75  ? 282  ALA   A CA   1 
ATOM   4279  C  C    . ALA   A  1  282 ? 31.801  -18.184 -28.943  1.00 57.46  ? 282  ALA   A C    1 
ATOM   4280  O  O    . ALA   A  1  282 ? 31.121  -17.614 -29.802  1.00 58.53  ? 282  ALA   A O    1 
ATOM   4281  C  CB   . ALA   A  1  282 ? 31.328  -20.590 -29.476  1.00 50.86  ? 282  ALA   A CB   1 
ATOM   4282  H  H    . ALA   A  1  282 ? 29.490  -18.924 -28.240  1.00 64.66  ? 282  ALA   A H    1 
ATOM   4283  H  HA   . ALA   A  1  282 ? 32.001  -19.795 -27.703  1.00 64.49  ? 282  ALA   A HA   1 
ATOM   4284  H  HB1  . ALA   A  1  282 ? 32.212  -20.665 -29.868  1.00 61.01  ? 282  ALA   A HB1  1 
ATOM   4285  H  HB2  . ALA   A  1  282 ? 31.066  -21.438 -29.086  1.00 61.01  ? 282  ALA   A HB2  1 
ATOM   4286  H  HB3  . ALA   A  1  282 ? 30.687  -20.326 -30.155  1.00 61.01  ? 282  ALA   A HB3  1 
ATOM   4287  N  N    . THR   A  1  283 ? 32.938  -17.687 -28.461  1.00 57.15  ? 283  THR   A N    1 
ATOM   4288  C  CA   . THR   A  1  283 ? 33.509  -16.443 -28.953  1.00 58.79  ? 283  THR   A CA   1 
ATOM   4289  C  C    . THR   A  1  283 ? 34.952  -16.354 -28.480  1.00 63.67  ? 283  THR   A C    1 
ATOM   4290  O  O    . THR   A  1  283 ? 35.272  -16.792 -27.372  1.00 64.23  ? 283  THR   A O    1 
ATOM   4291  C  CB   . THR   A  1  283 ? 32.710  -15.224 -28.468  1.00 58.85  ? 283  THR   A CB   1 
ATOM   4292  O  OG1  . THR   A  1  283 ? 33.296  -14.026 -28.992  1.00 60.47  ? 283  THR   A OG1  1 
ATOM   4293  C  CG2  . THR   A  1  283 ? 32.690  -15.153 -26.946  1.00 56.97  ? 283  THR   A CG2  1 
ATOM   4294  H  H    . THR   A  1  283 ? 33.402  -18.059 -27.840  1.00 68.56  ? 283  THR   A H    1 
ATOM   4295  H  HA   . THR   A  1  283 ? 33.499  -16.440 -29.923  1.00 70.53  ? 283  THR   A HA   1 
ATOM   4296  H  HB   . THR   A  1  283 ? 31.794  -15.301 -28.778  1.00 70.61  ? 283  THR   A HB   1 
ATOM   4297  H  HG1  . THR   A  1  283 ? 32.889  -13.353 -28.695  1.00 72.55  ? 283  THR   A HG1  1 
ATOM   4298  H  HG21 . THR   A  1  283 ? 32.159  -14.394 -26.656  1.00 68.34  ? 283  THR   A HG21 1 
ATOM   4299  H  HG22 . THR   A  1  283 ? 32.304  -15.964 -26.581  1.00 68.34  ? 283  THR   A HG22 1 
ATOM   4300  H  HG23 . THR   A  1  283 ? 33.593  -15.053 -26.606  1.00 68.34  ? 283  THR   A HG23 1 
ATOM   4301  N  N    . ASP   A  1  284 ? 35.815  -15.794 -29.325  1.00 68.14  ? 284  ASP   A N    1 
ATOM   4302  C  CA   . ASP   A  1  284 ? 37.227  -15.625 -28.991  1.00 67.17  ? 284  ASP   A CA   1 
ATOM   4303  C  C    . ASP   A  1  284 ? 37.363  -14.450 -28.031  1.00 66.06  ? 284  ASP   A C    1 
ATOM   4304  O  O    . ASP   A  1  284 ? 37.229  -13.291 -28.437  1.00 69.15  ? 284  ASP   A O    1 
ATOM   4305  C  CB   . ASP   A  1  284 ? 38.053  -15.397 -30.253  1.00 67.55  ? 284  ASP   A CB   1 
ATOM   4306  C  CG   . ASP   A  1  284 ? 39.527  -15.181 -29.955  1.00 69.11  ? 284  ASP   A CG   1 
ATOM   4307  O  OD1  . ASP   A  1  284 ? 39.967  -15.519 -28.836  1.00 69.01  ? 284  ASP   A OD1  1 
ATOM   4308  O  OD2  . ASP   A  1  284 ? 40.244  -14.664 -30.838  1.00 70.13  ? 284  ASP   A OD2  1 
ATOM   4309  H  H    . ASP   A  1  284 ? 35.605  -15.501 -30.106  1.00 81.75  ? 284  ASP   A H    1 
ATOM   4310  H  HA   . ASP   A  1  284 ? 37.553  -16.427 -28.554  1.00 80.59  ? 284  ASP   A HA   1 
ATOM   4311  H  HB2  . ASP   A  1  284 ? 37.973  -16.175 -30.828  1.00 81.04  ? 284  ASP   A HB2  1 
ATOM   4312  H  HB3  . ASP   A  1  284 ? 37.720  -14.610 -30.712  1.00 81.04  ? 284  ASP   A HB3  1 
ATOM   4313  N  N    . ILE   A  1  285 ? 37.644  -14.742 -26.761  1.00 64.32  ? 285  ILE   A N    1 
ATOM   4314  C  CA   . ILE   A  1  285 ? 37.655  -13.703 -25.738  1.00 65.82  ? 285  ILE   A CA   1 
ATOM   4315  C  C    . ILE   A  1  285 ? 39.033  -13.085 -25.520  1.00 67.98  ? 285  ILE   A C    1 
ATOM   4316  O  O    . ILE   A  1  285 ? 39.125  -12.005 -24.918  1.00 67.45  ? 285  ILE   A O    1 
ATOM   4317  C  CB   . ILE   A  1  285 ? 37.124  -14.265 -24.405  1.00 67.39  ? 285  ILE   A CB   1 
ATOM   4318  C  CG1  . ILE   A  1  285 ? 36.564  -13.142 -23.529  1.00 71.49  ? 285  ILE   A CG1  1 
ATOM   4319  C  CG2  . ILE   A  1  285 ? 38.220  -15.018 -23.654  1.00 68.71  ? 285  ILE   A CG2  1 
ATOM   4320  C  CD1  . ILE   A  1  285 ? 35.202  -12.646 -23.970  1.00 73.25  ? 285  ILE   A CD1  1 
ATOM   4321  H  H    . ILE   A  1  285 ? 37.831  -15.530 -26.470  1.00 77.16  ? 285  ILE   A H    1 
ATOM   4322  H  HA   . ILE   A  1  285 ? 37.068  -12.989 -26.033  1.00 78.96  ? 285  ILE   A HA   1 
ATOM   4323  H  HB   . ILE   A  1  285 ? 36.408  -14.886 -24.612  1.00 80.85  ? 285  ILE   A HB   1 
ATOM   4324  H  HG12 . ILE   A  1  285 ? 36.480  -13.468 -22.619  1.00 85.77  ? 285  ILE   A HG12 1 
ATOM   4325  H  HG13 . ILE   A  1  285 ? 37.176  -12.390 -23.557  1.00 85.77  ? 285  ILE   A HG13 1 
ATOM   4326  H  HG21 . ILE   A  1  285 ? 37.816  -15.532 -22.937  1.00 82.43  ? 285  ILE   A HG21 1 
ATOM   4327  H  HG22 . ILE   A  1  285 ? 38.674  -15.613 -24.271  1.00 82.43  ? 285  ILE   A HG22 1 
ATOM   4328  H  HG23 . ILE   A  1  285 ? 38.849  -14.378 -23.287  1.00 82.43  ? 285  ILE   A HG23 1 
ATOM   4329  H  HD11 . ILE   A  1  285 ? 34.901  -11.959 -23.355  1.00 87.88  ? 285  ILE   A HD11 1 
ATOM   4330  H  HD12 . ILE   A  1  285 ? 35.274  -12.280 -24.866  1.00 87.88  ? 285  ILE   A HD12 1 
ATOM   4331  H  HD13 . ILE   A  1  285 ? 34.578  -13.389 -23.966  1.00 87.88  ? 285  ILE   A HD13 1 
ATOM   4332  N  N    . ASN   A  1  286 ? 40.103  -13.725 -25.995  1.00 68.85  ? 286  ASN   A N    1 
ATOM   4333  C  CA   . ASN   A  1  286 ? 41.461  -13.268 -25.717  1.00 69.40  ? 286  ASN   A CA   1 
ATOM   4334  C  C    . ASN   A  1  286 ? 42.245  -12.911 -26.975  1.00 69.89  ? 286  ASN   A C    1 
ATOM   4335  O  O    . ASN   A  1  286 ? 43.464  -12.716 -26.897  1.00 76.09  ? 286  ASN   A O    1 
ATOM   4336  C  CB   . ASN   A  1  286 ? 42.218  -14.330 -24.914  1.00 69.25  ? 286  ASN   A CB   1 
ATOM   4337  C  CG   . ASN   A  1  286 ? 42.293  -15.660 -25.632  1.00 67.56  ? 286  ASN   A CG   1 
ATOM   4338  O  OD1  . ASN   A  1  286 ? 41.396  -16.017 -26.394  1.00 65.04  ? 286  ASN   A OD1  1 
ATOM   4339  N  ND2  . ASN   A  1  286 ? 43.367  -16.402 -25.391  1.00 69.23  ? 286  ASN   A ND2  1 
ATOM   4340  H  H    . ASN   A  1  286 ? 40.066  -14.432 -26.484  1.00 82.61  ? 286  ASN   A H    1 
ATOM   4341  H  HA   . ASN   A  1  286 ? 41.403  -12.462 -25.181  1.00 83.26  ? 286  ASN   A HA   1 
ATOM   4342  H  HB2  . ASN   A  1  286 ? 43.125  -14.022 -24.758  1.00 83.08  ? 286  ASN   A HB2  1 
ATOM   4343  H  HB3  . ASN   A  1  286 ? 41.765  -14.470 -24.068  1.00 83.08  ? 286  ASN   A HB3  1 
ATOM   4344  H  HD21 . ASN   A  1  286 ? 43.455  -17.166 -25.775  1.00 83.05  ? 286  ASN   A HD21 1 
ATOM   4345  H  HD22 . ASN   A  1  286 ? 43.973  -16.119 -24.852  1.00 83.05  ? 286  ASN   A HD22 1 
ATOM   4346  N  N    . GLY   A  1  287 ? 41.588  -12.828 -28.130  1.00 67.27  ? 287  GLY   A N    1 
ATOM   4347  C  CA   . GLY   A  1  287 ? 42.213  -12.262 -29.309  1.00 66.58  ? 287  GLY   A CA   1 
ATOM   4348  C  C    . GLY   A  1  287 ? 43.200  -13.146 -30.036  1.00 68.05  ? 287  GLY   A C    1 
ATOM   4349  O  O    . GLY   A  1  287 ? 44.030  -12.627 -30.789  1.00 70.45  ? 287  GLY   A O    1 
ATOM   4350  H  H    . GLY   A  1  287 ? 40.780  -13.094 -28.252  1.00 80.71  ? 287  GLY   A H    1 
ATOM   4351  H  HA2  . GLY   A  1  287 ? 41.515  -12.028 -29.941  1.00 79.88  ? 287  GLY   A HA2  1 
ATOM   4352  H  HA3  . GLY   A  1  287 ? 42.685  -11.457 -29.047  1.00 79.88  ? 287  GLY   A HA3  1 
ATOM   4353  N  N    . ASP   A  1  288 ? 43.142  -14.463 -29.847  1.00 67.69  ? 288  ASP   A N    1 
ATOM   4354  C  CA   . ASP   A  1  288 ? 44.021  -15.384 -30.557  1.00 70.41  ? 288  ASP   A CA   1 
ATOM   4355  C  C    . ASP   A  1  288 ? 43.331  -16.062 -31.735  1.00 75.64  ? 288  ASP   A C    1 
ATOM   4356  O  O    . ASP   A  1  288 ? 43.870  -17.030 -32.282  1.00 79.23  ? 288  ASP   A O    1 
ATOM   4357  C  CB   . ASP   A  1  288 ? 44.575  -16.440 -29.596  1.00 70.99  ? 288  ASP   A CB   1 
ATOM   4358  C  CG   . ASP   A  1  288 ? 43.487  -17.279 -28.948  1.00 72.35  ? 288  ASP   A CG   1 
ATOM   4359  O  OD1  . ASP   A  1  288 ? 42.291  -17.031 -29.215  1.00 71.92  ? 288  ASP   A OD1  1 
ATOM   4360  O  OD2  . ASP   A  1  288 ? 43.830  -18.192 -28.167  1.00 71.91  ? 288  ASP   A OD2  1 
ATOM   4361  H  H    . ASP   A  1  288 ? 42.595  -14.849 -29.307  1.00 81.21  ? 288  ASP   A H    1 
ATOM   4362  H  HA   . ASP   A  1  288 ? 44.773  -14.879 -30.904  1.00 84.47  ? 288  ASP   A HA   1 
ATOM   4363  H  HB2  . ASP   A  1  288 ? 45.161  -17.038 -30.087  1.00 85.17  ? 288  ASP   A HB2  1 
ATOM   4364  H  HB3  . ASP   A  1  288 ? 45.071  -15.996 -28.890  1.00 85.17  ? 288  ASP   A HB3  1 
ATOM   4365  N  N    . ASP   A  1  289 ? 42.158  -15.577 -32.136  1.00 76.28  ? 289  ASP   A N    1 
ATOM   4366  C  CA   . ASP   A  1  289 ? 41.386  -16.104 -33.258  1.00 75.83  ? 289  ASP   A CA   1 
ATOM   4367  C  C    . ASP   A  1  289 ? 40.935  -17.545 -33.046  1.00 71.40  ? 289  ASP   A C    1 
ATOM   4368  O  O    . ASP   A  1  289 ? 40.429  -18.174 -33.983  1.00 72.85  ? 289  ASP   A O    1 
ATOM   4369  C  CB   . ASP   A  1  289 ? 42.171  -15.995 -34.573  1.00 81.43  ? 289  ASP   A CB   1 
ATOM   4370  C  CG   . ASP   A  1  289 ? 42.357  -14.556 -35.023  1.00 85.07  ? 289  ASP   A CG   1 
ATOM   4371  O  OD1  . ASP   A  1  289 ? 41.406  -13.759 -34.882  1.00 84.86  ? 289  ASP   A OD1  1 
ATOM   4372  O  OD2  . ASP   A  1  289 ? 43.456  -14.222 -35.516  1.00 86.24  ? 289  ASP   A OD2  1 
ATOM   4373  H  H    . ASP   A  1  289 ? 41.771  -14.911 -31.754  1.00 91.52  ? 289  ASP   A H    1 
ATOM   4374  H  HA   . ASP   A  1  289 ? 40.583  -15.567 -33.341  1.00 90.98  ? 289  ASP   A HA   1 
ATOM   4375  H  HB2  . ASP   A  1  289 ? 43.049  -16.388 -34.451  1.00 97.70  ? 289  ASP   A HB2  1 
ATOM   4376  H  HB3  . ASP   A  1  289 ? 41.690  -16.468 -35.270  1.00 97.70  ? 289  ASP   A HB3  1 
ATOM   4377  N  N    . TYR   A  1  290 ? 41.102  -18.085 -31.842  1.00 69.35  ? 290  TYR   A N    1 
ATOM   4378  C  CA   . TYR   A  1  290 ? 40.591  -19.404 -31.492  1.00 68.19  ? 290  TYR   A CA   1 
ATOM   4379  C  C    . TYR   A  1  290 ? 39.343  -19.229 -30.637  1.00 67.56  ? 290  TYR   A C    1 
ATOM   4380  O  O    . TYR   A  1  290 ? 39.400  -18.615 -29.566  1.00 68.36  ? 290  TYR   A O    1 
ATOM   4381  C  CB   . TYR   A  1  290 ? 41.644  -20.224 -30.747  1.00 68.08  ? 290  TYR   A CB   1 
ATOM   4382  C  CG   . TYR   A  1  290 ? 42.719  -20.795 -31.642  1.00 70.58  ? 290  TYR   A CG   1 
ATOM   4383  C  CD1  . TYR   A  1  290 ? 42.496  -21.953 -32.374  1.00 68.09  ? 290  TYR   A CD1  1 
ATOM   4384  C  CD2  . TYR   A  1  290 ? 43.958  -20.180 -31.751  1.00 74.40  ? 290  TYR   A CD2  1 
ATOM   4385  C  CE1  . TYR   A  1  290 ? 43.474  -22.481 -33.193  1.00 70.49  ? 290  TYR   A CE1  1 
ATOM   4386  C  CE2  . TYR   A  1  290 ? 44.944  -20.700 -32.566  1.00 75.30  ? 290  TYR   A CE2  1 
ATOM   4387  C  CZ   . TYR   A  1  290 ? 44.697  -21.851 -33.285  1.00 73.87  ? 290  TYR   A CZ   1 
ATOM   4388  O  OH   . TYR   A  1  290 ? 45.677  -22.372 -34.098  1.00 72.00  ? 290  TYR   A OH   1 
ATOM   4389  H  H    . TYR   A  1  290 ? 41.516  -17.696 -31.196  1.00 83.20  ? 290  TYR   A H    1 
ATOM   4390  H  HA   . TYR   A  1  290 ? 40.355  -19.886 -32.300  1.00 81.81  ? 290  TYR   A HA   1 
ATOM   4391  H  HB2  . TYR   A  1  290 ? 42.076  -19.654 -30.092  1.00 81.67  ? 290  TYR   A HB2  1 
ATOM   4392  H  HB3  . TYR   A  1  290 ? 41.204  -20.966 -30.303  1.00 81.67  ? 290  TYR   A HB3  1 
ATOM   4393  H  HD1  . TYR   A  1  290 ? 41.673  -22.382 -32.312  1.00 81.68  ? 290  TYR   A HD1  1 
ATOM   4394  H  HD2  . TYR   A  1  290 ? 44.128  -19.404 -31.267  1.00 89.26  ? 290  TYR   A HD2  1 
ATOM   4395  H  HE1  . TYR   A  1  290 ? 43.310  -23.256 -33.679  1.00 84.57  ? 290  TYR   A HE1  1 
ATOM   4396  H  HE2  . TYR   A  1  290 ? 45.769  -20.277 -32.631  1.00 90.33  ? 290  TYR   A HE2  1 
ATOM   4397  H  HH   . TYR   A  1  290 ? 46.374  -21.907 -34.041  1.00 86.38  ? 290  TYR   A HH   1 
ATOM   4398  N  N    . ALA   A  1  291 ? 38.221  -19.764 -31.113  1.00 66.98  ? 291  ALA   A N    1 
ATOM   4399  C  CA   . ALA   A  1  291 ? 36.963  -19.624 -30.394  1.00 65.13  ? 291  ALA   A CA   1 
ATOM   4400  C  C    . ALA   A  1  291 ? 37.060  -20.261 -29.013  1.00 61.03  ? 291  ALA   A C    1 
ATOM   4401  O  O    . ALA   A  1  291 ? 37.636  -21.339 -28.845  1.00 59.49  ? 291  ALA   A O    1 
ATOM   4402  C  CB   . ALA   A  1  291 ? 35.824  -20.262 -31.189  1.00 65.75  ? 291  ALA   A CB   1 
ATOM   4403  H  H    . ALA   A  1  291 ? 38.163  -20.210 -31.846  1.00 80.35  ? 291  ALA   A H    1 
ATOM   4404  H  HA   . ALA   A  1  291 ? 36.763  -18.681 -30.280  1.00 78.14  ? 291  ALA   A HA   1 
ATOM   4405  H  HB1  . ALA   A  1  291 ? 34.996  -20.157 -30.695  1.00 78.88  ? 291  ALA   A HB1  1 
ATOM   4406  H  HB2  . ALA   A  1  291 ? 35.754  -19.821 -32.050  1.00 78.88  ? 291  ALA   A HB2  1 
ATOM   4407  H  HB3  . ALA   A  1  291 ? 36.017  -21.205 -31.315  1.00 78.88  ? 291  ALA   A HB3  1 
ATOM   4408  N  N    . ASP   A  1  292 ? 36.487  -19.583 -28.023  1.00 60.29  ? 292  ASP   A N    1 
ATOM   4409  C  CA   . ASP   A  1  292 ? 36.501  -20.030 -26.639  1.00 62.50  ? 292  ASP   A CA   1 
ATOM   4410  C  C    . ASP   A  1  292 ? 35.087  -20.384 -26.195  1.00 63.71  ? 292  ASP   A C    1 
ATOM   4411  O  O    . ASP   A  1  292 ? 34.111  -19.756 -26.614  1.00 66.93  ? 292  ASP   A O    1 
ATOM   4412  C  CB   . ASP   A  1  292 ? 37.092  -18.947 -25.732  1.00 64.36  ? 292  ASP   A CB   1 
ATOM   4413  C  CG   . ASP   A  1  292 ? 38.447  -18.455 -26.224  1.00 66.39  ? 292  ASP   A CG   1 
ATOM   4414  O  OD1  . ASP   A  1  292 ? 39.244  -19.290 -26.702  1.00 68.14  ? 292  ASP   A OD1  1 
ATOM   4415  O  OD2  . ASP   A  1  292 ? 38.715  -17.237 -26.147  1.00 66.96  ? 292  ASP   A OD2  1 
ATOM   4416  H  H    . ASP   A  1  292 ? 36.072  -18.839 -28.134  1.00 72.33  ? 292  ASP   A H    1 
ATOM   4417  H  HA   . ASP   A  1  292 ? 37.046  -20.827 -26.549  1.00 74.98  ? 292  ASP   A HA   1 
ATOM   4418  H  HB2  . ASP   A  1  292 ? 36.487  -18.190 -25.706  1.00 77.21  ? 292  ASP   A HB2  1 
ATOM   4419  H  HB3  . ASP   A  1  292 ? 37.209  -19.309 -24.840  1.00 77.21  ? 292  ASP   A HB3  1 
ATOM   4420  N  N    . VAL   A  1  293 ? 34.987  -21.399 -25.340  1.00 60.99  ? 293  VAL   A N    1 
ATOM   4421  C  CA   . VAL   A  1  293 ? 33.707  -21.973 -24.942  1.00 56.81  ? 293  VAL   A CA   1 
ATOM   4422  C  C    . VAL   A  1  293 ? 33.315  -21.425 -23.579  1.00 53.90  ? 293  VAL   A C    1 
ATOM   4423  O  O    . VAL   A  1  293 ? 34.134  -21.394 -22.651  1.00 56.44  ? 293  VAL   A O    1 
ATOM   4424  C  CB   . VAL   A  1  293 ? 33.772  -23.511 -24.913  1.00 56.72  ? 293  VAL   A CB   1 
ATOM   4425  C  CG1  . VAL   A  1  293 ? 32.443  -24.092 -24.446  1.00 57.15  ? 293  VAL   A CG1  1 
ATOM   4426  C  CG2  . VAL   A  1  293 ? 34.143  -24.053 -26.282  1.00 56.94  ? 293  VAL   A CG2  1 
ATOM   4427  H  H    . VAL   A  1  293 ? 35.663  -21.779 -24.969  1.00 73.17  ? 293  VAL   A H    1 
ATOM   4428  H  HA   . VAL   A  1  293 ? 33.030  -21.702 -25.582  1.00 68.15  ? 293  VAL   A HA   1 
ATOM   4429  H  HB   . VAL   A  1  293 ? 34.458  -23.784 -24.284  1.00 68.05  ? 293  VAL   A HB   1 
ATOM   4430  H  HG11 . VAL   A  1  293 ? 32.474  -25.058 -24.529  1.00 68.56  ? 293  VAL   A HG11 1 
ATOM   4431  H  HG12 . VAL   A  1  293 ? 32.298  -23.844 -23.519  1.00 68.56  ? 293  VAL   A HG12 1 
ATOM   4432  H  HG13 . VAL   A  1  293 ? 31.730  -23.736 -24.999  1.00 68.56  ? 293  VAL   A HG13 1 
ATOM   4433  H  HG21 . VAL   A  1  293 ? 34.157  -25.022 -26.244  1.00 68.31  ? 293  VAL   A HG21 1 
ATOM   4434  H  HG22 . VAL   A  1  293 ? 33.483  -23.757 -26.928  1.00 68.31  ? 293  VAL   A HG22 1 
ATOM   4435  H  HG23 . VAL   A  1  293 ? 35.019  -23.718 -26.527  1.00 68.31  ? 293  VAL   A HG23 1 
ATOM   4436  N  N    . PHE   A  1  294 ? 32.061  -20.998 -23.459  1.00 53.47  ? 294  PHE   A N    1 
ATOM   4437  C  CA   . PHE   A  1  294 ? 31.472  -20.569 -22.197  1.00 54.62  ? 294  PHE   A CA   1 
ATOM   4438  C  C    . PHE   A  1  294 ? 30.286  -21.474 -21.893  1.00 52.57  ? 294  PHE   A C    1 
ATOM   4439  O  O    . PHE   A  1  294 ? 29.464  -21.738 -22.776  1.00 51.27  ? 294  PHE   A O    1 
ATOM   4440  C  CB   . PHE   A  1  294 ? 31.027  -19.105 -22.264  1.00 55.93  ? 294  PHE   A CB   1 
ATOM   4441  C  CG   . PHE   A  1  294 ? 32.149  -18.141 -22.537  1.00 56.15  ? 294  PHE   A CG   1 
ATOM   4442  C  CD1  . PHE   A  1  294 ? 32.704  -18.042 -23.803  1.00 55.41  ? 294  PHE   A CD1  1 
ATOM   4443  C  CD2  . PHE   A  1  294 ? 32.647  -17.332 -21.528  1.00 59.01  ? 294  PHE   A CD2  1 
ATOM   4444  C  CE1  . PHE   A  1  294 ? 33.738  -17.158 -24.057  1.00 57.17  ? 294  PHE   A CE1  1 
ATOM   4445  C  CE2  . PHE   A  1  294 ? 33.680  -16.444 -21.776  1.00 60.17  ? 294  PHE   A CE2  1 
ATOM   4446  C  CZ   . PHE   A  1  294 ? 34.226  -16.357 -23.043  1.00 59.02  ? 294  PHE   A CZ   1 
ATOM   4447  H  H    . PHE   A  1  294 ? 31.513  -20.946 -24.120  1.00 64.15  ? 294  PHE   A H    1 
ATOM   4448  H  HA   . PHE   A  1  294 ? 32.120  -20.650 -21.480  1.00 65.53  ? 294  PHE   A HA   1 
ATOM   4449  H  HB2  . PHE   A  1  294 ? 30.375  -19.009 -22.976  1.00 67.10  ? 294  PHE   A HB2  1 
ATOM   4450  H  HB3  . PHE   A  1  294 ? 30.628  -18.861 -21.414  1.00 67.10  ? 294  PHE   A HB3  1 
ATOM   4451  H  HD1  . PHE   A  1  294 ? 32.377  -18.576 -24.490  1.00 66.48  ? 294  PHE   A HD1  1 
ATOM   4452  H  HD2  . PHE   A  1  294 ? 32.283  -17.386 -20.674  1.00 70.79  ? 294  PHE   A HD2  1 
ATOM   4453  H  HE1  . PHE   A  1  294 ? 34.104  -17.104 -24.911  1.00 68.58  ? 294  PHE   A HE1  1 
ATOM   4454  H  HE2  . PHE   A  1  294 ? 34.007  -15.907 -21.090  1.00 72.19  ? 294  PHE   A HE2  1 
ATOM   4455  H  HZ   . PHE   A  1  294 ? 34.920  -15.761 -23.212  1.00 70.81  ? 294  PHE   A HZ   1 
ATOM   4456  N  N    . ILE   A  1  295 ? 30.200  -21.947 -20.652  1.00 53.45  ? 295  ILE   A N    1 
ATOM   4457  C  CA   . ILE   A  1  295 ? 29.166  -22.888 -20.234  1.00 54.01  ? 295  ILE   A CA   1 
ATOM   4458  C  C    . ILE   A  1  295 ? 28.560  -22.391 -18.930  1.00 55.69  ? 295  ILE   A C    1 
ATOM   4459  O  O    . ILE   A  1  295 ? 29.290  -22.046 -17.994  1.00 59.89  ? 295  ILE   A O    1 
ATOM   4460  C  CB   . ILE   A  1  295 ? 29.726  -24.314 -20.060  1.00 54.59  ? 295  ILE   A CB   1 
ATOM   4461  C  CG1  . ILE   A  1  295 ? 30.428  -24.770 -21.343  1.00 57.93  ? 295  ILE   A CG1  1 
ATOM   4462  C  CG2  . ILE   A  1  295 ? 28.605  -25.281 -19.698  1.00 50.38  ? 295  ILE   A CG2  1 
ATOM   4463  C  CD1  . ILE   A  1  295 ? 31.215  -26.055 -21.193  1.00 58.74  ? 295  ILE   A CD1  1 
ATOM   4464  H  H    . ILE   A  1  295 ? 30.743  -21.733 -20.020  1.00 64.12  ? 295  ILE   A H    1 
ATOM   4465  H  HA   . ILE   A  1  295 ? 28.467  -22.913 -20.906  1.00 64.80  ? 295  ILE   A HA   1 
ATOM   4466  H  HB   . ILE   A  1  295 ? 30.374  -24.304 -19.339  1.00 65.49  ? 295  ILE   A HB   1 
ATOM   4467  H  HG12 . ILE   A  1  295 ? 29.759  -24.913 -22.030  1.00 69.49  ? 295  ILE   A HG12 1 
ATOM   4468  H  HG13 . ILE   A  1  295 ? 31.047  -24.077 -21.621  1.00 69.49  ? 295  ILE   A HG13 1 
ATOM   4469  H  HG21 . ILE   A  1  295 ? 28.972  -26.176 -19.622  1.00 60.44  ? 295  ILE   A HG21 1 
ATOM   4470  H  HG22 . ILE   A  1  295 ? 28.216  -25.010 -18.851  1.00 60.44  ? 295  ILE   A HG22 1 
ATOM   4471  H  HG23 . ILE   A  1  295 ? 27.930  -25.257 -20.394  1.00 60.44  ? 295  ILE   A HG23 1 
ATOM   4472  H  HD11 . ILE   A  1  295 ? 31.655  -26.256 -22.034  1.00 70.47  ? 295  ILE   A HD11 1 
ATOM   4473  H  HD12 . ILE   A  1  295 ? 31.876  -25.941 -20.493  1.00 70.47  ? 295  ILE   A HD12 1 
ATOM   4474  H  HD13 . ILE   A  1  295 ? 30.605  -26.773 -20.960  1.00 70.47  ? 295  ILE   A HD13 1 
ATOM   4475  N  N    . GLY   A  1  296 ? 27.233  -22.363 -18.868  1.00 56.76  ? 296  GLY   A N    1 
ATOM   4476  C  CA   . GLY   A  1  296 ? 26.517  -21.876 -17.700  1.00 56.05  ? 296  GLY   A CA   1 
ATOM   4477  C  C    . GLY   A  1  296 ? 25.929  -23.013 -16.882  1.00 58.97  ? 296  GLY   A C    1 
ATOM   4478  O  O    . GLY   A  1  296 ? 25.366  -23.962 -17.429  1.00 59.97  ? 296  GLY   A O    1 
ATOM   4479  H  H    . GLY   A  1  296 ? 26.717  -22.626 -19.504  1.00 68.09  ? 296  GLY   A H    1 
ATOM   4480  H  HA2  . GLY   A  1  296 ? 27.125  -21.374 -17.135  1.00 67.25  ? 296  GLY   A HA2  1 
ATOM   4481  H  HA3  . GLY   A  1  296 ? 25.795  -21.294 -17.982  1.00 67.25  ? 296  GLY   A HA3  1 
ATOM   4482  N  N    . ALA   A  1  297 ? 26.067  -22.899 -15.562  1.00 57.88  ? 297  ALA   A N    1 
ATOM   4483  C  CA   . ALA   A  1  297 ? 25.490  -23.843 -14.603  1.00 53.68  ? 297  ALA   A CA   1 
ATOM   4484  C  C    . ALA   A  1  297 ? 24.761  -23.019 -13.550  1.00 56.44  ? 297  ALA   A C    1 
ATOM   4485  O  O    . ALA   A  1  297 ? 25.263  -22.830 -12.434  1.00 61.03  ? 297  ALA   A O    1 
ATOM   4486  C  CB   . ALA   A  1  297 ? 26.565  -24.732 -13.978  1.00 53.08  ? 297  ALA   A CB   1 
ATOM   4487  H  H    . ALA   A  1  297 ? 26.505  -22.263 -15.185  1.00 69.43  ? 297  ALA   A H    1 
ATOM   4488  H  HA   . ALA   A  1  297 ? 24.854  -24.425 -15.048  1.00 64.39  ? 297  ALA   A HA   1 
ATOM   4489  H  HB1  . ALA   A  1  297 ? 26.147  -25.334 -13.343  1.00 63.67  ? 297  ALA   A HB1  1 
ATOM   4490  H  HB2  . ALA   A  1  297 ? 27.001  -25.241 -14.679  1.00 63.67  ? 297  ALA   A HB2  1 
ATOM   4491  H  HB3  . ALA   A  1  297 ? 27.214  -24.171 -13.524  1.00 63.67  ? 297  ALA   A HB3  1 
ATOM   4492  N  N    . PRO   A  1  298 ? 23.564  -22.515 -13.870  1.00 56.12  ? 298  PRO   A N    1 
ATOM   4493  C  CA   . PRO   A  1  298 ? 22.937  -21.498 -13.008  1.00 55.58  ? 298  PRO   A CA   1 
ATOM   4494  C  C    . PRO   A  1  298 ? 22.530  -22.002 -11.632  1.00 55.15  ? 298  PRO   A C    1 
ATOM   4495  O  O    . PRO   A  1  298 ? 22.157  -21.179 -10.787  1.00 54.54  ? 298  PRO   A O    1 
ATOM   4496  C  CB   . PRO   A  1  298 ? 21.705  -21.058 -13.817  1.00 57.33  ? 298  PRO   A CB   1 
ATOM   4497  C  CG   . PRO   A  1  298 ? 21.915  -21.595 -15.207  1.00 57.25  ? 298  PRO   A CG   1 
ATOM   4498  C  CD   . PRO   A  1  298 ? 22.728  -22.833 -15.039  1.00 55.20  ? 298  PRO   A CD   1 
ATOM   4499  H  HA   . PRO   A  1  298 ? 23.542  -20.747 -12.903  1.00 66.68  ? 298  PRO   A HA   1 
ATOM   4500  H  HB2  . PRO   A  1  298 ? 20.903  -21.432 -13.420  1.00 68.77  ? 298  PRO   A HB2  1 
ATOM   4501  H  HB3  . PRO   A  1  298 ? 21.649  -20.089 -13.827  1.00 68.77  ? 298  PRO   A HB3  1 
ATOM   4502  H  HG2  . PRO   A  1  298 ? 21.058  -21.799 -15.613  1.00 68.68  ? 298  PRO   A HG2  1 
ATOM   4503  H  HG3  . PRO   A  1  298 ? 22.390  -20.942 -15.743  1.00 68.68  ? 298  PRO   A HG3  1 
ATOM   4504  H  HD2  . PRO   A  1  298 ? 22.161  -23.600 -14.863  1.00 66.22  ? 298  PRO   A HD2  1 
ATOM   4505  H  HD3  . PRO   A  1  298 ? 23.276  -22.999 -15.823  1.00 66.22  ? 298  PRO   A HD3  1 
ATOM   4506  N  N    . LEU   A  1  299 ? 22.582  -23.308 -11.375  1.00 55.81  ? 299  LEU   A N    1 
ATOM   4507  C  CA   . LEU   A  1  299 ? 22.199  -23.862 -10.083  1.00 56.90  ? 299  LEU   A CA   1 
ATOM   4508  C  C    . LEU   A  1  299 ? 23.399  -24.351 -9.281   1.00 56.24  ? 299  LEU   A C    1 
ATOM   4509  O  O    . LEU   A  1  299 ? 23.219  -24.975 -8.230   1.00 56.21  ? 299  LEU   A O    1 
ATOM   4510  C  CB   . LEU   A  1  299 ? 21.197  -25.002 -10.279  1.00 59.13  ? 299  LEU   A CB   1 
ATOM   4511  C  CG   . LEU   A  1  299 ? 20.024  -24.699 -11.216  1.00 60.41  ? 299  LEU   A CG   1 
ATOM   4512  C  CD1  . LEU   A  1  299 ? 19.069  -25.882 -11.262  1.00 59.80  ? 299  LEU   A CD1  1 
ATOM   4513  C  CD2  . LEU   A  1  299 ? 19.292  -23.430 -10.801  1.00 60.47  ? 299  LEU   A CD2  1 
ATOM   4514  H  H    . LEU   A  1  299 ? 22.841  -23.900 -11.943  1.00 66.95  ? 299  LEU   A H    1 
ATOM   4515  H  HA   . LEU   A  1  299 ? 21.763  -23.168 -9.565   1.00 68.27  ? 299  LEU   A HA   1 
ATOM   4516  H  HB2  . LEU   A  1  299 ? 21.671  -25.764 -10.646  1.00 70.94  ? 299  LEU   A HB2  1 
ATOM   4517  H  HB3  . LEU   A  1  299 ? 20.823  -25.230 -9.413   1.00 70.94  ? 299  LEU   A HB3  1 
ATOM   4518  H  HG   . LEU   A  1  299 ? 20.372  -24.549 -12.110  1.00 72.48  ? 299  LEU   A HG   1 
ATOM   4519  H  HD11 . LEU   A  1  299 ? 18.330  -25.669 -11.852  1.00 71.74  ? 299  LEU   A HD11 1 
ATOM   4520  H  HD12 . LEU   A  1  299 ? 19.545  -26.659 -11.595  1.00 71.74  ? 299  LEU   A HD12 1 
ATOM   4521  H  HD13 . LEU   A  1  299 ? 18.739  -26.056 -10.367  1.00 71.74  ? 299  LEU   A HD13 1 
ATOM   4522  H  HD21 . LEU   A  1  299 ? 18.518  -23.311 -11.373  1.00 72.54  ? 299  LEU   A HD21 1 
ATOM   4523  H  HD22 . LEU   A  1  299 ? 19.011  -23.516 -9.877   1.00 72.54  ? 299  LEU   A HD22 1 
ATOM   4524  H  HD23 . LEU   A  1  299 ? 19.893  -22.674 -10.895  1.00 72.54  ? 299  LEU   A HD23 1 
ATOM   4525  N  N    . PHE   A  1  300 ? 24.615  -24.081 -9.750   1.00 56.16  ? 300  PHE   A N    1 
ATOM   4526  C  CA   . PHE   A  1  300 ? 25.810  -24.487 -9.024   1.00 59.58  ? 300  PHE   A CA   1 
ATOM   4527  C  C    . PHE   A  1  300 ? 25.842  -23.831 -7.649   1.00 59.34  ? 300  PHE   A C    1 
ATOM   4528  O  O    . PHE   A  1  300 ? 25.594  -22.629 -7.514   1.00 60.37  ? 300  PHE   A O    1 
ATOM   4529  C  CB   . PHE   A  1  300 ? 27.055  -24.112 -9.830   1.00 56.69  ? 300  PHE   A CB   1 
ATOM   4530  C  CG   . PHE   A  1  300 ? 28.349  -24.446 -9.145   1.00 54.28  ? 300  PHE   A CG   1 
ATOM   4531  C  CD1  . PHE   A  1  300 ? 28.948  -23.537 -8.288   1.00 57.65  ? 300  PHE   A CD1  1 
ATOM   4532  C  CD2  . PHE   A  1  300 ? 28.973  -25.662 -9.367   1.00 56.95  ? 300  PHE   A CD2  1 
ATOM   4533  C  CE1  . PHE   A  1  300 ? 30.141  -23.837 -7.656   1.00 58.00  ? 300  PHE   A CE1  1 
ATOM   4534  C  CE2  . PHE   A  1  300 ? 30.167  -25.969 -8.740   1.00 56.48  ? 300  PHE   A CE2  1 
ATOM   4535  C  CZ   . PHE   A  1  300 ? 30.752  -25.054 -7.882   1.00 57.50  ? 300  PHE   A CZ   1 
ATOM   4536  H  H    . PHE   A  1  300 ? 24.773  -23.664 -10.486  1.00 67.37  ? 300  PHE   A H    1 
ATOM   4537  H  HA   . PHE   A  1  300 ? 25.808  -25.449 -8.898   1.00 71.48  ? 300  PHE   A HA   1 
ATOM   4538  H  HB2  . PHE   A  1  300 ? 27.035  -24.591 -10.673  1.00 68.01  ? 300  PHE   A HB2  1 
ATOM   4539  H  HB3  . PHE   A  1  300 ? 27.044  -23.156 -9.991   1.00 68.01  ? 300  PHE   A HB3  1 
ATOM   4540  H  HD1  . PHE   A  1  300 ? 28.541  -22.715 -8.135   1.00 69.16  ? 300  PHE   A HD1  1 
ATOM   4541  H  HD2  . PHE   A  1  300 ? 28.585  -26.280 -9.943   1.00 68.32  ? 300  PHE   A HD2  1 
ATOM   4542  H  HE1  . PHE   A  1  300 ? 30.531  -23.219 -7.080   1.00 69.58  ? 300  PHE   A HE1  1 
ATOM   4543  H  HE2  . PHE   A  1  300 ? 30.577  -26.790 -8.894   1.00 67.75  ? 300  PHE   A HE2  1 
ATOM   4544  H  HZ   . PHE   A  1  300 ? 31.555  -25.258 -7.460   1.00 68.98  ? 300  PHE   A HZ   1 
ATOM   4545  N  N    . MET   A  1  301 ? 26.150  -24.625 -6.628   1.00 58.47  ? 301  MET   A N    1 
ATOM   4546  C  CA   . MET   A  1  301 ? 26.165  -24.161 -5.249   1.00 62.24  ? 301  MET   A CA   1 
ATOM   4547  C  C    . MET   A  1  301 ? 27.601  -23.959 -4.788   1.00 66.54  ? 301  MET   A C    1 
ATOM   4548  O  O    . MET   A  1  301 ? 28.422  -24.879 -4.871   1.00 65.49  ? 301  MET   A O    1 
ATOM   4549  C  CB   . MET   A  1  301 ? 25.453  -25.156 -4.330   1.00 65.01  ? 301  MET   A CB   1 
ATOM   4550  C  CG   . MET   A  1  301 ? 23.952  -25.238 -4.550   1.00 63.87  ? 301  MET   A CG   1 
ATOM   4551  S  SD   . MET   A  1  301 ? 23.141  -26.394 -3.427   1.00 62.74  ? 301  MET   A SD   1 
ATOM   4552  C  CE   . MET   A  1  301 ? 23.842  -27.952 -3.966   1.00 62.61  ? 301  MET   A CE   1 
ATOM   4553  H  H    . MET   A  1  301 ? 26.359  -25.455 -6.714   1.00 70.14  ? 301  MET   A H    1 
ATOM   4554  H  HA   . MET   A  1  301 ? 25.695  -23.314 -5.198   1.00 74.67  ? 301  MET   A HA   1 
ATOM   4555  H  HB2  . MET   A  1  301 ? 25.823  -26.039 -4.484   1.00 77.99  ? 301  MET   A HB2  1 
ATOM   4556  H  HB3  . MET   A  1  301 ? 25.602  -24.889 -3.409   1.00 77.99  ? 301  MET   A HB3  1 
ATOM   4557  H  HG2  . MET   A  1  301 ? 23.563  -24.361 -4.409   1.00 76.63  ? 301  MET   A HG2  1 
ATOM   4558  H  HG3  . MET   A  1  301 ? 23.782  -25.534 -5.459   1.00 76.63  ? 301  MET   A HG3  1 
ATOM   4559  H  HE1  . MET   A  1  301 ? 23.444  -28.672 -3.452   1.00 75.11  ? 301  MET   A HE1  1 
ATOM   4560  H  HE2  . MET   A  1  301 ? 23.651  -28.075 -4.909   1.00 75.11  ? 301  MET   A HE2  1 
ATOM   4561  H  HE3  . MET   A  1  301 ? 24.801  -27.934 -3.823   1.00 75.11  ? 301  MET   A HE3  1 
ATOM   4562  N  N    . ASP   A  1  302 ? 27.897  -22.758 -4.307   1.00 72.22  ? 302  ASP   A N    1 
ATOM   4563  C  CA   . ASP   A  1  302 ? 29.202  -22.428 -3.760   1.00 73.28  ? 302  ASP   A CA   1 
ATOM   4564  C  C    . ASP   A  1  302 ? 29.208  -22.662 -2.253   1.00 68.17  ? 302  ASP   A C    1 
ATOM   4565  O  O    . ASP   A  1  302 ? 28.160  -22.778 -1.614   1.00 67.30  ? 302  ASP   A O    1 
ATOM   4566  C  CB   . ASP   A  1  302 ? 29.557  -20.972 -4.070   1.00 83.74  ? 302  ASP   A CB   1 
ATOM   4567  C  CG   . ASP   A  1  302 ? 30.993  -20.632 -3.722   1.00 96.08  ? 302  ASP   A CG   1 
ATOM   4568  O  OD1  . ASP   A  1  302 ? 31.755  -21.551 -3.355   1.00 101.04 ? 302  ASP   A OD1  1 
ATOM   4569  O  OD2  . ASP   A  1  302 ? 31.359  -19.441 -3.814   1.00 100.67 ? 302  ASP   A OD2  1 
ATOM   4570  H  H    . ASP   A  1  302 ? 27.342  -22.101 -4.286   1.00 86.64  ? 302  ASP   A H    1 
ATOM   4571  H  HA   . ASP   A  1  302 ? 29.881  -22.993 -4.162   1.00 87.92  ? 302  ASP   A HA   1 
ATOM   4572  H  HB2  . ASP   A  1  302 ? 29.431  -20.811 -5.018   1.00 100.46 ? 302  ASP   A HB2  1 
ATOM   4573  H  HB3  . ASP   A  1  302 ? 28.977  -20.389 -3.555   1.00 100.46 ? 302  ASP   A HB3  1 
ATOM   4574  N  N    . ARG   A  1  303 ? 30.409  -22.738 -1.690   1.00 70.90  ? 303  ARG   A N    1 
ATOM   4575  C  CA   . ARG   A  1  303 ? 30.594  -22.851 -0.251   1.00 76.28  ? 303  ARG   A CA   1 
ATOM   4576  C  C    . ARG   A  1  303 ? 30.965  -21.485 0.312    1.00 78.92  ? 303  ARG   A C    1 
ATOM   4577  O  O    . ARG   A  1  303 ? 31.789  -20.768 -0.264   1.00 78.44  ? 303  ARG   A O    1 
ATOM   4578  C  CB   . ARG   A  1  303 ? 31.680  -23.878 0.079    1.00 82.87  ? 303  ARG   A CB   1 
ATOM   4579  C  CG   . ARG   A  1  303 ? 31.667  -24.368 1.519    1.00 92.41  ? 303  ARG   A CG   1 
ATOM   4580  C  CD   . ARG   A  1  303 ? 30.531  -25.349 1.787    1.00 96.94  ? 303  ARG   A CD   1 
ATOM   4581  N  NE   . ARG   A  1  303 ? 30.676  -26.599 1.043    1.00 95.76  ? 303  ARG   A NE   1 
ATOM   4582  C  CZ   . ARG   A  1  303 ? 29.959  -27.696 1.275    1.00 90.74  ? 303  ARG   A CZ   1 
ATOM   4583  N  NH1  . ARG   A  1  303 ? 29.044  -27.708 2.236    1.00 90.15  ? 303  ARG   A NH1  1 
ATOM   4584  N  NH2  . ARG   A  1  303 ? 30.159  -28.786 0.547    1.00 87.67  ? 303  ARG   A NH2  1 
ATOM   4585  H  H    . ARG   A  1  303 ? 31.146  -22.725 -2.132   1.00 85.06  ? 303  ARG   A H    1 
ATOM   4586  H  HA   . ARG   A  1  303 ? 29.773  -23.148 0.171    1.00 91.52  ? 303  ARG   A HA   1 
ATOM   4587  H  HB2  . ARG   A  1  303 ? 31.559  -24.650 -0.495   1.00 99.43  ? 303  ARG   A HB2  1 
ATOM   4588  H  HB3  . ARG   A  1  303 ? 32.547  -23.474 -0.086   1.00 99.43  ? 303  ARG   A HB3  1 
ATOM   4589  H  HG2  . ARG   A  1  303 ? 32.505  -24.819 1.709    1.00 110.88 ? 303  ARG   A HG2  1 
ATOM   4590  H  HG3  . ARG   A  1  303 ? 31.556  -23.610 2.113    1.00 110.88 ? 303  ARG   A HG3  1 
ATOM   4591  H  HD2  . ARG   A  1  303 ? 30.514  -25.564 2.733    1.00 116.31 ? 303  ARG   A HD2  1 
ATOM   4592  H  HD3  . ARG   A  1  303 ? 29.692  -24.940 1.524    1.00 116.31 ? 303  ARG   A HD3  1 
ATOM   4593  H  HE   . ARG   A  1  303 ? 31.263  -26.628 0.416    1.00 114.89 ? 303  ARG   A HE   1 
ATOM   4594  H  HH11 . ARG   A  1  303 ? 28.913  -27.005 2.714    1.00 108.16 ? 303  ARG   A HH11 1 
ATOM   4595  H  HH12 . ARG   A  1  303 ? 28.583  -28.420 2.382    1.00 108.16 ? 303  ARG   A HH12 1 
ATOM   4596  H  HH21 . ARG   A  1  303 ? 30.753  -28.785 -0.075   1.00 105.19 ? 303  ARG   A HH21 1 
ATOM   4597  H  HH22 . ARG   A  1  303 ? 29.695  -29.494 0.697    1.00 105.19 ? 303  ARG   A HH22 1 
ATOM   4598  N  N    . GLY   A  1  304 ? 30.345  -21.123 1.437    1.00 84.04  ? 304  GLY   A N    1 
ATOM   4599  C  CA   . GLY   A  1  304 ? 30.535  -19.820 2.032    1.00 85.84  ? 304  GLY   A CA   1 
ATOM   4600  C  C    . GLY   A  1  304 ? 31.504  -19.840 3.207    1.00 85.77  ? 304  GLY   A C    1 
ATOM   4601  O  O    . GLY   A  1  304 ? 31.953  -20.886 3.667    1.00 83.31  ? 304  GLY   A O    1 
ATOM   4602  H  H    . GLY   A  1  304 ? 29.804  -21.629 1.873    1.00 100.82 ? 304  GLY   A H    1 
ATOM   4603  H  HA2  . GLY   A  1  304 ? 30.882  -19.211 1.362    1.00 102.98 ? 304  GLY   A HA2  1 
ATOM   4604  H  HA3  . GLY   A  1  304 ? 29.681  -19.487 2.349    1.00 102.98 ? 304  GLY   A HA3  1 
ATOM   4605  N  N    . SER   A  1  305 ? 31.821  -18.634 3.689    1.00 86.70  ? 305  SER   A N    1 
ATOM   4606  C  CA   . SER   A  1  305 ? 32.718  -18.501 4.832    1.00 85.34  ? 305  SER   A CA   1 
ATOM   4607  C  C    . SER   A  1  305 ? 32.236  -19.336 6.010    1.00 83.86  ? 305  SER   A C    1 
ATOM   4608  O  O    . SER   A  1  305 ? 33.042  -19.947 6.723    1.00 83.26  ? 305  SER   A O    1 
ATOM   4609  C  CB   . SER   A  1  305 ? 32.835  -17.029 5.233    1.00 88.56  ? 305  SER   A CB   1 
ATOM   4610  O  OG   . SER   A  1  305 ? 33.506  -16.887 6.473    1.00 93.64  ? 305  SER   A OG   1 
ATOM   4611  H  H    . SER   A  1  305 ? 31.532  -17.888 3.374    1.00 104.02 ? 305  SER   A H    1 
ATOM   4612  H  HA   . SER   A  1  305 ? 33.600  -18.816 4.580    1.00 102.39 ? 305  SER   A HA   1 
ATOM   4613  H  HB2  . SER   A  1  305 ? 33.335  -16.556 4.549    1.00 106.26 ? 305  SER   A HB2  1 
ATOM   4614  H  HB3  . SER   A  1  305 ? 31.945  -16.653 5.312    1.00 106.26 ? 305  SER   A HB3  1 
ATOM   4615  H  HG   . SER   A  1  305 ? 33.008  -17.141 7.100    1.00 112.35 ? 305  SER   A HG   1 
ATOM   4616  N  N    . ASP   A  1  306 ? 30.923  -19.372 6.233    1.00 83.73  ? 306  ASP   A N    1 
ATOM   4617  C  CA   . ASP   A  1  306 ? 30.342  -20.206 7.277    1.00 81.91  ? 306  ASP   A CA   1 
ATOM   4618  C  C    . ASP   A  1  306 ? 30.322  -21.683 6.910    1.00 77.09  ? 306  ASP   A C    1 
ATOM   4619  O  O    . ASP   A  1  306 ? 29.915  -22.504 7.740    1.00 74.03  ? 306  ASP   A O    1 
ATOM   4620  C  CB   . ASP   A  1  306 ? 28.920  -19.733 7.585    1.00 85.18  ? 306  ASP   A CB   1 
ATOM   4621  C  CG   . ASP   A  1  306 ? 28.058  -19.637 6.345    1.00 86.89  ? 306  ASP   A CG   1 
ATOM   4622  O  OD1  . ASP   A  1  306 ? 28.523  -20.059 5.265    1.00 86.61  ? 306  ASP   A OD1  1 
ATOM   4623  O  OD2  . ASP   A  1  306 ? 26.921  -19.133 6.449    1.00 89.02  ? 306  ASP   A OD2  1 
ATOM   4624  H  H    . ASP   A  1  306 ? 30.344  -18.918 5.787    1.00 100.45 ? 306  ASP   A H    1 
ATOM   4625  H  HA   . ASP   A  1  306 ? 30.873  -20.109 8.084    1.00 98.27  ? 306  ASP   A HA   1 
ATOM   4626  H  HB2  . ASP   A  1  306 ? 28.502  -20.361 8.194    1.00 102.19 ? 306  ASP   A HB2  1 
ATOM   4627  H  HB3  . ASP   A  1  306 ? 28.960  -18.853 7.992    1.00 102.19 ? 306  ASP   A HB3  1 
ATOM   4628  N  N    . GLY   A  1  307 ? 30.750  -22.041 5.702    1.00 75.26  ? 307  GLY   A N    1 
ATOM   4629  C  CA   . GLY   A  1  307 ? 30.715  -23.418 5.264    1.00 75.81  ? 307  GLY   A CA   1 
ATOM   4630  C  C    . GLY   A  1  307 ? 29.375  -23.884 4.748    1.00 77.24  ? 307  GLY   A C    1 
ATOM   4631  O  O    . GLY   A  1  307 ? 29.185  -25.092 4.568    1.00 78.02  ? 307  GLY   A O    1 
ATOM   4632  H  H    . GLY   A  1  307 ? 31.068  -21.495 5.118    1.00 90.29  ? 307  GLY   A H    1 
ATOM   4633  H  HA2  . GLY   A  1  307 ? 31.363  -23.534 4.551    1.00 90.95  ? 307  GLY   A HA2  1 
ATOM   4634  H  HA3  . GLY   A  1  307 ? 30.960  -23.988 6.009    1.00 90.95  ? 307  GLY   A HA3  1 
ATOM   4635  N  N    . LYS   A  1  308 ? 28.439  -22.971 4.506    1.00 78.31  ? 308  LYS   A N    1 
ATOM   4636  C  CA   . LYS   A  1  308 ? 27.117  -23.331 4.016    1.00 80.55  ? 308  LYS   A CA   1 
ATOM   4637  C  C    . LYS   A  1  308 ? 27.084  -23.299 2.495    1.00 78.26  ? 308  LYS   A C    1 
ATOM   4638  O  O    . LYS   A  1  308 ? 27.637  -22.392 1.866    1.00 77.55  ? 308  LYS   A O    1 
ATOM   4639  C  CB   . LYS   A  1  308 ? 26.054  -22.380 4.569    1.00 88.84  ? 308  LYS   A CB   1 
ATOM   4640  C  CG   . LYS   A  1  308 ? 25.362  -22.884 5.822    1.00 98.27  ? 308  LYS   A CG   1 
ATOM   4641  C  CD   . LYS   A  1  308 ? 24.160  -22.023 6.172    1.00 104.23 ? 308  LYS   A CD   1 
ATOM   4642  C  CE   . LYS   A  1  308 ? 23.563  -22.418 7.512    1.00 109.10 ? 308  LYS   A CE   1 
ATOM   4643  N  NZ   . LYS   A  1  308 ? 23.276  -23.875 7.601    1.00 110.82 ? 308  LYS   A NZ   1 
ATOM   4644  H  H    . LYS   A  1  308 ? 28.549  -22.125 4.620    1.00 93.95  ? 308  LYS   A H    1 
ATOM   4645  H  HA   . LYS   A  1  308 ? 26.908  -24.231 4.309    1.00 96.64  ? 308  LYS   A HA   1 
ATOM   4646  H  HB2  . LYS   A  1  308 ? 26.477  -21.534 4.787    1.00 106.59 ? 308  LYS   A HB2  1 
ATOM   4647  H  HB3  . LYS   A  1  308 ? 25.374  -22.246 3.891    1.00 106.59 ? 308  LYS   A HB3  1 
ATOM   4648  H  HG2  . LYS   A  1  308 ? 25.056  -23.793 5.678    1.00 117.91 ? 308  LYS   A HG2  1 
ATOM   4649  H  HG3  . LYS   A  1  308 ? 25.984  -22.857 6.566    1.00 117.91 ? 308  LYS   A HG3  1 
ATOM   4650  H  HD2  . LYS   A  1  308 ? 24.433  -21.094 6.223    1.00 125.05 ? 308  LYS   A HD2  1 
ATOM   4651  H  HD3  . LYS   A  1  308 ? 23.478  -22.132 5.491    1.00 125.05 ? 308  LYS   A HD3  1 
ATOM   4652  H  HE2  . LYS   A  1  308 ? 24.189  -22.191 8.217    1.00 130.91 ? 308  LYS   A HE2  1 
ATOM   4653  H  HE3  . LYS   A  1  308 ? 22.729  -21.939 7.641    1.00 130.91 ? 308  LYS   A HE3  1 
ATOM   4654  H  HZ1  . LYS   A  1  308 ? 22.754  -24.040 8.302    1.00 132.96 ? 308  LYS   A HZ1  1 
ATOM   4655  H  HZ2  . LYS   A  1  308 ? 22.864  -24.150 6.862    1.00 132.96 ? 308  LYS   A HZ2  1 
ATOM   4656  H  HZ3  . LYS   A  1  308 ? 24.036  -24.330 7.694    1.00 132.96 ? 308  LYS   A HZ3  1 
ATOM   4657  N  N    . LEU   A  1  309 ? 26.432  -24.298 1.908    1.00 77.44  ? 309  LEU   A N    1 
ATOM   4658  C  CA   . LEU   A  1  309 ? 26.167  -24.268 0.479    1.00 72.67  ? 309  LEU   A CA   1 
ATOM   4659  C  C    . LEU   A  1  309 ? 25.177  -23.156 0.160    1.00 66.05  ? 309  LEU   A C    1 
ATOM   4660  O  O    . LEU   A  1  309 ? 24.177  -22.973 0.859    1.00 65.44  ? 309  LEU   A O    1 
ATOM   4661  C  CB   . LEU   A  1  309 ? 25.611  -25.609 0.005    1.00 71.62  ? 309  LEU   A CB   1 
ATOM   4662  C  CG   . LEU   A  1  309 ? 26.602  -26.758 -0.185   1.00 70.87  ? 309  LEU   A CG   1 
ATOM   4663  C  CD1  . LEU   A  1  309 ? 25.846  -28.045 -0.479   1.00 69.40  ? 309  LEU   A CD1  1 
ATOM   4664  C  CD2  . LEU   A  1  309 ? 27.588  -26.457 -1.302   1.00 69.72  ? 309  LEU   A CD2  1 
ATOM   4665  H  H    . LEU   A  1  309 ? 26.137  -24.997 2.313    1.00 92.90  ? 309  LEU   A H    1 
ATOM   4666  H  HA   . LEU   A  1  309 ? 26.994  -24.103 -0.001   1.00 87.18  ? 309  LEU   A HA   1 
ATOM   4667  H  HB2  . LEU   A  1  309 ? 24.958  -25.907 0.657    1.00 85.92  ? 309  LEU   A HB2  1 
ATOM   4668  H  HB3  . LEU   A  1  309 ? 25.181  -25.465 -0.853   1.00 85.92  ? 309  LEU   A HB3  1 
ATOM   4669  H  HG   . LEU   A  1  309 ? 27.114  -26.871 0.631    1.00 85.02  ? 309  LEU   A HG   1 
ATOM   4670  H  HD11 . LEU   A  1  309 ? 26.484  -28.764 -0.607   1.00 83.26  ? 309  LEU   A HD11 1 
ATOM   4671  H  HD12 . LEU   A  1  309 ? 25.265  -28.248 0.271    1.00 83.26  ? 309  LEU   A HD12 1 
ATOM   4672  H  HD13 . LEU   A  1  309 ? 25.318  -27.924 -1.283   1.00 83.26  ? 309  LEU   A HD13 1 
ATOM   4673  H  HD21 . LEU   A  1  309 ? 28.178  -27.219 -1.417   1.00 83.64  ? 309  LEU   A HD21 1 
ATOM   4674  H  HD22 . LEU   A  1  309 ? 27.096  -26.293 -2.122   1.00 83.64  ? 309  LEU   A HD22 1 
ATOM   4675  H  HD23 . LEU   A  1  309 ? 28.105  -25.671 -1.064   1.00 83.64  ? 309  LEU   A HD23 1 
ATOM   4676  N  N    . GLN   A  1  310 ? 25.464  -22.408 -0.901   1.00 63.41  ? 310  GLN   A N    1 
ATOM   4677  C  CA   . GLN   A  1  310 ? 24.581  -21.344 -1.362   1.00 65.11  ? 310  GLN   A CA   1 
ATOM   4678  C  C    . GLN   A  1  310 ? 24.515  -21.400 -2.878   1.00 60.38  ? 310  GLN   A C    1 
ATOM   4679  O  O    . GLN   A  1  310 ? 25.547  -21.319 -3.551   1.00 58.26  ? 310  GLN   A O    1 
ATOM   4680  C  CB   . GLN   A  1  310 ? 25.060  -19.969 -0.883   1.00 73.62  ? 310  GLN   A CB   1 
ATOM   4681  C  CG   . GLN   A  1  310 ? 26.567  -19.758 -0.937   1.00 83.29  ? 310  GLN   A CG   1 
ATOM   4682  C  CD   . GLN   A  1  310 ? 26.995  -18.465 -0.267   1.00 91.99  ? 310  GLN   A CD   1 
ATOM   4683  O  OE1  . GLN   A  1  310 ? 26.216  -17.840 0.454    1.00 94.49  ? 310  GLN   A OE1  1 
ATOM   4684  N  NE2  . GLN   A  1  310 ? 28.237  -18.059 -0.501   1.00 95.77  ? 310  GLN   A NE2  1 
ATOM   4685  H  H    . GLN   A  1  310 ? 26.175  -22.498 -1.376   1.00 76.07  ? 310  GLN   A H    1 
ATOM   4686  H  HA   . GLN   A  1  310 ? 23.688  -21.487 -1.011   1.00 78.11  ? 310  GLN   A HA   1 
ATOM   4687  H  HB2  . GLN   A  1  310 ? 24.651  -19.289 -1.441   1.00 88.32  ? 310  GLN   A HB2  1 
ATOM   4688  H  HB3  . GLN   A  1  310 ? 24.783  -19.851 0.039    1.00 88.32  ? 310  GLN   A HB3  1 
ATOM   4689  H  HG2  . GLN   A  1  310 ? 27.007  -20.494 -0.483   1.00 99.93  ? 310  GLN   A HG2  1 
ATOM   4690  H  HG3  . GLN   A  1  310 ? 26.849  -19.724 -1.865   1.00 99.93  ? 310  GLN   A HG3  1 
ATOM   4691  H  HE21 . GLN   A  1  310 ? 28.752  -18.522 -1.011   1.00 114.90 ? 310  GLN   A HE21 1 
ATOM   4692  H  HE22 . GLN   A  1  310 ? 28.527  -17.332 -0.144   1.00 114.90 ? 310  GLN   A HE22 1 
ATOM   4693  N  N    . GLU   A  1  311 ? 23.304  -21.551 -3.407   1.00 58.19  ? 311  GLU   A N    1 
ATOM   4694  C  CA   . GLU   A  1  311 ? 23.102  -21.603 -4.849   1.00 57.29  ? 311  GLU   A CA   1 
ATOM   4695  C  C    . GLU   A  1  311 ? 23.323  -20.218 -5.435   1.00 57.43  ? 311  GLU   A C    1 
ATOM   4696  O  O    . GLU   A  1  311 ? 22.551  -19.292 -5.167   1.00 56.28  ? 311  GLU   A O    1 
ATOM   4697  C  CB   . GLU   A  1  311 ? 21.702  -22.112 -5.169   1.00 59.53  ? 311  GLU   A CB   1 
ATOM   4698  C  CG   . GLU   A  1  311 ? 21.405  -22.252 -6.654   1.00 63.07  ? 311  GLU   A CG   1 
ATOM   4699  C  CD   . GLU   A  1  311 ? 19.986  -22.722 -6.919   1.00 68.12  ? 311  GLU   A CD   1 
ATOM   4700  O  OE1  . GLU   A  1  311 ? 19.604  -23.794 -6.401   1.00 71.79  ? 311  GLU   A OE1  1 
ATOM   4701  O  OE2  . GLU   A  1  311 ? 19.248  -22.013 -7.634   1.00 69.75  ? 311  GLU   A OE2  1 
ATOM   4702  H  H    . GLU   A  1  311 ? 22.580  -21.625 -2.949   1.00 69.81  ? 311  GLU   A H    1 
ATOM   4703  H  HA   . GLU   A  1  311 ? 23.744  -22.216 -5.241   1.00 68.73  ? 311  GLU   A HA   1 
ATOM   4704  H  HB2  . GLU   A  1  311 ? 21.591  -22.986 -4.764   1.00 71.42  ? 311  GLU   A HB2  1 
ATOM   4705  H  HB3  . GLU   A  1  311 ? 21.056  -21.490 -4.799   1.00 71.42  ? 311  GLU   A HB3  1 
ATOM   4706  H  HG2  . GLU   A  1  311 ? 21.522  -21.391 -7.084   1.00 75.67  ? 311  GLU   A HG2  1 
ATOM   4707  H  HG3  . GLU   A  1  311 ? 22.014  -22.901 -7.040   1.00 75.67  ? 311  GLU   A HG3  1 
ATOM   4708  N  N    . VAL   A  1  312 ? 24.374  -20.083 -6.246   1.00 57.02  ? 312  VAL   A N    1 
ATOM   4709  C  CA   . VAL   A  1  312 ? 24.709  -18.807 -6.861   1.00 57.80  ? 312  VAL   A CA   1 
ATOM   4710  C  C    . VAL   A  1  312 ? 24.945  -18.907 -8.370   1.00 58.55  ? 312  VAL   A C    1 
ATOM   4711  O  O    . VAL   A  1  312 ? 24.962  -17.880 -9.048   1.00 59.17  ? 312  VAL   A O    1 
ATOM   4712  C  CB   . VAL   A  1  312 ? 25.945  -18.181 -6.180   1.00 61.75  ? 312  VAL   A CB   1 
ATOM   4713  C  CG1  . VAL   A  1  312 ? 25.656  -17.895 -4.721   1.00 63.05  ? 312  VAL   A CG1  1 
ATOM   4714  C  CG2  . VAL   A  1  312 ? 27.160  -19.096 -6.325   1.00 61.79  ? 312  VAL   A CG2  1 
ATOM   4715  H  H    . VAL   A  1  312 ? 24.909  -20.723 -6.454   1.00 68.41  ? 312  VAL   A H    1 
ATOM   4716  H  HA   . VAL   A  1  312 ? 23.929  -18.242 -6.748   1.00 69.33  ? 312  VAL   A HA   1 
ATOM   4717  H  HB   . VAL   A  1  312 ? 26.153  -17.339 -6.616   1.00 74.09  ? 312  VAL   A HB   1 
ATOM   4718  H  HG11 . VAL   A  1  312 ? 26.446  -17.507 -4.313   1.00 75.65  ? 312  VAL   A HG11 1 
ATOM   4719  H  HG12 . VAL   A  1  312 ? 24.914  -17.273 -4.662   1.00 75.65  ? 312  VAL   A HG12 1 
ATOM   4720  H  HG13 . VAL   A  1  312 ? 25.428  -18.725 -4.275   1.00 75.65  ? 312  VAL   A HG13 1 
ATOM   4721  H  HG21 . VAL   A  1  312 ? 27.922  -18.681 -5.891   1.00 74.13  ? 312  VAL   A HG21 1 
ATOM   4722  H  HG22 . VAL   A  1  312 ? 26.965  -19.949 -5.905   1.00 74.13  ? 312  VAL   A HG22 1 
ATOM   4723  H  HG23 . VAL   A  1  312 ? 27.347  -19.226 -7.268   1.00 74.13  ? 312  VAL   A HG23 1 
ATOM   4724  N  N    . GLY   A  1  313 ? 25.125  -20.110 -8.912   1.00 58.01  ? 313  GLY   A N    1 
ATOM   4725  C  CA   . GLY   A  1  313 ? 25.434  -20.261 -10.323  1.00 57.00  ? 313  GLY   A CA   1 
ATOM   4726  C  C    . GLY   A  1  313 ? 26.924  -20.166 -10.596  1.00 56.98  ? 313  GLY   A C    1 
ATOM   4727  O  O    . GLY   A  1  313 ? 27.705  -19.646 -9.801   1.00 58.54  ? 313  GLY   A O    1 
ATOM   4728  H  H    . GLY   A  1  313 ? 25.072  -20.852 -8.480   1.00 69.59  ? 313  GLY   A H    1 
ATOM   4729  H  HA2  . GLY   A  1  313 ? 25.120  -21.126 -10.630  1.00 68.38  ? 313  GLY   A HA2  1 
ATOM   4730  H  HA3  . GLY   A  1  313 ? 24.984  -19.565 -10.827  1.00 68.38  ? 313  GLY   A HA3  1 
ATOM   4731  N  N    . GLN   A  1  314 ? 27.318  -20.692 -11.752  1.00 58.15  ? 314  GLN   A N    1 
ATOM   4732  C  CA   . GLN   A  1  314 ? 28.724  -20.725 -12.119  1.00 57.78  ? 314  GLN   A CA   1 
ATOM   4733  C  C    . GLN   A  1  314 ? 28.833  -20.819 -13.631  1.00 62.23  ? 314  GLN   A C    1 
ATOM   4734  O  O    . GLN   A  1  314 ? 28.066  -21.543 -14.271  1.00 66.81  ? 314  GLN   A O    1 
ATOM   4735  C  CB   . GLN   A  1  314 ? 29.441  -21.905 -11.456  1.00 57.35  ? 314  GLN   A CB   1 
ATOM   4736  C  CG   . GLN   A  1  314 ? 30.891  -22.068 -11.874  1.00 60.14  ? 314  GLN   A CG   1 
ATOM   4737  C  CD   . GLN   A  1  314 ? 31.580  -23.200 -11.141  1.00 62.19  ? 314  GLN   A CD   1 
ATOM   4738  O  OE1  . GLN   A  1  314 ? 31.628  -24.330 -11.626  1.00 61.93  ? 314  GLN   A OE1  1 
ATOM   4739  N  NE2  . GLN   A  1  314 ? 32.113  -22.904 -9.961   1.00 64.59  ? 314  GLN   A NE2  1 
ATOM   4740  H  H    . GLN   A  1  314 ? 26.790  -21.035 -12.337  1.00 69.77  ? 314  GLN   A H    1 
ATOM   4741  H  HA   . GLN   A  1  314 ? 29.157  -19.905 -11.835  1.00 69.32  ? 314  GLN   A HA   1 
ATOM   4742  H  HB2  . GLN   A  1  314 ? 29.425  -21.777 -10.494  1.00 68.80  ? 314  GLN   A HB2  1 
ATOM   4743  H  HB3  . GLN   A  1  314 ? 28.974  -22.723 -11.689  1.00 68.80  ? 314  GLN   A HB3  1 
ATOM   4744  H  HG2  . GLN   A  1  314 ? 30.928  -22.257 -12.824  1.00 72.14  ? 314  GLN   A HG2  1 
ATOM   4745  H  HG3  . GLN   A  1  314 ? 31.371  -21.247 -11.680  1.00 72.14  ? 314  GLN   A HG3  1 
ATOM   4746  H  HE21 . GLN   A  1  314 ? 32.057  -22.103 -9.652   1.00 77.49  ? 314  GLN   A HE21 1 
ATOM   4747  H  HE22 . GLN   A  1  314 ? 32.515  -23.513 -9.506   1.00 77.49  ? 314  GLN   A HE22 1 
ATOM   4748  N  N    . VAL   A  1  315 ? 29.785  -20.080 -14.190  1.00 61.11  ? 315  VAL   A N    1 
ATOM   4749  C  CA   . VAL   A  1  315 ? 30.090  -20.113 -15.614  1.00 57.98  ? 315  VAL   A CA   1 
ATOM   4750  C  C    . VAL   A  1  315 ? 31.526  -20.585 -15.774  1.00 59.01  ? 315  VAL   A C    1 
ATOM   4751  O  O    . VAL   A  1  315 ? 32.423  -20.106 -15.069  1.00 58.71  ? 315  VAL   A O    1 
ATOM   4752  C  CB   . VAL   A  1  315 ? 29.890  -18.736 -16.274  1.00 59.17  ? 315  VAL   A CB   1 
ATOM   4753  C  CG1  . VAL   A  1  315 ? 30.368  -18.758 -17.722  1.00 58.75  ? 315  VAL   A CG1  1 
ATOM   4754  C  CG2  . VAL   A  1  315 ? 28.430  -18.320 -16.198  1.00 59.43  ? 315  VAL   A CG2  1 
ATOM   4755  H  H    . VAL   A  1  315 ? 30.283  -19.534 -13.750  1.00 73.31  ? 315  VAL   A H    1 
ATOM   4756  H  HA   . VAL   A  1  315 ? 29.503  -20.747 -16.056  1.00 69.56  ? 315  VAL   A HA   1 
ATOM   4757  H  HB   . VAL   A  1  315 ? 30.420  -18.080 -15.794  1.00 70.98  ? 315  VAL   A HB   1 
ATOM   4758  H  HG11 . VAL   A  1  315 ? 30.131  -17.918 -18.146  1.00 70.48  ? 315  VAL   A HG11 1 
ATOM   4759  H  HG12 . VAL   A  1  315 ? 31.331  -18.875 -17.736  1.00 70.48  ? 315  VAL   A HG12 1 
ATOM   4760  H  HG13 . VAL   A  1  315 ? 29.939  -19.495 -18.185  1.00 70.48  ? 315  VAL   A HG13 1 
ATOM   4761  H  HG21 . VAL   A  1  315 ? 28.327  -17.454 -16.624  1.00 71.29  ? 315  VAL   A HG21 1 
ATOM   4762  H  HG22 . VAL   A  1  315 ? 27.889  -18.981 -16.657  1.00 71.29  ? 315  VAL   A HG22 1 
ATOM   4763  H  HG23 . VAL   A  1  315 ? 28.166  -18.264 -15.267  1.00 71.29  ? 315  VAL   A HG23 1 
ATOM   4764  N  N    . SER   A  1  316 ? 31.741  -21.525 -16.689  1.00 58.54  ? 316  SER   A N    1 
ATOM   4765  C  CA   . SER   A  1  316 ? 33.074  -22.012 -17.012  1.00 55.33  ? 316  SER   A CA   1 
ATOM   4766  C  C    . SER   A  1  316 ? 33.549  -21.363 -18.305  1.00 54.88  ? 316  SER   A C    1 
ATOM   4767  O  O    . SER   A  1  316 ? 32.778  -21.218 -19.258  1.00 55.07  ? 316  SER   A O    1 
ATOM   4768  C  CB   . SER   A  1  316 ? 33.086  -23.534 -17.158  1.00 55.44  ? 316  SER   A CB   1 
ATOM   4769  O  OG   . SER   A  1  316 ? 32.988  -23.917 -18.519  1.00 59.55  ? 316  SER   A OG   1 
ATOM   4770  H  H    . SER   A  1  316 ? 31.117  -21.902 -17.144  1.00 70.23  ? 316  SER   A H    1 
ATOM   4771  H  HA   . SER   A  1  316 ? 33.688  -21.778 -16.299  1.00 66.38  ? 316  SER   A HA   1 
ATOM   4772  H  HB2  . SER   A  1  316 ? 33.916  -23.879 -16.793  1.00 66.50  ? 316  SER   A HB2  1 
ATOM   4773  H  HB3  . SER   A  1  316 ? 32.331  -23.903 -16.672  1.00 66.50  ? 316  SER   A HB3  1 
ATOM   4774  H  HG   . SER   A  1  316 ? 33.002  -24.755 -18.583  1.00 71.44  ? 316  SER   A HG   1 
ATOM   4775  N  N    . VAL   A  1  317 ? 34.820  -20.973 -18.330  1.00 56.84  ? 317  VAL   A N    1 
ATOM   4776  C  CA   . VAL   A  1  317 ? 35.427  -20.305 -19.476  1.00 58.86  ? 317  VAL   A CA   1 
ATOM   4777  C  C    . VAL   A  1  317 ? 36.587  -21.174 -19.938  1.00 57.73  ? 317  VAL   A C    1 
ATOM   4778  O  O    . VAL   A  1  317 ? 37.579  -21.329 -19.215  1.00 60.07  ? 317  VAL   A O    1 
ATOM   4779  C  CB   . VAL   A  1  317 ? 35.898  -18.887 -19.130  1.00 58.25  ? 317  VAL   A CB   1 
ATOM   4780  C  CG1  . VAL   A  1  317 ? 36.506  -18.213 -20.350  1.00 60.77  ? 317  VAL   A CG1  1 
ATOM   4781  C  CG2  . VAL   A  1  317 ? 34.740  -18.063 -18.580  1.00 58.15  ? 317  VAL   A CG2  1 
ATOM   4782  H  H    . VAL   A  1  317 ? 35.366  -21.089 -17.675  1.00 68.19  ? 317  VAL   A H    1 
ATOM   4783  H  HA   . VAL   A  1  317 ? 34.781  -20.245 -20.197  1.00 70.62  ? 317  VAL   A HA   1 
ATOM   4784  H  HB   . VAL   A  1  317 ? 36.584  -18.941 -18.445  1.00 69.88  ? 317  VAL   A HB   1 
ATOM   4785  H  HG11 . VAL   A  1  317 ? 36.732  -17.296 -20.125  1.00 72.91  ? 317  VAL   A HG11 1 
ATOM   4786  H  HG12 . VAL   A  1  317 ? 37.306  -18.695 -20.612  1.00 72.91  ? 317  VAL   A HG12 1 
ATOM   4787  H  HG13 . VAL   A  1  317 ? 35.860  -18.226 -21.073  1.00 72.91  ? 317  VAL   A HG13 1 
ATOM   4788  H  HG21 . VAL   A  1  317 ? 35.048  -17.160 -18.407  1.00 69.76  ? 317  VAL   A HG21 1 
ATOM   4789  H  HG22 . VAL   A  1  317 ? 34.024  -18.049 -19.234  1.00 69.76  ? 317  VAL   A HG22 1 
ATOM   4790  H  HG23 . VAL   A  1  317 ? 34.427  -18.469 -17.756  1.00 69.76  ? 317  VAL   A HG23 1 
ATOM   4791  N  N    . SER   A  1  318 ? 36.473  -21.732 -21.142  1.00 58.19  ? 318  SER   A N    1 
ATOM   4792  C  CA   . SER   A  1  318 ? 37.448  -22.682 -21.675  1.00 62.90  ? 318  SER   A CA   1 
ATOM   4793  C  C    . SER   A  1  318 ? 38.106  -22.073 -22.910  1.00 62.41  ? 318  SER   A C    1 
ATOM   4794  O  O    . SER   A  1  318 ? 37.509  -22.044 -23.991  1.00 58.09  ? 318  SER   A O    1 
ATOM   4795  C  CB   . SER   A  1  318 ? 36.780  -24.014 -22.004  1.00 68.03  ? 318  SER   A CB   1 
ATOM   4796  O  OG   . SER   A  1  318 ? 36.096  -24.530 -20.875  1.00 74.76  ? 318  SER   A OG   1 
ATOM   4797  H  H    . SER   A  1  318 ? 35.823  -21.572 -21.681  1.00 69.81  ? 318  SER   A H    1 
ATOM   4798  H  HA   . SER   A  1  318 ? 38.140  -22.829 -21.011  1.00 75.47  ? 318  SER   A HA   1 
ATOM   4799  H  HB2  . SER   A  1  318 ? 36.143  -23.878 -22.723  1.00 81.62  ? 318  SER   A HB2  1 
ATOM   4800  H  HB3  . SER   A  1  318 ? 37.460  -24.649 -22.278  1.00 81.62  ? 318  SER   A HB3  1 
ATOM   4801  H  HG   . SER   A  1  318 ? 35.780  -25.288 -21.053  1.00 89.70  ? 318  SER   A HG   1 
ATOM   4802  N  N    . LEU   A  1  319 ? 39.336  -21.593 -22.747  1.00 65.40  ? 319  LEU   A N    1 
ATOM   4803  C  CA   . LEU   A  1  319 ? 40.094  -21.030 -23.857  1.00 68.26  ? 319  LEU   A CA   1 
ATOM   4804  C  C    . LEU   A  1  319 ? 40.625  -22.151 -24.741  1.00 69.74  ? 319  LEU   A C    1 
ATOM   4805  O  O    . LEU   A  1  319 ? 41.328  -23.049 -24.263  1.00 68.12  ? 319  LEU   A O    1 
ATOM   4806  C  CB   . LEU   A  1  319 ? 41.244  -20.173 -23.333  1.00 67.61  ? 319  LEU   A CB   1 
ATOM   4807  C  CG   . LEU   A  1  319 ? 40.921  -18.711 -23.021  1.00 70.18  ? 319  LEU   A CG   1 
ATOM   4808  C  CD1  . LEU   A  1  319 ? 39.657  -18.580 -22.188  1.00 71.80  ? 319  LEU   A CD1  1 
ATOM   4809  C  CD2  . LEU   A  1  319 ? 42.102  -18.075 -22.307  1.00 71.27  ? 319  LEU   A CD2  1 
ATOM   4810  H  H    . LEU   A  1  319 ? 39.756  -21.582 -21.997  1.00 78.46  ? 319  LEU   A H    1 
ATOM   4811  H  HA   . LEU   A  1  319 ? 39.510  -20.469 -24.390  1.00 81.89  ? 319  LEU   A HA   1 
ATOM   4812  H  HB2  . LEU   A  1  319 ? 41.567  -20.574 -22.511  1.00 81.12  ? 319  LEU   A HB2  1 
ATOM   4813  H  HB3  . LEU   A  1  319 ? 41.947  -20.173 -24.001  1.00 81.12  ? 319  LEU   A HB3  1 
ATOM   4814  H  HG   . LEU   A  1  319 ? 40.758  -18.239 -23.853  1.00 84.19  ? 319  LEU   A HG   1 
ATOM   4815  H  HD11 . LEU   A  1  319 ? 39.528  -17.648 -21.955  1.00 86.14  ? 319  LEU   A HD11 1 
ATOM   4816  H  HD12 . LEU   A  1  319 ? 38.902  -18.900 -22.706  1.00 86.14  ? 319  LEU   A HD12 1 
ATOM   4817  H  HD13 . LEU   A  1  319 ? 39.754  -19.112 -21.382  1.00 86.14  ? 319  LEU   A HD13 1 
ATOM   4818  H  HD21 . LEU   A  1  319 ? 41.889  -17.149 -22.108  1.00 85.50  ? 319  LEU   A HD21 1 
ATOM   4819  H  HD22 . LEU   A  1  319 ? 42.271  -18.559 -21.484  1.00 85.50  ? 319  LEU   A HD22 1 
ATOM   4820  H  HD23 . LEU   A  1  319 ? 42.881  -18.119 -22.883  1.00 85.50  ? 319  LEU   A HD23 1 
ATOM   4821  N  N    . GLN   A  1  320 ? 40.291  -22.100 -26.027  1.00 71.52  ? 320  GLN   A N    1 
ATOM   4822  C  CA   . GLN   A  1  320 ? 40.824  -23.064 -26.975  1.00 73.00  ? 320  GLN   A CA   1 
ATOM   4823  C  C    . GLN   A  1  320 ? 42.290  -22.764 -27.264  1.00 80.76  ? 320  GLN   A C    1 
ATOM   4824  O  O    . GLN   A  1  320 ? 42.718  -21.607 -27.289  1.00 84.92  ? 320  GLN   A O    1 
ATOM   4825  C  CB   . GLN   A  1  320 ? 40.020  -23.039 -28.275  1.00 65.54  ? 320  GLN   A CB   1 
ATOM   4826  C  CG   . GLN   A  1  320 ? 40.496  -24.042 -29.320  1.00 62.22  ? 320  GLN   A CG   1 
ATOM   4827  C  CD   . GLN   A  1  320 ? 39.745  -23.953 -30.643  1.00 63.66  ? 320  GLN   A CD   1 
ATOM   4828  O  OE1  . GLN   A  1  320 ? 40.062  -24.677 -31.586  1.00 64.99  ? 320  GLN   A OE1  1 
ATOM   4829  N  NE2  . GLN   A  1  320 ? 38.752  -23.068 -30.720  1.00 65.57  ? 320  GLN   A NE2  1 
ATOM   4830  H  H    . GLN   A  1  320 ? 39.759  -21.518 -26.372  1.00 85.81  ? 320  GLN   A H    1 
ATOM   4831  H  HA   . GLN   A  1  320 ? 40.759  -23.958 -26.602  1.00 87.58  ? 320  GLN   A HA   1 
ATOM   4832  H  HB2  . GLN   A  1  320 ? 39.093  -23.243 -28.071  1.00 78.63  ? 320  GLN   A HB2  1 
ATOM   4833  H  HB3  . GLN   A  1  320 ? 40.087  -22.153 -28.664  1.00 78.63  ? 320  GLN   A HB3  1 
ATOM   4834  H  HG2  . GLN   A  1  320 ? 41.435  -23.881 -29.501  1.00 74.64  ? 320  GLN   A HG2  1 
ATOM   4835  H  HG3  . GLN   A  1  320 ? 40.374  -24.938 -28.970  1.00 74.64  ? 320  GLN   A HG3  1 
ATOM   4836  H  HE21 . GLN   A  1  320 ? 38.560  -22.578 -30.040  1.00 78.66  ? 320  GLN   A HE21 1 
ATOM   4837  H  HE22 . GLN   A  1  320 ? 38.304  -22.988 -31.449  1.00 78.66  ? 320  GLN   A HE22 1 
ATOM   4838  N  N    . ARG   A  1  321 ? 43.062  -23.824 -27.483  1.00 80.11  ? 321  ARG   A N    1 
ATOM   4839  C  CA   . ARG   A  1  321 ? 44.475  -23.706 -27.803  1.00 80.00  ? 321  ARG   A CA   1 
ATOM   4840  C  C    . ARG   A  1  321 ? 44.782  -24.525 -29.048  1.00 78.22  ? 321  ARG   A C    1 
ATOM   4841  O  O    . ARG   A  1  321 ? 44.099  -25.506 -29.351  1.00 77.70  ? 321  ARG   A O    1 
ATOM   4842  C  CB   . ARG   A  1  321 ? 45.349  -24.166 -26.633  1.00 81.12  ? 321  ARG   A CB   1 
ATOM   4843  C  CG   . ARG   A  1  321 ? 44.951  -23.540 -25.306  1.00 86.12  ? 321  ARG   A CG   1 
ATOM   4844  C  CD   . ARG   A  1  321 ? 46.064  -23.645 -24.285  1.00 91.64  ? 321  ARG   A CD   1 
ATOM   4845  N  NE   . ARG   A  1  321 ? 46.522  -25.019 -24.119  1.00 94.81  ? 321  ARG   A NE   1 
ATOM   4846  C  CZ   . ARG   A  1  321 ? 47.556  -25.377 -23.367  1.00 95.11  ? 321  ARG   A CZ   1 
ATOM   4847  N  NH1  . ARG   A  1  321 ? 47.896  -26.654 -23.279  1.00 96.61  ? 321  ARG   A NH1  1 
ATOM   4848  N  NH2  . ARG   A  1  321 ? 48.253  -24.463 -22.704  1.00 94.10  ? 321  ARG   A NH2  1 
ATOM   4849  H  H    . ARG   A  1  321 ? 42.782  -24.637 -27.451  1.00 96.12  ? 321  ARG   A H    1 
ATOM   4850  H  HA   . ARG   A  1  321 ? 44.695  -22.781 -27.995  1.00 95.98  ? 321  ARG   A HA   1 
ATOM   4851  H  HB2  . ARG   A  1  321 ? 45.273  -25.129 -26.544  1.00 97.33  ? 321  ARG   A HB2  1 
ATOM   4852  H  HB3  . ARG   A  1  321 ? 46.270  -23.921 -26.814  1.00 97.33  ? 321  ARG   A HB3  1 
ATOM   4853  H  HG2  . ARG   A  1  321 ? 44.749  -22.601 -25.442  1.00 103.33 ? 321  ARG   A HG2  1 
ATOM   4854  H  HG3  . ARG   A  1  321 ? 44.172  -24.000 -24.955  1.00 103.33 ? 321  ARG   A HG3  1 
ATOM   4855  H  HD2  . ARG   A  1  321 ? 46.817  -23.107 -24.576  1.00 109.95 ? 321  ARG   A HD2  1 
ATOM   4856  H  HD3  . ARG   A  1  321 ? 45.742  -23.327 -23.427  1.00 109.95 ? 321  ARG   A HD3  1 
ATOM   4857  H  HE   . ARG   A  1  321 ? 46.095  -25.638 -24.536  1.00 113.75 ? 321  ARG   A HE   1 
ATOM   4858  H  HH11 . ARG   A  1  321 ? 47.447  -27.248 -23.709  1.00 115.91 ? 321  ARG   A HH11 1 
ATOM   4859  H  HH12 . ARG   A  1  321 ? 48.565  -26.888 -22.793  1.00 115.91 ? 321  ARG   A HH12 1 
ATOM   4860  H  HH21 . ARG   A  1  321 ? 48.036  -23.633 -22.761  1.00 112.90 ? 321  ARG   A HH21 1 
ATOM   4861  H  HH22 . ARG   A  1  321 ? 48.922  -24.701 -22.219  1.00 112.90 ? 321  ARG   A HH22 1 
ATOM   4862  N  N    . ALA   A  1  322 ? 45.823  -24.103 -29.770  1.00 79.92  ? 322  ALA   A N    1 
ATOM   4863  C  CA   . ALA   A  1  322 ? 46.173  -24.769 -31.021  1.00 84.08  ? 322  ALA   A CA   1 
ATOM   4864  C  C    . ALA   A  1  322 ? 46.441  -26.253 -30.812  1.00 85.94  ? 322  ALA   A C    1 
ATOM   4865  O  O    . ALA   A  1  322 ? 46.159  -27.065 -31.701  1.00 84.78  ? 322  ALA   A O    1 
ATOM   4866  C  CB   . ALA   A  1  322 ? 47.391  -24.093 -31.650  1.00 86.12  ? 322  ALA   A CB   1 
ATOM   4867  H  H    . ALA   A  1  322 ? 46.334  -23.444 -29.560  1.00 95.88  ? 322  ALA   A H    1 
ATOM   4868  H  HA   . ALA   A  1  322 ? 45.428  -24.683 -31.637  1.00 100.87 ? 322  ALA   A HA   1 
ATOM   4869  H  HB1  . ALA   A  1  322 ? 47.603  -24.539 -32.485  1.00 103.32 ? 322  ALA   A HB1  1 
ATOM   4870  H  HB2  . ALA   A  1  322 ? 47.184  -23.160 -31.816  1.00 103.32 ? 322  ALA   A HB2  1 
ATOM   4871  H  HB3  . ALA   A  1  322 ? 48.141  -24.162 -31.039  1.00 103.32 ? 322  ALA   A HB3  1 
ATOM   4872  N  N    . SER   A  1  323 ? 46.979  -26.627 -29.651  1.00 87.73  ? 323  SER   A N    1 
ATOM   4873  C  CA   . SER   A  1  323 ? 47.262  -28.025 -29.348  1.00 90.08  ? 323  SER   A CA   1 
ATOM   4874  C  C    . SER   A  1  323 ? 46.004  -28.872 -29.199  1.00 91.63  ? 323  SER   A C    1 
ATOM   4875  O  O    . SER   A  1  323 ? 46.123  -30.084 -28.985  1.00 90.25  ? 323  SER   A O    1 
ATOM   4876  C  CB   . SER   A  1  323 ? 48.096  -28.119 -28.069  1.00 92.89  ? 323  SER   A CB   1 
ATOM   4877  O  OG   . SER   A  1  323 ? 47.408  -27.548 -26.969  1.00 92.70  ? 323  SER   A OG   1 
ATOM   4878  H  H    . SER   A  1  323 ? 47.190  -26.084 -29.018  1.00 105.25 ? 323  SER   A H    1 
ATOM   4879  H  HA   . SER   A  1  323 ? 47.781  -28.398 -30.078  1.00 108.08 ? 323  SER   A HA   1 
ATOM   4880  H  HB2  . SER   A  1  323 ? 48.275  -29.053 -27.877  1.00 111.45 ? 323  SER   A HB2  1 
ATOM   4881  H  HB3  . SER   A  1  323 ? 48.930  -27.642 -28.201  1.00 111.45 ? 323  SER   A HB3  1 
ATOM   4882  H  HG   . SER   A  1  323 ? 47.906  -27.539 -26.292  1.00 111.22 ? 323  SER   A HG   1 
ATOM   4883  N  N    . GLY   A  1  324 ? 44.815  -28.279 -29.303  1.00 96.13  ? 324  GLY   A N    1 
ATOM   4884  C  CA   . GLY   A  1  324 ? 43.575  -29.013 -29.185  1.00 97.43  ? 324  GLY   A CA   1 
ATOM   4885  C  C    . GLY   A  1  324 ? 43.028  -29.115 -27.779  1.00 97.75  ? 324  GLY   A C    1 
ATOM   4886  O  O    . GLY   A  1  324 ? 41.865  -29.504 -27.611  1.00 97.10  ? 324  GLY   A O    1 
ATOM   4887  H  H    . GLY   A  1  324 ? 44.707  -27.438 -29.445  1.00 115.34 ? 324  GLY   A H    1 
ATOM   4888  H  HA2  . GLY   A  1  324 ? 42.903  -28.578 -29.733  1.00 116.90 ? 324  GLY   A HA2  1 
ATOM   4889  H  HA3  . GLY   A  1  324 ? 43.716  -29.915 -29.513  1.00 116.90 ? 324  GLY   A HA3  1 
ATOM   4890  N  N    . ASP   A  1  325 ? 43.823  -28.783 -26.766  1.00 98.99  ? 325  ASP   A N    1 
ATOM   4891  C  CA   . ASP   A  1  325 ? 43.361  -28.809 -25.390  1.00 99.48  ? 325  ASP   A CA   1 
ATOM   4892  C  C    . ASP   A  1  325 ? 42.482  -27.592 -25.107  1.00 97.45  ? 325  ASP   A C    1 
ATOM   4893  O  O    . ASP   A  1  325 ? 42.213  -26.763 -25.980  1.00 102.26 ? 325  ASP   A O    1 
ATOM   4894  C  CB   . ASP   A  1  325 ? 44.550  -28.851 -24.433  1.00 102.85 ? 325  ASP   A CB   1 
ATOM   4895  C  CG   . ASP   A  1  325 ? 45.363  -30.126 -24.564  1.00 109.66 ? 325  ASP   A CG   1 
ATOM   4896  O  OD1  . ASP   A  1  325 ? 44.913  -31.056 -25.267  1.00 112.84 ? 325  ASP   A OD1  1 
ATOM   4897  O  OD2  . ASP   A  1  325 ? 46.456  -30.199 -23.963  1.00 113.16 ? 325  ASP   A OD2  1 
ATOM   4898  H  H    . ASP   A  1  325 ? 44.642  -28.537 -26.855  1.00 118.77 ? 325  ASP   A H    1 
ATOM   4899  H  HA   . ASP   A  1  325 ? 42.831  -29.611 -25.258  1.00 119.35 ? 325  ASP   A HA   1 
ATOM   4900  H  HB2  . ASP   A  1  325 ? 45.135  -28.101 -24.622  1.00 123.40 ? 325  ASP   A HB2  1 
ATOM   4901  H  HB3  . ASP   A  1  325 ? 44.224  -28.795 -23.521  1.00 123.40 ? 325  ASP   A HB3  1 
ATOM   4902  N  N    . PHE   A  1  326 ? 42.028  -27.487 -23.861  1.00 87.96  ? 326  PHE   A N    1 
ATOM   4903  C  CA   . PHE   A  1  326 ? 41.271  -26.338 -23.392  1.00 77.90  ? 326  PHE   A CA   1 
ATOM   4904  C  C    . PHE   A  1  326 ? 41.832  -25.888 -22.053  1.00 69.26  ? 326  PHE   A C    1 
ATOM   4905  O  O    . PHE   A  1  326 ? 42.264  -26.711 -21.240  1.00 63.15  ? 326  PHE   A O    1 
ATOM   4906  C  CB   . PHE   A  1  326 ? 39.779  -26.661 -23.256  1.00 75.43  ? 326  PHE   A CB   1 
ATOM   4907  C  CG   . PHE   A  1  326 ? 39.039  -26.673 -24.564  1.00 71.48  ? 326  PHE   A CG   1 
ATOM   4908  C  CD1  . PHE   A  1  326 ? 38.880  -27.849 -25.277  1.00 69.77  ? 326  PHE   A CD1  1 
ATOM   4909  C  CD2  . PHE   A  1  326 ? 38.500  -25.506 -25.079  1.00 64.98  ? 326  PHE   A CD2  1 
ATOM   4910  C  CE1  . PHE   A  1  326 ? 38.197  -27.860 -26.479  1.00 66.81  ? 326  PHE   A CE1  1 
ATOM   4911  C  CE2  . PHE   A  1  326 ? 37.817  -25.511 -26.280  1.00 59.51  ? 326  PHE   A CE2  1 
ATOM   4912  C  CZ   . PHE   A  1  326 ? 37.666  -26.690 -26.980  1.00 62.10  ? 326  PHE   A CZ   1 
ATOM   4913  H  H    . PHE   A  1  326 ? 42.150  -28.086 -23.256  1.00 105.54 ? 326  PHE   A H    1 
ATOM   4914  H  HA   . PHE   A  1  326 ? 41.359  -25.608 -24.025  1.00 93.46  ? 326  PHE   A HA   1 
ATOM   4915  H  HB2  . PHE   A  1  326 ? 39.686  -27.540 -22.856  1.00 90.50  ? 326  PHE   A HB2  1 
ATOM   4916  H  HB3  . PHE   A  1  326 ? 39.366  -25.992 -22.689  1.00 90.50  ? 326  PHE   A HB3  1 
ATOM   4917  H  HD1  . PHE   A  1  326 ? 39.236  -28.641 -24.943  1.00 83.70  ? 326  PHE   A HD1  1 
ATOM   4918  H  HD2  . PHE   A  1  326 ? 38.599  -24.708 -24.610  1.00 77.96  ? 326  PHE   A HD2  1 
ATOM   4919  H  HE1  . PHE   A  1  326 ? 38.096  -28.656 -26.950  1.00 80.15  ? 326  PHE   A HE1  1 
ATOM   4920  H  HE2  . PHE   A  1  326 ? 37.460  -24.721 -26.617  1.00 71.40  ? 326  PHE   A HE2  1 
ATOM   4921  H  HZ   . PHE   A  1  326 ? 37.206  -26.696 -27.789  1.00 74.51  ? 326  PHE   A HZ   1 
ATOM   4922  N  N    . GLN   A  1  327 ? 41.831  -24.577 -21.837  1.00 65.07  ? 327  GLN   A N    1 
ATOM   4923  C  CA   . GLN   A  1  327 ? 42.285  -23.964 -20.593  1.00 64.69  ? 327  GLN   A CA   1 
ATOM   4924  C  C    . GLN   A  1  327 ? 41.058  -23.388 -19.898  1.00 65.24  ? 327  GLN   A C    1 
ATOM   4925  O  O    . GLN   A  1  327 ? 40.525  -22.357 -20.322  1.00 65.90  ? 327  GLN   A O    1 
ATOM   4926  C  CB   . GLN   A  1  327 ? 43.333  -22.891 -20.875  1.00 71.62  ? 327  GLN   A CB   1 
ATOM   4927  C  CG   . GLN   A  1  327 ? 44.039  -22.361 -19.646  1.00 81.24  ? 327  GLN   A CG   1 
ATOM   4928  C  CD   . GLN   A  1  327 ? 45.308  -21.610 -19.996  1.00 89.56  ? 327  GLN   A CD   1 
ATOM   4929  O  OE1  . GLN   A  1  327 ? 45.263  -20.528 -20.582  1.00 93.02  ? 327  GLN   A OE1  1 
ATOM   4930  N  NE2  . GLN   A  1  327 ? 46.451  -22.190 -19.649  1.00 91.79  ? 327  GLN   A NE2  1 
ATOM   4931  H  H    . GLN   A  1  327 ? 41.562  -24.001 -22.416  1.00 78.06  ? 327  GLN   A H    1 
ATOM   4932  H  HA   . GLN   A  1  327 ? 42.688  -24.629 -20.012  1.00 77.61  ? 327  GLN   A HA   1 
ATOM   4933  H  HB2  . GLN   A  1  327 ? 44.008  -23.267 -21.462  1.00 85.92  ? 327  GLN   A HB2  1 
ATOM   4934  H  HB3  . GLN   A  1  327 ? 42.896  -22.141 -21.309  1.00 85.92  ? 327  GLN   A HB3  1 
ATOM   4935  H  HG2  . GLN   A  1  327 ? 43.447  -21.752 -19.177  1.00 97.47  ? 327  GLN   A HG2  1 
ATOM   4936  H  HG3  . GLN   A  1  327 ? 44.276  -23.104 -19.070  1.00 97.47  ? 327  GLN   A HG3  1 
ATOM   4937  H  HE21 . GLN   A  1  327 ? 46.443  -22.951 -19.248  1.00 110.12 ? 327  GLN   A HE21 1 
ATOM   4938  H  HE22 . GLN   A  1  327 ? 47.200  -21.805 -19.825  1.00 110.12 ? 327  GLN   A HE22 1 
ATOM   4939  N  N    . THR   A  1  328 ? 40.611  -24.052 -18.835  1.00 63.08  ? 328  THR   A N    1 
ATOM   4940  C  CA   . THR   A  1  328 ? 39.318  -23.771 -18.232  1.00 59.88  ? 328  THR   A CA   1 
ATOM   4941  C  C    . THR   A  1  328 ? 39.466  -22.980 -16.937  1.00 55.14  ? 328  THR   A C    1 
ATOM   4942  O  O    . THR   A  1  328 ? 40.417  -23.163 -16.174  1.00 56.19  ? 328  THR   A O    1 
ATOM   4943  C  CB   . THR   A  1  328 ? 38.558  -25.071 -17.951  1.00 64.91  ? 328  THR   A CB   1 
ATOM   4944  O  OG1  . THR   A  1  328 ? 38.494  -25.863 -19.143  1.00 65.81  ? 328  THR   A OG1  1 
ATOM   4945  C  CG2  . THR   A  1  328 ? 37.142  -24.770 -17.479  1.00 64.90  ? 328  THR   A CG2  1 
ATOM   4946  H  H    . THR   A  1  328 ? 41.049  -24.680 -18.442  1.00 75.68  ? 328  THR   A H    1 
ATOM   4947  H  HA   . THR   A  1  328 ? 38.801  -23.231 -18.849  1.00 71.83  ? 328  THR   A HA   1 
ATOM   4948  H  HB   . THR   A  1  328 ? 39.018  -25.567 -17.255  1.00 77.87  ? 328  THR   A HB   1 
ATOM   4949  H  HG1  . THR   A  1  328 ? 38.053  -25.460 -19.733  1.00 78.95  ? 328  THR   A HG1  1 
ATOM   4950  H  HG21 . THR   A  1  328 ? 36.637  -25.594 -17.401  1.00 77.86  ? 328  THR   A HG21 1 
ATOM   4951  H  HG22 . THR   A  1  328 ? 37.167  -24.332 -16.614  1.00 77.86  ? 328  THR   A HG22 1 
ATOM   4952  H  HG23 . THR   A  1  328 ? 36.698  -24.188 -18.115  1.00 77.86  ? 328  THR   A HG23 1 
ATOM   4953  N  N    . THR   A  1  329 ? 38.500  -22.093 -16.703  1.00 60.21  ? 329  THR   A N    1 
ATOM   4954  C  CA   . THR   A  1  329 ? 38.416  -21.322 -15.473  1.00 70.26  ? 329  THR   A CA   1 
ATOM   4955  C  C    . THR   A  1  329 ? 36.945  -21.133 -15.130  1.00 66.51  ? 329  THR   A C    1 
ATOM   4956  O  O    . THR   A  1  329 ? 36.098  -21.011 -16.019  1.00 66.77  ? 329  THR   A O    1 
ATOM   4957  C  CB   . THR   A  1  329 ? 39.110  -19.959 -15.600  1.00 85.70  ? 329  THR   A CB   1 
ATOM   4958  O  OG1  . THR   A  1  329 ? 40.497  -20.148 -15.908  1.00 92.88  ? 329  THR   A OG1  1 
ATOM   4959  C  CG2  . THR   A  1  329 ? 38.985  -19.165 -14.305  1.00 91.23  ? 329  THR   A CG2  1 
ATOM   4960  H  H    . THR   A  1  329 ? 37.866  -21.918 -17.258  1.00 72.23  ? 329  THR   A H    1 
ATOM   4961  H  HA   . THR   A  1  329 ? 38.848  -21.807 -14.752  1.00 84.29  ? 329  THR   A HA   1 
ATOM   4962  H  HB   . THR   A  1  329 ? 38.687  -19.452 -16.311  1.00 102.82 ? 329  THR   A HB   1 
ATOM   4963  H  HG1  . THR   A  1  329 ? 40.877  -19.404 -15.990  1.00 111.43 ? 329  THR   A HG1  1 
ATOM   4964  H  HG21 . THR   A  1  329 ? 39.519  -18.357 -14.358  1.00 109.45 ? 329  THR   A HG21 1 
ATOM   4965  H  HG22 . THR   A  1  329 ? 38.059  -18.920 -14.153  1.00 109.45 ? 329  THR   A HG22 1 
ATOM   4966  H  HG23 . THR   A  1  329 ? 39.296  -19.699 -13.557  1.00 109.45 ? 329  THR   A HG23 1 
ATOM   4967  N  N    . LYS   A  1  330 ? 36.651  -21.109 -13.836  1.00 66.97  ? 330  LYS   A N    1 
ATOM   4968  C  CA   . LYS   A  1  330 ? 35.287  -20.989 -13.346  1.00 66.35  ? 330  LYS   A CA   1 
ATOM   4969  C  C    . LYS   A  1  330 ? 34.998  -19.551 -12.929  1.00 66.87  ? 330  LYS   A C    1 
ATOM   4970  O  O    . LYS   A  1  330 ? 35.904  -18.767 -12.637  1.00 70.65  ? 330  LYS   A O    1 
ATOM   4971  C  CB   . LYS   A  1  330 ? 35.050  -21.935 -12.167  1.00 66.39  ? 330  LYS   A CB   1 
ATOM   4972  C  CG   . LYS   A  1  330 ? 35.516  -23.366 -12.409  1.00 66.54  ? 330  LYS   A CG   1 
ATOM   4973  C  CD   . LYS   A  1  330 ? 34.638  -24.090 -13.419  1.00 67.43  ? 330  LYS   A CD   1 
ATOM   4974  C  CE   . LYS   A  1  330 ? 35.190  -25.472 -13.743  1.00 69.94  ? 330  LYS   A CE   1 
ATOM   4975  N  NZ   . LYS   A  1  330 ? 35.425  -26.290 -12.519  1.00 75.41  ? 330  LYS   A NZ   1 
ATOM   4976  H  H    . LYS   A  1  330 ? 37.238  -21.162 -13.210  1.00 80.35  ? 330  LYS   A H    1 
ATOM   4977  H  HA   . LYS   A  1  330 ? 34.669  -21.229 -14.054  1.00 79.60  ? 330  LYS   A HA   1 
ATOM   4978  H  HB2  . LYS   A  1  330 ? 35.531  -21.596 -11.396  1.00 79.65  ? 330  LYS   A HB2  1 
ATOM   4979  H  HB3  . LYS   A  1  330 ? 34.099  -21.964 -11.978  1.00 79.65  ? 330  LYS   A HB3  1 
ATOM   4980  H  HG2  . LYS   A  1  330 ? 36.424  -23.352 -12.751  1.00 79.83  ? 330  LYS   A HG2  1 
ATOM   4981  H  HG3  . LYS   A  1  330 ? 35.484  -23.858 -11.573  1.00 79.83  ? 330  LYS   A HG3  1 
ATOM   4982  H  HD2  . LYS   A  1  330 ? 33.746  -24.195 -13.054  1.00 80.90  ? 330  LYS   A HD2  1 
ATOM   4983  H  HD3  . LYS   A  1  330 ? 34.602  -23.575 -14.241  1.00 80.90  ? 330  LYS   A HD3  1 
ATOM   4984  H  HE2  . LYS   A  1  330 ? 34.556  -25.944 -14.304  1.00 83.90  ? 330  LYS   A HE2  1 
ATOM   4985  H  HE3  . LYS   A  1  330 ? 36.036  -25.376 -14.208  1.00 83.90  ? 330  LYS   A HE3  1 
ATOM   4986  H  HZ1  . LYS   A  1  330 ? 35.594  -27.134 -12.745  1.00 90.47  ? 330  LYS   A HZ1  1 
ATOM   4987  H  HZ2  . LYS   A  1  330 ? 36.120  -25.968 -12.066  1.00 90.47  ? 330  LYS   A HZ2  1 
ATOM   4988  H  HZ3  . LYS   A  1  330 ? 34.704  -26.270 -11.997  1.00 90.47  ? 330  LYS   A HZ3  1 
ATOM   4989  N  N    . LEU   A  1  331 ? 33.709  -19.215 -12.901  1.00 64.14  ? 331  LEU   A N    1 
ATOM   4990  C  CA   . LEU   A  1  331 ? 33.272  -17.860 -12.572  1.00 59.58  ? 331  LEU   A CA   1 
ATOM   4991  C  C    . LEU   A  1  331 ? 31.948  -17.974 -11.830  1.00 60.13  ? 331  LEU   A C    1 
ATOM   4992  O  O    . LEU   A  1  331 ? 30.932  -18.335 -12.430  1.00 65.56  ? 331  LEU   A O    1 
ATOM   4993  C  CB   . LEU   A  1  331 ? 33.130  -17.014 -13.833  1.00 58.48  ? 331  LEU   A CB   1 
ATOM   4994  C  CG   . LEU   A  1  331 ? 33.407  -15.516 -13.705  1.00 62.55  ? 331  LEU   A CG   1 
ATOM   4995  C  CD1  . LEU   A  1  331 ? 34.865  -15.256 -13.364  1.00 68.10  ? 331  LEU   A CD1  1 
ATOM   4996  C  CD2  . LEU   A  1  331 ? 33.023  -14.817 -14.997  1.00 61.89  ? 331  LEU   A CD2  1 
ATOM   4997  H  H    . LEU   A  1  331 ? 33.064  -19.758 -13.072  1.00 76.94  ? 331  LEU   A H    1 
ATOM   4998  H  HA   . LEU   A  1  331 ? 33.920  -17.435 -11.988  1.00 71.48  ? 331  LEU   A HA   1 
ATOM   4999  H  HB2  . LEU   A  1  331 ? 33.749  -17.360 -14.495  1.00 70.16  ? 331  LEU   A HB2  1 
ATOM   5000  H  HB3  . LEU   A  1  331 ? 32.218  -17.106 -14.151  1.00 70.16  ? 331  LEU   A HB3  1 
ATOM   5001  H  HG   . LEU   A  1  331 ? 32.874  -15.152 -12.981  1.00 75.04  ? 331  LEU   A HG   1 
ATOM   5002  H  HD11 . LEU   A  1  331 ? 35.020  -14.299 -13.349  1.00 81.70  ? 331  LEU   A HD11 1 
ATOM   5003  H  HD12 . LEU   A  1  331 ? 35.059  -15.636 -12.493  1.00 81.70  ? 331  LEU   A HD12 1 
ATOM   5004  H  HD13 . LEU   A  1  331 ? 35.426  -15.671 -14.038  1.00 81.70  ? 331  LEU   A HD13 1 
ATOM   5005  H  HD21 . LEU   A  1  331 ? 33.267  -13.880 -14.934  1.00 74.25  ? 331  LEU   A HD21 1 
ATOM   5006  H  HD22 . LEU   A  1  331 ? 33.497  -15.232 -15.734  1.00 74.25  ? 331  LEU   A HD22 1 
ATOM   5007  H  HD23 . LEU   A  1  331 ? 32.066  -14.901 -15.130  1.00 74.25  ? 331  LEU   A HD23 1 
ATOM   5008  N  N    . ASN   A  1  332 ? 31.958  -17.663 -10.539  1.00 57.39  ? 332  ASN   A N    1 
ATOM   5009  C  CA   . ASN   A  1  332 ? 30.804  -17.901 -9.686   1.00 58.52  ? 332  ASN   A CA   1 
ATOM   5010  C  C    . ASN   A  1  332 ? 29.887  -16.683 -9.638   1.00 57.80  ? 332  ASN   A C    1 
ATOM   5011  O  O    . ASN   A  1  332 ? 30.302  -15.546 -9.872   1.00 58.33  ? 332  ASN   A O    1 
ATOM   5012  C  CB   . ASN   A  1  332 ? 31.250  -18.267 -8.270   1.00 58.51  ? 332  ASN   A CB   1 
ATOM   5013  C  CG   . ASN   A  1  332 ? 31.814  -19.667 -8.184   1.00 62.75  ? 332  ASN   A CG   1 
ATOM   5014  O  OD1  . ASN   A  1  332 ? 32.098  -20.297 -9.202   1.00 62.71  ? 332  ASN   A OD1  1 
ATOM   5015  N  ND2  . ASN   A  1  332 ? 31.980  -20.165 -6.965   1.00 67.98  ? 332  ASN   A ND2  1 
ATOM   5016  H  H    . ASN   A  1  332 ? 32.628  -17.311 -10.131  1.00 68.85  ? 332  ASN   A H    1 
ATOM   5017  H  HA   . ASN   A  1  332 ? 30.295  -18.640 -10.053  1.00 70.20  ? 332  ASN   A HA   1 
ATOM   5018  H  HB2  . ASN   A  1  332 ? 31.939  -17.647 -7.985   1.00 70.20  ? 332  ASN   A HB2  1 
ATOM   5019  H  HB3  . ASN   A  1  332 ? 30.487  -18.213 -7.674   1.00 70.20  ? 332  ASN   A HB3  1 
ATOM   5020  H  HD21 . ASN   A  1  332 ? 32.298  -20.958 -6.864   1.00 81.56  ? 332  ASN   A HD21 1 
ATOM   5021  H  HD22 . ASN   A  1  332 ? 31.770  -19.695 -6.276   1.00 81.56  ? 332  ASN   A HD22 1 
ATOM   5022  N  N    . GLY   A  1  333 ? 28.621  -16.945 -9.324   1.00 56.63  ? 333  GLY   A N    1 
ATOM   5023  C  CA   . GLY   A  1  333 ? 27.652  -15.882 -9.166   1.00 57.06  ? 333  GLY   A CA   1 
ATOM   5024  C  C    . GLY   A  1  333 ? 27.869  -15.100 -7.885   1.00 61.41  ? 333  GLY   A C    1 
ATOM   5025  O  O    . GLY   A  1  333 ? 28.686  -15.443 -7.030   1.00 64.94  ? 333  GLY   A O    1 
ATOM   5026  H  H    . GLY   A  1  333 ? 28.303  -17.733 -9.198   1.00 67.94  ? 333  GLY   A H    1 
ATOM   5027  H  HA2  . GLY   A  1  333 ? 27.720  -15.270 -9.915   1.00 68.45  ? 333  GLY   A HA2  1 
ATOM   5028  H  HA3  . GLY   A  1  333 ? 26.759  -16.261 -9.147   1.00 68.45  ? 333  GLY   A HA3  1 
ATOM   5029  N  N    . PHE   A  1  334 ? 27.104  -14.017 -7.752   1.00 62.76  ? 334  PHE   A N    1 
ATOM   5030  C  CA   . PHE   A  1  334 ? 27.252  -13.094 -6.636   1.00 63.78  ? 334  PHE   A CA   1 
ATOM   5031  C  C    . PHE   A  1  334 ? 26.082  -13.110 -5.666   1.00 60.43  ? 334  PHE   A C    1 
ATOM   5032  O  O    . PHE   A  1  334 ? 26.280  -12.833 -4.481   1.00 60.31  ? 334  PHE   A O    1 
ATOM   5033  C  CB   . PHE   A  1  334 ? 27.440  -11.665 -7.159   1.00 67.58  ? 334  PHE   A CB   1 
ATOM   5034  C  CG   . PHE   A  1  334 ? 28.512  -11.541 -8.204   1.00 70.21  ? 334  PHE   A CG   1 
ATOM   5035  C  CD1  . PHE   A  1  334 ? 29.833  -11.350 -7.840   1.00 68.80  ? 334  PHE   A CD1  1 
ATOM   5036  C  CD2  . PHE   A  1  334 ? 28.197  -11.619 -9.551   1.00 70.59  ? 334  PHE   A CD2  1 
ATOM   5037  C  CE1  . PHE   A  1  334 ? 30.821  -11.238 -8.799   1.00 69.52  ? 334  PHE   A CE1  1 
ATOM   5038  C  CE2  . PHE   A  1  334 ? 29.179  -11.507 -10.515  1.00 71.29  ? 334  PHE   A CE2  1 
ATOM   5039  C  CZ   . PHE   A  1  334 ? 30.492  -11.316 -10.140  1.00 71.53  ? 334  PHE   A CZ   1 
ATOM   5040  H  H    . PHE   A  1  334 ? 26.484  -13.795 -8.306   1.00 75.29  ? 334  PHE   A H    1 
ATOM   5041  H  HA   . PHE   A  1  334 ? 28.047  -13.338 -6.136   1.00 76.52  ? 334  PHE   A HA   1 
ATOM   5042  H  HB2  . PHE   A  1  334 ? 26.606  -11.364 -7.553   1.00 81.08  ? 334  PHE   A HB2  1 
ATOM   5043  H  HB3  . PHE   A  1  334 ? 27.682  -11.090 -6.417   1.00 81.08  ? 334  PHE   A HB3  1 
ATOM   5044  H  HD1  . PHE   A  1  334 ? 30.059  -11.297 -6.939   1.00 82.54  ? 334  PHE   A HD1  1 
ATOM   5045  H  HD2  . PHE   A  1  334 ? 27.313  -11.749 -9.809   1.00 84.69  ? 334  PHE   A HD2  1 
ATOM   5046  H  HE1  . PHE   A  1  334 ? 31.706  -11.110 -8.544   1.00 83.40  ? 334  PHE   A HE1  1 
ATOM   5047  H  HE2  . PHE   A  1  334 ? 28.955  -11.560 -11.416  1.00 85.53  ? 334  PHE   A HE2  1 
ATOM   5048  H  HZ   . PHE   A  1  334 ? 31.156  -11.240 -10.787  1.00 85.81  ? 334  PHE   A HZ   1 
ATOM   5049  N  N    . GLU   A  1  335 ? 24.877  -13.426 -6.131   1.00 57.72  ? 335  GLU   A N    1 
ATOM   5050  C  CA   . GLU   A  1  335 ? 23.685  -13.434 -5.296   1.00 61.97  ? 335  GLU   A CA   1 
ATOM   5051  C  C    . GLU   A  1  335 ? 23.092  -14.834 -5.245   1.00 63.51  ? 335  GLU   A C    1 
ATOM   5052  O  O    . GLU   A  1  335 ? 23.095  -15.558 -6.245   1.00 65.85  ? 335  GLU   A O    1 
ATOM   5053  C  CB   . GLU   A  1  335 ? 22.636  -12.456 -5.823   1.00 65.26  ? 335  GLU   A CB   1 
ATOM   5054  C  CG   . GLU   A  1  335 ? 23.020  -10.997 -5.697   1.00 70.96  ? 335  GLU   A CG   1 
ATOM   5055  C  CD   . GLU   A  1  335 ? 22.108  -10.097 -6.506   1.00 77.72  ? 335  GLU   A CD   1 
ATOM   5056  O  OE1  . GLU   A  1  335 ? 21.931  -10.365 -7.714   1.00 79.02  ? 335  GLU   A OE1  1 
ATOM   5057  O  OE2  . GLU   A  1  335 ? 21.557  -9.132  -5.935   1.00 82.18  ? 335  GLU   A OE2  1 
ATOM   5058  H  H    . GLU   A  1  335 ? 24.723  -13.645 -6.949   1.00 69.24  ? 335  GLU   A H    1 
ATOM   5059  H  HA   . GLU   A  1  335 ? 23.929  -13.174 -4.394   1.00 74.35  ? 335  GLU   A HA   1 
ATOM   5060  H  HB2  . GLU   A  1  335 ? 22.487  -12.639 -6.763   1.00 78.29  ? 335  GLU   A HB2  1 
ATOM   5061  H  HB3  . GLU   A  1  335 ? 21.814  -12.586 -5.325   1.00 78.29  ? 335  GLU   A HB3  1 
ATOM   5062  H  HG2  . GLU   A  1  335 ? 22.960  -10.730 -4.766   1.00 85.14  ? 335  GLU   A HG2  1 
ATOM   5063  H  HG3  . GLU   A  1  335 ? 23.927  -10.877 -6.018   1.00 85.14  ? 335  GLU   A HG3  1 
ATOM   5064  N  N    . VAL   A  1  336 ? 22.572  -15.205 -4.076   1.00 61.36  ? 336  VAL   A N    1 
ATOM   5065  C  CA   . VAL   A  1  336 ? 21.971  -16.520 -3.912   1.00 63.38  ? 336  VAL   A CA   1 
ATOM   5066  C  C    . VAL   A  1  336 ? 20.678  -16.595 -4.712   1.00 62.88  ? 336  VAL   A C    1 
ATOM   5067  O  O    . VAL   A  1  336 ? 19.894  -15.637 -4.758   1.00 64.23  ? 336  VAL   A O    1 
ATOM   5068  C  CB   . VAL   A  1  336 ? 21.720  -16.813 -2.423   1.00 66.74  ? 336  VAL   A CB   1 
ATOM   5069  C  CG1  . VAL   A  1  336 ? 21.209  -18.233 -2.241   1.00 66.48  ? 336  VAL   A CG1  1 
ATOM   5070  C  CG2  . VAL   A  1  336 ? 22.990  -16.594 -1.612   1.00 71.62  ? 336  VAL   A CG2  1 
ATOM   5071  H  H    . VAL   A  1  336 ? 22.555  -14.715 -3.369   1.00 73.61  ? 336  VAL   A H    1 
ATOM   5072  H  HA   . VAL   A  1  336 ? 22.582  -17.191 -4.254   1.00 76.04  ? 336  VAL   A HA   1 
ATOM   5073  H  HB   . VAL   A  1  336 ? 21.043  -16.202 -2.094   1.00 80.07  ? 336  VAL   A HB   1 
ATOM   5074  H  HG11 . VAL   A  1  336 ? 21.064  -18.398 -1.296   1.00 79.76  ? 336  VAL   A HG11 1 
ATOM   5075  H  HG12 . VAL   A  1  336 ? 20.375  -18.333 -2.726   1.00 79.76  ? 336  VAL   A HG12 1 
ATOM   5076  H  HG13 . VAL   A  1  336 ? 21.870  -18.853 -2.588   1.00 79.76  ? 336  VAL   A HG13 1 
ATOM   5077  H  HG21 . VAL   A  1  336 ? 22.822  -16.843 -0.690   1.00 85.93  ? 336  VAL   A HG21 1 
ATOM   5078  H  HG22 . VAL   A  1  336 ? 23.698  -17.145 -1.980   1.00 85.93  ? 336  VAL   A HG22 1 
ATOM   5079  H  HG23 . VAL   A  1  336 ? 23.239  -15.658 -1.662   1.00 85.93  ? 336  VAL   A HG23 1 
ATOM   5080  N  N    . PHE   A  1  337 ? 20.454  -17.738 -5.359   1.00 59.78  ? 337  PHE   A N    1 
ATOM   5081  C  CA   . PHE   A  1  337 ? 19.244  -18.031 -6.122   1.00 59.61  ? 337  PHE   A CA   1 
ATOM   5082  C  C    . PHE   A  1  337 ? 19.039  -17.090 -7.304   1.00 61.58  ? 337  PHE   A C    1 
ATOM   5083  O  O    . PHE   A  1  337 ? 17.991  -17.150 -7.960   1.00 61.59  ? 337  PHE   A O    1 
ATOM   5084  C  CB   . PHE   A  1  337 ? 18.000  -18.000 -5.221   1.00 58.78  ? 337  PHE   A CB   1 
ATOM   5085  C  CG   . PHE   A  1  337 ? 17.969  -19.094 -4.189   1.00 62.77  ? 337  PHE   A CG   1 
ATOM   5086  C  CD1  . PHE   A  1  337 ? 18.207  -20.411 -4.547   1.00 63.15  ? 337  PHE   A CD1  1 
ATOM   5087  C  CD2  . PHE   A  1  337 ? 17.707  -18.803 -2.860   1.00 65.27  ? 337  PHE   A CD2  1 
ATOM   5088  C  CE1  . PHE   A  1  337 ? 18.181  -21.419 -3.601   1.00 63.85  ? 337  PHE   A CE1  1 
ATOM   5089  C  CE2  . PHE   A  1  337 ? 17.681  -19.806 -1.908   1.00 64.92  ? 337  PHE   A CE2  1 
ATOM   5090  C  CZ   . PHE   A  1  337 ? 17.917  -21.116 -2.280   1.00 64.12  ? 337  PHE   A CZ   1 
ATOM   5091  H  H    . PHE   A  1  337 ? 21.017  -18.388 -5.369   1.00 71.72  ? 337  PHE   A H    1 
ATOM   5092  H  HA   . PHE   A  1  337 ? 19.337  -18.925 -6.486   1.00 71.51  ? 337  PHE   A HA   1 
ATOM   5093  H  HB2  . PHE   A  1  337 ? 17.976  -17.151 -4.753   1.00 70.51  ? 337  PHE   A HB2  1 
ATOM   5094  H  HB3  . PHE   A  1  337 ? 17.211  -18.095 -5.777   1.00 70.51  ? 337  PHE   A HB3  1 
ATOM   5095  H  HD1  . PHE   A  1  337 ? 18.386  -20.620 -5.435   1.00 75.77  ? 337  PHE   A HD1  1 
ATOM   5096  H  HD2  . PHE   A  1  337 ? 17.546  -17.923 -2.605   1.00 78.31  ? 337  PHE   A HD2  1 
ATOM   5097  H  HE1  . PHE   A  1  337 ? 18.340  -22.299 -3.854   1.00 76.59  ? 337  PHE   A HE1  1 
ATOM   5098  H  HE2  . PHE   A  1  337 ? 17.504  -19.599 -1.018   1.00 77.89  ? 337  PHE   A HE2  1 
ATOM   5099  H  HZ   . PHE   A  1  337 ? 17.900  -21.793 -1.641   1.00 76.92  ? 337  PHE   A HZ   1 
ATOM   5100  N  N    . ALA   A  1  338 ? 20.011  -16.226 -7.603   1.00 63.30  ? 338  ALA   A N    1 
ATOM   5101  C  CA   . ALA   A  1  338 ? 19.885  -15.336 -8.752   1.00 63.49  ? 338  ALA   A CA   1 
ATOM   5102  C  C    . ALA   A  1  338 ? 20.066  -16.077 -10.069  1.00 59.94  ? 338  ALA   A C    1 
ATOM   5103  O  O    . ALA   A  1  338 ? 19.694  -15.547 -11.122  1.00 57.25  ? 338  ALA   A O    1 
ATOM   5104  C  CB   . ALA   A  1  338 ? 20.902  -14.197 -8.649   1.00 63.22  ? 338  ALA   A CB   1 
ATOM   5105  H  H    . ALA   A  1  338 ? 20.744  -16.138 -7.161   1.00 75.94  ? 338  ALA   A H    1 
ATOM   5106  H  HA   . ALA   A  1  338 ? 18.999  -14.943 -8.747   1.00 76.17  ? 338  ALA   A HA   1 
ATOM   5107  H  HB1  . ALA   A  1  338 ? 20.761  -13.581 -9.385   1.00 75.84  ? 338  ALA   A HB1  1 
ATOM   5108  H  HB2  . ALA   A  1  338 ? 20.777  -13.738 -7.804   1.00 75.84  ? 338  ALA   A HB2  1 
ATOM   5109  H  HB3  . ALA   A  1  338 ? 21.797  -14.568 -8.695   1.00 75.84  ? 338  ALA   A HB3  1 
ATOM   5110  N  N    . ARG   A  1  339 ? 20.628  -17.286 -10.032  1.00 58.14  ? 339  ARG   A N    1 
ATOM   5111  C  CA   . ARG   A  1  339 ? 20.831  -18.106 -11.227  1.00 60.40  ? 339  ARG   A CA   1 
ATOM   5112  C  C    . ARG   A  1  339 ? 21.778  -17.425 -12.211  1.00 61.83  ? 339  ARG   A C    1 
ATOM   5113  O  O    . ARG   A  1  339 ? 21.536  -17.390 -13.419  1.00 59.62  ? 339  ARG   A O    1 
ATOM   5114  C  CB   . ARG   A  1  339 ? 19.496  -18.451 -11.890  1.00 56.04  ? 339  ARG   A CB   1 
ATOM   5115  C  CG   . ARG   A  1  339 ? 18.600  -19.270 -10.979  1.00 56.52  ? 339  ARG   A CG   1 
ATOM   5116  C  CD   . ARG   A  1  339 ? 17.495  -19.991 -11.723  1.00 60.20  ? 339  ARG   A CD   1 
ATOM   5117  N  NE   . ARG   A  1  339 ? 16.716  -20.827 -10.814  1.00 63.54  ? 339  ARG   A NE   1 
ATOM   5118  C  CZ   . ARG   A  1  339 ? 15.590  -21.453 -11.141  1.00 62.68  ? 339  ARG   A CZ   1 
ATOM   5119  N  NH1  . ARG   A  1  339 ? 15.092  -21.343 -12.365  1.00 61.37  ? 339  ARG   A NH1  1 
ATOM   5120  N  NH2  . ARG   A  1  339 ? 14.959  -22.189 -10.237  1.00 64.49  ? 339  ARG   A NH2  1 
ATOM   5121  H  H    . ARG   A  1  339 ? 20.906  -17.662 -9.310   1.00 69.75  ? 339  ARG   A H    1 
ATOM   5122  H  HA   . ARG   A  1  339 ? 21.250  -18.939 -10.961  1.00 72.46  ? 339  ARG   A HA   1 
ATOM   5123  H  HB2  . ARG   A  1  339 ? 19.031  -17.630 -12.115  1.00 67.23  ? 339  ARG   A HB2  1 
ATOM   5124  H  HB3  . ARG   A  1  339 ? 19.664  -18.968 -12.694  1.00 67.23  ? 339  ARG   A HB3  1 
ATOM   5125  H  HG2  . ARG   A  1  339 ? 19.138  -19.937 -10.525  1.00 67.80  ? 339  ARG   A HG2  1 
ATOM   5126  H  HG3  . ARG   A  1  339 ? 18.186  -18.679 -10.331  1.00 67.80  ? 339  ARG   A HG3  1 
ATOM   5127  H  HD2  . ARG   A  1  339 ? 16.900  -19.341 -12.129  1.00 72.22  ? 339  ARG   A HD2  1 
ATOM   5128  H  HD3  . ARG   A  1  339 ? 17.882  -20.559 -12.408  1.00 72.22  ? 339  ARG   A HD3  1 
ATOM   5129  H  HE   . ARG   A  1  339 ? 17.006  -20.921 -10.010  1.00 76.22  ? 339  ARG   A HE   1 
ATOM   5130  H  HH11 . ARG   A  1  339 ? 15.498  -20.865 -12.953  1.00 73.62  ? 339  ARG   A HH11 1 
ATOM   5131  H  HH12 . ARG   A  1  339 ? 14.363  -21.751 -12.571  1.00 73.62  ? 339  ARG   A HH12 1 
ATOM   5132  H  HH21 . ARG   A  1  339 ? 15.278  -22.260 -9.442   1.00 77.37  ? 339  ARG   A HH21 1 
ATOM   5133  H  HH22 . ARG   A  1  339 ? 14.230  -22.595 -10.446  1.00 77.37  ? 339  ARG   A HH22 1 
ATOM   5134  N  N    . PHE   A  1  340 ? 22.867  -16.874 -11.678  1.00 63.05  ? 340  PHE   A N    1 
ATOM   5135  C  CA   . PHE   A  1  340 ? 23.960  -16.379 -12.502  1.00 61.80  ? 340  PHE   A CA   1 
ATOM   5136  C  C    . PHE   A  1  340 ? 24.374  -17.436 -13.517  1.00 59.69  ? 340  PHE   A C    1 
ATOM   5137  O  O    . PHE   A  1  340 ? 24.666  -18.579 -13.158  1.00 58.85  ? 340  PHE   A O    1 
ATOM   5138  C  CB   . PHE   A  1  340 ? 25.141  -16.003 -11.603  1.00 62.44  ? 340  PHE   A CB   1 
ATOM   5139  C  CG   . PHE   A  1  340 ? 26.366  -15.554 -12.349  1.00 62.55  ? 340  PHE   A CG   1 
ATOM   5140  C  CD1  . PHE   A  1  340 ? 26.554  -14.217 -12.661  1.00 62.26  ? 340  PHE   A CD1  1 
ATOM   5141  C  CD2  . PHE   A  1  340 ? 27.340  -16.467 -12.718  1.00 61.67  ? 340  PHE   A CD2  1 
ATOM   5142  C  CE1  . PHE   A  1  340 ? 27.686  -13.801 -13.340  1.00 61.44  ? 340  PHE   A CE1  1 
ATOM   5143  C  CE2  . PHE   A  1  340 ? 28.473  -16.059 -13.396  1.00 60.62  ? 340  PHE   A CE2  1 
ATOM   5144  C  CZ   . PHE   A  1  340 ? 28.648  -14.723 -13.706  1.00 59.54  ? 340  PHE   A CZ   1 
ATOM   5145  H  H    . PHE   A  1  340 ? 22.996  -16.776 -10.833  1.00 75.64  ? 340  PHE   A H    1 
ATOM   5146  H  HA   . PHE   A  1  340 ? 23.680  -15.587 -12.987  1.00 74.14  ? 340  PHE   A HA   1 
ATOM   5147  H  HB2  . PHE   A  1  340 ? 24.869  -15.277 -11.021  1.00 74.91  ? 340  PHE   A HB2  1 
ATOM   5148  H  HB3  . PHE   A  1  340 ? 25.387  -16.779 -11.075  1.00 74.91  ? 340  PHE   A HB3  1 
ATOM   5149  H  HD1  . PHE   A  1  340 ? 25.911  -13.593 -12.412  1.00 74.69  ? 340  PHE   A HD1  1 
ATOM   5150  H  HD2  . PHE   A  1  340 ? 27.231  -17.366 -12.506  1.00 73.99  ? 340  PHE   A HD2  1 
ATOM   5151  H  HE1  . PHE   A  1  340 ? 27.799  -12.902 -13.549  1.00 73.70  ? 340  PHE   A HE1  1 
ATOM   5152  H  HE2  . PHE   A  1  340 ? 29.117  -16.682 -13.644  1.00 72.72  ? 340  PHE   A HE2  1 
ATOM   5153  H  HZ   . PHE   A  1  340 ? 29.411  -14.446 -14.160  1.00 71.43  ? 340  PHE   A HZ   1 
ATOM   5154  N  N    . GLY   A  1  341 ? 24.391  -17.048 -14.790  1.00 58.27  ? 341  GLY   A N    1 
ATOM   5155  C  CA   . GLY   A  1  341 ? 24.775  -17.942 -15.861  1.00 56.40  ? 341  GLY   A CA   1 
ATOM   5156  C  C    . GLY   A  1  341 ? 23.633  -18.490 -16.688  1.00 60.03  ? 341  GLY   A C    1 
ATOM   5157  O  O    . GLY   A  1  341 ? 23.878  -19.311 -17.580  1.00 58.90  ? 341  GLY   A O    1 
ATOM   5158  H  H    . GLY   A  1  341 ? 24.180  -16.258 -15.057  1.00 69.91  ? 341  GLY   A H    1 
ATOM   5159  H  HA2  . GLY   A  1  341 ? 25.371  -17.467 -16.461  1.00 67.66  ? 341  GLY   A HA2  1 
ATOM   5160  H  HA3  . GLY   A  1  341 ? 25.249  -18.697 -15.477  1.00 67.66  ? 341  GLY   A HA3  1 
ATOM   5161  N  N    . SER   A  1  342 ? 22.393  -18.066 -16.425  1.00 58.81  ? 342  SER   A N    1 
ATOM   5162  C  CA   . SER   A  1  342 ? 21.266  -18.564 -17.207  1.00 52.11  ? 342  SER   A CA   1 
ATOM   5163  C  C    . SER   A  1  342 ? 21.379  -18.161 -18.670  1.00 51.73  ? 342  SER   A C    1 
ATOM   5164  O  O    . SER   A  1  342 ? 20.895  -18.881 -19.551  1.00 53.75  ? 342  SER   A O    1 
ATOM   5165  C  CB   . SER   A  1  342 ? 19.950  -18.052 -16.620  1.00 51.81  ? 342  SER   A CB   1 
ATOM   5166  O  OG   . SER   A  1  342 ? 19.759  -18.525 -15.299  1.00 53.85  ? 342  SER   A OG   1 
ATOM   5167  H  H    . SER   A  1  342 ? 22.184  -17.501 -15.811  1.00 70.55  ? 342  SER   A H    1 
ATOM   5168  H  HA   . SER   A  1  342 ? 21.260  -19.533 -17.159  1.00 62.51  ? 342  SER   A HA   1 
ATOM   5169  H  HB2  . SER   A  1  342 ? 19.969  -17.082 -16.607  1.00 62.15  ? 342  SER   A HB2  1 
ATOM   5170  H  HB3  . SER   A  1  342 ? 19.217  -18.362 -17.174  1.00 62.15  ? 342  SER   A HB3  1 
ATOM   5171  H  HG   . SER   A  1  342 ? 20.349  -18.208 -14.792  1.00 64.61  ? 342  SER   A HG   1 
ATOM   5172  N  N    . ALA   A  1  343 ? 22.006  -17.021 -18.950  1.00 56.34  ? 343  ALA   A N    1 
ATOM   5173  C  CA   . ALA   A  1  343 ? 22.180  -16.541 -20.313  1.00 56.73  ? 343  ALA   A CA   1 
ATOM   5174  C  C    . ALA   A  1  343 ? 23.582  -15.974 -20.465  1.00 56.67  ? 343  ALA   A C    1 
ATOM   5175  O  O    . ALA   A  1  343 ? 24.070  -15.258 -19.586  1.00 58.30  ? 343  ALA   A O    1 
ATOM   5176  C  CB   . ALA   A  1  343 ? 21.137  -15.475 -20.672  1.00 53.10  ? 343  ALA   A CB   1 
ATOM   5177  H  H    . ALA   A  1  343 ? 22.345  -16.501 -18.355  1.00 67.59  ? 343  ALA   A H    1 
ATOM   5178  H  HA   . ALA   A  1  343 ? 22.080  -17.279 -20.935  1.00 68.06  ? 343  ALA   A HA   1 
ATOM   5179  H  HB1  . ALA   A  1  343 ? 21.277  -15.193 -21.589  1.00 63.70  ? 343  ALA   A HB1  1 
ATOM   5180  H  HB2  . ALA   A  1  343 ? 20.250  -15.856 -20.575  1.00 63.70  ? 343  ALA   A HB2  1 
ATOM   5181  H  HB3  . ALA   A  1  343 ? 21.239  -14.719 -20.074  1.00 63.70  ? 343  ALA   A HB3  1 
ATOM   5182  N  N    . ILE   A  1  344 ? 24.224  -16.302 -21.583  1.00 56.07  ? 344  ILE   A N    1 
ATOM   5183  C  CA   . ILE   A  1  344 ? 25.589  -15.879 -21.875  1.00 56.09  ? 344  ILE   A CA   1 
ATOM   5184  C  C    . ILE   A  1  344 ? 25.585  -15.313 -23.288  1.00 59.48  ? 344  ILE   A C    1 
ATOM   5185  O  O    . ILE   A  1  344 ? 25.347  -16.049 -24.254  1.00 63.27  ? 344  ILE   A O    1 
ATOM   5186  C  CB   . ILE   A  1  344 ? 26.594  -17.031 -21.745  1.00 61.00  ? 344  ILE   A CB   1 
ATOM   5187  C  CG1  . ILE   A  1  344 ? 26.464  -17.692 -20.369  1.00 61.14  ? 344  ILE   A CG1  1 
ATOM   5188  C  CG2  . ILE   A  1  344 ? 28.011  -16.519 -21.961  1.00 63.56  ? 344  ILE   A CG2  1 
ATOM   5189  C  CD1  . ILE   A  1  344 ? 27.277  -18.961 -20.207  1.00 59.75  ? 344  ILE   A CD1  1 
ATOM   5190  H  H    . ILE   A  1  344 ? 23.878  -16.783 -22.206  1.00 67.26  ? 344  ILE   A H    1 
ATOM   5191  H  HA   . ILE   A  1  344 ? 25.853  -15.176 -21.261  1.00 67.29  ? 344  ILE   A HA   1 
ATOM   5192  H  HB   . ILE   A  1  344 ? 26.398  -17.693 -22.426  1.00 73.19  ? 344  ILE   A HB   1 
ATOM   5193  H  HG12 . ILE   A  1  344 ? 26.764  -17.064 -19.693  1.00 73.35  ? 344  ILE   A HG12 1 
ATOM   5194  H  HG13 . ILE   A  1  344 ? 25.533  -17.919 -20.221  1.00 73.35  ? 344  ILE   A HG13 1 
ATOM   5195  H  HG21 . ILE   A  1  344 ? 28.629  -17.264 -21.896  1.00 76.26  ? 344  ILE   A HG21 1 
ATOM   5196  H  HG22 . ILE   A  1  344 ? 28.071  -16.116 -22.841  1.00 76.26  ? 344  ILE   A HG22 1 
ATOM   5197  H  HG23 . ILE   A  1  344 ? 28.215  -15.859 -21.280  1.00 76.26  ? 344  ILE   A HG23 1 
ATOM   5198  H  HD11 . ILE   A  1  344 ? 27.103  -19.337 -19.330  1.00 71.68  ? 344  ILE   A HD11 1 
ATOM   5199  H  HD12 . ILE   A  1  344 ? 27.016  -19.592 -20.895  1.00 71.68  ? 344  ILE   A HD12 1 
ATOM   5200  H  HD13 . ILE   A  1  344 ? 28.218  -18.746 -20.294  1.00 71.68  ? 344  ILE   A HD13 1 
ATOM   5201  N  N    . ALA   A  1  345 ? 25.848  -14.017 -23.412  1.00 60.04  ? 345  ALA   A N    1 
ATOM   5202  C  CA   . ALA   A  1  345 ? 25.735  -13.317 -24.690  1.00 58.01  ? 345  ALA   A CA   1 
ATOM   5203  C  C    . ALA   A  1  345 ? 27.080  -12.760 -25.126  1.00 61.26  ? 345  ALA   A C    1 
ATOM   5204  O  O    . ALA   A  1  345 ? 27.578  -11.800 -24.507  1.00 61.26  ? 345  ALA   A O    1 
ATOM   5205  C  CB   . ALA   A  1  345 ? 24.710  -12.186 -24.585  1.00 56.16  ? 345  ALA   A CB   1 
ATOM   5206  H  H    . ALA   A  1  345 ? 26.097  -13.513 -22.761  1.00 72.03  ? 345  ALA   A H    1 
ATOM   5207  H  HA   . ALA   A  1  345 ? 25.448  -13.953 -25.364  1.00 69.59  ? 345  ALA   A HA   1 
ATOM   5208  H  HB1  . ALA   A  1  345 ? 24.674  -11.713 -25.432  1.00 67.37  ? 345  ALA   A HB1  1 
ATOM   5209  H  HB2  . ALA   A  1  345 ? 23.841  -12.566 -24.381  1.00 67.37  ? 345  ALA   A HB2  1 
ATOM   5210  H  HB3  . ALA   A  1  345 ? 24.980  -11.579 -23.879  1.00 67.37  ? 345  ALA   A HB3  1 
ATOM   5211  N  N    . PRO   A  1  346 ? 27.712  -13.310 -26.162  1.00 62.88  ? 346  PRO   A N    1 
ATOM   5212  C  CA   . PRO   A  1  346 ? 28.869  -12.625 -26.751  1.00 63.15  ? 346  PRO   A CA   1 
ATOM   5213  C  C    . PRO   A  1  346 ? 28.493  -11.211 -27.167  1.00 64.42  ? 346  PRO   A C    1 
ATOM   5214  O  O    . PRO   A  1  346 ? 27.428  -10.975 -27.743  1.00 65.00  ? 346  PRO   A O    1 
ATOM   5215  C  CB   . PRO   A  1  346 ? 29.225  -13.500 -27.958  1.00 62.07  ? 346  PRO   A CB   1 
ATOM   5216  C  CG   . PRO   A  1  346 ? 28.693  -14.852 -27.614  1.00 61.56  ? 346  PRO   A CG   1 
ATOM   5217  C  CD   . PRO   A  1  346 ? 27.450  -14.609 -26.807  1.00 59.19  ? 346  PRO   A CD   1 
ATOM   5218  H  HA   . PRO   A  1  346 ? 29.620  -12.605 -26.138  1.00 75.76  ? 346  PRO   A HA   1 
ATOM   5219  H  HB2  . PRO   A  1  346 ? 28.800  -13.152 -28.757  1.00 74.46  ? 346  PRO   A HB2  1 
ATOM   5220  H  HB3  . PRO   A  1  346 ? 30.187  -13.524 -28.077  1.00 74.46  ? 346  PRO   A HB3  1 
ATOM   5221  H  HG2  . PRO   A  1  346 ? 28.486  -15.339 -28.427  1.00 73.86  ? 346  PRO   A HG2  1 
ATOM   5222  H  HG3  . PRO   A  1  346 ? 29.351  -15.340 -27.093  1.00 73.86  ? 346  PRO   A HG3  1 
ATOM   5223  H  HD2  . PRO   A  1  346 ? 26.670  -14.559 -27.381  1.00 71.00  ? 346  PRO   A HD2  1 
ATOM   5224  H  HD3  . PRO   A  1  346 ? 27.328  -15.306 -26.143  1.00 71.00  ? 346  PRO   A HD3  1 
ATOM   5225  N  N    . LEU   A  1  347 ? 29.378  -10.263 -26.864  1.00 64.75  ? 347  LEU   A N    1 
ATOM   5226  C  CA   . LEU   A  1  347 ? 29.109  -8.849  -27.079  1.00 63.74  ? 347  LEU   A CA   1 
ATOM   5227  C  C    . LEU   A  1  347 ? 29.940  -8.241  -28.198  1.00 61.70  ? 347  LEU   A C    1 
ATOM   5228  O  O    . LEU   A  1  347 ? 29.777  -7.052  -28.495  1.00 60.44  ? 347  LEU   A O    1 
ATOM   5229  C  CB   . LEU   A  1  347 ? 29.370  -8.064  -25.787  1.00 62.90  ? 347  LEU   A CB   1 
ATOM   5230  C  CG   . LEU   A  1  347 ? 28.519  -8.408  -24.566  1.00 63.53  ? 347  LEU   A CG   1 
ATOM   5231  C  CD1  . LEU   A  1  347 ? 28.996  -7.605  -23.365  1.00 63.67  ? 347  LEU   A CD1  1 
ATOM   5232  C  CD2  . LEU   A  1  347 ? 27.051  -8.147  -24.844  1.00 64.23  ? 347  LEU   A CD2  1 
ATOM   5233  H  H    . LEU   A  1  347 ? 30.154  -10.420 -26.528  1.00 77.69  ? 347  LEU   A H    1 
ATOM   5234  H  HA   . LEU   A  1  347 ? 28.174  -8.754  -27.317  1.00 76.47  ? 347  LEU   A HA   1 
ATOM   5235  H  HB2  . LEU   A  1  347 ? 30.295  -8.208  -25.534  1.00 75.46  ? 347  LEU   A HB2  1 
ATOM   5236  H  HB3  . LEU   A  1  347 ? 29.220  -7.124  -25.977  1.00 75.46  ? 347  LEU   A HB3  1 
ATOM   5237  H  HG   . LEU   A  1  347 ? 28.612  -9.352  -24.362  1.00 76.22  ? 347  LEU   A HG   1 
ATOM   5238  H  HD11 . LEU   A  1  347 ? 28.437  -7.817  -22.602  1.00 76.39  ? 347  LEU   A HD11 1 
ATOM   5239  H  HD12 . LEU   A  1  347 ? 29.918  -7.839  -23.175  1.00 76.39  ? 347  LEU   A HD12 1 
ATOM   5240  H  HD13 . LEU   A  1  347 ? 28.930  -6.659  -23.572  1.00 76.39  ? 347  LEU   A HD13 1 
ATOM   5241  H  HD21 . LEU   A  1  347 ? 26.543  -8.309  -24.034  1.00 77.06  ? 347  LEU   A HD21 1 
ATOM   5242  H  HD22 . LEU   A  1  347 ? 26.942  -7.225  -25.124  1.00 77.06  ? 347  LEU   A HD22 1 
ATOM   5243  H  HD23 . LEU   A  1  347 ? 26.752  -8.744  -25.547  1.00 77.06  ? 347  LEU   A HD23 1 
ATOM   5244  N  N    . GLY   A  1  348 ? 30.814  -9.016  -28.832  1.00 61.42  ? 348  GLY   A N    1 
ATOM   5245  C  CA   . GLY   A  1  348 ? 31.814  -8.386  -29.661  1.00 61.02  ? 348  GLY   A CA   1 
ATOM   5246  C  C    . GLY   A  1  348 ? 32.790  -7.637  -28.766  1.00 64.82  ? 348  GLY   A C    1 
ATOM   5247  O  O    . GLY   A  1  348 ? 32.963  -7.950  -27.584  1.00 66.26  ? 348  GLY   A O    1 
ATOM   5248  H  H    . GLY   A  1  348 ? 30.843  -9.874  -28.797  1.00 73.69  ? 348  GLY   A H    1 
ATOM   5249  H  HA2  . GLY   A  1  348 ? 32.296  -9.055  -30.172  1.00 73.21  ? 348  GLY   A HA2  1 
ATOM   5250  H  HA3  . GLY   A  1  348 ? 31.397  -7.761  -30.274  1.00 73.21  ? 348  GLY   A HA3  1 
ATOM   5251  N  N    . ASP   A  1  349 ? 33.429  -6.623  -29.341  1.00 68.83  ? 349  ASP   A N    1 
ATOM   5252  C  CA   . ASP   A  1  349 ? 34.352  -5.771  -28.593  1.00 69.33  ? 349  ASP   A CA   1 
ATOM   5253  C  C    . ASP   A  1  349 ? 33.568  -4.550  -28.119  1.00 68.45  ? 349  ASP   A C    1 
ATOM   5254  O  O    . ASP   A  1  349 ? 33.457  -3.545  -28.821  1.00 72.20  ? 349  ASP   A O    1 
ATOM   5255  C  CB   . ASP   A  1  349 ? 35.556  -5.389  -29.443  1.00 73.82  ? 349  ASP   A CB   1 
ATOM   5256  C  CG   . ASP   A  1  349 ? 36.694  -4.819  -28.617  1.00 76.82  ? 349  ASP   A CG   1 
ATOM   5257  O  OD1  . ASP   A  1  349 ? 36.533  -4.688  -27.384  1.00 76.80  ? 349  ASP   A OD1  1 
ATOM   5258  O  OD2  . ASP   A  1  349 ? 37.753  -4.507  -29.201  1.00 79.20  ? 349  ASP   A OD2  1 
ATOM   5259  H  H    . ASP   A  1  349 ? 33.344  -6.406  -30.169  1.00 82.58  ? 349  ASP   A H    1 
ATOM   5260  H  HA   . ASP   A  1  349 ? 34.678  -6.251  -27.815  1.00 83.18  ? 349  ASP   A HA   1 
ATOM   5261  H  HB2  . ASP   A  1  349 ? 35.883  -6.178  -29.902  1.00 88.57  ? 349  ASP   A HB2  1 
ATOM   5262  H  HB3  . ASP   A  1  349 ? 35.287  -4.717  -30.089  1.00 88.57  ? 349  ASP   A HB3  1 
ATOM   5263  N  N    . LEU   A  1  350 ? 33.027  -4.649  -26.904  1.00 65.77  ? 350  LEU   A N    1 
ATOM   5264  C  CA   . LEU   A  1  350 ? 32.143  -3.605  -26.394  1.00 67.41  ? 350  LEU   A CA   1 
ATOM   5265  C  C    . LEU   A  1  350 ? 32.879  -2.278  -26.248  1.00 71.75  ? 350  LEU   A C    1 
ATOM   5266  O  O    . LEU   A  1  350 ? 32.396  -1.235  -26.704  1.00 71.16  ? 350  LEU   A O    1 
ATOM   5267  C  CB   . LEU   A  1  350 ? 31.546  -4.044  -25.056  1.00 65.35  ? 350  LEU   A CB   1 
ATOM   5268  C  CG   . LEU   A  1  350 ? 30.652  -3.027  -24.343  1.00 67.36  ? 350  LEU   A CG   1 
ATOM   5269  C  CD1  . LEU   A  1  350 ? 29.468  -2.622  -25.208  1.00 67.07  ? 350  LEU   A CD1  1 
ATOM   5270  C  CD2  . LEU   A  1  350 ? 30.178  -3.581  -23.006  1.00 66.22  ? 350  LEU   A CD2  1 
ATOM   5271  H  H    . LEU   A  1  350 ? 33.154  -5.304  -26.362  1.00 78.91  ? 350  LEU   A H    1 
ATOM   5272  H  HA   . LEU   A  1  350 ? 31.417  -3.472  -27.023  1.00 80.87  ? 350  LEU   A HA   1 
ATOM   5273  H  HB2  . LEU   A  1  350 ? 31.008  -4.836  -25.213  1.00 78.41  ? 350  LEU   A HB2  1 
ATOM   5274  H  HB3  . LEU   A  1  350 ? 32.277  -4.253  -24.454  1.00 78.41  ? 350  LEU   A HB3  1 
ATOM   5275  H  HG   . LEU   A  1  350 ? 31.173  -2.226  -24.174  1.00 80.81  ? 350  LEU   A HG   1 
ATOM   5276  H  HD11 . LEU   A  1  350 ? 28.920  -1.990  -24.718  1.00 80.47  ? 350  LEU   A HD11 1 
ATOM   5277  H  HD12 . LEU   A  1  350 ? 29.797  -2.212  -26.023  1.00 80.47  ? 350  LEU   A HD12 1 
ATOM   5278  H  HD13 . LEU   A  1  350 ? 28.948  -3.413  -25.423  1.00 80.47  ? 350  LEU   A HD13 1 
ATOM   5279  H  HD21 . LEU   A  1  350 ? 29.620  -2.919  -22.569  1.00 79.44  ? 350  LEU   A HD21 1 
ATOM   5280  H  HD22 . LEU   A  1  350 ? 29.668  -4.391  -23.163  1.00 79.44  ? 350  LEU   A HD22 1 
ATOM   5281  H  HD23 . LEU   A  1  350 ? 30.951  -3.779  -22.454  1.00 79.44  ? 350  LEU   A HD23 1 
ATOM   5282  N  N    . ASP   A  1  351 ? 34.047  -2.294  -25.613  1.00 76.80  ? 351  ASP   A N    1 
ATOM   5283  C  CA   . ASP   A  1  351 ? 34.816  -1.078  -25.385  1.00 79.96  ? 351  ASP   A CA   1 
ATOM   5284  C  C    . ASP   A  1  351 ? 35.838  -0.804  -26.482  1.00 82.07  ? 351  ASP   A C    1 
ATOM   5285  O  O    . ASP   A  1  351 ? 36.574  0.184   -26.387  1.00 85.21  ? 351  ASP   A O    1 
ATOM   5286  C  CB   . ASP   A  1  351 ? 35.525  -1.147  -24.028  1.00 80.30  ? 351  ASP   A CB   1 
ATOM   5287  C  CG   . ASP   A  1  351 ? 36.387  -2.381  -23.883  1.00 77.93  ? 351  ASP   A CG   1 
ATOM   5288  O  OD1  . ASP   A  1  351 ? 36.027  -3.429  -24.457  1.00 76.33  ? 351  ASP   A OD1  1 
ATOM   5289  O  OD2  . ASP   A  1  351 ? 37.424  -2.300  -23.193  1.00 78.19  ? 351  ASP   A OD2  1 
ATOM   5290  H  H    . ASP   A  1  351 ? 34.418  -3.005  -25.301  1.00 92.14  ? 351  ASP   A H    1 
ATOM   5291  H  HA   . ASP   A  1  351 ? 34.202  -0.327  -25.362  1.00 95.93  ? 351  ASP   A HA   1 
ATOM   5292  H  HB2  . ASP   A  1  351 ? 36.095  -0.369  -23.929  1.00 96.34  ? 351  ASP   A HB2  1 
ATOM   5293  H  HB3  . ASP   A  1  351 ? 34.859  -1.162  -23.324  1.00 96.34  ? 351  ASP   A HB3  1 
ATOM   5294  N  N    . GLN   A  1  352 ? 35.899  -1.643  -27.514  1.00 80.37  ? 352  GLN   A N    1 
ATOM   5295  C  CA   . GLN   A  1  352 ? 36.813  -1.443  -28.636  1.00 81.62  ? 352  GLN   A CA   1 
ATOM   5296  C  C    . GLN   A  1  352 ? 38.253  -1.295  -28.150  1.00 83.62  ? 352  GLN   A C    1 
ATOM   5297  O  O    . GLN   A  1  352 ? 38.985  -0.387  -28.553  1.00 85.39  ? 352  GLN   A O    1 
ATOM   5298  C  CB   . GLN   A  1  352 ? 36.391  -0.232  -29.472  1.00 83.58  ? 352  GLN   A CB   1 
ATOM   5299  C  CG   . GLN   A  1  352 ? 35.100  -0.430  -30.255  1.00 84.30  ? 352  GLN   A CG   1 
ATOM   5300  C  CD   . GLN   A  1  352 ? 35.256  -1.419  -31.396  1.00 82.16  ? 352  GLN   A CD   1 
ATOM   5301  O  OE1  . GLN   A  1  352 ? 35.874  -1.116  -32.417  1.00 80.96  ? 352  GLN   A OE1  1 
ATOM   5302  N  NE2  . GLN   A  1  352 ? 34.694  -2.610  -31.227  1.00 79.52  ? 352  GLN   A NE2  1 
ATOM   5303  H  H    . GLN   A  1  352 ? 35.413  -2.349  -27.588  1.00 96.42  ? 352  GLN   A H    1 
ATOM   5304  H  HA   . GLN   A  1  352 ? 36.775  -2.228  -29.205  1.00 97.92  ? 352  GLN   A HA   1 
ATOM   5305  H  HB2  . GLN   A  1  352 ? 36.260  0.524   -28.878  1.00 100.28 ? 352  GLN   A HB2  1 
ATOM   5306  H  HB3  . GLN   A  1  352 ? 37.094  -0.035  -30.109  1.00 100.28 ? 352  GLN   A HB3  1 
ATOM   5307  H  HG2  . GLN   A  1  352 ? 34.415  -0.767  -29.657  1.00 101.14 ? 352  GLN   A HG2  1 
ATOM   5308  H  HG3  . GLN   A  1  352 ? 34.824  0.420   -30.631  1.00 101.14 ? 352  GLN   A HG3  1 
ATOM   5309  H  HE21 . GLN   A  1  352 ? 34.270  -2.786  -30.500  1.00 95.41  ? 352  GLN   A HE21 1 
ATOM   5310  H  HE22 . GLN   A  1  352 ? 34.755  -3.205  -31.844  1.00 95.41  ? 352  GLN   A HE22 1 
ATOM   5311  N  N    . ASP   A  1  353 ? 38.661  -2.204  -27.266  1.00 82.96  ? 353  ASP   A N    1 
ATOM   5312  C  CA   . ASP   A  1  353 ? 40.034  -2.251  -26.786  1.00 81.80  ? 353  ASP   A CA   1 
ATOM   5313  C  C    . ASP   A  1  353 ? 40.867  -3.318  -27.484  1.00 79.19  ? 353  ASP   A C    1 
ATOM   5314  O  O    . ASP   A  1  353 ? 42.073  -3.401  -27.233  1.00 82.06  ? 353  ASP   A O    1 
ATOM   5315  C  CB   . ASP   A  1  353 ? 40.063  -2.486  -25.271  1.00 82.89  ? 353  ASP   A CB   1 
ATOM   5316  C  CG   . ASP   A  1  353 ? 39.576  -3.870  -24.880  1.00 83.25  ? 353  ASP   A CG   1 
ATOM   5317  O  OD1  . ASP   A  1  353 ? 38.905  -4.531  -25.702  1.00 84.01  ? 353  ASP   A OD1  1 
ATOM   5318  O  OD2  . ASP   A  1  353 ? 39.859  -4.292  -23.739  1.00 83.53  ? 353  ASP   A OD2  1 
ATOM   5319  H  H    . ASP   A  1  353 ? 38.152  -2.809  -26.928  1.00 99.54  ? 353  ASP   A H    1 
ATOM   5320  H  HA   . ASP   A  1  353 ? 40.448  -1.390  -26.959  1.00 98.14  ? 353  ASP   A HA   1 
ATOM   5321  H  HB2  . ASP   A  1  353 ? 40.974  -2.389  -24.953  1.00 99.45  ? 353  ASP   A HB2  1 
ATOM   5322  H  HB3  . ASP   A  1  353 ? 39.490  -1.834  -24.839  1.00 99.45  ? 353  ASP   A HB3  1 
ATOM   5323  N  N    . GLY   A  1  354 ? 40.257  -4.128  -28.348  1.00 74.27  ? 354  GLY   A N    1 
ATOM   5324  C  CA   . GLY   A  1  354 ? 40.954  -5.161  -29.089  1.00 74.49  ? 354  GLY   A CA   1 
ATOM   5325  C  C    . GLY   A  1  354 ? 40.604  -6.572  -28.673  1.00 73.41  ? 354  GLY   A C    1 
ATOM   5326  O  O    . GLY   A  1  354 ? 41.039  -7.521  -29.339  1.00 71.69  ? 354  GLY   A O    1 
ATOM   5327  H  H    . GLY   A  1  354 ? 39.416  -4.093  -28.524  1.00 89.10  ? 354  GLY   A H    1 
ATOM   5328  H  HA2  . GLY   A  1  354 ? 40.742  -5.067  -30.031  1.00 89.37  ? 354  GLY   A HA2  1 
ATOM   5329  H  HA3  . GLY   A  1  354 ? 41.909  -5.043  -28.966  1.00 89.37  ? 354  GLY   A HA3  1 
ATOM   5330  N  N    . PHE   A  1  355 ? 39.837  -6.744  -27.598  1.00 74.16  ? 355  PHE   A N    1 
ATOM   5331  C  CA   . PHE   A  1  355 ? 39.445  -8.056  -27.109  1.00 74.55  ? 355  PHE   A CA   1 
ATOM   5332  C  C    . PHE   A  1  355 ? 37.932  -8.118  -26.987  1.00 72.93  ? 355  PHE   A C    1 
ATOM   5333  O  O    . PHE   A  1  355 ? 37.303  -7.186  -26.478  1.00 71.45  ? 355  PHE   A O    1 
ATOM   5334  C  CB   . PHE   A  1  355 ? 40.090  -8.358  -25.753  1.00 77.11  ? 355  PHE   A CB   1 
ATOM   5335  C  CG   . PHE   A  1  355 ? 41.589  -8.327  -25.781  1.00 79.69  ? 355  PHE   A CG   1 
ATOM   5336  C  CD1  . PHE   A  1  355 ? 42.305  -9.409  -26.261  1.00 78.92  ? 355  PHE   A CD1  1 
ATOM   5337  C  CD2  . PHE   A  1  355 ? 42.283  -7.215  -25.333  1.00 80.55  ? 355  PHE   A CD2  1 
ATOM   5338  C  CE1  . PHE   A  1  355 ? 43.686  -9.384  -26.291  1.00 80.34  ? 355  PHE   A CE1  1 
ATOM   5339  C  CE2  . PHE   A  1  355 ? 43.664  -7.185  -25.360  1.00 79.67  ? 355  PHE   A CE2  1 
ATOM   5340  C  CZ   . PHE   A  1  355 ? 44.366  -8.270  -25.839  1.00 80.52  ? 355  PHE   A CZ   1 
ATOM   5341  H  H    . PHE   A  1  355 ? 39.525  -6.096  -27.126  1.00 88.97  ? 355  PHE   A H    1 
ATOM   5342  H  HA   . PHE   A  1  355 ? 39.728  -8.738  -27.738  1.00 89.44  ? 355  PHE   A HA   1 
ATOM   5343  H  HB2  . PHE   A  1  355 ? 39.792  -7.695  -25.111  1.00 92.52  ? 355  PHE   A HB2  1 
ATOM   5344  H  HB3  . PHE   A  1  355 ? 39.817  -9.243  -25.467  1.00 92.52  ? 355  PHE   A HB3  1 
ATOM   5345  H  HD1  . PHE   A  1  355 ? 41.852  -10.161 -26.566  1.00 94.68  ? 355  PHE   A HD1  1 
ATOM   5346  H  HD2  . PHE   A  1  355 ? 41.813  -6.480  -25.009  1.00 96.64  ? 355  PHE   A HD2  1 
ATOM   5347  H  HE1  . PHE   A  1  355 ? 44.157  -10.118 -26.615  1.00 96.39  ? 355  PHE   A HE1  1 
ATOM   5348  H  HE2  . PHE   A  1  355 ? 44.120  -6.433  -25.055  1.00 95.58  ? 355  PHE   A HE2  1 
ATOM   5349  H  HZ   . PHE   A  1  355 ? 45.296  -8.252  -25.859  1.00 96.61  ? 355  PHE   A HZ   1 
ATOM   5350  N  N    . ASN   A  1  356 ? 37.353  -9.218  -27.457  1.00 74.13  ? 356  ASN   A N    1 
ATOM   5351  C  CA   . ASN   A  1  356 ? 35.916  -9.396  -27.346  1.00 71.55  ? 356  ASN   A CA   1 
ATOM   5352  C  C    . ASN   A  1  356 ? 35.506  -9.506  -25.881  1.00 67.88  ? 356  ASN   A C    1 
ATOM   5353  O  O    . ASN   A  1  356 ? 36.295  -9.875  -25.006  1.00 65.30  ? 356  ASN   A O    1 
ATOM   5354  C  CB   . ASN   A  1  356 ? 35.463  -10.637 -28.111  1.00 68.35  ? 356  ASN   A CB   1 
ATOM   5355  C  CG   . ASN   A  1  356 ? 35.522  -10.448 -29.612  1.00 66.36  ? 356  ASN   A CG   1 
ATOM   5356  O  OD1  . ASN   A  1  356 ? 35.304  -9.347  -30.119  1.00 65.83  ? 356  ASN   A OD1  1 
ATOM   5357  N  ND2  . ASN   A  1  356 ? 35.815  -11.523 -30.332  1.00 67.54  ? 356  ASN   A ND2  1 
ATOM   5358  H  H    . ASN   A  1  356 ? 37.768  -9.868  -27.839  1.00 88.94  ? 356  ASN   A H    1 
ATOM   5359  H  HA   . ASN   A  1  356 ? 35.467  -8.628  -27.733  1.00 85.85  ? 356  ASN   A HA   1 
ATOM   5360  H  HB2  . ASN   A  1  356 ? 36.040  -11.381 -27.878  1.00 82.00  ? 356  ASN   A HB2  1 
ATOM   5361  H  HB3  . ASN   A  1  356 ? 34.545  -10.841 -27.869  1.00 82.00  ? 356  ASN   A HB3  1 
ATOM   5362  H  HD21 . ASN   A  1  356 ? 35.861  -11.467 -31.189  1.00 81.03  ? 356  ASN   A HD21 1 
ATOM   5363  H  HD22 . ASN   A  1  356 ? 35.960  -12.276 -29.942  1.00 81.03  ? 356  ASN   A HD22 1 
ATOM   5364  N  N    . ASP   A  1  357 ? 34.243  -9.186  -25.626  1.00 66.79  ? 357  ASP   A N    1 
ATOM   5365  C  CA   . ASP   A  1  357 ? 33.683  -9.135  -24.285  1.00 66.28  ? 357  ASP   A CA   1 
ATOM   5366  C  C    . ASP   A  1  357 ? 32.440  -10.013 -24.251  1.00 60.94  ? 357  ASP   A C    1 
ATOM   5367  O  O    . ASP   A  1  357 ? 32.053  -10.615 -25.258  1.00 58.65  ? 357  ASP   A O    1 
ATOM   5368  C  CB   . ASP   A  1  357 ? 33.379  -7.686  -23.890  1.00 73.95  ? 357  ASP   A CB   1 
ATOM   5369  C  CG   . ASP   A  1  357 ? 34.560  -6.761  -24.137  1.00 82.04  ? 357  ASP   A CG   1 
ATOM   5370  O  OD1  . ASP   A  1  357 ? 35.694  -7.133  -23.767  1.00 84.76  ? 357  ASP   A OD1  1 
ATOM   5371  O  OD2  . ASP   A  1  357 ? 34.366  -5.673  -24.719  1.00 85.77  ? 357  ASP   A OD2  1 
ATOM   5372  H  H    . ASP   A  1  357 ? 33.671  -8.988  -26.237  1.00 80.13  ? 357  ASP   A H    1 
ATOM   5373  H  HA   . ASP   A  1  357 ? 34.313  -9.492  -23.639  1.00 79.52  ? 357  ASP   A HA   1 
ATOM   5374  H  HB2  . ASP   A  1  357 ? 32.629  -7.364  -24.414  1.00 88.73  ? 357  ASP   A HB2  1 
ATOM   5375  H  HB3  . ASP   A  1  357 ? 33.162  -7.653  -22.945  1.00 88.73  ? 357  ASP   A HB3  1 
ATOM   5376  N  N    . ILE   A  1  358 ? 31.806  -10.098 -23.082  1.00 59.86  ? 358  ILE   A N    1 
ATOM   5377  C  CA   . ILE   A  1  358 ? 30.694  -11.022 -22.901  1.00 60.18  ? 358  ILE   A CA   1 
ATOM   5378  C  C    . ILE   A  1  358 ? 29.826  -10.521 -21.760  1.00 58.42  ? 358  ILE   A C    1 
ATOM   5379  O  O    . ILE   A  1  358 ? 30.312  -9.884  -20.822  1.00 57.35  ? 358  ILE   A O    1 
ATOM   5380  C  CB   . ILE   A  1  358 ? 31.214  -12.459 -22.642  1.00 62.60  ? 358  ILE   A CB   1 
ATOM   5381  C  CG1  . ILE   A  1  358 ? 30.158  -13.493 -23.031  1.00 66.51  ? 358  ILE   A CG1  1 
ATOM   5382  C  CG2  . ILE   A  1  358 ? 31.617  -12.633 -21.180  1.00 61.60  ? 358  ILE   A CG2  1 
ATOM   5383  C  CD1  . ILE   A  1  358 ? 30.743  -14.855 -23.321  1.00 69.42  ? 358  ILE   A CD1  1 
ATOM   5384  H  H    . ILE   A  1  358 ? 32.001  -9.633  -22.386  1.00 71.81  ? 358  ILE   A H    1 
ATOM   5385  H  HA   . ILE   A  1  358 ? 30.151  -11.024 -23.704  1.00 72.19  ? 358  ILE   A HA   1 
ATOM   5386  H  HB   . ILE   A  1  358 ? 31.998  -12.598 -23.196  1.00 75.10  ? 358  ILE   A HB   1 
ATOM   5387  H  HG12 . ILE   A  1  358 ? 29.527  -13.588 -22.301  1.00 79.79  ? 358  ILE   A HG12 1 
ATOM   5388  H  HG13 . ILE   A  1  358 ? 29.699  -13.189 -23.829  1.00 79.79  ? 358  ILE   A HG13 1 
ATOM   5389  H  HG21 . ILE   A  1  358 ? 32.101  -13.467 -21.083  1.00 73.90  ? 358  ILE   A HG21 1 
ATOM   5390  H  HG22 . ILE   A  1  358 ? 32.182  -11.889 -20.918  1.00 73.90  ? 358  ILE   A HG22 1 
ATOM   5391  H  HG23 . ILE   A  1  358 ? 30.816  -12.649 -20.632  1.00 73.90  ? 358  ILE   A HG23 1 
ATOM   5392  H  HD11 . ILE   A  1  358 ? 30.032  -15.450 -23.604  1.00 83.28  ? 358  ILE   A HD11 1 
ATOM   5393  H  HD12 . ILE   A  1  358 ? 31.405  -14.771 -24.026  1.00 83.28  ? 358  ILE   A HD12 1 
ATOM   5394  H  HD13 . ILE   A  1  358 ? 31.161  -15.197 -22.515  1.00 83.28  ? 358  ILE   A HD13 1 
ATOM   5395  N  N    . ALA   A  1  359 ? 28.532  -10.813 -21.847  1.00 58.23  ? 359  ALA   A N    1 
ATOM   5396  C  CA   . ALA   A  1  359 ? 27.574  -10.505 -20.797  1.00 58.64  ? 359  ALA   A CA   1 
ATOM   5397  C  C    . ALA   A  1  359 ? 27.027  -11.802 -20.217  1.00 60.98  ? 359  ALA   A C    1 
ATOM   5398  O  O    . ALA   A  1  359 ? 26.707  -12.737 -20.957  1.00 62.38  ? 359  ALA   A O    1 
ATOM   5399  C  CB   . ALA   A  1  359 ? 26.421  -9.649  -21.328  1.00 55.07  ? 359  ALA   A CB   1 
ATOM   5400  H  H    . ALA   A  1  359 ? 28.176  -11.202 -22.527  1.00 69.86  ? 359  ALA   A H    1 
ATOM   5401  H  HA   . ALA   A  1  359 ? 28.015  -10.008 -20.090  1.00 70.35  ? 359  ALA   A HA   1 
ATOM   5402  H  HB1  . ALA   A  1  359 ? 25.791  -9.486  -20.609  1.00 66.06  ? 359  ALA   A HB1  1 
ATOM   5403  H  HB2  . ALA   A  1  359 ? 26.777  -8.807  -21.653  1.00 66.06  ? 359  ALA   A HB2  1 
ATOM   5404  H  HB3  . ALA   A  1  359 ? 25.983  -10.124 -22.051  1.00 66.06  ? 359  ALA   A HB3  1 
ATOM   5405  N  N    . ILE   A  1  360 ? 26.925  -11.853 -18.892  1.00 59.38  ? 360  ILE   A N    1 
ATOM   5406  C  CA   . ILE   A  1  360 ? 26.357  -12.992 -18.181  1.00 57.60  ? 360  ILE   A CA   1 
ATOM   5407  C  C    . ILE   A  1  360 ? 25.191  -12.482 -17.348  1.00 57.66  ? 360  ILE   A C    1 
ATOM   5408  O  O    . ILE   A  1  360 ? 25.321  -11.478 -16.639  1.00 61.66  ? 360  ILE   A O    1 
ATOM   5409  C  CB   . ILE   A  1  360 ? 27.404  -13.696 -17.299  1.00 59.16  ? 360  ILE   A CB   1 
ATOM   5410  C  CG1  . ILE   A  1  360 ? 28.591  -14.147 -18.157  1.00 59.83  ? 360  ILE   A CG1  1 
ATOM   5411  C  CG2  . ILE   A  1  360 ? 26.774  -14.885 -16.583  1.00 59.09  ? 360  ILE   A CG2  1 
ATOM   5412  C  CD1  . ILE   A  1  360 ? 29.755  -14.712 -17.370  1.00 59.05  ? 360  ILE   A CD1  1 
ATOM   5413  H  H    . ILE   A  1  360 ? 27.186  -11.222 -18.370  1.00 71.24  ? 360  ILE   A H    1 
ATOM   5414  H  HA   . ILE   A  1  360 ? 26.021  -13.641 -18.819  1.00 69.10  ? 360  ILE   A HA   1 
ATOM   5415  H  HB   . ILE   A  1  360 ? 27.725  -13.071 -16.631  1.00 70.97  ? 360  ILE   A HB   1 
ATOM   5416  H  HG12 . ILE   A  1  360 ? 28.287  -14.837 -18.767  1.00 71.78  ? 360  ILE   A HG12 1 
ATOM   5417  H  HG13 . ILE   A  1  360 ? 28.918  -13.383 -18.657  1.00 71.78  ? 360  ILE   A HG13 1 
ATOM   5418  H  HG21 . ILE   A  1  360 ? 27.459  -15.347 -16.075  1.00 70.89  ? 360  ILE   A HG21 1 
ATOM   5419  H  HG22 . ILE   A  1  360 ? 26.081  -14.562 -15.985  1.00 70.89  ? 360  ILE   A HG22 1 
ATOM   5420  H  HG23 . ILE   A  1  360 ? 26.390  -15.484 -17.242  1.00 70.89  ? 360  ILE   A HG23 1 
ATOM   5421  H  HD11 . ILE   A  1  360 ? 30.480  -14.917 -17.982  1.00 70.84  ? 360  ILE   A HD11 1 
ATOM   5422  H  HD12 . ILE   A  1  360 ? 30.047  -14.053 -16.721  1.00 70.84  ? 360  ILE   A HD12 1 
ATOM   5423  H  HD13 . ILE   A  1  360 ? 29.467  -15.519 -16.915  1.00 70.84  ? 360  ILE   A HD13 1 
ATOM   5424  N  N    . ALA   A  1  361 ? 24.058  -13.172 -17.435  1.00 59.80  ? 361  ALA   A N    1 
ATOM   5425  C  CA   . ALA   A  1  361 ? 22.822  -12.724 -16.812  1.00 63.73  ? 361  ALA   A CA   1 
ATOM   5426  C  C    . ALA   A  1  361 ? 22.528  -13.515 -15.545  1.00 65.42  ? 361  ALA   A C    1 
ATOM   5427  O  O    . ALA   A  1  361 ? 22.690  -14.738 -15.506  1.00 59.65  ? 361  ALA   A O    1 
ATOM   5428  C  CB   . ALA   A  1  361 ? 21.648  -12.857 -17.786  1.00 64.86  ? 361  ALA   A CB   1 
ATOM   5429  H  H    . ALA   A  1  361 ? 23.981  -13.917 -17.857  1.00 71.74  ? 361  ALA   A H    1 
ATOM   5430  H  HA   . ALA   A  1  361 ? 22.920  -11.792 -16.562  1.00 76.46  ? 361  ALA   A HA   1 
ATOM   5431  H  HB1  . ALA   A  1  361 ? 20.841  -12.540 -17.351  1.00 77.81  ? 361  ALA   A HB1  1 
ATOM   5432  H  HB2  . ALA   A  1  361 ? 21.831  -12.323 -18.575  1.00 77.81  ? 361  ALA   A HB2  1 
ATOM   5433  H  HB3  . ALA   A  1  361 ? 21.547  -13.789 -18.033  1.00 77.81  ? 361  ALA   A HB3  1 
ATOM   5434  N  N    . ALA   A  1  362 ? 22.105  -12.798 -14.508  1.00 71.05  ? 362  ALA   A N    1 
ATOM   5435  C  CA   . ALA   A  1  362 ? 21.525  -13.383 -13.307  1.00 70.09  ? 362  ALA   A CA   1 
ATOM   5436  C  C    . ALA   A  1  362 ? 20.059  -12.964 -13.269  1.00 66.35  ? 362  ALA   A C    1 
ATOM   5437  O  O    . ALA   A  1  362 ? 19.705  -12.007 -12.568  1.00 66.36  ? 362  ALA   A O    1 
ATOM   5438  C  CB   . ALA   A  1  362 ? 22.268  -12.923 -12.054  1.00 71.09  ? 362  ALA   A CB   1 
ATOM   5439  H  H    . ALA   A  1  362 ? 22.144  -11.939 -14.476  1.00 85.25  ? 362  ALA   A H    1 
ATOM   5440  H  HA   . ALA   A  1  362 ? 21.591  -14.350 -13.321  1.00 84.09  ? 362  ALA   A HA   1 
ATOM   5441  H  HB1  . ALA   A  1  362 ? 21.870  -13.347 -11.278  1.00 85.29  ? 362  ALA   A HB1  1 
ATOM   5442  H  HB2  . ALA   A  1  362 ? 23.201  -13.179 -12.129  1.00 85.29  ? 362  ALA   A HB2  1 
ATOM   5443  H  HB3  . ALA   A  1  362 ? 22.194  -11.959 -11.979  1.00 85.29  ? 362  ALA   A HB3  1 
ATOM   5444  N  N    . PRO   A  1  363 ? 19.182  -13.648 -14.008  1.00 64.37  ? 363  PRO   A N    1 
ATOM   5445  C  CA   . PRO   A  1  363 ? 17.846  -13.085 -14.270  1.00 61.60  ? 363  PRO   A CA   1 
ATOM   5446  C  C    . PRO   A  1  363 ? 16.994  -12.868 -13.032  1.00 60.42  ? 363  PRO   A C    1 
ATOM   5447  O  O    . PRO   A  1  363 ? 16.007  -12.126 -13.110  1.00 63.74  ? 363  PRO   A O    1 
ATOM   5448  C  CB   . PRO   A  1  363 ? 17.204  -14.121 -15.206  1.00 57.46  ? 363  PRO   A CB   1 
ATOM   5449  C  CG   . PRO   A  1  363 ? 18.347  -14.901 -15.773  1.00 58.19  ? 363  PRO   A CG   1 
ATOM   5450  C  CD   . PRO   A  1  363 ? 19.383  -14.934 -14.696  1.00 61.40  ? 363  PRO   A CD   1 
ATOM   5451  H  HA   . PRO   A  1  363 ? 17.943  -12.238 -14.733  1.00 73.90  ? 363  PRO   A HA   1 
ATOM   5452  H  HB2  . PRO   A  1  363 ? 16.609  -14.697 -14.701  1.00 68.93  ? 363  PRO   A HB2  1 
ATOM   5453  H  HB3  . PRO   A  1  363 ? 16.711  -13.669 -15.909  1.00 68.93  ? 363  PRO   A HB3  1 
ATOM   5454  H  HG2  . PRO   A  1  363 ? 18.054  -15.798 -15.997  1.00 69.81  ? 363  PRO   A HG2  1 
ATOM   5455  H  HG3  . PRO   A  1  363 ? 18.688  -14.455 -16.565  1.00 69.81  ? 363  PRO   A HG3  1 
ATOM   5456  H  HD2  . PRO   A  1  363 ? 19.232  -15.678 -14.093  1.00 73.67  ? 363  PRO   A HD2  1 
ATOM   5457  H  HD3  . PRO   A  1  363 ? 20.275  -14.989 -15.075  1.00 73.67  ? 363  PRO   A HD3  1 
ATOM   5458  N  N    . TYR   A  1  364 ? 17.330  -13.483 -11.897  1.00 60.25  ? 364  TYR   A N    1 
ATOM   5459  C  CA   . TYR   A  1  364 ? 16.516  -13.371 -10.690  1.00 63.24  ? 364  TYR   A CA   1 
ATOM   5460  C  C    . TYR   A  1  364 ? 17.267  -12.686 -9.555   1.00 62.89  ? 364  TYR   A C    1 
ATOM   5461  O  O    . TYR   A  1  364 ? 16.878  -12.820 -8.389   1.00 63.60  ? 364  TYR   A O    1 
ATOM   5462  C  CB   . TYR   A  1  364 ? 16.023  -14.754 -10.259  1.00 65.97  ? 364  TYR   A CB   1 
ATOM   5463  C  CG   . TYR   A  1  364 ? 15.378  -15.527 -11.389  1.00 64.86  ? 364  TYR   A CG   1 
ATOM   5464  C  CD1  . TYR   A  1  364 ? 14.091  -15.228 -11.816  1.00 63.71  ? 364  TYR   A CD1  1 
ATOM   5465  C  CD2  . TYR   A  1  364 ? 16.061  -16.548 -12.035  1.00 63.34  ? 364  TYR   A CD2  1 
ATOM   5466  C  CE1  . TYR   A  1  364 ? 13.502  -15.928 -12.853  1.00 62.41  ? 364  TYR   A CE1  1 
ATOM   5467  C  CE2  . TYR   A  1  364 ? 15.480  -17.253 -13.072  1.00 61.35  ? 364  TYR   A CE2  1 
ATOM   5468  C  CZ   . TYR   A  1  364 ? 14.201  -16.940 -13.477  1.00 61.34  ? 364  TYR   A CZ   1 
ATOM   5469  O  OH   . TYR   A  1  364 ? 13.624  -17.643 -14.510  1.00 60.49  ? 364  TYR   A OH   1 
ATOM   5470  H  H    . TYR   A  1  364 ? 18.030  -13.973 -11.802  1.00 72.28  ? 364  TYR   A H    1 
ATOM   5471  H  HA   . TYR   A  1  364 ? 15.739  -12.825 -10.887  1.00 75.87  ? 364  TYR   A HA   1 
ATOM   5472  H  HB2  . TYR   A  1  364 ? 16.777  -15.271 -9.934   1.00 79.14  ? 364  TYR   A HB2  1 
ATOM   5473  H  HB3  . TYR   A  1  364 ? 15.365  -14.648 -9.554   1.00 79.14  ? 364  TYR   A HB3  1 
ATOM   5474  H  HD1  . TYR   A  1  364 ? 13.617  -14.546 -11.398  1.00 76.43  ? 364  TYR   A HD1  1 
ATOM   5475  H  HD2  . TYR   A  1  364 ? 16.926  -16.762 -11.766  1.00 75.98  ? 364  TYR   A HD2  1 
ATOM   5476  H  HE1  . TYR   A  1  364 ? 12.639  -15.717 -13.128  1.00 74.87  ? 364  TYR   A HE1  1 
ATOM   5477  H  HE2  . TYR   A  1  364 ? 15.950  -17.935 -13.494  1.00 73.60  ? 364  TYR   A HE2  1 
ATOM   5478  H  HH   . TYR   A  1  364 ? 14.156  -18.230 -14.790  1.00 72.57  ? 364  TYR   A HH   1 
ATOM   5479  N  N    . GLY   A  1  365 ? 18.329  -11.948 -9.868   1.00 67.43  ? 365  GLY   A N    1 
ATOM   5480  C  CA   . GLY   A  1  365 ? 19.046  -11.173 -8.879   1.00 69.19  ? 365  GLY   A CA   1 
ATOM   5481  C  C    . GLY   A  1  365 ? 18.500  -9.763  -8.754   1.00 69.64  ? 365  GLY   A C    1 
ATOM   5482  O  O    . GLY   A  1  365 ? 17.501  -9.386  -9.371   1.00 69.88  ? 365  GLY   A O    1 
ATOM   5483  H  H    . GLY   A  1  365 ? 18.654  -11.883 -10.661  1.00 80.90  ? 365  GLY   A H    1 
ATOM   5484  H  HA2  . GLY   A  1  365 ? 18.974  -11.608 -8.015   1.00 83.01  ? 365  GLY   A HA2  1 
ATOM   5485  H  HA3  . GLY   A  1  365 ? 19.981  -11.119 -9.129   1.00 83.01  ? 365  GLY   A HA3  1 
ATOM   5486  N  N    . GLY   A  1  366 ? 19.181  -8.970  -7.936   1.00 70.85  ? 366  GLY   A N    1 
ATOM   5487  C  CA   . GLY   A  1  366 ? 18.771  -7.603  -7.709   1.00 71.18  ? 366  GLY   A CA   1 
ATOM   5488  C  C    . GLY   A  1  366 ? 17.607  -7.501  -6.741   1.00 77.37  ? 366  GLY   A C    1 
ATOM   5489  O  O    . GLY   A  1  366 ? 17.178  -8.474  -6.114   1.00 79.94  ? 366  GLY   A O    1 
ATOM   5490  H  H    . GLY   A  1  366 ? 19.885  -9.205  -7.501   1.00 85.00  ? 366  GLY   A H    1 
ATOM   5491  H  HA2  . GLY   A  1  366 ? 19.516  -7.100  -7.345   1.00 85.39  ? 366  GLY   A HA2  1 
ATOM   5492  H  HA3  . GLY   A  1  366 ? 18.503  -7.204  -8.552   1.00 85.39  ? 366  GLY   A HA3  1 
ATOM   5493  N  N    . GLU   A  1  367 ? 17.087  -6.282  -6.630   1.00 83.02  ? 367  GLU   A N    1 
ATOM   5494  C  CA   . GLU   A  1  367 ? 16.003  -5.995  -5.701   1.00 90.10  ? 367  GLU   A CA   1 
ATOM   5495  C  C    . GLU   A  1  367 ? 14.673  -6.450  -6.289   1.00 88.63  ? 367  GLU   A C    1 
ATOM   5496  O  O    . GLU   A  1  367 ? 14.341  -6.116  -7.430   1.00 88.96  ? 367  GLU   A O    1 
ATOM   5497  C  CB   . GLU   A  1  367 ? 15.966  -4.501  -5.385   1.00 99.36  ? 367  GLU   A CB   1 
ATOM   5498  C  CG   . GLU   A  1  367 ? 17.286  -3.953  -4.863   1.00 106.94 ? 367  GLU   A CG   1 
ATOM   5499  C  CD   . GLU   A  1  367 ? 17.260  -2.451  -4.656   1.00 111.83 ? 367  GLU   A CD   1 
ATOM   5500  O  OE1  . GLU   A  1  367 ? 16.496  -1.763  -5.366   1.00 113.35 ? 367  GLU   A OE1  1 
ATOM   5501  O  OE2  . GLU   A  1  367 ? 18.002  -1.958  -3.781   1.00 113.31 ? 367  GLU   A OE2  1 
ATOM   5502  H  H    . GLU   A  1  367 ? 17.348  -5.600  -7.085   1.00 99.60  ? 367  GLU   A H    1 
ATOM   5503  H  HA   . GLU   A  1  367 ? 16.147  -6.479  -4.873   1.00 108.10 ? 367  GLU   A HA   1 
ATOM   5504  H  HB2  . GLU   A  1  367 ? 15.743  -4.016  -6.195   1.00 119.21 ? 367  GLU   A HB2  1 
ATOM   5505  H  HB3  . GLU   A  1  367 ? 15.290  -4.342  -4.707   1.00 119.21 ? 367  GLU   A HB3  1 
ATOM   5506  H  HG2  . GLU   A  1  367 ? 17.485  -4.369  -4.009   1.00 128.30 ? 367  GLU   A HG2  1 
ATOM   5507  H  HG3  . GLU   A  1  367 ? 17.987  -4.156  -5.502   1.00 128.30 ? 367  GLU   A HG3  1 
ATOM   5508  N  N    . ASP   A  1  368 ? 13.914  -7.216  -5.504   1.00 89.37  ? 368  ASP   A N    1 
ATOM   5509  C  CA   . ASP   A  1  368 ? 12.610  -7.728  -5.927   1.00 94.35  ? 368  ASP   A CA   1 
ATOM   5510  C  C    . ASP   A  1  368 ? 12.726  -8.546  -7.212   1.00 89.86  ? 368  ASP   A C    1 
ATOM   5511  O  O    . ASP   A  1  368 ? 11.887  -8.449  -8.111   1.00 89.56  ? 368  ASP   A O    1 
ATOM   5512  C  CB   . ASP   A  1  368 ? 11.601  -6.590  -6.098   1.00 104.65 ? 368  ASP   A CB   1 
ATOM   5513  C  CG   . ASP   A  1  368 ? 11.192  -5.970  -4.776   1.00 113.21 ? 368  ASP   A CG   1 
ATOM   5514  O  OD1  . ASP   A  1  368 ? 12.072  -5.433  -4.069   1.00 115.82 ? 368  ASP   A OD1  1 
ATOM   5515  O  OD2  . ASP   A  1  368 ? 9.988   -6.016  -4.446   1.00 116.12 ? 368  ASP   A OD2  1 
ATOM   5516  H  H    . ASP   A  1  368 ? 14.135  -7.456  -4.708   1.00 107.22 ? 368  ASP   A H    1 
ATOM   5517  H  HA   . ASP   A  1  368 ? 12.277  -8.322  -5.236   1.00 113.21 ? 368  ASP   A HA   1 
ATOM   5518  H  HB2  . ASP   A  1  368 ? 11.998  -5.895  -6.646   1.00 125.56 ? 368  ASP   A HB2  1 
ATOM   5519  H  HB3  . ASP   A  1  368 ? 10.803  -6.935  -6.527   1.00 125.56 ? 368  ASP   A HB3  1 
ATOM   5520  N  N    . LYS   A  1  369 ? 13.776  -9.363  -7.296   1.00 88.28  ? 369  LYS   A N    1 
ATOM   5521  C  CA   . LYS   A  1  369 ? 13.995  -10.255 -8.435   1.00 88.88  ? 369  LYS   A CA   1 
ATOM   5522  C  C    . LYS   A  1  369 ? 13.830  -9.518  -9.762   1.00 87.62  ? 369  LYS   A C    1 
ATOM   5523  O  O    . LYS   A  1  369 ? 13.242  -10.033 -10.715  1.00 92.01  ? 369  LYS   A O    1 
ATOM   5524  C  CB   . LYS   A  1  369 ? 13.055  -11.462 -8.379   1.00 90.66  ? 369  LYS   A CB   1 
ATOM   5525  C  CG   . LYS   A  1  369 ? 13.157  -12.293 -7.111   1.00 90.65  ? 369  LYS   A CG   1 
ATOM   5526  C  CD   . LYS   A  1  369 ? 12.494  -13.652 -7.298   1.00 86.56  ? 369  LYS   A CD   1 
ATOM   5527  C  CE   . LYS   A  1  369 ? 11.716  -14.077 -6.064   1.00 86.66  ? 369  LYS   A CE   1 
ATOM   5528  N  NZ   . LYS   A  1  369 ? 10.540  -13.196 -5.833   1.00 89.86  ? 369  LYS   A NZ   1 
ATOM   5529  H  H    . LYS   A  1  369 ? 14.388  -9.421  -6.694   1.00 105.92 ? 369  LYS   A H    1 
ATOM   5530  H  HA   . LYS   A  1  369 ? 14.909  -10.576 -8.388   1.00 106.64 ? 369  LYS   A HA   1 
ATOM   5531  H  HB2  . LYS   A  1  369 ? 12.141  -11.143 -8.445   1.00 108.78 ? 369  LYS   A HB2  1 
ATOM   5532  H  HB3  . LYS   A  1  369 ? 13.258  -12.045 -9.127   1.00 108.78 ? 369  LYS   A HB3  1 
ATOM   5533  H  HG2  . LYS   A  1  369 ? 14.091  -12.435 -6.892   1.00 108.76 ? 369  LYS   A HG2  1 
ATOM   5534  H  HG3  . LYS   A  1  369 ? 12.712  -11.831 -6.384   1.00 108.76 ? 369  LYS   A HG3  1 
ATOM   5535  H  HD2  . LYS   A  1  369 ? 11.876  -13.607 -8.045   1.00 103.85 ? 369  LYS   A HD2  1 
ATOM   5536  H  HD3  . LYS   A  1  369 ? 13.176  -14.320 -7.472   1.00 103.85 ? 369  LYS   A HD3  1 
ATOM   5537  H  HE2  . LYS   A  1  369 ? 11.399  -14.986 -6.182   1.00 103.98 ? 369  LYS   A HE2  1 
ATOM   5538  H  HE3  . LYS   A  1  369 ? 12.294  -14.025 -5.287   1.00 103.98 ? 369  LYS   A HE3  1 
ATOM   5539  H  HZ1  . LYS   A  1  369 ? 9.940   -13.615 -5.327   1.00 107.82 ? 369  LYS   A HZ1  1 
ATOM   5540  H  HZ2  . LYS   A  1  369 ? 10.795  -12.450 -5.420   1.00 107.82 ? 369  LYS   A HZ2  1 
ATOM   5541  H  HZ3  . LYS   A  1  369 ? 10.163  -12.981 -6.611   1.00 107.82 ? 369  LYS   A HZ3  1 
ATOM   5542  N  N    . LYS   A  1  370 ? 14.352  -8.294  -9.827   1.00 80.33  ? 370  LYS   A N    1 
ATOM   5543  C  CA   . LYS   A  1  370 ? 14.276  -7.507  -11.051  1.00 75.04  ? 370  LYS   A CA   1 
ATOM   5544  C  C    . LYS   A  1  370 ? 15.364  -7.865  -12.056  1.00 74.74  ? 370  LYS   A C    1 
ATOM   5545  O  O    . LYS   A  1  370 ? 15.373  -7.302  -13.155  1.00 79.01  ? 370  LYS   A O    1 
ATOM   5546  C  CB   . LYS   A  1  370 ? 14.351  -6.014  -10.727  1.00 74.97  ? 370  LYS   A CB   1 
ATOM   5547  C  CG   . LYS   A  1  370 ? 13.062  -5.434  -10.166  1.00 77.00  ? 370  LYS   A CG   1 
ATOM   5548  C  CD   . LYS   A  1  370 ? 13.181  -3.930  -9.977   1.00 80.98  ? 370  LYS   A CD   1 
ATOM   5549  C  CE   . LYS   A  1  370 ? 11.962  -3.351  -9.277   1.00 85.97  ? 370  LYS   A CE   1 
ATOM   5550  N  NZ   . LYS   A  1  370 ? 12.098  -1.886  -9.060   1.00 90.30  ? 370  LYS   A NZ   1 
ATOM   5551  H  H    . LYS   A  1  370 ? 14.754  -7.901  -9.176   1.00 96.38  ? 370  LYS   A H    1 
ATOM   5552  H  HA   . LYS   A  1  370 ? 13.417  -7.677  -11.469  1.00 90.03  ? 370  LYS   A HA   1 
ATOM   5553  H  HB2  . LYS   A  1  370 ? 15.048  -5.874  -10.067  1.00 89.94  ? 370  LYS   A HB2  1 
ATOM   5554  H  HB3  . LYS   A  1  370 ? 14.562  -5.530  -11.540  1.00 89.94  ? 370  LYS   A HB3  1 
ATOM   5555  H  HG2  . LYS   A  1  370 ? 12.334  -5.610  -10.782  1.00 92.39  ? 370  LYS   A HG2  1 
ATOM   5556  H  HG3  . LYS   A  1  370 ? 12.874  -5.838  -9.305   1.00 92.39  ? 370  LYS   A HG3  1 
ATOM   5557  H  HD2  . LYS   A  1  370 ? 13.962  -3.735  -9.436   1.00 97.15  ? 370  LYS   A HD2  1 
ATOM   5558  H  HD3  . LYS   A  1  370 ? 13.263  -3.503  -10.844  1.00 97.15  ? 370  LYS   A HD3  1 
ATOM   5559  H  HE2  . LYS   A  1  370 ? 11.175  -3.506  -9.823   1.00 103.15 ? 370  LYS   A HE2  1 
ATOM   5560  H  HE3  . LYS   A  1  370 ? 11.855  -3.779  -8.413   1.00 103.15 ? 370  LYS   A HE3  1 
ATOM   5561  H  HZ1  . LYS   A  1  370 ? 11.385  -1.575  -8.626   1.00 108.34 ? 370  LYS   A HZ1  1 
ATOM   5562  H  HZ2  . LYS   A  1  370 ? 12.826  -1.716  -8.577   1.00 108.34 ? 370  LYS   A HZ2  1 
ATOM   5563  H  HZ3  . LYS   A  1  370 ? 12.165  -1.467  -9.842   1.00 108.34 ? 370  LYS   A HZ3  1 
ATOM   5564  N  N    . GLY   A  1  371 ? 16.271  -8.767  -11.712  1.00 70.18  ? 371  GLY   A N    1 
ATOM   5565  C  CA   . GLY   A  1  371 ? 17.251  -9.258  -12.670  1.00 66.24  ? 371  GLY   A CA   1 
ATOM   5566  C  C    . GLY   A  1  371 ? 18.478  -8.375  -12.762  1.00 64.43  ? 371  GLY   A C    1 
ATOM   5567  O  O    . GLY   A  1  371 ? 18.435  -7.165  -12.542  1.00 64.86  ? 371  GLY   A O    1 
ATOM   5568  H  H    . GLY   A  1  371 ? 16.342  -9.113  -10.927  1.00 84.20  ? 371  GLY   A H    1 
ATOM   5569  H  HA2  . GLY   A  1  371 ? 17.536  -10.148 -12.408  1.00 79.47  ? 371  GLY   A HA2  1 
ATOM   5570  H  HA3  . GLY   A  1  371 ? 16.843  -9.303  -13.549  1.00 79.47  ? 371  GLY   A HA3  1 
ATOM   5571  N  N    . ILE   A  1  372 ? 19.603  -9.006  -13.101  1.00 63.92  ? 372  ILE   A N    1 
ATOM   5572  C  CA   . ILE   A  1  372 ? 20.882  -8.323  -13.243  1.00 66.60  ? 372  ILE   A CA   1 
ATOM   5573  C  C    . ILE   A  1  372 ? 21.635  -8.935  -14.416  1.00 67.30  ? 372  ILE   A C    1 
ATOM   5574  O  O    . ILE   A  1  372 ? 21.534  -10.135 -14.688  1.00 68.29  ? 372  ILE   A O    1 
ATOM   5575  C  CB   . ILE   A  1  372 ? 21.724  -8.407  -11.947  1.00 66.82  ? 372  ILE   A CB   1 
ATOM   5576  C  CG1  . ILE   A  1  372 ? 21.040  -7.617  -10.827  1.00 72.95  ? 372  ILE   A CG1  1 
ATOM   5577  C  CG2  . ILE   A  1  372 ? 23.146  -7.896  -12.185  1.00 64.30  ? 372  ILE   A CG2  1 
ATOM   5578  C  CD1  . ILE   A  1  372 ? 21.789  -7.623  -9.511   1.00 79.24  ? 372  ILE   A CD1  1 
ATOM   5579  H  H    . ILE   A  1  372 ? 19.648  -9.850  -13.257  1.00 76.68  ? 372  ILE   A H    1 
ATOM   5580  H  HA   . ILE   A  1  372 ? 20.724  -7.387  -13.442  1.00 79.90  ? 372  ILE   A HA   1 
ATOM   5581  H  HB   . ILE   A  1  372 ? 21.785  -9.337  -11.679  1.00 80.17  ? 372  ILE   A HB   1 
ATOM   5582  H  HG12 . ILE   A  1  372 ? 20.951  -6.693  -11.109  1.00 87.52  ? 372  ILE   A HG12 1 
ATOM   5583  H  HG13 . ILE   A  1  372 ? 20.164  -8.001  -10.668  1.00 87.52  ? 372  ILE   A HG13 1 
ATOM   5584  H  HG21 . ILE   A  1  372 ? 23.638  -7.927  -11.349  1.00 77.14  ? 372  ILE   A HG21 1 
ATOM   5585  H  HG22 . ILE   A  1  372 ? 23.579  -8.461  -12.845  1.00 77.14  ? 372  ILE   A HG22 1 
ATOM   5586  H  HG23 . ILE   A  1  372 ? 23.104  -6.982  -12.510  1.00 77.14  ? 372  ILE   A HG23 1 
ATOM   5587  H  HD11 . ILE   A  1  372 ? 21.228  -7.228  -8.826   1.00 95.07  ? 372  ILE   A HD11 1 
ATOM   5588  H  HD12 . ILE   A  1  372 ? 22.005  -8.539  -9.275   1.00 95.07  ? 372  ILE   A HD12 1 
ATOM   5589  H  HD13 . ILE   A  1  372 ? 22.604  -7.107  -9.609   1.00 95.07  ? 372  ILE   A HD13 1 
ATOM   5590  N  N    . VAL   A  1  373 ? 22.395  -8.093  -15.114  1.00 65.85  ? 373  VAL   A N    1 
ATOM   5591  C  CA   . VAL   A  1  373 ? 23.272  -8.515  -16.199  1.00 63.53  ? 373  VAL   A CA   1 
ATOM   5592  C  C    . VAL   A  1  373 ? 24.664  -7.971  -15.913  1.00 62.85  ? 373  VAL   A C    1 
ATOM   5593  O  O    . VAL   A  1  373 ? 24.828  -6.769  -15.677  1.00 64.41  ? 373  VAL   A O    1 
ATOM   5594  C  CB   . VAL   A  1  373 ? 22.772  -8.025  -17.572  1.00 62.27  ? 373  VAL   A CB   1 
ATOM   5595  C  CG1  . VAL   A  1  373 ? 23.800  -8.324  -18.661  1.00 61.68  ? 373  VAL   A CG1  1 
ATOM   5596  C  CG2  . VAL   A  1  373 ? 21.438  -8.667  -17.912  1.00 63.32  ? 373  VAL   A CG2  1 
ATOM   5597  H  H    . VAL   A  1  373 ? 22.418  -7.245  -14.971  1.00 79.00  ? 373  VAL   A H    1 
ATOM   5598  H  HA   . VAL   A  1  373 ? 23.313  -9.484  -16.223  1.00 76.22  ? 373  VAL   A HA   1 
ATOM   5599  H  HB   . VAL   A  1  373 ? 22.647  -7.064  -17.531  1.00 74.71  ? 373  VAL   A HB   1 
ATOM   5600  H  HG11 . VAL   A  1  373 ? 23.410  -8.126  -19.526  1.00 74.00  ? 373  VAL   A HG11 1 
ATOM   5601  H  HG12 . VAL   A  1  373 ? 24.583  -7.771  -18.516  1.00 74.00  ? 373  VAL   A HG12 1 
ATOM   5602  H  HG13 . VAL   A  1  373 ? 24.044  -9.262  -18.615  1.00 74.00  ? 373  VAL   A HG13 1 
ATOM   5603  H  HG21 . VAL   A  1  373 ? 21.147  -8.350  -18.781  1.00 75.96  ? 373  VAL   A HG21 1 
ATOM   5604  H  HG22 . VAL   A  1  373 ? 21.547  -9.631  -17.931  1.00 75.96  ? 373  VAL   A HG22 1 
ATOM   5605  H  HG23 . VAL   A  1  373 ? 20.788  -8.422  -17.236  1.00 75.96  ? 373  VAL   A HG23 1 
ATOM   5606  N  N    . TYR   A  1  374 ? 25.659  -8.851  -15.933  1.00 62.35  ? 374  TYR   A N    1 
ATOM   5607  C  CA   . TYR   A  1  374 ? 27.043  -8.474  -15.683  1.00 64.46  ? 374  TYR   A CA   1 
ATOM   5608  C  C    . TYR   A  1  374 ? 27.805  -8.407  -16.999  1.00 63.00  ? 374  TYR   A C    1 
ATOM   5609  O  O    . TYR   A  1  374 ? 27.565  -9.206  -17.909  1.00 60.12  ? 374  TYR   A O    1 
ATOM   5610  C  CB   . TYR   A  1  374 ? 27.716  -9.469  -14.736  1.00 67.91  ? 374  TYR   A CB   1 
ATOM   5611  C  CG   . TYR   A  1  374 ? 27.058  -9.553  -13.376  1.00 70.03  ? 374  TYR   A CG   1 
ATOM   5612  C  CD1  . TYR   A  1  374 ? 27.419  -8.685  -12.355  1.00 70.44  ? 374  TYR   A CD1  1 
ATOM   5613  C  CD2  . TYR   A  1  374 ? 26.076  -10.500 -13.115  1.00 70.64  ? 374  TYR   A CD2  1 
ATOM   5614  C  CE1  . TYR   A  1  374 ? 26.820  -8.757  -11.112  1.00 70.28  ? 374  TYR   A CE1  1 
ATOM   5615  C  CE2  . TYR   A  1  374 ? 25.472  -10.580 -11.875  1.00 68.39  ? 374  TYR   A CE2  1 
ATOM   5616  C  CZ   . TYR   A  1  374 ? 25.848  -9.705  -10.877  1.00 67.73  ? 374  TYR   A CZ   1 
ATOM   5617  O  OH   . TYR   A  1  374 ? 25.251  -9.779  -9.640   1.00 67.42  ? 374  TYR   A OH   1 
ATOM   5618  H  H    . TYR   A  1  374 ? 25.555  -9.689  -16.093  1.00 74.80  ? 374  TYR   A H    1 
ATOM   5619  H  HA   . TYR   A  1  374 ? 27.072  -7.598  -15.268  1.00 77.33  ? 374  TYR   A HA   1 
ATOM   5620  H  HB2  . TYR   A  1  374 ? 27.683  -10.352 -15.136  1.00 81.47  ? 374  TYR   A HB2  1 
ATOM   5621  H  HB3  . TYR   A  1  374 ? 28.638  -9.199  -14.603  1.00 81.47  ? 374  TYR   A HB3  1 
ATOM   5622  H  HD1  . TYR   A  1  374 ? 28.075  -8.044  -12.510  1.00 84.51  ? 374  TYR   A HD1  1 
ATOM   5623  H  HD2  . TYR   A  1  374 ? 25.821  -11.090 -13.787  1.00 84.75  ? 374  TYR   A HD2  1 
ATOM   5624  H  HE1  . TYR   A  1  374 ? 27.072  -8.168  -10.437  1.00 84.31  ? 374  TYR   A HE1  1 
ATOM   5625  H  HE2  . TYR   A  1  374 ? 24.817  -11.219 -11.714  1.00 82.04  ? 374  TYR   A HE2  1 
ATOM   5626  H  HH   . TYR   A  1  374 ? 24.654  -10.370 -9.643   1.00 80.89  ? 374  TYR   A HH   1 
ATOM   5627  N  N    . ILE   A  1  375 ? 28.718  -7.444  -17.095  1.00 66.07  ? 375  ILE   A N    1 
ATOM   5628  C  CA   . ILE   A  1  375 ? 29.546  -7.243  -18.279  1.00 65.90  ? 375  ILE   A CA   1 
ATOM   5629  C  C    . ILE   A  1  375 ? 30.974  -7.623  -17.916  1.00 65.19  ? 375  ILE   A C    1 
ATOM   5630  O  O    . ILE   A  1  375 ? 31.543  -7.085  -16.958  1.00 68.97  ? 375  ILE   A O    1 
ATOM   5631  C  CB   . ILE   A  1  375 ? 29.474  -5.793  -18.784  1.00 67.84  ? 375  ILE   A CB   1 
ATOM   5632  C  CG1  . ILE   A  1  375 ? 28.025  -5.396  -19.085  1.00 71.17  ? 375  ILE   A CG1  1 
ATOM   5633  C  CG2  . ILE   A  1  375 ? 30.344  -5.614  -20.025  1.00 68.23  ? 375  ILE   A CG2  1 
ATOM   5634  C  CD1  . ILE   A  1  375 ? 27.360  -6.227  -20.167  1.00 72.41  ? 375  ILE   A CD1  1 
ATOM   5635  H  H    . ILE   A  1  375 ? 28.880  -6.879  -16.468  1.00 79.27  ? 375  ILE   A H    1 
ATOM   5636  H  HA   . ILE   A  1  375 ? 29.239  -7.828  -18.990  1.00 79.06  ? 375  ILE   A HA   1 
ATOM   5637  H  HB   . ILE   A  1  375 ? 29.812  -5.213  -18.083  1.00 81.39  ? 375  ILE   A HB   1 
ATOM   5638  H  HG12 . ILE   A  1  375 ? 27.502  -5.497  -18.274  1.00 85.38  ? 375  ILE   A HG12 1 
ATOM   5639  H  HG13 . ILE   A  1  375 ? 28.012  -4.470  -19.375  1.00 85.38  ? 375  ILE   A HG13 1 
ATOM   5640  H  HG21 . ILE   A  1  375 ? 30.201  -4.724  -20.385  1.00 81.85  ? 375  ILE   A HG21 1 
ATOM   5641  H  HG22 . ILE   A  1  375 ? 31.276  -5.724  -19.776  1.00 81.85  ? 375  ILE   A HG22 1 
ATOM   5642  H  HG23 . ILE   A  1  375 ? 30.097  -6.281  -20.683  1.00 81.85  ? 375  ILE   A HG23 1 
ATOM   5643  H  HD11 . ILE   A  1  375 ? 26.452  -5.910  -20.296  1.00 86.88  ? 375  ILE   A HD11 1 
ATOM   5644  H  HD12 . ILE   A  1  375 ? 27.863  -6.134  -20.991  1.00 86.88  ? 375  ILE   A HD12 1 
ATOM   5645  H  HD13 . ILE   A  1  375 ? 27.349  -7.157  -19.890  1.00 86.88  ? 375  ILE   A HD13 1 
ATOM   5646  N  N    . PHE   A  1  376 ? 31.551  -8.547  -18.679  1.00 64.07  ? 376  PHE   A N    1 
ATOM   5647  C  CA   . PHE   A  1  376 ? 32.913  -9.019  -18.461  1.00 68.40  ? 376  PHE   A CA   1 
ATOM   5648  C  C    . PHE   A  1  376 ? 33.739  -8.712  -19.699  1.00 68.71  ? 376  PHE   A C    1 
ATOM   5649  O  O    . PHE   A  1  376 ? 33.407  -9.166  -20.800  1.00 67.15  ? 376  PHE   A O    1 
ATOM   5650  C  CB   . PHE   A  1  376 ? 32.935  -10.517 -18.156  1.00 68.53  ? 376  PHE   A CB   1 
ATOM   5651  C  CG   . PHE   A  1  376 ? 32.291  -10.876 -16.851  1.00 69.48  ? 376  PHE   A CG   1 
ATOM   5652  C  CD1  . PHE   A  1  376 ? 30.934  -11.136 -16.780  1.00 68.07  ? 376  PHE   A CD1  1 
ATOM   5653  C  CD2  . PHE   A  1  376 ? 33.045  -10.952 -15.694  1.00 69.93  ? 376  PHE   A CD2  1 
ATOM   5654  C  CE1  . PHE   A  1  376 ? 30.340  -11.465 -15.576  1.00 67.76  ? 376  PHE   A CE1  1 
ATOM   5655  C  CE2  . PHE   A  1  376 ? 32.458  -11.281 -14.489  1.00 69.60  ? 376  PHE   A CE2  1 
ATOM   5656  C  CZ   . PHE   A  1  376 ? 31.103  -11.539 -14.430  1.00 68.71  ? 376  PHE   A CZ   1 
ATOM   5657  H  H    . PHE   A  1  376 ? 31.163  -8.924  -19.348  1.00 76.86  ? 376  PHE   A H    1 
ATOM   5658  H  HA   . PHE   A  1  376 ? 33.302  -8.549  -17.707  1.00 82.06  ? 376  PHE   A HA   1 
ATOM   5659  H  HB2  . PHE   A  1  376 ? 32.459  -10.986 -18.860  1.00 82.22  ? 376  PHE   A HB2  1 
ATOM   5660  H  HB3  . PHE   A  1  376 ? 33.857  -10.816 -18.124  1.00 82.22  ? 376  PHE   A HB3  1 
ATOM   5661  H  HD1  . PHE   A  1  376 ? 30.415  -11.087 -17.550  1.00 81.66  ? 376  PHE   A HD1  1 
ATOM   5662  H  HD2  . PHE   A  1  376 ? 33.958  -10.780 -15.729  1.00 83.90  ? 376  PHE   A HD2  1 
ATOM   5663  H  HE1  . PHE   A  1  376 ? 29.427  -11.638 -15.540  1.00 81.29  ? 376  PHE   A HE1  1 
ATOM   5664  H  HE2  . PHE   A  1  376 ? 32.974  -11.328 -13.717  1.00 83.50  ? 376  PHE   A HE2  1 
ATOM   5665  H  HZ   . PHE   A  1  376 ? 30.705  -11.761 -13.619  1.00 82.43  ? 376  PHE   A HZ   1 
ATOM   5666  N  N    . ASN   A  1  377 ? 34.809  -7.944  -19.518  1.00 68.09  ? 377  ASN   A N    1 
ATOM   5667  C  CA   . ASN   A  1  377 ? 35.690  -7.576  -20.614  1.00 68.33  ? 377  ASN   A CA   1 
ATOM   5668  C  C    . ASN   A  1  377 ? 36.781  -8.623  -20.781  1.00 67.82  ? 377  ASN   A C    1 
ATOM   5669  O  O    . ASN   A  1  377 ? 37.276  -9.186  -19.801  1.00 68.89  ? 377  ASN   A O    1 
ATOM   5670  C  CB   . ASN   A  1  377 ? 36.318  -6.206  -20.366  1.00 70.61  ? 377  ASN   A CB   1 
ATOM   5671  C  CG   . ASN   A  1  377 ? 35.290  -5.101  -20.299  1.00 70.25  ? 377  ASN   A CG   1 
ATOM   5672  O  OD1  . ASN   A  1  377 ? 34.761  -4.796  -19.232  1.00 67.18  ? 377  ASN   A OD1  1 
ATOM   5673  N  ND2  . ASN   A  1  377 ? 34.996  -4.495  -21.442  1.00 73.04  ? 377  ASN   A ND2  1 
ATOM   5674  H  H    . ASN   A  1  377 ? 35.047  -7.620  -18.757  1.00 81.69  ? 377  ASN   A H    1 
ATOM   5675  H  HA   . ASN   A  1  377 ? 35.179  -7.530  -21.437  1.00 81.98  ? 377  ASN   A HA   1 
ATOM   5676  H  HB2  . ASN   A  1  377 ? 36.796  -6.224  -19.522  1.00 84.72  ? 377  ASN   A HB2  1 
ATOM   5677  H  HB3  . ASN   A  1  377 ? 36.932  -6.002  -21.089  1.00 84.72  ? 377  ASN   A HB3  1 
ATOM   5678  H  HD21 . ASN   A  1  377 ? 34.416  -3.860  -21.456  1.00 87.62  ? 377  ASN   A HD21 1 
ATOM   5679  H  HD22 . ASN   A  1  377 ? 35.386  -4.737  -22.170  1.00 87.62  ? 377  ASN   A HD22 1 
ATOM   5680  N  N    . GLY   A  1  378 ? 37.148  -8.882  -22.033  1.00 65.30  ? 378  GLY   A N    1 
ATOM   5681  C  CA   . GLY   A  1  378 ? 38.204  -9.822  -22.322  1.00 64.29  ? 378  GLY   A CA   1 
ATOM   5682  C  C    . GLY   A  1  378 ? 39.572  -9.170  -22.364  1.00 67.76  ? 378  GLY   A C    1 
ATOM   5683  O  O    . GLY   A  1  378 ? 39.706  -7.955  -22.499  1.00 68.95  ? 378  GLY   A O    1 
ATOM   5684  H  H    . GLY   A  1  378 ? 36.796  -8.521  -22.730  1.00 78.34  ? 378  GLY   A H    1 
ATOM   5685  H  HA2  . GLY   A  1  378 ? 38.215  -10.510 -21.638  1.00 77.12  ? 378  GLY   A HA2  1 
ATOM   5686  H  HA3  . GLY   A  1  378 ? 38.037  -10.236 -23.183  1.00 77.12  ? 378  GLY   A HA3  1 
ATOM   5687  N  N    . ARG   A  1  379 ? 40.600  -10.005 -22.238  1.00 70.57  ? 379  ARG   A N    1 
ATOM   5688  C  CA   . ARG   A  1  379 ? 41.980  -9.554  -22.330  1.00 74.09  ? 379  ARG   A CA   1 
ATOM   5689  C  C    . ARG   A  1  379 ? 42.832  -10.725 -22.806  1.00 72.27  ? 379  ARG   A C    1 
ATOM   5690  O  O    . ARG   A  1  379 ? 42.345  -11.847 -22.971  1.00 69.37  ? 379  ARG   A O    1 
ATOM   5691  C  CB   . ARG   A  1  379 ? 42.466  -8.984  -20.993  1.00 80.57  ? 379  ARG   A CB   1 
ATOM   5692  C  CG   . ARG   A  1  379 ? 42.191  -9.861  -19.785  1.00 85.47  ? 379  ARG   A CG   1 
ATOM   5693  C  CD   . ARG   A  1  379 ? 42.626  -9.163  -18.505  1.00 93.00  ? 379  ARG   A CD   1 
ATOM   5694  N  NE   . ARG   A  1  379 ? 42.453  -10.002 -17.323  1.00 98.97  ? 379  ARG   A NE   1 
ATOM   5695  C  CZ   . ARG   A  1  379 ? 42.807  -9.644  -16.093  1.00 102.65 ? 379  ARG   A CZ   1 
ATOM   5696  N  NH1  . ARG   A  1  379 ? 43.358  -8.457  -15.874  1.00 104.46 ? 379  ARG   A NH1  1 
ATOM   5697  N  NH2  . ARG   A  1  379 ? 42.610  -10.474 -15.078  1.00 101.87 ? 379  ARG   A NH2  1 
ATOM   5698  H  H    . ARG   A  1  379 ? 40.520  -10.849 -22.096  1.00 84.66  ? 379  ARG   A H    1 
ATOM   5699  H  HA   . ARG   A  1  379 ? 42.046  -8.847  -22.991  1.00 88.88  ? 379  ARG   A HA   1 
ATOM   5700  H  HB2  . ARG   A  1  379 ? 43.426  -8.853  -21.046  1.00 96.66  ? 379  ARG   A HB2  1 
ATOM   5701  H  HB3  . ARG   A  1  379 ? 42.023  -8.134  -20.843  1.00 96.66  ? 379  ARG   A HB3  1 
ATOM   5702  H  HG2  . ARG   A  1  379 ? 41.240  -10.046 -19.728  1.00 102.55 ? 379  ARG   A HG2  1 
ATOM   5703  H  HG3  . ARG   A  1  379 ? 42.686  -10.691 -19.867  1.00 102.55 ? 379  ARG   A HG3  1 
ATOM   5704  H  HD2  . ARG   A  1  379 ? 43.565  -8.931  -18.574  1.00 111.58 ? 379  ARG   A HD2  1 
ATOM   5705  H  HD3  . ARG   A  1  379 ? 42.094  -8.361  -18.385  1.00 111.58 ? 379  ARG   A HD3  1 
ATOM   5706  H  HE   . ARG   A  1  379 ? 42.099  -10.779 -17.430  1.00 118.75 ? 379  ARG   A HE   1 
ATOM   5707  H  HH11 . ARG   A  1  379 ? 43.488  -7.916  -16.530  1.00 125.33 ? 379  ARG   A HH11 1 
ATOM   5708  H  HH12 . ARG   A  1  379 ? 43.586  -8.229  -15.077  1.00 125.33 ? 379  ARG   A HH12 1 
ATOM   5709  H  HH21 . ARG   A  1  379 ? 42.254  -11.245 -15.215  1.00 122.22 ? 379  ARG   A HH21 1 
ATOM   5710  H  HH22 . ARG   A  1  379 ? 42.839  -10.242 -14.282  1.00 122.22 ? 379  ARG   A HH22 1 
ATOM   5711  N  N    . SER   A  1  380 ? 44.118  -10.450 -23.031  1.00 74.57  ? 380  SER   A N    1 
ATOM   5712  C  CA   . SER   A  1  380 ? 44.989  -11.437 -23.663  1.00 75.61  ? 380  SER   A CA   1 
ATOM   5713  C  C    . SER   A  1  380 ? 45.058  -12.728 -22.856  1.00 70.56  ? 380  SER   A C    1 
ATOM   5714  O  O    . SER   A  1  380 ? 45.148  -13.821 -23.428  1.00 66.10  ? 380  SER   A O    1 
ATOM   5715  C  CB   . SER   A  1  380 ? 46.387  -10.850 -23.854  1.00 77.30  ? 380  SER   A CB   1 
ATOM   5716  O  OG   . SER   A  1  380 ? 46.915  -10.383 -22.624  1.00 80.12  ? 380  SER   A OG   1 
ATOM   5717  H  H    . SER   A  1  380 ? 44.506  -9.709  -22.829  1.00 89.46  ? 380  SER   A H    1 
ATOM   5718  H  HA   . SER   A  1  380 ? 44.625  -11.655 -24.536  1.00 90.71  ? 380  SER   A HA   1 
ATOM   5719  H  HB2  . SER   A  1  380 ? 46.972  -11.538 -24.206  1.00 92.74  ? 380  SER   A HB2  1 
ATOM   5720  H  HB3  . SER   A  1  380 ? 46.335  -10.108 -24.476  1.00 92.74  ? 380  SER   A HB3  1 
ATOM   5721  H  HG   . SER   A  1  380 ? 47.671  -10.041 -22.748  1.00 96.13  ? 380  SER   A HG   1 
ATOM   5722  N  N    . THR   A  1  381 ? 45.021  -12.628 -21.526  1.00 71.51  ? 381  THR   A N    1 
ATOM   5723  C  CA   . THR   A  1  381 ? 45.137  -13.827 -20.702  1.00 76.62  ? 381  THR   A CA   1 
ATOM   5724  C  C    . THR   A  1  381 ? 43.854  -14.648 -20.720  1.00 74.82  ? 381  THR   A C    1 
ATOM   5725  O  O    . THR   A  1  381 ? 43.899  -15.873 -20.559  1.00 73.46  ? 381  THR   A O    1 
ATOM   5726  C  CB   . THR   A  1  381 ? 45.491  -13.450 -19.264  1.00 82.87  ? 381  THR   A CB   1 
ATOM   5727  O  OG1  . THR   A  1  381 ? 44.420  -12.691 -18.689  1.00 87.81  ? 381  THR   A OG1  1 
ATOM   5728  C  CG2  . THR   A  1  381 ? 46.769  -12.626 -19.224  1.00 85.11  ? 381  THR   A CG2  1 
ATOM   5729  H  H    . THR   A  1  381 ? 44.932  -11.894 -21.087  1.00 85.80  ? 381  THR   A H    1 
ATOM   5730  H  HA   . THR   A  1  381 ? 45.854  -14.375 -21.057  1.00 91.92  ? 381  THR   A HA   1 
ATOM   5731  H  HB   . THR   A  1  381 ? 45.632  -14.257 -18.744  1.00 99.42  ? 381  THR   A HB   1 
ATOM   5732  H  HG1  . THR   A  1  381 ? 44.590  -12.517 -17.885  1.00 105.35 ? 381  THR   A HG1  1 
ATOM   5733  H  HG21 . THR   A  1  381 ? 47.002  -12.419 -18.305  1.00 102.11 ? 381  THR   A HG21 1 
ATOM   5734  H  HG22 . THR   A  1  381 ? 47.497  -13.123 -19.629  1.00 102.11 ? 381  THR   A HG22 1 
ATOM   5735  H  HG23 . THR   A  1  381 ? 46.645  -11.797 -19.712  1.00 102.11 ? 381  THR   A HG23 1 
ATOM   5736  N  N    . GLY   A  1  382 ? 42.711  -13.997 -20.912  1.00 75.26  ? 382  GLY   A N    1 
ATOM   5737  C  CA   . GLY   A  1  382 ? 41.432  -14.676 -20.914  1.00 74.51  ? 382  GLY   A CA   1 
ATOM   5738  C  C    . GLY   A  1  382 ? 40.303  -13.694 -20.688  1.00 77.89  ? 382  GLY   A C    1 
ATOM   5739  O  O    . GLY   A  1  382 ? 40.249  -12.647 -21.338  1.00 84.47  ? 382  GLY   A O    1 
ATOM   5740  H  H    . GLY   A  1  382 ? 42.654  -13.149 -21.044  1.00 90.29  ? 382  GLY   A H    1 
ATOM   5741  H  HA2  . GLY   A  1  382 ? 41.297  -15.116 -21.768  1.00 89.39  ? 382  GLY   A HA2  1 
ATOM   5742  H  HA3  . GLY   A  1  382 ? 41.413  -15.342 -20.209  1.00 89.39  ? 382  GLY   A HA3  1 
ATOM   5743  N  N    . LEU   A  1  383 ? 39.399  -14.016 -19.770  1.00 75.87  ? 383  LEU   A N    1 
ATOM   5744  C  CA   . LEU   A  1  383 ? 38.330  -13.110 -19.382  1.00 75.46  ? 383  LEU   A CA   1 
ATOM   5745  C  C    . LEU   A  1  383 ? 38.678  -12.453 -18.054  1.00 74.69  ? 383  LEU   A C    1 
ATOM   5746  O  O    . LEU   A  1  383 ? 39.156  -13.115 -17.128  1.00 75.16  ? 383  LEU   A O    1 
ATOM   5747  C  CB   . LEU   A  1  383 ? 36.995  -13.847 -19.260  1.00 73.74  ? 383  LEU   A CB   1 
ATOM   5748  C  CG   . LEU   A  1  383 ? 35.779  -12.962 -18.978  1.00 73.65  ? 383  LEU   A CG   1 
ATOM   5749  C  CD1  . LEU   A  1  383 ? 35.511  -12.028 -20.151  1.00 75.30  ? 383  LEU   A CD1  1 
ATOM   5750  C  CD2  . LEU   A  1  383 ? 34.557  -13.814 -18.677  1.00 72.22  ? 383  LEU   A CD2  1 
ATOM   5751  H  H    . LEU   A  1  383 ? 39.385  -14.768 -19.352  1.00 91.02  ? 383  LEU   A H    1 
ATOM   5752  H  HA   . LEU   A  1  383 ? 38.229  -12.421 -20.057  1.00 90.53  ? 383  LEU   A HA   1 
ATOM   5753  H  HB2  . LEU   A  1  383 ? 36.827  -14.313 -20.094  1.00 88.47  ? 383  LEU   A HB2  1 
ATOM   5754  H  HB3  . LEU   A  1  383 ? 37.064  -14.484 -18.532  1.00 88.47  ? 383  LEU   A HB3  1 
ATOM   5755  H  HG   . LEU   A  1  383 ? 35.960  -12.414 -18.198  1.00 88.36  ? 383  LEU   A HG   1 
ATOM   5756  H  HD11 . LEU   A  1  383 ? 34.698  -11.528 -19.978  1.00 90.34  ? 383  LEU   A HD11 1 
ATOM   5757  H  HD12 . LEU   A  1  383 ? 36.260  -11.418 -20.246  1.00 90.34  ? 383  LEU   A HD12 1 
ATOM   5758  H  HD13 . LEU   A  1  383 ? 35.410  -12.556 -20.958  1.00 90.34  ? 383  LEU   A HD13 1 
ATOM   5759  H  HD21 . LEU   A  1  383 ? 33.799  -13.232 -18.514  1.00 86.64  ? 383  LEU   A HD21 1 
ATOM   5760  H  HD22 . LEU   A  1  383 ? 34.376  -14.387 -19.438  1.00 86.64  ? 383  LEU   A HD22 1 
ATOM   5761  H  HD23 . LEU   A  1  383 ? 34.735  -14.354 -17.891  1.00 86.64  ? 383  LEU   A HD23 1 
ATOM   5762  N  N    . ASN   A  1  384 ? 38.443  -11.147 -17.968  1.00 74.13  ? 384  ASN   A N    1 
ATOM   5763  C  CA   . ASN   A  1  384 ? 38.627  -10.439 -16.708  1.00 75.40  ? 384  ASN   A CA   1 
ATOM   5764  C  C    . ASN   A  1  384 ? 37.586  -10.930 -15.709  1.00 76.02  ? 384  ASN   A C    1 
ATOM   5765  O  O    . ASN   A  1  384 ? 36.380  -10.795 -15.941  1.00 76.89  ? 384  ASN   A O    1 
ATOM   5766  C  CB   . ASN   A  1  384 ? 38.511  -8.932  -16.920  1.00 78.32  ? 384  ASN   A CB   1 
ATOM   5767  C  CG   . ASN   A  1  384 ? 38.938  -8.138  -15.701  1.00 81.19  ? 384  ASN   A CG   1 
ATOM   5768  O  OD1  . ASN   A  1  384 ? 39.021  -8.672  -14.595  1.00 81.06  ? 384  ASN   A OD1  1 
ATOM   5769  N  ND2  . ASN   A  1  384 ? 39.210  -6.854  -15.897  1.00 85.02  ? 384  ASN   A ND2  1 
ATOM   5770  H  H    . ASN   A  1  384 ? 38.179  -10.653 -18.620  1.00 88.94  ? 384  ASN   A H    1 
ATOM   5771  H  HA   . ASN   A  1  384 ? 39.513  -10.616 -16.355  1.00 90.46  ? 384  ASN   A HA   1 
ATOM   5772  H  HB2  . ASN   A  1  384 ? 39.078  -8.672  -17.663  1.00 93.97  ? 384  ASN   A HB2  1 
ATOM   5773  H  HB3  . ASN   A  1  384 ? 37.587  -8.710  -17.115  1.00 93.97  ? 384  ASN   A HB3  1 
ATOM   5774  H  HD21 . ASN   A  1  384 ? 39.456  -6.360  -15.237  1.00 102.01 ? 384  ASN   A HD21 1 
ATOM   5775  H  HD22 . ASN   A  1  384 ? 39.139  -6.515  -16.684  1.00 102.01 ? 384  ASN   A HD22 1 
ATOM   5776  N  N    . ALA   A  1  385 ? 38.052  -11.505 -14.599  1.00 76.64  ? 385  ALA   A N    1 
ATOM   5777  C  CA   . ALA   A  1  385 ? 37.144  -12.160 -13.666  1.00 74.32  ? 385  ALA   A CA   1 
ATOM   5778  C  C    . ALA   A  1  385 ? 36.218  -11.182 -12.956  1.00 69.40  ? 385  ALA   A C    1 
ATOM   5779  O  O    . ALA   A  1  385 ? 35.199  -11.608 -12.403  1.00 68.31  ? 385  ALA   A O    1 
ATOM   5780  C  CB   . ALA   A  1  385 ? 37.944  -12.953 -12.633  1.00 78.39  ? 385  ALA   A CB   1 
ATOM   5781  H  H    . ALA   A  1  385 ? 38.880  -11.527 -14.367  1.00 91.95  ? 385  ALA   A H    1 
ATOM   5782  H  HA   . ALA   A  1  385 ? 36.589  -12.779 -14.165  1.00 89.17  ? 385  ALA   A HA   1 
ATOM   5783  H  HB1  . ALA   A  1  385 ? 37.328  -13.385 -12.021  1.00 94.04  ? 385  ALA   A HB1  1 
ATOM   5784  H  HB2  . ALA   A  1  385 ? 38.478  -13.620 -13.091  1.00 94.04  ? 385  ALA   A HB2  1 
ATOM   5785  H  HB3  . ALA   A  1  385 ? 38.521  -12.344 -12.146  1.00 94.04  ? 385  ALA   A HB3  1 
ATOM   5786  N  N    . VAL   A  1  386 ? 36.539  -9.897  -12.958  1.00 68.18  ? 386  VAL   A N    1 
ATOM   5787  C  CA   . VAL   A  1  386 ? 35.748  -8.879  -12.270  1.00 69.96  ? 386  VAL   A CA   1 
ATOM   5788  C  C    . VAL   A  1  386 ? 34.854  -8.193  -13.298  1.00 72.02  ? 386  VAL   A C    1 
ATOM   5789  O  O    . VAL   A  1  386 ? 35.365  -7.724  -14.325  1.00 73.53  ? 386  VAL   A O    1 
ATOM   5790  C  CB   . VAL   A  1  386 ? 36.646  -7.851  -11.559  1.00 72.42  ? 386  VAL   A CB   1 
ATOM   5791  C  CG1  . VAL   A  1  386 ? 35.801  -6.870  -10.759  1.00 73.61  ? 386  VAL   A CG1  1 
ATOM   5792  C  CG2  . VAL   A  1  386 ? 37.647  -8.556  -10.657  1.00 72.59  ? 386  VAL   A CG2  1 
ATOM   5793  H  H    . VAL   A  1  386 ? 37.229  -9.579  -13.361  1.00 81.80  ? 386  VAL   A H    1 
ATOM   5794  H  HA   . VAL   A  1  386 ? 35.183  -9.305  -11.607  1.00 83.94  ? 386  VAL   A HA   1 
ATOM   5795  H  HB   . VAL   A  1  386 ? 37.141  -7.350  -12.225  1.00 86.88  ? 386  VAL   A HB   1 
ATOM   5796  H  HG11 . VAL   A  1  386 ? 36.388  -6.256  -10.290  1.00 88.31  ? 386  VAL   A HG11 1 
ATOM   5797  H  HG12 . VAL   A  1  386 ? 35.227  -6.378  -11.368  1.00 88.31  ? 386  VAL   A HG12 1 
ATOM   5798  H  HG13 . VAL   A  1  386 ? 35.262  -7.363  -10.122  1.00 88.31  ? 386  VAL   A HG13 1 
ATOM   5799  H  HG21 . VAL   A  1  386 ? 38.167  -7.890  -10.181  1.00 87.09  ? 386  VAL   A HG21 1 
ATOM   5800  H  HG22 . VAL   A  1  386 ? 37.166  -9.113  -10.025  1.00 87.09  ? 386  VAL   A HG22 1 
ATOM   5801  H  HG23 . VAL   A  1  386 ? 38.232  -9.104  -11.203  1.00 87.09  ? 386  VAL   A HG23 1 
ATOM   5802  N  N    . PRO   A  1  387 ? 33.543  -8.113  -13.072  1.00 71.94  ? 387  PRO   A N    1 
ATOM   5803  C  CA   . PRO   A  1  387 ? 32.682  -7.418  -14.035  1.00 71.71  ? 387  PRO   A CA   1 
ATOM   5804  C  C    . PRO   A  1  387 ? 32.919  -5.917  -14.000  1.00 70.61  ? 387  PRO   A C    1 
ATOM   5805  O  O    . PRO   A  1  387 ? 33.026  -5.310  -12.931  1.00 72.83  ? 387  PRO   A O    1 
ATOM   5806  C  CB   . PRO   A  1  387 ? 31.266  -7.778  -13.573  1.00 70.87  ? 387  PRO   A CB   1 
ATOM   5807  C  CG   . PRO   A  1  387 ? 31.408  -8.060  -12.120  1.00 70.25  ? 387  PRO   A CG   1 
ATOM   5808  C  CD   . PRO   A  1  387 ? 32.773  -8.666  -11.943  1.00 71.10  ? 387  PRO   A CD   1 
ATOM   5809  H  HA   . PRO   A  1  387 ? 32.825  -7.750  -14.935  1.00 86.03  ? 387  PRO   A HA   1 
ATOM   5810  H  HB2  . PRO   A  1  387 ? 30.667  -7.031  -13.726  1.00 85.02  ? 387  PRO   A HB2  1 
ATOM   5811  H  HB3  . PRO   A  1  387 ? 30.950  -8.560  -14.051  1.00 85.02  ? 387  PRO   A HB3  1 
ATOM   5812  H  HG2  . PRO   A  1  387 ? 31.333  -7.233  -11.618  1.00 84.28  ? 387  PRO   A HG2  1 
ATOM   5813  H  HG3  . PRO   A  1  387 ? 30.718  -8.681  -11.839  1.00 84.28  ? 387  PRO   A HG3  1 
ATOM   5814  H  HD2  . PRO   A  1  387 ? 33.162  -8.398  -11.096  1.00 85.30  ? 387  PRO   A HD2  1 
ATOM   5815  H  HD3  . PRO   A  1  387 ? 32.729  -9.634  -11.996  1.00 85.30  ? 387  PRO   A HD3  1 
ATOM   5816  N  N    . SER   A  1  388 ? 33.001  -5.321  -15.186  1.00 68.04  ? 388  SER   A N    1 
ATOM   5817  C  CA   . SER   A  1  388 ? 33.246  -3.892  -15.323  1.00 67.39  ? 388  SER   A CA   1 
ATOM   5818  C  C    . SER   A  1  388 ? 31.962  -3.074  -15.359  1.00 68.16  ? 388  SER   A C    1 
ATOM   5819  O  O    . SER   A  1  388 ? 32.032  -1.842  -15.421  1.00 66.62  ? 388  SER   A O    1 
ATOM   5820  C  CB   . SER   A  1  388 ? 34.058  -3.619  -16.592  1.00 66.82  ? 388  SER   A CB   1 
ATOM   5821  O  OG   . SER   A  1  388 ? 33.335  -4.005  -17.746  1.00 67.35  ? 388  SER   A OG   1 
ATOM   5822  H  H    . SER   A  1  388 ? 32.917  -5.731  -15.937  1.00 81.63  ? 388  SER   A H    1 
ATOM   5823  H  HA   . SER   A  1  388 ? 33.768  -3.594  -14.562  1.00 80.84  ? 388  SER   A HA   1 
ATOM   5824  H  HB2  . SER   A  1  388 ? 34.253  -2.670  -16.643  1.00 80.17  ? 388  SER   A HB2  1 
ATOM   5825  H  HB3  . SER   A  1  388 ? 34.884  -4.126  -16.553  1.00 80.17  ? 388  SER   A HB3  1 
ATOM   5826  H  HG   . SER   A  1  388 ? 33.787  -3.844  -18.436  1.00 80.80  ? 388  SER   A HG   1 
ATOM   5827  N  N    . GLN   A  1  389 ? 30.800  -3.721  -15.324  1.00 69.80  ? 389  GLN   A N    1 
ATOM   5828  C  CA   . GLN   A  1  389 ? 29.534  -3.005  -15.339  1.00 70.64  ? 389  GLN   A CA   1 
ATOM   5829  C  C    . GLN   A  1  389 ? 28.437  -3.946  -14.868  1.00 68.96  ? 389  GLN   A C    1 
ATOM   5830  O  O    . GLN   A  1  389 ? 28.527  -5.164  -15.042  1.00 66.91  ? 389  GLN   A O    1 
ATOM   5831  C  CB   . GLN   A  1  389 ? 29.213  -2.459  -16.734  1.00 72.17  ? 389  GLN   A CB   1 
ATOM   5832  C  CG   . GLN   A  1  389 ? 28.145  -1.379  -16.739  1.00 74.60  ? 389  GLN   A CG   1 
ATOM   5833  C  CD   . GLN   A  1  389 ? 28.047  -0.661  -18.070  1.00 75.02  ? 389  GLN   A CD   1 
ATOM   5834  O  OE1  . GLN   A  1  389 ? 28.683  -1.052  -19.049  1.00 75.72  ? 389  GLN   A OE1  1 
ATOM   5835  N  NE2  . GLN   A  1  389 ? 27.250  0.401   -18.112  1.00 73.62  ? 389  GLN   A NE2  1 
ATOM   5836  H  H    . GLN   A  1  389 ? 30.721  -4.577  -15.292  1.00 83.74  ? 389  GLN   A H    1 
ATOM   5837  H  HA   . GLN   A  1  389 ? 29.578  -2.256  -14.724  1.00 84.75  ? 389  GLN   A HA   1 
ATOM   5838  H  HB2  . GLN   A  1  389 ? 30.020  -2.078  -17.113  1.00 86.59  ? 389  GLN   A HB2  1 
ATOM   5839  H  HB3  . GLN   A  1  389 ? 28.897  -3.189  -17.289  1.00 86.59  ? 389  GLN   A HB3  1 
ATOM   5840  H  HG2  . GLN   A  1  389 ? 27.283  -1.784  -16.553  1.00 89.50  ? 389  GLN   A HG2  1 
ATOM   5841  H  HG3  . GLN   A  1  389 ? 28.356  -0.721  -16.058  1.00 89.50  ? 389  GLN   A HG3  1 
ATOM   5842  H  HE21 . GLN   A  1  389 ? 26.824  0.646   -17.407  1.00 88.32  ? 389  GLN   A HE21 1 
ATOM   5843  H  HE22 . GLN   A  1  389 ? 27.161  0.843   -18.844  1.00 88.32  ? 389  GLN   A HE22 1 
ATOM   5844  N  N    . ILE   A  1  390 ? 27.402  -3.364  -14.269  1.00 70.40  ? 390  ILE   A N    1 
ATOM   5845  C  CA   . ILE   A  1  390 ? 26.266  -4.110  -13.741  1.00 68.08  ? 390  ILE   A CA   1 
ATOM   5846  C  C    . ILE   A  1  390 ? 24.996  -3.432  -14.234  1.00 69.99  ? 390  ILE   A C    1 
ATOM   5847  O  O    . ILE   A  1  390 ? 24.745  -2.266  -13.907  1.00 73.80  ? 390  ILE   A O    1 
ATOM   5848  C  CB   . ILE   A  1  390 ? 26.286  -4.180  -12.204  1.00 69.25  ? 390  ILE   A CB   1 
ATOM   5849  C  CG1  . ILE   A  1  390 ? 27.525  -4.948  -11.731  1.00 69.95  ? 390  ILE   A CG1  1 
ATOM   5850  C  CG2  . ILE   A  1  390 ? 25.012  -4.839  -11.679  1.00 70.25  ? 390  ILE   A CG2  1 
ATOM   5851  C  CD1  . ILE   A  1  390 ? 27.748  -4.908  -10.231  1.00 71.36  ? 390  ILE   A CD1  1 
ATOM   5852  H  H    . ILE   A  1  390 ? 27.334  -2.514  -14.153  1.00 84.47  ? 390  ILE   A H    1 
ATOM   5853  H  HA   . ILE   A  1  390 ? 26.283  -5.016  -14.087  1.00 81.68  ? 390  ILE   A HA   1 
ATOM   5854  H  HB   . ILE   A  1  390 ? 26.327  -3.277  -11.854  1.00 83.08  ? 390  ILE   A HB   1 
ATOM   5855  H  HG12 . ILE   A  1  390 ? 27.431  -5.878  -11.990  1.00 83.92  ? 390  ILE   A HG12 1 
ATOM   5856  H  HG13 . ILE   A  1  390 ? 28.308  -4.563  -12.155  1.00 83.92  ? 390  ILE   A HG13 1 
ATOM   5857  H  HG21 . ILE   A  1  390 ? 25.071  -4.915  -10.714  1.00 84.28  ? 390  ILE   A HG21 1 
ATOM   5858  H  HG22 . ILE   A  1  390 ? 24.250  -4.291  -11.922  1.00 84.28  ? 390  ILE   A HG22 1 
ATOM   5859  H  HG23 . ILE   A  1  390 ? 24.926  -5.720  -12.075  1.00 84.28  ? 390  ILE   A HG23 1 
ATOM   5860  H  HD11 . ILE   A  1  390 ? 28.565  -5.386  -10.021  1.00 85.62  ? 390  ILE   A HD11 1 
ATOM   5861  H  HD12 . ILE   A  1  390 ? 27.823  -3.984  -9.947   1.00 85.62  ? 390  ILE   A HD12 1 
ATOM   5862  H  HD13 . ILE   A  1  390 ? 26.995  -5.330  -9.789   1.00 85.62  ? 390  ILE   A HD13 1 
ATOM   5863  N  N    . LEU   A  1  391 ? 24.203  -4.156  -15.016  1.00 69.53  ? 391  LEU   A N    1 
ATOM   5864  C  CA   . LEU   A  1  391 ? 22.931  -3.661  -15.523  1.00 67.69  ? 391  LEU   A CA   1 
ATOM   5865  C  C    . LEU   A  1  391 ? 21.802  -4.234  -14.678  1.00 72.07  ? 391  LEU   A C    1 
ATOM   5866  O  O    . LEU   A  1  391 ? 21.761  -5.443  -14.428  1.00 74.67  ? 391  LEU   A O    1 
ATOM   5867  C  CB   . LEU   A  1  391 ? 22.740  -4.040  -16.992  1.00 66.18  ? 391  LEU   A CB   1 
ATOM   5868  C  CG   . LEU   A  1  391 ? 23.573  -3.287  -18.032  1.00 71.49  ? 391  LEU   A CG   1 
ATOM   5869  C  CD1  . LEU   A  1  391 ? 25.063  -3.539  -17.862  1.00 75.72  ? 391  LEU   A CD1  1 
ATOM   5870  C  CD2  . LEU   A  1  391 ? 23.126  -3.682  -19.431  1.00 73.17  ? 391  LEU   A CD2  1 
ATOM   5871  H  H    . LEU   A  1  391 ? 24.385  -4.957  -15.272  1.00 83.41  ? 391  LEU   A H    1 
ATOM   5872  H  HA   . LEU   A  1  391 ? 22.909  -2.693  -15.459  1.00 81.21  ? 391  LEU   A HA   1 
ATOM   5873  H  HB2  . LEU   A  1  391 ? 22.958  -4.981  -17.086  1.00 79.40  ? 391  LEU   A HB2  1 
ATOM   5874  H  HB3  . LEU   A  1  391 ? 21.808  -3.892  -17.217  1.00 79.40  ? 391  LEU   A HB3  1 
ATOM   5875  H  HG   . LEU   A  1  391 ? 23.433  -2.335  -17.907  1.00 85.77  ? 391  LEU   A HG   1 
ATOM   5876  H  HD11 . LEU   A  1  391 ? 25.541  -3.116  -18.592  1.00 90.84  ? 391  LEU   A HD11 1 
ATOM   5877  H  HD12 . LEU   A  1  391 ? 25.353  -3.163  -17.016  1.00 90.84  ? 391  LEU   A HD12 1 
ATOM   5878  H  HD13 . LEU   A  1  391 ? 25.225  -4.496  -17.871  1.00 90.84  ? 391  LEU   A HD13 1 
ATOM   5879  H  HD21 . LEU   A  1  391 ? 23.673  -3.214  -20.081  1.00 87.79  ? 391  LEU   A HD21 1 
ATOM   5880  H  HD22 . LEU   A  1  391 ? 23.231  -4.640  -19.537  1.00 87.79  ? 391  LEU   A HD22 1 
ATOM   5881  H  HD23 . LEU   A  1  391 ? 22.194  -3.437  -19.545  1.00 87.79  ? 391  LEU   A HD23 1 
ATOM   5882  N  N    . GLU   A  1  392 ? 20.894  -3.367  -14.241  1.00 72.80  ? 392  GLU   A N    1 
ATOM   5883  C  CA   . GLU   A  1  392 ? 19.782  -3.754  -13.388  1.00 72.43  ? 392  GLU   A CA   1 
ATOM   5884  C  C    . GLU   A  1  392 ? 18.463  -3.459  -14.090  1.00 71.93  ? 392  GLU   A C    1 
ATOM   5885  O  O    . GLU   A  1  392 ? 18.345  -2.489  -14.844  1.00 73.85  ? 392  GLU   A O    1 
ATOM   5886  C  CB   . GLU   A  1  392 ? 19.826  -3.010  -12.047  1.00 76.65  ? 392  GLU   A CB   1 
ATOM   5887  C  CG   . GLU   A  1  392 ? 21.128  -3.175  -11.281  1.00 83.02  ? 392  GLU   A CG   1 
ATOM   5888  C  CD   . GLU   A  1  392 ? 21.240  -2.215  -10.114  1.00 90.78  ? 392  GLU   A CD   1 
ATOM   5889  O  OE1  . GLU   A  1  392 ? 21.347  -0.995  -10.357  1.00 94.09  ? 392  GLU   A OE1  1 
ATOM   5890  O  OE2  . GLU   A  1  392 ? 21.212  -2.680  -8.955   1.00 94.13  ? 392  GLU   A OE2  1 
ATOM   5891  H  H    . GLU   A  1  392 ? 20.904  -2.528  -14.431  1.00 87.34  ? 392  GLU   A H    1 
ATOM   5892  H  HA   . GLU   A  1  392 ? 19.827  -4.706  -13.212  1.00 86.90  ? 392  GLU   A HA   1 
ATOM   5893  H  HB2  . GLU   A  1  392 ? 19.702  -2.062  -12.214  1.00 91.96  ? 392  GLU   A HB2  1 
ATOM   5894  H  HB3  . GLU   A  1  392 ? 19.110  -3.344  -11.484  1.00 91.96  ? 392  GLU   A HB3  1 
ATOM   5895  H  HG2  . GLU   A  1  392 ? 21.179  -4.079  -10.933  1.00 99.60  ? 392  GLU   A HG2  1 
ATOM   5896  H  HG3  . GLU   A  1  392 ? 21.872  -3.008  -11.881  1.00 99.60  ? 392  GLU   A HG3  1 
ATOM   5897  N  N    . GLY   A  1  393 ? 17.472  -4.310  -13.835  1.00 69.43  ? 393  GLY   A N    1 
ATOM   5898  C  CA   . GLY   A  1  393 ? 16.136  -4.100  -14.362  1.00 69.95  ? 393  GLY   A CA   1 
ATOM   5899  C  C    . GLY   A  1  393 ? 15.316  -3.226  -13.427  1.00 73.09  ? 393  GLY   A C    1 
ATOM   5900  O  O    . GLY   A  1  393 ? 15.404  -3.344  -12.206  1.00 73.52  ? 393  GLY   A O    1 
ATOM   5901  H  H    . GLY   A  1  393 ? 17.553  -5.019  -13.355  1.00 83.30  ? 393  GLY   A H    1 
ATOM   5902  H  HA2  . GLY   A  1  393 ? 16.191  -3.666  -15.227  1.00 83.92  ? 393  GLY   A HA2  1 
ATOM   5903  H  HA3  . GLY   A  1  393 ? 15.687  -4.954  -14.465  1.00 83.92  ? 393  GLY   A HA3  1 
ATOM   5904  N  N    . GLN   A  1  394 ? 14.516  -2.344  -14.021  1.00 75.90  ? 394  GLN   A N    1 
ATOM   5905  C  CA   . GLN   A  1  394 ? 13.725  -1.380  -13.270  1.00 79.78  ? 394  GLN   A CA   1 
ATOM   5906  C  C    . GLN   A  1  394 ? 12.266  -1.790  -13.121  1.00 79.58  ? 394  GLN   A C    1 
ATOM   5907  O  O    . GLN   A  1  394 ? 11.493  -1.054  -12.499  1.00 82.40  ? 394  GLN   A O    1 
ATOM   5908  C  CB   . GLN   A  1  394 ? 13.789  -0.004  -13.946  1.00 83.36  ? 394  GLN   A CB   1 
ATOM   5909  C  CG   . GLN   A  1  394 ? 15.143  0.349   -14.542  1.00 85.30  ? 394  GLN   A CG   1 
ATOM   5910  C  CD   . GLN   A  1  394 ? 16.234  0.442   -13.495  1.00 89.62  ? 394  GLN   A CD   1 
ATOM   5911  O  OE1  . GLN   A  1  394 ? 15.959  0.603   -12.306  1.00 91.20  ? 394  GLN   A OE1  1 
ATOM   5912  N  NE2  . GLN   A  1  394 ? 17.483  0.338   -13.933  1.00 91.99  ? 394  GLN   A NE2  1 
ATOM   5913  H  H    . GLN   A  1  394 ? 14.415  -2.285  -14.873  1.00 91.06  ? 394  GLN   A H    1 
ATOM   5914  H  HA   . GLN   A  1  394 ? 14.107  -1.303  -12.382  1.00 95.72  ? 394  GLN   A HA   1 
ATOM   5915  H  HB2  . GLN   A  1  394 ? 13.139  0.016   -14.666  1.00 100.01 ? 394  GLN   A HB2  1 
ATOM   5916  H  HB3  . GLN   A  1  394 ? 13.574  0.674   -13.287  1.00 100.01 ? 394  GLN   A HB3  1 
ATOM   5917  H  HG2  . GLN   A  1  394 ? 15.396  -0.336  -15.180  1.00 102.34 ? 394  GLN   A HG2  1 
ATOM   5918  H  HG3  . GLN   A  1  394 ? 15.078  1.209   -14.986  1.00 102.34 ? 394  GLN   A HG3  1 
ATOM   5919  H  HE21 . GLN   A  1  394 ? 17.636  0.224   -14.772  1.00 110.37 ? 394  GLN   A HE21 1 
ATOM   5920  H  HE22 . GLN   A  1  394 ? 18.138  0.385   -13.379  1.00 110.37 ? 394  GLN   A HE22 1 
ATOM   5921  N  N    . TRP   A  1  395 ? 11.869  -2.935  -13.670  1.00 75.97  ? 395  TRP   A N    1 
ATOM   5922  C  CA   . TRP   A  1  395 ? 10.467  -3.316  -13.765  1.00 75.95  ? 395  TRP   A CA   1 
ATOM   5923  C  C    . TRP   A  1  395 ? 10.173  -4.529  -12.895  1.00 76.54  ? 395  TRP   A C    1 
ATOM   5924  O  O    . TRP   A  1  395 ? 10.943  -5.495  -12.872  1.00 78.05  ? 395  TRP   A O    1 
ATOM   5925  C  CB   . TRP   A  1  395 ? 10.092  -3.609  -15.219  1.00 79.46  ? 395  TRP   A CB   1 
ATOM   5926  C  CG   . TRP   A  1  395 ? 10.439  -2.477  -16.128  1.00 87.19  ? 395  TRP   A CG   1 
ATOM   5927  C  CD1  . TRP   A  1  395 ? 9.634   -1.435  -16.482  1.00 94.95  ? 395  TRP   A CD1  1 
ATOM   5928  C  CD2  . TRP   A  1  395 ? 11.692  -2.259  -16.786  1.00 87.16  ? 395  TRP   A CD2  1 
ATOM   5929  N  NE1  . TRP   A  1  395 ? 10.307  -0.584  -17.325  1.00 97.79  ? 395  TRP   A NE1  1 
ATOM   5930  C  CE2  . TRP   A  1  395 ? 11.573  -1.068  -17.527  1.00 92.50  ? 395  TRP   A CE2  1 
ATOM   5931  C  CE3  . TRP   A  1  395 ? 12.903  -2.958  -16.822  1.00 84.22  ? 395  TRP   A CE3  1 
ATOM   5932  C  CZ2  . TRP   A  1  395 ? 12.618  -0.559  -18.298  1.00 91.79  ? 395  TRP   A CZ2  1 
ATOM   5933  C  CZ3  . TRP   A  1  395 ? 13.940  -2.452  -17.587  1.00 86.08  ? 395  TRP   A CZ3  1 
ATOM   5934  C  CH2  . TRP   A  1  395 ? 13.790  -1.264  -18.314  1.00 88.96  ? 395  TRP   A CH2  1 
ATOM   5935  H  H    . TRP   A  1  395 ? 12.407  -3.518  -14.002  1.00 91.15  ? 395  TRP   A H    1 
ATOM   5936  H  HA   . TRP   A  1  395 ? 9.915   -2.589  -13.437  1.00 91.12  ? 395  TRP   A HA   1 
ATOM   5937  H  HB2  . TRP   A  1  395 ? 10.572  -4.397  -15.519  1.00 95.33  ? 395  TRP   A HB2  1 
ATOM   5938  H  HB3  . TRP   A  1  395 ? 9.136   -3.762  -15.277  1.00 95.33  ? 395  TRP   A HB3  1 
ATOM   5939  H  HD1  . TRP   A  1  395 ? 8.758   -1.317  -16.195  1.00 113.93 ? 395  TRP   A HD1  1 
ATOM   5940  H  HE1  . TRP   A  1  395 ? 9.986   0.136   -17.670  1.00 117.32 ? 395  TRP   A HE1  1 
ATOM   5941  H  HE3  . TRP   A  1  395 ? 13.010  -3.748  -16.342  1.00 101.04 ? 395  TRP   A HE3  1 
ATOM   5942  H  HZ2  . TRP   A  1  395 ? 12.522  0.229   -18.782  1.00 110.12 ? 395  TRP   A HZ2  1 
ATOM   5943  H  HZ3  . TRP   A  1  395 ? 14.750  -2.908  -17.620  1.00 103.28 ? 395  TRP   A HZ3  1 
ATOM   5944  H  HH2  . TRP   A  1  395 ? 14.504  -0.947  -18.818  1.00 106.73 ? 395  TRP   A HH2  1 
ATOM   5945  N  N    . ALA   A  1  396 ? 9.050   -4.467  -12.183  1.00 76.95  ? 396  ALA   A N    1 
ATOM   5946  C  CA   . ALA   A  1  396 ? 8.563   -5.558  -11.355  1.00 81.67  ? 396  ALA   A CA   1 
ATOM   5947  C  C    . ALA   A  1  396 ? 7.202   -6.008  -11.869  1.00 87.17  ? 396  ALA   A C    1 
ATOM   5948  O  O    . ALA   A  1  396 ? 6.443   -5.216  -12.436  1.00 89.94  ? 396  ALA   A O    1 
ATOM   5949  C  CB   . ALA   A  1  396 ? 8.459   -5.134  -9.885   1.00 80.83  ? 396  ALA   A CB   1 
ATOM   5950  H  H    . ALA   A  1  396 ? 8.538   -3.777  -12.166  1.00 92.32  ? 396  ALA   A H    1 
ATOM   5951  H  HA   . ALA   A  1  396 ? 9.173   -6.311  -11.404  1.00 97.98  ? 396  ALA   A HA   1 
ATOM   5952  H  HB1  . ALA   A  1  396 ? 8.170   -5.895  -9.357   1.00 96.98  ? 396  ALA   A HB1  1 
ATOM   5953  H  HB2  . ALA   A  1  396 ? 9.329   -4.831  -9.581   1.00 96.98  ? 396  ALA   A HB2  1 
ATOM   5954  H  HB3  . ALA   A  1  396 ? 7.813   -4.414  -9.809   1.00 96.98  ? 396  ALA   A HB3  1 
ATOM   5955  N  N    . ALA   A  1  397 ? 6.900   -7.288  -11.671  1.00 91.19  ? 397  ALA   A N    1 
ATOM   5956  C  CA   . ALA   A  1  397 ? 5.666   -7.897  -12.153  1.00 100.12 ? 397  ALA   A CA   1 
ATOM   5957  C  C    . ALA   A  1  397 ? 4.917   -8.545  -10.991  1.00 105.94 ? 397  ALA   A C    1 
ATOM   5958  O  O    . ALA   A  1  397 ? 5.365   -8.521  -9.842   1.00 105.26 ? 397  ALA   A O    1 
ATOM   5959  C  CB   . ALA   A  1  397 ? 5.962   -8.920  -13.254  1.00 102.79 ? 397  ALA   A CB   1 
ATOM   5960  H  H    . ALA   A  1  397 ? 7.408   -7.837  -11.247  1.00 109.41 ? 397  ALA   A H    1 
ATOM   5961  H  HA   . ALA   A  1  397 ? 5.099   -7.203  -12.525  1.00 120.13 ? 397  ALA   A HA   1 
ATOM   5962  H  HB1  . ALA   A  1  397 ? 5.422   -8.711  -14.033  1.00 123.32 ? 397  ALA   A HB1  1 
ATOM   5963  H  HB2  . ALA   A  1  397 ? 6.903   -8.874  -13.483  1.00 123.32 ? 397  ALA   A HB2  1 
ATOM   5964  H  HB3  . ALA   A  1  397 ? 5.743   -9.807  -12.928  1.00 123.32 ? 397  ALA   A HB3  1 
ATOM   5965  N  N    . ARG   A  1  398 ? 3.756   -9.134  -11.302  1.00 111.60 ? 398  ARG   A N    1 
ATOM   5966  C  CA   . ARG   A  1  398 ? 2.904   -9.739  -10.288  1.00 113.44 ? 398  ARG   A CA   1 
ATOM   5967  C  C    . ARG   A  1  398 ? 2.497   -11.179 -10.579  1.00 110.42 ? 398  ARG   A C    1 
ATOM   5968  O  O    . ARG   A  1  398 ? 1.820   -11.786 -9.742   1.00 113.47 ? 398  ARG   A O    1 
ATOM   5969  C  CB   . ARG   A  1  398 ? 1.629   -8.900  -10.092  1.00 118.43 ? 398  ARG   A CB   1 
ATOM   5970  C  CG   . ARG   A  1  398 ? 1.795   -7.750  -9.113   1.00 125.59 ? 398  ARG   A CG   1 
ATOM   5971  C  CD   . ARG   A  1  398 ? 0.527   -6.919  -8.981   1.00 133.43 ? 398  ARG   A CD   1 
ATOM   5972  N  NE   . ARG   A  1  398 ? 0.020   -6.465  -10.273  1.00 137.29 ? 398  ARG   A NE   1 
ATOM   5973  C  CZ   . ARG   A  1  398 ? 0.612   -5.551  -11.034  1.00 137.61 ? 398  ARG   A CZ   1 
ATOM   5974  N  NH1  . ARG   A  1  398 ? 1.751   -4.991  -10.648  1.00 137.27 ? 398  ARG   A NH1  1 
ATOM   5975  N  NH2  . ARG   A  1  398 ? 0.069   -5.203  -12.192  1.00 137.43 ? 398  ARG   A NH2  1 
ATOM   5976  H  H    . ARG   A  1  398 ? 3.443   -9.193  -12.101  1.00 133.90 ? 398  ARG   A H    1 
ATOM   5977  H  HA   . ARG   A  1  398 ? 3.401   -9.746  -9.455   1.00 136.11 ? 398  ARG   A HA   1 
ATOM   5978  H  HB2  . ARG   A  1  398 ? 1.370   -8.524  -10.948  1.00 142.10 ? 398  ARG   A HB2  1 
ATOM   5979  H  HB3  . ARG   A  1  398 ? 0.925   -9.476  -9.756   1.00 142.10 ? 398  ARG   A HB3  1 
ATOM   5980  H  HG2  . ARG   A  1  398 ? 2.014   -8.106  -8.238   1.00 150.69 ? 398  ARG   A HG2  1 
ATOM   5981  H  HG3  . ARG   A  1  398 ? 2.506   -7.168  -9.422   1.00 150.69 ? 398  ARG   A HG3  1 
ATOM   5982  H  HD2  . ARG   A  1  398 ? -0.162  -7.455  -8.558   1.00 160.09 ? 398  ARG   A HD2  1 
ATOM   5983  H  HD3  . ARG   A  1  398 ? 0.716   -6.136  -8.440   1.00 160.09 ? 398  ARG   A HD3  1 
ATOM   5984  H  HE   . ARG   A  1  398 ? -0.712  -6.813  -10.560  1.00 164.73 ? 398  ARG   A HE   1 
ATOM   5985  H  HH11 . ARG   A  1  398 ? 2.111   -5.218  -9.901   1.00 164.70 ? 398  ARG   A HH11 1 
ATOM   5986  H  HH12 . ARG   A  1  398 ? 2.130   -4.400  -11.145  1.00 164.70 ? 398  ARG   A HH12 1 
ATOM   5987  H  HH21 . ARG   A  1  398 ? -0.666  -5.568  -12.449  1.00 164.90 ? 398  ARG   A HH21 1 
ATOM   5988  H  HH22 . ARG   A  1  398 ? 0.451   -4.611  -12.686  1.00 164.90 ? 398  ARG   A HH22 1 
ATOM   5989  N  N    . SER   A  1  399 ? 2.877   -11.743 -11.727  1.00 105.26 ? 399  SER   A N    1 
ATOM   5990  C  CA   . SER   A  1  399 ? 2.512   -13.115 -12.069  1.00 104.11 ? 399  SER   A CA   1 
ATOM   5991  C  C    . SER   A  1  399 ? 3.728   -14.028 -12.159  1.00 94.66  ? 399  SER   A C    1 
ATOM   5992  O  O    . SER   A  1  399 ? 3.800   -15.027 -11.437  1.00 90.39  ? 399  SER   A O    1 
ATOM   5993  C  CB   . SER   A  1  399 ? 1.740   -13.133 -13.395  1.00 115.15 ? 399  SER   A CB   1 
ATOM   5994  O  OG   . SER   A  1  399 ? 2.574   -12.718 -14.464  1.00 121.70 ? 399  SER   A OG   1 
ATOM   5995  H  H    . SER   A  1  399 ? 3.350   -11.348 -12.327  1.00 126.29 ? 399  SER   A H    1 
ATOM   5996  H  HA   . SER   A  1  399 ? 1.936   -13.461 -11.369  1.00 124.91 ? 399  SER   A HA   1 
ATOM   5997  H  HB2  . SER   A  1  399 ? 1.428   -14.035 -13.568  1.00 138.17 ? 399  SER   A HB2  1 
ATOM   5998  H  HB3  . SER   A  1  399 ? 0.985   -12.527 -13.330  1.00 138.17 ? 399  SER   A HB3  1 
ATOM   5999  H  HG   . SER   A  1  399 ? 2.267   -12.999 -15.193  1.00 146.02 ? 399  SER   A HG   1 
ATOM   6000  N  N    . CYS   A  1  400 ? 4.692   -13.707 -13.021  1.00 90.99  ? 400  CYS   A N    1 
ATOM   6001  C  CA   . CYS   A  1  400 ? 5.924   -14.459 -13.204  1.00 80.47  ? 400  CYS   A CA   1 
ATOM   6002  C  C    . CYS   A  1  400 ? 7.083   -13.473 -13.137  1.00 78.76  ? 400  CYS   A C    1 
ATOM   6003  O  O    . CYS   A  1  400 ? 6.968   -12.354 -13.653  1.00 81.22  ? 400  CYS   A O    1 
ATOM   6004  C  CB   . CYS   A  1  400 ? 5.911   -15.199 -14.553  1.00 78.27  ? 400  CYS   A CB   1 
ATOM   6005  S  SG   . CYS   A  1  400 ? 7.271   -16.367 -14.884  1.00 80.11  ? 400  CYS   A SG   1 
ATOM   6006  H  H    . CYS   A  1  400 ? 4.650   -13.021 -13.537  1.00 109.17 ? 400  CYS   A H    1 
ATOM   6007  H  HA   . CYS   A  1  400 ? 6.039   -15.129 -12.512  1.00 96.54  ? 400  CYS   A HA   1 
ATOM   6008  H  HB2  . CYS   A  1  400 ? 5.086   -15.707 -14.605  1.00 93.90  ? 400  CYS   A HB2  1 
ATOM   6009  H  HB3  . CYS   A  1  400 ? 5.935   -14.533 -15.258  1.00 93.90  ? 400  CYS   A HB3  1 
ATOM   6010  N  N    . PRO   A  1  401 ? 8.195   -13.835 -12.500  1.00 76.85  ? 401  PRO   A N    1 
ATOM   6011  C  CA   . PRO   A  1  401 ? 9.230   -12.842 -12.231  1.00 72.57  ? 401  PRO   A CA   1 
ATOM   6012  C  C    . PRO   A  1  401 ? 9.726   -12.205 -13.521  1.00 69.54  ? 401  PRO   A C    1 
ATOM   6013  O  O    . PRO   A  1  401 ? 9.779   -12.861 -14.574  1.00 70.09  ? 401  PRO   A O    1 
ATOM   6014  C  CB   . PRO   A  1  401 ? 10.334  -13.652 -11.537  1.00 71.59  ? 401  PRO   A CB   1 
ATOM   6015  C  CG   . PRO   A  1  401 ? 9.999   -15.085 -11.767  1.00 74.78  ? 401  PRO   A CG   1 
ATOM   6016  C  CD   . PRO   A  1  401 ? 8.521   -15.142 -11.903  1.00 77.52  ? 401  PRO   A CD   1 
ATOM   6017  H  HA   . PRO   A  1  401 ? 8.899   -12.154 -11.633  1.00 87.06  ? 401  PRO   A HA   1 
ATOM   6018  H  HB2  . PRO   A  1  401 ? 11.194  -13.433 -11.928  1.00 85.89  ? 401  PRO   A HB2  1 
ATOM   6019  H  HB3  . PRO   A  1  401 ? 10.339  -13.449 -10.588  1.00 85.89  ? 401  PRO   A HB3  1 
ATOM   6020  H  HG2  . PRO   A  1  401 ? 10.431  -15.395 -12.578  1.00 89.72  ? 401  PRO   A HG2  1 
ATOM   6021  H  HG3  . PRO   A  1  401 ? 10.295  -15.615 -11.010  1.00 89.72  ? 401  PRO   A HG3  1 
ATOM   6022  H  HD2  . PRO   A  1  401 ? 8.255   -15.867 -12.490  1.00 93.01  ? 401  PRO   A HD2  1 
ATOM   6023  H  HD3  . PRO   A  1  401 ? 8.096   -15.243 -11.037  1.00 93.01  ? 401  PRO   A HD3  1 
ATOM   6024  N  N    . PRO   A  1  402 ? 10.100  -10.920 -13.470  1.00 69.38  ? 402  PRO   A N    1 
ATOM   6025  C  CA   . PRO   A  1  402 ? 10.522  -10.225 -14.702  1.00 69.37  ? 402  PRO   A CA   1 
ATOM   6026  C  C    . PRO   A  1  402 ? 11.554  -10.978 -15.523  1.00 66.34  ? 402  PRO   A C    1 
ATOM   6027  O  O    . PRO   A  1  402 ? 11.509  -10.933 -16.759  1.00 66.66  ? 402  PRO   A O    1 
ATOM   6028  C  CB   . PRO   A  1  402 ? 11.094  -8.901  -14.173  1.00 70.76  ? 402  PRO   A CB   1 
ATOM   6029  C  CG   . PRO   A  1  402 ? 10.451  -8.687  -12.855  1.00 70.18  ? 402  PRO   A CG   1 
ATOM   6030  C  CD   . PRO   A  1  402 ? 10.082  -10.029 -12.297  1.00 70.08  ? 402  PRO   A CD   1 
ATOM   6031  H  HA   . PRO   A  1  402 ? 9.740   -10.055 -15.251  1.00 83.22  ? 402  PRO   A HA   1 
ATOM   6032  H  HB2  . PRO   A  1  402 ? 12.057  -8.974  -14.079  1.00 84.90  ? 402  PRO   A HB2  1 
ATOM   6033  H  HB3  . PRO   A  1  402 ? 10.875  -8.181  -14.785  1.00 84.90  ? 402  PRO   A HB3  1 
ATOM   6034  H  HG2  . PRO   A  1  402 ? 11.075  -8.238  -12.265  1.00 84.20  ? 402  PRO   A HG2  1 
ATOM   6035  H  HG3  . PRO   A  1  402 ? 9.656   -8.143  -12.974  1.00 84.20  ? 402  PRO   A HG3  1 
ATOM   6036  H  HD2  . PRO   A  1  402 ? 10.734  -10.316 -11.639  1.00 84.07  ? 402  PRO   A HD2  1 
ATOM   6037  H  HD3  . PRO   A  1  402 ? 9.198   -10.003 -11.899  1.00 84.07  ? 402  PRO   A HD3  1 
ATOM   6038  N  N    . SER   A  1  403 ? 12.493  -11.662 -14.871  1.00 62.85  ? 403  SER   A N    1 
ATOM   6039  C  CA   . SER   A  1  403 ? 13.529  -12.424 -15.566  1.00 64.83  ? 403  SER   A CA   1 
ATOM   6040  C  C    . SER   A  1  403 ? 14.301  -11.541 -16.544  1.00 60.37  ? 403  SER   A C    1 
ATOM   6041  O  O    . SER   A  1  403 ? 14.612  -11.942 -17.669  1.00 56.01  ? 403  SER   A O    1 
ATOM   6042  C  CB   . SER   A  1  403 ? 12.927  -13.636 -16.278  1.00 73.94  ? 403  SER   A CB   1 
ATOM   6043  O  OG   . SER   A  1  403 ? 12.023  -13.234 -17.292  1.00 83.90  ? 403  SER   A OG   1 
ATOM   6044  H  H    . SER   A  1  403 ? 12.551  -11.701 -14.014  1.00 75.40  ? 403  SER   A H    1 
ATOM   6045  H  HA   . SER   A  1  403 ? 14.167  -12.749 -14.911  1.00 77.78  ? 403  SER   A HA   1 
ATOM   6046  H  HB2  . SER   A  1  403 ? 13.642  -14.152 -16.680  1.00 88.70  ? 403  SER   A HB2  1 
ATOM   6047  H  HB3  . SER   A  1  403 ? 12.451  -14.177 -15.629  1.00 88.70  ? 403  SER   A HB3  1 
ATOM   6048  H  HG   . SER   A  1  403 ? 12.448  -12.981 -17.971  1.00 100.67 ? 403  SER   A HG   1 
ATOM   6049  N  N    . PHE   A  1  404 ? 14.606  -10.320 -16.111  1.00 61.42  ? 404  PHE   A N    1 
ATOM   6050  C  CA   . PHE   A  1  404 ? 15.464  -9.420  -16.869  1.00 60.33  ? 404  PHE   A CA   1 
ATOM   6051  C  C    . PHE   A  1  404 ? 16.823  -10.066 -17.099  1.00 61.27  ? 404  PHE   A C    1 
ATOM   6052  O  O    . PHE   A  1  404 ? 17.571  -10.312 -16.146  1.00 58.64  ? 404  PHE   A O    1 
ATOM   6053  C  CB   . PHE   A  1  404 ? 15.605  -8.096  -16.116  1.00 61.59  ? 404  PHE   A CB   1 
ATOM   6054  C  CG   . PHE   A  1  404 ? 16.660  -7.172  -16.668  1.00 60.49  ? 404  PHE   A CG   1 
ATOM   6055  C  CD1  . PHE   A  1  404 ? 17.967  -7.237  -16.208  1.00 59.52  ? 404  PHE   A CD1  1 
ATOM   6056  C  CD2  . PHE   A  1  404 ? 16.337  -6.216  -17.619  1.00 61.74  ? 404  PHE   A CD2  1 
ATOM   6057  C  CE1  . PHE   A  1  404 ? 18.937  -6.380  -16.702  1.00 62.44  ? 404  PHE   A CE1  1 
ATOM   6058  C  CE2  . PHE   A  1  404 ? 17.303  -5.354  -18.116  1.00 61.97  ? 404  PHE   A CE2  1 
ATOM   6059  C  CZ   . PHE   A  1  404 ? 18.604  -5.436  -17.656  1.00 61.67  ? 404  PHE   A CZ   1 
ATOM   6060  H  H    . PHE   A  1  404 ? 14.323  -9.986  -15.371  1.00 73.69  ? 404  PHE   A H    1 
ATOM   6061  H  HA   . PHE   A  1  404 ? 15.075  -9.232  -17.738  1.00 72.37  ? 404  PHE   A HA   1 
ATOM   6062  H  HB2  . PHE   A  1  404 ? 14.756  -7.627  -16.154  1.00 73.89  ? 404  PHE   A HB2  1 
ATOM   6063  H  HB3  . PHE   A  1  404 ? 15.837  -8.288  -15.194  1.00 73.89  ? 404  PHE   A HB3  1 
ATOM   6064  H  HD1  . PHE   A  1  404 ? 18.195  -7.864  -15.560  1.00 71.40  ? 404  PHE   A HD1  1 
ATOM   6065  H  HD2  . PHE   A  1  404 ? 15.462  -6.151  -17.926  1.00 74.07  ? 404  PHE   A HD2  1 
ATOM   6066  H  HE1  . PHE   A  1  404 ? 19.811  -6.439  -16.392  1.00 74.91  ? 404  PHE   A HE1  1 
ATOM   6067  H  HE2  . PHE   A  1  404 ? 17.076  -4.722  -18.759  1.00 74.34  ? 404  PHE   A HE2  1 
ATOM   6068  H  HZ   . PHE   A  1  404 ? 19.253  -4.859  -17.987  1.00 73.98  ? 404  PHE   A HZ   1 
ATOM   6069  N  N    . GLY   A  1  405 ? 17.144  -10.347 -18.360  1.00 60.47  ? 405  GLY   A N    1 
ATOM   6070  C  CA   . GLY   A  1  405 ? 18.380  -11.006 -18.728  1.00 59.07  ? 405  GLY   A CA   1 
ATOM   6071  C  C    . GLY   A  1  405 ? 18.215  -12.450 -19.143  1.00 60.47  ? 405  GLY   A C    1 
ATOM   6072  O  O    . GLY   A  1  405 ? 19.190  -13.059 -19.602  1.00 59.75  ? 405  GLY   A O    1 
ATOM   6073  H  H    . GLY   A  1  405 ? 16.644  -10.157 -19.034  1.00 72.55  ? 405  GLY   A H    1 
ATOM   6074  H  HA2  . GLY   A  1  405 ? 18.781  -10.526 -19.470  1.00 70.86  ? 405  GLY   A HA2  1 
ATOM   6075  H  HA3  . GLY   A  1  405 ? 18.985  -10.980 -17.971  1.00 70.86  ? 405  GLY   A HA3  1 
ATOM   6076  N  N    . TYR   A  1  406 ? 17.013  -13.019 -18.999  1.00 61.16  ? 406  TYR   A N    1 
ATOM   6077  C  CA   . TYR   A  1  406 ? 16.783  -14.402 -19.403  1.00 59.98  ? 406  TYR   A CA   1 
ATOM   6078  C  C    . TYR   A  1  406 ? 17.250  -14.652 -20.829  1.00 60.78  ? 406  TYR   A C    1 
ATOM   6079  O  O    . TYR   A  1  406 ? 17.637  -15.775 -21.172  1.00 63.44  ? 406  TYR   A O    1 
ATOM   6080  C  CB   . TYR   A  1  406 ? 15.296  -14.737 -19.265  1.00 59.42  ? 406  TYR   A CB   1 
ATOM   6081  C  CG   . TYR   A  1  406 ? 14.972  -16.211 -19.364  1.00 59.03  ? 406  TYR   A CG   1 
ATOM   6082  C  CD1  . TYR   A  1  406 ? 14.675  -16.800 -20.588  1.00 56.16  ? 406  TYR   A CD1  1 
ATOM   6083  C  CD2  . TYR   A  1  406 ? 14.952  -17.012 -18.231  1.00 63.36  ? 406  TYR   A CD2  1 
ATOM   6084  C  CE1  . TYR   A  1  406 ? 14.375  -18.146 -20.679  1.00 58.44  ? 406  TYR   A CE1  1 
ATOM   6085  C  CE2  . TYR   A  1  406 ? 14.653  -18.357 -18.313  1.00 64.19  ? 406  TYR   A CE2  1 
ATOM   6086  C  CZ   . TYR   A  1  406 ? 14.365  -18.918 -19.539  1.00 64.89  ? 406  TYR   A CZ   1 
ATOM   6087  O  OH   . TYR   A  1  406 ? 14.066  -20.256 -19.625  1.00 70.08  ? 406  TYR   A OH   1 
ATOM   6088  H  H    . TYR   A  1  406 ? 16.322  -12.626 -18.671  1.00 73.38  ? 406  TYR   A H    1 
ATOM   6089  H  HA   . TYR   A  1  406 ? 17.282  -14.993 -18.817  1.00 71.96  ? 406  TYR   A HA   1 
ATOM   6090  H  HB2  . TYR   A  1  406 ? 14.989  -14.427 -18.399  1.00 71.28  ? 406  TYR   A HB2  1 
ATOM   6091  H  HB3  . TYR   A  1  406 ? 14.811  -14.283 -19.971  1.00 71.28  ? 406  TYR   A HB3  1 
ATOM   6092  H  HD1  . TYR   A  1  406 ? 14.679  -16.279 -21.358  1.00 67.37  ? 406  TYR   A HD1  1 
ATOM   6093  H  HD2  . TYR   A  1  406 ? 15.144  -16.637 -17.402  1.00 76.01  ? 406  TYR   A HD2  1 
ATOM   6094  H  HE1  . TYR   A  1  406 ? 14.180  -18.527 -21.504  1.00 70.11  ? 406  TYR   A HE1  1 
ATOM   6095  H  HE2  . TYR   A  1  406 ? 14.646  -18.882 -17.545  1.00 77.01  ? 406  TYR   A HE2  1 
ATOM   6096  H  HH   . TYR   A  1  406 ? 14.066  -20.600 -18.859  1.00 84.07  ? 406  TYR   A HH   1 
ATOM   6097  N  N    . SER   A  1  407 ? 17.218  -13.622 -21.670  1.00 60.92  ? 407  SER   A N    1 
ATOM   6098  C  CA   . SER   A  1  407 ? 17.712  -13.702 -23.035  1.00 59.66  ? 407  SER   A CA   1 
ATOM   6099  C  C    . SER   A  1  407 ? 18.475  -12.426 -23.350  1.00 59.44  ? 407  SER   A C    1 
ATOM   6100  O  O    . SER   A  1  407 ? 18.132  -11.343 -22.866  1.00 58.65  ? 407  SER   A O    1 
ATOM   6101  C  CB   . SER   A  1  407 ? 16.570  -13.897 -24.038  1.00 58.15  ? 407  SER   A CB   1 
ATOM   6102  O  OG   . SER   A  1  407 ? 15.642  -12.830 -23.959  1.00 63.59  ? 407  SER   A OG   1 
ATOM   6103  H  H    . SER   A  1  407 ? 16.906  -12.847 -21.466  1.00 73.09  ? 407  SER   A H    1 
ATOM   6104  H  HA   . SER   A  1  407 ? 18.318  -14.454 -23.125  1.00 71.57  ? 407  SER   A HA   1 
ATOM   6105  H  HB2  . SER   A  1  407 ? 16.939  -13.929 -24.935  1.00 69.76  ? 407  SER   A HB2  1 
ATOM   6106  H  HB3  . SER   A  1  407 ? 16.112  -14.729 -23.839  1.00 69.76  ? 407  SER   A HB3  1 
ATOM   6107  H  HG   . SER   A  1  407 ? 14.874  -13.101 -24.165  1.00 76.29  ? 407  SER   A HG   1 
ATOM   6108  N  N    . MET   A  1  408 ? 19.519  -12.563 -24.163  1.00 59.22  ? 408  MET   A N    1 
ATOM   6109  C  CA   . MET   A  1  408 ? 20.346  -11.426 -24.533  1.00 55.31  ? 408  MET   A CA   1 
ATOM   6110  C  C    . MET   A  1  408 ? 20.910  -11.654 -25.926  1.00 55.42  ? 408  MET   A C    1 
ATOM   6111  O  O    . MET   A  1  408 ? 20.974  -12.785 -26.416  1.00 56.50  ? 408  MET   A O    1 
ATOM   6112  C  CB   . MET   A  1  408 ? 21.493  -11.207 -23.538  1.00 55.09  ? 408  MET   A CB   1 
ATOM   6113  C  CG   . MET   A  1  408 ? 21.058  -10.827 -22.135  1.00 55.86  ? 408  MET   A CG   1 
ATOM   6114  S  SD   . MET   A  1  408 ? 22.458  -10.525 -21.037  1.00 56.89  ? 408  MET   A SD   1 
ATOM   6115  C  CE   . MET   A  1  408 ? 23.280  -12.117 -21.054  1.00 54.09  ? 408  MET   A CE   1 
ATOM   6116  H  H    . MET   A  1  408 ? 19.767  -13.308 -24.514  1.00 71.05  ? 408  MET   A H    1 
ATOM   6117  H  HA   . MET   A  1  408 ? 19.791  -10.631 -24.537  1.00 66.35  ? 408  MET   A HA   1 
ATOM   6118  H  HB2  . MET   A  1  408 ? 22.003  -12.029 -23.472  1.00 66.09  ? 408  MET   A HB2  1 
ATOM   6119  H  HB3  . MET   A  1  408 ? 22.057  -10.492 -23.872  1.00 66.09  ? 408  MET   A HB3  1 
ATOM   6120  H  HG2  . MET   A  1  408 ? 20.527  -10.016 -22.176  1.00 67.01  ? 408  MET   A HG2  1 
ATOM   6121  H  HG3  . MET   A  1  408 ? 20.532  -11.549 -21.759  1.00 67.01  ? 408  MET   A HG3  1 
ATOM   6122  H  HE1  . MET   A  1  408 ? 24.025  -12.094 -20.434  1.00 64.89  ? 408  MET   A HE1  1 
ATOM   6123  H  HE2  . MET   A  1  408 ? 22.647  -12.802 -20.786  1.00 64.89  ? 408  MET   A HE2  1 
ATOM   6124  H  HE3  . MET   A  1  408 ? 23.602  -12.296 -21.952  1.00 64.89  ? 408  MET   A HE3  1 
ATOM   6125  N  N    . LYS   A  1  409 ? 21.320  -10.558 -26.557  1.00 57.99  ? 409  LYS   A N    1 
ATOM   6126  C  CA   . LYS   A  1  409 ? 21.990  -10.616 -27.848  1.00 58.60  ? 409  LYS   A CA   1 
ATOM   6127  C  C    . LYS   A  1  409 ? 22.761  -9.320  -28.036  1.00 63.08  ? 409  LYS   A C    1 
ATOM   6128  O  O    . LYS   A  1  409 ? 22.184  -8.234  -27.926  1.00 68.97  ? 409  LYS   A O    1 
ATOM   6129  C  CB   . LYS   A  1  409 ? 20.991  -10.811 -28.991  1.00 61.13  ? 409  LYS   A CB   1 
ATOM   6130  C  CG   . LYS   A  1  409 ? 21.647  -11.089 -30.333  1.00 63.94  ? 409  LYS   A CG   1 
ATOM   6131  C  CD   . LYS   A  1  409 ? 22.225  -12.493 -30.384  1.00 67.82  ? 409  LYS   A CD   1 
ATOM   6132  C  CE   . LYS   A  1  409 ? 22.934  -12.755 -31.701  1.00 77.13  ? 409  LYS   A CE   1 
ATOM   6133  N  NZ   . LYS   A  1  409 ? 23.516  -14.123 -31.752  1.00 84.14  ? 409  LYS   A NZ   1 
ATOM   6134  H  H    . LYS   A  1  409 ? 21.221  -9.759  -26.253  1.00 69.57  ? 409  LYS   A H    1 
ATOM   6135  H  HA   . LYS   A  1  409 ? 22.609  -11.363 -27.863  1.00 70.30  ? 409  LYS   A HA   1 
ATOM   6136  H  HB2  . LYS   A  1  409 ? 20.418  -11.564 -28.780  1.00 73.33  ? 409  LYS   A HB2  1 
ATOM   6137  H  HB3  . LYS   A  1  409 ? 20.459  -10.005 -29.082  1.00 73.33  ? 409  LYS   A HB3  1 
ATOM   6138  H  HG2  . LYS   A  1  409 ? 20.987  -11.005 -31.039  1.00 76.71  ? 409  LYS   A HG2  1 
ATOM   6139  H  HG3  . LYS   A  1  409 ? 22.368  -10.456 -30.477  1.00 76.71  ? 409  LYS   A HG3  1 
ATOM   6140  H  HD2  . LYS   A  1  409 ? 22.867  -12.602 -29.666  1.00 81.37  ? 409  LYS   A HD2  1 
ATOM   6141  H  HD3  . LYS   A  1  409 ? 21.508  -13.139 -30.290  1.00 81.37  ? 409  LYS   A HD3  1 
ATOM   6142  H  HE2  . LYS   A  1  409 ? 22.298  -12.668 -32.429  1.00 92.53  ? 409  LYS   A HE2  1 
ATOM   6143  H  HE3  . LYS   A  1  409 ? 23.653  -12.114 -31.811  1.00 92.53  ? 409  LYS   A HE3  1 
ATOM   6144  H  HZ1  . LYS   A  1  409 ? 24.012  -14.215 -32.485  1.00 100.95 ? 409  LYS   A HZ1  1 
ATOM   6145  H  HZ2  . LYS   A  1  409 ? 24.029  -14.262 -31.037  1.00 100.95 ? 409  LYS   A HZ2  1 
ATOM   6146  H  HZ3  . LYS   A  1  409 ? 22.866  -14.730 -31.763  1.00 100.95 ? 409  LYS   A HZ3  1 
ATOM   6147  N  N    . GLY   A  1  410 ? 24.056  -9.442  -28.309  1.00 61.28  ? 410  GLY   A N    1 
ATOM   6148  C  CA   . GLY   A  1  410 ? 24.911  -8.301  -28.549  1.00 60.81  ? 410  GLY   A CA   1 
ATOM   6149  C  C    . GLY   A  1  410 ? 25.645  -8.439  -29.864  1.00 66.06  ? 410  GLY   A C    1 
ATOM   6150  O  O    . GLY   A  1  410 ? 25.190  -9.129  -30.787  1.00 66.51  ? 410  GLY   A O    1 
ATOM   6151  H  H    . GLY   A  1  410 ? 24.467  -10.195 -28.362  1.00 73.52  ? 410  GLY   A H    1 
ATOM   6152  H  HA2  . GLY   A  1  410 ? 24.376  -7.492  -28.575  1.00 72.95  ? 410  GLY   A HA2  1 
ATOM   6153  H  HA3  . GLY   A  1  410 ? 25.563  -8.226  -27.835  1.00 72.95  ? 410  GLY   A HA3  1 
ATOM   6154  N  N    . ALA   A  1  411 ? 26.787  -7.762  -29.951  1.00 67.20  ? 411  ALA   A N    1 
ATOM   6155  C  CA   . ALA   A  1  411 ? 27.698  -7.834  -31.084  1.00 63.07  ? 411  ALA   A CA   1 
ATOM   6156  C  C    . ALA   A  1  411 ? 27.129  -7.205  -32.349  1.00 62.91  ? 411  ALA   A C    1 
ATOM   6157  O  O    . ALA   A  1  411 ? 27.537  -7.569  -33.457  1.00 64.18  ? 411  ALA   A O    1 
ATOM   6158  C  CB   . ALA   A  1  411 ? 28.103  -9.284  -31.367  1.00 61.27  ? 411  ALA   A CB   1 
ATOM   6159  H  H    . ALA   A  1  411 ? 27.065  -7.230  -29.336  1.00 80.62  ? 411  ALA   A H    1 
ATOM   6160  H  HA   . ALA   A  1  411 ? 28.495  -7.330  -30.855  1.00 75.66  ? 411  ALA   A HA   1 
ATOM   6161  H  HB1  . ALA   A  1  411 ? 28.733  -9.298  -32.105  1.00 73.50  ? 411  ALA   A HB1  1 
ATOM   6162  H  HB2  . ALA   A  1  411 ? 28.517  -9.658  -30.573  1.00 73.50  ? 411  ALA   A HB2  1 
ATOM   6163  H  HB3  . ALA   A  1  411 ? 27.311  -9.794  -31.599  1.00 73.50  ? 411  ALA   A HB3  1 
ATOM   6164  N  N    . THR   A  1  412 ? 26.196  -6.263  -32.219  1.00 62.40  ? 412  THR   A N    1 
ATOM   6165  C  CA   . THR   A  1  412 ? 25.665  -5.535  -33.364  1.00 64.28  ? 412  THR   A CA   1 
ATOM   6166  C  C    . THR   A  1  412 ? 25.664  -4.047  -33.051  1.00 65.75  ? 412  THR   A C    1 
ATOM   6167  O  O    . THR   A  1  412 ? 25.115  -3.623  -32.029  1.00 65.91  ? 412  THR   A O    1 
ATOM   6168  C  CB   . THR   A  1  412 ? 24.250  -6.003  -33.722  1.00 63.87  ? 412  THR   A CB   1 
ATOM   6169  O  OG1  . THR   A  1  412 ? 24.278  -7.394  -34.066  1.00 66.95  ? 412  THR   A OG1  1 
ATOM   6170  C  CG2  . THR   A  1  412 ? 23.695  -5.203  -34.898  1.00 63.20  ? 412  THR   A CG2  1 
ATOM   6171  H  H    . THR   A  1  412 ? 25.853  -6.026  -31.467  1.00 74.86  ? 412  THR   A H    1 
ATOM   6172  H  HA   . THR   A  1  412 ? 26.235  -5.687  -34.134  1.00 77.12  ? 412  THR   A HA   1 
ATOM   6173  H  HB   . THR   A  1  412 ? 23.664  -5.868  -32.960  1.00 76.63  ? 412  THR   A HB   1 
ATOM   6174  H  HG1  . THR   A  1  412 ? 23.570  -7.768  -33.810  1.00 80.32  ? 412  THR   A HG1  1 
ATOM   6175  H  HG21 . THR   A  1  412 ? 22.848  -5.579  -35.185  1.00 75.82  ? 412  THR   A HG21 1 
ATOM   6176  H  HG22 . THR   A  1  412 ? 23.556  -4.280  -34.636  1.00 75.82  ? 412  THR   A HG22 1 
ATOM   6177  H  HG23 . THR   A  1  412 ? 24.319  -5.229  -35.641  1.00 75.82  ? 412  THR   A HG23 1 
ATOM   6178  N  N    . ASP   A  1  413 ? 26.276  -3.262  -33.935  1.00 67.37  ? 413  ASP   A N    1 
ATOM   6179  C  CA   . ASP   A  1  413 ? 26.350  -1.809  -33.788  1.00 70.93  ? 413  ASP   A CA   1 
ATOM   6180  C  C    . ASP   A  1  413 ? 25.140  -1.217  -34.498  1.00 74.07  ? 413  ASP   A C    1 
ATOM   6181  O  O    . ASP   A  1  413 ? 25.190  -0.876  -35.680  1.00 79.42  ? 413  ASP   A O    1 
ATOM   6182  C  CB   . ASP   A  1  413 ? 27.661  -1.281  -34.358  1.00 70.73  ? 413  ASP   A CB   1 
ATOM   6183  C  CG   . ASP   A  1  413 ? 27.847  0.206   -34.121  1.00 73.65  ? 413  ASP   A CG   1 
ATOM   6184  O  OD1  . ASP   A  1  413 ? 27.118  0.775   -33.280  1.00 73.61  ? 413  ASP   A OD1  1 
ATOM   6185  O  OD2  . ASP   A  1  413 ? 28.721  0.809   -34.780  1.00 75.76  ? 413  ASP   A OD2  1 
ATOM   6186  H  H    . ASP   A  1  413 ? 26.666  -3.554  -34.645  1.00 80.83  ? 413  ASP   A H    1 
ATOM   6187  H  HA   . ASP   A  1  413 ? 26.309  -1.568  -32.849  1.00 85.09  ? 413  ASP   A HA   1 
ATOM   6188  H  HB2  . ASP   A  1  413 ? 28.399  -1.747  -33.935  1.00 84.86  ? 413  ASP   A HB2  1 
ATOM   6189  H  HB3  . ASP   A  1  413 ? 27.674  -1.437  -35.315  1.00 84.86  ? 413  ASP   A HB3  1 
ATOM   6190  N  N    . ILE   A  1  414 ? 24.034  -1.086  -33.763  1.00 71.54  ? 414  ILE   A N    1 
ATOM   6191  C  CA   . ILE   A  1  414 ? 22.775  -0.719  -34.403  1.00 72.91  ? 414  ILE   A CA   1 
ATOM   6192  C  C    . ILE   A  1  414 ? 22.713  0.775   -34.704  1.00 76.48  ? 414  ILE   A C    1 
ATOM   6193  O  O    . ILE   A  1  414 ? 22.007  1.191   -35.629  1.00 81.01  ? 414  ILE   A O    1 
ATOM   6194  C  CB   . ILE   A  1  414 ? 21.584  -1.160  -33.536  1.00 69.81  ? 414  ILE   A CB   1 
ATOM   6195  C  CG1  . ILE   A  1  414 ? 20.282  -1.019  -34.327  1.00 73.76  ? 414  ILE   A CG1  1 
ATOM   6196  C  CG2  . ILE   A  1  414 ? 21.513  -0.337  -32.259  1.00 66.39  ? 414  ILE   A CG2  1 
ATOM   6197  C  CD1  . ILE   A  1  414 ? 19.084  -1.634  -33.648  1.00 74.23  ? 414  ILE   A CD1  1 
ATOM   6198  H  H    . ILE   A  1  414 ? 23.988  -1.203  -32.912  1.00 85.83  ? 414  ILE   A H    1 
ATOM   6199  H  HA   . ILE   A  1  414 ? 22.725  -1.188  -35.250  1.00 87.47  ? 414  ILE   A HA   1 
ATOM   6200  H  HB   . ILE   A  1  414 ? 21.711  -2.091  -33.294  1.00 83.76  ? 414  ILE   A HB   1 
ATOM   6201  H  HG12 . ILE   A  1  414 ? 20.097  -0.076  -34.455  1.00 88.49  ? 414  ILE   A HG12 1 
ATOM   6202  H  HG13 . ILE   A  1  414 ? 20.391  -1.456  -35.186  1.00 88.49  ? 414  ILE   A HG13 1 
ATOM   6203  H  HG21 . ILE   A  1  414 ? 20.857  -0.733  -31.664  1.00 79.65  ? 414  ILE   A HG21 1 
ATOM   6204  H  HG22 . ILE   A  1  414 ? 22.385  -0.335  -31.835  1.00 79.65  ? 414  ILE   A HG22 1 
ATOM   6205  H  HG23 . ILE   A  1  414 ? 21.252  0.570   -32.482  1.00 79.65  ? 414  ILE   A HG23 1 
ATOM   6206  H  HD11 . ILE   A  1  414 ? 18.317  -1.566  -34.237  1.00 89.06  ? 414  ILE   A HD11 1 
ATOM   6207  H  HD12 . ILE   A  1  414 ? 19.273  -2.567  -33.458  1.00 89.06  ? 414  ILE   A HD12 1 
ATOM   6208  H  HD13 . ILE   A  1  414 ? 18.910  -1.158  -32.821  1.00 89.06  ? 414  ILE   A HD13 1 
ATOM   6209  N  N    . ASP   A  1  415 ? 23.430  1.602   -33.945  1.00 77.66  ? 415  ASP   A N    1 
ATOM   6210  C  CA   . ASP   A  1  415 ? 23.470  3.037   -34.190  1.00 78.57  ? 415  ASP   A CA   1 
ATOM   6211  C  C    . ASP   A  1  415 ? 24.682  3.455   -35.014  1.00 79.45  ? 415  ASP   A C    1 
ATOM   6212  O  O    . ASP   A  1  415 ? 24.899  4.655   -35.214  1.00 84.90  ? 415  ASP   A O    1 
ATOM   6213  C  CB   . ASP   A  1  415 ? 23.448  3.801   -32.864  1.00 81.26  ? 415  ASP   A CB   1 
ATOM   6214  C  CG   . ASP   A  1  415 ? 24.687  3.559   -32.030  1.00 87.07  ? 415  ASP   A CG   1 
ATOM   6215  O  OD1  . ASP   A  1  415 ? 25.415  2.585   -32.311  1.00 87.56  ? 415  ASP   A OD1  1 
ATOM   6216  O  OD2  . ASP   A  1  415 ? 24.929  4.343   -31.088  1.00 89.59  ? 415  ASP   A OD2  1 
ATOM   6217  H  H    . ASP   A  1  415 ? 23.906  1.350   -33.275  1.00 93.18  ? 415  ASP   A H    1 
ATOM   6218  H  HA   . ASP   A  1  415 ? 22.674  3.286   -34.687  1.00 94.27  ? 415  ASP   A HA   1 
ATOM   6219  H  HB2  . ASP   A  1  415 ? 23.390  4.752   -33.048  1.00 97.49  ? 415  ASP   A HB2  1 
ATOM   6220  H  HB3  . ASP   A  1  415 ? 22.678  3.516   -32.348  1.00 97.49  ? 415  ASP   A HB3  1 
ATOM   6221  N  N    . LYS   A  1  416 ? 25.473  2.496   -35.495  1.00 78.74  ? 416  LYS   A N    1 
ATOM   6222  C  CA   . LYS   A  1  416 ? 26.617  2.777   -36.360  1.00 84.37  ? 416  LYS   A CA   1 
ATOM   6223  C  C    . LYS   A  1  416 ? 27.591  3.761   -35.717  1.00 84.54  ? 416  LYS   A C    1 
ATOM   6224  O  O    . LYS   A  1  416 ? 28.234  4.555   -36.409  1.00 88.17  ? 416  LYS   A O    1 
ATOM   6225  C  CB   . LYS   A  1  416 ? 26.156  3.305   -37.723  1.00 95.15  ? 416  LYS   A CB   1 
ATOM   6226  C  CG   . LYS   A  1  416 ? 25.556  2.249   -38.639  1.00 105.07 ? 416  LYS   A CG   1 
ATOM   6227  C  CD   . LYS   A  1  416 ? 26.631  1.333   -39.203  1.00 112.33 ? 416  LYS   A CD   1 
ATOM   6228  C  CE   . LYS   A  1  416 ? 26.077  0.403   -40.270  1.00 114.65 ? 416  LYS   A CE   1 
ATOM   6229  N  NZ   . LYS   A  1  416 ? 27.143  -0.452  -40.862  1.00 114.12 ? 416  LYS   A NZ   1 
ATOM   6230  H  H    . LYS   A  1  416 ? 25.365  1.659   -35.330  1.00 94.46  ? 416  LYS   A H    1 
ATOM   6231  H  HA   . LYS   A  1  416 ? 27.099  1.947   -36.501  1.00 101.23 ? 416  LYS   A HA   1 
ATOM   6232  H  HB2  . LYS   A  1  416 ? 25.480  3.985   -37.578  1.00 114.16 ? 416  LYS   A HB2  1 
ATOM   6233  H  HB3  . LYS   A  1  416 ? 26.920  3.690   -38.180  1.00 114.16 ? 416  LYS   A HB3  1 
ATOM   6234  H  HG2  . LYS   A  1  416 ? 24.926  1.709   -38.138  1.00 126.06 ? 416  LYS   A HG2  1 
ATOM   6235  H  HG3  . LYS   A  1  416 ? 25.105  2.684   -39.380  1.00 126.06 ? 416  LYS   A HG3  1 
ATOM   6236  H  HD2  . LYS   A  1  416 ? 27.333  1.871   -39.603  1.00 134.78 ? 416  LYS   A HD2  1 
ATOM   6237  H  HD3  . LYS   A  1  416 ? 26.997  0.790   -38.487  1.00 134.78 ? 416  LYS   A HD3  1 
ATOM   6238  H  HE2  . LYS   A  1  416 ? 25.407  -0.176  -39.874  1.00 137.56 ? 416  LYS   A HE2  1 
ATOM   6239  H  HE3  . LYS   A  1  416 ? 25.680  0.931   -40.981  1.00 137.56 ? 416  LYS   A HE3  1 
ATOM   6240  H  HZ1  . LYS   A  1  416 ? 26.795  -0.986  -41.484  1.00 136.92 ? 416  LYS   A HZ1  1 
ATOM   6241  H  HZ2  . LYS   A  1  416 ? 27.769  0.057   -41.237  1.00 136.92 ? 416  LYS   A HZ2  1 
ATOM   6242  H  HZ3  . LYS   A  1  416 ? 27.518  -0.953  -40.229  1.00 136.92 ? 416  LYS   A HZ3  1 
ATOM   6243  N  N    . ASN   A  1  417 ? 27.718  3.717   -34.393  1.00 82.38  ? 417  ASN   A N    1 
ATOM   6244  C  CA   . ASN   A  1  417 ? 28.627  4.603   -33.680  1.00 80.19  ? 417  ASN   A CA   1 
ATOM   6245  C  C    . ASN   A  1  417 ? 30.003  3.986   -33.461  1.00 76.30  ? 417  ASN   A C    1 
ATOM   6246  O  O    . ASN   A  1  417 ? 30.867  4.634   -32.860  1.00 76.09  ? 417  ASN   A O    1 
ATOM   6247  C  CB   . ASN   A  1  417 ? 28.026  5.004   -32.328  1.00 78.26  ? 417  ASN   A CB   1 
ATOM   6248  C  CG   . ASN   A  1  417 ? 28.285  3.977   -31.242  1.00 77.59  ? 417  ASN   A CG   1 
ATOM   6249  O  OD1  . ASN   A  1  417 ? 28.209  2.770   -31.478  1.00 79.55  ? 417  ASN   A OD1  1 
ATOM   6250  N  ND2  . ASN   A  1  417 ? 28.597  4.454   -30.042  1.00 77.01  ? 417  ASN   A ND2  1 
ATOM   6251  H  H    . ASN   A  1  417 ? 27.283  3.177   -33.884  1.00 98.83  ? 417  ASN   A H    1 
ATOM   6252  H  HA   . ASN   A  1  417 ? 28.743  5.411   -34.204  1.00 96.21  ? 417  ASN   A HA   1 
ATOM   6253  H  HB2  . ASN   A  1  417 ? 28.418  5.845   -32.045  1.00 93.89  ? 417  ASN   A HB2  1 
ATOM   6254  H  HB3  . ASN   A  1  417 ? 27.066  5.102   -32.425  1.00 93.89  ? 417  ASN   A HB3  1 
ATOM   6255  H  HD21 . ASN   A  1  417 ? 28.754  3.914   -29.392  1.00 92.40  ? 417  ASN   A HD21 1 
ATOM   6256  H  HD22 . ASN   A  1  417 ? 28.644  5.304   -29.916  1.00 92.40  ? 417  ASN   A HD22 1 
ATOM   6257  N  N    . GLY   A  1  418 ? 30.228  2.759   -33.929  1.00 71.89  ? 418  GLY   A N    1 
ATOM   6258  C  CA   . GLY   A  1  418 ? 31.517  2.110   -33.815  1.00 70.18  ? 418  GLY   A CA   1 
ATOM   6259  C  C    . GLY   A  1  418 ? 31.676  1.187   -32.628  1.00 71.18  ? 418  GLY   A C    1 
ATOM   6260  O  O    . GLY   A  1  418 ? 32.771  0.644   -32.434  1.00 69.75  ? 418  GLY   A O    1 
ATOM   6261  H  H    . GLY   A  1  418 ? 29.634  2.279   -34.324  1.00 86.25  ? 418  GLY   A H    1 
ATOM   6262  H  HA2  . GLY   A  1  418 ? 31.671  1.587   -34.617  1.00 84.20  ? 418  GLY   A HA2  1 
ATOM   6263  H  HA3  . GLY   A  1  418 ? 32.202  2.794   -33.749  1.00 84.20  ? 418  GLY   A HA3  1 
ATOM   6264  N  N    . TYR   A  1  419 ? 30.626  0.986   -31.832  1.00 75.37  ? 419  TYR   A N    1 
ATOM   6265  C  CA   . TYR   A  1  419 ? 30.698  0.151   -30.642  1.00 76.95  ? 419  TYR   A CA   1 
ATOM   6266  C  C    . TYR   A  1  419 ? 29.492  -0.780  -30.608  1.00 76.49  ? 419  TYR   A C    1 
ATOM   6267  O  O    . TYR   A  1  419 ? 28.354  -0.324  -30.813  1.00 77.85  ? 419  TYR   A O    1 
ATOM   6268  C  CB   . TYR   A  1  419 ? 30.753  1.023   -29.378  1.00 78.17  ? 419  TYR   A CB   1 
ATOM   6269  C  CG   . TYR   A  1  419 ? 32.014  1.857   -29.277  1.00 77.38  ? 419  TYR   A CG   1 
ATOM   6270  C  CD1  . TYR   A  1  419 ? 32.169  3.015   -30.029  1.00 78.97  ? 419  TYR   A CD1  1 
ATOM   6271  C  CD2  . TYR   A  1  419 ? 33.050  1.484   -28.431  1.00 74.07  ? 419  TYR   A CD2  1 
ATOM   6272  C  CE1  . TYR   A  1  419 ? 33.322  3.774   -29.944  1.00 78.57  ? 419  TYR   A CE1  1 
ATOM   6273  C  CE2  . TYR   A  1  419 ? 34.203  2.240   -28.335  1.00 74.71  ? 419  TYR   A CE2  1 
ATOM   6274  C  CZ   . TYR   A  1  419 ? 34.335  3.381   -29.095  1.00 75.96  ? 419  TYR   A CZ   1 
ATOM   6275  O  OH   . TYR   A  1  419 ? 35.483  4.134   -28.997  1.00 74.64  ? 419  TYR   A OH   1 
ATOM   6276  H  H    . TYR   A  1  419 ? 29.850  1.331   -31.965  1.00 90.43  ? 419  TYR   A H    1 
ATOM   6277  H  HA   . TYR   A  1  419 ? 31.497  -0.398  -30.674  1.00 92.33  ? 419  TYR   A HA   1 
ATOM   6278  H  HB2  . TYR   A  1  419 ? 29.995  1.629   -29.383  1.00 93.78  ? 419  TYR   A HB2  1 
ATOM   6279  H  HB3  . TYR   A  1  419 ? 30.712  0.448   -28.598  1.00 93.78  ? 419  TYR   A HB3  1 
ATOM   6280  H  HD1  . TYR   A  1  419 ? 31.486  3.284   -30.600  1.00 94.75  ? 419  TYR   A HD1  1 
ATOM   6281  H  HD2  . TYR   A  1  419 ? 32.966  0.712   -27.919  1.00 88.86  ? 419  TYR   A HD2  1 
ATOM   6282  H  HE1  . TYR   A  1  419 ? 33.413  4.545   -30.456  1.00 94.26  ? 419  TYR   A HE1  1 
ATOM   6283  H  HE2  . TYR   A  1  419 ? 34.886  1.979   -27.761  1.00 89.63  ? 419  TYR   A HE2  1 
ATOM   6284  H  HH   . TYR   A  1  419 ? 35.411  4.831   -29.461  1.00 89.55  ? 419  TYR   A HH   1 
ATOM   6285  N  N    . PRO   A  1  420 ? 29.683  -2.078  -30.360  1.00 75.00  ? 420  PRO   A N    1 
ATOM   6286  C  CA   . PRO   A  1  420 ? 28.539  -2.998  -30.368  1.00 69.53  ? 420  PRO   A CA   1 
ATOM   6287  C  C    . PRO   A  1  420 ? 27.574  -2.715  -29.228  1.00 68.98  ? 420  PRO   A C    1 
ATOM   6288  O  O    . PRO   A  1  420 ? 27.957  -2.235  -28.159  1.00 73.07  ? 420  PRO   A O    1 
ATOM   6289  C  CB   . PRO   A  1  420 ? 29.185  -4.382  -30.213  1.00 67.85  ? 420  PRO   A CB   1 
ATOM   6290  C  CG   . PRO   A  1  420 ? 30.626  -4.191  -30.523  1.00 71.72  ? 420  PRO   A CG   1 
ATOM   6291  C  CD   . PRO   A  1  420 ? 30.949  -2.791  -30.117  1.00 74.11  ? 420  PRO   A CD   1 
ATOM   6292  H  HA   . PRO   A  1  420 ? 28.068  -2.946  -31.215  1.00 83.42  ? 420  PRO   A HA   1 
ATOM   6293  H  HB2  . PRO   A  1  420 ? 29.067  -4.698  -29.304  1.00 81.40  ? 420  PRO   A HB2  1 
ATOM   6294  H  HB3  . PRO   A  1  420 ? 28.778  -5.004  -30.836  1.00 81.40  ? 420  PRO   A HB3  1 
ATOM   6295  H  HG2  . PRO   A  1  420 ? 31.157  -4.826  -30.017  1.00 86.04  ? 420  PRO   A HG2  1 
ATOM   6296  H  HG3  . PRO   A  1  420 ? 30.776  -4.316  -31.473  1.00 86.04  ? 420  PRO   A HG3  1 
ATOM   6297  H  HD2  . PRO   A  1  420 ? 31.195  -2.750  -29.180  1.00 88.91  ? 420  PRO   A HD2  1 
ATOM   6298  H  HD3  . PRO   A  1  420 ? 31.662  -2.427  -30.664  1.00 88.91  ? 420  PRO   A HD3  1 
ATOM   6299  N  N    . ASP   A  1  421 ? 26.306  -3.039  -29.468  1.00 67.48  ? 421  ASP   A N    1 
ATOM   6300  C  CA   . ASP   A  1  421 ? 25.219  -2.762  -28.541  1.00 66.68  ? 421  ASP   A CA   1 
ATOM   6301  C  C    . ASP   A  1  421 ? 24.571  -4.068  -28.096  1.00 63.66  ? 421  ASP   A C    1 
ATOM   6302  O  O    . ASP   A  1  421 ? 24.805  -5.134  -28.672  1.00 63.58  ? 421  ASP   A O    1 
ATOM   6303  C  CB   . ASP   A  1  421 ? 24.194  -1.826  -29.193  1.00 67.76  ? 421  ASP   A CB   1 
ATOM   6304  C  CG   . ASP   A  1  421 ? 24.840  -0.577  -29.773  1.00 70.65  ? 421  ASP   A CG   1 
ATOM   6305  O  OD1  . ASP   A  1  421 ? 25.651  0.057   -29.065  1.00 72.20  ? 421  ASP   A OD1  1 
ATOM   6306  O  OD2  . ASP   A  1  421 ? 24.560  -0.239  -30.942  1.00 73.86  ? 421  ASP   A OD2  1 
ATOM   6307  H  H    . ASP   A  1  421 ? 26.045  -3.433  -30.186  1.00 80.96  ? 421  ASP   A H    1 
ATOM   6308  H  HA   . ASP   A  1  421 ? 25.562  -2.326  -27.745  1.00 80.00  ? 421  ASP   A HA   1 
ATOM   6309  H  HB2  . ASP   A  1  421 ? 23.745  -2.296  -29.913  1.00 81.30  ? 421  ASP   A HB2  1 
ATOM   6310  H  HB3  . ASP   A  1  421 ? 23.547  -1.548  -28.525  1.00 81.30  ? 421  ASP   A HB3  1 
ATOM   6311  N  N    . LEU   A  1  422 ? 23.747  -3.976  -27.052  1.00 64.45  ? 422  LEU   A N    1 
ATOM   6312  C  CA   . LEU   A  1  422 ? 23.221  -5.145  -26.360  1.00 66.08  ? 422  LEU   A CA   1 
ATOM   6313  C  C    . LEU   A  1  422 ? 21.708  -5.058  -26.240  1.00 69.93  ? 422  LEU   A C    1 
ATOM   6314  O  O    . LEU   A  1  422 ? 21.170  -4.014  -25.859  1.00 73.11  ? 422  LEU   A O    1 
ATOM   6315  C  CB   . LEU   A  1  422 ? 23.844  -5.275  -24.963  1.00 66.08  ? 422  LEU   A CB   1 
ATOM   6316  C  CG   . LEU   A  1  422 ? 23.246  -6.344  -24.045  1.00 66.03  ? 422  LEU   A CG   1 
ATOM   6317  C  CD1  . LEU   A  1  422 ? 23.420  -7.730  -24.645  1.00 65.11  ? 422  LEU   A CD1  1 
ATOM   6318  C  CD2  . LEU   A  1  422 ? 23.874  -6.271  -22.662  1.00 67.74  ? 422  LEU   A CD2  1 
ATOM   6319  H  H    . LEU   A  1  422 ? 23.475  -3.230  -26.722  1.00 77.32  ? 422  LEU   A H    1 
ATOM   6320  H  HA   . LEU   A  1  422 ? 23.428  -5.936  -26.883  1.00 79.28  ? 422  LEU   A HA   1 
ATOM   6321  H  HB2  . LEU   A  1  422 ? 24.784  -5.486  -25.072  1.00 79.27  ? 422  LEU   A HB2  1 
ATOM   6322  H  HB3  . LEU   A  1  422 ? 23.745  -4.423  -24.510  1.00 79.27  ? 422  LEU   A HB3  1 
ATOM   6323  H  HG   . LEU   A  1  422 ? 22.295  -6.181  -23.952  1.00 79.22  ? 422  LEU   A HG   1 
ATOM   6324  H  HD11 . LEU   A  1  422 ? 23.066  -8.388  -24.027  1.00 78.11  ? 422  LEU   A HD11 1 
ATOM   6325  H  HD12 . LEU   A  1  422 ? 22.939  -7.772  -25.486  1.00 78.11  ? 422  LEU   A HD12 1 
ATOM   6326  H  HD13 . LEU   A  1  422 ? 24.365  -7.892  -24.795  1.00 78.11  ? 422  LEU   A HD13 1 
ATOM   6327  H  HD21 . LEU   A  1  422 ? 23.478  -6.954  -22.099  1.00 81.27  ? 422  LEU   A HD21 1 
ATOM   6328  H  HD22 . LEU   A  1  422 ? 24.830  -6.421  -22.741  1.00 81.27  ? 422  LEU   A HD22 1 
ATOM   6329  H  HD23 . LEU   A  1  422 ? 23.707  -5.393  -22.286  1.00 81.27  ? 422  LEU   A HD23 1 
ATOM   6330  N  N    . ILE   A  1  423 ? 21.029  -6.161  -26.552  1.00 70.19  ? 423  ILE   A N    1 
ATOM   6331  C  CA   . ILE   A  1  423 ? 19.600  -6.313  -26.302  1.00 68.21  ? 423  ILE   A CA   1 
ATOM   6332  C  C    . ILE   A  1  423 ? 19.427  -7.211  -25.085  1.00 69.20  ? 423  ILE   A C    1 
ATOM   6333  O  O    . ILE   A  1  423 ? 20.049  -8.279  -25.000  1.00 70.52  ? 423  ILE   A O    1 
ATOM   6334  C  CB   . ILE   A  1  423 ? 18.868  -6.905  -27.519  1.00 67.15  ? 423  ILE   A CB   1 
ATOM   6335  C  CG1  . ILE   A  1  423 ? 19.149  -6.081  -28.776  1.00 75.77  ? 423  ILE   A CG1  1 
ATOM   6336  C  CG2  . ILE   A  1  423 ? 17.365  -6.957  -27.252  1.00 61.74  ? 423  ILE   A CG2  1 
ATOM   6337  C  CD1  . ILE   A  1  423 ? 18.617  -6.712  -30.051  1.00 80.27  ? 423  ILE   A CD1  1 
ATOM   6338  H  H    . ILE   A  1  423 ? 21.385  -6.852  -26.920  1.00 84.21  ? 423  ILE   A H    1 
ATOM   6339  H  HA   . ILE   A  1  423 ? 19.216  -5.443  -26.112  1.00 81.83  ? 423  ILE   A HA   1 
ATOM   6340  H  HB   . ILE   A  1  423 ? 19.200  -7.805  -27.662  1.00 80.56  ? 423  ILE   A HB   1 
ATOM   6341  H  HG12 . ILE   A  1  423 ? 18.730  -5.211  -28.679  1.00 90.90  ? 423  ILE   A HG12 1 
ATOM   6342  H  HG13 . ILE   A  1  423 ? 20.108  -5.978  -28.873  1.00 90.90  ? 423  ILE   A HG13 1 
ATOM   6343  H  HG21 . ILE   A  1  423 ? 16.920  -7.339  -28.025  1.00 74.07  ? 423  ILE   A HG21 1 
ATOM   6344  H  HG22 . ILE   A  1  423 ? 17.202  -7.508  -26.471  1.00 74.07  ? 423  ILE   A HG22 1 
ATOM   6345  H  HG23 . ILE   A  1  423 ? 17.041  -6.056  -27.096  1.00 74.07  ? 423  ILE   A HG23 1 
ATOM   6346  H  HD11 . ILE   A  1  423 ? 18.909  -6.184  -30.810  1.00 96.30  ? 423  ILE   A HD11 1 
ATOM   6347  H  HD12 . ILE   A  1  423 ? 18.963  -7.615  -30.124  1.00 96.30  ? 423  ILE   A HD12 1 
ATOM   6348  H  HD13 . ILE   A  1  423 ? 17.648  -6.731  -30.014  1.00 96.30  ? 423  ILE   A HD13 1 
ATOM   6349  N  N    . VAL   A  1  424 ? 18.587  -6.784  -24.147  1.00 68.00  ? 424  VAL   A N    1 
ATOM   6350  C  CA   . VAL   A  1  424 ? 18.260  -7.561  -22.958  1.00 62.76  ? 424  VAL   A CA   1 
ATOM   6351  C  C    . VAL   A  1  424 ? 16.751  -7.753  -22.918  1.00 64.35  ? 424  VAL   A C    1 
ATOM   6352  O  O    . VAL   A  1  424 ? 15.995  -6.776  -22.967  1.00 65.33  ? 424  VAL   A O    1 
ATOM   6353  C  CB   . VAL   A  1  424 ? 18.754  -6.877  -21.670  1.00 60.34  ? 424  VAL   A CB   1 
ATOM   6354  C  CG1  . VAL   A  1  424 ? 18.370  -7.708  -20.453  1.00 62.00  ? 424  VAL   A CG1  1 
ATOM   6355  C  CG2  . VAL   A  1  424 ? 20.259  -6.664  -21.722  1.00 60.64  ? 424  VAL   A CG2  1 
ATOM   6356  H  H    . VAL   A  1  424 ? 18.184  -6.025  -24.179  1.00 81.58  ? 424  VAL   A H    1 
ATOM   6357  H  HA   . VAL   A  1  424 ? 18.683  -8.432  -23.020  1.00 75.29  ? 424  VAL   A HA   1 
ATOM   6358  H  HB   . VAL   A  1  424 ? 18.331  -6.008  -21.591  1.00 72.39  ? 424  VAL   A HB   1 
ATOM   6359  H  HG11 . VAL   A  1  424 ? 18.804  -7.338  -19.668  1.00 74.38  ? 424  VAL   A HG11 1 
ATOM   6360  H  HG12 . VAL   A  1  424 ? 17.407  -7.680  -20.342  1.00 74.38  ? 424  VAL   A HG12 1 
ATOM   6361  H  HG13 . VAL   A  1  424 ? 18.661  -8.623  -20.591  1.00 74.38  ? 424  VAL   A HG13 1 
ATOM   6362  H  HG21 . VAL   A  1  424 ? 20.548  -6.252  -20.893  1.00 72.74  ? 424  VAL   A HG21 1 
ATOM   6363  H  HG22 . VAL   A  1  424 ? 20.696  -7.523  -21.834  1.00 72.74  ? 424  VAL   A HG22 1 
ATOM   6364  H  HG23 . VAL   A  1  424 ? 20.470  -6.085  -22.470  1.00 72.74  ? 424  VAL   A HG23 1 
ATOM   6365  N  N    . GLY   A  1  425 ? 16.319  -9.006  -22.829  1.00 63.75  ? 425  GLY   A N    1 
ATOM   6366  C  CA   . GLY   A  1  425 ? 14.911  -9.335  -22.750  1.00 60.95  ? 425  GLY   A CA   1 
ATOM   6367  C  C    . GLY   A  1  425 ? 14.464  -9.563  -21.318  1.00 58.15  ? 425  GLY   A C    1 
ATOM   6368  O  O    . GLY   A  1  425 ? 15.227  -10.036 -20.480  1.00 57.97  ? 425  GLY   A O    1 
ATOM   6369  H  H    . GLY   A  1  425 ? 16.836  -9.693  -22.812  1.00 76.48  ? 425  GLY   A H    1 
ATOM   6370  H  HA2  . GLY   A  1  425 ? 14.387  -8.609  -23.124  1.00 73.12  ? 425  GLY   A HA2  1 
ATOM   6371  H  HA3  . GLY   A  1  425 ? 14.739  -10.143 -23.259  1.00 73.12  ? 425  GLY   A HA3  1 
ATOM   6372  N  N    . ALA   A  1  426 ? 13.208  -9.206  -21.044  1.00 58.35  ? 426  ALA   A N    1 
ATOM   6373  C  CA   . ALA   A  1  426 ? 12.574  -9.460  -19.747  1.00 60.18  ? 426  ALA   A CA   1 
ATOM   6374  C  C    . ALA   A  1  426 ? 11.146  -9.917  -20.041  1.00 62.81  ? 426  ALA   A C    1 
ATOM   6375  O  O    . ALA   A  1  426 ? 10.226  -9.098  -20.117  1.00 66.95  ? 426  ALA   A O    1 
ATOM   6376  C  CB   . ALA   A  1  426 ? 12.606  -8.222  -18.861  1.00 60.58  ? 426  ALA   A CB   1 
ATOM   6377  H  H    . ALA   A  1  426 ? 12.692  -8.808  -21.605  1.00 70.00  ? 426  ALA   A H    1 
ATOM   6378  H  HA   . ALA   A  1  426 ? 13.044  -10.170 -19.284  1.00 72.19  ? 426  ALA   A HA   1 
ATOM   6379  H  HB1  . ALA   A  1  426 ? 12.202  -8.436  -18.005  1.00 72.67  ? 426  ALA   A HB1  1 
ATOM   6380  H  HB2  . ALA   A  1  426 ? 13.528  -7.949  -18.732  1.00 72.67  ? 426  ALA   A HB2  1 
ATOM   6381  H  HB3  . ALA   A  1  426 ? 12.107  -7.511  -19.293  1.00 72.67  ? 426  ALA   A HB3  1 
ATOM   6382  N  N    . PHE   A  1  427 ? 10.965  -11.231 -20.198  1.00 59.22  ? 427  PHE   A N    1 
ATOM   6383  C  CA   . PHE   A  1  427 ? 9.666   -11.750 -20.611  1.00 61.02  ? 427  PHE   A CA   1 
ATOM   6384  C  C    . PHE   A  1  427 ? 8.645   -11.751 -19.481  1.00 65.76  ? 427  PHE   A C    1 
ATOM   6385  O  O    . PHE   A  1  427 ? 7.440   -11.742 -19.758  1.00 69.21  ? 427  PHE   A O    1 
ATOM   6386  C  CB   . PHE   A  1  427 ? 9.816   -13.164 -21.187  1.00 61.55  ? 427  PHE   A CB   1 
ATOM   6387  C  CG   . PHE   A  1  427 ? 10.041  -14.238 -20.156  1.00 59.93  ? 427  PHE   A CG   1 
ATOM   6388  C  CD1  . PHE   A  1  427 ? 8.968   -14.879 -19.556  1.00 58.77  ? 427  PHE   A CD1  1 
ATOM   6389  C  CD2  . PHE   A  1  427 ? 11.324  -14.632 -19.812  1.00 57.14  ? 427  PHE   A CD2  1 
ATOM   6390  C  CE1  . PHE   A  1  427 ? 9.172   -15.875 -18.618  1.00 56.97  ? 427  PHE   A CE1  1 
ATOM   6391  C  CE2  . PHE   A  1  427 ? 11.532  -15.629 -18.874  1.00 55.69  ? 427  PHE   A CE2  1 
ATOM   6392  C  CZ   . PHE   A  1  427 ? 10.455  -16.250 -18.278  1.00 57.12  ? 427  PHE   A CZ   1 
ATOM   6393  H  H    . PHE   A  1  427 ? 11.569  -11.830 -20.072  1.00 71.04  ? 427  PHE   A H    1 
ATOM   6394  H  HA   . PHE   A  1  427 ? 9.319   -11.184 -21.318  1.00 73.20  ? 427  PHE   A HA   1 
ATOM   6395  H  HB2  . PHE   A  1  427 ? 9.005   -13.388 -21.671  1.00 73.84  ? 427  PHE   A HB2  1 
ATOM   6396  H  HB3  . PHE   A  1  427 ? 10.575  -13.174 -21.791  1.00 73.84  ? 427  PHE   A HB3  1 
ATOM   6397  H  HD1  . PHE   A  1  427 ? 8.101   -14.637 -19.788  1.00 70.51  ? 427  PHE   A HD1  1 
ATOM   6398  H  HD2  . PHE   A  1  427 ? 12.055  -14.221 -20.216  1.00 68.54  ? 427  PHE   A HD2  1 
ATOM   6399  H  HE1  . PHE   A  1  427 ? 8.444   -16.291 -18.216  1.00 68.35  ? 427  PHE   A HE1  1 
ATOM   6400  H  HE2  . PHE   A  1  427 ? 12.398  -15.881 -18.647  1.00 66.80  ? 427  PHE   A HE2  1 
ATOM   6401  H  HZ   . PHE   A  1  427 ? 10.593  -16.920 -17.649  1.00 68.52  ? 427  PHE   A HZ   1 
ATOM   6402  N  N    . GLY   A  1  428 ? 9.090   -11.752 -18.224  1.00 64.80  ? 428  GLY   A N    1 
ATOM   6403  C  CA   . GLY   A  1  428 ? 8.149   -11.699 -17.120  1.00 65.94  ? 428  GLY   A CA   1 
ATOM   6404  C  C    . GLY   A  1  428 ? 7.366   -10.403 -17.072  1.00 62.87  ? 428  GLY   A C    1 
ATOM   6405  O  O    . GLY   A  1  428 ? 6.247   -10.368 -16.552  1.00 61.94  ? 428  GLY   A O    1 
ATOM   6406  H  H    . GLY   A  1  428 ? 9.918   -11.783 -17.992  1.00 77.74  ? 428  GLY   A H    1 
ATOM   6407  H  HA2  . GLY   A  1  428 ? 7.519   -12.431 -17.203  1.00 79.11  ? 428  GLY   A HA2  1 
ATOM   6408  H  HA3  . GLY   A  1  428 ? 8.633   -11.791 -16.284  1.00 79.11  ? 428  GLY   A HA3  1 
ATOM   6409  N  N    . VAL   A  1  429 ? 7.938   -9.325  -17.606  1.00 64.16  ? 429  VAL   A N    1 
ATOM   6410  C  CA   . VAL   A  1  429 ? 7.269   -8.034  -17.698  1.00 68.02  ? 429  VAL   A CA   1 
ATOM   6411  C  C    . VAL   A  1  429 ? 7.006   -7.645  -19.146  1.00 72.51  ? 429  VAL   A C    1 
ATOM   6412  O  O    . VAL   A  1  429 ? 6.675   -6.487  -19.423  1.00 75.52  ? 429  VAL   A O    1 
ATOM   6413  C  CB   . VAL   A  1  429 ? 8.070   -6.938  -16.975  1.00 65.81  ? 429  VAL   A CB   1 
ATOM   6414  C  CG1  . VAL   A  1  429 ? 8.081   -7.194  -15.477  1.00 66.19  ? 429  VAL   A CG1  1 
ATOM   6415  C  CG2  . VAL   A  1  429 ? 9.491   -6.868  -17.518  1.00 65.80  ? 429  VAL   A CG2  1 
ATOM   6416  H  H    . VAL   A  1  429 ? 8.735   -9.319  -17.929  1.00 76.97  ? 429  VAL   A H    1 
ATOM   6417  H  HA   . VAL   A  1  429 ? 6.408   -8.110  -17.258  1.00 81.60  ? 429  VAL   A HA   1 
ATOM   6418  H  HB   . VAL   A  1  429 ? 7.645   -6.081  -17.135  1.00 78.95  ? 429  VAL   A HB   1 
ATOM   6419  H  HG11 . VAL   A  1  429 ? 8.597   -6.497  -15.042  1.00 79.41  ? 429  VAL   A HG11 1 
ATOM   6420  H  HG12 . VAL   A  1  429 ? 7.169   -7.184  -15.149  1.00 79.41  ? 429  VAL   A HG12 1 
ATOM   6421  H  HG13 . VAL   A  1  429 ? 8.485   -8.059  -15.308  1.00 79.41  ? 429  VAL   A HG13 1 
ATOM   6422  H  HG21 . VAL   A  1  429 ? 9.956   -6.130  -17.093  1.00 78.94  ? 429  VAL   A HG21 1 
ATOM   6423  H  HG22 . VAL   A  1  429 ? 9.945   -7.702  -17.322  1.00 78.94  ? 429  VAL   A HG22 1 
ATOM   6424  H  HG23 . VAL   A  1  429 ? 9.456   -6.728  -18.477  1.00 78.94  ? 429  VAL   A HG23 1 
ATOM   6425  N  N    . ASP   A  1  430 ? 7.150   -8.584  -20.079  1.00 71.64  ? 430  ASP   A N    1 
ATOM   6426  C  CA   . ASP   A  1  430 ? 6.834   -8.348  -21.485  1.00 67.39  ? 430  ASP   A CA   1 
ATOM   6427  C  C    . ASP   A  1  430 ? 7.588   -7.128  -22.009  1.00 69.63  ? 430  ASP   A C    1 
ATOM   6428  O  O    . ASP   A  1  430 ? 7.021   -6.233  -22.639  1.00 68.87  ? 430  ASP   A O    1 
ATOM   6429  C  CB   . ASP   A  1  430 ? 5.325   -8.190  -21.671  1.00 65.33  ? 430  ASP   A CB   1 
ATOM   6430  C  CG   . ASP   A  1  430 ? 4.547   -9.379  -21.139  1.00 72.23  ? 430  ASP   A CG   1 
ATOM   6431  O  OD1  . ASP   A  1  430 ? 4.761   -10.504 -21.639  1.00 74.05  ? 430  ASP   A OD1  1 
ATOM   6432  O  OD2  . ASP   A  1  430 ? 3.734   -9.193  -20.208  1.00 75.29  ? 430  ASP   A OD2  1 
ATOM   6433  H  H    . ASP   A  1  430 ? 7.434   -9.380  -19.919  1.00 85.95  ? 430  ASP   A H    1 
ATOM   6434  H  HA   . ASP   A  1  430 ? 7.123   -9.113  -22.006  1.00 80.84  ? 430  ASP   A HA   1 
ATOM   6435  H  HB2  . ASP   A  1  430 ? 5.028   -7.399  -21.196  1.00 78.38  ? 430  ASP   A HB2  1 
ATOM   6436  H  HB3  . ASP   A  1  430 ? 5.130   -8.102  -22.617  1.00 78.38  ? 430  ASP   A HB3  1 
ATOM   6437  N  N    . ARG   A  1  431 ? 8.892   -7.103  -21.741  1.00 71.75  ? 431  ARG   A N    1 
ATOM   6438  C  CA   . ARG   A  1  431 ? 9.738   -5.965  -22.062  1.00 76.26  ? 431  ARG   A CA   1 
ATOM   6439  C  C    . ARG   A  1  431 ? 11.021  -6.439  -22.729  1.00 71.76  ? 431  ARG   A C    1 
ATOM   6440  O  O    . ARG   A  1  431 ? 11.478  -7.564  -22.512  1.00 68.80  ? 431  ARG   A O    1 
ATOM   6441  C  CB   . ARG   A  1  431 ? 10.086  -5.160  -20.801  1.00 83.13  ? 431  ARG   A CB   1 
ATOM   6442  C  CG   . ARG   A  1  431 ? 10.233  -3.665  -21.029  1.00 91.16  ? 431  ARG   A CG   1 
ATOM   6443  C  CD   . ARG   A  1  431 ? 8.892   -2.959  -20.905  1.00 95.95  ? 431  ARG   A CD   1 
ATOM   6444  N  NE   . ARG   A  1  431 ? 8.347   -3.067  -19.553  1.00 99.02  ? 431  ARG   A NE   1 
ATOM   6445  C  CZ   . ARG   A  1  431 ? 7.126   -2.680  -19.201  1.00 103.12 ? 431  ARG   A CZ   1 
ATOM   6446  N  NH1  . ARG   A  1  431 ? 6.304   -2.155  -20.101  1.00 104.37 ? 431  ARG   A NH1  1 
ATOM   6447  N  NH2  . ARG   A  1  431 ? 6.723   -2.820  -17.945  1.00 104.66 ? 431  ARG   A NH2  1 
ATOM   6448  H  H    . ARG   A  1  431 ? 9.316   -7.750  -21.366  1.00 86.09  ? 431  ARG   A H    1 
ATOM   6449  H  HA   . ARG   A  1  431 ? 9.272   -5.386  -22.685  1.00 91.49  ? 431  ARG   A HA   1 
ATOM   6450  H  HB2  . ARG   A  1  431 ? 9.381   -5.288  -20.148  1.00 99.74  ? 431  ARG   A HB2  1 
ATOM   6451  H  HB3  . ARG   A  1  431 ? 10.929  -5.486  -20.449  1.00 99.74  ? 431  ARG   A HB3  1 
ATOM   6452  H  HG2  . ARG   A  1  431 ? 10.837  -3.295  -20.367  1.00 109.38 ? 431  ARG   A HG2  1 
ATOM   6453  H  HG3  . ARG   A  1  431 ? 10.581  -3.507  -21.921  1.00 109.38 ? 431  ARG   A HG3  1 
ATOM   6454  H  HD2  . ARG   A  1  431 ? 9.005   -2.018  -21.113  1.00 115.12 ? 431  ARG   A HD2  1 
ATOM   6455  H  HD3  . ARG   A  1  431 ? 8.260   -3.362  -21.521  1.00 115.12 ? 431  ARG   A HD3  1 
ATOM   6456  H  HE   . ARG   A  1  431 ? 8.852   -3.405  -18.944  1.00 118.80 ? 431  ARG   A HE   1 
ATOM   6457  H  HH11 . ARG   A  1  431 ? 6.561   -2.065  -20.917  1.00 125.23 ? 431  ARG   A HH11 1 
ATOM   6458  H  HH12 . ARG   A  1  431 ? 5.515   -1.906  -19.869  1.00 125.23 ? 431  ARG   A HH12 1 
ATOM   6459  H  HH21 . ARG   A  1  431 ? 7.252   -3.162  -17.360  1.00 125.57 ? 431  ARG   A HH21 1 
ATOM   6460  H  HH22 . ARG   A  1  431 ? 5.932   -2.569  -17.717  1.00 125.57 ? 431  ARG   A HH22 1 
ATOM   6461  N  N    . ALA   A  1  432 ? 11.596  -5.558  -23.545  1.00 69.22  ? 432  ALA   A N    1 
ATOM   6462  C  CA   . ALA   A  1  432 ? 12.902  -5.770  -24.154  1.00 64.34  ? 432  ALA   A CA   1 
ATOM   6463  C  C    . ALA   A  1  432 ? 13.610  -4.427  -24.225  1.00 67.05  ? 432  ALA   A C    1 
ATOM   6464  O  O    . ALA   A  1  432 ? 13.007  -3.423  -24.617  1.00 70.05  ? 432  ALA   A O    1 
ATOM   6465  C  CB   . ALA   A  1  432 ? 12.785  -6.390  -25.550  1.00 61.39  ? 432  ALA   A CB   1 
ATOM   6466  H  H    . ALA   A  1  432 ? 11.237  -4.808  -23.766  1.00 83.04  ? 432  ALA   A H    1 
ATOM   6467  H  HA   . ALA   A  1  432 ? 13.427  -6.378  -23.610  1.00 77.19  ? 432  ALA   A HA   1 
ATOM   6468  H  HB1  . ALA   A  1  432 ? 13.675  -6.514  -25.916  1.00 73.65  ? 432  ALA   A HB1  1 
ATOM   6469  H  HB2  . ALA   A  1  432 ? 12.334  -7.245  -25.479  1.00 73.65  ? 432  ALA   A HB2  1 
ATOM   6470  H  HB3  . ALA   A  1  432 ? 12.274  -5.792  -26.119  1.00 73.65  ? 432  ALA   A HB3  1 
ATOM   6471  N  N    . ILE   A  1  433 ? 14.885  -4.409  -23.844  1.00 67.68  ? 433  ILE   A N    1 
ATOM   6472  C  CA   . ILE   A  1  433 ? 15.630  -3.171  -23.660  1.00 68.53  ? 433  ILE   A CA   1 
ATOM   6473  C  C    . ILE   A  1  433 ? 16.892  -3.219  -24.508  1.00 67.52  ? 433  ILE   A C    1 
ATOM   6474  O  O    . ILE   A  1  433 ? 17.603  -4.230  -24.516  1.00 67.57  ? 433  ILE   A O    1 
ATOM   6475  C  CB   . ILE   A  1  433 ? 15.984  -2.939  -22.177  1.00 73.18  ? 433  ILE   A CB   1 
ATOM   6476  C  CG1  . ILE   A  1  433 ? 14.722  -3.004  -21.315  1.00 79.36  ? 433  ILE   A CG1  1 
ATOM   6477  C  CG2  . ILE   A  1  433 ? 16.670  -1.593  -21.991  1.00 74.25  ? 433  ILE   A CG2  1 
ATOM   6478  C  CD1  . ILE   A  1  433 ? 14.432  -4.378  -20.746  1.00 85.15  ? 433  ILE   A CD1  1 
ATOM   6479  H  H    . ILE   A  1  433 ? 15.346  -5.117  -23.684  1.00 81.19  ? 433  ILE   A H    1 
ATOM   6480  H  HA   . ILE   A  1  433 ? 15.091  -2.427  -23.972  1.00 82.21  ? 433  ILE   A HA   1 
ATOM   6481  H  HB   . ILE   A  1  433 ? 16.594  -3.641  -21.901  1.00 87.80  ? 433  ILE   A HB   1 
ATOM   6482  H  HG12 . ILE   A  1  433 ? 14.823  -2.392  -20.569  1.00 95.22  ? 433  ILE   A HG12 1 
ATOM   6483  H  HG13 . ILE   A  1  433 ? 13.961  -2.744  -21.857  1.00 95.22  ? 433  ILE   A HG13 1 
ATOM   6484  H  HG21 . ILE   A  1  433 ? 16.852  -1.459  -21.047  1.00 89.08  ? 433  ILE   A HG21 1 
ATOM   6485  H  HG22 . ILE   A  1  433 ? 17.501  -1.589  -22.492  1.00 89.08  ? 433  ILE   A HG22 1 
ATOM   6486  H  HG23 . ILE   A  1  433 ? 16.084  -0.892  -22.317  1.00 89.08  ? 433  ILE   A HG23 1 
ATOM   6487  H  HD11 . ILE   A  1  433 ? 13.631  -4.331  -20.200  1.00 102.17 ? 433  ILE   A HD11 1 
ATOM   6488  H  HD12 . ILE   A  1  433 ? 14.298  -5.001  -21.477  1.00 102.17 ? 433  ILE   A HD12 1 
ATOM   6489  H  HD13 . ILE   A  1  433 ? 15.185  -4.660  -20.204  1.00 102.17 ? 433  ILE   A HD13 1 
ATOM   6490  N  N    . LEU   A  1  434 ? 17.169  -2.124  -25.214  1.00 69.87  ? 434  LEU   A N    1 
ATOM   6491  C  CA   . LEU   A  1  434 ? 18.388  -1.965  -25.997  1.00 68.76  ? 434  LEU   A CA   1 
ATOM   6492  C  C    . LEU   A  1  434 ? 19.308  -0.992  -25.273  1.00 65.89  ? 434  LEU   A C    1 
ATOM   6493  O  O    . LEU   A  1  434 ? 18.919  0.148   -24.998  1.00 64.10  ? 434  LEU   A O    1 
ATOM   6494  C  CB   . LEU   A  1  434 ? 18.083  -1.457  -27.406  1.00 73.66  ? 434  LEU   A CB   1 
ATOM   6495  C  CG   . LEU   A  1  434 ? 19.311  -1.065  -28.236  1.00 79.33  ? 434  LEU   A CG   1 
ATOM   6496  C  CD1  . LEU   A  1  434 ? 20.151  -2.290  -28.569  1.00 77.86  ? 434  LEU   A CD1  1 
ATOM   6497  C  CD2  . LEU   A  1  434 ? 18.904  -0.330  -29.502  1.00 85.65  ? 434  LEU   A CD2  1 
ATOM   6498  H  H    . LEU   A  1  434 ? 16.648  -1.441  -25.255  1.00 83.83  ? 434  LEU   A H    1 
ATOM   6499  H  HA   . LEU   A  1  434 ? 18.833  -2.824  -26.072  1.00 82.50  ? 434  LEU   A HA   1 
ATOM   6500  H  HB2  . LEU   A  1  434 ? 17.616  -2.156  -27.889  1.00 88.37  ? 434  LEU   A HB2  1 
ATOM   6501  H  HB3  . LEU   A  1  434 ? 17.519  -0.671  -27.332  1.00 88.37  ? 434  LEU   A HB3  1 
ATOM   6502  H  HG   . LEU   A  1  434 ? 19.858  -0.461  -27.710  1.00 95.18  ? 434  LEU   A HG   1 
ATOM   6503  H  HD11 . LEU   A  1  434 ? 20.924  -2.013  -29.084  1.00 93.41  ? 434  LEU   A HD11 1 
ATOM   6504  H  HD12 . LEU   A  1  434 ? 20.438  -2.710  -27.742  1.00 93.41  ? 434  LEU   A HD12 1 
ATOM   6505  H  HD13 . LEU   A  1  434 ? 19.614  -2.911  -29.086  1.00 93.41  ? 434  LEU   A HD13 1 
ATOM   6506  H  HD21 . LEU   A  1  434 ? 19.701  0.001   -29.945  1.00 102.76 ? 434  LEU   A HD21 1 
ATOM   6507  H  HD22 . LEU   A  1  434 ? 18.432  -0.945  -30.086  1.00 102.76 ? 434  LEU   A HD22 1 
ATOM   6508  H  HD23 . LEU   A  1  434 ? 18.325  0.411   -29.264  1.00 102.76 ? 434  LEU   A HD23 1 
ATOM   6509  N  N    . TYR   A  1  435 ? 20.522  -1.442  -24.972  1.00 65.65  ? 435  TYR   A N    1 
ATOM   6510  C  CA   . TYR   A  1  435 ? 21.556  -0.608  -24.377  1.00 65.97  ? 435  TYR   A CA   1 
ATOM   6511  C  C    . TYR   A  1  435 ? 22.589  -0.290  -25.449  1.00 66.10  ? 435  TYR   A C    1 
ATOM   6512  O  O    . TYR   A  1  435 ? 23.146  -1.204  -26.067  1.00 65.23  ? 435  TYR   A O    1 
ATOM   6513  C  CB   . TYR   A  1  435 ? 22.216  -1.310  -23.191  1.00 68.58  ? 435  TYR   A CB   1 
ATOM   6514  C  CG   . TYR   A  1  435 ? 21.293  -1.556  -22.020  1.00 70.69  ? 435  TYR   A CG   1 
ATOM   6515  C  CD1  . TYR   A  1  435 ? 20.558  -2.729  -21.923  1.00 70.10  ? 435  TYR   A CD1  1 
ATOM   6516  C  CD2  . TYR   A  1  435 ? 21.164  -0.617  -21.006  1.00 73.17  ? 435  TYR   A CD2  1 
ATOM   6517  C  CE1  . TYR   A  1  435 ? 19.715  -2.959  -20.850  1.00 69.54  ? 435  TYR   A CE1  1 
ATOM   6518  C  CE2  . TYR   A  1  435 ? 20.325  -0.837  -19.931  1.00 73.69  ? 435  TYR   A CE2  1 
ATOM   6519  C  CZ   . TYR   A  1  435 ? 19.603  -2.008  -19.858  1.00 69.74  ? 435  TYR   A CZ   1 
ATOM   6520  O  OH   . TYR   A  1  435 ? 18.769  -2.228  -18.785  1.00 66.62  ? 435  TYR   A OH   1 
ATOM   6521  H  H    . TYR   A  1  435 ? 20.776  -2.253  -25.108  1.00 78.76  ? 435  TYR   A H    1 
ATOM   6522  H  HA   . TYR   A  1  435 ? 21.165  0.221   -24.059  1.00 79.15  ? 435  TYR   A HA   1 
ATOM   6523  H  HB2  . TYR   A  1  435 ? 22.550  -2.171  -23.488  1.00 82.27  ? 435  TYR   A HB2  1 
ATOM   6524  H  HB3  . TYR   A  1  435 ? 22.951  -0.760  -22.876  1.00 82.27  ? 435  TYR   A HB3  1 
ATOM   6525  H  HD1  . TYR   A  1  435 ? 20.633  -3.372  -22.591  1.00 84.10  ? 435  TYR   A HD1  1 
ATOM   6526  H  HD2  . TYR   A  1  435 ? 21.651  0.174   -21.051  1.00 87.79  ? 435  TYR   A HD2  1 
ATOM   6527  H  HE1  . TYR   A  1  435 ? 19.228  -3.749  -20.799  1.00 83.43  ? 435  TYR   A HE1  1 
ATOM   6528  H  HE2  . TYR   A  1  435 ? 20.248  -0.197  -19.260  1.00 88.40  ? 435  TYR   A HE2  1 
ATOM   6529  H  HH   . TYR   A  1  435 ? 18.527  -3.032  -18.770  1.00 79.92  ? 435  TYR   A HH   1 
ATOM   6530  N  N    . ARG   A  1  436 ? 22.841  0.997   -25.669  1.00 67.86  ? 436  ARG   A N    1 
ATOM   6531  C  CA   . ARG   A  1  436 ? 23.820  1.433   -26.654  1.00 69.93  ? 436  ARG   A CA   1 
ATOM   6532  C  C    . ARG   A  1  436 ? 25.165  1.674   -25.983  1.00 69.46  ? 436  ARG   A C    1 
ATOM   6533  O  O    . ARG   A  1  436 ? 25.231  2.131   -24.838  1.00 68.09  ? 436  ARG   A O    1 
ATOM   6534  C  CB   . ARG   A  1  436 ? 23.345  2.703   -27.360  1.00 74.13  ? 436  ARG   A CB   1 
ATOM   6535  C  CG   . ARG   A  1  436 ? 22.027  2.530   -28.096  1.00 78.64  ? 436  ARG   A CG   1 
ATOM   6536  C  CD   . ARG   A  1  436 ? 21.773  3.682   -29.047  1.00 83.61  ? 436  ARG   A CD   1 
ATOM   6537  N  NE   . ARG   A  1  436 ? 21.646  4.955   -28.345  1.00 87.97  ? 436  ARG   A NE   1 
ATOM   6538  C  CZ   . ARG   A  1  436 ? 21.661  6.142   -28.942  1.00 96.48  ? 436  ARG   A CZ   1 
ATOM   6539  N  NH1  . ARG   A  1  436 ? 21.808  6.223   -30.259  1.00 100.36 ? 436  ARG   A NH1  1 
ATOM   6540  N  NH2  . ARG   A  1  436 ? 21.536  7.249   -28.223  1.00 99.93  ? 436  ARG   A NH2  1 
ATOM   6541  H  H    . ARG   A  1  436 ? 22.452  1.643   -25.255  1.00 81.41  ? 436  ARG   A H    1 
ATOM   6542  H  HA   . ARG   A  1  436 ? 23.936  0.743   -27.325  1.00 83.89  ? 436  ARG   A HA   1 
ATOM   6543  H  HB2  . ARG   A  1  436 ? 23.226  3.402   -26.699  1.00 88.94  ? 436  ARG   A HB2  1 
ATOM   6544  H  HB3  . ARG   A  1  436 ? 24.015  2.970   -28.008  1.00 88.94  ? 436  ARG   A HB3  1 
ATOM   6545  H  HG2  . ARG   A  1  436 ? 22.051  1.708   -28.611  1.00 94.35  ? 436  ARG   A HG2  1 
ATOM   6546  H  HG3  . ARG   A  1  436 ? 21.301  2.498   -27.454  1.00 94.35  ? 436  ARG   A HG3  1 
ATOM   6547  H  HD2  . ARG   A  1  436 ? 22.515  3.752   -29.668  1.00 100.31 ? 436  ARG   A HD2  1 
ATOM   6548  H  HD3  . ARG   A  1  436 ? 20.949  3.520   -29.531  1.00 100.31 ? 436  ARG   A HD3  1 
ATOM   6549  H  HE   . ARG   A  1  436 ? 21.555  4.936   -27.490  1.00 105.55 ? 436  ARG   A HE   1 
ATOM   6550  H  HH11 . ARG   A  1  436 ? 21.893  5.507   -30.727  1.00 120.41 ? 436  ARG   A HH11 1 
ATOM   6551  H  HH12 . ARG   A  1  436 ? 21.818  6.992   -30.644  1.00 120.41 ? 436  ARG   A HH12 1 
ATOM   6552  H  HH21 . ARG   A  1  436 ? 21.445  7.199   -27.369  1.00 119.89 ? 436  ARG   A HH21 1 
ATOM   6553  H  HH22 . ARG   A  1  436 ? 21.546  8.017   -28.610  1.00 119.89 ? 436  ARG   A HH22 1 
ATOM   6554  N  N    . ALA   A  1  437 ? 26.238  1.359   -26.704  1.00 68.47  ? 437  ALA   A N    1 
ATOM   6555  C  CA   . ALA   A  1  437 ? 27.590  1.472   -26.175  1.00 70.07  ? 437  ALA   A CA   1 
ATOM   6556  C  C    . ALA   A  1  437 ? 28.141  2.868   -26.433  1.00 72.38  ? 437  ALA   A C    1 
ATOM   6557  O  O    . ALA   A  1  437 ? 28.123  3.353   -27.569  1.00 66.51  ? 437  ALA   A O    1 
ATOM   6558  C  CB   . ALA   A  1  437 ? 28.503  0.420   -26.806  1.00 69.52  ? 437  ALA   A CB   1 
ATOM   6559  H  H    . ALA   A  1  437 ? 26.206  1.074   -27.515  1.00 82.15  ? 437  ALA   A H    1 
ATOM   6560  H  HA   . ALA   A  1  437 ? 27.569  1.327   -25.217  1.00 84.07  ? 437  ALA   A HA   1 
ATOM   6561  H  HB1  . ALA   A  1  437 ? 29.402  0.533   -26.460  1.00 83.41  ? 437  ALA   A HB1  1 
ATOM   6562  H  HB2  . ALA   A  1  437 ? 28.170  -0.463  -26.580  1.00 83.41  ? 437  ALA   A HB2  1 
ATOM   6563  H  HB3  . ALA   A  1  437 ? 28.501  0.537   -27.769  1.00 83.41  ? 437  ALA   A HB3  1 
ATOM   6564  N  N    . ARG   A  1  438 ? 28.632  3.508   -25.373  1.00 77.03  ? 438  ARG   A N    1 
ATOM   6565  C  CA   . ARG   A  1  438 ? 29.226  4.830   -25.479  1.00 79.68  ? 438  ARG   A CA   1 
ATOM   6566  C  C    . ARG   A  1  438 ? 30.669  4.728   -25.973  1.00 79.60  ? 438  ARG   A C    1 
ATOM   6567  O  O    . ARG   A  1  438 ? 31.367  3.757   -25.671  1.00 80.33  ? 438  ARG   A O    1 
ATOM   6568  C  CB   . ARG   A  1  438 ? 29.201  5.532   -24.126  1.00 83.27  ? 438  ARG   A CB   1 
ATOM   6569  C  CG   . ARG   A  1  438 ? 27.811  5.716   -23.542  1.00 86.36  ? 438  ARG   A CG   1 
ATOM   6570  C  CD   . ARG   A  1  438 ? 27.866  5.985   -22.045  1.00 87.44  ? 438  ARG   A CD   1 
ATOM   6571  N  NE   . ARG   A  1  438 ? 28.583  7.216   -21.720  1.00 87.31  ? 438  ARG   A NE   1 
ATOM   6572  C  CZ   . ARG   A  1  438 ? 28.764  7.671   -20.483  1.00 86.52  ? 438  ARG   A CZ   1 
ATOM   6573  N  NH1  . ARG   A  1  438 ? 28.281  6.999   -19.446  1.00 86.75  ? 438  ARG   A NH1  1 
ATOM   6574  N  NH2  . ARG   A  1  438 ? 29.429  8.801   -20.282  1.00 87.46  ? 438  ARG   A NH2  1 
ATOM   6575  H  H    . ARG   A  1  438 ? 28.632  3.191   -24.573  1.00 92.42  ? 438  ARG   A H    1 
ATOM   6576  H  HA   . ARG   A  1  438 ? 28.721  5.364   -26.112  1.00 95.60  ? 438  ARG   A HA   1 
ATOM   6577  H  HB2  . ARG   A  1  438 ? 29.718  5.007   -23.495  1.00 99.90  ? 438  ARG   A HB2  1 
ATOM   6578  H  HB3  . ARG   A  1  438 ? 29.596  6.412   -24.227  1.00 99.90  ? 438  ARG   A HB3  1 
ATOM   6579  H  HG2  . ARG   A  1  438 ? 27.379  6.470   -23.972  1.00 103.62 ? 438  ARG   A HG2  1 
ATOM   6580  H  HG3  . ARG   A  1  438 ? 27.292  4.909   -23.687  1.00 103.62 ? 438  ARG   A HG3  1 
ATOM   6581  H  HD2  . ARG   A  1  438 ? 26.961  6.066   -21.704  1.00 104.91 ? 438  ARG   A HD2  1 
ATOM   6582  H  HD3  . ARG   A  1  438 ? 28.321  5.249   -21.607  1.00 104.91 ? 438  ARG   A HD3  1 
ATOM   6583  H  HE   . ARG   A  1  438 ? 28.908  7.675   -22.369  1.00 104.75 ? 438  ARG   A HE   1 
ATOM   6584  H  HH11 . ARG   A  1  438 ? 27.850  6.266   -19.571  1.00 104.08 ? 438  ARG   A HH11 1 
ATOM   6585  H  HH12 . ARG   A  1  438 ? 28.400  7.297   -18.648  1.00 104.08 ? 438  ARG   A HH12 1 
ATOM   6586  H  HH21 . ARG   A  1  438 ? 29.743  9.240   -20.952  1.00 104.93 ? 438  ARG   A HH21 1 
ATOM   6587  H  HH22 . ARG   A  1  438 ? 29.545  9.095   -19.483  1.00 104.93 ? 438  ARG   A HH22 1 
ATOM   6588  N  N    . PRO   A  1  439 ? 31.141  5.715   -26.731  1.00 78.87  ? 439  PRO   A N    1 
ATOM   6589  C  CA   . PRO   A  1  439 ? 32.540  5.687   -27.171  1.00 78.70  ? 439  PRO   A CA   1 
ATOM   6590  C  C    . PRO   A  1  439 ? 33.495  5.891   -26.006  1.00 76.84  ? 439  PRO   A C    1 
ATOM   6591  O  O    . PRO   A  1  439 ? 33.178  6.556   -25.017  1.00 76.27  ? 439  PRO   A O    1 
ATOM   6592  C  CB   . PRO   A  1  439 ? 32.624  6.839   -28.180  1.00 82.11  ? 439  PRO   A CB   1 
ATOM   6593  C  CG   . PRO   A  1  439 ? 31.501  7.746   -27.819  1.00 82.22  ? 439  PRO   A CG   1 
ATOM   6594  C  CD   . PRO   A  1  439 ? 30.408  6.862   -27.296  1.00 78.93  ? 439  PRO   A CD   1 
ATOM   6595  H  HA   . PRO   A  1  439 ? 32.748  4.851   -27.619  1.00 94.43  ? 439  PRO   A HA   1 
ATOM   6596  H  HB2  . PRO   A  1  439 ? 33.477  7.292   -28.094  1.00 98.52  ? 439  PRO   A HB2  1 
ATOM   6597  H  HB3  . PRO   A  1  439 ? 32.518  6.497   -29.081  1.00 98.52  ? 439  PRO   A HB3  1 
ATOM   6598  H  HG2  . PRO   A  1  439 ? 31.792  8.372   -27.138  1.00 98.65  ? 439  PRO   A HG2  1 
ATOM   6599  H  HG3  . PRO   A  1  439 ? 31.205  8.228   -28.607  1.00 98.65  ? 439  PRO   A HG3  1 
ATOM   6600  H  HD2  . PRO   A  1  439 ? 29.896  7.316   -26.609  1.00 94.70  ? 439  PRO   A HD2  1 
ATOM   6601  H  HD3  . PRO   A  1  439 ? 29.821  6.577   -28.013  1.00 94.70  ? 439  PRO   A HD3  1 
ATOM   6602  N  N    . VAL   A  1  440 ? 34.683  5.303   -26.136  1.00 76.70  ? 440  VAL   A N    1 
ATOM   6603  C  CA   . VAL   A  1  440 ? 35.664  5.242   -25.057  1.00 77.08  ? 440  VAL   A CA   1 
ATOM   6604  C  C    . VAL   A  1  440 ? 36.826  6.165   -25.392  1.00 79.46  ? 440  VAL   A C    1 
ATOM   6605  O  O    . VAL   A  1  440 ? 37.413  6.071   -26.477  1.00 81.51  ? 440  VAL   A O    1 
ATOM   6606  C  CB   . VAL   A  1  440 ? 36.155  3.801   -24.829  1.00 76.13  ? 440  VAL   A CB   1 
ATOM   6607  C  CG1  . VAL   A  1  440 ? 37.201  3.759   -23.722  1.00 75.68  ? 440  VAL   A CG1  1 
ATOM   6608  C  CG2  . VAL   A  1  440 ? 34.983  2.894   -24.494  1.00 75.04  ? 440  VAL   A CG2  1 
ATOM   6609  H  H    . VAL   A  1  440 ? 34.949  4.923   -26.860  1.00 92.02  ? 440  VAL   A H    1 
ATOM   6610  H  HA   . VAL   A  1  440 ? 35.253  5.563   -24.240  1.00 92.48  ? 440  VAL   A HA   1 
ATOM   6611  H  HB   . VAL   A  1  440 ? 36.570  3.477   -25.644  1.00 91.34  ? 440  VAL   A HB   1 
ATOM   6612  H  HG11 . VAL   A  1  440 ? 37.430  2.834   -23.540  1.00 90.80  ? 440  VAL   A HG11 1 
ATOM   6613  H  HG12 . VAL   A  1  440 ? 37.989  4.243   -24.013  1.00 90.80  ? 440  VAL   A HG12 1 
ATOM   6614  H  HG13 . VAL   A  1  440 ? 36.834  4.172   -22.925  1.00 90.80  ? 440  VAL   A HG13 1 
ATOM   6615  H  HG21 . VAL   A  1  440 ? 35.314  1.997   -24.332  1.00 90.03  ? 440  VAL   A HG21 1 
ATOM   6616  H  HG22 . VAL   A  1  440 ? 34.540  3.231   -23.699  1.00 90.03  ? 440  VAL   A HG22 1 
ATOM   6617  H  HG23 . VAL   A  1  440 ? 34.364  2.889   -25.240  1.00 90.03  ? 440  VAL   A HG23 1 
ATOM   6618  N  N    . ILE   A  1  441 ? 37.159  7.049   -24.457  1.00 79.86  ? 441  ILE   A N    1 
ATOM   6619  C  CA   . ILE   A  1  441 ? 38.281  7.969   -24.594  1.00 82.79  ? 441  ILE   A CA   1 
ATOM   6620  C  C    . ILE   A  1  441 ? 39.439  7.415   -23.773  1.00 85.77  ? 441  ILE   A C    1 
ATOM   6621  O  O    . ILE   A  1  441 ? 39.374  7.373   -22.540  1.00 84.47  ? 441  ILE   A O    1 
ATOM   6622  C  CB   . ILE   A  1  441 ? 37.912  9.388   -24.139  1.00 82.97  ? 441  ILE   A CB   1 
ATOM   6623  C  CG1  . ILE   A  1  441 ? 36.693  9.903   -24.910  1.00 81.68  ? 441  ILE   A CG1  1 
ATOM   6624  C  CG2  . ILE   A  1  441 ? 39.102  10.329  -24.329  1.00 86.54  ? 441  ILE   A CG2  1 
ATOM   6625  C  CD1  . ILE   A  1  441 ? 36.121  11.201  -24.366  1.00 82.10  ? 441  ILE   A CD1  1 
ATOM   6626  H  H    . ILE   A  1  441 ? 36.737  7.136   -23.712  1.00 95.81  ? 441  ILE   A H    1 
ATOM   6627  H  HA   . ILE   A  1  441 ? 38.550  8.003   -25.526  1.00 99.33  ? 441  ILE   A HA   1 
ATOM   6628  H  HB   . ILE   A  1  441 ? 37.685  9.357   -23.196  1.00 99.54  ? 441  ILE   A HB   1 
ATOM   6629  H  HG12 . ILE   A  1  441 ? 36.950  10.058  -25.832  1.00 97.99  ? 441  ILE   A HG12 1 
ATOM   6630  H  HG13 . ILE   A  1  441 ? 35.993  9.232   -24.870  1.00 97.99  ? 441  ILE   A HG13 1 
ATOM   6631  H  HG21 . ILE   A  1  441 ? 38.859  11.213  -24.012  1.00 103.82 ? 441  ILE   A HG21 1 
ATOM   6632  H  HG22 . ILE   A  1  441 ? 39.856  9.991   -23.822  1.00 103.82 ? 441  ILE   A HG22 1 
ATOM   6633  H  HG23 . ILE   A  1  441 ? 39.327  10.366  -25.272  1.00 103.82 ? 441  ILE   A HG23 1 
ATOM   6634  H  HD11 . ILE   A  1  441 ? 35.444  11.529  -24.977  1.00 98.50  ? 441  ILE   A HD11 1 
ATOM   6635  H  HD12 . ILE   A  1  441 ? 35.727  11.032  -23.495  1.00 98.50  ? 441  ILE   A HD12 1 
ATOM   6636  H  HD13 . ILE   A  1  441 ? 36.837  11.851  -24.284  1.00 98.50  ? 441  ILE   A HD13 1 
ATOM   6637  N  N    . THR   A  1  442 ? 40.501  6.986   -24.450  1.00 89.71  ? 442  THR   A N    1 
ATOM   6638  C  CA   . THR   A  1  442 ? 41.738  6.631   -23.768  1.00 92.29  ? 442  THR   A CA   1 
ATOM   6639  C  C    . THR   A  1  442 ? 42.519  7.903   -23.462  1.00 92.83  ? 442  THR   A C    1 
ATOM   6640  O  O    . THR   A  1  442 ? 42.723  8.743   -24.344  1.00 90.86  ? 442  THR   A O    1 
ATOM   6641  C  CB   . THR   A  1  442 ? 42.576  5.684   -24.626  1.00 95.75  ? 442  THR   A CB   1 
ATOM   6642  O  OG1  . THR   A  1  442 ? 41.846  4.473   -24.858  1.00 94.16  ? 442  THR   A OG1  1 
ATOM   6643  C  CG2  . THR   A  1  442 ? 43.892  5.355   -23.934  1.00 97.79  ? 442  THR   A CG2  1 
ATOM   6644  H  H    . THR   A  1  442 ? 40.529  6.892   -25.304  1.00 107.64 ? 442  THR   A H    1 
ATOM   6645  H  HA   . THR   A  1  442 ? 41.537  6.174   -22.937  1.00 110.73 ? 442  THR   A HA   1 
ATOM   6646  H  HB   . THR   A  1  442 ? 42.776  6.110   -25.474  1.00 114.88 ? 442  THR   A HB   1 
ATOM   6647  H  HG1  . THR   A  1  442 ? 42.352  3.893   -25.195  1.00 112.97 ? 442  THR   A HG1  1 
ATOM   6648  H  HG21 . THR   A  1  442 ? 44.359  4.659   -24.423  1.00 117.33 ? 442  THR   A HG21 1 
ATOM   6649  H  HG22 . THR   A  1  442 ? 44.454  6.145   -23.898  1.00 117.33 ? 442  THR   A HG22 1 
ATOM   6650  H  HG23 . THR   A  1  442 ? 43.724  5.047   -23.030  1.00 117.33 ? 442  THR   A HG23 1 
ATOM   6651  N  N    . VAL   A  1  443 ? 42.953  8.047   -22.212  1.00 93.39  ? 443  VAL   A N    1 
ATOM   6652  C  CA   . VAL   A  1  443 ? 43.605  9.262   -21.738  1.00 93.90  ? 443  VAL   A CA   1 
ATOM   6653  C  C    . VAL   A  1  443 ? 45.010  8.918   -21.265  1.00 92.76  ? 443  VAL   A C    1 
ATOM   6654  O  O    . VAL   A  1  443 ? 45.201  7.961   -20.505  1.00 90.78  ? 443  VAL   A O    1 
ATOM   6655  C  CB   . VAL   A  1  443 ? 42.797  9.933   -20.611  1.00 93.43  ? 443  VAL   A CB   1 
ATOM   6656  C  CG1  . VAL   A  1  443 ? 43.516  11.176  -20.111  1.00 94.16  ? 443  VAL   A CG1  1 
ATOM   6657  C  CG2  . VAL   A  1  443 ? 41.399  10.281  -21.100  1.00 93.35  ? 443  VAL   A CG2  1 
ATOM   6658  H  H    . VAL   A  1  443 ? 42.879  7.439   -21.608  1.00 112.05 ? 443  VAL   A H    1 
ATOM   6659  H  HA   . VAL   A  1  443 ? 43.683  9.885   -22.476  1.00 112.66 ? 443  VAL   A HA   1 
ATOM   6660  H  HB   . VAL   A  1  443 ? 42.714  9.314   -19.868  1.00 112.10 ? 443  VAL   A HB   1 
ATOM   6661  H  HG11 . VAL   A  1  443 ? 42.896  11.712  -19.592  1.00 112.97 ? 443  VAL   A HG11 1 
ATOM   6662  H  HG12 . VAL   A  1  443 ? 44.265  10.906  -19.557  1.00 112.97 ? 443  VAL   A HG12 1 
ATOM   6663  H  HG13 . VAL   A  1  443 ? 43.835  11.684  -20.874  1.00 112.97 ? 443  VAL   A HG13 1 
ATOM   6664  H  HG21 . VAL   A  1  443 ? 40.958  10.829  -20.432  1.00 112.00 ? 443  VAL   A HG21 1 
ATOM   6665  H  HG22 . VAL   A  1  443 ? 41.469  10.770  -21.935  1.00 112.00 ? 443  VAL   A HG22 1 
ATOM   6666  H  HG23 . VAL   A  1  443 ? 40.899  9.461   -21.237  1.00 112.00 ? 443  VAL   A HG23 1 
ATOM   6667  N  N    . ASN   A  1  444 ? 45.987  9.701   -21.717  1.00 94.20  ? 444  ASN   A N    1 
ATOM   6668  C  CA   . ASN   A  1  444 ? 47.382  9.573   -21.307  1.00 95.87  ? 444  ASN   A CA   1 
ATOM   6669  C  C    . ASN   A  1  444 ? 47.735  10.790  -20.460  1.00 94.17  ? 444  ASN   A C    1 
ATOM   6670  O  O    . ASN   A  1  444 ? 47.792  11.913  -20.974  1.00 96.79  ? 444  ASN   A O    1 
ATOM   6671  C  CB   . ASN   A  1  444 ? 48.302  9.470   -22.521  1.00 101.77 ? 444  ASN   A CB   1 
ATOM   6672  C  CG   . ASN   A  1  444 ? 48.364  8.068   -23.091  1.00 106.15 ? 444  ASN   A CG   1 
ATOM   6673  O  OD1  . ASN   A  1  444 ? 47.346  7.495   -23.479  1.00 107.86 ? 444  ASN   A OD1  1 
ATOM   6674  N  ND2  . ASN   A  1  444 ? 49.569  7.513   -23.159  1.00 107.05 ? 444  ASN   A ND2  1 
ATOM   6675  H  H    . ASN   A  1  444 ? 45.861  10.337  -22.282  1.00 113.02 ? 444  ASN   A H    1 
ATOM   6676  H  HA   . ASN   A  1  444 ? 47.491  8.773   -20.770  1.00 115.02 ? 444  ASN   A HA   1 
ATOM   6677  H  HB2  . ASN   A  1  444 ? 47.975  10.062  -23.217  1.00 122.10 ? 444  ASN   A HB2  1 
ATOM   6678  H  HB3  . ASN   A  1  444 ? 49.200  9.728   -22.261  1.00 122.10 ? 444  ASN   A HB3  1 
ATOM   6679  H  HD21 . ASN   A  1  444 ? 49.659  6.718   -23.474  1.00 128.44 ? 444  ASN   A HD21 1 
ATOM   6680  H  HD22 . ASN   A  1  444 ? 50.259  7.949   -22.887  1.00 128.44 ? 444  ASN   A HD22 1 
ATOM   6681  N  N    . ALA   A  1  445 ? 47.966  10.570  -19.170  1.00 89.21  ? 445  ALA   A N    1 
ATOM   6682  C  CA   . ALA   A  1  445 ? 48.317  11.632  -18.241  1.00 85.32  ? 445  ALA   A CA   1 
ATOM   6683  C  C    . ALA   A  1  445 ? 49.786  11.530  -17.852  1.00 83.49  ? 445  ALA   A C    1 
ATOM   6684  O  O    . ALA   A  1  445 ? 50.417  10.478  -17.980  1.00 82.73  ? 445  ALA   A O    1 
ATOM   6685  C  CB   . ALA   A  1  445 ? 47.441  11.578  -16.985  1.00 83.92  ? 445  ALA   A CB   1 
ATOM   6686  H  H    . ALA   A  1  445 ? 47.924  9.793   -18.803  1.00 107.04 ? 445  ALA   A H    1 
ATOM   6687  H  HA   . ALA   A  1  445 ? 48.176  12.490  -18.672  1.00 102.36 ? 445  ALA   A HA   1 
ATOM   6688  H  HB1  . ALA   A  1  445 ? 47.664  12.328  -16.412  1.00 100.69 ? 445  ALA   A HB1  1 
ATOM   6689  H  HB2  . ALA   A  1  445 ? 46.508  11.628  -17.248  1.00 100.69 ? 445  ALA   A HB2  1 
ATOM   6690  H  HB3  . ALA   A  1  445 ? 47.609  10.744  -16.519  1.00 100.69 ? 445  ALA   A HB3  1 
ATOM   6691  N  N    . GLY   A  1  446 ? 50.321  12.644  -17.373  1.00 83.89  ? 446  GLY   A N    1 
ATOM   6692  C  CA   . GLY   A  1  446 ? 51.706  12.695  -16.936  1.00 87.49  ? 446  GLY   A CA   1 
ATOM   6693  C  C    . GLY   A  1  446 ? 51.876  13.723  -15.842  1.00 94.35  ? 446  GLY   A C    1 
ATOM   6694  O  O    . GLY   A  1  446 ? 51.196  14.754  -15.823  1.00 98.99  ? 446  GLY   A O    1 
ATOM   6695  H  H    . GLY   A  1  446 ? 49.900  13.389  -17.290  1.00 100.64 ? 446  GLY   A H    1 
ATOM   6696  H  HA2  . GLY   A  1  446 ? 51.976  11.828  -16.597  1.00 104.97 ? 446  GLY   A HA2  1 
ATOM   6697  H  HA3  . GLY   A  1  446 ? 52.277  12.935  -17.683  1.00 104.97 ? 446  GLY   A HA3  1 
ATOM   6698  N  N    . LEU   A  1  447 ? 52.794  13.437  -14.921  1.00 94.03  ? 447  LEU   A N    1 
ATOM   6699  C  CA   . LEU   A  1  447 ? 53.054  14.311  -13.783  1.00 92.46  ? 447  LEU   A CA   1 
ATOM   6700  C  C    . LEU   A  1  447 ? 54.542  14.276  -13.474  1.00 96.11  ? 447  LEU   A C    1 
ATOM   6701  O  O    . LEU   A  1  447 ? 55.101  13.203  -13.230  1.00 98.68  ? 447  LEU   A O    1 
ATOM   6702  C  CB   . LEU   A  1  447 ? 52.237  13.881  -12.561  1.00 88.37  ? 447  LEU   A CB   1 
ATOM   6703  C  CG   . LEU   A  1  447 ? 52.385  14.746  -11.308  1.00 90.25  ? 447  LEU   A CG   1 
ATOM   6704  C  CD1  . LEU   A  1  447 ? 51.866  16.155  -11.550  1.00 91.55  ? 447  LEU   A CD1  1 
ATOM   6705  C  CD2  . LEU   A  1  447 ? 51.662  14.102  -10.135  1.00 90.41  ? 447  LEU   A CD2  1 
ATOM   6706  H  H    . LEU   A  1  447 ? 53.285  12.731  -14.935  1.00 112.82 ? 447  LEU   A H    1 
ATOM   6707  H  HA   . LEU   A  1  447 ? 52.811  15.223  -14.009  1.00 110.94 ? 447  LEU   A HA   1 
ATOM   6708  H  HB2  . LEU   A  1  447 ? 51.299  13.892  -12.807  1.00 106.03 ? 447  LEU   A HB2  1 
ATOM   6709  H  HB3  . LEU   A  1  447 ? 52.506  12.981  -12.320  1.00 106.03 ? 447  LEU   A HB3  1 
ATOM   6710  H  HG   . LEU   A  1  447 ? 53.326  14.816  -11.085  1.00 108.28 ? 447  LEU   A HG   1 
ATOM   6711  H  HD11 . LEU   A  1  447 ? 51.945  16.666  -10.730  1.00 109.84 ? 447  LEU   A HD11 1 
ATOM   6712  H  HD12 . LEU   A  1  447 ? 52.393  16.570  -12.251  1.00 109.84 ? 447  LEU   A HD12 1 
ATOM   6713  H  HD13 . LEU   A  1  447 ? 50.936  16.107  -11.821  1.00 109.84 ? 447  LEU   A HD13 1 
ATOM   6714  H  HD21 . LEU   A  1  447 ? 51.765  14.667  -9.353   1.00 108.47 ? 447  LEU   A HD21 1 
ATOM   6715  H  HD22 . LEU   A  1  447 ? 50.722  14.010  -10.356  1.00 108.47 ? 447  LEU   A HD22 1 
ATOM   6716  H  HD23 . LEU   A  1  447 ? 52.050  13.229  -9.966   1.00 108.47 ? 447  LEU   A HD23 1 
ATOM   6717  N  N    . GLU   A  1  448 ? 55.178  15.446  -13.484  1.00 98.00  ? 448  GLU   A N    1 
ATOM   6718  C  CA   . GLU   A  1  448 ? 56.606  15.572  -13.235  1.00 101.40 ? 448  GLU   A CA   1 
ATOM   6719  C  C    . GLU   A  1  448 ? 56.839  16.581  -12.120  1.00 98.35  ? 448  GLU   A C    1 
ATOM   6720  O  O    . GLU   A  1  448 ? 56.223  17.651  -12.102  1.00 98.12  ? 448  GLU   A O    1 
ATOM   6721  C  CB   . GLU   A  1  448 ? 57.354  16.010  -14.500  1.00 112.36 ? 448  GLU   A CB   1 
ATOM   6722  C  CG   . GLU   A  1  448 ? 57.107  15.120  -15.710  1.00 119.36 ? 448  GLU   A CG   1 
ATOM   6723  C  CD   . GLU   A  1  448 ? 57.767  15.652  -16.968  1.00 126.45 ? 448  GLU   A CD   1 
ATOM   6724  O  OE1  . GLU   A  1  448 ? 58.602  16.574  -16.856  1.00 130.34 ? 448  GLU   A OE1  1 
ATOM   6725  O  OE2  . GLU   A  1  448 ? 57.449  15.151  -18.067  1.00 126.96 ? 448  GLU   A OE2  1 
ATOM   6726  H  H    . GLU   A  1  448 ? 54.790  16.199  -13.636  1.00 117.58 ? 448  GLU   A H    1 
ATOM   6727  H  HA   . GLU   A  1  448 ? 56.964  14.716  -12.950  1.00 121.66 ? 448  GLU   A HA   1 
ATOM   6728  H  HB2  . GLU   A  1  448 ? 57.070  16.908  -14.733  1.00 134.82 ? 448  GLU   A HB2  1 
ATOM   6729  H  HB3  . GLU   A  1  448 ? 58.306  16.000  -14.317  1.00 134.82 ? 448  GLU   A HB3  1 
ATOM   6730  H  HG2  . GLU   A  1  448 ? 57.466  14.237  -15.532  1.00 143.21 ? 448  GLU   A HG2  1 
ATOM   6731  H  HG3  . GLU   A  1  448 ? 56.152  15.063  -15.872  1.00 143.21 ? 448  GLU   A HG3  1 
ATOM   6732  N  N    . VAL   A  1  449 ? 57.728  16.233  -11.193  1.00 96.66  ? 449  VAL   A N    1 
ATOM   6733  C  CA   . VAL   A  1  449 ? 58.075  17.083  -10.059  1.00 97.25  ? 449  VAL   A CA   1 
ATOM   6734  C  C    . VAL   A  1  449 ? 59.588  17.250  -10.067  1.00 101.11 ? 449  VAL   A C    1 
ATOM   6735  O  O    . VAL   A  1  449 ? 60.324  16.288  -9.815   1.00 103.37 ? 449  VAL   A O    1 
ATOM   6736  C  CB   . VAL   A  1  449 ? 57.600  16.494  -8.723   1.00 92.40  ? 449  VAL   A CB   1 
ATOM   6737  C  CG1  . VAL   A  1  449 ? 57.998  17.398  -7.563   1.00 93.55  ? 449  VAL   A CG1  1 
ATOM   6738  C  CG2  . VAL   A  1  449 ? 56.096  16.279  -8.744   1.00 90.74  ? 449  VAL   A CG2  1 
ATOM   6739  H  H    . VAL   A  1  449 ? 58.155  15.487  -11.201  1.00 115.97 ? 449  VAL   A H    1 
ATOM   6740  H  HA   . VAL   A  1  449 ? 57.667  17.955  -10.172  1.00 116.68 ? 449  VAL   A HA   1 
ATOM   6741  H  HB   . VAL   A  1  449 ? 58.027  15.633  -8.591   1.00 110.86 ? 449  VAL   A HB   1 
ATOM   6742  H  HG11 . VAL   A  1  449 ? 57.629  17.039  -6.741   1.00 112.24 ? 449  VAL   A HG11 1 
ATOM   6743  H  HG12 . VAL   A  1  449 ? 58.966  17.429  -7.505   1.00 112.24 ? 449  VAL   A HG12 1 
ATOM   6744  H  HG13 . VAL   A  1  449 ? 57.648  18.289  -7.722   1.00 112.24 ? 449  VAL   A HG13 1 
ATOM   6745  H  HG21 . VAL   A  1  449 ? 55.819  15.903  -7.894   1.00 108.86 ? 449  VAL   A HG21 1 
ATOM   6746  H  HG22 . VAL   A  1  449 ? 55.657  17.132  -8.887   1.00 108.86 ? 449  VAL   A HG22 1 
ATOM   6747  H  HG23 . VAL   A  1  449 ? 55.874  15.668  -9.464   1.00 108.86 ? 449  VAL   A HG23 1 
ATOM   6748  N  N    . TYR   A  1  450 ? 60.056  18.468  -10.354  1.00 101.61 ? 450  TYR   A N    1 
ATOM   6749  C  CA   . TYR   A  1  450 ? 61.482  18.765  -10.398  1.00 105.20 ? 450  TYR   A CA   1 
ATOM   6750  C  C    . TYR   A  1  450 ? 61.737  20.083  -9.672   1.00 108.98 ? 450  TYR   A C    1 
ATOM   6751  O  O    . TYR   A  1  450 ? 61.064  21.088  -9.966   1.00 113.78 ? 450  TYR   A O    1 
ATOM   6752  C  CB   . TYR   A  1  450 ? 61.990  18.842  -11.842  1.00 106.85 ? 450  TYR   A CB   1 
ATOM   6753  C  CG   . TYR   A  1  450 ? 61.191  19.774  -12.725  1.00 109.91 ? 450  TYR   A CG   1 
ATOM   6754  C  CD1  . TYR   A  1  450 ? 60.021  19.347  -13.338  1.00 108.05 ? 450  TYR   A CD1  1 
ATOM   6755  C  CD2  . TYR   A  1  450 ? 61.609  21.078  -12.950  1.00 114.82 ? 450  TYR   A CD2  1 
ATOM   6756  C  CE1  . TYR   A  1  450 ? 59.287  20.193  -14.146  1.00 110.88 ? 450  TYR   A CE1  1 
ATOM   6757  C  CE2  . TYR   A  1  450 ? 60.881  21.932  -13.757  1.00 117.26 ? 450  TYR   A CE2  1 
ATOM   6758  C  CZ   . TYR   A  1  450 ? 59.720  21.484  -14.352  1.00 115.95 ? 450  TYR   A CZ   1 
ATOM   6759  O  OH   . TYR   A  1  450 ? 58.989  22.326  -15.157  1.00 119.30 ? 450  TYR   A OH   1 
ATOM   6760  H  H    . TYR   A  1  450 ? 59.556  19.146  -10.528  1.00 121.91 ? 450  TYR   A H    1 
ATOM   6761  H  HA   . TYR   A  1  450 ? 61.962  18.063  -9.930   1.00 126.22 ? 450  TYR   A HA   1 
ATOM   6762  H  HB2  . TYR   A  1  450 ? 62.907  19.157  -11.833  1.00 128.20 ? 450  TYR   A HB2  1 
ATOM   6763  H  HB3  . TYR   A  1  450 ? 61.948  17.955  -12.234  1.00 128.20 ? 450  TYR   A HB3  1 
ATOM   6764  H  HD1  . TYR   A  1  450 ? 59.725  18.476  -13.201  1.00 129.64 ? 450  TYR   A HD1  1 
ATOM   6765  H  HD2  . TYR   A  1  450 ? 62.392  21.383  -12.551  1.00 137.76 ? 450  TYR   A HD2  1 
ATOM   6766  H  HE1  . TYR   A  1  450 ? 58.505  19.893  -14.550  1.00 133.04 ? 450  TYR   A HE1  1 
ATOM   6767  H  HE2  . TYR   A  1  450 ? 61.173  22.804  -13.899  1.00 140.69 ? 450  TYR   A HE2  1 
ATOM   6768  H  HH   . TYR   A  1  450 ? 59.032  23.112  -14.866  1.00 143.14 ? 450  TYR   A HH   1 
ATOM   6769  N  N    . PRO   A  1  451 ? 62.691  20.126  -8.723   1.00 108.02 ? 451  PRO   A N    1 
ATOM   6770  C  CA   . PRO   A  1  451 ? 63.531  19.008  -8.272   1.00 106.90 ? 451  PRO   A CA   1 
ATOM   6771  C  C    . PRO   A  1  451 ? 62.769  18.010  -7.407   1.00 103.37 ? 451  PRO   A C    1 
ATOM   6772  O  O    . PRO   A  1  451 ? 61.758  18.368  -6.804   1.00 100.52 ? 451  PRO   A O    1 
ATOM   6773  C  CB   . PRO   A  1  451 ? 64.632  19.702  -7.465   1.00 110.74 ? 451  PRO   A CB   1 
ATOM   6774  C  CG   . PRO   A  1  451 ? 63.994  20.941  -6.958   1.00 111.41 ? 451  PRO   A CG   1 
ATOM   6775  C  CD   . PRO   A  1  451 ? 63.036  21.382  -8.032   1.00 110.49 ? 451  PRO   A CD   1 
ATOM   6776  H  HA   . PRO   A  1  451 ? 63.925  18.544  -9.027   1.00 128.26 ? 451  PRO   A HA   1 
ATOM   6777  H  HB2  . PRO   A  1  451 ? 64.918  19.132  -6.734   1.00 132.87 ? 451  PRO   A HB2  1 
ATOM   6778  H  HB3  . PRO   A  1  451 ? 65.386  19.908  -8.040   1.00 132.87 ? 451  PRO   A HB3  1 
ATOM   6779  H  HG2  . PRO   A  1  451 ? 63.521  20.751  -6.133   1.00 133.68 ? 451  PRO   A HG2  1 
ATOM   6780  H  HG3  . PRO   A  1  451 ? 64.671  21.618  -6.804   1.00 133.68 ? 451  PRO   A HG3  1 
ATOM   6781  H  HD2  . PRO   A  1  451 ? 62.246  21.789  -7.642   1.00 132.57 ? 451  PRO   A HD2  1 
ATOM   6782  H  HD3  . PRO   A  1  451 ? 63.464  22.004  -8.641   1.00 132.57 ? 451  PRO   A HD3  1 
ATOM   6783  N  N    . SER   A  1  452 ? 63.256  16.769  -7.349   1.00 108.14 ? 452  SER   A N    1 
ATOM   6784  C  CA   . SER   A  1  452 ? 62.578  15.735  -6.574   1.00 108.39 ? 452  SER   A CA   1 
ATOM   6785  C  C    . SER   A  1  452 ? 62.990  15.785  -5.107   1.00 111.33 ? 452  SER   A C    1 
ATOM   6786  O  O    . SER   A  1  452 ? 62.136  15.759  -4.214   1.00 113.82 ? 452  SER   A O    1 
ATOM   6787  C  CB   . SER   A  1  452 ? 62.871  14.357  -7.170   1.00 104.75 ? 452  SER   A CB   1 
ATOM   6788  O  OG   . SER   A  1  452 ? 62.193  13.339  -6.456   1.00 103.69 ? 452  SER   A OG   1 
ATOM   6789  H  H    . SER   A  1  452 ? 63.971  16.504  -7.747   1.00 129.75 ? 452  SER   A H    1 
ATOM   6790  H  HA   . SER   A  1  452 ? 61.621  15.885  -6.622   1.00 130.04 ? 452  SER   A HA   1 
ATOM   6791  H  HB2  . SER   A  1  452 ? 62.577  14.344  -8.094   1.00 125.68 ? 452  SER   A HB2  1 
ATOM   6792  H  HB3  . SER   A  1  452 ? 63.826  14.191  -7.124   1.00 125.68 ? 452  SER   A HB3  1 
ATOM   6793  H  HG   . SER   A  1  452 ? 62.363  12.589  -6.794   1.00 124.41 ? 452  SER   A HG   1 
ATOM   6794  N  N    . ILE   A  1  453 ? 64.291  15.851  -4.840   1.00 107.80 ? 453  ILE   A N    1 
ATOM   6795  C  CA   . ILE   A  1  453 ? 64.800  15.981  -3.480   1.00 105.51 ? 453  ILE   A CA   1 
ATOM   6796  C  C    . ILE   A  1  453 ? 64.811  17.459  -3.113   1.00 106.56 ? 453  ILE   A C    1 
ATOM   6797  O  O    . ILE   A  1  453 ? 65.245  18.304  -3.905   1.00 104.55 ? 453  ILE   A O    1 
ATOM   6798  C  CB   . ILE   A  1  453 ? 66.202  15.363  -3.353   1.00 104.72 ? 453  ILE   A CB   1 
ATOM   6799  C  CG1  . ILE   A  1  453 ? 66.158  13.866  -3.673   1.00 101.85 ? 453  ILE   A CG1  1 
ATOM   6800  C  CG2  . ILE   A  1  453 ? 66.760  15.573  -1.951   1.00 105.01 ? 453  ILE   A CG2  1 
ATOM   6801  C  CD1  . ILE   A  1  453 ? 66.440  13.534  -5.122   1.00 100.96 ? 453  ILE   A CD1  1 
ATOM   6802  H  H    . ILE   A  1  453 ? 64.907  15.821  -5.440   1.00 129.34 ? 453  ILE   A H    1 
ATOM   6803  H  HA   . ILE   A  1  453 ? 64.211  15.515  -2.867   1.00 126.59 ? 453  ILE   A HA   1 
ATOM   6804  H  HB   . ILE   A  1  453 ? 66.782  15.808  -3.991   1.00 125.64 ? 453  ILE   A HB   1 
ATOM   6805  H  HG12 . ILE   A  1  453 ? 66.824  13.413  -3.132   1.00 122.20 ? 453  ILE   A HG12 1 
ATOM   6806  H  HG13 . ILE   A  1  453 ? 65.273  13.529  -3.461   1.00 122.20 ? 453  ILE   A HG13 1 
ATOM   6807  H  HG21 . ILE   A  1  453 ? 67.617  15.125  -1.881   1.00 125.99 ? 453  ILE   A HG21 1 
ATOM   6808  H  HG22 . ILE   A  1  453 ? 66.869  16.524  -1.793   1.00 125.99 ? 453  ILE   A HG22 1 
ATOM   6809  H  HG23 . ILE   A  1  453 ? 66.139  15.201  -1.305   1.00 125.99 ? 453  ILE   A HG23 1 
ATOM   6810  H  HD11 . ILE   A  1  453 ? 66.447  12.570  -5.230   1.00 121.13 ? 453  ILE   A HD11 1 
ATOM   6811  H  HD12 . ILE   A  1  453 ? 65.746  13.924  -5.676   1.00 121.13 ? 453  ILE   A HD12 1 
ATOM   6812  H  HD13 . ILE   A  1  453 ? 67.304  13.901  -5.368   1.00 121.13 ? 453  ILE   A HD13 1 
ATOM   6813  N  N    . LEU   A  1  454 ? 64.337  17.771  -1.909   1.00 106.18 ? 454  LEU   A N    1 
ATOM   6814  C  CA   . LEU   A  1  454 ? 64.144  19.145  -1.466   1.00 106.01 ? 454  LEU   A CA   1 
ATOM   6815  C  C    . LEU   A  1  454 ? 64.986  19.408  -0.227   1.00 107.98 ? 454  LEU   A C    1 
ATOM   6816  O  O    . LEU   A  1  454 ? 64.987  18.603  0.710    1.00 107.92 ? 454  LEU   A O    1 
ATOM   6817  C  CB   . LEU   A  1  454 ? 62.666  19.413  -1.164   1.00 103.63 ? 454  LEU   A CB   1 
ATOM   6818  C  CG   . LEU   A  1  454 ? 61.676  18.982  -2.248   1.00 101.75 ? 454  LEU   A CG   1 
ATOM   6819  C  CD1  . LEU   A  1  454 ? 60.251  19.048  -1.724   1.00 99.35  ? 454  LEU   A CD1  1 
ATOM   6820  C  CD2  . LEU   A  1  454 ? 61.832  19.839  -3.494   1.00 102.51 ? 454  LEU   A CD2  1 
ATOM   6821  H  H    . LEU   A  1  454 ? 64.116  17.188  -1.317   1.00 127.40 ? 454  LEU   A H    1 
ATOM   6822  H  HA   . LEU   A  1  454 ? 64.436  19.753  -2.163   1.00 127.19 ? 454  LEU   A HA   1 
ATOM   6823  H  HB2  . LEU   A  1  454 ? 62.431  18.937  -0.353   1.00 124.34 ? 454  LEU   A HB2  1 
ATOM   6824  H  HB3  . LEU   A  1  454 ? 62.552  20.368  -1.033   1.00 124.34 ? 454  LEU   A HB3  1 
ATOM   6825  H  HG   . LEU   A  1  454 ? 61.864  18.063  -2.497   1.00 122.08 ? 454  LEU   A HG   1 
ATOM   6826  H  HD11 . LEU   A  1  454 ? 59.639  18.818  -2.441   1.00 119.20 ? 454  LEU   A HD11 1 
ATOM   6827  H  HD12 . LEU   A  1  454 ? 60.154  18.419  -0.992   1.00 119.20 ? 454  LEU   A HD12 1 
ATOM   6828  H  HD13 . LEU   A  1  454 ? 60.070  19.948  -1.412   1.00 119.20 ? 454  LEU   A HD13 1 
ATOM   6829  H  HD21 . LEU   A  1  454 ? 61.162  19.575  -4.144   1.00 122.99 ? 454  LEU   A HD21 1 
ATOM   6830  H  HD22 . LEU   A  1  454 ? 61.710  20.771  -3.253   1.00 122.99 ? 454  LEU   A HD22 1 
ATOM   6831  H  HD23 . LEU   A  1  454 ? 62.720  19.705  -3.860   1.00 122.99 ? 454  LEU   A HD23 1 
ATOM   6832  N  N    . ASN   A  1  455 ? 65.698  20.532  -0.225   1.00 110.31 ? 455  ASN   A N    1 
ATOM   6833  C  CA   . ASN   A  1  455 ? 66.489  20.970  0.919    1.00 113.60 ? 455  ASN   A CA   1 
ATOM   6834  C  C    . ASN   A  1  455 ? 65.811  22.184  1.541    1.00 115.31 ? 455  ASN   A C    1 
ATOM   6835  O  O    . ASN   A  1  455 ? 65.706  23.236  0.902    1.00 114.80 ? 455  ASN   A O    1 
ATOM   6836  C  CB   . ASN   A  1  455 ? 67.922  21.308  0.506    1.00 115.44 ? 455  ASN   A CB   1 
ATOM   6837  C  CG   . ASN   A  1  455 ? 68.801  21.672  1.692    1.00 118.71 ? 455  ASN   A CG   1 
ATOM   6838  O  OD1  . ASN   A  1  455 ? 68.316  21.844  2.810    1.00 120.64 ? 455  ASN   A OD1  1 
ATOM   6839  N  ND2  . ASN   A  1  455 ? 70.101  21.798  1.449    1.00 120.50 ? 455  ASN   A ND2  1 
ATOM   6840  H  H    . ASN   A  1  455 ? 65.738  21.072  -0.894   1.00 132.35 ? 455  ASN   A H    1 
ATOM   6841  H  HA   . ASN   A  1  455 ? 66.524  20.259  1.578    1.00 136.30 ? 455  ASN   A HA   1 
ATOM   6842  H  HB2  . ASN   A  1  455 ? 68.314  20.538  0.066    1.00 138.50 ? 455  ASN   A HB2  1 
ATOM   6843  H  HB3  . ASN   A  1  455 ? 67.906  22.065  -0.100   1.00 138.50 ? 455  ASN   A HB3  1 
ATOM   6844  H  HD21 . ASN   A  1  455 ? 70.639  22.003  2.088    1.00 144.58 ? 455  ASN   A HD21 1 
ATOM   6845  H  HD22 . ASN   A  1  455 ? 70.404  21.675  0.654    1.00 144.58 ? 455  ASN   A HD22 1 
ATOM   6846  N  N    . GLN   A  1  456 ? 65.358  22.035  2.788    1.00 116.02 ? 456  GLN   A N    1 
ATOM   6847  C  CA   . GLN   A  1  456 ? 64.680  23.137  3.462    1.00 118.74 ? 456  GLN   A CA   1 
ATOM   6848  C  C    . GLN   A  1  456 ? 65.590  24.352  3.586    1.00 123.67 ? 456  GLN   A C    1 
ATOM   6849  O  O    . GLN   A  1  456 ? 65.149  25.490  3.389    1.00 125.21 ? 456  GLN   A O    1 
ATOM   6850  C  CB   . GLN   A  1  456 ? 64.201  22.685  4.841    1.00 121.89 ? 456  GLN   A CB   1 
ATOM   6851  C  CG   . GLN   A  1  456 ? 63.221  21.523  4.802    1.00 126.02 ? 456  GLN   A CG   1 
ATOM   6852  C  CD   . GLN   A  1  456 ? 63.344  20.615  6.008    1.00 133.32 ? 456  GLN   A CD   1 
ATOM   6853  O  OE1  . GLN   A  1  456 ? 62.371  20.383  6.725    1.00 137.48 ? 456  GLN   A OE1  1 
ATOM   6854  N  NE2  . GLN   A  1  456 ? 64.543  20.088  6.232    1.00 134.07 ? 456  GLN   A NE2  1 
ATOM   6855  H  H    . GLN   A  1  456 ? 65.431  21.318  3.256    1.00 139.21 ? 456  GLN   A H    1 
ATOM   6856  H  HA   . GLN   A  1  456 ? 63.904  23.395  2.941    1.00 142.47 ? 456  GLN   A HA   1 
ATOM   6857  H  HB2  . GLN   A  1  456 ? 64.970  22.405  5.361    1.00 146.25 ? 456  GLN   A HB2  1 
ATOM   6858  H  HB3  . GLN   A  1  456 ? 63.759  23.430  5.277    1.00 146.25 ? 456  GLN   A HB3  1 
ATOM   6859  H  HG2  . GLN   A  1  456 ? 62.316  21.873  4.780    1.00 151.20 ? 456  GLN   A HG2  1 
ATOM   6860  H  HG3  . GLN   A  1  456 ? 63.390  20.992  4.008    1.00 151.20 ? 456  GLN   A HG3  1 
ATOM   6861  H  HE21 . GLN   A  1  456 ? 65.198  20.270  5.705    1.00 160.86 ? 456  GLN   A HE21 1 
ATOM   6862  H  HE22 . GLN   A  1  456 ? 64.664  19.566  6.905    1.00 160.86 ? 456  GLN   A HE22 1 
ATOM   6863  N  N    . ASP   A  1  457 ? 66.866  24.131  3.916    1.00 125.18 ? 457  ASP   A N    1 
ATOM   6864  C  CA   . ASP   A  1  457 ? 67.804  25.245  4.003    1.00 125.77 ? 457  ASP   A CA   1 
ATOM   6865  C  C    . ASP   A  1  457 ? 67.907  25.991  2.680    1.00 126.04 ? 457  ASP   A C    1 
ATOM   6866  O  O    . ASP   A  1  457 ? 68.173  27.199  2.668    1.00 126.57 ? 457  ASP   A O    1 
ATOM   6867  C  CB   . ASP   A  1  457 ? 69.181  24.743  4.435    1.00 125.86 ? 457  ASP   A CB   1 
ATOM   6868  C  CG   . ASP   A  1  457 ? 69.283  24.541  5.931    1.00 126.74 ? 457  ASP   A CG   1 
ATOM   6869  O  OD1  . ASP   A  1  457 ? 68.256  24.692  6.625    1.00 125.92 ? 457  ASP   A OD1  1 
ATOM   6870  O  OD2  . ASP   A  1  457 ? 70.394  24.238  6.415    1.00 129.07 ? 457  ASP   A OD2  1 
ATOM   6871  H  H    . ASP   A  1  457 ? 67.205  23.360  4.090    1.00 150.20 ? 457  ASP   A H    1 
ATOM   6872  H  HA   . ASP   A  1  457 ? 67.487  25.866  4.677    1.00 150.90 ? 457  ASP   A HA   1 
ATOM   6873  H  HB2  . ASP   A  1  457 ? 69.358  23.892  4.004    1.00 151.01 ? 457  ASP   A HB2  1 
ATOM   6874  H  HB3  . ASP   A  1  457 ? 69.852  25.393  4.173    1.00 151.01 ? 457  ASP   A HB3  1 
ATOM   6875  N  N    . ASN   A  1  458 ? 67.701  25.299  1.563    1.00 126.96 ? 458  ASN   A N    1 
ATOM   6876  C  CA   . ASN   A  1  458 ? 67.719  25.960  0.266    1.00 128.05 ? 458  ASN   A CA   1 
ATOM   6877  C  C    . ASN   A  1  458 ? 66.476  26.827  0.104    1.00 130.46 ? 458  ASN   A C    1 
ATOM   6878  O  O    . ASN   A  1  458 ? 65.352  26.369  0.329    1.00 125.20 ? 458  ASN   A O    1 
ATOM   6879  C  CB   . ASN   A  1  458 ? 67.790  24.930  -0.857   1.00 121.89 ? 458  ASN   A CB   1 
ATOM   6880  C  CG   . ASN   A  1  458 ? 68.008  25.570  -2.209   1.00 119.89 ? 458  ASN   A CG   1 
ATOM   6881  O  OD1  . ASN   A  1  458 ? 68.762  26.533  -2.339   1.00 122.72 ? 458  ASN   A OD1  1 
ATOM   6882  N  ND2  . ASN   A  1  458 ? 67.335  25.049  -3.222   1.00 117.10 ? 458  ASN   A ND2  1 
ATOM   6883  H  H    . ASN   A  1  458 ? 67.550  24.453  1.531    1.00 152.33 ? 458  ASN   A H    1 
ATOM   6884  H  HA   . ASN   A  1  458 ? 68.504  26.526  0.206    1.00 153.64 ? 458  ASN   A HA   1 
ATOM   6885  H  HB2  . ASN   A  1  458 ? 68.529  24.326  -0.687   1.00 146.25 ? 458  ASN   A HB2  1 
ATOM   6886  H  HB3  . ASN   A  1  458 ? 66.957  24.435  -0.888   1.00 146.25 ? 458  ASN   A HB3  1 
ATOM   6887  H  HD21 . ASN   A  1  458 ? 66.809  24.381  -3.091   1.00 140.49 ? 458  ASN   A HD21 1 
ATOM   6888  H  HD22 . ASN   A  1  458 ? 67.425  25.377  -4.011   1.00 140.49 ? 458  ASN   A HD22 1 
ATOM   6889  N  N    . LYS   A  1  459 ? 66.683  28.082  -0.295   1.00 137.33 ? 459  LYS   A N    1 
ATOM   6890  C  CA   . LYS   A  1  459 ? 65.588  29.042  -0.431   1.00 136.79 ? 459  LYS   A CA   1 
ATOM   6891  C  C    . LYS   A  1  459 ? 65.929  29.962  -1.600   1.00 141.70 ? 459  LYS   A C    1 
ATOM   6892  O  O    . LYS   A  1  459 ? 66.763  30.862  -1.459   1.00 145.94 ? 459  LYS   A O    1 
ATOM   6893  C  CB   . LYS   A  1  459 ? 65.387  29.826  0.859    1.00 133.20 ? 459  LYS   A CB   1 
ATOM   6894  C  CG   . LYS   A  1  459 ? 64.564  29.100  1.915    1.00 127.14 ? 459  LYS   A CG   1 
ATOM   6895  C  CD   . LYS   A  1  459 ? 64.944  29.548  3.320    1.00 126.94 ? 459  LYS   A CD   1 
ATOM   6896  C  CE   . LYS   A  1  459 ? 64.105  28.854  4.384    1.00 125.43 ? 459  LYS   A CE   1 
ATOM   6897  N  NZ   . LYS   A  1  459 ? 62.816  29.555  4.643    1.00 125.90 ? 459  LYS   A NZ   1 
ATOM   6898  H  H    . LYS   A  1  459 ? 67.455  28.404  -0.495   1.00 164.77 ? 459  LYS   A H    1 
ATOM   6899  H  HA   . LYS   A  1  459 ? 64.767  28.570  -0.639   1.00 164.12 ? 459  LYS   A HA   1 
ATOM   6900  H  HB2  . LYS   A  1  459 ? 66.256  30.016  1.244    1.00 159.82 ? 459  LYS   A HB2  1 
ATOM   6901  H  HB3  . LYS   A  1  459 ? 64.928  30.654  0.649    1.00 159.82 ? 459  LYS   A HB3  1 
ATOM   6902  H  HG2  . LYS   A  1  459 ? 63.623  29.292  1.778    1.00 152.55 ? 459  LYS   A HG2  1 
ATOM   6903  H  HG3  . LYS   A  1  459 ? 64.722  28.145  1.846    1.00 152.55 ? 459  LYS   A HG3  1 
ATOM   6904  H  HD2  . LYS   A  1  459 ? 65.876  29.334  3.482    1.00 152.30 ? 459  LYS   A HD2  1 
ATOM   6905  H  HD3  . LYS   A  1  459 ? 64.805  30.504  3.399    1.00 152.30 ? 459  LYS   A HD3  1 
ATOM   6906  H  HE2  . LYS   A  1  459 ? 63.902  27.952  4.090    1.00 150.50 ? 459  LYS   A HE2  1 
ATOM   6907  H  HE3  . LYS   A  1  459 ? 64.605  28.828  5.215    1.00 150.50 ? 459  LYS   A HE3  1 
ATOM   6908  H  HZ1  . LYS   A  1  459 ? 62.635  29.547  5.515    1.00 151.07 ? 459  LYS   A HZ1  1 
ATOM   6909  H  HZ2  . LYS   A  1  459 ? 62.867  30.399  4.366    1.00 151.07 ? 459  LYS   A HZ2  1 
ATOM   6910  H  HZ3  . LYS   A  1  459 ? 62.155  29.148  4.207    1.00 151.07 ? 459  LYS   A HZ3  1 
ATOM   6911  N  N    . THR   A  1  460 ? 65.284  29.730  -2.746   1.00 140.88 ? 460  THR   A N    1 
ATOM   6912  C  CA   . THR   A  1  460 ? 65.497  30.537  -3.942   1.00 141.63 ? 460  THR   A CA   1 
ATOM   6913  C  C    . THR   A  1  460 ? 64.172  30.991  -4.545   1.00 139.94 ? 460  THR   A C    1 
ATOM   6914  O  O    . THR   A  1  460 ? 64.087  31.242  -5.751   1.00 141.15 ? 460  THR   A O    1 
ATOM   6915  C  CB   . THR   A  1  460 ? 66.315  29.770  -4.982   1.00 140.75 ? 460  THR   A CB   1 
ATOM   6916  O  OG1  . THR   A  1  460 ? 65.730  28.479  -5.197   1.00 137.55 ? 460  THR   A OG1  1 
ATOM   6917  C  CG2  . THR   A  1  460 ? 67.759  29.608  -4.519   1.00 142.68 ? 460  THR   A CG2  1 
ATOM   6918  H  H    . THR   A  1  460 ? 64.709  29.100  -2.853   1.00 169.04 ? 460  THR   A H    1 
ATOM   6919  H  HA   . THR   A  1  460 ? 65.997  31.330  -3.689   1.00 169.94 ? 460  THR   A HA   1 
ATOM   6920  H  HB   . THR   A  1  460 ? 66.320  30.263  -5.817   1.00 168.88 ? 460  THR   A HB   1 
ATOM   6921  H  HG1  . THR   A  1  460 ? 65.622  28.346  -6.019   1.00 165.04 ? 460  THR   A HG1  1 
ATOM   6922  H  HG21 . THR   A  1  460 ? 68.246  29.047  -5.142   1.00 171.20 ? 460  THR   A HG21 1 
ATOM   6923  H  HG22 . THR   A  1  460 ? 68.191  30.475  -4.472   1.00 171.20 ? 460  THR   A HG22 1 
ATOM   6924  H  HG23 . THR   A  1  460 ? 67.782  29.197  -3.641   1.00 171.20 ? 460  THR   A HG23 1 
ATOM   6925  N  N    . CYS   A  1  461 ? 63.131  31.102  -3.722   1.00 133.70 ? 461  CYS   A N    1 
ATOM   6926  C  CA   . CYS   A  1  461 ? 61.834  31.592  -4.160   1.00 135.48 ? 461  CYS   A CA   1 
ATOM   6927  C  C    . CYS   A  1  461 ? 61.305  32.608  -3.159   1.00 139.01 ? 461  CYS   A C    1 
ATOM   6928  O  O    . CYS   A  1  461 ? 61.771  32.694  -2.020   1.00 142.53 ? 461  CYS   A O    1 
ATOM   6929  C  CB   . CYS   A  1  461 ? 60.813  30.460  -4.320   1.00 134.28 ? 461  CYS   A CB   1 
ATOM   6930  S  SG   . CYS   A  1  461 ? 60.908  29.570  -5.878   1.00 134.55 ? 461  CYS   A SG   1 
ATOM   6931  H  H    . CYS   A  1  461 ? 63.156  30.895  -2.888   1.00 160.42 ? 461  CYS   A H    1 
ATOM   6932  H  HA   . CYS   A  1  461 ? 61.942  32.028  -5.020   1.00 162.56 ? 461  CYS   A HA   1 
ATOM   6933  H  HB2  . CYS   A  1  461 ? 60.954  29.817  -3.607   1.00 161.12 ? 461  CYS   A HB2  1 
ATOM   6934  H  HB3  . CYS   A  1  461 ? 59.922  30.838  -4.254   1.00 161.12 ? 461  CYS   A HB3  1 
ATOM   6935  N  N    . SER   A  1  462 ? 60.311  33.376  -3.602   1.00 137.58 ? 462  SER   A N    1 
ATOM   6936  C  CA   . SER   A  1  462 ? 59.670  34.399  -2.789   1.00 137.66 ? 462  SER   A CA   1 
ATOM   6937  C  C    . SER   A  1  462 ? 58.164  34.193  -2.822   1.00 132.55 ? 462  SER   A C    1 
ATOM   6938  O  O    . SER   A  1  462 ? 57.589  33.929  -3.883   1.00 128.77 ? 462  SER   A O    1 
ATOM   6939  C  CB   . SER   A  1  462 ? 60.022  35.807  -3.292   1.00 142.82 ? 462  SER   A CB   1 
ATOM   6940  O  OG   . SER   A  1  462 ? 59.621  35.988  -4.639   1.00 143.81 ? 462  SER   A OG   1 
ATOM   6941  H  H    . SER   A  1  462 ? 59.984  33.319  -4.395   1.00 165.07 ? 462  SER   A H    1 
ATOM   6942  H  HA   . SER   A  1  462 ? 59.968  34.325  -1.869   1.00 165.18 ? 462  SER   A HA   1 
ATOM   6943  H  HB2  . SER   A  1  462 ? 59.566  36.461  -2.738   1.00 171.36 ? 462  SER   A HB2  1 
ATOM   6944  H  HB3  . SER   A  1  462 ? 60.982  35.932  -3.230   1.00 171.36 ? 462  SER   A HB3  1 
ATOM   6945  H  HG   . SER   A  1  462 ? 58.806  36.187  -4.673   1.00 172.55 ? 462  SER   A HG   1 
ATOM   6946  N  N    . LEU   A  1  463 ? 57.526  34.313  -1.661   1.00 132.53 ? 463  LEU   A N    1 
ATOM   6947  C  CA   . LEU   A  1  463 ? 56.090  34.108  -1.580   1.00 129.92 ? 463  LEU   A CA   1 
ATOM   6948  C  C    . LEU   A  1  463 ? 55.339  35.314  -2.134   1.00 133.87 ? 463  LEU   A C    1 
ATOM   6949  O  O    . LEU   A  1  463 ? 55.895  36.409  -2.245   1.00 134.23 ? 463  LEU   A O    1 
ATOM   6950  C  CB   . LEU   A  1  463 ? 55.662  33.863  -0.136   1.00 128.68 ? 463  LEU   A CB   1 
ATOM   6951  C  CG   . LEU   A  1  463 ? 55.713  32.431  0.405    1.00 122.31 ? 463  LEU   A CG   1 
ATOM   6952  C  CD1  . LEU   A  1  463 ? 55.261  32.427  1.862    1.00 124.14 ? 463  LEU   A CD1  1 
ATOM   6953  C  CD2  . LEU   A  1  463 ? 54.863  31.459  -0.405   1.00 114.50 ? 463  LEU   A CD2  1 
ATOM   6954  H  H    . LEU   A  1  463 ? 57.902  34.511  -0.913   1.00 159.01 ? 463  LEU   A H    1 
ATOM   6955  H  HA   . LEU   A  1  463 ? 55.854  33.327  -2.104   1.00 155.89 ? 463  LEU   A HA   1 
ATOM   6956  H  HB2  . LEU   A  1  463 ? 56.239  34.394  0.435    1.00 154.40 ? 463  LEU   A HB2  1 
ATOM   6957  H  HB3  . LEU   A  1  463 ? 54.743  34.159  -0.048   1.00 154.40 ? 463  LEU   A HB3  1 
ATOM   6958  H  HG   . LEU   A  1  463 ? 56.628  32.117  0.336    1.00 146.75 ? 463  LEU   A HG   1 
ATOM   6959  H  HD11 . LEU   A  1  463 ? 55.128  31.510  2.149    1.00 148.95 ? 463  LEU   A HD11 1 
ATOM   6960  H  HD12 . LEU   A  1  463 ? 55.946  32.847  2.406    1.00 148.95 ? 463  LEU   A HD12 1 
ATOM   6961  H  HD13 . LEU   A  1  463 ? 54.430  32.922  1.936    1.00 148.95 ? 463  LEU   A HD13 1 
ATOM   6962  H  HD21 . LEU   A  1  463 ? 55.332  30.613  -0.476   1.00 137.38 ? 463  LEU   A HD21 1 
ATOM   6963  H  HD22 . LEU   A  1  463 ? 54.014  31.330  0.046    1.00 137.38 ? 463  LEU   A HD22 1 
ATOM   6964  H  HD23 . LEU   A  1  463 ? 54.715  31.830  -1.289   1.00 137.38 ? 463  LEU   A HD23 1 
ATOM   6965  N  N    . PRO   A  1  464 ? 54.067  35.136  -2.489   1.00 134.45 ? 464  PRO   A N    1 
ATOM   6966  C  CA   . PRO   A  1  464 ? 53.258  36.280  -2.924   1.00 138.70 ? 464  PRO   A CA   1 
ATOM   6967  C  C    . PRO   A  1  464 ? 53.319  37.402  -1.898   1.00 144.62 ? 464  PRO   A C    1 
ATOM   6968  O  O    . PRO   A  1  464 ? 53.316  37.164  -0.688   1.00 146.37 ? 464  PRO   A O    1 
ATOM   6969  C  CB   . PRO   A  1  464 ? 51.847  35.695  -3.046   1.00 135.94 ? 464  PRO   A CB   1 
ATOM   6970  C  CG   . PRO   A  1  464 ? 52.048  34.233  -3.236   1.00 128.54 ? 464  PRO   A CG   1 
ATOM   6971  C  CD   . PRO   A  1  464 ? 53.312  33.871  -2.517   1.00 127.87 ? 464  PRO   A CD   1 
ATOM   6972  H  HA   . PRO   A  1  464 ? 53.549  36.605  -3.790   1.00 166.42 ? 464  PRO   A HA   1 
ATOM   6973  H  HB2  . PRO   A  1  464 ? 51.345  35.874  -2.235   1.00 163.11 ? 464  PRO   A HB2  1 
ATOM   6974  H  HB3  . PRO   A  1  464 ? 51.394  36.085  -3.809   1.00 163.11 ? 464  PRO   A HB3  1 
ATOM   6975  H  HG2  . PRO   A  1  464 ? 51.293  33.752  -2.861   1.00 154.22 ? 464  PRO   A HG2  1 
ATOM   6976  H  HG3  . PRO   A  1  464 ? 52.127  34.038  -4.183   1.00 154.22 ? 464  PRO   A HG3  1 
ATOM   6977  H  HD2  . PRO   A  1  464 ? 53.120  33.564  -1.616   1.00 153.42 ? 464  PRO   A HD2  1 
ATOM   6978  H  HD3  . PRO   A  1  464 ? 53.801  33.188  -3.002   1.00 153.42 ? 464  PRO   A HD3  1 
ATOM   6979  N  N    . GLY   A  1  465 ? 53.374  38.631  -2.390   1.00 147.88 ? 465  GLY   A N    1 
ATOM   6980  C  CA   . GLY   A  1  465 ? 53.580  39.773  -1.525   1.00 151.25 ? 465  GLY   A CA   1 
ATOM   6981  C  C    . GLY   A  1  465 ? 55.055  40.016  -1.271   1.00 152.50 ? 465  GLY   A C    1 
ATOM   6982  O  O    . GLY   A  1  465 ? 55.931  39.614  -2.043   1.00 147.34 ? 465  GLY   A O    1 
ATOM   6983  H  H    . GLY   A  1  465 ? 53.293  38.828  -3.223   1.00 177.44 ? 465  GLY   A H    1 
ATOM   6984  H  HA2  . GLY   A  1  465 ? 53.203  40.566  -1.939   1.00 181.48 ? 465  GLY   A HA2  1 
ATOM   6985  H  HA3  . GLY   A  1  465 ? 53.140  39.621  -0.675   1.00 181.48 ? 465  GLY   A HA3  1 
ATOM   6986  N  N    . THR   A  1  466 ? 55.331  40.685  -0.155   1.00 159.66 ? 466  THR   A N    1 
ATOM   6987  C  CA   . THR   A  1  466 ? 56.700  41.019  0.212    1.00 160.51 ? 466  THR   A CA   1 
ATOM   6988  C  C    . THR   A  1  466 ? 57.401  39.917  1.000    1.00 153.99 ? 466  THR   A C    1 
ATOM   6989  O  O    . THR   A  1  466 ? 58.592  40.058  1.298    1.00 153.79 ? 466  THR   A O    1 
ATOM   6990  C  CB   . THR   A  1  466 ? 56.725  42.319  1.022    1.00 164.89 ? 466  THR   A CB   1 
ATOM   6991  O  OG1  . THR   A  1  466 ? 55.791  42.226  2.104    1.00 164.17 ? 466  THR   A OG1  1 
ATOM   6992  C  CG2  . THR   A  1  466 ? 56.364  43.511  0.141    1.00 169.19 ? 466  THR   A CG2  1 
ATOM   6993  H  H    . THR   A  1  466 ? 54.739  40.957  0.406    1.00 191.57 ? 466  THR   A H    1 
ATOM   6994  H  HA   . THR   A  1  466 ? 57.206  41.161  -0.604   1.00 192.60 ? 466  THR   A HA   1 
ATOM   6995  H  HB   . THR   A  1  466 ? 57.617  42.462  1.375    1.00 197.85 ? 466  THR   A HB   1 
ATOM   6996  H  HG1  . THR   A  1  466 ? 55.335  42.930  2.151    1.00 196.98 ? 466  THR   A HG1  1 
ATOM   6997  H  HG21 . THR   A  1  466 ? 56.567  44.339  0.603    1.00 203.01 ? 466  THR   A HG21 1 
ATOM   6998  H  HG22 . THR   A  1  466 ? 56.872  43.478  -0.685   1.00 203.01 ? 466  THR   A HG22 1 
ATOM   6999  H  HG23 . THR   A  1  466 ? 55.417  43.492  -0.071   1.00 203.01 ? 466  THR   A HG23 1 
ATOM   7000  N  N    . ALA   A  1  467 ? 56.704  38.835  1.345    1.00 149.19 ? 467  ALA   A N    1 
ATOM   7001  C  CA   . ALA   A  1  467 ? 57.337  37.727  2.052    1.00 150.23 ? 467  ALA   A CA   1 
ATOM   7002  C  C    . ALA   A  1  467 ? 58.387  37.063  1.165    1.00 158.65 ? 467  ALA   A C    1 
ATOM   7003  O  O    . ALA   A  1  467 ? 58.212  36.956  -0.052   1.00 163.49 ? 467  ALA   A O    1 
ATOM   7004  C  CB   . ALA   A  1  467 ? 56.285  36.706  2.486    1.00 141.19 ? 467  ALA   A CB   1 
ATOM   7005  H  H    . ALA   A  1  467 ? 55.868  38.719  1.182    1.00 179.01 ? 467  ALA   A H    1 
ATOM   7006  H  HA   . ALA   A  1  467 ? 57.780  38.059  2.849    1.00 180.25 ? 467  ALA   A HA   1 
ATOM   7007  H  HB1  . ALA   A  1  467 ? 56.721  35.993  2.979    1.00 169.41 ? 467  ALA   A HB1  1 
ATOM   7008  H  HB2  . ALA   A  1  467 ? 55.631  37.146  3.050    1.00 169.41 ? 467  ALA   A HB2  1 
ATOM   7009  H  HB3  . ALA   A  1  467 ? 55.851  36.344  1.697    1.00 169.41 ? 467  ALA   A HB3  1 
ATOM   7010  N  N    . LEU   A  1  468 ? 59.477  36.599  1.781    1.00 158.39 ? 468  LEU   A N    1 
ATOM   7011  C  CA   . LEU   A  1  468 ? 60.639  36.125  1.038    1.00 153.06 ? 468  LEU   A CA   1 
ATOM   7012  C  C    . LEU   A  1  468 ? 61.183  34.836  1.651    1.00 149.49 ? 468  LEU   A C    1 
ATOM   7013  O  O    . LEU   A  1  468 ? 60.747  34.391  2.716    1.00 151.01 ? 468  LEU   A O    1 
ATOM   7014  C  CB   . LEU   A  1  468 ? 61.739  37.201  1.006    1.00 151.59 ? 468  LEU   A CB   1 
ATOM   7015  C  CG   . LEU   A  1  468 ? 61.359  38.562  0.408    1.00 150.43 ? 468  LEU   A CG   1 
ATOM   7016  C  CD1  . LEU   A  1  468 ? 62.511  39.563  0.529    1.00 153.18 ? 468  LEU   A CD1  1 
ATOM   7017  C  CD2  . LEU   A  1  468 ? 60.914  38.410  -1.044   1.00 146.15 ? 468  LEU   A CD2  1 
ATOM   7018  H  H    . LEU   A  1  468 ? 59.565  36.551  2.635    1.00 190.05 ? 468  LEU   A H    1 
ATOM   7019  H  HA   . LEU   A  1  468 ? 60.361  35.914  0.133    1.00 183.65 ? 468  LEU   A HA   1 
ATOM   7020  H  HB2  . LEU   A  1  468 ? 62.026  37.363  1.918    1.00 181.89 ? 468  LEU   A HB2  1 
ATOM   7021  H  HB3  . LEU   A  1  468 ? 62.479  36.857  0.481    1.00 181.89 ? 468  LEU   A HB3  1 
ATOM   7022  H  HG   . LEU   A  1  468 ? 60.612  38.921  0.911    1.00 180.50 ? 468  LEU   A HG   1 
ATOM   7023  H  HD11 . LEU   A  1  468 ? 62.531  40.119  -0.265   1.00 183.80 ? 468  LEU   A HD11 1 
ATOM   7024  H  HD12 . LEU   A  1  468 ? 62.370  40.113  1.315    1.00 183.80 ? 468  LEU   A HD12 1 
ATOM   7025  H  HD13 . LEU   A  1  468 ? 63.346  39.075  0.612    1.00 183.80 ? 468  LEU   A HD13 1 
ATOM   7026  H  HD21 . LEU   A  1  468 ? 61.055  39.251  -1.507   1.00 175.36 ? 468  LEU   A HD21 1 
ATOM   7027  H  HD22 . LEU   A  1  468 ? 61.438  37.710  -1.463   1.00 175.36 ? 468  LEU   A HD22 1 
ATOM   7028  H  HD23 . LEU   A  1  468 ? 59.973  38.175  -1.063   1.00 175.36 ? 468  LEU   A HD23 1 
ATOM   7029  N  N    . LYS   A  1  469 ? 62.163  34.245  0.957    1.00 143.14 ? 469  LYS   A N    1 
ATOM   7030  C  CA   . LYS   A  1  469 ? 63.002  33.155  1.469    1.00 135.67 ? 469  LYS   A CA   1 
ATOM   7031  C  C    . LYS   A  1  469 ? 62.190  31.897  1.803    1.00 132.19 ? 469  LYS   A C    1 
ATOM   7032  O  O    . LYS   A  1  469 ? 61.983  31.544  2.966    1.00 130.60 ? 469  LYS   A O    1 
ATOM   7033  C  CB   . LYS   A  1  469 ? 63.790  33.599  2.707    1.00 133.95 ? 469  LYS   A CB   1 
ATOM   7034  C  CG   . LYS   A  1  469 ? 64.547  34.904  2.553    1.00 136.32 ? 469  LYS   A CG   1 
ATOM   7035  C  CD   . LYS   A  1  469 ? 64.311  35.813  3.751    1.00 140.93 ? 469  LYS   A CD   1 
ATOM   7036  C  CE   . LYS   A  1  469 ? 65.612  36.293  4.365    1.00 145.02 ? 469  LYS   A CE   1 
ATOM   7037  N  NZ   . LYS   A  1  469 ? 65.388  36.761  5.760    1.00 148.58 ? 469  LYS   A NZ   1 
ATOM   7038  H  H    . LYS   A  1  469 ? 62.369  34.468  0.152    1.00 171.75 ? 469  LYS   A H    1 
ATOM   7039  H  HA   . LYS   A  1  469 ? 63.615  32.929  0.752    1.00 162.79 ? 469  LYS   A HA   1 
ATOM   7040  H  HB2  . LYS   A  1  469 ? 63.168  33.709  3.444    1.00 160.72 ? 469  LYS   A HB2  1 
ATOM   7041  H  HB3  . LYS   A  1  469 ? 64.439  32.911  2.921    1.00 160.72 ? 469  LYS   A HB3  1 
ATOM   7042  H  HG2  . LYS   A  1  469 ? 65.497  34.722  2.487    1.00 163.57 ? 469  LYS   A HG2  1 
ATOM   7043  H  HG3  . LYS   A  1  469 ? 64.241  35.363  1.754    1.00 163.57 ? 469  LYS   A HG3  1 
ATOM   7044  H  HD2  . LYS   A  1  469 ? 63.805  36.591  3.467    1.00 169.10 ? 469  LYS   A HD2  1 
ATOM   7045  H  HD3  . LYS   A  1  469 ? 63.818  35.326  4.429    1.00 169.10 ? 469  LYS   A HD3  1 
ATOM   7046  H  HE2  . LYS   A  1  469 ? 66.252  35.565  4.382    1.00 174.01 ? 469  LYS   A HE2  1 
ATOM   7047  H  HE3  . LYS   A  1  469 ? 65.964  37.032  3.844    1.00 174.01 ? 469  LYS   A HE3  1 
ATOM   7048  H  HZ1  . LYS   A  1  469 ? 66.115  37.177  6.061    1.00 178.28 ? 469  LYS   A HZ1  1 
ATOM   7049  H  HZ2  . LYS   A  1  469 ? 64.701  37.325  5.785    1.00 178.28 ? 469  LYS   A HZ2  1 
ATOM   7050  H  HZ3  . LYS   A  1  469 ? 65.212  36.067  6.288    1.00 178.28 ? 469  LYS   A HZ3  1 
ATOM   7051  N  N    . VAL   A  1  470 ? 61.719  31.234  0.749    1.00 131.07 ? 470  VAL   A N    1 
ATOM   7052  C  CA   . VAL   A  1  470 ? 61.049  29.946  0.887    1.00 125.60 ? 470  VAL   A CA   1 
ATOM   7053  C  C    . VAL   A  1  470 ? 61.657  28.927  -0.070   1.00 122.72 ? 470  VAL   A C    1 
ATOM   7054  O  O    . VAL   A  1  470 ? 62.074  29.258  -1.185   1.00 124.11 ? 470  VAL   A O    1 
ATOM   7055  C  CB   . VAL   A  1  470 ? 59.531  30.096  0.651    1.00 120.56 ? 470  VAL   A CB   1 
ATOM   7056  C  CG1  . VAL   A  1  470 ? 58.859  28.761  0.554    1.00 113.36 ? 470  VAL   A CG1  1 
ATOM   7057  C  CG2  . VAL   A  1  470 ? 58.905  30.889  1.783    1.00 124.84 ? 470  VAL   A CG2  1 
ATOM   7058  H  H    . VAL   A  1  470 ? 61.777  31.513  -0.062   1.00 157.27 ? 470  VAL   A H    1 
ATOM   7059  H  HA   . VAL   A  1  470 ? 61.201  29.603  1.782    1.00 150.70 ? 470  VAL   A HA   1 
ATOM   7060  H  HB   . VAL   A  1  470 ? 59.402  30.565  -0.188   1.00 144.65 ? 470  VAL   A HB   1 
ATOM   7061  H  HG11 . VAL   A  1  470 ? 57.954  28.886  0.228    1.00 136.02 ? 470  VAL   A HG11 1 
ATOM   7062  H  HG12 . VAL   A  1  470 ? 59.358  28.201  -0.061   1.00 136.02 ? 470  VAL   A HG12 1 
ATOM   7063  H  HG13 . VAL   A  1  470 ? 58.841  28.353  1.433    1.00 136.02 ? 470  VAL   A HG13 1 
ATOM   7064  H  HG21 . VAL   A  1  470 ? 57.959  31.005  1.602    1.00 149.79 ? 470  VAL   A HG21 1 
ATOM   7065  H  HG22 . VAL   A  1  470 ? 59.026  30.403  2.614    1.00 149.79 ? 470  VAL   A HG22 1 
ATOM   7066  H  HG23 . VAL   A  1  470 ? 59.340  31.755  1.841    1.00 149.79 ? 470  VAL   A HG23 1 
ATOM   7067  N  N    . SER   A  1  471 ? 61.704  27.670  0.382    1.00 120.20 ? 471  SER   A N    1 
ATOM   7068  C  CA   . SER   A  1  471 ? 62.129  26.554  -0.457   1.00 120.08 ? 471  SER   A CA   1 
ATOM   7069  C  C    . SER   A  1  471 ? 61.004  26.164  -1.408   1.00 118.92 ? 471  SER   A C    1 
ATOM   7070  O  O    . SER   A  1  471 ? 59.845  26.055  -0.999   1.00 122.66 ? 471  SER   A O    1 
ATOM   7071  C  CB   . SER   A  1  471 ? 62.513  25.354  0.412    1.00 117.67 ? 471  SER   A CB   1 
ATOM   7072  O  OG   . SER   A  1  471 ? 63.332  24.444  -0.302   1.00 115.22 ? 471  SER   A OG   1 
ATOM   7073  H  H    . SER   A  1  471 ? 61.490  27.438  1.182    1.00 144.22 ? 471  SER   A H    1 
ATOM   7074  H  HA   . SER   A  1  471 ? 62.905  26.810  -0.979   1.00 144.07 ? 471  SER   A HA   1 
ATOM   7075  H  HB2  . SER   A  1  471 ? 63.000  25.671  1.189    1.00 141.18 ? 471  SER   A HB2  1 
ATOM   7076  H  HB3  . SER   A  1  471 ? 61.705  24.896  0.691    1.00 141.18 ? 471  SER   A HB3  1 
ATOM   7077  H  HG   . SER   A  1  471 ? 64.027  24.832  -0.569   1.00 138.24 ? 471  SER   A HG   1 
ATOM   7078  N  N    . CYS   A  1  472 ? 61.346  25.938  -2.679   1.00 113.85 ? 472  CYS   A N    1 
ATOM   7079  C  CA   . CYS   A  1  472 ? 60.336  25.738  -3.708   1.00 112.73 ? 472  CYS   A CA   1 
ATOM   7080  C  C    . CYS   A  1  472 ? 60.757  24.655  -4.692   1.00 112.68 ? 472  CYS   A C    1 
ATOM   7081  O  O    . CYS   A  1  472 ? 61.922  24.256  -4.761   1.00 108.29 ? 472  CYS   A O    1 
ATOM   7082  C  CB   . CYS   A  1  472 ? 60.064  27.038  -4.476   1.00 118.10 ? 472  CYS   A CB   1 
ATOM   7083  S  SG   . CYS   A  1  472 ? 61.523  27.726  -5.300   1.00 125.09 ? 472  CYS   A SG   1 
ATOM   7084  H  H    . CYS   A  1  472 ? 62.156  25.897  -2.964   1.00 136.60 ? 472  CYS   A H    1 
ATOM   7085  H  HA   . CYS   A  1  472 ? 59.524  25.433  -3.274   1.00 135.26 ? 472  CYS   A HA   1 
ATOM   7086  H  HB2  . CYS   A  1  472 ? 59.396  26.863  -5.157   1.00 141.70 ? 472  CYS   A HB2  1 
ATOM   7087  H  HB3  . CYS   A  1  472 ? 59.735  27.704  -3.853   1.00 141.70 ? 472  CYS   A HB3  1 
ATOM   7088  N  N    . PHE   A  1  473 ? 59.772  24.196  -5.464   1.00 117.38 ? 473  PHE   A N    1 
ATOM   7089  C  CA   . PHE   A  1  473 ? 59.976  23.218  -6.523   1.00 119.20 ? 473  PHE   A CA   1 
ATOM   7090  C  C    . PHE   A  1  473 ? 58.826  23.352  -7.511   1.00 117.40 ? 473  PHE   A C    1 
ATOM   7091  O  O    . PHE   A  1  473 ? 57.795  23.960  -7.208   1.00 116.24 ? 473  PHE   A O    1 
ATOM   7092  C  CB   . PHE   A  1  473 ? 60.062  21.794  -5.966   1.00 117.36 ? 473  PHE   A CB   1 
ATOM   7093  C  CG   . PHE   A  1  473 ? 58.826  21.351  -5.236   1.00 115.74 ? 473  PHE   A CG   1 
ATOM   7094  C  CD1  . PHE   A  1  473 ? 58.592  21.753  -3.932   1.00 118.16 ? 473  PHE   A CD1  1 
ATOM   7095  C  CD2  . PHE   A  1  473 ? 57.901  20.526  -5.853   1.00 112.73 ? 473  PHE   A CD2  1 
ATOM   7096  C  CE1  . PHE   A  1  473 ? 57.456  21.344  -3.259   1.00 117.42 ? 473  PHE   A CE1  1 
ATOM   7097  C  CE2  . PHE   A  1  473 ? 56.764  20.113  -5.185   1.00 112.51 ? 473  PHE   A CE2  1 
ATOM   7098  C  CZ   . PHE   A  1  473 ? 56.542  20.523  -3.887   1.00 114.66 ? 473  PHE   A CZ   1 
ATOM   7099  H  H    . PHE   A  1  473 ? 58.953  24.445  -5.389   1.00 140.83 ? 473  PHE   A H    1 
ATOM   7100  H  HA   . PHE   A  1  473 ? 60.807  23.401  -6.989   1.00 143.02 ? 473  PHE   A HA   1 
ATOM   7101  H  HB2  . PHE   A  1  473 ? 60.206  21.179  -6.702   1.00 140.82 ? 473  PHE   A HB2  1 
ATOM   7102  H  HB3  . PHE   A  1  473 ? 60.805  21.747  -5.344   1.00 140.82 ? 473  PHE   A HB3  1 
ATOM   7103  H  HD1  . PHE   A  1  473 ? 59.206  22.305  -3.503   1.00 141.78 ? 473  PHE   A HD1  1 
ATOM   7104  H  HD2  . PHE   A  1  473 ? 58.047  20.245  -6.728   1.00 135.25 ? 473  PHE   A HD2  1 
ATOM   7105  H  HE1  . PHE   A  1  473 ? 57.307  21.623  -2.384   1.00 140.89 ? 473  PHE   A HE1  1 
ATOM   7106  H  HE2  . PHE   A  1  473 ? 56.150  19.559  -5.610   1.00 134.99 ? 473  PHE   A HE2  1 
ATOM   7107  H  HZ   . PHE   A  1  473 ? 55.777  20.246  -3.435   1.00 137.58 ? 473  PHE   A HZ   1 
ATOM   7108  N  N    . ASN   A  1  474 ? 59.013  22.778  -8.696   1.00 115.64 ? 474  ASN   A N    1 
ATOM   7109  C  CA   . ASN   A  1  474 ? 58.055  22.901  -9.785   1.00 113.96 ? 474  ASN   A CA   1 
ATOM   7110  C  C    . ASN   A  1  474 ? 57.217  21.634  -9.924   1.00 108.06 ? 474  ASN   A C    1 
ATOM   7111  O  O    . ASN   A  1  474 ? 57.647  20.537  -9.560   1.00 102.98 ? 474  ASN   A O    1 
ATOM   7112  C  CB   . ASN   A  1  474 ? 58.772  23.186  -11.108  1.00 117.62 ? 474  ASN   A CB   1 
ATOM   7113  C  CG   . ASN   A  1  474 ? 59.568  24.476  -11.076  1.00 127.01 ? 474  ASN   A CG   1 
ATOM   7114  O  OD1  . ASN   A  1  474 ? 59.751  25.080  -10.019  1.00 132.46 ? 474  ASN   A OD1  1 
ATOM   7115  N  ND2  . ASN   A  1  474 ? 60.050  24.904  -12.239  1.00 129.82 ? 474  ASN   A ND2  1 
ATOM   7116  H  H    . ASN   A  1  474 ? 59.702  22.304  -8.895   1.00 138.74 ? 474  ASN   A H    1 
ATOM   7117  H  HA   . ASN   A  1  474 ? 57.454  23.637  -9.591   1.00 136.73 ? 474  ASN   A HA   1 
ATOM   7118  H  HB2  . ASN   A  1  474 ? 59.386  22.459  -11.298  1.00 141.12 ? 474  ASN   A HB2  1 
ATOM   7119  H  HB3  . ASN   A  1  474 ? 58.113  23.257  -11.816  1.00 141.12 ? 474  ASN   A HB3  1 
ATOM   7120  H  HD21 . ASN   A  1  474 ? 60.508  25.631  -12.273  1.00 155.77 ? 474  ASN   A HD21 1 
ATOM   7121  H  HD22 . ASN   A  1  474 ? 59.904  24.453  -12.956  1.00 155.77 ? 474  ASN   A HD22 1 
ATOM   7122  N  N    . VAL   A  1  475 ? 56.008  21.803  -10.458  1.00 108.70 ? 475  VAL   A N    1 
ATOM   7123  C  CA   . VAL   A  1  475 ? 55.102  20.700  -10.761  1.00 101.94 ? 475  VAL   A CA   1 
ATOM   7124  C  C    . VAL   A  1  475 ? 54.551  20.919  -12.163  1.00 101.06 ? 475  VAL   A C    1 
ATOM   7125  O  O    . VAL   A  1  475 ? 54.080  22.016  -12.483  1.00 100.17 ? 475  VAL   A O    1 
ATOM   7126  C  CB   . VAL   A  1  475 ? 53.953  20.598  -9.738   1.00 98.17  ? 475  VAL   A CB   1 
ATOM   7127  C  CG1  . VAL   A  1  475 ? 52.976  19.494  -10.133  1.00 96.15  ? 475  VAL   A CG1  1 
ATOM   7128  C  CG2  . VAL   A  1  475 ? 54.502  20.349  -8.342   1.00 95.53  ? 475  VAL   A CG2  1 
ATOM   7129  H  H    . VAL   A  1  475 ? 55.681  22.573  -10.660  1.00 130.42 ? 475  VAL   A H    1 
ATOM   7130  H  HA   . VAL   A  1  475 ? 55.593  19.864  -10.744  1.00 122.31 ? 475  VAL   A HA   1 
ATOM   7131  H  HB   . VAL   A  1  475 ? 53.470  21.439  -9.729   1.00 117.78 ? 475  VAL   A HB   1 
ATOM   7132  H  HG11 . VAL   A  1  475 ? 52.315  19.392  -9.431   1.00 115.36 ? 475  VAL   A HG11 1 
ATOM   7133  H  HG12 . VAL   A  1  475 ? 52.541  19.741  -10.964  1.00 115.36 ? 475  VAL   A HG12 1 
ATOM   7134  H  HG13 . VAL   A  1  475 ? 53.467  18.666  -10.249  1.00 115.36 ? 475  VAL   A HG13 1 
ATOM   7135  H  HG21 . VAL   A  1  475 ? 53.762  20.283  -7.719   1.00 114.62 ? 475  VAL   A HG21 1 
ATOM   7136  H  HG22 . VAL   A  1  475 ? 55.007  19.521  -8.345   1.00 114.62 ? 475  VAL   A HG22 1 
ATOM   7137  H  HG23 . VAL   A  1  475 ? 55.079  21.088  -8.093   1.00 114.62 ? 475  VAL   A HG23 1 
ATOM   7138  N  N    . ARG   A  1  476 ? 54.604  19.876  -12.994  1.00 101.47 ? 476  ARG   A N    1 
ATOM   7139  C  CA   . ARG   A  1  476 ? 54.202  19.955  -14.400  1.00 104.76 ? 476  ARG   A CA   1 
ATOM   7140  C  C    . ARG   A  1  476 ? 53.301  18.767  -14.727  1.00 100.93 ? 476  ARG   A C    1 
ATOM   7141  O  O    . ARG   A  1  476 ? 53.779  17.695  -15.108  1.00 98.79  ? 476  ARG   A O    1 
ATOM   7142  C  CB   . ARG   A  1  476 ? 55.429  19.993  -15.309  1.00 110.93 ? 476  ARG   A CB   1 
ATOM   7143  C  CG   . ARG   A  1  476 ? 55.105  20.029  -16.793  1.00 115.65 ? 476  ARG   A CG   1 
ATOM   7144  C  CD   . ARG   A  1  476 ? 56.375  20.052  -17.630  1.00 122.37 ? 476  ARG   A CD   1 
ATOM   7145  N  NE   . ARG   A  1  476 ? 56.091  20.242  -19.052  1.00 129.93 ? 476  ARG   A NE   1 
ATOM   7146  C  CZ   . ARG   A  1  476 ? 56.431  19.397  -20.024  1.00 135.48 ? 476  ARG   A CZ   1 
ATOM   7147  N  NH1  . ARG   A  1  476 ? 57.095  18.277  -19.763  1.00 134.22 ? 476  ARG   A NH1  1 
ATOM   7148  N  NH2  . ARG   A  1  476 ? 56.113  19.685  -21.278  1.00 141.13 ? 476  ARG   A NH2  1 
ATOM   7149  H  H    . ARG   A  1  476 ? 54.876  19.095  -12.761  1.00 121.75 ? 476  ARG   A H    1 
ATOM   7150  H  HA   . ARG   A  1  476 ? 53.681  20.763  -14.528  1.00 125.69 ? 476  ARG   A HA   1 
ATOM   7151  H  HB2  . ARG   A  1  476 ? 55.944  20.788  -15.100  1.00 133.10 ? 476  ARG   A HB2  1 
ATOM   7152  H  HB3  . ARG   A  1  476 ? 55.961  19.199  -15.143  1.00 133.10 ? 476  ARG   A HB3  1 
ATOM   7153  H  HG2  . ARG   A  1  476 ? 54.595  19.240  -17.031  1.00 138.76 ? 476  ARG   A HG2  1 
ATOM   7154  H  HG3  . ARG   A  1  476 ? 54.592  20.828  -16.992  1.00 138.76 ? 476  ARG   A HG3  1 
ATOM   7155  H  HD2  . ARG   A  1  476 ? 56.939  20.783  -17.334  1.00 146.82 ? 476  ARG   A HD2  1 
ATOM   7156  H  HD3  . ARG   A  1  476 ? 56.842  19.208  -17.525  1.00 146.82 ? 476  ARG   A HD3  1 
ATOM   7157  H  HE   . ARG   A  1  476 ? 55.670  20.957  -19.279  1.00 155.90 ? 476  ARG   A HE   1 
ATOM   7158  H  HH11 . ARG   A  1  476 ? 57.314  18.086  -18.953  1.00 161.04 ? 476  ARG   A HH11 1 
ATOM   7159  H  HH12 . ARG   A  1  476 ? 57.307  17.743  -20.403  1.00 161.04 ? 476  ARG   A HH12 1 
ATOM   7160  H  HH21 . ARG   A  1  476 ? 55.691  20.412  -21.458  1.00 169.34 ? 476  ARG   A HH21 1 
ATOM   7161  H  HH22 . ARG   A  1  476 ? 56.329  19.145  -21.911  1.00 169.34 ? 476  ARG   A HH22 1 
ATOM   7162  N  N    . PHE   A  1  477 ? 51.994  18.965  -14.584  1.00 100.26 ? 477  PHE   A N    1 
ATOM   7163  C  CA   . PHE   A  1  477 ? 51.010  17.957  -14.950  1.00 98.98  ? 477  PHE   A CA   1 
ATOM   7164  C  C    . PHE   A  1  477 ? 50.633  18.103  -16.419  1.00 98.69  ? 477  PHE   A C    1 
ATOM   7165  O  O    . PHE   A  1  477 ? 50.538  19.218  -16.941  1.00 98.78  ? 477  PHE   A O    1 
ATOM   7166  C  CB   . PHE   A  1  477 ? 49.764  18.076  -14.068  1.00 100.78 ? 477  PHE   A CB   1 
ATOM   7167  C  CG   . PHE   A  1  477 ? 48.927  19.297  -14.344  1.00 106.52 ? 477  PHE   A CG   1 
ATOM   7168  C  CD1  . PHE   A  1  477 ? 49.385  20.566  -14.023  1.00 111.25 ? 477  PHE   A CD1  1 
ATOM   7169  C  CD2  . PHE   A  1  477 ? 47.668  19.172  -14.905  1.00 106.97 ? 477  PHE   A CD2  1 
ATOM   7170  C  CE1  . PHE   A  1  477 ? 48.611  21.683  -14.271  1.00 114.31 ? 477  PHE   A CE1  1 
ATOM   7171  C  CE2  . PHE   A  1  477 ? 46.888  20.286  -15.152  1.00 110.31 ? 477  PHE   A CE2  1 
ATOM   7172  C  CZ   . PHE   A  1  477 ? 47.361  21.542  -14.835  1.00 113.57 ? 477  PHE   A CZ   1 
ATOM   7173  H  H    . PHE   A  1  477 ? 51.648  19.688  -14.271  1.00 120.29 ? 477  PHE   A H    1 
ATOM   7174  H  HA   . PHE   A  1  477 ? 51.385  17.072  -14.820  1.00 118.76 ? 477  PHE   A HA   1 
ATOM   7175  H  HB2  . PHE   A  1  477 ? 49.205  17.296  -14.214  1.00 120.91 ? 477  PHE   A HB2  1 
ATOM   7176  H  HB3  . PHE   A  1  477 ? 50.044  18.114  -13.140  1.00 120.91 ? 477  PHE   A HB3  1 
ATOM   7177  H  HD1  . PHE   A  1  477 ? 50.225  20.666  -13.635  1.00 133.48 ? 477  PHE   A HD1  1 
ATOM   7178  H  HD2  . PHE   A  1  477 ? 47.343  18.327  -15.119  1.00 128.35 ? 477  PHE   A HD2  1 
ATOM   7179  H  HE1  . PHE   A  1  477 ? 48.933  22.529  -14.059  1.00 137.15 ? 477  PHE   A HE1  1 
ATOM   7180  H  HE2  . PHE   A  1  477 ? 46.045  20.188  -15.533  1.00 132.35 ? 477  PHE   A HE2  1 
ATOM   7181  H  HZ   . PHE   A  1  477 ? 46.837  22.293  -15.001  1.00 136.26 ? 477  PHE   A HZ   1 
ATOM   7182  N  N    . CYS   A  1  478 ? 50.422  16.968  -17.083  1.00 100.39 ? 478  CYS   A N    1 
ATOM   7183  C  CA   . CYS   A  1  478 ? 50.122  16.929  -18.506  1.00 106.15 ? 478  CYS   A CA   1 
ATOM   7184  C  C    . CYS   A  1  478 ? 48.944  15.997  -18.754  1.00 105.77 ? 478  CYS   A C    1 
ATOM   7185  O  O    . CYS   A  1  478 ? 48.626  15.131  -17.935  1.00 103.67 ? 478  CYS   A O    1 
ATOM   7186  C  CB   . CYS   A  1  478 ? 51.332  16.458  -19.324  1.00 110.90 ? 478  CYS   A CB   1 
ATOM   7187  S  SG   . CYS   A  1  478 ? 52.845  17.424  -19.105  1.00 118.71 ? 478  CYS   A SG   1 
ATOM   7188  H  H    . CYS   A  1  478 ? 50.449  16.189  -16.718  1.00 120.45 ? 478  CYS   A H    1 
ATOM   7189  H  HA   . CYS   A  1  478 ? 49.877  17.819  -18.804  1.00 127.36 ? 478  CYS   A HA   1 
ATOM   7190  H  HB2  . CYS   A  1  478 ? 51.534  15.544  -19.070  1.00 133.06 ? 478  CYS   A HB2  1 
ATOM   7191  H  HB3  . CYS   A  1  478 ? 51.098  16.497  -20.264  1.00 133.06 ? 478  CYS   A HB3  1 
ATOM   7192  N  N    . LEU   A  1  479 ? 48.302  16.174  -19.907  1.00 106.00 ? 479  LEU   A N    1 
ATOM   7193  C  CA   . LEU   A  1  479 ? 47.122  15.394  -20.250  1.00 101.32 ? 479  LEU   A CA   1 
ATOM   7194  C  C    . LEU   A  1  479 ? 47.036  15.252  -21.763  1.00 99.18  ? 479  LEU   A C    1 
ATOM   7195  O  O    . LEU   A  1  479 ? 47.391  16.174  -22.503  1.00 97.56  ? 479  LEU   A O    1 
ATOM   7196  C  CB   . LEU   A  1  479 ? 45.856  16.054  -19.687  1.00 100.93 ? 479  LEU   A CB   1 
ATOM   7197  C  CG   . LEU   A  1  479 ? 44.740  15.177  -19.110  1.00 100.10 ? 479  LEU   A CG   1 
ATOM   7198  C  CD1  . LEU   A  1  479 ? 45.224  14.238  -18.012  1.00 98.37  ? 479  LEU   A CD1  1 
ATOM   7199  C  CD2  . LEU   A  1  479 ? 43.636  16.078  -18.566  1.00 102.43 ? 479  LEU   A CD2  1 
ATOM   7200  H  H    . LEU   A  1  479 ? 48.533  16.744  -20.509  1.00 127.18 ? 479  LEU   A H    1 
ATOM   7201  H  HA   . LEU   A  1  479 ? 47.191  14.500  -19.880  1.00 121.56 ? 479  LEU   A HA   1 
ATOM   7202  H  HB2  . LEU   A  1  479 ? 46.134  16.647  -18.971  1.00 121.10 ? 479  LEU   A HB2  1 
ATOM   7203  H  HB3  . LEU   A  1  479 ? 45.454  16.567  -20.405  1.00 121.10 ? 479  LEU   A HB3  1 
ATOM   7204  H  HG   . LEU   A  1  479 ? 44.403  14.612  -19.823  1.00 120.10 ? 479  LEU   A HG   1 
ATOM   7205  H  HD11 . LEU   A  1  479 ? 44.574  13.528  -17.894  1.00 118.03 ? 479  LEU   A HD11 1 
ATOM   7206  H  HD12 . LEU   A  1  479 ? 46.080  13.863  -18.272  1.00 118.03 ? 479  LEU   A HD12 1 
ATOM   7207  H  HD13 . LEU   A  1  479 ? 45.319  14.740  -17.187  1.00 118.03 ? 479  LEU   A HD13 1 
ATOM   7208  H  HD21 . LEU   A  1  479 ? 42.987  15.532  -18.095  1.00 122.90 ? 479  LEU   A HD21 1 
ATOM   7209  H  HD22 . LEU   A  1  479 ? 44.027  16.725  -17.959  1.00 122.90 ? 479  LEU   A HD22 1 
ATOM   7210  H  HD23 . LEU   A  1  479 ? 43.208  16.535  -19.307  1.00 122.90 ? 479  LEU   A HD23 1 
ATOM   7211  N  N    . LYS   A  1  480 ? 46.576  14.085  -22.210  1.00 98.95  ? 480  LYS   A N    1 
ATOM   7212  C  CA   . LYS   A  1  480 ? 46.433  13.773  -23.626  1.00 102.57 ? 480  LYS   A CA   1 
ATOM   7213  C  C    . LYS   A  1  480 ? 45.298  12.771  -23.771  1.00 104.26 ? 480  LYS   A C    1 
ATOM   7214  O  O    . LYS   A  1  480 ? 45.122  11.901  -22.914  1.00 105.47 ? 480  LYS   A O    1 
ATOM   7215  C  CB   . LYS   A  1  480 ? 47.731  13.201  -24.211  1.00 102.37 ? 480  LYS   A CB   1 
ATOM   7216  C  CG   . LYS   A  1  480 ? 47.651  12.810  -25.683  1.00 104.85 ? 480  LYS   A CG   1 
ATOM   7217  C  CD   . LYS   A  1  480 ? 48.947  12.160  -26.150  1.00 104.78 ? 480  LYS   A CD   1 
ATOM   7218  C  CE   . LYS   A  1  480 ? 48.899  11.811  -27.631  1.00 106.62 ? 480  LYS   A CE   1 
ATOM   7219  N  NZ   . LYS   A  1  480 ? 50.066  10.992  -28.063  1.00 105.07 ? 480  LYS   A NZ   1 
ATOM   7220  H  H    . LYS   A  1  480 ? 46.333  13.439  -21.696  1.00 118.72 ? 480  LYS   A H    1 
ATOM   7221  H  HA   . LYS   A  1  480 ? 46.213  14.573  -24.127  1.00 123.07 ? 480  LYS   A HA   1 
ATOM   7222  H  HB2  . LYS   A  1  480 ? 48.428  13.870  -24.124  1.00 122.82 ? 480  LYS   A HB2  1 
ATOM   7223  H  HB3  . LYS   A  1  480 ? 47.971  12.406  -23.710  1.00 122.82 ? 480  LYS   A HB3  1 
ATOM   7224  H  HG2  . LYS   A  1  480 ? 46.927  12.176  -25.809  1.00 125.80 ? 480  LYS   A HG2  1 
ATOM   7225  H  HG3  . LYS   A  1  480 ? 47.495  13.602  -26.219  1.00 125.80 ? 480  LYS   A HG3  1 
ATOM   7226  H  HD2  . LYS   A  1  480 ? 49.684  12.774  -26.006  1.00 125.72 ? 480  LYS   A HD2  1 
ATOM   7227  H  HD3  . LYS   A  1  480 ? 49.094  11.342  -25.650  1.00 125.72 ? 480  LYS   A HD3  1 
ATOM   7228  H  HE2  . LYS   A  1  480 ? 48.092  11.304  -27.811  1.00 127.93 ? 480  LYS   A HE2  1 
ATOM   7229  H  HE3  . LYS   A  1  480 ? 48.898  12.631  -28.149  1.00 127.93 ? 480  LYS   A HE3  1 
ATOM   7230  H  HZ1  . LYS   A  1  480 ? 49.979  10.768  -28.920  1.00 126.06 ? 480  LYS   A HZ1  1 
ATOM   7231  H  HZ2  . LYS   A  1  480 ? 50.818  11.456  -27.960  1.00 126.06 ? 480  LYS   A HZ2  1 
ATOM   7232  H  HZ3  . LYS   A  1  480 ? 50.115  10.250  -27.574  1.00 126.06 ? 480  LYS   A HZ3  1 
ATOM   7233  N  N    . ALA   A  1  481 ? 44.533  12.893  -24.855  1.00 103.81 ? 481  ALA   A N    1 
ATOM   7234  C  CA   . ALA   A  1  481 ? 43.343  12.075  -25.040  1.00 101.17 ? 481  ALA   A CA   1 
ATOM   7235  C  C    . ALA   A  1  481 ? 43.178  11.703  -26.506  1.00 105.99 ? 481  ALA   A C    1 
ATOM   7236  O  O    . ALA   A  1  481 ? 43.663  12.392  -27.407  1.00 112.23 ? 481  ALA   A O    1 
ATOM   7237  C  CB   . ALA   A  1  481 ? 42.084  12.800  -24.540  1.00 99.88  ? 481  ALA   A CB   1 
ATOM   7238  H  H    . ALA   A  1  481 ? 44.685  13.444  -25.497  1.00 124.56 ? 481  ALA   A H    1 
ATOM   7239  H  HA   . ALA   A  1  481 ? 43.452  11.251  -24.540  1.00 121.39 ? 481  ALA   A HA   1 
ATOM   7240  H  HB1  . ALA   A  1  481 ? 41.316  12.223  -24.669  1.00 119.84 ? 481  ALA   A HB1  1 
ATOM   7241  H  HB2  . ALA   A  1  481 ? 42.191  13.004  -23.598  1.00 119.84 ? 481  ALA   A HB2  1 
ATOM   7242  H  HB3  . ALA   A  1  481 ? 41.970  13.620  -25.046  1.00 119.84 ? 481  ALA   A HB3  1 
ATOM   7243  N  N    . ASP   A  1  482 ? 42.479  10.593  -26.727  1.00 105.21 ? 482  ASP   A N    1 
ATOM   7244  C  CA   . ASP   A  1  482 ? 42.164  10.116  -28.067  1.00 107.58 ? 482  ASP   A CA   1 
ATOM   7245  C  C    . ASP   A  1  482 ? 41.002  9.139   -27.943  1.00 103.44 ? 482  ASP   A C    1 
ATOM   7246  O  O    . ASP   A  1  482 ? 40.590  8.774   -26.840  1.00 97.25  ? 482  ASP   A O    1 
ATOM   7247  C  CB   . ASP   A  1  482 ? 43.381  9.460   -28.725  1.00 111.71 ? 482  ASP   A CB   1 
ATOM   7248  C  CG   . ASP   A  1  482 ? 43.324  9.505   -30.240  1.00 119.39 ? 482  ASP   A CG   1 
ATOM   7249  O  OD1  . ASP   A  1  482 ? 42.416  10.165  -30.789  1.00 122.28 ? 482  ASP   A OD1  1 
ATOM   7250  O  OD2  . ASP   A  1  482 ? 44.192  8.879   -30.883  1.00 121.87 ? 482  ASP   A OD2  1 
ATOM   7251  H  H    . ASP   A  1  482 ? 42.169  10.089  -26.103  1.00 126.23 ? 482  ASP   A H    1 
ATOM   7252  H  HA   . ASP   A  1  482 ? 41.888  10.856  -28.629  1.00 129.08 ? 482  ASP   A HA   1 
ATOM   7253  H  HB2  . ASP   A  1  482 ? 44.183  9.926   -28.441  1.00 134.03 ? 482  ASP   A HB2  1 
ATOM   7254  H  HB3  . ASP   A  1  482 ? 43.425  8.530   -28.454  1.00 134.03 ? 482  ASP   A HB3  1 
ATOM   7255  N  N    . GLY   A  1  483 ? 40.474  8.719   -29.088  1.00 106.57 ? 483  GLY   A N    1 
ATOM   7256  C  CA   . GLY   A  1  483 ? 39.343  7.810   -29.063  1.00 106.77 ? 483  GLY   A CA   1 
ATOM   7257  C  C    . GLY   A  1  483 ? 39.103  7.170   -30.412  1.00 108.74 ? 483  GLY   A C    1 
ATOM   7258  O  O    . GLY   A  1  483 ? 39.801  7.442   -31.393  1.00 112.80 ? 483  GLY   A O    1 
ATOM   7259  H  H    . GLY   A  1  483 ? 40.747  8.942   -29.872  1.00 127.86 ? 483  GLY   A H    1 
ATOM   7260  H  HA2  . GLY   A  1  483 ? 39.507  7.107   -28.414  1.00 128.11 ? 483  GLY   A HA2  1 
ATOM   7261  H  HA3  . GLY   A  1  483 ? 38.543  8.295   -28.806  1.00 128.11 ? 483  GLY   A HA3  1 
ATOM   7262  N  N    . LYS   A  1  484 ? 38.089  6.305   -30.441  1.00 104.74 ? 484  LYS   A N    1 
ATOM   7263  C  CA   . LYS   A  1  484 ? 37.682  5.573   -31.634  1.00 104.14 ? 484  LYS   A CA   1 
ATOM   7264  C  C    . LYS   A  1  484 ? 36.193  5.791   -31.854  1.00 104.20 ? 484  LYS   A C    1 
ATOM   7265  O  O    . LYS   A  1  484 ? 35.399  5.650   -30.918  1.00 101.30 ? 484  LYS   A O    1 
ATOM   7266  C  CB   . LYS   A  1  484 ? 38.004  4.074   -31.491  1.00 102.30 ? 484  LYS   A CB   1 
ATOM   7267  C  CG   . LYS   A  1  484 ? 37.029  3.093   -32.159  1.00 103.79 ? 484  LYS   A CG   1 
ATOM   7268  C  CD   . LYS   A  1  484 ? 37.098  3.133   -33.679  1.00 104.89 ? 484  LYS   A CD   1 
ATOM   7269  C  CE   . LYS   A  1  484 ? 36.533  1.853   -34.288  1.00 103.96 ? 484  LYS   A CE   1 
ATOM   7270  N  NZ   . LYS   A  1  484 ? 35.163  1.535   -33.794  1.00 101.72 ? 484  LYS   A NZ   1 
ATOM   7271  H  H    . LYS   A  1  484 ? 37.605  6.119   -29.754  1.00 125.67 ? 484  LYS   A H    1 
ATOM   7272  H  HA   . LYS   A  1  484 ? 38.152  5.908   -32.414  1.00 124.95 ? 484  LYS   A HA   1 
ATOM   7273  H  HB2  . LYS   A  1  484 ? 38.878  3.916   -31.881  1.00 122.74 ? 484  LYS   A HB2  1 
ATOM   7274  H  HB3  . LYS   A  1  484 ? 38.019  3.859   -30.545  1.00 122.74 ? 484  LYS   A HB3  1 
ATOM   7275  H  HG2  . LYS   A  1  484 ? 37.244  2.191   -31.874  1.00 124.53 ? 484  LYS   A HG2  1 
ATOM   7276  H  HG3  . LYS   A  1  484 ? 36.123  3.318   -31.895  1.00 124.53 ? 484  LYS   A HG3  1 
ATOM   7277  H  HD2  . LYS   A  1  484 ? 36.578  3.884   -34.006  1.00 125.85 ? 484  LYS   A HD2  1 
ATOM   7278  H  HD3  . LYS   A  1  484 ? 38.023  3.223   -33.958  1.00 125.85 ? 484  LYS   A HD3  1 
ATOM   7279  H  HE2  . LYS   A  1  484 ? 36.489  1.954   -35.251  1.00 124.73 ? 484  LYS   A HE2  1 
ATOM   7280  H  HE3  . LYS   A  1  484 ? 37.114  1.110   -34.058  1.00 124.73 ? 484  LYS   A HE3  1 
ATOM   7281  H  HZ1  . LYS   A  1  484 ? 35.195  0.855   -33.222  1.00 122.05 ? 484  LYS   A HZ1  1 
ATOM   7282  H  HZ2  . LYS   A  1  484 ? 34.816  2.244   -33.382  1.00 122.05 ? 484  LYS   A HZ2  1 
ATOM   7283  H  HZ3  . LYS   A  1  484 ? 34.637  1.313   -34.477  1.00 122.05 ? 484  LYS   A HZ3  1 
ATOM   7284  N  N    . GLY   A  1  485 ? 35.822  6.141   -33.077  1.00 110.20 ? 485  GLY   A N    1 
ATOM   7285  C  CA   . GLY   A  1  485 ? 34.429  6.262   -33.450  1.00 117.54 ? 485  GLY   A CA   1 
ATOM   7286  C  C    . GLY   A  1  485 ? 33.945  7.696   -33.510  1.00 124.27 ? 485  GLY   A C    1 
ATOM   7287  O  O    . GLY   A  1  485 ? 34.713  8.650   -33.658  1.00 122.75 ? 485  GLY   A O    1 
ATOM   7288  H  H    . GLY   A  1  485 ? 36.370  6.315   -33.717  1.00 132.22 ? 485  GLY   A H    1 
ATOM   7289  H  HA2  . GLY   A  1  485 ? 34.299  5.863   -34.325  1.00 141.03 ? 485  GLY   A HA2  1 
ATOM   7290  H  HA3  . GLY   A  1  485 ? 33.885  5.787   -32.803  1.00 141.03 ? 485  GLY   A HA3  1 
ATOM   7291  N  N    . VAL   A  1  486 ? 32.627  7.840   -33.387  1.00 131.89 ? 486  VAL   A N    1 
ATOM   7292  C  CA   . VAL   A  1  486 ? 31.976  9.144   -33.452  1.00 136.83 ? 486  VAL   A CA   1 
ATOM   7293  C  C    . VAL   A  1  486 ? 32.252  9.900   -32.159  1.00 134.43 ? 486  VAL   A C    1 
ATOM   7294  O  O    . VAL   A  1  486 ? 31.661  9.601   -31.116  1.00 135.27 ? 486  VAL   A O    1 
ATOM   7295  C  CB   . VAL   A  1  486 ? 30.464  8.990   -33.699  1.00 138.42 ? 486  VAL   A CB   1 
ATOM   7296  C  CG1  . VAL   A  1  486 ? 29.748  10.320  -33.525  1.00 141.53 ? 486  VAL   A CG1  1 
ATOM   7297  C  CG2  . VAL   A  1  486 ? 30.207  8.422   -35.090  1.00 139.46 ? 486  VAL   A CG2  1 
ATOM   7298  H  H    . VAL   A  1  486 ? 32.081  7.187   -33.263  1.00 158.25 ? 486  VAL   A H    1 
ATOM   7299  H  HA   . VAL   A  1  486 ? 32.351  9.655   -34.186  1.00 164.17 ? 486  VAL   A HA   1 
ATOM   7300  H  HB   . VAL   A  1  486 ? 30.105  8.370   -33.044  1.00 166.09 ? 486  VAL   A HB   1 
ATOM   7301  H  HG11 . VAL   A  1  486 ? 28.840  10.235  -33.857  1.00 169.82 ? 486  VAL   A HG11 1 
ATOM   7302  H  HG12 . VAL   A  1  486 ? 29.735  10.551  -32.583  1.00 169.82 ? 486  VAL   A HG12 1 
ATOM   7303  H  HG13 . VAL   A  1  486 ? 30.221  11.002  -34.026  1.00 169.82 ? 486  VAL   A HG13 1 
ATOM   7304  H  HG21 . VAL   A  1  486 ? 29.257  8.259   -35.194  1.00 167.33 ? 486  VAL   A HG21 1 
ATOM   7305  H  HG22 . VAL   A  1  486 ? 30.507  9.064   -35.753  1.00 167.33 ? 486  VAL   A HG22 1 
ATOM   7306  H  HG23 . VAL   A  1  486 ? 30.698  7.591   -35.187  1.00 167.33 ? 486  VAL   A HG23 1 
ATOM   7307  N  N    . LEU   A  1  487 ? 33.145  10.885  -32.219  1.00 129.69 ? 487  LEU   A N    1 
ATOM   7308  C  CA   . LEU   A  1  487 ? 33.526  11.651  -31.042  1.00 123.18 ? 487  LEU   A CA   1 
ATOM   7309  C  C    . LEU   A  1  487 ? 33.796  13.092  -31.442  1.00 124.84 ? 487  LEU   A C    1 
ATOM   7310  O  O    . LEU   A  1  487 ? 34.228  13.348  -32.574  1.00 126.77 ? 487  LEU   A O    1 
ATOM   7311  C  CB   . LEU   A  1  487 ? 34.769  11.059  -30.362  1.00 118.35 ? 487  LEU   A CB   1 
ATOM   7312  C  CG   . LEU   A  1  487 ? 34.548  9.752   -29.600  1.00 116.63 ? 487  LEU   A CG   1 
ATOM   7313  C  CD1  . LEU   A  1  487 ? 35.371  8.623   -30.202  1.00 118.19 ? 487  LEU   A CD1  1 
ATOM   7314  C  CD2  . LEU   A  1  487 ? 34.879  9.942   -28.128  1.00 112.16 ? 487  LEU   A CD2  1 
ATOM   7315  H  H    . LEU   A  1  487 ? 33.547  11.128  -32.939  1.00 155.60 ? 487  LEU   A H    1 
ATOM   7316  H  HA   . LEU   A  1  487 ? 32.790  11.648  -30.410  1.00 147.79 ? 487  LEU   A HA   1 
ATOM   7317  H  HB2  . LEU   A  1  487 ? 35.435  10.886  -31.046  1.00 142.00 ? 487  LEU   A HB2  1 
ATOM   7318  H  HB3  . LEU   A  1  487 ? 35.107  11.710  -29.727  1.00 142.00 ? 487  LEU   A HB3  1 
ATOM   7319  H  HG   . LEU   A  1  487 ? 33.615  9.497   -29.672  1.00 139.93 ? 487  LEU   A HG   1 
ATOM   7320  H  HD11 . LEU   A  1  487 ? 35.371  7.871   -29.588  1.00 141.81 ? 487  LEU   A HD11 1 
ATOM   7321  H  HD12 . LEU   A  1  487 ? 34.975  8.360   -31.047  1.00 141.81 ? 487  LEU   A HD12 1 
ATOM   7322  H  HD13 . LEU   A  1  487 ? 36.278  8.934   -30.343  1.00 141.81 ? 487  LEU   A HD13 1 
ATOM   7323  H  HD21 . LEU   A  1  487 ? 34.717  9.110   -27.657  1.00 134.58 ? 487  LEU   A HD21 1 
ATOM   7324  H  HD22 . LEU   A  1  487 ? 35.811  10.194  -28.043  1.00 134.58 ? 487  LEU   A HD22 1 
ATOM   7325  H  HD23 . LEU   A  1  487 ? 34.313  10.642  -27.765  1.00 134.58 ? 487  LEU   A HD23 1 
ATOM   7326  N  N    . PRO   A  1  488 ? 33.560  14.048  -30.550  1.00 124.93 ? 488  PRO   A N    1 
ATOM   7327  C  CA   . PRO   A  1  488 ? 33.885  15.443  -30.857  1.00 124.19 ? 488  PRO   A CA   1 
ATOM   7328  C  C    . PRO   A  1  488 ? 35.384  15.695  -30.777  1.00 119.67 ? 488  PRO   A C    1 
ATOM   7329  O  O    . PRO   A  1  488 ? 36.132  14.980  -30.108  1.00 113.47 ? 488  PRO   A O    1 
ATOM   7330  C  CB   . PRO   A  1  488 ? 33.131  16.229  -29.780  1.00 124.56 ? 488  PRO   A CB   1 
ATOM   7331  C  CG   . PRO   A  1  488 ? 33.044  15.286  -28.630  1.00 122.58 ? 488  PRO   A CG   1 
ATOM   7332  C  CD   . PRO   A  1  488 ? 32.932  13.906  -29.222  1.00 123.48 ? 488  PRO   A CD   1 
ATOM   7333  H  HA   . PRO   A  1  488 ? 33.555  15.697  -31.733  1.00 149.01 ? 488  PRO   A HA   1 
ATOM   7334  H  HB2  . PRO   A  1  488 ? 33.628  17.027  -29.541  1.00 149.45 ? 488  PRO   A HB2  1 
ATOM   7335  H  HB3  . PRO   A  1  488 ? 32.248  16.472  -30.101  1.00 149.45 ? 488  PRO   A HB3  1 
ATOM   7336  H  HG2  . PRO   A  1  488 ? 33.844  15.360  -28.087  1.00 147.08 ? 488  PRO   A HG2  1 
ATOM   7337  H  HG3  . PRO   A  1  488 ? 32.261  15.494  -28.097  1.00 147.08 ? 488  PRO   A HG3  1 
ATOM   7338  H  HD2  . PRO   A  1  488 ? 33.412  13.259  -28.681  1.00 148.16 ? 488  PRO   A HD2  1 
ATOM   7339  H  HD3  . PRO   A  1  488 ? 32.002  13.642  -29.306  1.00 148.16 ? 488  PRO   A HD3  1 
ATOM   7340  N  N    . ARG   A  1  489 ? 35.815  16.741  -31.484  1.00 123.82 ? 489  ARG   A N    1 
ATOM   7341  C  CA   . ARG   A  1  489 ? 37.234  17.068  -31.522  1.00 122.34 ? 489  ARG   A CA   1 
ATOM   7342  C  C    . ARG   A  1  489 ? 37.712  17.739  -30.242  1.00 122.36 ? 489  ARG   A C    1 
ATOM   7343  O  O    . ARG   A  1  489 ? 38.895  17.640  -29.912  1.00 119.46 ? 489  ARG   A O    1 
ATOM   7344  C  CB   . ARG   A  1  489 ? 37.539  17.979  -32.711  1.00 123.63 ? 489  ARG   A CB   1 
ATOM   7345  C  CG   . ARG   A  1  489 ? 37.385  17.309  -34.056  1.00 125.04 ? 489  ARG   A CG   1 
ATOM   7346  C  CD   . ARG   A  1  489 ? 37.743  18.260  -35.180  1.00 130.47 ? 489  ARG   A CD   1 
ATOM   7347  N  NE   . ARG   A  1  489 ? 37.523  17.658  -36.490  1.00 133.60 ? 489  ARG   A NE   1 
ATOM   7348  C  CZ   . ARG   A  1  489 ? 37.683  18.296  -37.645  1.00 139.08 ? 489  ARG   A CZ   1 
ATOM   7349  N  NH1  . ARG   A  1  489 ? 38.066  19.566  -37.660  1.00 141.82 ? 489  ARG   A NH1  1 
ATOM   7350  N  NH2  . ARG   A  1  489 ? 37.458  17.662  -38.786  1.00 142.22 ? 489  ARG   A NH2  1 
ATOM   7351  H  H    . ARG   A  1  489 ? 35.312  17.267  -31.942  1.00 148.57 ? 489  ARG   A H    1 
ATOM   7352  H  HA   . ARG   A  1  489 ? 37.728  16.240  -31.634  1.00 146.79 ? 489  ARG   A HA   1 
ATOM   7353  H  HB2  . ARG   A  1  489 ? 36.931  18.735  -32.686  1.00 148.33 ? 489  ARG   A HB2  1 
ATOM   7354  H  HB3  . ARG   A  1  489 ? 38.455  18.288  -32.638  1.00 148.33 ? 489  ARG   A HB3  1 
ATOM   7355  H  HG2  . ARG   A  1  489 ? 37.976  16.541  -34.104  1.00 150.03 ? 489  ARG   A HG2  1 
ATOM   7356  H  HG3  . ARG   A  1  489 ? 36.465  17.028  -34.174  1.00 150.03 ? 489  ARG   A HG3  1 
ATOM   7357  H  HD2  . ARG   A  1  489 ? 37.192  19.055  -35.114  1.00 156.54 ? 489  ARG   A HD2  1 
ATOM   7358  H  HD3  . ARG   A  1  489 ? 38.681  18.500  -35.110  1.00 156.54 ? 489  ARG   A HD3  1 
ATOM   7359  H  HE   . ARG   A  1  489 ? 37.273  16.836  -36.517  1.00 160.30 ? 489  ARG   A HE   1 
ATOM   7360  H  HH11 . ARG   A  1  489 ? 38.212  19.980  -36.921  1.00 170.16 ? 489  ARG   A HH11 1 
ATOM   7361  H  HH12 . ARG   A  1  489 ? 38.169  19.975  -38.410  1.00 170.16 ? 489  ARG   A HH12 1 
ATOM   7362  H  HH21 . ARG   A  1  489 ? 37.208  16.839  -38.779  1.00 170.64 ? 489  ARG   A HH21 1 
ATOM   7363  H  HH22 . ARG   A  1  489 ? 37.561  18.074  -39.534  1.00 170.64 ? 489  ARG   A HH22 1 
ATOM   7364  N  N    . LYS   A  1  490 ? 36.831  18.426  -29.522  1.00 125.79 ? 490  LYS   A N    1 
ATOM   7365  C  CA   . LYS   A  1  490 ? 37.199  19.184  -28.334  1.00 127.98 ? 490  LYS   A CA   1 
ATOM   7366  C  C    . LYS   A  1  490 ? 36.660  18.491  -27.089  1.00 125.92 ? 490  LYS   A C    1 
ATOM   7367  O  O    . LYS   A  1  490 ? 35.536  17.980  -27.089  1.00 129.27 ? 490  LYS   A O    1 
ATOM   7368  C  CB   . LYS   A  1  490 ? 36.662  20.617  -28.429  1.00 135.56 ? 490  LYS   A CB   1 
ATOM   7369  C  CG   . LYS   A  1  490 ? 37.232  21.591  -27.407  1.00 137.56 ? 490  LYS   A CG   1 
ATOM   7370  C  CD   . LYS   A  1  490 ? 36.844  23.026  -27.750  1.00 144.42 ? 490  LYS   A CD   1 
ATOM   7371  C  CE   . LYS   A  1  490 ? 36.194  23.740  -26.574  1.00 146.07 ? 490  LYS   A CE   1 
ATOM   7372  N  NZ   . LYS   A  1  490 ? 34.881  23.143  -26.207  1.00 146.33 ? 490  LYS   A NZ   1 
ATOM   7373  H  H    . LYS   A  1  490 ? 35.992  18.467  -29.707  1.00 150.93 ? 490  LYS   A H    1 
ATOM   7374  H  HA   . LYS   A  1  490 ? 38.165  19.227  -28.251  1.00 153.56 ? 490  LYS   A HA   1 
ATOM   7375  H  HB2  . LYS   A  1  490 ? 36.872  20.965  -29.310  1.00 162.65 ? 490  LYS   A HB2  1 
ATOM   7376  H  HB3  . LYS   A  1  490 ? 35.701  20.593  -28.301  1.00 162.65 ? 490  LYS   A HB3  1 
ATOM   7377  H  HG2  . LYS   A  1  490 ? 36.882  21.379  -26.528  1.00 165.05 ? 490  LYS   A HG2  1 
ATOM   7378  H  HG3  . LYS   A  1  490 ? 38.200  21.527  -27.404  1.00 165.05 ? 490  LYS   A HG3  1 
ATOM   7379  H  HD2  . LYS   A  1  490 ? 37.639  23.520  -28.002  1.00 173.29 ? 490  LYS   A HD2  1 
ATOM   7380  H  HD3  . LYS   A  1  490 ? 36.211  23.018  -28.485  1.00 173.29 ? 490  LYS   A HD3  1 
ATOM   7381  H  HE2  . LYS   A  1  490 ? 36.780  23.680  -25.803  1.00 175.27 ? 490  LYS   A HE2  1 
ATOM   7382  H  HE3  . LYS   A  1  490 ? 36.048  24.670  -26.808  1.00 175.27 ? 490  LYS   A HE3  1 
ATOM   7383  H  HZ1  . LYS   A  1  490 ? 34.343  23.771  -25.876  1.00 175.57 ? 490  LYS   A HZ1  1 
ATOM   7384  H  HZ2  . LYS   A  1  490 ? 34.499  22.784  -26.925  1.00 175.57 ? 490  LYS   A HZ2  1 
ATOM   7385  H  HZ3  . LYS   A  1  490 ? 34.996  22.509  -25.593  1.00 175.57 ? 490  LYS   A HZ3  1 
ATOM   7386  N  N    . LEU   A  1  491 ? 37.472  18.469  -26.031  1.00 121.68 ? 491  LEU   A N    1 
ATOM   7387  C  CA   . LEU   A  1  491 ? 37.117  17.805  -24.782  1.00 119.21 ? 491  LEU   A CA   1 
ATOM   7388  C  C    . LEU   A  1  491 ? 37.521  18.685  -23.610  1.00 122.94 ? 491  LEU   A C    1 
ATOM   7389  O  O    . LEU   A  1  491 ? 38.649  19.183  -23.568  1.00 124.49 ? 491  LEU   A O    1 
ATOM   7390  C  CB   . LEU   A  1  491 ? 37.800  16.437  -24.672  1.00 113.71 ? 491  LEU   A CB   1 
ATOM   7391  C  CG   . LEU   A  1  491 ? 37.251  15.344  -25.589  1.00 112.74 ? 491  LEU   A CG   1 
ATOM   7392  C  CD1  . LEU   A  1  491 ? 38.378  14.471  -26.116  1.00 109.97 ? 491  LEU   A CD1  1 
ATOM   7393  C  CD2  . LEU   A  1  491 ? 36.223  14.501  -24.850  1.00 111.59 ? 491  LEU   A CD2  1 
ATOM   7394  H  H    . LEU   A  1  491 ? 38.249  18.838  -26.015  1.00 146.00 ? 491  LEU   A H    1 
ATOM   7395  H  HA   . LEU   A  1  491 ? 36.156  17.677  -24.747  1.00 143.03 ? 491  LEU   A HA   1 
ATOM   7396  H  HB2  . LEU   A  1  491 ? 38.740  16.548  -24.887  1.00 136.43 ? 491  LEU   A HB2  1 
ATOM   7397  H  HB3  . LEU   A  1  491 ? 37.704  16.122  -23.759  1.00 136.43 ? 491  LEU   A HB3  1 
ATOM   7398  H  HG   . LEU   A  1  491 ? 36.814  15.759  -26.350  1.00 135.26 ? 491  LEU   A HG   1 
ATOM   7399  H  HD11 . LEU   A  1  491 ? 38.001  13.765  -26.663  1.00 131.95 ? 491  LEU   A HD11 1 
ATOM   7400  H  HD12 . LEU   A  1  491 ? 38.978  15.017  -26.648  1.00 131.95 ? 491  LEU   A HD12 1 
ATOM   7401  H  HD13 . LEU   A  1  491 ? 38.857  14.088  -25.365  1.00 131.95 ? 491  LEU   A HD13 1 
ATOM   7402  H  HD21 . LEU   A  1  491 ? 35.946  13.768  -25.422  1.00 133.89 ? 491  LEU   A HD21 1 
ATOM   7403  H  HD22 . LEU   A  1  491 ? 36.625  14.153  -24.039  1.00 133.89 ? 491  LEU   A HD22 1 
ATOM   7404  H  HD23 . LEU   A  1  491 ? 35.459  15.056  -24.630  1.00 133.89 ? 491  LEU   A HD23 1 
ATOM   7405  N  N    . ASN   A  1  492 ? 36.607  18.861  -22.656  1.00 125.43 ? 492  ASN   A N    1 
ATOM   7406  C  CA   . ASN   A  1  492 ? 36.807  19.750  -21.512  1.00 127.33 ? 492  ASN   A CA   1 
ATOM   7407  C  C    . ASN   A  1  492 ? 37.077  18.907  -20.269  1.00 122.81 ? 492  ASN   A C    1 
ATOM   7408  O  O    . ASN   A  1  492 ? 36.152  18.340  -19.680  1.00 123.83 ? 492  ASN   A O    1 
ATOM   7409  C  CB   . ASN   A  1  492 ? 35.588  20.647  -21.307  1.00 132.36 ? 492  ASN   A CB   1 
ATOM   7410  C  CG   . ASN   A  1  492 ? 35.125  21.306  -22.592  1.00 136.27 ? 492  ASN   A CG   1 
ATOM   7411  O  OD1  . ASN   A  1  492 ? 35.914  21.526  -23.511  1.00 138.82 ? 492  ASN   A OD1  1 
ATOM   7412  N  ND2  . ASN   A  1  492 ? 33.838  21.625  -22.661  1.00 136.93 ? 492  ASN   A ND2  1 
ATOM   7413  H  H    . ASN   A  1  492 ? 35.843  18.466  -22.650  1.00 150.50 ? 492  ASN   A H    1 
ATOM   7414  H  HA   . ASN   A  1  492 ? 37.587  20.301  -21.680  1.00 152.77 ? 492  ASN   A HA   1 
ATOM   7415  H  HB2  . ASN   A  1  492 ? 34.856  20.113  -20.963  1.00 158.82 ? 492  ASN   A HB2  1 
ATOM   7416  H  HB3  . ASN   A  1  492 ? 35.813  21.348  -20.675  1.00 158.82 ? 492  ASN   A HB3  1 
ATOM   7417  H  HD21 . ASN   A  1  492 ? 33.526  22.001  -23.369  1.00 164.29 ? 492  ASN   A HD21 1 
ATOM   7418  H  HD22 . ASN   A  1  492 ? 33.317  21.456  -21.998  1.00 164.29 ? 492  ASN   A HD22 1 
ATOM   7419  N  N    . PHE   A  1  493 ? 38.341  18.843  -19.861  1.00 117.79 ? 493  PHE   A N    1 
ATOM   7420  C  CA   . PHE   A  1  493 ? 38.731  18.105  -18.670  1.00 112.26 ? 493  PHE   A CA   1 
ATOM   7421  C  C    . PHE   A  1  493 ? 38.780  19.022  -17.451  1.00 114.45 ? 493  PHE   A C    1 
ATOM   7422  O  O    . PHE   A  1  493 ? 38.948  20.239  -17.559  1.00 116.92 ? 493  PHE   A O    1 
ATOM   7423  C  CB   . PHE   A  1  493 ? 40.097  17.443  -18.866  1.00 107.49 ? 493  PHE   A CB   1 
ATOM   7424  C  CG   . PHE   A  1  493 ? 40.051  16.182  -19.679  1.00 104.57 ? 493  PHE   A CG   1 
ATOM   7425  C  CD1  . PHE   A  1  493 ? 40.015  16.233  -21.062  1.00 104.83 ? 493  PHE   A CD1  1 
ATOM   7426  C  CD2  . PHE   A  1  493 ? 40.054  14.943  -19.060  1.00 102.38 ? 493  PHE   A CD2  1 
ATOM   7427  C  CE1  . PHE   A  1  493 ? 39.977  15.072  -21.812  1.00 103.54 ? 493  PHE   A CE1  1 
ATOM   7428  C  CE2  . PHE   A  1  493 ? 40.015  13.779  -19.804  1.00 101.35 ? 493  PHE   A CE2  1 
ATOM   7429  C  CZ   . PHE   A  1  493 ? 39.977  13.844  -21.182  1.00 102.30 ? 493  PHE   A CZ   1 
ATOM   7430  H  H    . PHE   A  1  493 ? 38.998  19.224  -20.264  1.00 141.33 ? 493  PHE   A H    1 
ATOM   7431  H  HA   . PHE   A  1  493 ? 38.074  17.412  -18.504  1.00 134.70 ? 493  PHE   A HA   1 
ATOM   7432  H  HB2  . PHE   A  1  493 ? 40.683  18.067  -19.321  1.00 128.97 ? 493  PHE   A HB2  1 
ATOM   7433  H  HB3  . PHE   A  1  493 ? 40.462  17.220  -17.995  1.00 128.97 ? 493  PHE   A HB3  1 
ATOM   7434  H  HD1  . PHE   A  1  493 ? 40.018  17.058  -21.492  1.00 125.77 ? 493  PHE   A HD1  1 
ATOM   7435  H  HD2  . PHE   A  1  493 ? 40.081  14.894  -18.131  1.00 122.84 ? 493  PHE   A HD2  1 
ATOM   7436  H  HE1  . PHE   A  1  493 ? 39.950  15.118  -22.741  1.00 124.23 ? 493  PHE   A HE1  1 
ATOM   7437  H  HE2  . PHE   A  1  493 ? 40.015  12.953  -19.377  1.00 121.61 ? 493  PHE   A HE2  1 
ATOM   7438  H  HZ   . PHE   A  1  493 ? 39.951  13.062  -21.685  1.00 122.74 ? 493  PHE   A HZ   1 
ATOM   7439  N  N    . GLN   A  1  494 ? 38.634  18.411  -16.277  1.00 115.91 ? 494  GLN   A N    1 
ATOM   7440  C  CA   . GLN   A  1  494 ? 38.753  19.095  -14.992  1.00 119.36 ? 494  GLN   A CA   1 
ATOM   7441  C  C    . GLN   A  1  494 ? 39.842  18.391  -14.191  1.00 111.60 ? 494  GLN   A C    1 
ATOM   7442  O  O    . GLN   A  1  494 ? 39.647  17.259  -13.735  1.00 108.69 ? 494  GLN   A O    1 
ATOM   7443  C  CB   . GLN   A  1  494 ? 37.425  19.087  -14.234  1.00 127.06 ? 494  GLN   A CB   1 
ATOM   7444  C  CG   . GLN   A  1  494 ? 36.577  20.339  -14.423  1.00 135.55 ? 494  GLN   A CG   1 
ATOM   7445  C  CD   . GLN   A  1  494 ? 35.810  20.345  -15.730  1.00 139.87 ? 494  GLN   A CD   1 
ATOM   7446  O  OE1  . GLN   A  1  494 ? 35.125  19.378  -16.066  1.00 140.33 ? 494  GLN   A OE1  1 
ATOM   7447  N  NE2  . GLN   A  1  494 ? 35.915  21.441  -16.472  1.00 141.98 ? 494  GLN   A NE2  1 
ATOM   7448  H  H    . GLN   A  1  494 ? 38.460  17.573  -16.197  1.00 139.07 ? 494  GLN   A H    1 
ATOM   7449  H  HA   . GLN   A  1  494 ? 39.013  20.018  -15.137  1.00 143.21 ? 494  GLN   A HA   1 
ATOM   7450  H  HB2  . GLN   A  1  494 ? 36.901  18.330  -14.538  1.00 152.46 ? 494  GLN   A HB2  1 
ATOM   7451  H  HB3  . GLN   A  1  494 ? 37.612  19.002  -13.286  1.00 152.46 ? 494  GLN   A HB3  1 
ATOM   7452  H  HG2  . GLN   A  1  494 ? 35.934  20.396  -13.699  1.00 162.63 ? 494  GLN   A HG2  1 
ATOM   7453  H  HG3  . GLN   A  1  494 ? 37.157  21.116  -14.414  1.00 162.63 ? 494  GLN   A HG3  1 
ATOM   7454  H  HE21 . GLN   A  1  494 ? 36.400  22.098  -16.203  1.00 170.36 ? 494  GLN   A HE21 1 
ATOM   7455  H  HE22 . GLN   A  1  494 ? 35.499  21.494  -17.223  1.00 170.36 ? 494  GLN   A HE22 1 
ATOM   7456  N  N    . VAL   A  1  495 ? 40.982  19.056  -14.021  1.00 108.03 ? 495  VAL   A N    1 
ATOM   7457  C  CA   . VAL   A  1  495 ? 42.134  18.492  -13.327  1.00 101.55 ? 495  VAL   A CA   1 
ATOM   7458  C  C    . VAL   A  1  495 ? 42.255  19.143  -11.956  1.00 101.90 ? 495  VAL   A C    1 
ATOM   7459  O  O    . VAL   A  1  495 ? 41.960  20.333  -11.793  1.00 102.80 ? 495  VAL   A O    1 
ATOM   7460  C  CB   . VAL   A  1  495 ? 43.433  18.684  -14.136  1.00 99.44  ? 495  VAL   A CB   1 
ATOM   7461  C  CG1  . VAL   A  1  495 ? 44.623  18.119  -13.371  1.00 96.53  ? 495  VAL   A CG1  1 
ATOM   7462  C  CG2  . VAL   A  1  495 ? 43.316  18.025  -15.503  1.00 98.87  ? 495  VAL   A CG2  1 
ATOM   7463  H  H    . VAL   A  1  495 ? 41.115  19.857  -14.306  1.00 129.62 ? 495  VAL   A H    1 
ATOM   7464  H  HA   . VAL   A  1  495 ? 41.988  17.541  -13.201  1.00 121.85 ? 495  VAL   A HA   1 
ATOM   7465  H  HB   . VAL   A  1  495 ? 43.580  19.633  -14.270  1.00 119.30 ? 495  VAL   A HB   1 
ATOM   7466  H  HG11 . VAL   A  1  495 ? 45.394  18.095  -13.959  1.00 115.81 ? 495  VAL   A HG11 1 
ATOM   7467  H  HG12 . VAL   A  1  495 ? 44.806  18.688  -12.608  1.00 115.81 ? 495  VAL   A HG12 1 
ATOM   7468  H  HG13 . VAL   A  1  495 ? 44.408  17.222  -13.071  1.00 115.81 ? 495  VAL   A HG13 1 
ATOM   7469  H  HG21 . VAL   A  1  495 ? 44.141  18.167  -15.993  1.00 118.62 ? 495  VAL   A HG21 1 
ATOM   7470  H  HG22 . VAL   A  1  495 ? 43.161  17.075  -15.384  1.00 118.62 ? 495  VAL   A HG22 1 
ATOM   7471  H  HG23 . VAL   A  1  495 ? 42.573  18.424  -15.983  1.00 118.62 ? 495  VAL   A HG23 1 
ATOM   7472  N  N    . GLU   A  1  496 ? 42.691  18.358  -10.973  1.00 103.80 ? 496  GLU   A N    1 
ATOM   7473  C  CA   . GLU   A  1  496 ? 42.925  18.843  -9.620   1.00 109.19 ? 496  GLU   A CA   1 
ATOM   7474  C  C    . GLU   A  1  496 ? 44.248  18.288  -9.112   1.00 110.31 ? 496  GLU   A C    1 
ATOM   7475  O  O    . GLU   A  1  496 ? 44.580  17.126  -9.366   1.00 110.44 ? 496  GLU   A O    1 
ATOM   7476  C  CB   . GLU   A  1  496 ? 41.789  18.439  -8.671   1.00 109.15 ? 496  GLU   A CB   1 
ATOM   7477  C  CG   . GLU   A  1  496 ? 40.615  19.407  -8.655   1.00 112.67 ? 496  GLU   A CG   1 
ATOM   7478  C  CD   . GLU   A  1  496 ? 39.538  18.999  -7.670   1.00 113.11 ? 496  GLU   A CD   1 
ATOM   7479  O  OE1  . GLU   A  1  496 ? 39.740  18.003  -6.944   1.00 110.43 ? 496  GLU   A OE1  1 
ATOM   7480  O  OE2  . GLU   A  1  496 ? 38.489  19.675  -7.624   1.00 115.85 ? 496  GLU   A OE2  1 
ATOM   7481  H  H    . GLU   A  1  496 ? 42.863  17.521  -11.069  1.00 124.54 ? 496  GLU   A H    1 
ATOM   7482  H  HA   . GLU   A  1  496 ? 42.982  19.811  -9.627   1.00 131.01 ? 496  GLU   A HA   1 
ATOM   7483  H  HB2  . GLU   A  1  496 ? 41.451  17.571  -8.943   1.00 130.96 ? 496  GLU   A HB2  1 
ATOM   7484  H  HB3  . GLU   A  1  496 ? 42.141  18.389  -7.769   1.00 130.96 ? 496  GLU   A HB3  1 
ATOM   7485  H  HG2  . GLU   A  1  496 ? 40.934  20.287  -8.403   1.00 135.19 ? 496  GLU   A HG2  1 
ATOM   7486  H  HG3  . GLU   A  1  496 ? 40.218  19.438  -9.539   1.00 135.19 ? 496  GLU   A HG3  1 
ATOM   7487  N  N    . LEU   A  1  497 ? 44.998  19.124  -8.399   1.00 109.39 ? 497  LEU   A N    1 
ATOM   7488  C  CA   . LEU   A  1  497 ? 46.279  18.747  -7.817   1.00 103.20 ? 497  LEU   A CA   1 
ATOM   7489  C  C    . LEU   A  1  497 ? 46.219  18.911  -6.305   1.00 102.58 ? 497  LEU   A C    1 
ATOM   7490  O  O    . LEU   A  1  497 ? 45.629  19.871  -5.800   1.00 104.12 ? 497  LEU   A O    1 
ATOM   7491  C  CB   . LEU   A  1  497 ? 47.417  19.600  -8.393   1.00 101.39 ? 497  LEU   A CB   1 
ATOM   7492  C  CG   . LEU   A  1  497 ? 47.759  19.374  -9.868   1.00 99.70  ? 497  LEU   A CG   1 
ATOM   7493  C  CD1  . LEU   A  1  497 ? 48.714  20.449  -10.367  1.00 99.90  ? 497  LEU   A CD1  1 
ATOM   7494  C  CD2  . LEU   A  1  497 ? 48.361  17.993  -10.076  1.00 97.27  ? 497  LEU   A CD2  1 
ATOM   7495  H  H    . LEU   A  1  497 ? 44.778  19.939  -8.236   1.00 131.25 ? 497  LEU   A H    1 
ATOM   7496  H  HA   . LEU   A  1  497 ? 46.467  17.817  -8.015   1.00 123.82 ? 497  LEU   A HA   1 
ATOM   7497  H  HB2  . LEU   A  1  497 ? 47.173  20.533  -8.296   1.00 121.64 ? 497  LEU   A HB2  1 
ATOM   7498  H  HB3  . LEU   A  1  497 ? 48.221  19.413  -7.882   1.00 121.64 ? 497  LEU   A HB3  1 
ATOM   7499  H  HG   . LEU   A  1  497 ? 46.943  19.429  -10.388  1.00 119.62 ? 497  LEU   A HG   1 
ATOM   7500  H  HD11 . LEU   A  1  497 ? 48.961  20.251  -11.284  1.00 119.86 ? 497  LEU   A HD11 1 
ATOM   7501  H  HD12 . LEU   A  1  497 ? 48.270  21.311  -10.323  1.00 119.86 ? 497  LEU   A HD12 1 
ATOM   7502  H  HD13 . LEU   A  1  497 ? 49.505  20.455  -9.806   1.00 119.86 ? 497  LEU   A HD13 1 
ATOM   7503  H  HD21 . LEU   A  1  497 ? 48.586  17.885  -11.013  1.00 116.70 ? 497  LEU   A HD21 1 
ATOM   7504  H  HD22 . LEU   A  1  497 ? 49.159  17.910  -9.532   1.00 116.70 ? 497  LEU   A HD22 1 
ATOM   7505  H  HD23 . LEU   A  1  497 ? 47.711  17.322  -9.813   1.00 116.70 ? 497  LEU   A HD23 1 
ATOM   7506  N  N    . LEU   A  1  498 ? 46.828  17.971  -5.582   1.00 101.71 ? 498  LEU   A N    1 
ATOM   7507  C  CA   . LEU   A  1  498 ? 46.887  18.026  -4.127   1.00 103.80 ? 498  LEU   A CA   1 
ATOM   7508  C  C    . LEU   A  1  498 ? 48.292  17.664  -3.673   1.00 100.93 ? 498  LEU   A C    1 
ATOM   7509  O  O    . LEU   A  1  498 ? 48.805  16.599  -4.030   1.00 99.07  ? 498  LEU   A O    1 
ATOM   7510  C  CB   . LEU   A  1  498 ? 45.864  17.079  -3.486   1.00 103.53 ? 498  LEU   A CB   1 
ATOM   7511  C  CG   . LEU   A  1  498 ? 45.980  16.927  -1.966   1.00 103.89 ? 498  LEU   A CG   1 
ATOM   7512  C  CD1  . LEU   A  1  498 ? 45.871  18.276  -1.267   1.00 107.15 ? 498  LEU   A CD1  1 
ATOM   7513  C  CD2  . LEU   A  1  498 ? 44.930  15.964  -1.435   1.00 101.86 ? 498  LEU   A CD2  1 
ATOM   7514  H  H    . LEU   A  1  498 ? 47.219  17.283  -5.919   1.00 122.03 ? 498  LEU   A H    1 
ATOM   7515  H  HA   . LEU   A  1  498 ? 46.690  18.928  -3.831   1.00 124.55 ? 498  LEU   A HA   1 
ATOM   7516  H  HB2  . LEU   A  1  498 ? 44.974  17.414  -3.678   1.00 124.21 ? 498  LEU   A HB2  1 
ATOM   7517  H  HB3  . LEU   A  1  498 ? 45.977  16.198  -3.876   1.00 124.21 ? 498  LEU   A HB3  1 
ATOM   7518  H  HG   . LEU   A  1  498 ? 46.855  16.560  -1.762   1.00 124.65 ? 498  LEU   A HG   1 
ATOM   7519  H  HD11 . LEU   A  1  498 ? 45.898  18.138  -0.307   1.00 128.56 ? 498  LEU   A HD11 1 
ATOM   7520  H  HD12 . LEU   A  1  498 ? 46.614  18.836  -1.542   1.00 128.56 ? 498  LEU   A HD12 1 
ATOM   7521  H  HD13 . LEU   A  1  498 ? 45.032  18.694  -1.517   1.00 128.56 ? 498  LEU   A HD13 1 
ATOM   7522  H  HD21 . LEU   A  1  498 ? 45.036  15.878  -0.475   1.00 122.21 ? 498  LEU   A HD21 1 
ATOM   7523  H  HD22 . LEU   A  1  498 ? 44.048  16.314  -1.641   1.00 122.21 ? 498  LEU   A HD22 1 
ATOM   7524  H  HD23 . LEU   A  1  498 ? 45.050  15.100  -1.860   1.00 122.21 ? 498  LEU   A HD23 1 
ATOM   7525  N  N    . LEU   A  1  499 ? 48.906  18.543  -2.887   1.00 102.62 ? 499  LEU   A N    1 
ATOM   7526  C  CA   . LEU   A  1  499 ? 50.230  18.299  -2.334   1.00 102.06 ? 499  LEU   A CA   1 
ATOM   7527  C  C    . LEU   A  1  499 ? 50.105  17.665  -0.955   1.00 103.00 ? 499  LEU   A C    1 
ATOM   7528  O  O    . LEU   A  1  499 ? 49.187  17.977  -0.193   1.00 103.75 ? 499  LEU   A O    1 
ATOM   7529  C  CB   . LEU   A  1  499 ? 51.023  19.601  -2.229   1.00 104.13 ? 499  LEU   A CB   1 
ATOM   7530  C  CG   . LEU   A  1  499 ? 50.987  20.532  -3.441   1.00 107.14 ? 499  LEU   A CG   1 
ATOM   7531  C  CD1  . LEU   A  1  499 ? 51.428  21.929  -3.034   1.00 111.70 ? 499  LEU   A CD1  1 
ATOM   7532  C  CD2  . LEU   A  1  499 ? 51.859  19.999  -4.567   1.00 106.00 ? 499  LEU   A CD2  1 
ATOM   7533  H  H    . LEU   A  1  499 ? 48.569  19.300  -2.657   1.00 123.13 ? 499  LEU   A H    1 
ATOM   7534  H  HA   . LEU   A  1  499 ? 50.719  17.695  -2.915   1.00 122.45 ? 499  LEU   A HA   1 
ATOM   7535  H  HB2  . LEU   A  1  499 ? 50.674  20.103  -1.476   1.00 124.94 ? 499  LEU   A HB2  1 
ATOM   7536  H  HB3  . LEU   A  1  499 ? 51.953  19.373  -2.074   1.00 124.94 ? 499  LEU   A HB3  1 
ATOM   7537  H  HG   . LEU   A  1  499 ? 50.079  20.579  -3.778   1.00 128.55 ? 499  LEU   A HG   1 
ATOM   7538  H  HD11 . LEU   A  1  499 ? 51.621  22.445  -3.833   1.00 134.02 ? 499  LEU   A HD11 1 
ATOM   7539  H  HD12 . LEU   A  1  499 ? 50.714  22.352  -2.532   1.00 134.02 ? 499  LEU   A HD12 1 
ATOM   7540  H  HD13 . LEU   A  1  499 ? 52.224  21.862  -2.484   1.00 134.02 ? 499  LEU   A HD13 1 
ATOM   7541  H  HD21 . LEU   A  1  499 ? 51.891  20.657  -5.280   1.00 127.19 ? 499  LEU   A HD21 1 
ATOM   7542  H  HD22 . LEU   A  1  499 ? 52.752  19.837  -4.226   1.00 127.19 ? 499  LEU   A HD22 1 
ATOM   7543  H  HD23 . LEU   A  1  499 ? 51.476  19.172  -4.899   1.00 127.19 ? 499  LEU   A HD23 1 
ATOM   7544  N  N    . ASP   A  1  500 ? 51.045  16.775  -0.637   1.00 102.98 ? 500  ASP   A N    1 
ATOM   7545  C  CA   . ASP   A  1  500 ? 51.067  16.078  0.649    1.00 106.03 ? 500  ASP   A CA   1 
ATOM   7546  C  C    . ASP   A  1  500 ? 49.721  15.408  0.919    1.00 106.89 ? 500  ASP   A C    1 
ATOM   7547  O  O    . ASP   A  1  500 ? 49.133  15.538  1.994    1.00 110.41 ? 500  ASP   A O    1 
ATOM   7548  C  CB   . ASP   A  1  500 ? 51.441  17.036  1.782    1.00 111.50 ? 500  ASP   A CB   1 
ATOM   7549  C  CG   . ASP   A  1  500 ? 52.151  16.339  2.931    1.00 112.88 ? 500  ASP   A CG   1 
ATOM   7550  O  OD1  . ASP   A  1  500 ? 52.298  15.100  2.886    1.00 110.24 ? 500  ASP   A OD1  1 
ATOM   7551  O  OD2  . ASP   A  1  500 ? 52.567  17.035  3.882    1.00 116.25 ? 500  ASP   A OD2  1 
ATOM   7552  H  H    . ASP   A  1  500 ? 51.693  16.554  -1.159   1.00 123.56 ? 500  ASP   A H    1 
ATOM   7553  H  HA   . ASP   A  1  500 ? 51.742  15.382  0.613    1.00 127.22 ? 500  ASP   A HA   1 
ATOM   7554  H  HB2  . ASP   A  1  500 ? 52.034  17.721  1.435    1.00 133.79 ? 500  ASP   A HB2  1 
ATOM   7555  H  HB3  . ASP   A  1  500 ? 50.633  17.444  2.132    1.00 133.79 ? 500  ASP   A HB3  1 
ATOM   7556  N  N    . LYS   A  1  501 ? 49.232  14.677  -0.085   1.00 105.02 ? 501  LYS   A N    1 
ATOM   7557  C  CA   . LYS   A  1  501 ? 47.922  14.046  0.032    1.00 105.86 ? 501  LYS   A CA   1 
ATOM   7558  C  C    . LYS   A  1  501 ? 47.910  12.973  1.113    1.00 105.32 ? 501  LYS   A C    1 
ATOM   7559  O  O    . LYS   A  1  501 ? 46.906  12.805  1.816    1.00 106.92 ? 501  LYS   A O    1 
ATOM   7560  C  CB   . LYS   A  1  501 ? 47.508  13.444  -1.311   1.00 105.17 ? 501  LYS   A CB   1 
ATOM   7561  C  CG   . LYS   A  1  501 ? 46.463  12.345  -1.186   1.00 105.48 ? 501  LYS   A CG   1 
ATOM   7562  C  CD   . LYS   A  1  501 ? 45.716  12.114  -2.486   1.00 103.60 ? 501  LYS   A CD   1 
ATOM   7563  C  CE   . LYS   A  1  501 ? 44.488  11.244  -2.262   1.00 102.63 ? 501  LYS   A CE   1 
ATOM   7564  N  NZ   . LYS   A  1  501 ? 43.438  11.947  -1.469   1.00 104.41 ? 501  LYS   A NZ   1 
ATOM   7565  H  H    . LYS   A  1  501 ? 49.634  14.534  -0.832   1.00 126.01 ? 501  LYS   A H    1 
ATOM   7566  H  HA   . LYS   A  1  501 ? 47.276  14.727  0.276    1.00 127.02 ? 501  LYS   A HA   1 
ATOM   7567  H  HB2  . LYS   A  1  501 ? 47.136  14.146  -1.868   1.00 126.18 ? 501  LYS   A HB2  1 
ATOM   7568  H  HB3  . LYS   A  1  501 ? 48.291  13.062  -1.738   1.00 126.18 ? 501  LYS   A HB3  1 
ATOM   7569  H  HG2  . LYS   A  1  501 ? 46.900  11.516  -0.937   1.00 126.56 ? 501  LYS   A HG2  1 
ATOM   7570  H  HG3  . LYS   A  1  501 ? 45.817  12.596  -0.507   1.00 126.56 ? 501  LYS   A HG3  1 
ATOM   7571  H  HD2  . LYS   A  1  501 ? 45.426  12.966  -2.848   1.00 124.31 ? 501  LYS   A HD2  1 
ATOM   7572  H  HD3  . LYS   A  1  501 ? 46.299  11.665  -3.118   1.00 124.31 ? 501  LYS   A HD3  1 
ATOM   7573  H  HE2  . LYS   A  1  501 ? 44.107  11.003  -3.121   1.00 123.14 ? 501  LYS   A HE2  1 
ATOM   7574  H  HE3  . LYS   A  1  501 ? 44.748  10.444  -1.779   1.00 123.14 ? 501  LYS   A HE3  1 
ATOM   7575  H  HZ1  . LYS   A  1  501 ? 42.661  11.519  -1.546   1.00 125.28 ? 501  LYS   A HZ1  1 
ATOM   7576  H  HZ2  . LYS   A  1  501 ? 43.671  11.971  -0.611   1.00 125.28 ? 501  LYS   A HZ2  1 
ATOM   7577  H  HZ3  . LYS   A  1  501 ? 43.340  12.780  -1.765   1.00 125.28 ? 501  LYS   A HZ3  1 
ATOM   7578  N  N    . LEU   A  1  502 ? 49.013  12.238  1.264    1.00 106.23 ? 502  LEU   A N    1 
ATOM   7579  C  CA   . LEU   A  1  502 ? 48.990  11.047  2.107    1.00 113.19 ? 502  LEU   A CA   1 
ATOM   7580  C  C    . LEU   A  1  502 ? 48.678  11.376  3.562    1.00 120.49 ? 502  LEU   A C    1 
ATOM   7581  O  O    . LEU   A  1  502 ? 48.131  10.530  4.280    1.00 124.44 ? 502  LEU   A O    1 
ATOM   7582  C  CB   . LEU   A  1  502 ? 50.325  10.308  2.002    1.00 116.65 ? 502  LEU   A CB   1 
ATOM   7583  C  CG   . LEU   A  1  502 ? 50.356  9.194   0.953    1.00 117.94 ? 502  LEU   A CG   1 
ATOM   7584  C  CD1  . LEU   A  1  502 ? 51.761  8.638   0.782    1.00 120.51 ? 502  LEU   A CD1  1 
ATOM   7585  C  CD2  . LEU   A  1  502 ? 49.383  8.084   1.330    1.00 116.44 ? 502  LEU   A CD2  1 
ATOM   7586  H  H    . LEU   A  1  502 ? 49.771  12.404  0.895    1.00 127.46 ? 502  LEU   A H    1 
ATOM   7587  H  HA   . LEU   A  1  502 ? 48.290  10.457  1.786    1.00 135.80 ? 502  LEU   A HA   1 
ATOM   7588  H  HB2  . LEU   A  1  502 ? 51.014  10.950  1.769    1.00 139.97 ? 502  LEU   A HB2  1 
ATOM   7589  H  HB3  . LEU   A  1  502 ? 50.522  9.906   2.863    1.00 139.97 ? 502  LEU   A HB3  1 
ATOM   7590  H  HG   . LEU   A  1  502 ? 50.084  9.564   0.099    1.00 141.51 ? 502  LEU   A HG   1 
ATOM   7591  H  HD11 . LEU   A  1  502 ? 51.785  8.079   -0.010   1.00 144.60 ? 502  LEU   A HD11 1 
ATOM   7592  H  HD12 . LEU   A  1  502 ? 52.383  9.376   0.684    1.00 144.60 ? 502  LEU   A HD12 1 
ATOM   7593  H  HD13 . LEU   A  1  502 ? 51.990  8.113   1.564    1.00 144.60 ? 502  LEU   A HD13 1 
ATOM   7594  H  HD21 . LEU   A  1  502 ? 49.722  7.239   0.995    1.00 139.71 ? 502  LEU   A HD21 1 
ATOM   7595  H  HD22 . LEU   A  1  502 ? 49.303  8.049   2.296    1.00 139.71 ? 502  LEU   A HD22 1 
ATOM   7596  H  HD23 . LEU   A  1  502 ? 48.518  8.274   0.934    1.00 139.71 ? 502  LEU   A HD23 1 
ATOM   7597  N  N    . LYS   A  1  503 ? 49.007  12.582  4.018    1.00 122.19 ? 503  LYS   A N    1 
ATOM   7598  C  CA   . LYS   A  1  503 ? 48.712  12.947  5.397    1.00 122.96 ? 503  LYS   A CA   1 
ATOM   7599  C  C    . LYS   A  1  503 ? 47.204  12.984  5.621    1.00 126.91 ? 503  LYS   A C    1 
ATOM   7600  O  O    . LYS   A  1  503 ? 46.468  13.642  4.881    1.00 125.06 ? 503  LYS   A O    1 
ATOM   7601  C  CB   . LYS   A  1  503 ? 49.336  14.301  5.741    1.00 119.07 ? 503  LYS   A CB   1 
ATOM   7602  C  CG   . LYS   A  1  503 ? 50.860  14.291  5.828    1.00 111.80 ? 503  LYS   A CG   1 
ATOM   7603  C  CD   . LYS   A  1  503 ? 51.359  13.217  6.785    1.00 105.98 ? 503  LYS   A CD   1 
ATOM   7604  C  CE   . LYS   A  1  503 ? 52.428  13.736  7.730    1.00 104.04 ? 503  LYS   A CE   1 
ATOM   7605  N  NZ   . LYS   A  1  503 ? 52.633  12.787  8.860    1.00 104.57 ? 503  LYS   A NZ   1 
ATOM   7606  H  H    . LYS   A  1  503 ? 49.394  13.195  3.556    1.00 146.60 ? 503  LYS   A H    1 
ATOM   7607  H  HA   . LYS   A  1  503 ? 49.096  12.284  5.992    1.00 147.53 ? 503  LYS   A HA   1 
ATOM   7608  H  HB2  . LYS   A  1  503 ? 49.086  14.939  5.055    1.00 142.86 ? 503  LYS   A HB2  1 
ATOM   7609  H  HB3  . LYS   A  1  503 ? 48.995  14.589  6.602    1.00 142.86 ? 503  LYS   A HB3  1 
ATOM   7610  H  HG2  . LYS   A  1  503 ? 51.231  14.111  4.949    1.00 134.14 ? 503  LYS   A HG2  1 
ATOM   7611  H  HG3  . LYS   A  1  503 ? 51.169  15.152  6.148    1.00 134.14 ? 503  LYS   A HG3  1 
ATOM   7612  H  HD2  . LYS   A  1  503 ? 50.615  12.897  7.319    1.00 127.16 ? 503  LYS   A HD2  1 
ATOM   7613  H  HD3  . LYS   A  1  503 ? 51.739  12.486  6.273    1.00 127.16 ? 503  LYS   A HD3  1 
ATOM   7614  H  HE2  . LYS   A  1  503 ? 53.266  13.831  7.251    1.00 124.83 ? 503  LYS   A HE2  1 
ATOM   7615  H  HE3  . LYS   A  1  503 ? 52.153  14.593  8.092    1.00 124.83 ? 503  LYS   A HE3  1 
ATOM   7616  H  HZ1  . LYS   A  1  503 ? 53.499  12.732  9.058    1.00 125.47 ? 503  LYS   A HZ1  1 
ATOM   7617  H  HZ2  . LYS   A  1  503 ? 52.190  13.069  9.578    1.00 125.47 ? 503  LYS   A HZ2  1 
ATOM   7618  H  HZ3  . LYS   A  1  503 ? 52.336  11.978  8.636    1.00 125.47 ? 503  LYS   A HZ3  1 
ATOM   7619  N  N    . GLN   A  1  504 ? 46.751  12.273  6.650    1.00 131.54 ? 504  GLN   A N    1 
ATOM   7620  C  CA   . GLN   A  1  504 ? 45.334  12.165  6.952    1.00 132.06 ? 504  GLN   A CA   1 
ATOM   7621  C  C    . GLN   A  1  504 ? 44.823  13.449  7.604    1.00 125.38 ? 504  GLN   A C    1 
ATOM   7622  O  O    . GLN   A  1  504 ? 45.592  14.314  8.030    1.00 121.20 ? 504  GLN   A O    1 
ATOM   7623  C  CB   . GLN   A  1  504 ? 45.076  10.970  7.868    1.00 138.05 ? 504  GLN   A CB   1 
ATOM   7624  C  CG   . GLN   A  1  504 ? 45.389  9.617   7.246    1.00 135.92 ? 504  GLN   A CG   1 
ATOM   7625  C  CD   . GLN   A  1  504 ? 44.300  9.140   6.306    1.00 133.10 ? 504  GLN   A CD   1 
ATOM   7626  O  OE1  . GLN   A  1  504 ? 44.235  9.555   5.149    1.00 129.57 ? 504  GLN   A OE1  1 
ATOM   7627  N  NE2  . GLN   A  1  504 ? 43.434  8.261   6.801    1.00 134.35 ? 504  GLN   A NE2  1 
ATOM   7628  H  H    . GLN   A  1  504 ? 47.254  11.838  7.195    1.00 157.83 ? 504  GLN   A H    1 
ATOM   7629  H  HA   . GLN   A  1  504 ? 44.844  12.029  6.126    1.00 158.45 ? 504  GLN   A HA   1 
ATOM   7630  H  HB2  . GLN   A  1  504 ? 45.630  11.062  8.660    1.00 165.64 ? 504  GLN   A HB2  1 
ATOM   7631  H  HB3  . GLN   A  1  504 ? 44.139  10.968  8.117    1.00 165.64 ? 504  GLN   A HB3  1 
ATOM   7632  H  HG2  . GLN   A  1  504 ? 46.213  9.684   6.739    1.00 163.08 ? 504  GLN   A HG2  1 
ATOM   7633  H  HG3  . GLN   A  1  504 ? 45.486  8.958   7.951    1.00 163.08 ? 504  GLN   A HG3  1 
ATOM   7634  H  HE21 . GLN   A  1  504 ? 43.510  7.994   7.615    1.00 161.20 ? 504  GLN   A HE21 1 
ATOM   7635  H  HE22 . GLN   A  1  504 ? 42.797  7.960   6.308    1.00 161.20 ? 504  GLN   A HE22 1 
ATOM   7636  N  N    . LYS   A  1  505 ? 43.499  13.565  7.676    1.00 123.29 ? 505  LYS   A N    1 
ATOM   7637  C  CA   . LYS   A  1  505 ? 42.887  14.727  8.307    1.00 123.38 ? 505  LYS   A CA   1 
ATOM   7638  C  C    . LYS   A  1  505 ? 43.365  14.859  9.748    1.00 124.28 ? 505  LYS   A C    1 
ATOM   7639  O  O    . LYS   A  1  505 ? 43.415  13.880  10.498   1.00 123.47 ? 505  LYS   A O    1 
ATOM   7640  C  CB   . LYS   A  1  505 ? 41.364  14.615  8.260    1.00 123.51 ? 505  LYS   A CB   1 
ATOM   7641  C  CG   . LYS   A  1  505 ? 40.787  14.682  6.855    1.00 119.97 ? 505  LYS   A CG   1 
ATOM   7642  C  CD   . LYS   A  1  505 ? 39.271  14.573  6.875    1.00 122.54 ? 505  LYS   A CD   1 
ATOM   7643  C  CE   . LYS   A  1  505 ? 38.684  14.693  5.478    1.00 119.51 ? 505  LYS   A CE   1 
ATOM   7644  N  NZ   . LYS   A  1  505 ? 37.201  14.565  5.488    1.00 119.98 ? 505  LYS   A NZ   1 
ATOM   7645  H  H    . LYS   A  1  505 ? 42.938  12.989  7.370    1.00 147.93 ? 505  LYS   A H    1 
ATOM   7646  H  HA   . LYS   A  1  505 ? 43.143  15.529  7.826    1.00 148.03 ? 505  LYS   A HA   1 
ATOM   7647  H  HB2  . LYS   A  1  505 ? 41.102  13.765  8.647    1.00 148.20 ? 505  LYS   A HB2  1 
ATOM   7648  H  HB3  . LYS   A  1  505 ? 40.982  15.344  8.772    1.00 148.20 ? 505  LYS   A HB3  1 
ATOM   7649  H  HG2  . LYS   A  1  505 ? 41.027  15.529  6.448    1.00 143.95 ? 505  LYS   A HG2  1 
ATOM   7650  H  HG3  . LYS   A  1  505 ? 41.139  13.949  6.326    1.00 143.95 ? 505  LYS   A HG3  1 
ATOM   7651  H  HD2  . LYS   A  1  505 ? 39.016  13.711  7.239    1.00 147.03 ? 505  LYS   A HD2  1 
ATOM   7652  H  HD3  . LYS   A  1  505 ? 38.905  15.285  7.421    1.00 147.03 ? 505  LYS   A HD3  1 
ATOM   7653  H  HE2  . LYS   A  1  505 ? 38.912  15.560  5.108    1.00 143.40 ? 505  LYS   A HE2  1 
ATOM   7654  H  HE3  . LYS   A  1  505 ? 39.045  13.988  4.917    1.00 143.40 ? 505  LYS   A HE3  1 
ATOM   7655  H  HZ1  . LYS   A  1  505 ? 36.843  15.123  4.894    1.00 143.95 ? 505  LYS   A HZ1  1 
ATOM   7656  H  HZ2  . LYS   A  1  505 ? 36.965  13.732  5.280    1.00 143.95 ? 505  LYS   A HZ2  1 
ATOM   7657  H  HZ3  . LYS   A  1  505 ? 36.884  14.762  6.296    1.00 143.95 ? 505  LYS   A HZ3  1 
ATOM   7658  N  N    . GLY   A  1  506 ? 43.714  16.084  10.133   1.00 125.81 ? 506  GLY   A N    1 
ATOM   7659  C  CA   . GLY   A  1  506 ? 44.306  16.339  11.426   1.00 127.98 ? 506  GLY   A CA   1 
ATOM   7660  C  C    . GLY   A  1  506 ? 45.815  16.257  11.455   1.00 124.24 ? 506  GLY   A C    1 
ATOM   7661  O  O    . GLY   A  1  506 ? 46.408  16.429  12.528   1.00 123.72 ? 506  GLY   A O    1 
ATOM   7662  H  H    . GLY   A  1  506 ? 43.614  16.789  9.650    1.00 150.95 ? 506  GLY   A H    1 
ATOM   7663  H  HA2  . GLY   A  1  506 ? 44.051  17.229  11.715   1.00 153.55 ? 506  GLY   A HA2  1 
ATOM   7664  H  HA3  . GLY   A  1  506 ? 43.961  15.690  12.060   1.00 153.55 ? 506  GLY   A HA3  1 
ATOM   7665  N  N    . ALA   A  1  507 ? 46.454  15.999  10.318   1.00 121.98 ? 507  ALA   A N    1 
ATOM   7666  C  CA   . ALA   A  1  507 ? 47.904  15.933  10.218   1.00 120.32 ? 507  ALA   A CA   1 
ATOM   7667  C  C    . ALA   A  1  507 ? 48.416  17.113  9.405    1.00 120.13 ? 507  ALA   A C    1 
ATOM   7668  O  O    . ALA   A  1  507 ? 47.784  17.526  8.426    1.00 118.23 ? 507  ALA   A O    1 
ATOM   7669  C  CB   . ALA   A  1  507 ? 48.352  14.619  9.575    1.00 114.13 ? 507  ALA   A CB   1 
ATOM   7670  H  H    . ALA   A  1  507 ? 46.056  15.854  9.570    1.00 146.36 ? 507  ALA   A H    1 
ATOM   7671  H  HA   . ALA   A  1  507 ? 48.295  15.982  11.105   1.00 144.37 ? 507  ALA   A HA   1 
ATOM   7672  H  HB1  . ALA   A  1  507 ? 49.307  14.658  9.409    1.00 136.94 ? 507  ALA   A HB1  1 
ATOM   7673  H  HB2  . ALA   A  1  507 ? 48.151  13.887  10.179   1.00 136.94 ? 507  ALA   A HB2  1 
ATOM   7674  H  HB3  . ALA   A  1  507 ? 47.876  14.498  8.739    1.00 136.94 ? 507  ALA   A HB3  1 
ATOM   7675  N  N    . ILE   A  1  508 ? 49.566  17.649  9.811    1.00 121.00 ? 508  ILE   A N    1 
ATOM   7676  C  CA   . ILE   A  1  508 ? 50.105  18.834  9.159    1.00 119.19 ? 508  ILE   A CA   1 
ATOM   7677  C  C    . ILE   A  1  508 ? 50.473  18.499  7.721    1.00 118.33 ? 508  ILE   A C    1 
ATOM   7678  O  O    . ILE   A  1  508 ? 50.970  17.403  7.425    1.00 114.55 ? 508  ILE   A O    1 
ATOM   7679  C  CB   . ILE   A  1  508 ? 51.326  19.370  9.925    1.00 115.71 ? 508  ILE   A CB   1 
ATOM   7680  C  CG1  . ILE   A  1  508 ? 51.029  19.515  11.420   1.00 117.10 ? 508  ILE   A CG1  1 
ATOM   7681  C  CG2  . ILE   A  1  508 ? 51.747  20.721  9.364    1.00 116.16 ? 508  ILE   A CG2  1 
ATOM   7682  C  CD1  . ILE   A  1  508 ? 52.278  19.536  12.281   1.00 117.42 ? 508  ILE   A CD1  1 
ATOM   7683  H  H    . ILE   A  1  508 ? 50.048  17.346  10.456   1.00 145.18 ? 508  ILE   A H    1 
ATOM   7684  H  HA   . ILE   A  1  508 ? 49.424  19.525  9.157    1.00 143.01 ? 508  ILE   A HA   1 
ATOM   7685  H  HB   . ILE   A  1  508 ? 52.043  18.726  9.813    1.00 138.83 ? 508  ILE   A HB   1 
ATOM   7686  H  HG12 . ILE   A  1  508 ? 50.553  20.348  11.565   1.00 140.50 ? 508  ILE   A HG12 1 
ATOM   7687  H  HG13 . ILE   A  1  508 ? 50.482  18.766  11.705   1.00 140.50 ? 508  ILE   A HG13 1 
ATOM   7688  H  HG21 . ILE   A  1  508 ? 52.420  21.108  9.945    1.00 139.37 ? 508  ILE   A HG21 1 
ATOM   7689  H  HG22 . ILE   A  1  508 ? 52.111  20.594  8.474    1.00 139.37 ? 508  ILE   A HG22 1 
ATOM   7690  H  HG23 . ILE   A  1  508 ? 50.971  21.302  9.324    1.00 139.37 ? 508  ILE   A HG23 1 
ATOM   7691  H  HD11 . ILE   A  1  508 ? 52.024  19.710  13.201   1.00 140.89 ? 508  ILE   A HD11 1 
ATOM   7692  H  HD12 . ILE   A  1  508 ? 52.720  18.675  12.217   1.00 140.89 ? 508  ILE   A HD12 1 
ATOM   7693  H  HD13 . ILE   A  1  508 ? 52.869  20.236  11.963   1.00 140.89 ? 508  ILE   A HD13 1 
ATOM   7694  N  N    . ARG   A  1  509 ? 50.231  19.443  6.817    1.00 121.85 ? 509  ARG   A N    1 
ATOM   7695  C  CA   . ARG   A  1  509 ? 50.596  19.307  5.412    1.00 120.59 ? 509  ARG   A CA   1 
ATOM   7696  C  C    . ARG   A  1  509 ? 51.782  20.216  5.125    1.00 120.78 ? 509  ARG   A C    1 
ATOM   7697  O  O    . ARG   A  1  509 ? 51.692  21.437  5.290    1.00 125.64 ? 509  ARG   A O    1 
ATOM   7698  C  CB   . ARG   A  1  509 ? 49.413  19.635  4.503    1.00 121.11 ? 509  ARG   A CB   1 
ATOM   7699  C  CG   . ARG   A  1  509 ? 48.428  18.488  4.395    1.00 121.11 ? 509  ARG   A CG   1 
ATOM   7700  C  CD   . ARG   A  1  509 ? 47.154  18.907  3.699    1.00 126.61 ? 509  ARG   A CD   1 
ATOM   7701  N  NE   . ARG   A  1  509 ? 46.300  17.759  3.408    1.00 131.04 ? 509  ARG   A NE   1 
ATOM   7702  C  CZ   . ARG   A  1  509 ? 45.013  17.844  3.089    1.00 138.82 ? 509  ARG   A CZ   1 
ATOM   7703  N  NH1  . ARG   A  1  509 ? 44.418  19.028  3.027    1.00 144.14 ? 509  ARG   A NH1  1 
ATOM   7704  N  NH2  . ARG   A  1  509 ? 44.319  16.743  2.839    1.00 139.34 ? 509  ARG   A NH2  1 
ATOM   7705  H  H    . ARG   A  1  509 ? 49.847  20.191  6.999    1.00 146.20 ? 509  ARG   A H    1 
ATOM   7706  H  HA   . ARG   A  1  509 ? 50.865  18.393  5.229    1.00 144.68 ? 509  ARG   A HA   1 
ATOM   7707  H  HB2  . ARG   A  1  509 ? 48.942  20.403  4.862    1.00 145.31 ? 509  ARG   A HB2  1 
ATOM   7708  H  HB3  . ARG   A  1  509 ? 49.743  19.833  3.613    1.00 145.31 ? 509  ARG   A HB3  1 
ATOM   7709  H  HG2  . ARG   A  1  509 ? 48.830  17.768  3.885    1.00 145.32 ? 509  ARG   A HG2  1 
ATOM   7710  H  HG3  . ARG   A  1  509 ? 48.200  18.178  5.285    1.00 145.32 ? 509  ARG   A HG3  1 
ATOM   7711  H  HD2  . ARG   A  1  509 ? 46.661  19.516  4.271    1.00 151.91 ? 509  ARG   A HD2  1 
ATOM   7712  H  HD3  . ARG   A  1  509 ? 47.374  19.343  2.861    1.00 151.91 ? 509  ARG   A HD3  1 
ATOM   7713  H  HE   . ARG   A  1  509 ? 46.654  16.976  3.446    1.00 157.22 ? 509  ARG   A HE   1 
ATOM   7714  H  HH11 . ARG   A  1  509 ? 44.865  19.743  3.194    1.00 172.95 ? 509  ARG   A HH11 1 
ATOM   7715  H  HH12 . ARG   A  1  509 ? 43.585  19.080  2.820    1.00 172.95 ? 509  ARG   A HH12 1 
ATOM   7716  H  HH21 . ARG   A  1  509 ? 44.701  15.974  2.883    1.00 167.19 ? 509  ARG   A HH21 1 
ATOM   7717  H  HH22 . ARG   A  1  509 ? 43.486  16.798  2.632    1.00 167.19 ? 509  ARG   A HH22 1 
ATOM   7718  N  N    . ARG   A  1  510 ? 52.887  19.612  4.688    1.00 113.80 ? 510  ARG   A N    1 
ATOM   7719  C  CA   . ARG   A  1  510 ? 54.161  20.316  4.615    1.00 109.22 ? 510  ARG   A CA   1 
ATOM   7720  C  C    . ARG   A  1  510 ? 54.286  21.179  3.367    1.00 104.84 ? 510  ARG   A C    1 
ATOM   7721  O  O    . ARG   A  1  510 ? 54.910  22.245  3.421    1.00 104.96 ? 510  ARG   A O    1 
ATOM   7722  C  CB   . ARG   A  1  510 ? 55.302  19.299  4.667    1.00 105.96 ? 510  ARG   A CB   1 
ATOM   7723  C  CG   . ARG   A  1  510 ? 55.302  18.463  5.937    1.00 108.13 ? 510  ARG   A CG   1 
ATOM   7724  C  CD   . ARG   A  1  510 ? 56.053  17.155  5.767    1.00 108.35 ? 510  ARG   A CD   1 
ATOM   7725  N  NE   . ARG   A  1  510 ? 55.308  16.211  4.940    1.00 108.40 ? 510  ARG   A NE   1 
ATOM   7726  C  CZ   . ARG   A  1  510 ? 55.540  14.902  4.895    1.00 109.88 ? 510  ARG   A CZ   1 
ATOM   7727  N  NH1  . ARG   A  1  510 ? 56.498  14.363  5.637    1.00 110.42 ? 510  ARG   A NH1  1 
ATOM   7728  N  NH2  . ARG   A  1  510 ? 54.804  14.128  4.109    1.00 110.21 ? 510  ARG   A NH2  1 
ATOM   7729  H  H    . ARG   A  1  510 ? 52.924  18.793  4.427    1.00 136.54 ? 510  ARG   A H    1 
ATOM   7730  H  HA   . ARG   A  1  510 ? 54.235  20.908  5.380    1.00 131.05 ? 510  ARG   A HA   1 
ATOM   7731  H  HB2  . ARG   A  1  510 ? 55.219  18.695  3.913    1.00 127.13 ? 510  ARG   A HB2  1 
ATOM   7732  H  HB3  . ARG   A  1  510 ? 56.147  19.773  4.622    1.00 127.13 ? 510  ARG   A HB3  1 
ATOM   7733  H  HG2  . ARG   A  1  510 ? 55.729  18.966  6.648    1.00 129.74 ? 510  ARG   A HG2  1 
ATOM   7734  H  HG3  . ARG   A  1  510 ? 54.386  18.256  6.181    1.00 129.74 ? 510  ARG   A HG3  1 
ATOM   7735  H  HD2  . ARG   A  1  510 ? 56.906  17.328  5.339    1.00 130.00 ? 510  ARG   A HD2  1 
ATOM   7736  H  HD3  . ARG   A  1  510 ? 56.195  16.751  6.638    1.00 130.00 ? 510  ARG   A HD3  1 
ATOM   7737  H  HE   . ARG   A  1  510 ? 54.676  16.522  4.447    1.00 130.06 ? 510  ARG   A HE   1 
ATOM   7738  H  HH11 . ARG   A  1  510 ? 56.974  14.861  6.152    1.00 132.48 ? 510  ARG   A HH11 1 
ATOM   7739  H  HH12 . ARG   A  1  510 ? 56.643  13.516  5.604    1.00 132.48 ? 510  ARG   A HH12 1 
ATOM   7740  H  HH21 . ARG   A  1  510 ? 54.179  14.472  3.629    1.00 132.24 ? 510  ARG   A HH21 1 
ATOM   7741  H  HH22 . ARG   A  1  510 ? 54.953  13.281  4.079    1.00 132.24 ? 510  ARG   A HH22 1 
ATOM   7742  N  N    . ALA   A  1  511 ? 53.714  20.748  2.249    1.00 102.04 ? 511  ALA   A N    1 
ATOM   7743  C  CA   . ALA   A  1  511 ? 53.860  21.443  0.978    1.00 102.04 ? 511  ALA   A CA   1 
ATOM   7744  C  C    . ALA   A  1  511 ? 52.617  22.265  0.668    1.00 102.70 ? 511  ALA   A C    1 
ATOM   7745  O  O    . ALA   A  1  511 ? 51.490  21.836  0.934    1.00 102.11 ? 511  ALA   A O    1 
ATOM   7746  C  CB   . ALA   A  1  511 ? 54.121  20.450  -0.157   1.00 99.78  ? 511  ALA   A CB   1 
ATOM   7747  H  H    . ALA   A  1  511 ? 53.226  20.041  2.201    1.00 122.43 ? 511  ALA   A H    1 
ATOM   7748  H  HA   . ALA   A  1  511 ? 54.613  22.051  1.037    1.00 122.43 ? 511  ALA   A HA   1 
ATOM   7749  H  HB1  . ALA   A  1  511 ? 54.169  20.935  -0.996   1.00 119.71 ? 511  ALA   A HB1  1 
ATOM   7750  H  HB2  . ALA   A  1  511 ? 54.960  19.993  0.010    1.00 119.71 ? 511  ALA   A HB2  1 
ATOM   7751  H  HB3  . ALA   A  1  511 ? 53.395  19.808  -0.187   1.00 119.71 ? 511  ALA   A HB3  1 
ATOM   7752  N  N    . LEU   A  1  512 ? 52.834  23.451  0.103    1.00 104.28 ? 512  LEU   A N    1 
ATOM   7753  C  CA   . LEU   A  1  512 ? 51.761  24.337  -0.322   1.00 105.99 ? 512  LEU   A CA   1 
ATOM   7754  C  C    . LEU   A  1  512 ? 52.122  24.919  -1.680   1.00 103.95 ? 512  LEU   A C    1 
ATOM   7755  O  O    . LEU   A  1  512 ? 53.300  25.033  -2.027   1.00 102.50 ? 512  LEU   A O    1 
ATOM   7756  C  CB   . LEU   A  1  512 ? 51.526  25.474  0.682    1.00 112.79 ? 512  LEU   A CB   1 
ATOM   7757  C  CG   . LEU   A  1  512 ? 51.250  25.086  2.136    1.00 113.71 ? 512  LEU   A CG   1 
ATOM   7758  C  CD1  . LEU   A  1  512 ? 51.214  26.330  3.012    1.00 116.39 ? 512  LEU   A CD1  1 
ATOM   7759  C  CD2  . LEU   A  1  512 ? 49.949  24.309  2.263    1.00 111.79 ? 512  LEU   A CD2  1 
ATOM   7760  H  H    . LEU   A  1  512 ? 53.618  23.771  -0.049   1.00 125.12 ? 512  LEU   A H    1 
ATOM   7761  H  HA   . LEU   A  1  512 ? 50.935  23.834  -0.403   1.00 127.17 ? 512  LEU   A HA   1 
ATOM   7762  H  HB2  . LEU   A  1  512 ? 52.318  26.034  0.687    1.00 135.33 ? 512  LEU   A HB2  1 
ATOM   7763  H  HB3  . LEU   A  1  512 ? 50.760  25.986  0.378    1.00 135.33 ? 512  LEU   A HB3  1 
ATOM   7764  H  HG   . LEU   A  1  512 ? 51.964  24.508  2.445    1.00 136.43 ? 512  LEU   A HG   1 
ATOM   7765  H  HD11 . LEU   A  1  512 ? 51.040  26.066  3.929    1.00 139.65 ? 512  LEU   A HD11 1 
ATOM   7766  H  HD12 . LEU   A  1  512 ? 52.071  26.782  2.955    1.00 139.65 ? 512  LEU   A HD12 1 
ATOM   7767  H  HD13 . LEU   A  1  512 ? 50.509  26.918  2.697    1.00 139.65 ? 512  LEU   A HD13 1 
ATOM   7768  H  HD21 . LEU   A  1  512 ? 49.811  24.075  3.194    1.00 134.13 ? 512  LEU   A HD21 1 
ATOM   7769  H  HD22 . LEU   A  1  512 ? 49.218  24.864  1.950    1.00 134.13 ? 512  LEU   A HD22 1 
ATOM   7770  H  HD23 . LEU   A  1  512 ? 50.008  23.505  1.724    1.00 134.13 ? 512  LEU   A HD23 1 
ATOM   7771  N  N    . PHE   A  1  513 ? 51.100  25.283  -2.449   1.00 105.27 ? 513  PHE   A N    1 
ATOM   7772  C  CA   . PHE   A  1  513 ? 51.329  25.930  -3.732   1.00 107.92 ? 513  PHE   A CA   1 
ATOM   7773  C  C    . PHE   A  1  513 ? 51.703  27.393  -3.526   1.00 111.34 ? 513  PHE   A C    1 
ATOM   7774  O  O    . PHE   A  1  513 ? 51.236  28.054  -2.593   1.00 113.00 ? 513  PHE   A O    1 
ATOM   7775  C  CB   . PHE   A  1  513 ? 50.094  25.816  -4.625   1.00 110.77 ? 513  PHE   A CB   1 
ATOM   7776  C  CG   . PHE   A  1  513 ? 49.925  24.459  -5.245   1.00 110.17 ? 513  PHE   A CG   1 
ATOM   7777  C  CD1  . PHE   A  1  513 ? 50.820  24.006  -6.201   1.00 109.18 ? 513  PHE   A CD1  1 
ATOM   7778  C  CD2  . PHE   A  1  513 ? 48.873  23.638  -4.876   1.00 110.01 ? 513  PHE   A CD2  1 
ATOM   7779  C  CE1  . PHE   A  1  513 ? 50.672  22.759  -6.774   1.00 106.86 ? 513  PHE   A CE1  1 
ATOM   7780  C  CE2  . PHE   A  1  513 ? 48.719  22.390  -5.448   1.00 108.02 ? 513  PHE   A CE2  1 
ATOM   7781  C  CZ   . PHE   A  1  513 ? 49.619  21.950  -6.399   1.00 106.54 ? 513  PHE   A CZ   1 
ATOM   7782  H  H    . PHE   A  1  513 ? 50.272  25.167  -2.250   1.00 126.31 ? 513  PHE   A H    1 
ATOM   7783  H  HA   . PHE   A  1  513 ? 52.062  25.492  -4.192   1.00 129.49 ? 513  PHE   A HA   1 
ATOM   7784  H  HB2  . PHE   A  1  513 ? 49.305  26.000  -4.091   1.00 132.90 ? 513  PHE   A HB2  1 
ATOM   7785  H  HB3  . PHE   A  1  513 ? 50.167  26.464  -5.343   1.00 132.90 ? 513  PHE   A HB3  1 
ATOM   7786  H  HD1  . PHE   A  1  513 ? 51.529  24.549  -6.460   1.00 131.00 ? 513  PHE   A HD1  1 
ATOM   7787  H  HD2  . PHE   A  1  513 ? 48.265  23.930  -4.237   1.00 132.00 ? 513  PHE   A HD2  1 
ATOM   7788  H  HE1  . PHE   A  1  513 ? 51.282  22.464  -7.411   1.00 128.21 ? 513  PHE   A HE1  1 
ATOM   7789  H  HE2  . PHE   A  1  513 ? 48.009  21.846  -5.193   1.00 129.60 ? 513  PHE   A HE2  1 
ATOM   7790  H  HZ   . PHE   A  1  513 ? 49.516  21.110  -6.786   1.00 127.83 ? 513  PHE   A HZ   1 
ATOM   7791  N  N    . LEU   A  1  514 ? 52.561  27.897  -4.416   1.00 112.09 ? 514  LEU   A N    1 
ATOM   7792  C  CA   . LEU   A  1  514 ? 53.126  29.229  -4.234   1.00 118.69 ? 514  LEU   A CA   1 
ATOM   7793  C  C    . LEU   A  1  514 ? 52.037  30.296  -4.261   1.00 126.07 ? 514  LEU   A C    1 
ATOM   7794  O  O    . LEU   A  1  514 ? 51.862  31.051  -3.298   1.00 131.01 ? 514  LEU   A O    1 
ATOM   7795  C  CB   . LEU   A  1  514 ? 54.177  29.501  -5.313   1.00 118.96 ? 514  LEU   A CB   1 
ATOM   7796  C  CG   . LEU   A  1  514 ? 55.060  30.730  -5.080   1.00 121.94 ? 514  LEU   A CG   1 
ATOM   7797  C  CD1  . LEU   A  1  514 ? 55.981  30.515  -3.886   1.00 122.95 ? 514  LEU   A CD1  1 
ATOM   7798  C  CD2  . LEU   A  1  514 ? 55.865  31.060  -6.327   1.00 120.03 ? 514  LEU   A CD2  1 
ATOM   7799  H  H    . LEU   A  1  514 ? 52.827  27.490  -5.125   1.00 134.49 ? 514  LEU   A H    1 
ATOM   7800  H  HA   . LEU   A  1  514 ? 53.563  29.268  -3.369   1.00 142.41 ? 514  LEU   A HA   1 
ATOM   7801  H  HB2  . LEU   A  1  514 ? 54.763  28.730  -5.368   1.00 142.74 ? 514  LEU   A HB2  1 
ATOM   7802  H  HB3  . LEU   A  1  514 ? 53.719  29.630  -6.159   1.00 142.74 ? 514  LEU   A HB3  1 
ATOM   7803  H  HG   . LEU   A  1  514 ? 54.490  31.489  -4.883   1.00 146.31 ? 514  LEU   A HG   1 
ATOM   7804  H  HD11 . LEU   A  1  514 ? 56.561  31.287  -3.791   1.00 147.52 ? 514  LEU   A HD11 1 
ATOM   7805  H  HD12 . LEU   A  1  514 ? 55.443  30.406  -3.087   1.00 147.52 ? 514  LEU   A HD12 1 
ATOM   7806  H  HD13 . LEU   A  1  514 ? 56.514  29.718  -4.037   1.00 147.52 ? 514  LEU   A HD13 1 
ATOM   7807  H  HD21 . LEU   A  1  514 ? 56.428  31.828  -6.145   1.00 144.02 ? 514  LEU   A HD21 1 
ATOM   7808  H  HD22 . LEU   A  1  514 ? 56.414  30.295  -6.560   1.00 144.02 ? 514  LEU   A HD22 1 
ATOM   7809  H  HD23 . LEU   A  1  514 ? 55.254  31.262  -7.053   1.00 144.02 ? 514  LEU   A HD23 1 
ATOM   7810  N  N    . TYR   A  1  515 ? 51.291  30.372  -5.365   1.00 127.32 ? 515  TYR   A N    1 
ATOM   7811  C  CA   . TYR   A  1  515 ? 50.280  31.415  -5.507   1.00 131.01 ? 515  TYR   A CA   1 
ATOM   7812  C  C    . TYR   A  1  515 ? 49.179  31.266  -4.462   1.00 126.48 ? 515  TYR   A C    1 
ATOM   7813  O  O    . TYR   A  1  515 ? 48.890  32.202  -3.707   1.00 127.10 ? 515  TYR   A O    1 
ATOM   7814  C  CB   . TYR   A  1  515 ? 49.693  31.377  -6.920   1.00 136.45 ? 515  TYR   A CB   1 
ATOM   7815  C  CG   . TYR   A  1  515 ? 50.506  32.140  -7.941   1.00 145.35 ? 515  TYR   A CG   1 
ATOM   7816  C  CD1  . TYR   A  1  515 ? 51.664  31.598  -8.484   1.00 144.89 ? 515  TYR   A CD1  1 
ATOM   7817  C  CD2  . TYR   A  1  515 ? 50.114  33.402  -8.363   1.00 154.22 ? 515  TYR   A CD2  1 
ATOM   7818  C  CE1  . TYR   A  1  515 ? 52.408  32.295  -9.417   1.00 149.98 ? 515  TYR   A CE1  1 
ATOM   7819  C  CE2  . TYR   A  1  515 ? 50.851  34.105  -9.296   1.00 159.22 ? 515  TYR   A CE2  1 
ATOM   7820  C  CZ   . TYR   A  1  515 ? 51.997  33.547  -9.819   1.00 157.71 ? 515  TYR   A CZ   1 
ATOM   7821  O  OH   . TYR   A  1  515 ? 52.733  34.246  -10.748  1.00 162.79 ? 515  TYR   A OH   1 
ATOM   7822  H  H    . TYR   A  1  515 ? 51.350  29.838  -6.036   1.00 152.76 ? 515  TYR   A H    1 
ATOM   7823  H  HA   . TYR   A  1  515 ? 50.700  32.279  -5.375   1.00 157.20 ? 515  TYR   A HA   1 
ATOM   7824  H  HB2  . TYR   A  1  515 ? 49.643  30.453  -7.212   1.00 163.72 ? 515  TYR   A HB2  1 
ATOM   7825  H  HB3  . TYR   A  1  515 ? 48.804  31.766  -6.899   1.00 163.72 ? 515  TYR   A HB3  1 
ATOM   7826  H  HD1  . TYR   A  1  515 ? 51.943  30.753  -8.215   1.00 173.84 ? 515  TYR   A HD1  1 
ATOM   7827  H  HD2  . TYR   A  1  515 ? 49.341  33.781  -8.012   1.00 185.05 ? 515  TYR   A HD2  1 
ATOM   7828  H  HE1  . TYR   A  1  515 ? 53.182  31.921  -9.772   1.00 179.95 ? 515  TYR   A HE1  1 
ATOM   7829  H  HE2  . TYR   A  1  515 ? 50.575  34.950  -9.569   1.00 191.05 ? 515  TYR   A HE2  1 
ATOM   7830  H  HH   . TYR   A  1  515 ? 52.395  35.005  -10.870  1.00 195.33 ? 515  TYR   A HH   1 
ATOM   7831  N  N    . SER   A  1  516 ? 48.557  30.088  -4.399   1.00 125.46 ? 516  SER   A N    1 
ATOM   7832  C  CA   . SER   A  1  516 ? 47.367  29.920  -3.572   1.00 129.41 ? 516  SER   A CA   1 
ATOM   7833  C  C    . SER   A  1  516 ? 47.694  29.845  -2.085   1.00 126.57 ? 516  SER   A C    1 
ATOM   7834  O  O    . SER   A  1  516 ? 46.839  30.170  -1.253   1.00 127.92 ? 516  SER   A O    1 
ATOM   7835  C  CB   . SER   A  1  516 ? 46.615  28.658  -3.998   1.00 131.92 ? 516  SER   A CB   1 
ATOM   7836  O  OG   . SER   A  1  516 ? 45.580  28.346  -3.083   1.00 137.22 ? 516  SER   A OG   1 
ATOM   7837  H  H    . SER   A  1  516 ? 48.802  29.379  -4.820   1.00 150.53 ? 516  SER   A H    1 
ATOM   7838  H  HA   . SER   A  1  516 ? 46.794  30.690  -3.708   1.00 155.27 ? 516  SER   A HA   1 
ATOM   7839  H  HB2  . SER   A  1  516 ? 46.227  28.805  -4.875   1.00 158.29 ? 516  SER   A HB2  1 
ATOM   7840  H  HB3  . SER   A  1  516 ? 47.239  27.917  -4.032   1.00 158.29 ? 516  SER   A HB3  1 
ATOM   7841  H  HG   . SER   A  1  516 ? 45.336  27.548  -3.186   1.00 164.64 ? 516  SER   A HG   1 
ATOM   7842  N  N    . ARG   A  1  517 ? 48.906  29.425  -1.729   1.00 122.16 ? 517  ARG   A N    1 
ATOM   7843  C  CA   . ARG   A  1  517 ? 49.260  29.118  -0.344   1.00 118.16 ? 517  ARG   A CA   1 
ATOM   7844  C  C    . ARG   A  1  517 ? 48.361  28.032  0.242    1.00 112.14 ? 517  ARG   A C    1 
ATOM   7845  O  O    . ARG   A  1  517 ? 48.218  27.926  1.465    1.00 111.38 ? 517  ARG   A O    1 
ATOM   7846  C  CB   . ARG   A  1  517 ? 49.223  30.377  0.535    1.00 123.28 ? 517  ARG   A CB   1 
ATOM   7847  C  CG   . ARG   A  1  517 ? 50.580  31.062  0.671    1.00 125.59 ? 517  ARG   A CG   1 
ATOM   7848  C  CD   . ARG   A  1  517 ? 50.525  32.555  0.374    1.00 131.67 ? 517  ARG   A CD   1 
ATOM   7849  N  NE   . ARG   A  1  517 ? 50.218  33.354  1.558    1.00 137.58 ? 517  ARG   A NE   1 
ATOM   7850  C  CZ   . ARG   A  1  517 ? 50.307  34.680  1.607    1.00 144.85 ? 517  ARG   A CZ   1 
ATOM   7851  N  NH1  . ARG   A  1  517 ? 50.010  35.325  2.726    1.00 149.86 ? 517  ARG   A NH1  1 
ATOM   7852  N  NH2  . ARG   A  1  517 ? 50.697  35.363  0.538    1.00 147.52 ? 517  ARG   A NH2  1 
ATOM   7853  H  H    . ARG   A  1  517 ? 49.553  29.308  -2.283   1.00 146.57 ? 517  ARG   A H    1 
ATOM   7854  H  HA   . ARG   A  1  517 ? 50.170  28.782  -0.329   1.00 141.77 ? 517  ARG   A HA   1 
ATOM   7855  H  HB2  . ARG   A  1  517 ? 48.606  31.015  0.143    1.00 147.91 ? 517  ARG   A HB2  1 
ATOM   7856  H  HB3  . ARG   A  1  517 ? 48.924  30.130  1.424    1.00 147.91 ? 517  ARG   A HB3  1 
ATOM   7857  H  HG2  . ARG   A  1  517 ? 50.901  30.949  1.579    1.00 150.69 ? 517  ARG   A HG2  1 
ATOM   7858  H  HG3  . ARG   A  1  517 ? 51.202  30.656  0.047    1.00 150.69 ? 517  ARG   A HG3  1 
ATOM   7859  H  HD2  . ARG   A  1  517 ? 51.387  32.842  0.034    1.00 157.98 ? 517  ARG   A HD2  1 
ATOM   7860  H  HD3  . ARG   A  1  517 ? 49.836  32.721  -0.287   1.00 157.98 ? 517  ARG   A HD3  1 
ATOM   7861  H  HE   . ARG   A  1  517 ? 49.963  32.941  2.267    1.00 165.08 ? 517  ARG   A HE   1 
ATOM   7862  H  HH11 . ARG   A  1  517 ? 49.759  34.887  3.422    1.00 179.81 ? 517  ARG   A HH11 1 
ATOM   7863  H  HH12 . ARG   A  1  517 ? 50.068  36.183  2.757    1.00 179.81 ? 517  ARG   A HH12 1 
ATOM   7864  H  HH21 . ARG   A  1  517 ? 50.893  34.948  -0.189   1.00 177.00 ? 517  ARG   A HH21 1 
ATOM   7865  H  HH22 . ARG   A  1  517 ? 50.753  36.221  0.573    1.00 177.00 ? 517  ARG   A HH22 1 
ATOM   7866  N  N    . SER   A  1  518 ? 47.755  27.217  -0.621   1.00 109.06 ? 518  SER   A N    1 
ATOM   7867  C  CA   . SER   A  1  518 ? 46.942  26.077  -0.235   1.00 108.70 ? 518  SER   A CA   1 
ATOM   7868  C  C    . SER   A  1  518 ? 47.513  24.808  -0.856   1.00 106.79 ? 518  SER   A C    1 
ATOM   7869  O  O    . SER   A  1  518 ? 48.185  24.870  -1.891   1.00 104.41 ? 518  SER   A O    1 
ATOM   7870  C  CB   . SER   A  1  518 ? 45.485  26.252  -0.685   1.00 110.44 ? 518  SER   A CB   1 
ATOM   7871  O  OG   . SER   A  1  518 ? 45.374  26.207  -2.097   1.00 109.32 ? 518  SER   A OG   1 
ATOM   7872  H  H    . SER   A  1  518 ? 47.805  27.312  -1.475   1.00 130.86 ? 518  SER   A H    1 
ATOM   7873  H  HA   . SER   A  1  518 ? 46.944  25.985  0.730    1.00 130.43 ? 518  SER   A HA   1 
ATOM   7874  H  HB2  . SER   A  1  518 ? 44.951  25.538  -0.304   1.00 132.51 ? 518  SER   A HB2  1 
ATOM   7875  H  HB3  . SER   A  1  518 ? 45.161  27.111  -0.372   1.00 132.51 ? 518  SER   A HB3  1 
ATOM   7876  H  HG   . SER   A  1  518 ? 45.519  25.426  -2.371   1.00 131.16 ? 518  SER   A HG   1 
ATOM   7877  N  N    . PRO   A  1  519 ? 47.267  23.641  -0.255   1.00 109.35 ? 519  PRO   A N    1 
ATOM   7878  C  CA   . PRO   A  1  519 ? 47.796  22.394  -0.819   1.00 109.76 ? 519  PRO   A CA   1 
ATOM   7879  C  C    . PRO   A  1  519 ? 47.055  21.906  -2.053   1.00 111.76 ? 519  PRO   A C    1 
ATOM   7880  O  O    . PRO   A  1  519 ? 47.466  20.898  -2.637   1.00 107.50 ? 519  PRO   A O    1 
ATOM   7881  C  CB   . PRO   A  1  519 ? 47.639  21.404  0.343    1.00 107.31 ? 519  PRO   A CB   1 
ATOM   7882  C  CG   . PRO   A  1  519 ? 46.445  21.895  1.077    1.00 108.94 ? 519  PRO   A CG   1 
ATOM   7883  C  CD   . PRO   A  1  519 ? 46.475  23.401  0.966    1.00 111.32 ? 519  PRO   A CD   1 
ATOM   7884  H  HA   . PRO   A  1  519 ? 48.738  22.491  -1.030   1.00 131.69 ? 519  PRO   A HA   1 
ATOM   7885  H  HB2  . PRO   A  1  519 ? 47.495  20.508  0.001    1.00 128.76 ? 519  PRO   A HB2  1 
ATOM   7886  H  HB3  . PRO   A  1  519 ? 48.428  21.422  0.906    1.00 128.76 ? 519  PRO   A HB3  1 
ATOM   7887  H  HG2  . PRO   A  1  519 ? 45.641  21.538  0.669    1.00 130.71 ? 519  PRO   A HG2  1 
ATOM   7888  H  HG3  . PRO   A  1  519 ? 46.497  21.620  2.006    1.00 130.71 ? 519  PRO   A HG3  1 
ATOM   7889  H  HD2  . PRO   A  1  519 ? 45.578  23.757  0.870    1.00 133.56 ? 519  PRO   A HD2  1 
ATOM   7890  H  HD3  . PRO   A  1  519 ? 46.907  23.795  1.740    1.00 133.56 ? 519  PRO   A HD3  1 
ATOM   7891  N  N    . SER   A  1  520 ? 45.988  22.587  -2.466   1.00 115.54 ? 520  SER   A N    1 
ATOM   7892  C  CA   . SER   A  1  520 ? 45.180  22.171  -3.602   1.00 112.94 ? 520  SER   A CA   1 
ATOM   7893  C  C    . SER   A  1  520 ? 45.187  23.247  -4.680   1.00 111.15 ? 520  SER   A C    1 
ATOM   7894  O  O    . SER   A  1  520 ? 45.263  24.445  -4.389   1.00 111.49 ? 520  SER   A O    1 
ATOM   7895  C  CB   . SER   A  1  520 ? 43.735  21.882  -3.177   1.00 117.14 ? 520  SER   A CB   1 
ATOM   7896  O  OG   . SER   A  1  520 ? 43.082  23.067  -2.754   1.00 125.72 ? 520  SER   A OG   1 
ATOM   7897  H  H    . SER   A  1  520 ? 45.708  23.310  -2.094   1.00 138.63 ? 520  SER   A H    1 
ATOM   7898  H  HA   . SER   A  1  520 ? 45.559  21.363  -3.982   1.00 135.51 ? 520  SER   A HA   1 
ATOM   7899  H  HB2  . SER   A  1  520 ? 43.253  21.510  -3.932   1.00 140.55 ? 520  SER   A HB2  1 
ATOM   7900  H  HB3  . SER   A  1  520 ? 43.743  21.248  -2.443   1.00 140.55 ? 520  SER   A HB3  1 
ATOM   7901  H  HG   . SER   A  1  520 ? 42.276  22.906  -2.584   1.00 150.84 ? 520  SER   A HG   1 
ATOM   7902  N  N    . HIS   A  1  521 ? 45.106  22.802  -5.932   1.00 109.13 ? 521  HIS   A N    1 
ATOM   7903  C  CA   . HIS   A  1  521 ? 45.006  23.702  -7.077   1.00 111.95 ? 521  HIS   A CA   1 
ATOM   7904  C  C    . HIS   A  1  521 ? 44.155  23.028  -8.140   1.00 114.21 ? 521  HIS   A C    1 
ATOM   7905  O  O    . HIS   A  1  521 ? 44.510  21.949  -8.624   1.00 111.41 ? 521  HIS   A O    1 
ATOM   7906  C  CB   . HIS   A  1  521 ? 46.387  24.052  -7.636   1.00 106.99 ? 521  HIS   A CB   1 
ATOM   7907  C  CG   . HIS   A  1  521 ? 46.347  24.663  -9.002   1.00 104.54 ? 521  HIS   A CG   1 
ATOM   7908  N  ND1  . HIS   A  1  521 ? 46.530  23.926  -10.152  1.00 101.10 ? 521  HIS   A ND1  1 
ATOM   7909  C  CD2  . HIS   A  1  521 ? 46.141  25.940  -9.404   1.00 107.15 ? 521  HIS   A CD2  1 
ATOM   7910  C  CE1  . HIS   A  1  521 ? 46.441  24.722  -11.203  1.00 102.88 ? 521  HIS   A CE1  1 
ATOM   7911  N  NE2  . HIS   A  1  521 ? 46.205  25.950  -10.776  1.00 106.98 ? 521  HIS   A NE2  1 
ATOM   7912  H  H    . HIS   A  1  521 ? 45.107  21.969  -6.148   1.00 130.94 ? 521  HIS   A H    1 
ATOM   7913  H  HA   . HIS   A  1  521 ? 44.573  24.526  -6.802   1.00 134.33 ? 521  HIS   A HA   1 
ATOM   7914  H  HB2  . HIS   A  1  521 ? 46.814  24.686  -7.039   1.00 128.36 ? 521  HIS   A HB2  1 
ATOM   7915  H  HB3  . HIS   A  1  521 ? 46.916  23.240  -7.690   1.00 128.36 ? 521  HIS   A HB3  1 
ATOM   7916  H  HD2  . HIS   A  1  521 ? 45.985  26.674  -8.853   1.00 128.57 ? 521  HIS   A HD2  1 
ATOM   7917  H  HE1  . HIS   A  1  521 ? 46.529  24.462  -12.091  1.00 123.44 ? 521  HIS   A HE1  1 
ATOM   7918  H  HE2  . HIS   A  1  521 ? 46.108  26.642  -11.276  1.00 128.36 ? 521  HIS   A HE2  1 
ATOM   7919  N  N    . SER   A  1  522 ? 43.043  23.660  -8.500   1.00 117.73 ? 522  SER   A N    1 
ATOM   7920  C  CA   . SER   A  1  522 ? 42.130  23.136  -9.504   1.00 115.72 ? 522  SER   A CA   1 
ATOM   7921  C  C    . SER   A  1  522 ? 42.395  23.798  -10.851  1.00 117.69 ? 522  SER   A C    1 
ATOM   7922  O  O    . SER   A  1  522 ? 43.032  24.851  -10.939  1.00 123.01 ? 522  SER   A O    1 
ATOM   7923  C  CB   . SER   A  1  522 ? 40.677  23.363  -9.080   1.00 118.15 ? 522  SER   A CB   1 
ATOM   7924  O  OG   . SER   A  1  522 ? 39.787  22.589  -9.866   1.00 118.92 ? 522  SER   A OG   1 
ATOM   7925  H  H    . SER   A  1  522 ? 42.791  24.412  -8.167   1.00 141.26 ? 522  SER   A H    1 
ATOM   7926  H  HA   . SER   A  1  522 ? 42.267  22.181  -9.603   1.00 138.85 ? 522  SER   A HA   1 
ATOM   7927  H  HB2  . SER   A  1  522 ? 40.577  23.108  -8.150   1.00 141.76 ? 522  SER   A HB2  1 
ATOM   7928  H  HB3  . SER   A  1  522 ? 40.460  24.301  -9.192   1.00 141.76 ? 522  SER   A HB3  1 
ATOM   7929  H  HG   . SER   A  1  522 ? 39.005  22.661  -9.569   1.00 142.68 ? 522  SER   A HG   1 
ATOM   7930  N  N    . LYS   A  1  523 ? 41.894  23.164  -11.912  1.00 114.03 ? 523  LYS   A N    1 
ATOM   7931  C  CA   . LYS   A  1  523 ? 42.139  23.662  -13.260  1.00 114.71 ? 523  LYS   A CA   1 
ATOM   7932  C  C    . LYS   A  1  523 ? 41.210  23.027  -14.287  1.00 116.25 ? 523  LYS   A C    1 
ATOM   7933  O  O    . LYS   A  1  523 ? 41.068  21.801  -14.334  1.00 112.47 ? 523  LYS   A O    1 
ATOM   7934  C  CB   . LYS   A  1  523 ? 43.599  23.404  -13.652  1.00 109.98 ? 523  LYS   A CB   1 
ATOM   7935  C  CG   . LYS   A  1  523 ? 43.982  23.905  -15.038  1.00 110.23 ? 523  LYS   A CG   1 
ATOM   7936  C  CD   . LYS   A  1  523 ? 44.021  25.423  -15.093  1.00 116.45 ? 523  LYS   A CD   1 
ATOM   7937  C  CE   . LYS   A  1  523 ? 44.260  25.916  -16.509  1.00 120.75 ? 523  LYS   A CE   1 
ATOM   7938  N  NZ   . LYS   A  1  523 ? 44.547  27.376  -16.562  1.00 127.24 ? 523  LYS   A NZ   1 
ATOM   7939  H  H    . LYS   A  1  523 ? 41.414  22.451  -11.875  1.00 136.81 ? 523  LYS   A H    1 
ATOM   7940  H  HA   . LYS   A  1  523 ? 41.967  24.616  -13.266  1.00 137.63 ? 523  LYS   A HA   1 
ATOM   7941  H  HB2  . LYS   A  1  523 ? 44.174  23.850  -13.011  1.00 131.96 ? 523  LYS   A HB2  1 
ATOM   7942  H  HB3  . LYS   A  1  523 ? 43.759  22.448  -13.632  1.00 131.96 ? 523  LYS   A HB3  1 
ATOM   7943  H  HG2  . LYS   A  1  523 ? 44.862  23.570  -15.269  1.00 132.26 ? 523  LYS   A HG2  1 
ATOM   7944  H  HG3  . LYS   A  1  523 ? 43.329  23.594  -15.684  1.00 132.26 ? 523  LYS   A HG3  1 
ATOM   7945  H  HD2  . LYS   A  1  523 ? 43.173  25.779  -14.784  1.00 139.72 ? 523  LYS   A HD2  1 
ATOM   7946  H  HD3  . LYS   A  1  523 ? 44.741  25.748  -14.530  1.00 139.72 ? 523  LYS   A HD3  1 
ATOM   7947  H  HE2  . LYS   A  1  523 ? 45.021  25.446  -16.884  1.00 144.88 ? 523  LYS   A HE2  1 
ATOM   7948  H  HE3  . LYS   A  1  523 ? 43.469  25.745  -17.042  1.00 144.88 ? 523  LYS   A HE3  1 
ATOM   7949  H  HZ1  . LYS   A  1  523 ? 44.708  27.624  -17.401  1.00 152.67 ? 523  LYS   A HZ1  1 
ATOM   7950  H  HZ2  . LYS   A  1  523 ? 43.850  27.834  -16.253  1.00 152.67 ? 523  LYS   A HZ2  1 
ATOM   7951  H  HZ3  . LYS   A  1  523 ? 45.260  27.564  -16.064  1.00 152.67 ? 523  LYS   A HZ3  1 
ATOM   7952  N  N    . ASN   A  1  524 ? 40.574  23.857  -15.111  1.00 120.70 ? 524  ASN   A N    1 
ATOM   7953  C  CA   . ASN   A  1  524 ? 39.875  23.392  -16.299  1.00 120.17 ? 524  ASN   A CA   1 
ATOM   7954  C  C    . ASN   A  1  524 ? 40.849  23.352  -17.472  1.00 121.70 ? 524  ASN   A C    1 
ATOM   7955  O  O    . ASN   A  1  524 ? 41.770  24.167  -17.563  1.00 126.49 ? 524  ASN   A O    1 
ATOM   7956  C  CB   . ASN   A  1  524 ? 38.694  24.306  -16.637  1.00 122.48 ? 524  ASN   A CB   1 
ATOM   7957  C  CG   . ASN   A  1  524 ? 37.629  24.309  -15.559  1.00 121.27 ? 524  ASN   A CG   1 
ATOM   7958  O  OD1  . ASN   A  1  524 ? 37.573  23.409  -14.723  1.00 115.63 ? 524  ASN   A OD1  1 
ATOM   7959  N  ND2  . ASN   A  1  524 ? 36.770  25.322  -15.578  1.00 127.10 ? 524  ASN   A ND2  1 
ATOM   7960  H  H    . ASN   A  1  524 ? 40.535  24.709  -14.999  1.00 144.82 ? 524  ASN   A H    1 
ATOM   7961  H  HA   . ASN   A  1  524 ? 39.520  22.503  -16.146  1.00 144.19 ? 524  ASN   A HA   1 
ATOM   7962  H  HB2  . ASN   A  1  524 ? 39.017  25.214  -16.742  1.00 146.96 ? 524  ASN   A HB2  1 
ATOM   7963  H  HB3  . ASN   A  1  524 ? 38.285  24.001  -17.462  1.00 146.96 ? 524  ASN   A HB3  1 
ATOM   7964  H  HD21 . ASN   A  1  524 ? 36.147  25.369  -14.987  1.00 152.50 ? 524  ASN   A HD21 1 
ATOM   7965  H  HD22 . ASN   A  1  524 ? 36.837  25.931  -16.182  1.00 152.50 ? 524  ASN   A HD22 1 
ATOM   7966  N  N    . MET   A  1  525 ? 40.642  22.391  -18.372  1.00 118.71 ? 525  MET   A N    1 
ATOM   7967  C  CA   . MET   A  1  525 ? 41.521  22.214  -19.519  1.00 117.90 ? 525  MET   A CA   1 
ATOM   7968  C  C    . MET   A  1  525 ? 40.686  21.944  -20.764  1.00 121.81 ? 525  MET   A C    1 
ATOM   7969  O  O    . MET   A  1  525 ? 39.459  21.820  -20.704  1.00 127.52 ? 525  MET   A O    1 
ATOM   7970  C  CB   . MET   A  1  525 ? 42.525  21.078  -19.284  1.00 111.18 ? 525  MET   A CB   1 
ATOM   7971  C  CG   . MET   A  1  525 ? 43.639  21.421  -18.311  1.00 109.72 ? 525  MET   A CG   1 
ATOM   7972  S  SD   . MET   A  1  525 ? 44.948  20.179  -18.279  1.00 105.22 ? 525  MET   A SD   1 
ATOM   7973  C  CE   . MET   A  1  525 ? 45.594  20.307  -19.947  1.00 105.40 ? 525  MET   A CE   1 
ATOM   7974  H  H    . MET   A  1  525 ? 39.994  21.826  -18.336  1.00 142.43 ? 525  MET   A H    1 
ATOM   7975  H  HA   . MET   A  1  525 ? 42.014  23.040  -19.645  1.00 141.46 ? 525  MET   A HA   1 
ATOM   7976  H  HB2  . MET   A  1  525 ? 42.048  20.312  -18.926  1.00 133.39 ? 525  MET   A HB2  1 
ATOM   7977  H  HB3  . MET   A  1  525 ? 42.935  20.846  -20.132  1.00 133.39 ? 525  MET   A HB3  1 
ATOM   7978  H  HG2  . MET   A  1  525 ? 44.036  22.268  -18.571  1.00 131.65 ? 525  MET   A HG2  1 
ATOM   7979  H  HG3  . MET   A  1  525 ? 43.269  21.489  -17.417  1.00 131.65 ? 525  MET   A HG3  1 
ATOM   7980  H  HE1  . MET   A  1  525 ? 46.375  19.736  -20.028  1.00 126.47 ? 525  MET   A HE1  1 
ATOM   7981  H  HE2  . MET   A  1  525 ? 44.911  20.023  -20.573  1.00 126.47 ? 525  MET   A HE2  1 
ATOM   7982  H  HE3  . MET   A  1  525 ? 45.840  21.229  -20.121  1.00 126.47 ? 525  MET   A HE3  1 
ATOM   7983  N  N    . THR   A  1  526 ? 41.371  21.851  -21.903  1.00 118.48 ? 526  THR   A N    1 
ATOM   7984  C  CA   . THR   A  1  526 ? 40.723  21.602  -23.187  1.00 116.62 ? 526  THR   A CA   1 
ATOM   7985  C  C    . THR   A  1  526 ? 41.736  20.946  -24.114  1.00 117.25 ? 526  THR   A C    1 
ATOM   7986  O  O    . THR   A  1  526 ? 42.783  21.534  -24.400  1.00 120.93 ? 526  THR   A O    1 
ATOM   7987  C  CB   . THR   A  1  526 ? 40.195  22.902  -23.799  1.00 117.60 ? 526  THR   A CB   1 
ATOM   7988  O  OG1  . THR   A  1  526 ? 39.338  23.561  -22.859  1.00 115.93 ? 526  THR   A OG1  1 
ATOM   7989  C  CG2  . THR   A  1  526 ? 39.420  22.619  -25.081  1.00 119.17 ? 526  THR   A CG2  1 
ATOM   7990  H  H    . THR   A  1  526 ? 42.226  21.930  -21.959  1.00 142.16 ? 526  THR   A H    1 
ATOM   7991  H  HA   . THR   A  1  526 ? 39.976  20.996  -23.063  1.00 139.92 ? 526  THR   A HA   1 
ATOM   7992  H  HB   . THR   A  1  526 ? 40.942  23.481  -24.019  1.00 141.10 ? 526  THR   A HB   1 
ATOM   7993  H  HG1  . THR   A  1  526 ? 38.841  23.000  -22.481  1.00 139.09 ? 526  THR   A HG1  1 
ATOM   7994  H  HG21 . THR   A  1  526 ? 39.063  23.446  -25.441  1.00 142.99 ? 526  THR   A HG21 1 
ATOM   7995  H  HG22 . THR   A  1  526 ? 40.006  22.216  -25.740  1.00 142.99 ? 526  THR   A HG22 1 
ATOM   7996  H  HG23 . THR   A  1  526 ? 38.686  22.012  -24.897  1.00 142.99 ? 526  THR   A HG23 1 
ATOM   7997  N  N    . ILE   A  1  527 ? 41.423  19.734  -24.580  1.00 114.83 ? 527  ILE   A N    1 
ATOM   7998  C  CA   . ILE   A  1  527 ? 42.311  18.961  -25.441  1.00 115.40 ? 527  ILE   A CA   1 
ATOM   7999  C  C    . ILE   A  1  527 ? 41.485  18.321  -26.548  1.00 110.36 ? 527  ILE   A C    1 
ATOM   8000  O  O    . ILE   A  1  527 ? 40.281  18.095  -26.405  1.00 109.29 ? 527  ILE   A O    1 
ATOM   8001  C  CB   . ILE   A  1  527 ? 43.087  17.882  -24.648  1.00 120.64 ? 527  ILE   A CB   1 
ATOM   8002  C  CG1  . ILE   A  1  527 ? 44.003  18.556  -23.623  1.00 122.74 ? 527  ILE   A CG1  1 
ATOM   8003  C  CG2  . ILE   A  1  527 ? 43.892  16.978  -25.587  1.00 124.43 ? 527  ILE   A CG2  1 
ATOM   8004  C  CD1  . ILE   A  1  527 ? 44.766  17.599  -22.745  1.00 119.55 ? 527  ILE   A CD1  1 
ATOM   8005  H  H    . ILE   A  1  527 ? 40.683  19.332  -24.406  1.00 137.78 ? 527  ILE   A H    1 
ATOM   8006  H  HA   . ILE   A  1  527 ? 42.957  19.553  -25.857  1.00 138.47 ? 527  ILE   A HA   1 
ATOM   8007  H  HB   . ILE   A  1  527 ? 42.447  17.323  -24.181  1.00 144.75 ? 527  ILE   A HB   1 
ATOM   8008  H  HG12 . ILE   A  1  527 ? 44.652  19.099  -24.097  1.00 147.26 ? 527  ILE   A HG12 1 
ATOM   8009  H  HG13 . ILE   A  1  527 ? 43.461  19.116  -23.045  1.00 147.26 ? 527  ILE   A HG13 1 
ATOM   8010  H  HG21 . ILE   A  1  527 ? 44.432  16.372  -25.056  1.00 149.29 ? 527  ILE   A HG21 1 
ATOM   8011  H  HG22 . ILE   A  1  527 ? 43.277  16.473  -26.143  1.00 149.29 ? 527  ILE   A HG22 1 
ATOM   8012  H  HG23 . ILE   A  1  527 ? 44.464  17.530  -26.143  1.00 149.29 ? 527  ILE   A HG23 1 
ATOM   8013  H  HD11 . ILE   A  1  527 ? 45.251  18.104  -22.073  1.00 143.44 ? 527  ILE   A HD11 1 
ATOM   8014  H  HD12 . ILE   A  1  527 ? 44.139  16.995  -22.316  1.00 143.44 ? 527  ILE   A HD12 1 
ATOM   8015  H  HD13 . ILE   A  1  527 ? 45.388  17.095  -23.293  1.00 143.44 ? 527  ILE   A HD13 1 
ATOM   8016  N  N    . SER   A  1  528 ? 42.149  18.033  -27.666  1.00 110.40 ? 528  SER   A N    1 
ATOM   8017  C  CA   . SER   A  1  528 ? 41.504  17.434  -28.823  1.00 117.19 ? 528  SER   A CA   1 
ATOM   8018  C  C    . SER   A  1  528 ? 42.061  16.042  -29.099  1.00 117.07 ? 528  SER   A C    1 
ATOM   8019  O  O    . SER   A  1  528 ? 43.195  15.714  -28.739  1.00 114.76 ? 528  SER   A O    1 
ATOM   8020  C  CB   . SER   A  1  528 ? 41.667  18.318  -30.067  1.00 127.87 ? 528  SER   A CB   1 
ATOM   8021  O  OG   . SER   A  1  528 ? 43.029  18.620  -30.313  1.00 132.35 ? 528  SER   A OG   1 
ATOM   8022  H  H    . SER   A  1  528 ? 42.990  18.179  -27.776  1.00 132.45 ? 528  SER   A H    1 
ATOM   8023  H  HA   . SER   A  1  528 ? 40.558  17.335  -28.635  1.00 140.61 ? 528  SER   A HA   1 
ATOM   8024  H  HB2  . SER   A  1  528 ? 41.307  17.849  -30.835  1.00 153.42 ? 528  SER   A HB2  1 
ATOM   8025  H  HB3  . SER   A  1  528 ? 41.183  19.147  -29.928  1.00 153.42 ? 528  SER   A HB3  1 
ATOM   8026  H  HG   . SER   A  1  528 ? 43.098  19.100  -30.999  1.00 158.80 ? 528  SER   A HG   1 
ATOM   8027  N  N    . ARG   A  1  529 ? 41.235  15.226  -29.755  1.00 122.21 ? 529  ARG   A N    1 
ATOM   8028  C  CA   . ARG   A  1  529 ? 41.603  13.846  -30.041  1.00 124.53 ? 529  ARG   A CA   1 
ATOM   8029  C  C    . ARG   A  1  529 ? 42.881  13.788  -30.867  1.00 131.80 ? 529  ARG   A C    1 
ATOM   8030  O  O    . ARG   A  1  529 ? 43.093  14.594  -31.776  1.00 136.47 ? 529  ARG   A O    1 
ATOM   8031  C  CB   . ARG   A  1  529 ? 40.473  13.138  -30.792  1.00 123.31 ? 529  ARG   A CB   1 
ATOM   8032  C  CG   . ARG   A  1  529 ? 39.158  13.070  -30.035  1.00 120.11 ? 529  ARG   A CG   1 
ATOM   8033  C  CD   . ARG   A  1  529 ? 38.093  12.321  -30.829  1.00 121.86 ? 529  ARG   A CD   1 
ATOM   8034  N  NE   . ARG   A  1  529 ? 37.832  12.938  -32.129  1.00 128.14 ? 529  ARG   A NE   1 
ATOM   8035  C  CZ   . ARG   A  1  529 ? 38.313  12.503  -33.293  1.00 132.01 ? 529  ARG   A CZ   1 
ATOM   8036  N  NH1  . ARG   A  1  529 ? 39.091  11.429  -33.353  1.00 130.68 ? 529  ARG   A NH1  1 
ATOM   8037  N  NH2  . ARG   A  1  529 ? 38.007  13.148  -34.410  1.00 136.66 ? 529  ARG   A NH2  1 
ATOM   8038  H  H    . ARG   A  1  529 ? 40.456  15.450  -30.044  1.00 146.63 ? 529  ARG   A H    1 
ATOM   8039  H  HA   . ARG   A  1  529 ? 41.755  13.381  -29.204  1.00 149.42 ? 529  ARG   A HA   1 
ATOM   8040  H  HB2  . ARG   A  1  529 ? 40.309  13.612  -31.622  1.00 147.95 ? 529  ARG   A HB2  1 
ATOM   8041  H  HB3  . ARG   A  1  529 ? 40.750  12.227  -30.979  1.00 147.95 ? 529  ARG   A HB3  1 
ATOM   8042  H  HG2  . ARG   A  1  529 ? 39.294  12.606  -29.195  1.00 144.12 ? 529  ARG   A HG2  1 
ATOM   8043  H  HG3  . ARG   A  1  529 ? 38.836  13.970  -29.869  1.00 144.12 ? 529  ARG   A HG3  1 
ATOM   8044  H  HD2  . ARG   A  1  529 ? 38.392  11.411  -30.982  1.00 146.21 ? 529  ARG   A HD2  1 
ATOM   8045  H  HD3  . ARG   A  1  529 ? 37.264  12.318  -30.325  1.00 146.21 ? 529  ARG   A HD3  1 
ATOM   8046  H  HE   . ARG   A  1  529 ? 37.329  13.636  -32.143  1.00 153.75 ? 529  ARG   A HE   1 
ATOM   8047  H  HH11 . ARG   A  1  529 ? 39.292  11.002  -32.634  1.00 156.79 ? 529  ARG   A HH11 1 
ATOM   8048  H  HH12 . ARG   A  1  529 ? 39.394  11.159  -34.112  1.00 156.79 ? 529  ARG   A HH12 1 
ATOM   8049  H  HH21 . ARG   A  1  529 ? 37.501  13.843  -34.380  1.00 163.98 ? 529  ARG   A HH21 1 
ATOM   8050  H  HH22 . ARG   A  1  529 ? 38.314  12.872  -35.164  1.00 163.98 ? 529  ARG   A HH22 1 
ATOM   8051  N  N    . GLY   A  1  530 ? 43.737  12.821  -30.541  1.00 132.10 ? 530  GLY   A N    1 
ATOM   8052  C  CA   . GLY   A  1  530 ? 44.986  12.637  -31.254  1.00 133.42 ? 530  GLY   A CA   1 
ATOM   8053  C  C    . GLY   A  1  530 ? 45.939  13.806  -31.118  1.00 134.08 ? 530  GLY   A C    1 
ATOM   8054  O  O    . GLY   A  1  530 ? 47.003  13.822  -31.745  1.00 136.05 ? 530  GLY   A O    1 
ATOM   8055  H  H    . GLY   A  1  530 ? 43.611  12.256  -29.905  1.00 158.51 ? 530  GLY   A H    1 
ATOM   8056  H  HA2  . GLY   A  1  530 ? 45.430  11.845  -30.913  1.00 160.08 ? 530  GLY   A HA2  1 
ATOM   8057  H  HA3  . GLY   A  1  530 ? 44.796  12.511  -32.197  1.00 160.08 ? 530  GLY   A HA3  1 
ATOM   8058  N  N    . GLY   A  1  531 ? 45.575  14.788  -30.300  1.00 131.71 ? 531  GLY   A N    1 
ATOM   8059  C  CA   . GLY   A  1  531 ? 46.384  15.974  -30.135  1.00 129.80 ? 531  GLY   A CA   1 
ATOM   8060  C  C    . GLY   A  1  531 ? 47.657  15.691  -29.361  1.00 124.34 ? 531  GLY   A C    1 
ATOM   8061  O  O    . GLY   A  1  531 ? 47.914  14.587  -28.883  1.00 121.81 ? 531  GLY   A O    1 
ATOM   8062  H  H    . GLY   A  1  531 ? 44.856  14.785  -29.828  1.00 158.03 ? 531  GLY   A H    1 
ATOM   8063  H  HA2  . GLY   A  1  531 ? 46.626  16.323  -31.007  1.00 155.74 ? 531  GLY   A HA2  1 
ATOM   8064  H  HA3  . GLY   A  1  531 ? 45.875  16.647  -29.656  1.00 155.74 ? 531  GLY   A HA3  1 
ATOM   8065  N  N    . LEU   A  1  532 ? 48.471  16.734  -29.234  1.00 123.99 ? 532  LEU   A N    1 
ATOM   8066  C  CA   . LEU   A  1  532 ? 49.754  16.609  -28.564  1.00 122.33 ? 532  LEU   A CA   1 
ATOM   8067  C  C    . LEU   A  1  532 ? 49.569  16.631  -27.048  1.00 121.27 ? 532  LEU   A C    1 
ATOM   8068  O  O    . LEU   A  1  532 ? 48.476  16.874  -26.527  1.00 121.45 ? 532  LEU   A O    1 
ATOM   8069  C  CB   . LEU   A  1  532 ? 50.695  17.731  -29.000  1.00 122.86 ? 532  LEU   A CB   1 
ATOM   8070  C  CG   . LEU   A  1  532 ? 50.640  18.124  -30.479  1.00 126.73 ? 532  LEU   A CG   1 
ATOM   8071  C  CD1  . LEU   A  1  532 ? 51.657  19.218  -30.772  1.00 129.22 ? 532  LEU   A CD1  1 
ATOM   8072  C  CD2  . LEU   A  1  532 ? 50.864  16.923  -31.385  1.00 127.60 ? 532  LEU   A CD2  1 
ATOM   8073  H  H    . LEU   A  1  532 ? 48.302  17.524  -29.528  1.00 148.77 ? 532  LEU   A H    1 
ATOM   8074  H  HA   . LEU   A  1  532 ? 50.160  15.762  -28.809  1.00 146.77 ? 532  LEU   A HA   1 
ATOM   8075  H  HB2  . LEU   A  1  532 ? 50.477  18.524  -28.485  1.00 147.41 ? 532  LEU   A HB2  1 
ATOM   8076  H  HB3  . LEU   A  1  532 ? 51.604  17.452  -28.812  1.00 147.41 ? 532  LEU   A HB3  1 
ATOM   8077  H  HG   . LEU   A  1  532 ? 49.754  18.468  -30.674  1.00 152.06 ? 532  LEU   A HG   1 
ATOM   8078  H  HD11 . LEU   A  1  532 ? 51.586  19.474  -31.705  1.00 155.04 ? 532  LEU   A HD11 1 
ATOM   8079  H  HD12 . LEU   A  1  532 ? 51.472  19.983  -30.204  1.00 155.04 ? 532  LEU   A HD12 1 
ATOM   8080  H  HD13 . LEU   A  1  532 ? 52.548  18.879  -30.590  1.00 155.04 ? 532  LEU   A HD13 1 
ATOM   8081  H  HD21 . LEU   A  1  532 ? 50.822  17.212  -32.310  1.00 153.10 ? 532  LEU   A HD21 1 
ATOM   8082  H  HD22 . LEU   A  1  532 ? 51.737  16.543  -31.197  1.00 153.10 ? 532  LEU   A HD22 1 
ATOM   8083  H  HD23 . LEU   A  1  532 ? 50.173  16.264  -31.213  1.00 153.10 ? 532  LEU   A HD23 1 
ATOM   8084  N  N    . MET   A  1  533 ? 50.662  16.372  -26.335  1.00 120.01 ? 533  MET   A N    1 
ATOM   8085  C  CA   . MET   A  1  533 ? 50.650  16.364  -24.874  1.00 117.90 ? 533  MET   A CA   1 
ATOM   8086  C  C    . MET   A  1  533 ? 50.535  17.798  -24.377  1.00 120.77 ? 533  MET   A C    1 
ATOM   8087  O  O    . MET   A  1  533 ? 51.513  18.550  -24.373  1.00 127.46 ? 533  MET   A O    1 
ATOM   8088  C  CB   . MET   A  1  533 ? 51.911  15.698  -24.336  1.00 116.26 ? 533  MET   A CB   1 
ATOM   8089  C  CG   . MET   A  1  533 ? 51.792  15.241  -22.894  1.00 113.41 ? 533  MET   A CG   1 
ATOM   8090  S  SD   . MET   A  1  533 ? 51.194  13.543  -22.774  1.00 110.86 ? 533  MET   A SD   1 
ATOM   8091  C  CE   . MET   A  1  533 ? 50.338  13.587  -21.202  1.00 108.06 ? 533  MET   A CE   1 
ATOM   8092  H  H    . MET   A  1  533 ? 51.431  16.196  -26.678  1.00 143.99 ? 533  MET   A H    1 
ATOM   8093  H  HA   . MET   A  1  533 ? 49.885  15.853  -24.567  1.00 141.45 ? 533  MET   A HA   1 
ATOM   8094  H  HB2  . MET   A  1  533 ? 52.108  14.919  -24.879  1.00 139.49 ? 533  MET   A HB2  1 
ATOM   8095  H  HB3  . MET   A  1  533 ? 52.644  16.332  -24.387  1.00 139.49 ? 533  MET   A HB3  1 
ATOM   8096  H  HG2  . MET   A  1  533 ? 52.664  15.286  -22.472  1.00 136.07 ? 533  MET   A HG2  1 
ATOM   8097  H  HG3  . MET   A  1  533 ? 51.167  15.817  -22.427  1.00 136.07 ? 533  MET   A HG3  1 
ATOM   8098  H  HE1  . MET   A  1  533 ? 50.091  12.683  -20.953  1.00 129.66 ? 533  MET   A HE1  1 
ATOM   8099  H  HE2  . MET   A  1  533 ? 50.928  13.965  -20.532  1.00 129.66 ? 533  MET   A HE2  1 
ATOM   8100  H  HE3  . MET   A  1  533 ? 49.543  14.135  -21.291  1.00 129.66 ? 533  MET   A HE3  1 
ATOM   8101  N  N    . GLN   A  1  534 ? 49.336  18.188  -23.954  1.00 115.39 ? 534  GLN   A N    1 
ATOM   8102  C  CA   . GLN   A  1  534 ? 49.095  19.531  -23.443  1.00 111.99 ? 534  GLN   A CA   1 
ATOM   8103  C  C    . GLN   A  1  534 ? 49.451  19.580  -21.960  1.00 108.98 ? 534  GLN   A C    1 
ATOM   8104  O  O    . GLN   A  1  534 ? 48.829  18.892  -21.144  1.00 104.71 ? 534  GLN   A O    1 
ATOM   8105  C  CB   . GLN   A  1  534 ? 47.639  19.929  -23.671  1.00 110.67 ? 534  GLN   A CB   1 
ATOM   8106  C  CG   . GLN   A  1  534 ? 47.313  21.355  -23.258  1.00 112.94 ? 534  GLN   A CG   1 
ATOM   8107  C  CD   . GLN   A  1  534 ? 45.883  21.750  -23.585  1.00 114.09 ? 534  GLN   A CD   1 
ATOM   8108  O  OE1  . GLN   A  1  534 ? 45.189  22.343  -22.760  1.00 113.70 ? 534  GLN   A OE1  1 
ATOM   8109  N  NE2  . GLN   A  1  534 ? 45.439  21.429  -24.796  1.00 115.65 ? 534  GLN   A NE2  1 
ATOM   8110  H  H    . GLN   A  1  534 ? 48.638  17.685  -23.953  1.00 138.44 ? 534  GLN   A H    1 
ATOM   8111  H  HA   . GLN   A  1  534 ? 49.662  20.166  -23.908  1.00 134.37 ? 534  GLN   A HA   1 
ATOM   8112  H  HB2  . GLN   A  1  534 ? 47.438  19.843  -24.616  1.00 132.78 ? 534  GLN   A HB2  1 
ATOM   8113  H  HB3  . GLN   A  1  534 ? 47.071  19.336  -23.155  1.00 132.78 ? 534  GLN   A HB3  1 
ATOM   8114  H  HG2  . GLN   A  1  534 ? 47.437  21.442  -22.300  1.00 135.51 ? 534  GLN   A HG2  1 
ATOM   8115  H  HG3  . GLN   A  1  534 ? 47.907  21.963  -23.726  1.00 135.51 ? 534  GLN   A HG3  1 
ATOM   8116  H  HE21 . GLN   A  1  534 ? 45.955  21.019  -25.348  1.00 138.76 ? 534  GLN   A HE21 1 
ATOM   8117  H  HE22 . GLN   A  1  534 ? 44.636  21.632  -25.027  1.00 138.76 ? 534  GLN   A HE22 1 
ATOM   8118  N  N    . CYS   A  1  535 ? 50.443  20.396  -21.615  1.00 111.97 ? 535  CYS   A N    1 
ATOM   8119  C  CA   . CYS   A  1  535 ? 50.993  20.456  -20.268  1.00 111.69 ? 535  CYS   A CA   1 
ATOM   8120  C  C    . CYS   A  1  535 ? 50.716  21.811  -19.627  1.00 109.87 ? 535  CYS   A C    1 
ATOM   8121  O  O    . CYS   A  1  535 ? 50.206  22.740  -20.259  1.00 110.39 ? 535  CYS   A O    1 
ATOM   8122  C  CB   . CYS   A  1  535 ? 52.503  20.193  -20.293  1.00 118.20 ? 535  CYS   A CB   1 
ATOM   8123  S  SG   . CYS   A  1  535 ? 52.987  18.531  -20.803  1.00 121.40 ? 535  CYS   A SG   1 
ATOM   8124  H  H    . CYS   A  1  535 ? 50.823  20.940  -22.161  1.00 134.34 ? 535  CYS   A H    1 
ATOM   8125  H  HA   . CYS   A  1  535 ? 50.561  19.775  -19.728  1.00 134.00 ? 535  CYS   A HA   1 
ATOM   8126  H  HB2  . CYS   A  1  535 ? 52.912  20.817  -20.912  1.00 141.82 ? 535  CYS   A HB2  1 
ATOM   8127  H  HB3  . CYS   A  1  535 ? 52.853  20.335  -19.399  1.00 141.82 ? 535  CYS   A HB3  1 
ATOM   8128  N  N    . GLU   A  1  536 ? 51.068  21.910  -18.345  1.00 107.94 ? 536  GLU   A N    1 
ATOM   8129  C  CA   . GLU   A  1  536 ? 50.970  23.166  -17.611  1.00 111.79 ? 536  GLU   A CA   1 
ATOM   8130  C  C    . GLU   A  1  536 ? 51.817  23.067  -16.352  1.00 109.83 ? 536  GLU   A C    1 
ATOM   8131  O  O    . GLU   A  1  536 ? 51.757  22.058  -15.642  1.00 105.55 ? 536  GLU   A O    1 
ATOM   8132  C  CB   . GLU   A  1  536 ? 49.518  23.491  -17.254  1.00 114.63 ? 536  GLU   A CB   1 
ATOM   8133  C  CG   . GLU   A  1  536 ? 49.005  24.747  -17.931  1.00 124.05 ? 536  GLU   A CG   1 
ATOM   8134  C  CD   . GLU   A  1  536 ? 47.627  25.146  -17.460  1.00 129.13 ? 536  GLU   A CD   1 
ATOM   8135  O  OE1  . GLU   A  1  536 ? 46.849  25.664  -18.288  1.00 133.14 ? 536  GLU   A OE1  1 
ATOM   8136  O  OE2  . GLU   A  1  536 ? 47.321  24.940  -16.266  1.00 128.84 ? 536  GLU   A OE2  1 
ATOM   8137  H  H    . GLU   A  1  536 ? 51.370  21.257  -17.875  1.00 129.51 ? 536  GLU   A H    1 
ATOM   8138  H  HA   . GLU   A  1  536 ? 51.317  23.886  -18.161  1.00 134.13 ? 536  GLU   A HA   1 
ATOM   8139  H  HB2  . GLU   A  1  536 ? 48.953  22.751  -17.529  1.00 137.54 ? 536  GLU   A HB2  1 
ATOM   8140  H  HB3  . GLU   A  1  536 ? 49.451  23.620  -16.295  1.00 137.54 ? 536  GLU   A HB3  1 
ATOM   8141  H  HG2  . GLU   A  1  536 ? 49.611  25.479  -17.738  1.00 148.84 ? 536  GLU   A HG2  1 
ATOM   8142  H  HG3  . GLU   A  1  536 ? 48.963  24.595  -18.888  1.00 148.84 ? 536  GLU   A HG3  1 
ATOM   8143  N  N    . GLU   A  1  537 ? 52.592  24.114  -16.078  1.00 111.98 ? 537  GLU   A N    1 
ATOM   8144  C  CA   . GLU   A  1  537 ? 53.503  24.154  -14.944  1.00 108.32 ? 537  GLU   A CA   1 
ATOM   8145  C  C    . GLU   A  1  537 ? 52.996  25.114  -13.875  1.00 109.55 ? 537  GLU   A C    1 
ATOM   8146  O  O    . GLU   A  1  537 ? 52.271  26.070  -14.162  1.00 111.40 ? 537  GLU   A O    1 
ATOM   8147  C  CB   . GLU   A  1  537 ? 54.906  24.598  -15.374  1.00 109.67 ? 537  GLU   A CB   1 
ATOM   8148  C  CG   . GLU   A  1  537 ? 55.585  23.700  -16.390  1.00 111.53 ? 537  GLU   A CG   1 
ATOM   8149  C  CD   . GLU   A  1  537 ? 57.022  24.115  -16.652  1.00 121.27 ? 537  GLU   A CD   1 
ATOM   8150  O  OE1  . GLU   A  1  537 ? 57.719  24.487  -15.684  1.00 124.51 ? 537  GLU   A OE1  1 
ATOM   8151  O  OE2  . GLU   A  1  537 ? 57.453  24.077  -17.824  1.00 125.97 ? 537  GLU   A OE2  1 
ATOM   8152  H  H    . GLU   A  1  537 ? 52.607  24.832  -16.550  1.00 134.35 ? 537  GLU   A H    1 
ATOM   8153  H  HA   . GLU   A  1  537 ? 53.554  23.264  -14.562  1.00 129.97 ? 537  GLU   A HA   1 
ATOM   8154  H  HB2  . GLU   A  1  537 ? 54.841  25.482  -15.767  1.00 131.58 ? 537  GLU   A HB2  1 
ATOM   8155  H  HB3  . GLU   A  1  537 ? 55.473  24.626  -14.587  1.00 131.58 ? 537  GLU   A HB3  1 
ATOM   8156  H  HG2  . GLU   A  1  537 ? 55.589  22.789  -16.057  1.00 133.81 ? 537  GLU   A HG2  1 
ATOM   8157  H  HG3  . GLU   A  1  537 ? 55.100  23.744  -17.229  1.00 133.81 ? 537  GLU   A HG3  1 
ATOM   8158  N  N    . LEU   A  1  538 ? 53.395  24.845  -12.634  1.00 108.82 ? 538  LEU   A N    1 
ATOM   8159  C  CA   . LEU   A  1  538 ? 53.223  25.788  -11.537  1.00 111.13 ? 538  LEU   A CA   1 
ATOM   8160  C  C    . LEU   A  1  538 ? 54.261  25.444  -10.477  1.00 113.28 ? 538  LEU   A C    1 
ATOM   8161  O  O    . LEU   A  1  538 ? 54.976  24.445  -10.586  1.00 114.04 ? 538  LEU   A O    1 
ATOM   8162  C  CB   . LEU   A  1  538 ? 51.798  25.757  -10.975  1.00 107.56 ? 538  LEU   A CB   1 
ATOM   8163  C  CG   . LEU   A  1  538 ? 51.423  24.701  -9.935   1.00 104.00 ? 538  LEU   A CG   1 
ATOM   8164  C  CD1  . LEU   A  1  538 ? 50.020  24.989  -9.412   1.00 101.43 ? 538  LEU   A CD1  1 
ATOM   8165  C  CD2  . LEU   A  1  538 ? 51.504  23.299  -10.509  1.00 102.76 ? 538  LEU   A CD2  1 
ATOM   8166  H  H    . LEU   A  1  538 ? 53.774  24.110  -12.400  1.00 130.57 ? 538  LEU   A H    1 
ATOM   8167  H  HA   . LEU   A  1  538 ? 53.385  26.692  -11.847  1.00 133.34 ? 538  LEU   A HA   1 
ATOM   8168  H  HB2  . LEU   A  1  538 ? 51.632  26.618  -10.561  1.00 129.06 ? 538  LEU   A HB2  1 
ATOM   8169  H  HB3  . LEU   A  1  538 ? 51.195  25.628  -11.724  1.00 129.06 ? 538  LEU   A HB3  1 
ATOM   8170  H  HG   . LEU   A  1  538 ? 52.053  24.740  -9.199   1.00 124.77 ? 538  LEU   A HG   1 
ATOM   8171  H  HD11 . LEU   A  1  538 ? 49.767  24.292  -8.787   1.00 121.69 ? 538  LEU   A HD11 1 
ATOM   8172  H  HD12 . LEU   A  1  538 ? 50.020  25.850  -8.964   1.00 121.69 ? 538  LEU   A HD12 1 
ATOM   8173  H  HD13 . LEU   A  1  538 ? 49.401  25.005  -10.159  1.00 121.69 ? 538  LEU   A HD13 1 
ATOM   8174  H  HD21 . LEU   A  1  538 ? 51.298  22.660  -9.810   1.00 123.30 ? 538  LEU   A HD21 1 
ATOM   8175  H  HD22 . LEU   A  1  538 ? 50.863  23.217  -11.233  1.00 123.30 ? 538  LEU   A HD22 1 
ATOM   8176  H  HD23 . LEU   A  1  538 ? 52.402  23.146  -10.843  1.00 123.30 ? 538  LEU   A HD23 1 
ATOM   8177  N  N    . ILE   A  1  539 ? 54.342  26.286  -9.450   1.00 112.59 ? 539  ILE   A N    1 
ATOM   8178  C  CA   . ILE   A  1  539 ? 55.387  26.187  -8.439   1.00 107.86 ? 539  ILE   A CA   1 
ATOM   8179  C  C    . ILE   A  1  539 ? 54.748  25.987  -7.073   1.00 105.19 ? 539  ILE   A C    1 
ATOM   8180  O  O    . ILE   A  1  539 ? 53.709  26.582  -6.766   1.00 104.46 ? 539  ILE   A O    1 
ATOM   8181  C  CB   . ILE   A  1  539 ? 56.297  27.434  -8.443   1.00 110.72 ? 539  ILE   A CB   1 
ATOM   8182  C  CG1  . ILE   A  1  539 ? 56.650  27.808  -9.887   1.00 111.42 ? 539  ILE   A CG1  1 
ATOM   8183  C  CG2  . ILE   A  1  539 ? 57.548  27.173  -7.611   1.00 109.80 ? 539  ILE   A CG2  1 
ATOM   8184  C  CD1  . ILE   A  1  539 ? 57.752  28.840  -10.026  1.00 113.69 ? 539  ILE   A CD1  1 
ATOM   8185  H  H    . ILE   A  1  539 ? 53.793  26.934  -9.317   1.00 135.09 ? 539  ILE   A H    1 
ATOM   8186  H  HA   . ILE   A  1  539 ? 55.932  25.407  -8.626   1.00 129.41 ? 539  ILE   A HA   1 
ATOM   8187  H  HB   . ILE   A  1  539 ? 55.824  28.181  -8.043   1.00 132.84 ? 539  ILE   A HB   1 
ATOM   8188  H  HG12 . ILE   A  1  539 ? 56.941  27.007  -10.350  1.00 133.69 ? 539  ILE   A HG12 1 
ATOM   8189  H  HG13 . ILE   A  1  539 ? 55.858  28.169  -10.314  1.00 133.69 ? 539  ILE   A HG13 1 
ATOM   8190  H  HG21 . ILE   A  1  539 ? 58.072  27.988  -7.565   1.00 131.75 ? 539  ILE   A HG21 1 
ATOM   8191  H  HG22 . ILE   A  1  539 ? 57.282  26.899  -6.720   1.00 131.75 ? 539  ILE   A HG22 1 
ATOM   8192  H  HG23 . ILE   A  1  539 ? 58.066  26.470  -8.033   1.00 131.75 ? 539  ILE   A HG23 1 
ATOM   8193  H  HD11 . ILE   A  1  539 ? 57.839  29.086  -10.960  1.00 136.41 ? 539  ILE   A HD11 1 
ATOM   8194  H  HD12 . ILE   A  1  539 ? 57.522  29.621  -9.499   1.00 136.41 ? 539  ILE   A HD12 1 
ATOM   8195  H  HD13 . ILE   A  1  539 ? 58.584  28.458  -9.706   1.00 136.41 ? 539  ILE   A HD13 1 
ATOM   8196  N  N    . ALA   A  1  540 ? 55.376  25.142  -6.257   1.00 105.78 ? 540  ALA   A N    1 
ATOM   8197  C  CA   . ALA   A  1  540 ? 54.932  24.845  -4.904   1.00 108.11 ? 540  ALA   A CA   1 
ATOM   8198  C  C    . ALA   A  1  540 ? 56.093  25.070  -3.945   1.00 113.17 ? 540  ALA   A C    1 
ATOM   8199  O  O    . ALA   A  1  540 ? 57.250  25.188  -4.357   1.00 115.99 ? 540  ALA   A O    1 
ATOM   8200  C  CB   . ALA   A  1  540 ? 54.410  23.408  -4.787   1.00 103.02 ? 540  ALA   A CB   1 
ATOM   8201  H  H    . ALA   A  1  540 ? 56.088  24.713  -6.477   1.00 126.92 ? 540  ALA   A H    1 
ATOM   8202  H  HA   . ALA   A  1  540 ? 54.210  25.446  -4.659   1.00 129.71 ? 540  ALA   A HA   1 
ATOM   8203  H  HB1  . ALA   A  1  540 ? 54.159  23.237  -3.866   1.00 123.61 ? 540  ALA   A HB1  1 
ATOM   8204  H  HB2  . ALA   A  1  540 ? 53.637  23.305  -5.365   1.00 123.61 ? 540  ALA   A HB2  1 
ATOM   8205  H  HB3  . ALA   A  1  540 ? 55.110  22.795  -5.058   1.00 123.61 ? 540  ALA   A HB3  1 
ATOM   8206  N  N    . TYR   A  1  541 ? 55.781  25.126  -2.650   1.00 113.57 ? 541  TYR   A N    1 
ATOM   8207  C  CA   . TYR   A  1  541 ? 56.783  25.479  -1.656   1.00 113.92 ? 541  TYR   A CA   1 
ATOM   8208  C  C    . TYR   A  1  541 ? 56.557  24.707  -0.364   1.00 109.21 ? 541  TYR   A C    1 
ATOM   8209  O  O    . TYR   A  1  541 ? 55.457  24.227  -0.081   1.00 105.14 ? 541  TYR   A O    1 
ATOM   8210  C  CB   . TYR   A  1  541 ? 56.782  26.993  -1.394   1.00 119.95 ? 541  TYR   A CB   1 
ATOM   8211  C  CG   . TYR   A  1  541 ? 55.723  27.522  -0.437   1.00 124.94 ? 541  TYR   A CG   1 
ATOM   8212  C  CD1  . TYR   A  1  541 ? 54.496  27.975  -0.901   1.00 127.51 ? 541  TYR   A CD1  1 
ATOM   8213  C  CD2  . TYR   A  1  541 ? 55.971  27.606  0.929    1.00 127.28 ? 541  TYR   A CD2  1 
ATOM   8214  C  CE1  . TYR   A  1  541 ? 53.542  28.478  -0.030   1.00 130.52 ? 541  TYR   A CE1  1 
ATOM   8215  C  CE2  . TYR   A  1  541 ? 55.032  28.113  1.802    1.00 130.66 ? 541  TYR   A CE2  1 
ATOM   8216  C  CZ   . TYR   A  1  541 ? 53.818  28.544  1.321    1.00 130.80 ? 541  TYR   A CZ   1 
ATOM   8217  O  OH   . TYR   A  1  541 ? 52.883  29.042  2.198    1.00 130.71 ? 541  TYR   A OH   1 
ATOM   8218  H  H    . TYR   A  1  541 ? 55.000  24.964  -2.328   1.00 136.27 ? 541  TYR   A H    1 
ATOM   8219  H  HA   . TYR   A  1  541 ? 57.659  25.216  -1.980   1.00 136.68 ? 541  TYR   A HA   1 
ATOM   8220  H  HB2  . TYR   A  1  541 ? 57.645  27.235  -1.023   1.00 143.92 ? 541  TYR   A HB2  1 
ATOM   8221  H  HB3  . TYR   A  1  541 ? 56.648  27.445  -2.242   1.00 143.92 ? 541  TYR   A HB3  1 
ATOM   8222  H  HD1  . TYR   A  1  541 ? 54.310  27.940  -1.812   1.00 152.99 ? 541  TYR   A HD1  1 
ATOM   8223  H  HD2  . TYR   A  1  541 ? 56.789  27.313  1.262    1.00 152.72 ? 541  TYR   A HD2  1 
ATOM   8224  H  HE1  . TYR   A  1  541 ? 52.720  28.770  -0.353   1.00 156.61 ? 541  TYR   A HE1  1 
ATOM   8225  H  HE2  . TYR   A  1  541 ? 55.219  28.164  2.711    1.00 156.77 ? 541  TYR   A HE2  1 
ATOM   8226  H  HH   . TYR   A  1  541 ? 52.210  29.314  1.776    1.00 156.83 ? 541  TYR   A HH   1 
ATOM   8227  N  N    . LEU   A  1  542 ? 57.633  24.585  0.411    1.00 110.88 ? 542  LEU   A N    1 
ATOM   8228  C  CA   . LEU   A  1  542 ? 57.617  23.925  1.707    1.00 109.78 ? 542  LEU   A CA   1 
ATOM   8229  C  C    . LEU   A  1  542 ? 57.477  24.951  2.825    1.00 113.09 ? 542  LEU   A C    1 
ATOM   8230  O  O    . LEU   A  1  542 ? 57.954  26.084  2.720    1.00 113.99 ? 542  LEU   A O    1 
ATOM   8231  C  CB   . LEU   A  1  542 ? 58.895  23.110  1.926    1.00 108.42 ? 542  LEU   A CB   1 
ATOM   8232  C  CG   . LEU   A  1  542 ? 58.924  21.657  1.449    1.00 106.90 ? 542  LEU   A CG   1 
ATOM   8233  C  CD1  . LEU   A  1  542 ? 60.273  21.024  1.771    1.00 104.48 ? 542  LEU   A CD1  1 
ATOM   8234  C  CD2  . LEU   A  1  542 ? 57.802  20.851  2.080    1.00 109.30 ? 542  LEU   A CD2  1 
ATOM   8235  H  H    . LEU   A  1  542 ? 58.409  24.889  0.197    1.00 133.04 ? 542  LEU   A H    1 
ATOM   8236  H  HA   . LEU   A  1  542 ? 56.858  23.322  1.743    1.00 131.71 ? 542  LEU   A HA   1 
ATOM   8237  H  HB2  . LEU   A  1  542 ? 59.616  23.567  1.465    1.00 130.08 ? 542  LEU   A HB2  1 
ATOM   8238  H  HB3  . LEU   A  1  542 ? 59.071  23.091  2.880    1.00 130.08 ? 542  LEU   A HB3  1 
ATOM   8239  H  HG   . LEU   A  1  542 ? 58.795  21.642  0.487    1.00 128.26 ? 542  LEU   A HG   1 
ATOM   8240  H  HD11 . LEU   A  1  542 ? 60.308  20.138  1.378    1.00 125.36 ? 542  LEU   A HD11 1 
ATOM   8241  H  HD12 . LEU   A  1  542 ? 60.978  21.578  1.402    1.00 125.36 ? 542  LEU   A HD12 1 
ATOM   8242  H  HD13 . LEU   A  1  542 ? 60.371  20.962  2.734    1.00 125.36 ? 542  LEU   A HD13 1 
ATOM   8243  H  HD21 . LEU   A  1  542 ? 57.931  19.912  1.872    1.00 131.15 ? 542  LEU   A HD21 1 
ATOM   8244  H  HD22 . LEU   A  1  542 ? 57.821  20.982  3.041    1.00 131.15 ? 542  LEU   A HD22 1 
ATOM   8245  H  HD23 . LEU   A  1  542 ? 56.954  21.156  1.722    1.00 131.15 ? 542  LEU   A HD23 1 
ATOM   8246  N  N    . ARG   A  1  543 ? 56.824  24.534  3.906    1.00 114.96 ? 543  ARG   A N    1 
ATOM   8247  C  CA   . ARG   A  1  543 ? 56.681  25.377  5.080    1.00 122.67 ? 543  ARG   A CA   1 
ATOM   8248  C  C    . ARG   A  1  543 ? 57.987  25.408  5.873    1.00 127.38 ? 543  ARG   A C    1 
ATOM   8249  O  O    . ARG   A  1  543 ? 58.913  24.629  5.633    1.00 131.01 ? 543  ARG   A O    1 
ATOM   8250  C  CB   . ARG   A  1  543 ? 55.542  24.876  5.965    1.00 124.70 ? 543  ARG   A CB   1 
ATOM   8251  C  CG   . ARG   A  1  543 ? 54.142  25.143  5.424    1.00 128.74 ? 543  ARG   A CG   1 
ATOM   8252  C  CD   . ARG   A  1  543 ? 53.883  26.624  5.149    1.00 136.58 ? 543  ARG   A CD   1 
ATOM   8253  N  NE   . ARG   A  1  543 ? 54.520  27.508  6.123    1.00 139.95 ? 543  ARG   A NE   1 
ATOM   8254  C  CZ   . ARG   A  1  543 ? 54.501  28.836  6.054    1.00 139.22 ? 543  ARG   A CZ   1 
ATOM   8255  N  NH1  . ARG   A  1  543 ? 55.111  29.556  6.985    1.00 141.82 ? 543  ARG   A NH1  1 
ATOM   8256  N  NH2  . ARG   A  1  543 ? 53.876  29.447  5.056    1.00 137.28 ? 543  ARG   A NH2  1 
ATOM   8257  H  H    . ARG   A  1  543 ? 56.453  23.762  3.982    1.00 137.93 ? 543  ARG   A H    1 
ATOM   8258  H  HA   . ARG   A  1  543 ? 56.471  26.281  4.797    1.00 147.19 ? 543  ARG   A HA   1 
ATOM   8259  H  HB2  . ARG   A  1  543 ? 55.634  23.916  6.071    1.00 149.63 ? 543  ARG   A HB2  1 
ATOM   8260  H  HB3  . ARG   A  1  543 ? 55.608  25.313  6.829    1.00 149.63 ? 543  ARG   A HB3  1 
ATOM   8261  H  HG2  . ARG   A  1  543 ? 54.028  24.661  4.590    1.00 154.47 ? 543  ARG   A HG2  1 
ATOM   8262  H  HG3  . ARG   A  1  543 ? 53.488  24.841  6.074    1.00 154.47 ? 543  ARG   A HG3  1 
ATOM   8263  H  HD2  . ARG   A  1  543 ? 54.231  26.847  4.272    1.00 163.88 ? 543  ARG   A HD2  1 
ATOM   8264  H  HD3  . ARG   A  1  543 ? 52.927  26.787  5.179    1.00 163.88 ? 543  ARG   A HD3  1 
ATOM   8265  H  HE   . ARG   A  1  543 ? 54.933  27.145  6.785    1.00 167.92 ? 543  ARG   A HE   1 
ATOM   8266  H  HH11 . ARG   A  1  543 ? 55.518  29.165  7.633    1.00 170.16 ? 543  ARG   A HH11 1 
ATOM   8267  H  HH12 . ARG   A  1  543 ? 55.099  30.415  6.940    1.00 170.16 ? 543  ARG   A HH12 1 
ATOM   8268  H  HH21 . ARG   A  1  543 ? 53.480  28.984  4.449    1.00 164.71 ? 543  ARG   A HH21 1 
ATOM   8269  H  HH22 . ARG   A  1  543 ? 53.868  30.306  5.015    1.00 164.71 ? 543  ARG   A HH22 1 
ATOM   8270  N  N    . ASP   A  1  544 ? 58.052  26.328  6.832    1.00 128.24 ? 544  ASP   A N    1 
ATOM   8271  C  CA   . ASP   A  1  544 ? 59.219  26.418  7.697    1.00 129.97 ? 544  ASP   A CA   1 
ATOM   8272  C  C    . ASP   A  1  544 ? 59.320  25.183  8.586    1.00 136.18 ? 544  ASP   A C    1 
ATOM   8273  O  O    . ASP   A  1  544 ? 58.314  24.615  9.020    1.00 137.94 ? 544  ASP   A O    1 
ATOM   8274  C  CB   . ASP   A  1  544 ? 59.153  27.683  8.554    1.00 127.80 ? 544  ASP   A CB   1 
ATOM   8275  C  CG   . ASP   A  1  544 ? 59.420  28.948  7.753    1.00 127.95 ? 544  ASP   A CG   1 
ATOM   8276  O  OD1  . ASP   A  1  544 ? 59.645  28.847  6.528    1.00 125.82 ? 544  ASP   A OD1  1 
ATOM   8277  O  OD2  . ASP   A  1  544 ? 59.410  30.045  8.351    1.00 132.74 ? 544  ASP   A OD2  1 
ATOM   8278  H  H    . ASP   A  1  544 ? 57.438  26.906  6.999    1.00 153.87 ? 544  ASP   A H    1 
ATOM   8279  H  HA   . ASP   A  1  544 ? 60.022  26.469  7.155    1.00 155.95 ? 544  ASP   A HA   1 
ATOM   8280  H  HB2  . ASP   A  1  544 ? 58.268  27.756  8.944    1.00 153.34 ? 544  ASP   A HB2  1 
ATOM   8281  H  HB3  . ASP   A  1  544 ? 59.820  27.625  9.256    1.00 153.34 ? 544  ASP   A HB3  1 
ATOM   8282  N  N    . GLU   A  1  545 ? 60.562  24.767  8.854    1.00 139.01 ? 545  GLU   A N    1 
ATOM   8283  C  CA   . GLU   A  1  545 ? 60.787  23.578  9.668    1.00 137.85 ? 545  GLU   A CA   1 
ATOM   8284  C  C    . GLU   A  1  545 ? 60.077  23.672  11.012   1.00 137.54 ? 545  GLU   A C    1 
ATOM   8285  O  O    . GLU   A  1  545 ? 59.695  22.647  11.588   1.00 138.44 ? 545  GLU   A O    1 
ATOM   8286  C  CB   . GLU   A  1  545 ? 62.286  23.368  9.890    1.00 141.18 ? 545  GLU   A CB   1 
ATOM   8287  C  CG   . GLU   A  1  545 ? 63.104  23.241  8.614    1.00 141.85 ? 545  GLU   A CG   1 
ATOM   8288  C  CD   . GLU   A  1  545 ? 64.581  23.062  8.894    1.00 146.79 ? 545  GLU   A CD   1 
ATOM   8289  O  OE1  . GLU   A  1  545 ? 65.000  23.309  10.044   1.00 150.91 ? 545  GLU   A OE1  1 
ATOM   8290  O  OE2  . GLU   A  1  545 ? 65.320  22.672  7.967    1.00 147.03 ? 545  GLU   A OE2  1 
ATOM   8291  H  H    . GLU   A  1  545 ? 61.280  25.153  8.578    1.00 166.80 ? 545  GLU   A H    1 
ATOM   8292  H  HA   . GLU   A  1  545 ? 60.438  22.808  9.192    1.00 165.40 ? 545  GLU   A HA   1 
ATOM   8293  H  HB2  . GLU   A  1  545 ? 62.633  24.126  10.385   1.00 169.40 ? 545  GLU   A HB2  1 
ATOM   8294  H  HB3  . GLU   A  1  545 ? 62.411  22.553  10.400   1.00 169.40 ? 545  GLU   A HB3  1 
ATOM   8295  H  HG2  . GLU   A  1  545 ? 62.796  22.469  8.114    1.00 170.20 ? 545  GLU   A HG2  1 
ATOM   8296  H  HG3  . GLU   A  1  545 ? 62.993  24.046  8.083    1.00 170.20 ? 545  GLU   A HG3  1 
ATOM   8297  N  N    . SER   A  1  546 ? 59.892  24.890  11.526   1.00 134.33 ? 546  SER   A N    1 
ATOM   8298  C  CA   . SER   A  1  546 ? 59.261  25.066  12.827   1.00 128.43 ? 546  SER   A CA   1 
ATOM   8299  C  C    . SER   A  1  546 ? 57.820  24.575  12.850   1.00 123.90 ? 546  SER   A C    1 
ATOM   8300  O  O    . SER   A  1  546 ? 57.286  24.311  13.932   1.00 125.56 ? 546  SER   A O    1 
ATOM   8301  C  CB   . SER   A  1  546 ? 59.306  26.542  13.228   1.00 127.95 ? 546  SER   A CB   1 
ATOM   8302  O  OG   . SER   A  1  546 ? 58.749  27.359  12.212   1.00 123.82 ? 546  SER   A OG   1 
ATOM   8303  H  H    . SER   A  1  546 ? 60.122  25.624  11.141   1.00 161.18 ? 546  SER   A H    1 
ATOM   8304  H  HA   . SER   A  1  546 ? 59.759  24.553  13.483   1.00 154.09 ? 546  SER   A HA   1 
ATOM   8305  H  HB2  . SER   A  1  546 ? 58.798  26.663  14.045   1.00 153.52 ? 546  SER   A HB2  1 
ATOM   8306  H  HB3  . SER   A  1  546 ? 60.230  26.802  13.370   1.00 153.52 ? 546  SER   A HB3  1 
ATOM   8307  H  HG   . SER   A  1  546 ? 58.754  28.163  12.455   1.00 148.57 ? 546  SER   A HG   1 
ATOM   8308  N  N    . GLU   A  1  547 ? 57.181  24.442  11.688   1.00 118.98 ? 547  GLU   A N    1 
ATOM   8309  C  CA   . GLU   A  1  547 ? 55.765  24.105  11.632   1.00 119.00 ? 547  GLU   A CA   1 
ATOM   8310  C  C    . GLU   A  1  547 ? 55.505  22.614  11.472   1.00 115.27 ? 547  GLU   A C    1 
ATOM   8311  O  O    . GLU   A  1  547 ? 54.379  22.169  11.720   1.00 111.21 ? 547  GLU   A O    1 
ATOM   8312  C  CB   . GLU   A  1  547 ? 55.096  24.867  10.484   1.00 120.54 ? 547  GLU   A CB   1 
ATOM   8313  C  CG   . GLU   A  1  547 ? 55.276  26.374  10.579   1.00 128.77 ? 547  GLU   A CG   1 
ATOM   8314  C  CD   . GLU   A  1  547 ? 54.486  27.130  9.528    1.00 132.90 ? 547  GLU   A CD   1 
ATOM   8315  O  OE1  . GLU   A  1  547 ? 53.980  26.489  8.583    1.00 130.49 ? 547  GLU   A OE1  1 
ATOM   8316  O  OE2  . GLU   A  1  547 ? 54.369  28.368  9.650    1.00 138.87 ? 547  GLU   A OE2  1 
ATOM   8317  H  H    . GLU   A  1  547 ? 57.549  24.542  10.917   1.00 142.75 ? 547  GLU   A H    1 
ATOM   8318  H  HA   . GLU   A  1  547 ? 55.346  24.382  12.462   1.00 142.78 ? 547  GLU   A HA   1 
ATOM   8319  H  HB2  . GLU   A  1  547 ? 55.482  24.573  9.644    1.00 144.62 ? 547  GLU   A HB2  1 
ATOM   8320  H  HB3  . GLU   A  1  547 ? 54.144  24.679  10.495   1.00 144.62 ? 547  GLU   A HB3  1 
ATOM   8321  H  HG2  . GLU   A  1  547 ? 54.976  26.673  11.451   1.00 154.51 ? 547  GLU   A HG2  1 
ATOM   8322  H  HG3  . GLU   A  1  547 ? 56.214  26.588  10.459   1.00 154.51 ? 547  GLU   A HG3  1 
ATOM   8323  N  N    . PHE   A  1  548 ? 56.507  21.834  11.070   1.00 118.10 ? 548  PHE   A N    1 
ATOM   8324  C  CA   . PHE   A  1  548 ? 56.362  20.388  10.958   1.00 118.63 ? 548  PHE   A CA   1 
ATOM   8325  C  C    . PHE   A  1  548 ? 57.662  19.722  11.379   1.00 120.74 ? 548  PHE   A C    1 
ATOM   8326  O  O    . PHE   A  1  548 ? 58.735  20.084  10.888   1.00 121.06 ? 548  PHE   A O    1 
ATOM   8327  C  CB   . PHE   A  1  548 ? 55.995  19.970  9.527    1.00 114.61 ? 548  PHE   A CB   1 
ATOM   8328  C  CG   . PHE   A  1  548 ? 57.054  20.289  8.508    1.00 114.21 ? 548  PHE   A CG   1 
ATOM   8329  C  CD1  . PHE   A  1  548 ? 57.127  21.547  7.936    1.00 117.79 ? 548  PHE   A CD1  1 
ATOM   8330  C  CD2  . PHE   A  1  548 ? 57.967  19.324  8.110    1.00 110.96 ? 548  PHE   A CD2  1 
ATOM   8331  C  CE1  . PHE   A  1  548 ? 58.095  21.841  6.995    1.00 118.00 ? 548  PHE   A CE1  1 
ATOM   8332  C  CE2  . PHE   A  1  548 ? 58.936  19.613  7.167    1.00 111.48 ? 548  PHE   A CE2  1 
ATOM   8333  C  CZ   . PHE   A  1  548 ? 59.000  20.873  6.609    1.00 115.67 ? 548  PHE   A CZ   1 
ATOM   8334  H  H    . PHE   A  1  548 ? 57.287  22.124  10.854   1.00 141.70 ? 548  PHE   A H    1 
ATOM   8335  H  HA   . PHE   A  1  548 ? 55.657  20.090  11.553   1.00 142.34 ? 548  PHE   A HA   1 
ATOM   8336  H  HB2  . PHE   A  1  548 ? 55.849  19.012  9.511    1.00 137.52 ? 548  PHE   A HB2  1 
ATOM   8337  H  HB3  . PHE   A  1  548 ? 55.185  20.434  9.266    1.00 137.52 ? 548  PHE   A HB3  1 
ATOM   8338  H  HD1  . PHE   A  1  548 ? 56.517  22.202  8.189    1.00 141.33 ? 548  PHE   A HD1  1 
ATOM   8339  H  HD2  . PHE   A  1  548 ? 57.927  18.472  8.481    1.00 133.14 ? 548  PHE   A HD2  1 
ATOM   8340  H  HE1  . PHE   A  1  548 ? 58.136  22.692  6.621    1.00 141.58 ? 548  PHE   A HE1  1 
ATOM   8341  H  HE2  . PHE   A  1  548 ? 59.545  18.959  6.909    1.00 133.76 ? 548  PHE   A HE2  1 
ATOM   8342  H  HZ   . PHE   A  1  548 ? 59.651  21.070  5.975    1.00 138.79 ? 548  PHE   A HZ   1 
ATOM   8343  N  N    . ARG   A  1  549 ? 57.564  18.757  12.296   1.00 122.06 ? 549  ARG   A N    1 
ATOM   8344  C  CA   . ARG   A  1  549 ? 58.704  17.950  12.710   1.00 123.84 ? 549  ARG   A CA   1 
ATOM   8345  C  C    . ARG   A  1  549 ? 58.691  16.566  12.066   1.00 121.32 ? 549  ARG   A C    1 
ATOM   8346  O  O    . ARG   A  1  549 ? 59.269  15.621  12.614   1.00 118.53 ? 549  ARG   A O    1 
ATOM   8347  C  CB   . ARG   A  1  549 ? 58.749  17.832  14.236   1.00 128.04 ? 549  ARG   A CB   1 
ATOM   8348  C  CG   . ARG   A  1  549 ? 57.555  17.133  14.865   1.00 128.14 ? 549  ARG   A CG   1 
ATOM   8349  C  CD   . ARG   A  1  549 ? 57.779  16.897  16.354   1.00 131.67 ? 549  ARG   A CD   1 
ATOM   8350  N  NE   . ARG   A  1  549 ? 58.068  18.135  17.074   1.00 134.30 ? 549  ARG   A NE   1 
ATOM   8351  C  CZ   . ARG   A  1  549 ? 58.406  18.196  18.359   1.00 137.67 ? 549  ARG   A CZ   1 
ATOM   8352  N  NH1  . ARG   A  1  549 ? 58.649  19.370  18.925   1.00 139.53 ? 549  ARG   A NH1  1 
ATOM   8353  N  NH2  . ARG   A  1  549 ? 58.504  17.087  19.080   1.00 138.80 ? 549  ARG   A NH2  1 
ATOM   8354  H  H    . ARG   A  1  549 ? 56.832  18.550  12.697   1.00 146.46 ? 549  ARG   A H    1 
ATOM   8355  H  HA   . ARG   A  1  549 ? 59.517  18.400  12.431   1.00 148.59 ? 549  ARG   A HA   1 
ATOM   8356  H  HB2  . ARG   A  1  549 ? 59.542  17.330  14.481   1.00 153.63 ? 549  ARG   A HB2  1 
ATOM   8357  H  HB3  . ARG   A  1  549 ? 58.794  18.726  14.611   1.00 153.63 ? 549  ARG   A HB3  1 
ATOM   8358  H  HG2  . ARG   A  1  549 ? 56.765  17.685  14.758   1.00 153.75 ? 549  ARG   A HG2  1 
ATOM   8359  H  HG3  . ARG   A  1  549 ? 57.421  16.274  14.435   1.00 153.75 ? 549  ARG   A HG3  1 
ATOM   8360  H  HD2  . ARG   A  1  549 ? 56.980  16.504  16.738   1.00 157.98 ? 549  ARG   A HD2  1 
ATOM   8361  H  HD3  . ARG   A  1  549 ? 58.533  16.297  16.472   1.00 157.98 ? 549  ARG   A HD3  1 
ATOM   8362  H  HE   . ARG   A  1  549 ? 58.015  18.874  16.637   1.00 161.14 ? 549  ARG   A HE   1 
ATOM   8363  H  HH11 . ARG   A  1  549 ? 58.588  20.092  18.461   1.00 167.41 ? 549  ARG   A HH11 1 
ATOM   8364  H  HH12 . ARG   A  1  549 ? 58.867  19.410  19.756   1.00 167.41 ? 549  ARG   A HH12 1 
ATOM   8365  H  HH21 . ARG   A  1  549 ? 58.349  16.323  18.717   1.00 166.54 ? 549  ARG   A HH21 1 
ATOM   8366  H  HH22 . ARG   A  1  549 ? 58.723  17.132  19.911   1.00 166.54 ? 549  ARG   A HH22 1 
ATOM   8367  N  N    . ASP   A  1  550 ? 58.043  16.432  10.912   1.00 123.26 ? 550  ASP   A N    1 
ATOM   8368  C  CA   . ASP   A  1  550 ? 58.017  15.190  10.145   1.00 122.54 ? 550  ASP   A CA   1 
ATOM   8369  C  C    . ASP   A  1  550 ? 58.752  15.441  8.832    1.00 122.87 ? 550  ASP   A C    1 
ATOM   8370  O  O    . ASP   A  1  550 ? 58.173  15.967  7.877    1.00 121.13 ? 550  ASP   A O    1 
ATOM   8371  C  CB   . ASP   A  1  550 ? 56.586  14.722  9.900    1.00 118.41 ? 550  ASP   A CB   1 
ATOM   8372  C  CG   . ASP   A  1  550 ? 56.524  13.430  9.109    1.00 111.93 ? 550  ASP   A CG   1 
ATOM   8373  O  OD1  . ASP   A  1  550 ? 57.595  12.858  8.816    1.00 109.30 ? 550  ASP   A OD1  1 
ATOM   8374  O  OD2  . ASP   A  1  550 ? 55.404  12.989  8.781    1.00 108.83 ? 550  ASP   A OD2  1 
ATOM   8375  H  H    . ASP   A  1  550 ? 57.597  17.068  10.541   1.00 147.89 ? 550  ASP   A H    1 
ATOM   8376  H  HA   . ASP   A  1  550 ? 58.483  14.497  10.640   1.00 147.03 ? 550  ASP   A HA   1 
ATOM   8377  H  HB2  . ASP   A  1  550 ? 56.151  14.572  10.754   1.00 142.07 ? 550  ASP   A HB2  1 
ATOM   8378  H  HB3  . ASP   A  1  550 ? 56.111  15.404  9.401    1.00 142.07 ? 550  ASP   A HB3  1 
ATOM   8379  N  N    . LYS   A  1  551 ? 60.029  15.065  8.792    1.00 124.39 ? 551  LYS   A N    1 
ATOM   8380  C  CA   . LYS   A  1  551 ? 60.848  15.182  7.593    1.00 122.19 ? 551  LYS   A CA   1 
ATOM   8381  C  C    . LYS   A  1  551 ? 61.132  13.829  6.953    1.00 117.48 ? 551  LYS   A C    1 
ATOM   8382  O  O    . LYS   A  1  551 ? 61.923  13.754  6.007    1.00 114.33 ? 551  LYS   A O    1 
ATOM   8383  C  CB   . LYS   A  1  551 ? 62.165  15.888  7.922    1.00 123.99 ? 551  LYS   A CB   1 
ATOM   8384  C  CG   . LYS   A  1  551 ? 62.005  17.263  8.551    1.00 126.12 ? 551  LYS   A CG   1 
ATOM   8385  C  CD   . LYS   A  1  551 ? 63.361  17.859  8.900    1.00 128.08 ? 551  LYS   A CD   1 
ATOM   8386  C  CE   . LYS   A  1  551 ? 63.231  19.203  9.599    1.00 130.92 ? 551  LYS   A CE   1 
ATOM   8387  N  NZ   . LYS   A  1  551 ? 64.563  19.776  9.935    1.00 134.18 ? 551  LYS   A NZ   1 
ATOM   8388  H  H    . LYS   A  1  551 ? 60.451  14.731  9.463    1.00 149.25 ? 551  LYS   A H    1 
ATOM   8389  H  HA   . LYS   A  1  551 ? 60.370  15.725  6.946    1.00 146.61 ? 551  LYS   A HA   1 
ATOM   8390  H  HB2  . LYS   A  1  551 ? 62.663  15.336  8.546    1.00 148.77 ? 551  LYS   A HB2  1 
ATOM   8391  H  HB3  . LYS   A  1  551 ? 62.670  15.998  7.101    1.00 148.77 ? 551  LYS   A HB3  1 
ATOM   8392  H  HG2  . LYS   A  1  551 ? 61.561  17.856  7.925    1.00 151.32 ? 551  LYS   A HG2  1 
ATOM   8393  H  HG3  . LYS   A  1  551 ? 61.483  17.189  9.365    1.00 151.32 ? 551  LYS   A HG3  1 
ATOM   8394  H  HD2  . LYS   A  1  551 ? 63.832  17.253  9.494    1.00 153.68 ? 551  LYS   A HD2  1 
ATOM   8395  H  HD3  . LYS   A  1  551 ? 63.872  17.989  8.086    1.00 153.68 ? 551  LYS   A HD3  1 
ATOM   8396  H  HE2  . LYS   A  1  551 ? 62.770  19.825  9.014    1.00 157.09 ? 551  LYS   A HE2  1 
ATOM   8397  H  HE3  . LYS   A  1  551 ? 62.731  19.089  10.422   1.00 157.09 ? 551  LYS   A HE3  1 
ATOM   8398  H  HZ1  . LYS   A  1  551 ? 64.465  20.585  10.292   1.00 161.00 ? 551  LYS   A HZ1  1 
ATOM   8399  H  HZ2  . LYS   A  1  551 ? 64.982  19.251  10.518   1.00 161.00 ? 551  LYS   A HZ2  1 
ATOM   8400  H  HZ3  . LYS   A  1  551 ? 65.059  19.844  9.199    1.00 161.00 ? 551  LYS   A HZ3  1 
ATOM   8401  N  N    . LEU   A  1  552 ? 60.502  12.759  7.442    1.00 116.87 ? 552  LEU   A N    1 
ATOM   8402  C  CA   . LEU   A  1  552 ? 60.782  11.403  6.983    1.00 115.16 ? 552  LEU   A CA   1 
ATOM   8403  C  C    . LEU   A  1  552 ? 59.816  10.949  5.894    1.00 112.02 ? 552  LEU   A C    1 
ATOM   8404  O  O    . LEU   A  1  552 ? 60.245  10.548  4.808    1.00 109.17 ? 552  LEU   A O    1 
ATOM   8405  C  CB   . LEU   A  1  552 ? 60.727  10.432  8.170    1.00 117.20 ? 552  LEU   A CB   1 
ATOM   8406  C  CG   . LEU   A  1  552 ? 62.058  10.059  8.823    1.00 121.02 ? 552  LEU   A CG   1 
ATOM   8407  C  CD1  . LEU   A  1  552 ? 62.796  11.291  9.322    1.00 123.76 ? 552  LEU   A CD1  1 
ATOM   8408  C  CD2  . LEU   A  1  552 ? 61.811  9.077   9.959    1.00 124.10 ? 552  LEU   A CD2  1 
ATOM   8409  H  H    . LEU   A  1  552 ? 59.898  12.797  8.052    1.00 140.22 ? 552  LEU   A H    1 
ATOM   8410  H  HA   . LEU   A  1  552 ? 61.678  11.387  6.610    1.00 138.17 ? 552  LEU   A HA   1 
ATOM   8411  H  HB2  . LEU   A  1  552 ? 60.177  10.834  8.860    1.00 140.62 ? 552  LEU   A HB2  1 
ATOM   8412  H  HB3  . LEU   A  1  552 ? 60.322  9.606   7.862    1.00 140.62 ? 552  LEU   A HB3  1 
ATOM   8413  H  HG   . LEU   A  1  552 ? 62.630  9.637   8.163    1.00 145.21 ? 552  LEU   A HG   1 
ATOM   8414  H  HD11 . LEU   A  1  552 ? 63.630  11.015  9.733    1.00 148.49 ? 552  LEU   A HD11 1 
ATOM   8415  H  HD12 . LEU   A  1  552 ? 62.976  11.877  8.571    1.00 148.49 ? 552  LEU   A HD12 1 
ATOM   8416  H  HD13 . LEU   A  1  552 ? 62.241  11.749  9.973    1.00 148.49 ? 552  LEU   A HD13 1 
ATOM   8417  H  HD21 . LEU   A  1  552 ? 62.660  8.710   10.250   1.00 148.91 ? 552  LEU   A HD21 1 
ATOM   8418  H  HD22 . LEU   A  1  552 ? 61.383  9.544   10.693   1.00 148.91 ? 552  LEU   A HD22 1 
ATOM   8419  H  HD23 . LEU   A  1  552 ? 61.235  8.365   9.640    1.00 148.91 ? 552  LEU   A HD23 1 
ATOM   8420  N  N    . THR   A  1  553 ? 58.518  10.995  6.168    1.00 112.37 ? 553  THR   A N    1 
ATOM   8421  C  CA   . THR   A  1  553 ? 57.550  10.492  5.206    1.00 108.89 ? 553  THR   A CA   1 
ATOM   8422  C  C    . THR   A  1  553 ? 57.621  11.319  3.924    1.00 105.58 ? 553  THR   A C    1 
ATOM   8423  O  O    . THR   A  1  553 ? 57.761  12.546  3.984    1.00 108.89 ? 553  THR   A O    1 
ATOM   8424  C  CB   . THR   A  1  553 ? 56.131  10.539  5.778    1.00 109.96 ? 553  THR   A CB   1 
ATOM   8425  O  OG1  . THR   A  1  553 ? 55.678  11.897  5.837    1.00 113.37 ? 553  THR   A OG1  1 
ATOM   8426  C  CG2  . THR   A  1  553 ? 56.085  9.926   7.177    1.00 111.00 ? 553  THR   A CG2  1 
ATOM   8427  H  H    . THR   A  1  553 ? 58.176  11.308  6.893    1.00 134.82 ? 553  THR   A H    1 
ATOM   8428  H  HA   . THR   A  1  553 ? 57.757  9.567   4.997    1.00 130.65 ? 553  THR   A HA   1 
ATOM   8429  H  HB   . THR   A  1  553 ? 55.540  10.026  5.205    1.00 131.93 ? 553  THR   A HB   1 
ATOM   8430  H  HG1  . THR   A  1  553 ? 54.875  11.922  6.085    1.00 136.02 ? 553  THR   A HG1  1 
ATOM   8431  H  HG21 . THR   A  1  553 ? 55.164  9.830   7.467    1.00 133.18 ? 553  THR   A HG21 1 
ATOM   8432  H  HG22 . THR   A  1  553 ? 56.506  9.052   7.171    1.00 133.18 ? 553  THR   A HG22 1 
ATOM   8433  H  HG23 . THR   A  1  553 ? 56.555  10.497  7.805    1.00 133.18 ? 553  THR   A HG23 1 
ATOM   8434  N  N    . PRO   A  1  554 ? 57.535  10.691  2.753    1.00 100.12 ? 554  PRO   A N    1 
ATOM   8435  C  CA   . PRO   A  1  554 ? 57.612  11.456  1.505    1.00 97.85  ? 554  PRO   A CA   1 
ATOM   8436  C  C    . PRO   A  1  554 ? 56.392  12.341  1.306    1.00 97.21  ? 554  PRO   A C    1 
ATOM   8437  O  O    . PRO   A  1  554 ? 55.351  12.178  1.948    1.00 97.43  ? 554  PRO   A O    1 
ATOM   8438  C  CB   . PRO   A  1  554 ? 57.696  10.373  0.424    1.00 95.35  ? 554  PRO   A CB   1 
ATOM   8439  C  CG   . PRO   A  1  554 ? 57.079  9.167   1.044    1.00 94.54  ? 554  PRO   A CG   1 
ATOM   8440  C  CD   . PRO   A  1  554 ? 57.407  9.243   2.506    1.00 97.61  ? 554  PRO   A CD   1 
ATOM   8441  H  HA   . PRO   A  1  554 ? 58.415  12.001  1.486    1.00 117.41 ? 554  PRO   A HA   1 
ATOM   8442  H  HB2  . PRO   A  1  554 ? 57.201  10.651  -0.363   1.00 114.40 ? 554  PRO   A HB2  1 
ATOM   8443  H  HB3  . PRO   A  1  554 ? 58.623  10.208  0.191    1.00 114.40 ? 554  PRO   A HB3  1 
ATOM   8444  H  HG2  . PRO   A  1  554 ? 56.119  9.184   0.906    1.00 113.43 ? 554  PRO   A HG2  1 
ATOM   8445  H  HG3  . PRO   A  1  554 ? 57.456  8.366   0.648    1.00 113.43 ? 554  PRO   A HG3  1 
ATOM   8446  H  HD2  . PRO   A  1  554 ? 56.692  8.863   3.040    1.00 117.11 ? 554  PRO   A HD2  1 
ATOM   8447  H  HD3  . PRO   A  1  554 ? 58.241  8.785   2.696    1.00 117.11 ? 554  PRO   A HD3  1 
ATOM   8448  N  N    . ILE   A  1  555 ? 56.541  13.297  0.393    1.00 96.21  ? 555  ILE   A N    1 
ATOM   8449  C  CA   . ILE   A  1  555 ? 55.484  14.239  0.043    1.00 96.39  ? 555  ILE   A CA   1 
ATOM   8450  C  C    . ILE   A  1  555 ? 54.952  13.840  -1.326   1.00 96.71  ? 555  ILE   A C    1 
ATOM   8451  O  O    . ILE   A  1  555 ? 55.672  13.926  -2.329   1.00 98.60  ? 555  ILE   A O    1 
ATOM   8452  C  CB   . ILE   A  1  555 ? 55.986  15.689  0.033    1.00 95.00  ? 555  ILE   A CB   1 
ATOM   8453  C  CG1  . ILE   A  1  555 ? 56.569  16.064  1.397    1.00 94.78  ? 555  ILE   A CG1  1 
ATOM   8454  C  CG2  . ILE   A  1  555 ? 54.849  16.626  -0.357   1.00 94.98  ? 555  ILE   A CG2  1 
ATOM   8455  C  CD1  . ILE   A  1  555 ? 57.339  17.364  1.390    1.00 95.58  ? 555  ILE   A CD1  1 
ATOM   8456  H  H    . ILE   A  1  555 ? 57.268  13.423  -0.049   1.00 115.43 ? 555  ILE   A H    1 
ATOM   8457  H  HA   . ILE   A  1  555 ? 54.766  14.165  0.691    1.00 115.65 ? 555  ILE   A HA   1 
ATOM   8458  H  HB   . ILE   A  1  555 ? 56.694  15.773  -0.624   1.00 113.98 ? 555  ILE   A HB   1 
ATOM   8459  H  HG12 . ILE   A  1  555 ? 55.843  16.153  2.034    1.00 113.72 ? 555  ILE   A HG12 1 
ATOM   8460  H  HG13 . ILE   A  1  555 ? 57.175  15.362  1.682    1.00 113.72 ? 555  ILE   A HG13 1 
ATOM   8461  H  HG21 . ILE   A  1  555 ? 55.055  17.521  -0.044   1.00 113.95 ? 555  ILE   A HG21 1 
ATOM   8462  H  HG22 . ILE   A  1  555 ? 54.757  16.627  -1.323   1.00 113.95 ? 555  ILE   A HG22 1 
ATOM   8463  H  HG23 . ILE   A  1  555 ? 54.027  16.314  0.053    1.00 113.95 ? 555  ILE   A HG23 1 
ATOM   8464  H  HD11 . ILE   A  1  555 ? 57.776  17.478  2.248    1.00 114.68 ? 555  ILE   A HD11 1 
ATOM   8465  H  HD12 . ILE   A  1  555 ? 58.003  17.334  0.683    1.00 114.68 ? 555  ILE   A HD12 1 
ATOM   8466  H  HD13 . ILE   A  1  555 ? 56.722  18.096  1.233    1.00 114.68 ? 555  ILE   A HD13 1 
ATOM   8467  N  N    . THR   A  1  556 ? 53.692  13.415  -1.373   1.00 95.47  ? 556  THR   A N    1 
ATOM   8468  C  CA   . THR   A  1  556 ? 53.071  12.974  -2.614   1.00 96.79  ? 556  THR   A CA   1 
ATOM   8469  C  C    . THR   A  1  556 ? 52.371  14.138  -3.302   1.00 98.62  ? 556  THR   A C    1 
ATOM   8470  O  O    . THR   A  1  556 ? 51.611  14.878  -2.670   1.00 102.88 ? 556  THR   A O    1 
ATOM   8471  C  CB   . THR   A  1  556 ? 52.062  11.854  -2.351   1.00 98.00  ? 556  THR   A CB   1 
ATOM   8472  O  OG1  . THR   A  1  556 ? 51.224  12.208  -1.243   1.00 103.93 ? 556  THR   A OG1  1 
ATOM   8473  C  CG2  . THR   A  1  556 ? 52.774  10.544  -2.058   1.00 94.97  ? 556  THR   A CG2  1 
ATOM   8474  H  H    . THR   A  1  556 ? 53.172  13.373  -0.690   1.00 114.54 ? 556  THR   A H    1 
ATOM   8475  H  HA   . THR   A  1  556 ? 53.765  12.639  -3.203   1.00 116.13 ? 556  THR   A HA   1 
ATOM   8476  H  HB   . THR   A  1  556 ? 51.512  11.725  -3.139   1.00 117.58 ? 556  THR   A HB   1 
ATOM   8477  H  HG1  . THR   A  1  556 ? 50.511  11.765  -1.269   1.00 124.70 ? 556  THR   A HG1  1 
ATOM   8478  H  HG21 . THR   A  1  556 ? 52.129  9.824   -1.989   1.00 113.94 ? 556  THR   A HG21 1 
ATOM   8479  H  HG22 . THR   A  1  556 ? 53.399  10.339  -2.771   1.00 113.94 ? 556  THR   A HG22 1 
ATOM   8480  H  HG23 . THR   A  1  556 ? 53.262  10.612  -1.222   1.00 113.94 ? 556  THR   A HG23 1 
ATOM   8481  N  N    . ILE   A  1  557 ? 52.633  14.295  -4.595   1.00 96.71  ? 557  ILE   A N    1 
ATOM   8482  C  CA   . ILE   A  1  557 ? 51.881  15.202  -5.452   1.00 96.30  ? 557  ILE   A CA   1 
ATOM   8483  C  C    . ILE   A  1  557 ? 50.839  14.352  -6.167   1.00 96.48  ? 557  ILE   A C    1 
ATOM   8484  O  O    . ILE   A  1  557 ? 51.177  13.532  -7.028   1.00 95.41  ? 557  ILE   A O    1 
ATOM   8485  C  CB   . ILE   A  1  557 ? 52.790  15.940  -6.444   1.00 95.19  ? 557  ILE   A CB   1 
ATOM   8486  C  CG1  . ILE   A  1  557 ? 53.784  16.841  -5.703   1.00 95.37  ? 557  ILE   A CG1  1 
ATOM   8487  C  CG2  . ILE   A  1  557 ? 51.969  16.797  -7.404   1.00 97.52  ? 557  ILE   A CG2  1 
ATOM   8488  C  CD1  . ILE   A  1  557 ? 54.884  16.101  -4.969   1.00 92.92  ? 557  ILE   A CD1  1 
ATOM   8489  H  H    . ILE   A  1  557 ? 53.259  13.875  -5.009   1.00 116.03 ? 557  ILE   A H    1 
ATOM   8490  H  HA   . ILE   A  1  557 ? 51.432  15.873  -4.914   1.00 115.54 ? 557  ILE   A HA   1 
ATOM   8491  H  HB   . ILE   A  1  557 ? 53.274  15.265  -6.945   1.00 114.21 ? 557  ILE   A HB   1 
ATOM   8492  H  HG12 . ILE   A  1  557 ? 54.208  17.428  -6.349   1.00 114.43 ? 557  ILE   A HG12 1 
ATOM   8493  H  HG13 . ILE   A  1  557 ? 53.296  17.365  -5.049   1.00 114.43 ? 557  ILE   A HG13 1 
ATOM   8494  H  HG21 . ILE   A  1  557 ? 52.548  17.123  -8.110   1.00 117.01 ? 557  ILE   A HG21 1 
ATOM   8495  H  HG22 . ILE   A  1  557 ? 51.259  16.255  -7.782   1.00 117.01 ? 557  ILE   A HG22 1 
ATOM   8496  H  HG23 . ILE   A  1  557 ? 51.590  17.544  -6.915   1.00 117.01 ? 557  ILE   A HG23 1 
ATOM   8497  H  HD11 . ILE   A  1  557 ? 55.655  16.683  -4.885   1.00 111.48 ? 557  ILE   A HD11 1 
ATOM   8498  H  HD12 . ILE   A  1  557 ? 54.562  15.850  -4.089   1.00 111.48 ? 557  ILE   A HD12 1 
ATOM   8499  H  HD13 . ILE   A  1  557 ? 55.121  15.307  -5.473   1.00 111.48 ? 557  ILE   A HD13 1 
ATOM   8500  N  N    . PHE   A  1  558 ? 49.574  14.534  -5.804   1.00 97.89  ? 558  PHE   A N    1 
ATOM   8501  C  CA   . PHE   A  1  558 ? 48.477  13.754  -6.356   1.00 98.15  ? 558  PHE   A CA   1 
ATOM   8502  C  C    . PHE   A  1  558 ? 47.787  14.544  -7.458   1.00 97.27  ? 558  PHE   A C    1 
ATOM   8503  O  O    . PHE   A  1  558 ? 47.578  15.754  -7.331   1.00 100.05 ? 558  PHE   A O    1 
ATOM   8504  C  CB   . PHE   A  1  558 ? 47.470  13.387  -5.265   1.00 102.27 ? 558  PHE   A CB   1 
ATOM   8505  C  CG   . PHE   A  1  558 ? 46.349  12.508  -5.740   1.00 104.95 ? 558  PHE   A CG   1 
ATOM   8506  C  CD1  . PHE   A  1  558 ? 46.566  11.165  -5.995   1.00 104.41 ? 558  PHE   A CD1  1 
ATOM   8507  C  CD2  . PHE   A  1  558 ? 45.074  13.021  -5.918   1.00 108.34 ? 558  PHE   A CD2  1 
ATOM   8508  C  CE1  . PHE   A  1  558 ? 45.537  10.353  -6.425   1.00 105.45 ? 558  PHE   A CE1  1 
ATOM   8509  C  CE2  . PHE   A  1  558 ? 44.041  12.212  -6.349   1.00 109.12 ? 558  PHE   A CE2  1 
ATOM   8510  C  CZ   . PHE   A  1  558 ? 44.273  10.877  -6.602   1.00 107.50 ? 558  PHE   A CZ   1 
ATOM   8511  H  H    . PHE   A  1  558 ? 49.322  15.117  -5.224   1.00 117.44 ? 558  PHE   A H    1 
ATOM   8512  H  HA   . PHE   A  1  558 ? 48.821  12.932  -6.740   1.00 117.76 ? 558  PHE   A HA   1 
ATOM   8513  H  HB2  . PHE   A  1  558 ? 47.936  12.915  -4.557   1.00 122.71 ? 558  PHE   A HB2  1 
ATOM   8514  H  HB3  . PHE   A  1  558 ? 47.078  14.203  -4.916   1.00 122.71 ? 558  PHE   A HB3  1 
ATOM   8515  H  HD1  . PHE   A  1  558 ? 47.415  10.806  -5.874   1.00 125.27 ? 558  PHE   A HD1  1 
ATOM   8516  H  HD2  . PHE   A  1  558 ? 44.912  13.920  -5.746   1.00 129.98 ? 558  PHE   A HD2  1 
ATOM   8517  H  HE1  . PHE   A  1  558 ? 45.696  9.452   -6.596   1.00 126.52 ? 558  PHE   A HE1  1 
ATOM   8518  H  HE2  . PHE   A  1  558 ? 43.190  12.568  -6.467   1.00 130.93 ? 558  PHE   A HE2  1 
ATOM   8519  H  HZ   . PHE   A  1  558 ? 43.578  10.331  -6.892   1.00 128.98 ? 558  PHE   A HZ   1 
ATOM   8520  N  N    . MET   A  1  559 ? 47.440  13.854  -8.541   1.00 95.37  ? 559  MET   A N    1 
ATOM   8521  C  CA   . MET   A  1  559 ? 46.741  14.457  -9.666   1.00 97.84  ? 559  MET   A CA   1 
ATOM   8522  C  C    . MET   A  1  559 ? 45.520  13.617  -9.999   1.00 102.15 ? 559  MET   A C    1 
ATOM   8523  O  O    . MET   A  1  559 ? 45.635  12.409  -10.234  1.00 104.84 ? 559  MET   A O    1 
ATOM   8524  C  CB   . MET   A  1  559 ? 47.649  14.574  -10.895  1.00 95.75  ? 559  MET   A CB   1 
ATOM   8525  C  CG   . MET   A  1  559 ? 46.951  15.142  -12.123  1.00 96.89  ? 559  MET   A CG   1 
ATOM   8526  S  SD   . MET   A  1  559 ? 47.925  14.951  -13.625  1.00 96.47  ? 559  MET   A SD   1 
ATOM   8527  C  CE   . MET   A  1  559 ? 46.695  15.333  -14.868  1.00 98.02  ? 559  MET   A CE   1 
ATOM   8528  H  H    . MET   A  1  559 ? 47.603  13.016  -8.647   1.00 114.43 ? 559  MET   A H    1 
ATOM   8529  H  HA   . MET   A  1  559 ? 46.459  15.352  -9.419   1.00 117.39 ? 559  MET   A HA   1 
ATOM   8530  H  HB2  . MET   A  1  559 ? 48.391  15.161  -10.680  1.00 114.88 ? 559  MET   A HB2  1 
ATOM   8531  H  HB3  . MET   A  1  559 ? 47.979  13.692  -11.124  1.00 114.88 ? 559  MET   A HB3  1 
ATOM   8532  H  HG2  . MET   A  1  559 ? 46.108  14.678  -12.251  1.00 116.25 ? 559  MET   A HG2  1 
ATOM   8533  H  HG3  . MET   A  1  559 ? 46.791  16.089  -11.987  1.00 116.25 ? 559  MET   A HG3  1 
ATOM   8534  H  HE1  . MET   A  1  559 ? 47.115  15.323  -15.742  1.00 117.60 ? 559  MET   A HE1  1 
ATOM   8535  H  HE2  . MET   A  1  559 ? 45.992  14.666  -14.832  1.00 117.60 ? 559  MET   A HE2  1 
ATOM   8536  H  HE3  . MET   A  1  559 ? 46.327  16.212  -14.689  1.00 117.60 ? 559  MET   A HE3  1 
ATOM   8537  N  N    . GLU   A  1  560 ? 44.359  14.262  -10.023  1.00 103.36 ? 560  GLU   A N    1 
ATOM   8538  C  CA   . GLU   A  1  560 ? 43.098  13.640  -10.396  1.00 102.78 ? 560  GLU   A CA   1 
ATOM   8539  C  C    . GLU   A  1  560 ? 42.492  14.442  -11.537  1.00 104.05 ? 560  GLU   A C    1 
ATOM   8540  O  O    . GLU   A  1  560 ? 42.377  15.669  -11.439  1.00 107.79 ? 560  GLU   A O    1 
ATOM   8541  C  CB   . GLU   A  1  560 ? 42.141  13.595  -9.203   1.00 108.74 ? 560  GLU   A CB   1 
ATOM   8542  C  CG   . GLU   A  1  560 ? 40.819  12.903  -9.471   1.00 119.60 ? 560  GLU   A CG   1 
ATOM   8543  C  CD   . GLU   A  1  560 ? 39.924  12.887  -8.248   1.00 131.39 ? 560  GLU   A CD   1 
ATOM   8544  O  OE1  . GLU   A  1  560 ? 40.335  13.438  -7.204   1.00 135.49 ? 560  GLU   A OE1  1 
ATOM   8545  O  OE2  . GLU   A  1  560 ? 38.811  12.325  -8.328   1.00 135.99 ? 560  GLU   A OE2  1 
ATOM   8546  H  H    . GLU   A  1  560 ? 44.275  15.093  -9.818   1.00 124.01 ? 560  GLU   A H    1 
ATOM   8547  H  HA   . GLU   A  1  560 ? 43.243  12.729  -10.698  1.00 123.32 ? 560  GLU   A HA   1 
ATOM   8548  H  HB2  . GLU   A  1  560 ? 42.577  13.121  -8.478   1.00 130.47 ? 560  GLU   A HB2  1 
ATOM   8549  H  HB3  . GLU   A  1  560 ? 41.944  14.506  -8.933   1.00 130.47 ? 560  GLU   A HB3  1 
ATOM   8550  H  HG2  . GLU   A  1  560 ? 40.352  13.371  -10.181  1.00 143.50 ? 560  GLU   A HG2  1 
ATOM   8551  H  HG3  . GLU   A  1  560 ? 40.988  11.985  -9.734   1.00 143.50 ? 560  GLU   A HG3  1 
ATOM   8552  N  N    . TYR   A  1  561 ? 42.117  13.760  -12.617  1.00 102.74 ? 561  TYR   A N    1 
ATOM   8553  C  CA   . TYR   A  1  561 ? 41.531  14.422  -13.774  1.00 104.83 ? 561  TYR   A CA   1 
ATOM   8554  C  C    . TYR   A  1  561 ? 40.190  13.785  -14.099  1.00 106.77 ? 561  TYR   A C    1 
ATOM   8555  O  O    . TYR   A  1  561 ? 40.090  12.560  -14.228  1.00 103.28 ? 561  TYR   A O    1 
ATOM   8556  C  CB   . TYR   A  1  561 ? 42.465  14.367  -14.991  1.00 102.95 ? 561  TYR   A CB   1 
ATOM   8557  C  CG   . TYR   A  1  561 ? 42.736  12.980  -15.525  1.00 99.11  ? 561  TYR   A CG   1 
ATOM   8558  C  CD1  . TYR   A  1  561 ? 43.791  12.222  -15.036  1.00 95.94  ? 561  TYR   A CD1  1 
ATOM   8559  C  CD2  . TYR   A  1  561 ? 41.948  12.436  -16.530  1.00 99.27  ? 561  TYR   A CD2  1 
ATOM   8560  C  CE1  . TYR   A  1  561 ? 44.047  10.957  -15.527  1.00 93.39  ? 561  TYR   A CE1  1 
ATOM   8561  C  CE2  . TYR   A  1  561 ? 42.195  11.172  -17.025  1.00 97.10  ? 561  TYR   A CE2  1 
ATOM   8562  C  CZ   . TYR   A  1  561 ? 43.247  10.438  -16.523  1.00 94.56  ? 561  TYR   A CZ   1 
ATOM   8563  O  OH   . TYR   A  1  561 ? 43.497  9.178   -17.013  1.00 94.58  ? 561  TYR   A OH   1 
ATOM   8564  H  H    . TYR   A  1  561 ? 42.193  12.908  -12.700  1.00 123.26 ? 561  TYR   A H    1 
ATOM   8565  H  HA   . TYR   A  1  561 ? 41.375  15.356  -13.561  1.00 125.77 ? 561  TYR   A HA   1 
ATOM   8566  H  HB2  . TYR   A  1  561 ? 42.064  14.881  -15.709  1.00 123.52 ? 561  TYR   A HB2  1 
ATOM   8567  H  HB3  . TYR   A  1  561 ? 43.318  14.754  -14.741  1.00 123.52 ? 561  TYR   A HB3  1 
ATOM   8568  H  HD1  . TYR   A  1  561 ? 44.335  12.571  -14.368  1.00 115.11 ? 561  TYR   A HD1  1 
ATOM   8569  H  HD2  . TYR   A  1  561 ? 41.242  12.933  -16.876  1.00 119.10 ? 561  TYR   A HD2  1 
ATOM   8570  H  HE1  . TYR   A  1  561 ? 44.754  10.457  -15.188  1.00 112.05 ? 561  TYR   A HE1  1 
ATOM   8571  H  HE2  . TYR   A  1  561 ? 41.654  10.817  -17.693  1.00 116.50 ? 561  TYR   A HE2  1 
ATOM   8572  H  HH   . TYR   A  1  561 ? 44.157  8.841   -16.617  1.00 113.48 ? 561  TYR   A HH   1 
ATOM   8573  N  N    . ARG   A  1  562 ? 39.169  14.625  -14.222  1.00 114.10 ? 562  ARG   A N    1 
ATOM   8574  C  CA   . ARG   A  1  562 ? 37.810  14.214  -14.524  1.00 119.66 ? 562  ARG   A CA   1 
ATOM   8575  C  C    . ARG   A  1  562 ? 37.349  14.942  -15.779  1.00 123.02 ? 562  ARG   A C    1 
ATOM   8576  O  O    . ARG   A  1  562 ? 37.927  15.957  -16.178  1.00 126.08 ? 562  ARG   A O    1 
ATOM   8577  C  CB   . ARG   A  1  562 ? 36.879  14.519  -13.346  1.00 124.09 ? 562  ARG   A CB   1 
ATOM   8578  C  CG   . ARG   A  1  562 ? 35.594  13.714  -13.322  1.00 127.95 ? 562  ARG   A CG   1 
ATOM   8579  C  CD   . ARG   A  1  562 ? 34.793  14.005  -12.060  1.00 131.86 ? 562  ARG   A CD   1 
ATOM   8580  N  NE   . ARG   A  1  562 ? 34.639  15.439  -11.827  1.00 135.40 ? 562  ARG   A NE   1 
ATOM   8581  C  CZ   . ARG   A  1  562 ? 33.844  16.233  -12.538  1.00 138.90 ? 562  ARG   A CZ   1 
ATOM   8582  N  NH1  . ARG   A  1  562 ? 33.130  15.739  -13.541  1.00 139.95 ? 562  ARG   A NH1  1 
ATOM   8583  N  NH2  . ARG   A  1  562 ? 33.769  17.525  -12.251  1.00 140.56 ? 562  ARG   A NH2  1 
ATOM   8584  H  H    . ARG   A  1  562 ? 39.246  15.477  -14.131  1.00 136.90 ? 562  ARG   A H    1 
ATOM   8585  H  HA   . ARG   A  1  562 ? 37.767  13.260  -14.693  1.00 143.57 ? 562  ARG   A HA   1 
ATOM   8586  H  HB2  . ARG   A  1  562 ? 37.355  14.332  -12.521  1.00 148.89 ? 562  ARG   A HB2  1 
ATOM   8587  H  HB3  . ARG   A  1  562 ? 36.634  15.457  -13.382  1.00 148.89 ? 562  ARG   A HB3  1 
ATOM   8588  H  HG2  . ARG   A  1  562 ? 35.051  13.948  -14.091  1.00 153.52 ? 562  ARG   A HG2  1 
ATOM   8589  H  HG3  . ARG   A  1  562 ? 35.805  12.767  -13.340  1.00 153.52 ? 562  ARG   A HG3  1 
ATOM   8590  H  HD2  . ARG   A  1  562 ? 33.909  13.615  -12.146  1.00 158.21 ? 562  ARG   A HD2  1 
ATOM   8591  H  HD3  . ARG   A  1  562 ? 35.252  13.622  -11.296  1.00 158.21 ? 562  ARG   A HD3  1 
ATOM   8592  H  HE   . ARG   A  1  562 ? 35.092  15.793  -11.188  1.00 162.47 ? 562  ARG   A HE   1 
ATOM   8593  H  HH11 . ARG   A  1  562 ? 33.180  14.903  -13.734  1.00 167.92 ? 562  ARG   A HH11 1 
ATOM   8594  H  HH12 . ARG   A  1  562 ? 32.618  16.256  -13.999  1.00 167.92 ? 562  ARG   A HH12 1 
ATOM   8595  H  HH21 . ARG   A  1  562 ? 34.235  17.850  -11.605  1.00 168.65 ? 562  ARG   A HH21 1 
ATOM   8596  H  HH22 . ARG   A  1  562 ? 33.255  18.038  -12.711  1.00 168.65 ? 562  ARG   A HH22 1 
ATOM   8597  N  N    . LEU   A  1  563 ? 36.300  14.414  -16.405  1.00 122.45 ? 563  LEU   A N    1 
ATOM   8598  C  CA   . LEU   A  1  563 ? 35.805  14.932  -17.676  1.00 123.31 ? 563  LEU   A CA   1 
ATOM   8599  C  C    . LEU   A  1  563 ? 34.326  15.254  -17.548  1.00 124.54 ? 563  LEU   A C    1 
ATOM   8600  O  O    . LEU   A  1  563 ? 33.531  14.387  -17.170  1.00 125.80 ? 563  LEU   A O    1 
ATOM   8601  C  CB   . LEU   A  1  563 ? 36.040  13.920  -18.804  1.00 121.41 ? 563  LEU   A CB   1 
ATOM   8602  C  CG   . LEU   A  1  563 ? 35.317  14.153  -20.134  1.00 121.99 ? 563  LEU   A CG   1 
ATOM   8603  C  CD1  . LEU   A  1  563 ? 35.699  15.489  -20.746  1.00 125.76 ? 563  LEU   A CD1  1 
ATOM   8604  C  CD2  . LEU   A  1  563 ? 35.618  13.013  -21.098  1.00 116.57 ? 563  LEU   A CD2  1 
ATOM   8605  H  H    . LEU   A  1  563 ? 35.851  13.744  -16.107  1.00 146.92 ? 563  LEU   A H    1 
ATOM   8606  H  HA   . LEU   A  1  563 ? 36.272  15.755  -17.889  1.00 147.95 ? 563  LEU   A HA   1 
ATOM   8607  H  HB2  . LEU   A  1  563 ? 36.990  13.911  -19.000  1.00 145.67 ? 563  LEU   A HB2  1 
ATOM   8608  H  HB3  . LEU   A  1  563 ? 35.759  13.049  -18.483  1.00 145.67 ? 563  LEU   A HB3  1 
ATOM   8609  H  HG   . LEU   A  1  563 ? 34.361  14.177  -19.971  1.00 146.37 ? 563  LEU   A HG   1 
ATOM   8610  H  HD11 . LEU   A  1  563 ? 35.236  15.593  -21.592  1.00 150.89 ? 563  LEU   A HD11 1 
ATOM   8611  H  HD12 . LEU   A  1  563 ? 35.442  16.200  -20.139  1.00 150.89 ? 563  LEU   A HD12 1 
ATOM   8612  H  HD13 . LEU   A  1  563 ? 36.658  15.507  -20.890  1.00 150.89 ? 563  LEU   A HD13 1 
ATOM   8613  H  HD21 . LEU   A  1  563 ? 35.822  13.383  -21.971  1.00 139.87 ? 563  LEU   A HD21 1 
ATOM   8614  H  HD22 . LEU   A  1  563 ? 36.379  12.512  -20.766  1.00 139.87 ? 563  LEU   A HD22 1 
ATOM   8615  H  HD23 . LEU   A  1  563 ? 34.841  12.436  -21.157  1.00 139.87 ? 563  LEU   A HD23 1 
ATOM   8616  N  N    . ASP   A  1  564 ? 33.959  16.495  -17.862  1.00 125.56 ? 564  ASP   A N    1 
ATOM   8617  C  CA   . ASP   A  1  564 ? 32.552  16.861  -17.990  1.00 129.32 ? 564  ASP   A CA   1 
ATOM   8618  C  C    . ASP   A  1  564 ? 31.980  16.121  -19.193  1.00 132.13 ? 564  ASP   A C    1 
ATOM   8619  O  O    . ASP   A  1  564 ? 32.310  16.438  -20.340  1.00 132.97 ? 564  ASP   A O    1 
ATOM   8620  C  CB   . ASP   A  1  564 ? 32.403  18.371  -18.145  1.00 132.49 ? 564  ASP   A CB   1 
ATOM   8621  C  CG   . ASP   A  1  564 ? 30.965  18.834  -17.994  1.00 138.84 ? 564  ASP   A CG   1 
ATOM   8622  O  OD1  . ASP   A  1  564 ? 30.046  18.043  -18.295  1.00 139.67 ? 564  ASP   A OD1  1 
ATOM   8623  O  OD2  . ASP   A  1  564 ? 30.752  19.991  -17.573  1.00 143.02 ? 564  ASP   A OD2  1 
ATOM   8624  H  H    . ASP   A  1  564 ? 34.507  17.143  -18.004  1.00 150.65 ? 564  ASP   A H    1 
ATOM   8625  H  HA   . ASP   A  1  564 ? 32.066  16.603  -17.191  1.00 155.17 ? 564  ASP   A HA   1 
ATOM   8626  H  HB2  . ASP   A  1  564 ? 32.934  18.813  -17.463  1.00 158.97 ? 564  ASP   A HB2  1 
ATOM   8627  H  HB3  . ASP   A  1  564 ? 32.712  18.631  -19.027  1.00 158.97 ? 564  ASP   A HB3  1 
ATOM   8628  N  N    . TYR   A  1  565 ? 31.134  15.124  -18.937  1.00 133.39 ? 565  TYR   A N    1 
ATOM   8629  C  CA   . TYR   A  1  565 ? 30.691  14.236  -20.005  1.00 134.15 ? 565  TYR   A CA   1 
ATOM   8630  C  C    . TYR   A  1  565 ? 29.623  14.867  -20.893  1.00 144.04 ? 565  TYR   A C    1 
ATOM   8631  O  O    . TYR   A  1  565 ? 29.589  14.589  -22.097  1.00 147.35 ? 565  TYR   A O    1 
ATOM   8632  C  CB   . TYR   A  1  565 ? 30.158  12.929  -19.409  1.00 128.55 ? 565  TYR   A CB   1 
ATOM   8633  C  CG   . TYR   A  1  565 ? 31.218  11.990  -18.859  1.00 123.77 ? 565  TYR   A CG   1 
ATOM   8634  C  CD1  . TYR   A  1  565 ? 32.488  11.926  -19.422  1.00 124.95 ? 565  TYR   A CD1  1 
ATOM   8635  C  CD2  . TYR   A  1  565 ? 30.942  11.159  -17.779  1.00 121.24 ? 565  TYR   A CD2  1 
ATOM   8636  C  CE1  . TYR   A  1  565 ? 33.449  11.067  -18.923  1.00 123.38 ? 565  TYR   A CE1  1 
ATOM   8637  C  CE2  . TYR   A  1  565 ? 31.899  10.297  -17.274  1.00 119.55 ? 565  TYR   A CE2  1 
ATOM   8638  C  CZ   . TYR   A  1  565 ? 33.150  10.255  -17.850  1.00 120.40 ? 565  TYR   A CZ   1 
ATOM   8639  O  OH   . TYR   A  1  565 ? 34.108  9.400   -17.353  1.00 117.03 ? 565  TYR   A OH   1 
ATOM   8640  H  H    . TYR   A  1  565 ? 30.806  14.944  -18.162  1.00 160.05 ? 565  TYR   A H    1 
ATOM   8641  H  HA   . TYR   A  1  565 ? 31.456  14.032  -20.565  1.00 160.97 ? 565  TYR   A HA   1 
ATOM   8642  H  HB2  . TYR   A  1  565 ? 29.557  13.147  -18.680  1.00 154.24 ? 565  TYR   A HB2  1 
ATOM   8643  H  HB3  . TYR   A  1  565 ? 29.678  12.450  -20.103  1.00 154.24 ? 565  TYR   A HB3  1 
ATOM   8644  H  HD1  . TYR   A  1  565 ? 32.694  12.471  -20.147  1.00 149.92 ? 565  TYR   A HD1  1 
ATOM   8645  H  HD2  . TYR   A  1  565 ? 30.098  11.184  -17.389  1.00 145.47 ? 565  TYR   A HD2  1 
ATOM   8646  H  HE1  . TYR   A  1  565 ? 34.295  11.037  -19.310  1.00 148.03 ? 565  TYR   A HE1  1 
ATOM   8647  H  HE2  . TYR   A  1  565 ? 31.699  9.748   -16.550  1.00 143.44 ? 565  TYR   A HE2  1 
ATOM   8648  H  HH   . TYR   A  1  565 ? 33.811  8.998   -16.677  1.00 140.42 ? 565  TYR   A HH   1 
ATOM   8649  N  N    . ARG   A  1  566 ? 28.752  15.710  -20.334  1.00 148.49 ? 566  ARG   A N    1 
ATOM   8650  C  CA   . ARG   A  1  566 ? 27.615  16.205  -21.104  1.00 152.06 ? 566  ARG   A CA   1 
ATOM   8651  C  C    . ARG   A  1  566 ? 28.049  17.041  -22.302  1.00 156.09 ? 566  ARG   A C    1 
ATOM   8652  O  O    . ARG   A  1  566 ? 27.372  17.039  -23.336  1.00 156.98 ? 566  ARG   A O    1 
ATOM   8653  C  CB   . ARG   A  1  566 ? 26.686  17.027  -20.209  1.00 150.07 ? 566  ARG   A CB   1 
ATOM   8654  C  CG   . ARG   A  1  566 ? 25.979  16.222  -19.132  1.00 143.86 ? 566  ARG   A CG   1 
ATOM   8655  C  CD   . ARG   A  1  566 ? 24.930  17.056  -18.403  1.00 144.42 ? 566  ARG   A CD   1 
ATOM   8656  N  NE   . ARG   A  1  566 ? 23.766  17.344  -19.240  1.00 147.21 ? 566  ARG   A NE   1 
ATOM   8657  C  CZ   . ARG   A  1  566 ? 23.601  18.450  -19.963  1.00 149.12 ? 566  ARG   A CZ   1 
ATOM   8658  N  NH1  . ARG   A  1  566 ? 24.525  19.403  -19.971  1.00 149.85 ? 566  ARG   A NH1  1 
ATOM   8659  N  NH2  . ARG   A  1  566 ? 22.501  18.604  -20.686  1.00 150.82 ? 566  ARG   A NH2  1 
ATOM   8660  H  H    . ARG   A  1  566 ? 28.798  16.005  -19.527  1.00 178.16 ? 566  ARG   A H    1 
ATOM   8661  H  HA   . ARG   A  1  566 ? 27.122  15.438  -21.437  1.00 182.46 ? 566  ARG   A HA   1 
ATOM   8662  H  HB2  . ARG   A  1  566 ? 27.210  17.713  -19.766  1.00 180.07 ? 566  ARG   A HB2  1 
ATOM   8663  H  HB3  . ARG   A  1  566 ? 26.004  17.437  -20.764  1.00 180.07 ? 566  ARG   A HB3  1 
ATOM   8664  H  HG2  . ARG   A  1  566 ? 25.534  15.462  -19.539  1.00 172.61 ? 566  ARG   A HG2  1 
ATOM   8665  H  HG3  . ARG   A  1  566 ? 26.630  15.915  -18.481  1.00 172.61 ? 566  ARG   A HG3  1 
ATOM   8666  H  HD2  . ARG   A  1  566 ? 24.626  16.570  -17.621  1.00 173.29 ? 566  ARG   A HD2  1 
ATOM   8667  H  HD3  . ARG   A  1  566 ? 25.326  17.900  -18.136  1.00 173.29 ? 566  ARG   A HD3  1 
ATOM   8668  H  HE   . ARG   A  1  566 ? 23.140  16.755  -19.267  1.00 176.64 ? 566  ARG   A HE   1 
ATOM   8669  H  HH11 . ARG   A  1  566 ? 25.242  19.311  -19.505  1.00 179.80 ? 566  ARG   A HH11 1 
ATOM   8670  H  HH12 . ARG   A  1  566 ? 24.407  20.113  -20.442  1.00 179.80 ? 566  ARG   A HH12 1 
ATOM   8671  H  HH21 . ARG   A  1  566 ? 21.897  17.991  -20.685  1.00 180.96 ? 566  ARG   A HH21 1 
ATOM   8672  H  HH22 . ARG   A  1  566 ? 22.390  19.316  -21.154  1.00 180.96 ? 566  ARG   A HH22 1 
ATOM   8673  N  N    . THR   A  1  567 ? 29.168  17.760  -22.189  1.00 156.97 ? 567  THR   A N    1 
ATOM   8674  C  CA   . THR   A  1  567 ? 29.535  18.710  -23.235  1.00 158.30 ? 567  THR   A CA   1 
ATOM   8675  C  C    . THR   A  1  567 ? 29.983  18.013  -24.515  1.00 157.28 ? 567  THR   A C    1 
ATOM   8676  O  O    . THR   A  1  567 ? 29.839  18.578  -25.605  1.00 163.04 ? 567  THR   A O    1 
ATOM   8677  C  CB   . THR   A  1  567 ? 30.637  19.647  -22.733  1.00 153.90 ? 567  THR   A CB   1 
ATOM   8678  O  OG1  . THR   A  1  567 ? 30.978  20.584  -23.762  1.00 155.70 ? 567  THR   A OG1  1 
ATOM   8679  C  CG2  . THR   A  1  567 ? 31.881  18.863  -22.331  1.00 146.79 ? 567  THR   A CG2  1 
ATOM   8680  H  H    . THR   A  1  567 ? 29.718  17.718  -21.530  1.00 188.34 ? 567  THR   A H    1 
ATOM   8681  H  HA   . THR   A  1  567 ? 28.754  19.244  -23.447  1.00 189.94 ? 567  THR   A HA   1 
ATOM   8682  H  HB   . THR   A  1  567 ? 30.316  20.123  -21.951  1.00 184.66 ? 567  THR   A HB   1 
ATOM   8683  H  HG1  . THR   A  1  567 ? 31.502  21.166  -23.458  1.00 186.82 ? 567  THR   A HG1  1 
ATOM   8684  H  HG21 . THR   A  1  567 ? 32.572  19.472  -22.025  1.00 176.13 ? 567  THR   A HG21 1 
ATOM   8685  H  HG22 . THR   A  1  567 ? 31.667  18.244  -21.616  1.00 176.13 ? 567  THR   A HG22 1 
ATOM   8686  H  HG23 . THR   A  1  567 ? 32.217  18.363  -23.091  1.00 176.13 ? 567  THR   A HG23 1 
ATOM   8687  N  N    . ALA   A  1  568 ? 30.517  16.795  -24.412  1.00 147.84 ? 568  ALA   A N    1 
ATOM   8688  C  CA   . ALA   A  1  568 ? 31.062  16.076  -25.558  1.00 139.44 ? 568  ALA   A CA   1 
ATOM   8689  C  C    . ALA   A  1  568 ? 30.057  15.104  -26.170  1.00 137.63 ? 568  ALA   A C    1 
ATOM   8690  O  O    . ALA   A  1  568 ? 30.449  14.071  -26.721  1.00 133.14 ? 568  ALA   A O    1 
ATOM   8691  C  CB   . ALA   A  1  568 ? 32.335  15.333  -25.153  1.00 130.98 ? 568  ALA   A CB   1 
ATOM   8692  H  H    . ALA   A  1  568 ? 30.575  16.359  -23.674  1.00 177.39 ? 568  ALA   A H    1 
ATOM   8693  H  HA   . ALA   A  1  568 ? 31.293  16.724  -26.242  1.00 167.30 ? 568  ALA   A HA   1 
ATOM   8694  H  HB1  . ALA   A  1  568 ? 32.686  14.862  -25.926  1.00 157.15 ? 568  ALA   A HB1  1 
ATOM   8695  H  HB2  . ALA   A  1  568 ? 32.988  15.975  -24.834  1.00 157.15 ? 568  ALA   A HB2  1 
ATOM   8696  H  HB3  . ALA   A  1  568 ? 32.122  14.700  -24.450  1.00 157.15 ? 568  ALA   A HB3  1 
ATOM   8697  N  N    . ALA   A  1  569 ? 28.767  15.424  -26.099  1.00 141.79 ? 569  ALA   A N    1 
ATOM   8698  C  CA   . ALA   A  1  569 ? 27.736  14.524  -26.591  1.00 143.41 ? 569  ALA   A CA   1 
ATOM   8699  C  C    . ALA   A  1  569 ? 27.769  14.459  -28.119  1.00 145.85 ? 569  ALA   A C    1 
ATOM   8700  O  O    . ALA   A  1  569 ? 28.617  15.063  -28.782  1.00 148.22 ? 569  ALA   A O    1 
ATOM   8701  C  CB   . ALA   A  1  569 ? 26.364  14.972  -26.095  1.00 146.33 ? 569  ALA   A CB   1 
ATOM   8702  H  H    . ALA   A  1  569 ? 28.465  16.159  -25.770  1.00 170.13 ? 569  ALA   A H    1 
ATOM   8703  H  HA   . ALA   A  1  569 ? 27.911  13.634  -26.247  1.00 172.08 ? 569  ALA   A HA   1 
ATOM   8704  H  HB1  . ALA   A  1  569 ? 25.692  14.353  -26.421  1.00 175.58 ? 569  ALA   A HB1  1 
ATOM   8705  H  HB2  . ALA   A  1  569 ? 26.365  14.977  -25.125  1.00 175.58 ? 569  ALA   A HB2  1 
ATOM   8706  H  HB3  . ALA   A  1  569 ? 26.183  15.864  -26.430  1.00 175.58 ? 569  ALA   A HB3  1 
ATOM   8707  N  N    . ASP   A  1  570 ? 26.824  13.705  -28.681  1.00 145.34 ? 570  ASP   A N    1 
ATOM   8708  C  CA   . ASP   A  1  570 ? 26.724  13.509  -30.120  1.00 146.58 ? 570  ASP   A CA   1 
ATOM   8709  C  C    . ASP   A  1  570 ? 25.266  13.622  -30.541  1.00 143.59 ? 570  ASP   A C    1 
ATOM   8710  O  O    . ASP   A  1  570 ? 24.362  13.746  -29.710  1.00 142.78 ? 570  ASP   A O    1 
ATOM   8711  C  CB   . ASP   A  1  570 ? 27.303  12.150  -30.536  1.00 149.68 ? 570  ASP   A CB   1 
ATOM   8712  C  CG   . ASP   A  1  570 ? 28.816  12.157  -30.596  1.00 151.22 ? 570  ASP   A CG   1 
ATOM   8713  O  OD1  . ASP   A  1  570 ? 29.377  13.003  -31.325  1.00 154.59 ? 570  ASP   A OD1  1 
ATOM   8714  O  OD2  . ASP   A  1  570 ? 29.444  11.323  -29.911  1.00 148.51 ? 570  ASP   A OD2  1 
ATOM   8715  H  H    . ASP   A  1  570 ? 26.217  13.289  -28.236  1.00 174.39 ? 570  ASP   A H    1 
ATOM   8716  H  HA   . ASP   A  1  570 ? 27.222  14.207  -30.573  1.00 175.88 ? 570  ASP   A HA   1 
ATOM   8717  H  HB2  . ASP   A  1  570 ? 27.031  11.479  -29.891  1.00 179.60 ? 570  ASP   A HB2  1 
ATOM   8718  H  HB3  . ASP   A  1  570 ? 26.968  11.919  -31.417  1.00 179.60 ? 570  ASP   A HB3  1 
ATOM   8719  N  N    . THR   A  1  571 ? 25.042  13.583  -31.859  1.00 142.09 ? 571  THR   A N    1 
ATOM   8720  C  CA   . THR   A  1  571 ? 23.678  13.630  -32.378  1.00 143.35 ? 571  THR   A CA   1 
ATOM   8721  C  C    . THR   A  1  571 ? 22.816  12.527  -31.780  1.00 147.82 ? 571  THR   A C    1 
ATOM   8722  O  O    . THR   A  1  571 ? 21.612  12.720  -31.574  1.00 151.73 ? 571  THR   A O    1 
ATOM   8723  C  CB   . THR   A  1  571 ? 23.687  13.520  -33.905  1.00 137.28 ? 571  THR   A CB   1 
ATOM   8724  O  OG1  . THR   A  1  571 ? 22.341  13.430  -34.389  1.00 137.78 ? 571  THR   A OG1  1 
ATOM   8725  C  CG2  . THR   A  1  571 ? 24.473  12.293  -34.363  1.00 131.20 ? 571  THR   A CG2  1 
ATOM   8726  H  H    . THR   A  1  571 ? 25.653  13.531  -32.461  1.00 170.48 ? 571  THR   A H    1 
ATOM   8727  H  HA   . THR   A  1  571 ? 23.287  14.485  -32.142  1.00 172.00 ? 571  THR   A HA   1 
ATOM   8728  H  HB   . THR   A  1  571 ? 24.116  14.307  -34.278  1.00 164.72 ? 571  THR   A HB   1 
ATOM   8729  H  HG1  . THR   A  1  571 ? 22.342  13.315  -35.221  1.00 165.31 ? 571  THR   A HG1  1 
ATOM   8730  H  HG21 . THR   A  1  571 ? 24.415  12.203  -35.327  1.00 157.42 ? 571  THR   A HG21 1 
ATOM   8731  H  HG22 . THR   A  1  571 ? 25.405  12.383  -34.111  1.00 157.42 ? 571  THR   A HG22 1 
ATOM   8732  H  HG23 . THR   A  1  571 ? 24.111  11.494  -33.949  1.00 157.42 ? 571  THR   A HG23 1 
ATOM   8733  N  N    . THR   A  1  572 ? 23.411  11.367  -31.497  1.00 144.93 ? 572  THR   A N    1 
ATOM   8734  C  CA   . THR   A  1  572 ? 22.682  10.296  -30.832  1.00 139.83 ? 572  THR   A CA   1 
ATOM   8735  C  C    . THR   A  1  572 ? 22.216  10.697  -29.440  1.00 138.76 ? 572  THR   A C    1 
ATOM   8736  O  O    . THR   A  1  572 ? 21.261  10.107  -28.923  1.00 136.47 ? 572  THR   A O    1 
ATOM   8737  C  CB   . THR   A  1  572 ? 23.568  9.053   -30.726  1.00 130.51 ? 572  THR   A CB   1 
ATOM   8738  O  OG1  . THR   A  1  572 ? 24.853  9.426   -30.210  1.00 120.85 ? 572  THR   A OG1  1 
ATOM   8739  C  CG2  . THR   A  1  572 ? 23.739  8.391   -32.086  1.00 132.36 ? 572  THR   A CG2  1 
ATOM   8740  H  H    . THR   A  1  572 ? 24.230  11.179  -31.679  1.00 173.90 ? 572  THR   A H    1 
ATOM   8741  H  HA   . THR   A  1  572 ? 21.902  10.077  -31.364  1.00 167.78 ? 572  THR   A HA   1 
ATOM   8742  H  HB   . THR   A  1  572 ? 23.152  8.410   -30.130  1.00 156.59 ? 572  THR   A HB   1 
ATOM   8743  H  HG1  . THR   A  1  572 ? 25.337  8.744   -30.123  1.00 145.01 ? 572  THR   A HG1  1 
ATOM   8744  H  HG21 . THR   A  1  572 ? 24.292  7.598   -32.002  1.00 158.81 ? 572  THR   A HG21 1 
ATOM   8745  H  HG22 . THR   A  1  572 ? 22.873  8.134   -32.441  1.00 158.81 ? 572  THR   A HG22 1 
ATOM   8746  H  HG23 . THR   A  1  572 ? 24.162  9.007   -32.704  1.00 158.81 ? 572  THR   A HG23 1 
ATOM   8747  N  N    . GLY   A  1  573 ? 22.856  11.690  -28.830  1.00 138.28 ? 573  GLY   A N    1 
ATOM   8748  C  CA   . GLY   A  1  573 ? 22.691  11.950  -27.419  1.00 131.75 ? 573  GLY   A CA   1 
ATOM   8749  C  C    . GLY   A  1  573 ? 23.603  11.128  -26.542  1.00 118.69 ? 573  GLY   A C    1 
ATOM   8750  O  O    . GLY   A  1  573 ? 23.394  11.081  -25.324  1.00 116.00 ? 573  GLY   A O    1 
ATOM   8751  H  H    . GLY   A  1  573 ? 23.398  12.230  -29.224  1.00 165.91 ? 573  GLY   A H    1 
ATOM   8752  H  HA2  . GLY   A  1  573 ? 22.872  12.888  -27.247  1.00 158.08 ? 573  GLY   A HA2  1 
ATOM   8753  H  HA3  . GLY   A  1  573 ? 21.774  11.755  -27.167  1.00 158.08 ? 573  GLY   A HA3  1 
ATOM   8754  N  N    . LEU   A  1  574 ? 24.615  10.489  -27.124  1.00 110.36 ? 574  LEU   A N    1 
ATOM   8755  C  CA   . LEU   A  1  574 ? 25.446  9.507   -26.439  1.00 103.83 ? 574  LEU   A CA   1 
ATOM   8756  C  C    . LEU   A  1  574 ? 26.754  10.174  -26.033  1.00 103.50 ? 574  LEU   A C    1 
ATOM   8757  O  O    . LEU   A  1  574 ? 27.575  10.522  -26.888  1.00 102.18 ? 574  LEU   A O    1 
ATOM   8758  C  CB   . LEU   A  1  574 ? 25.695  8.305   -27.347  1.00 102.56 ? 574  LEU   A CB   1 
ATOM   8759  C  CG   . LEU   A  1  574 ? 25.912  6.942   -26.688  1.00 99.84  ? 574  LEU   A CG   1 
ATOM   8760  C  CD1  . LEU   A  1  574 ? 24.697  6.523   -25.875  1.00 101.83 ? 574  LEU   A CD1  1 
ATOM   8761  C  CD2  . LEU   A  1  574 ? 26.219  5.907   -27.757  1.00 100.71 ? 574  LEU   A CD2  1 
ATOM   8762  H  H    . LEU   A  1  574 ? 24.846  10.612  -27.943  1.00 132.41 ? 574  LEU   A H    1 
ATOM   8763  H  HA   . LEU   A  1  574 ? 25.000  9.203   -25.633  1.00 124.58 ? 574  LEU   A HA   1 
ATOM   8764  H  HB2  . LEU   A  1  574 ? 24.927  8.213   -27.932  1.00 123.06 ? 574  LEU   A HB2  1 
ATOM   8765  H  HB3  . LEU   A  1  574 ? 26.491  8.491   -27.870  1.00 123.06 ? 574  LEU   A HB3  1 
ATOM   8766  H  HG   . LEU   A  1  574 ? 26.662  7.000   -26.077  1.00 119.79 ? 574  LEU   A HG   1 
ATOM   8767  H  HD11 . LEU   A  1  574 ? 24.829  5.617   -25.554  1.00 122.18 ? 574  LEU   A HD11 1 
ATOM   8768  H  HD12 . LEU   A  1  574 ? 24.596  7.129   -25.124  1.00 122.18 ? 574  LEU   A HD12 1 
ATOM   8769  H  HD13 . LEU   A  1  574 ? 23.910  6.563   -26.440  1.00 122.18 ? 574  LEU   A HD13 1 
ATOM   8770  H  HD21 . LEU   A  1  574 ? 26.345  5.043   -27.333  1.00 120.84 ? 574  LEU   A HD21 1 
ATOM   8771  H  HD22 . LEU   A  1  574 ? 25.476  5.864   -28.379  1.00 120.84 ? 574  LEU   A HD22 1 
ATOM   8772  H  HD23 . LEU   A  1  574 ? 27.028  6.166   -28.225  1.00 120.84 ? 574  LEU   A HD23 1 
ATOM   8773  N  N    . GLN   A  1  575 ? 26.944  10.351  -24.732  1.00 106.54 ? 575  GLN   A N    1 
ATOM   8774  C  CA   . GLN   A  1  575 ? 28.155  10.973  -24.228  1.00 107.89 ? 575  GLN   A CA   1 
ATOM   8775  C  C    . GLN   A  1  575 ? 29.295  9.956   -24.195  1.00 103.77 ? 575  GLN   A C    1 
ATOM   8776  O  O    . GLN   A  1  575 ? 29.067  8.768   -23.959  1.00 103.33 ? 575  GLN   A O    1 
ATOM   8777  C  CB   . GLN   A  1  575 ? 27.925  11.523  -22.824  1.00 113.46 ? 575  GLN   A CB   1 
ATOM   8778  C  CG   . GLN   A  1  575 ? 26.671  12.372  -22.675  1.00 124.29 ? 575  GLN   A CG   1 
ATOM   8779  C  CD   . GLN   A  1  575 ? 26.304  12.608  -21.224  1.00 130.60 ? 575  GLN   A CD   1 
ATOM   8780  O  OE1  . GLN   A  1  575 ? 27.034  12.212  -20.315  1.00 129.20 ? 575  GLN   A OE1  1 
ATOM   8781  N  NE2  . GLN   A  1  575 ? 25.164  13.251  -20.999  1.00 137.25 ? 575  GLN   A NE2  1 
ATOM   8782  H  H    . GLN   A  1  575 ? 26.386  10.118  -24.121  1.00 127.83 ? 575  GLN   A H    1 
ATOM   8783  H  HA   . GLN   A  1  575 ? 28.411  11.710  -24.805  1.00 129.44 ? 575  GLN   A HA   1 
ATOM   8784  H  HB2  . GLN   A  1  575 ? 27.849  10.777  -22.209  1.00 136.13 ? 575  GLN   A HB2  1 
ATOM   8785  H  HB3  . GLN   A  1  575 ? 28.684  12.077  -22.581  1.00 136.13 ? 575  GLN   A HB3  1 
ATOM   8786  H  HG2  . GLN   A  1  575 ? 26.820  13.235  -23.093  1.00 149.13 ? 575  GLN   A HG2  1 
ATOM   8787  H  HG3  . GLN   A  1  575 ? 25.928  11.919  -23.104  1.00 149.13 ? 575  GLN   A HG3  1 
ATOM   8788  H  HE21 . GLN   A  1  575 ? 24.678  13.510  -21.660  1.00 164.68 ? 575  GLN   A HE21 1 
ATOM   8789  H  HE22 . GLN   A  1  575 ? 24.912  13.409  -20.192  1.00 164.68 ? 575  GLN   A HE22 1 
ATOM   8790  N  N    . PRO   A  1  576 ? 30.528  10.394  -24.433  1.00 101.93 ? 576  PRO   A N    1 
ATOM   8791  C  CA   . PRO   A  1  576 ? 31.672  9.487   -24.292  1.00 99.79  ? 576  PRO   A CA   1 
ATOM   8792  C  C    . PRO   A  1  576 ? 31.987  9.241   -22.826  1.00 98.48  ? 576  PRO   A C    1 
ATOM   8793  O  O    . PRO   A  1  576 ? 31.523  9.948   -21.928  1.00 101.28 ? 576  PRO   A O    1 
ATOM   8794  C  CB   . PRO   A  1  576 ? 32.807  10.234  -24.995  1.00 99.99  ? 576  PRO   A CB   1 
ATOM   8795  C  CG   . PRO   A  1  576 ? 32.454  11.669  -24.835  1.00 101.16 ? 576  PRO   A CG   1 
ATOM   8796  C  CD   . PRO   A  1  576 ? 30.947  11.738  -24.869  1.00 102.76 ? 576  PRO   A CD   1 
ATOM   8797  H  HA   . PRO   A  1  576 ? 31.512  8.643   -24.742  1.00 119.73 ? 576  PRO   A HA   1 
ATOM   8798  H  HB2  . PRO   A  1  576 ? 33.654  10.033  -24.568  1.00 119.97 ? 576  PRO   A HB2  1 
ATOM   8799  H  HB3  . PRO   A  1  576 ? 32.840  9.985   -25.932  1.00 119.97 ? 576  PRO   A HB3  1 
ATOM   8800  H  HG2  . PRO   A  1  576 ? 32.792  11.995  -23.986  1.00 121.37 ? 576  PRO   A HG2  1 
ATOM   8801  H  HG3  . PRO   A  1  576 ? 32.836  12.182  -25.564  1.00 121.37 ? 576  PRO   A HG3  1 
ATOM   8802  H  HD2  . PRO   A  1  576 ? 30.619  12.416  -24.257  1.00 123.29 ? 576  PRO   A HD2  1 
ATOM   8803  H  HD3  . PRO   A  1  576 ? 30.631  11.922  -25.767  1.00 123.29 ? 576  PRO   A HD3  1 
ATOM   8804  N  N    . ILE   A  1  577 ? 32.796  8.212   -22.588  1.00 95.52  ? 577  ILE   A N    1 
ATOM   8805  C  CA   . ILE   A  1  577 ? 33.187  7.821   -21.243  1.00 95.50  ? 577  ILE   A CA   1 
ATOM   8806  C  C    . ILE   A  1  577 ? 34.687  7.572   -21.222  1.00 95.02  ? 577  ILE   A C    1 
ATOM   8807  O  O    . ILE   A  1  577 ? 35.280  7.140   -22.216  1.00 95.19  ? 577  ILE   A O    1 
ATOM   8808  C  CB   . ILE   A  1  577 ? 32.418  6.569   -20.762  1.00 99.04  ? 577  ILE   A CB   1 
ATOM   8809  C  CG1  . ILE   A  1  577 ? 32.691  6.314   -19.277  1.00 97.89  ? 577  ILE   A CG1  1 
ATOM   8810  C  CG2  . ILE   A  1  577 ? 32.805  5.352   -21.593  1.00 101.65 ? 577  ILE   A CG2  1 
ATOM   8811  C  CD1  . ILE   A  1  577 ? 31.850  5.204   -18.683  1.00 98.51  ? 577  ILE   A CD1  1 
ATOM   8812  H  H    . ILE   A  1  577 ? 33.136  7.717   -23.204  1.00 114.61 ? 577  ILE   A H    1 
ATOM   8813  H  HA   . ILE   A  1  577 ? 32.993  8.547   -20.630  1.00 114.59 ? 577  ILE   A HA   1 
ATOM   8814  H  HB   . ILE   A  1  577 ? 31.469  6.730   -20.878  1.00 118.83 ? 577  ILE   A HB   1 
ATOM   8815  H  HG12 . ILE   A  1  577 ? 33.623  6.069   -19.169  1.00 117.45 ? 577  ILE   A HG12 1 
ATOM   8816  H  HG13 . ILE   A  1  577 ? 32.501  7.126   -18.782  1.00 117.45 ? 577  ILE   A HG13 1 
ATOM   8817  H  HG21 . ILE   A  1  577 ? 32.208  4.619   -21.376  1.00 121.97 ? 577  ILE   A HG21 1 
ATOM   8818  H  HG22 . ILE   A  1  577 ? 32.727  5.575   -22.534  1.00 121.97 ? 577  ILE   A HG22 1 
ATOM   8819  H  HG23 . ILE   A  1  577 ? 33.720  5.106   -21.387  1.00 121.97 ? 577  ILE   A HG23 1 
ATOM   8820  H  HD11 . ILE   A  1  577 ? 32.029  5.148   -17.731  1.00 118.19 ? 577  ILE   A HD11 1 
ATOM   8821  H  HD12 . ILE   A  1  577 ? 30.913  5.404   -18.832  1.00 118.19 ? 577  ILE   A HD12 1 
ATOM   8822  H  HD13 . ILE   A  1  577 ? 32.083  4.367   -19.114  1.00 118.19 ? 577  ILE   A HD13 1 
ATOM   8823  N  N    . LEU   A  1  578 ? 35.300  7.853   -20.076  1.00 95.05  ? 578  LEU   A N    1 
ATOM   8824  C  CA   . LEU   A  1  578 ? 36.729  7.629   -19.919  1.00 94.13  ? 578  LEU   A CA   1 
ATOM   8825  C  C    . LEU   A  1  578 ? 37.022  6.139   -19.803  1.00 90.85  ? 578  LEU   A C    1 
ATOM   8826  O  O    . LEU   A  1  578 ? 36.287  5.394   -19.149  1.00 88.45  ? 578  LEU   A O    1 
ATOM   8827  C  CB   . LEU   A  1  578 ? 37.250  8.360   -18.683  1.00 94.39  ? 578  LEU   A CB   1 
ATOM   8828  C  CG   . LEU   A  1  578 ? 37.227  9.888   -18.744  1.00 98.00  ? 578  LEU   A CG   1 
ATOM   8829  C  CD1  . LEU   A  1  578 ? 37.631  10.487  -17.405  1.00 97.49  ? 578  LEU   A CD1  1 
ATOM   8830  C  CD2  . LEU   A  1  578 ? 38.143  10.389  -19.849  1.00 99.48  ? 578  LEU   A CD2  1 
ATOM   8831  H  H    . LEU   A  1  578 ? 34.912  8.173   -19.379  1.00 114.04 ? 578  LEU   A H    1 
ATOM   8832  H  HA   . LEU   A  1  578 ? 37.197  7.976   -20.695  1.00 112.94 ? 578  LEU   A HA   1 
ATOM   8833  H  HB2  . LEU   A  1  578 ? 36.706  8.096   -17.924  1.00 113.25 ? 578  LEU   A HB2  1 
ATOM   8834  H  HB3  . LEU   A  1  578 ? 38.171  8.093   -18.539  1.00 113.25 ? 578  LEU   A HB3  1 
ATOM   8835  H  HG   . LEU   A  1  578 ? 36.324  10.181  -18.942  1.00 117.58 ? 578  LEU   A HG   1 
ATOM   8836  H  HD11 . LEU   A  1  578 ? 37.623  11.454  -17.477  1.00 116.97 ? 578  LEU   A HD11 1 
ATOM   8837  H  HD12 . LEU   A  1  578 ? 36.998  10.200  -16.728  1.00 116.97 ? 578  LEU   A HD12 1 
ATOM   8838  H  HD13 . LEU   A  1  578 ? 38.522  10.179  -17.177  1.00 116.97 ? 578  LEU   A HD13 1 
ATOM   8839  H  HD21 . LEU   A  1  578 ? 38.189  11.357  -19.807  1.00 119.35 ? 578  LEU   A HD21 1 
ATOM   8840  H  HD22 . LEU   A  1  578 ? 39.027  10.010  -19.722  1.00 119.35 ? 578  LEU   A HD22 1 
ATOM   8841  H  HD23 . LEU   A  1  578 ? 37.784  10.111  -20.706  1.00 119.35 ? 578  LEU   A HD23 1 
ATOM   8842  N  N    . ASN   A  1  579 ? 38.101  5.707   -20.450  1.00 91.50  ? 579  ASN   A N    1 
ATOM   8843  C  CA   . ASN   A  1  579 ? 38.531  4.318   -20.360  1.00 90.50  ? 579  ASN   A CA   1 
ATOM   8844  C  C    . ASN   A  1  579 ? 38.707  3.919   -18.902  1.00 88.86  ? 579  ASN   A C    1 
ATOM   8845  O  O    . ASN   A  1  579 ? 39.576  4.448   -18.202  1.00 87.79  ? 579  ASN   A O    1 
ATOM   8846  C  CB   . ASN   A  1  579 ? 39.839  4.125   -21.131  1.00 89.77  ? 579  ASN   A CB   1 
ATOM   8847  C  CG   . ASN   A  1  579 ? 40.237  2.665   -21.255  1.00 89.34  ? 579  ASN   A CG   1 
ATOM   8848  O  OD1  . ASN   A  1  579 ? 39.794  1.818   -20.479  1.00 87.73  ? 579  ASN   A OD1  1 
ATOM   8849  N  ND2  . ASN   A  1  579 ? 41.084  2.366   -22.233  1.00 90.09  ? 579  ASN   A ND2  1 
ATOM   8850  H  H    . ASN   A  1  579 ? 38.601  6.199   -20.948  1.00 109.78 ? 579  ASN   A H    1 
ATOM   8851  H  HA   . ASN   A  1  579 ? 37.860  3.743   -20.761  1.00 108.58 ? 579  ASN   A HA   1 
ATOM   8852  H  HB2  . ASN   A  1  579 ? 39.734  4.485   -22.026  1.00 107.71 ? 579  ASN   A HB2  1 
ATOM   8853  H  HB3  . ASN   A  1  579 ? 40.551  4.592   -20.667  1.00 107.71 ? 579  ASN   A HB3  1 
ATOM   8854  H  HD21 . ASN   A  1  579 ? 41.341  1.553   -22.346  1.00 108.09 ? 579  ASN   A HD21 1 
ATOM   8855  H  HD22 . ASN   A  1  579 ? 41.375  2.985   -22.755  1.00 108.09 ? 579  ASN   A HD22 1 
ATOM   8856  N  N    . GLN   A  1  580 ? 37.877  2.980   -18.447  1.00 91.66  ? 580  GLN   A N    1 
ATOM   8857  C  CA   . GLN   A  1  580 ? 37.874  2.585   -17.045  1.00 92.73  ? 580  GLN   A CA   1 
ATOM   8858  C  C    . GLN   A  1  580 ? 39.090  1.754   -16.659  1.00 89.80  ? 580  GLN   A C    1 
ATOM   8859  O  O    . GLN   A  1  580 ? 39.338  1.573   -15.462  1.00 88.37  ? 580  GLN   A O    1 
ATOM   8860  C  CB   . GLN   A  1  580 ? 36.594  1.806   -16.738  1.00 98.76  ? 580  GLN   A CB   1 
ATOM   8861  C  CG   . GLN   A  1  580 ? 36.356  1.539   -15.261  1.00 103.35 ? 580  GLN   A CG   1 
ATOM   8862  C  CD   . GLN   A  1  580 ? 34.880  1.532   -14.908  1.00 108.78 ? 580  GLN   A CD   1 
ATOM   8863  O  OE1  . GLN   A  1  580 ? 34.124  2.406   -15.334  1.00 111.41 ? 580  GLN   A OE1  1 
ATOM   8864  N  NE2  . GLN   A  1  580 ? 34.461  0.541   -14.130  1.00 108.49 ? 580  GLN   A NE2  1 
ATOM   8865  H  H    . GLN   A  1  580 ? 37.307  2.558   -18.933  1.00 109.97 ? 580  GLN   A H    1 
ATOM   8866  H  HA   . GLN   A  1  580 ? 37.884  3.383   -16.494  1.00 111.26 ? 580  GLN   A HA   1 
ATOM   8867  H  HB2  . GLN   A  1  580 ? 35.837  2.314   -17.069  1.00 118.50 ? 580  GLN   A HB2  1 
ATOM   8868  H  HB3  . GLN   A  1  580 ? 36.639  0.948   -17.187  1.00 118.50 ? 580  GLN   A HB3  1 
ATOM   8869  H  HG2  . GLN   A  1  580 ? 36.725  0.673   -15.031  1.00 124.00 ? 580  GLN   A HG2  1 
ATOM   8870  H  HG3  . GLN   A  1  580 ? 36.788  2.233   -14.739  1.00 124.00 ? 580  GLN   A HG3  1 
ATOM   8871  H  HE21 . GLN   A  1  580 ? 35.018  -0.053  -13.854  1.00 130.17 ? 580  GLN   A HE21 1 
ATOM   8872  H  HE22 . GLN   A  1  580 ? 33.633  0.494   -13.902  1.00 130.17 ? 580  GLN   A HE22 1 
ATOM   8873  N  N    . PHE   A  1  581 ? 39.855  1.257   -17.631  1.00 93.59  ? 581  PHE   A N    1 
ATOM   8874  C  CA   . PHE   A  1  581 ? 41.006  0.413   -17.339  1.00 98.23  ? 581  PHE   A CA   1 
ATOM   8875  C  C    . PHE   A  1  581 ? 42.295  1.203   -17.152  1.00 102.86 ? 581  PHE   A C    1 
ATOM   8876  O  O    . PHE   A  1  581 ? 43.259  0.660   -16.601  1.00 104.13 ? 581  PHE   A O    1 
ATOM   8877  C  CB   . PHE   A  1  581 ? 41.195  -0.620  -18.456  1.00 98.72  ? 581  PHE   A CB   1 
ATOM   8878  C  CG   . PHE   A  1  581 ? 40.047  -1.585  -18.588  1.00 96.31  ? 581  PHE   A CG   1 
ATOM   8879  C  CD1  . PHE   A  1  581 ? 39.406  -2.084  -17.464  1.00 90.53  ? 581  PHE   A CD1  1 
ATOM   8880  C  CD2  . PHE   A  1  581 ? 39.605  -1.989  -19.837  1.00 96.49  ? 581  PHE   A CD2  1 
ATOM   8881  C  CE1  . PHE   A  1  581 ? 38.351  -2.969  -17.584  1.00 88.84  ? 581  PHE   A CE1  1 
ATOM   8882  C  CE2  . PHE   A  1  581 ? 38.549  -2.874  -19.962  1.00 93.92  ? 581  PHE   A CE2  1 
ATOM   8883  C  CZ   . PHE   A  1  581 ? 37.922  -3.363  -18.835  1.00 91.83  ? 581  PHE   A CZ   1 
ATOM   8884  H  H    . PHE   A  1  581 ? 39.726  1.396   -18.470  1.00 112.29 ? 581  PHE   A H    1 
ATOM   8885  H  HA   . PHE   A  1  581 ? 40.840  -0.069  -16.514  1.00 117.86 ? 581  PHE   A HA   1 
ATOM   8886  H  HB2  . PHE   A  1  581 ? 41.287  -0.153  -19.301  1.00 118.45 ? 581  PHE   A HB2  1 
ATOM   8887  H  HB3  . PHE   A  1  581 ? 41.995  -1.135  -18.272  1.00 118.45 ? 581  PHE   A HB3  1 
ATOM   8888  H  HD1  . PHE   A  1  581 ? 39.690  -1.819  -16.619  1.00 108.62 ? 581  PHE   A HD1  1 
ATOM   8889  H  HD2  . PHE   A  1  581 ? 40.023  -1.661  -20.600  1.00 115.77 ? 581  PHE   A HD2  1 
ATOM   8890  H  HE1  . PHE   A  1  581 ? 37.930  -3.298  -16.823  1.00 106.58 ? 581  PHE   A HE1  1 
ATOM   8891  H  HE2  . PHE   A  1  581 ? 38.262  -3.139  -20.806  1.00 112.69 ? 581  PHE   A HE2  1 
ATOM   8892  H  HZ   . PHE   A  1  581 ? 37.211  -3.958  -18.917  1.00 110.18 ? 581  PHE   A HZ   1 
ATOM   8893  N  N    . THR   A  1  582 ? 42.341  2.461   -17.594  1.00 105.71 ? 582  THR   A N    1 
ATOM   8894  C  CA   . THR   A  1  582 ? 43.470  3.333   -17.300  1.00 105.59 ? 582  THR   A CA   1 
ATOM   8895  C  C    . THR   A  1  582 ? 43.126  4.180   -16.086  1.00 105.72 ? 582  THR   A C    1 
ATOM   8896  O  O    . THR   A  1  582 ? 42.146  4.941   -16.142  1.00 109.39 ? 582  THR   A O    1 
ATOM   8897  C  CB   . THR   A  1  582 ? 43.798  4.229   -18.490  1.00 104.96 ? 582  THR   A CB   1 
ATOM   8898  O  OG1  . THR   A  1  582 ? 42.800  5.250   -18.617  1.00 107.38 ? 582  THR   A OG1  1 
ATOM   8899  C  CG2  . THR   A  1  582 ? 43.865  3.415   -19.779  1.00 103.00 ? 582  THR   A CG2  1 
ATOM   8900  H  H    . THR   A  1  582 ? 41.726  2.832   -18.068  1.00 126.83 ? 582  THR   A H    1 
ATOM   8901  H  HA   . THR   A  1  582 ? 44.254  2.795   -17.106  1.00 126.68 ? 582  THR   A HA   1 
ATOM   8902  H  HB   . THR   A  1  582 ? 44.664  4.644   -18.351  1.00 125.94 ? 582  THR   A HB   1 
ATOM   8903  H  HG1  . THR   A  1  582 ? 42.073  4.984   -18.291  1.00 128.83 ? 582  THR   A HG1  1 
ATOM   8904  H  HG21 . THR   A  1  582 ? 44.145  3.981   -20.515  1.00 123.59 ? 582  THR   A HG21 1 
ATOM   8905  H  HG22 . THR   A  1  582 ? 44.500  2.688   -19.681  1.00 123.59 ? 582  THR   A HG22 1 
ATOM   8906  H  HG23 . THR   A  1  582 ? 42.992  3.044   -19.983  1.00 123.59 ? 582  THR   A HG23 1 
ATOM   8907  N  N    . PRO   A  1  583 ? 43.866  4.090   -14.980  1.00 100.52 ? 583  PRO   A N    1 
ATOM   8908  C  CA   . PRO   A  1  583 ? 43.492  4.865   -13.790  1.00 96.70  ? 583  PRO   A CA   1 
ATOM   8909  C  C    . PRO   A  1  583 ? 43.457  6.357   -14.082  1.00 92.92  ? 583  PRO   A C    1 
ATOM   8910  O  O    . PRO   A  1  583 ? 44.314  6.894   -14.787  1.00 90.85  ? 583  PRO   A O    1 
ATOM   8911  C  CB   . PRO   A  1  583 ? 44.588  4.513   -12.776  1.00 96.70  ? 583  PRO   A CB   1 
ATOM   8912  C  CG   . PRO   A  1  583 ? 45.136  3.209   -13.240  1.00 97.46  ? 583  PRO   A CG   1 
ATOM   8913  C  CD   . PRO   A  1  583 ? 45.047  3.244   -14.735  1.00 98.35  ? 583  PRO   A CD   1 
ATOM   8914  H  HA   . PRO   A  1  583 ? 42.628  4.579   -13.454  1.00 116.02 ? 583  PRO   A HA   1 
ATOM   8915  H  HB2  . PRO   A  1  583 ? 45.274  5.199   -12.780  1.00 116.02 ? 583  PRO   A HB2  1 
ATOM   8916  H  HB3  . PRO   A  1  583 ? 44.203  4.433   -11.889  1.00 116.02 ? 583  PRO   A HB3  1 
ATOM   8917  H  HG2  . PRO   A  1  583 ? 46.058  3.119   -12.952  1.00 116.94 ? 583  PRO   A HG2  1 
ATOM   8918  H  HG3  . PRO   A  1  583 ? 44.603  2.482   -12.880  1.00 116.94 ? 583  PRO   A HG3  1 
ATOM   8919  H  HD2  . PRO   A  1  583 ? 45.844  3.642   -15.119  1.00 118.00 ? 583  PRO   A HD2  1 
ATOM   8920  H  HD3  . PRO   A  1  583 ? 44.915  2.352   -15.094  1.00 118.00 ? 583  PRO   A HD3  1 
ATOM   8921  N  N    . ALA   A  1  584 ? 42.447  7.028   -13.526  1.00 93.40  ? 584  ALA   A N    1 
ATOM   8922  C  CA   . ALA   A  1  584 ? 42.261  8.459   -13.711  1.00 96.78  ? 584  ALA   A CA   1 
ATOM   8923  C  C    . ALA   A  1  584 ? 43.009  9.287   -12.672  1.00 95.65  ? 584  ALA   A C    1 
ATOM   8924  O  O    . ALA   A  1  584 ? 42.722  10.480  -12.520  1.00 96.53  ? 584  ALA   A O    1 
ATOM   8925  C  CB   . ALA   A  1  584 ? 40.770  8.805   -13.679  1.00 99.87  ? 584  ALA   A CB   1 
ATOM   8926  H  H    . ALA   A  1  584 ? 41.847  6.664   -13.029  1.00 112.06 ? 584  ALA   A H    1 
ATOM   8927  H  HA   . ALA   A  1  584 ? 42.605  8.699   -14.585  1.00 116.12 ? 584  ALA   A HA   1 
ATOM   8928  H  HB1  . ALA   A  1  584 ? 40.665  9.762   -13.801  1.00 119.82 ? 584  ALA   A HB1  1 
ATOM   8929  H  HB2  . ALA   A  1  584 ? 40.320  8.328   -14.393  1.00 119.82 ? 584  ALA   A HB2  1 
ATOM   8930  H  HB3  . ALA   A  1  584 ? 40.403  8.539   -12.821  1.00 119.82 ? 584  ALA   A HB3  1 
ATOM   8931  N  N    . ASN   A  1  585 ? 43.953  8.683   -11.954  1.00 93.99  ? 585  ASN   A N    1 
ATOM   8932  C  CA   . ASN   A  1  585 ? 44.759  9.395   -10.974  1.00 92.89  ? 585  ASN   A CA   1 
ATOM   8933  C  C    . ASN   A  1  585 ? 46.202  8.925   -11.076  1.00 90.82  ? 585  ASN   A C    1 
ATOM   8934  O  O    . ASN   A  1  585 ? 46.463  7.740   -11.299  1.00 89.41  ? 585  ASN   A O    1 
ATOM   8935  C  CB   . ASN   A  1  585 ? 44.237  9.182   -9.546   1.00 93.59  ? 585  ASN   A CB   1 
ATOM   8936  C  CG   . ASN   A  1  585 ? 44.128  7.717   -9.175   1.00 94.97  ? 585  ASN   A CG   1 
ATOM   8937  O  OD1  . ASN   A  1  585 ? 45.128  7.000   -9.129   1.00 96.83  ? 585  ASN   A OD1  1 
ATOM   8938  N  ND2  . ASN   A  1  585 ? 42.911  7.266   -8.892   1.00 94.45  ? 585  ASN   A ND2  1 
ATOM   8939  H  H    . ASN   A  1  585 ? 44.147  7.848   -12.019  1.00 112.77 ? 585  ASN   A H    1 
ATOM   8940  H  HA   . ASN   A  1  585 ? 44.733  10.346  -11.164  1.00 111.44 ? 585  ASN   A HA   1 
ATOM   8941  H  HB2  . ASN   A  1  585 ? 44.845  9.605   -8.920   1.00 112.29 ? 585  ASN   A HB2  1 
ATOM   8942  H  HB3  . ASN   A  1  585 ? 43.354  9.577   -9.469   1.00 112.29 ? 585  ASN   A HB3  1 
ATOM   8943  H  HD21 . ASN   A  1  585 ? 42.797  6.442   -8.675   1.00 113.32 ? 585  ASN   A HD21 1 
ATOM   8944  H  HD22 . ASN   A  1  585 ? 42.236  7.799   -8.924   1.00 113.32 ? 585  ASN   A HD22 1 
ATOM   8945  N  N    . ILE   A  1  586 ? 47.135  9.865   -10.917  1.00 91.50  ? 586  ILE   A N    1 
ATOM   8946  C  CA   . ILE   A  1  586 ? 48.562  9.570   -10.924  1.00 91.34  ? 586  ILE   A CA   1 
ATOM   8947  C  C    . ILE   A  1  586 ? 49.215  10.354  -9.797   1.00 90.97  ? 586  ILE   A C    1 
ATOM   8948  O  O    . ILE   A  1  586 ? 48.696  11.372  -9.333   1.00 92.51  ? 586  ILE   A O    1 
ATOM   8949  C  CB   . ILE   A  1  586 ? 49.233  9.908   -12.274  1.00 92.25  ? 586  ILE   A CB   1 
ATOM   8950  C  CG1  . ILE   A  1  586 ? 48.910  11.345  -12.692  1.00 94.06  ? 586  ILE   A CG1  1 
ATOM   8951  C  CG2  . ILE   A  1  586 ? 48.790  8.919   -13.339  1.00 93.82  ? 586  ILE   A CG2  1 
ATOM   8952  C  CD1  . ILE   A  1  586 ? 49.567  11.763  -13.993  1.00 95.59  ? 586  ILE   A CD1  1 
ATOM   8953  H  H    . ILE   A  1  586 ? 46.959  10.698  -10.801  1.00 109.78 ? 586  ILE   A H    1 
ATOM   8954  H  HA   . ILE   A  1  586 ? 48.694  8.623   -10.760  1.00 109.59 ? 586  ILE   A HA   1 
ATOM   8955  H  HB   . ILE   A  1  586 ? 50.195  9.837   -12.168  1.00 110.68 ? 586  ILE   A HB   1 
ATOM   8956  H  HG12 . ILE   A  1  586 ? 47.950  11.429  -12.804  1.00 112.85 ? 586  ILE   A HG12 1 
ATOM   8957  H  HG13 . ILE   A  1  586 ? 49.217  11.948  -11.997  1.00 112.85 ? 586  ILE   A HG13 1 
ATOM   8958  H  HG21 . ILE   A  1  586 ? 49.300  9.076   -14.149  1.00 112.56 ? 586  ILE   A HG21 1 
ATOM   8959  H  HG22 . ILE   A  1  586 ? 48.948  8.017   -13.018  1.00 112.56 ? 586  ILE   A HG22 1 
ATOM   8960  H  HG23 . ILE   A  1  586 ? 47.844  9.046   -13.514  1.00 112.56 ? 586  ILE   A HG23 1 
ATOM   8961  H  HD11 . ILE   A  1  586 ? 49.407  12.708  -14.137  1.00 114.68 ? 586  ILE   A HD11 1 
ATOM   8962  H  HD12 . ILE   A  1  586 ? 50.520  11.594  -13.934  1.00 114.68 ? 586  ILE   A HD12 1 
ATOM   8963  H  HD13 . ILE   A  1  586 ? 49.184  11.247  -14.720  1.00 114.68 ? 586  ILE   A HD13 1 
ATOM   8964  N  N    . SER   A  1  587 ? 50.374  9.868   -9.357   1.00 89.82  ? 587  SER   A N    1 
ATOM   8965  C  CA   . SER   A  1  587 ? 51.034  10.445  -8.196   1.00 91.77  ? 587  SER   A CA   1 
ATOM   8966  C  C    . SER   A  1  587 ? 52.540  10.270  -8.297   1.00 87.16  ? 587  SER   A C    1 
ATOM   8967  O  O    . SER   A  1  587 ? 53.030  9.190   -8.643   1.00 84.92  ? 587  SER   A O    1 
ATOM   8968  C  CB   . SER   A  1  587 ? 50.519  9.804   -6.901   1.00 97.86  ? 587  SER   A CB   1 
ATOM   8969  O  OG   . SER   A  1  587 ? 50.701  8.398   -6.922   1.00 103.07 ? 587  SER   A OG   1 
ATOM   8970  H  H    . SER   A  1  587 ? 50.793  9.208   -9.715   1.00 107.77 ? 587  SER   A H    1 
ATOM   8971  H  HA   . SER   A  1  587 ? 50.851  11.397  -8.179   1.00 110.10 ? 587  SER   A HA   1 
ATOM   8972  H  HB2  . SER   A  1  587 ? 51.010  10.173  -6.150   1.00 117.42 ? 587  SER   A HB2  1 
ATOM   8973  H  HB3  . SER   A  1  587 ? 49.573  9.998   -6.807   1.00 117.42 ? 587  SER   A HB3  1 
ATOM   8974  H  HG   . SER   A  1  587 ? 50.430  8.063   -6.201   1.00 123.66 ? 587  SER   A HG   1 
ATOM   8975  N  N    . ARG   A  1  588 ? 53.258  11.346  -7.997   1.00 86.88  ? 588  ARG   A N    1 
ATOM   8976  C  CA   . ARG   A  1  588 ? 54.700  11.339  -7.809   1.00 84.11  ? 588  ARG   A CA   1 
ATOM   8977  C  C    . ARG   A  1  588 ? 54.994  11.877  -6.415   1.00 84.77  ? 588  ARG   A C    1 
ATOM   8978  O  O    . ARG   A  1  588 ? 54.209  12.652  -5.860   1.00 87.64  ? 588  ARG   A O    1 
ATOM   8979  C  CB   . ARG   A  1  588 ? 55.408  12.194  -8.864   1.00 87.48  ? 588  ARG   A CB   1 
ATOM   8980  C  CG   . ARG   A  1  588 ? 55.141  11.773  -10.303  1.00 92.63  ? 588  ARG   A CG   1 
ATOM   8981  C  CD   . ARG   A  1  588 ? 55.989  10.579  -10.715  1.00 98.70  ? 588  ARG   A CD   1 
ATOM   8982  N  NE   . ARG   A  1  588 ? 56.012  10.404  -12.166  1.00 103.73 ? 588  ARG   A NE   1 
ATOM   8983  C  CZ   . ARG   A  1  588 ? 55.125  9.694   -12.859  1.00 104.96 ? 588  ARG   A CZ   1 
ATOM   8984  N  NH1  . ARG   A  1  588 ? 54.124  9.075   -12.245  1.00 103.00 ? 588  ARG   A NH1  1 
ATOM   8985  N  NH2  . ARG   A  1  588 ? 55.240  9.603   -14.177  1.00 105.90 ? 588  ARG   A NH2  1 
ATOM   8986  H  H    . ARG   A  1  588 ? 52.915  12.128  -7.892   1.00 104.24 ? 588  ARG   A H    1 
ATOM   8987  H  HA   . ARG   A  1  588 ? 55.052  10.439  -7.887   1.00 100.91 ? 588  ARG   A HA   1 
ATOM   8988  H  HB2  . ARG   A  1  588 ? 55.110  13.112  -8.768   1.00 104.96 ? 588  ARG   A HB2  1 
ATOM   8989  H  HB3  . ARG   A  1  588 ? 56.365  12.138  -8.716   1.00 104.96 ? 588  ARG   A HB3  1 
ATOM   8990  H  HG2  . ARG   A  1  588 ? 54.207  11.527  -10.396  1.00 111.13 ? 588  ARG   A HG2  1 
ATOM   8991  H  HG3  . ARG   A  1  588 ? 55.351  12.511  -10.896  1.00 111.13 ? 588  ARG   A HG3  1 
ATOM   8992  H  HD2  . ARG   A  1  588 ? 56.900  10.713  -10.410  1.00 118.42 ? 588  ARG   A HD2  1 
ATOM   8993  H  HD3  . ARG   A  1  588 ? 55.622  9.774   -10.318  1.00 118.42 ? 588  ARG   A HD3  1 
ATOM   8994  H  HE   . ARG   A  1  588 ? 56.645  10.788  -12.604  1.00 124.45 ? 588  ARG   A HE   1 
ATOM   8995  H  HH11 . ARG   A  1  588 ? 54.044  9.130   -11.390  1.00 123.58 ? 588  ARG   A HH11 1 
ATOM   8996  H  HH12 . ARG   A  1  588 ? 53.556  8.618   -12.701  1.00 123.58 ? 588  ARG   A HH12 1 
ATOM   8997  H  HH21 . ARG   A  1  588 ? 55.886  10.002  -14.581  1.00 127.06 ? 588  ARG   A HH21 1 
ATOM   8998  H  HH22 . ARG   A  1  588 ? 54.669  9.145   -14.628  1.00 127.06 ? 588  ARG   A HH22 1 
ATOM   8999  N  N    . GLN   A  1  589 ? 56.122  11.463  -5.842   1.00 84.56  ? 589  GLN   A N    1 
ATOM   9000  C  CA   . GLN   A  1  589 ? 56.461  11.842  -4.477   1.00 87.61  ? 589  GLN   A CA   1 
ATOM   9001  C  C    . GLN   A  1  589 ? 57.851  12.454  -4.414   1.00 88.07  ? 589  GLN   A C    1 
ATOM   9002  O  O    . GLN   A  1  589 ? 58.799  11.942  -5.017   1.00 87.63  ? 589  GLN   A O    1 
ATOM   9003  C  CB   . GLN   A  1  589 ? 56.378  10.637  -3.528   1.00 88.03  ? 589  GLN   A CB   1 
ATOM   9004  C  CG   . GLN   A  1  589 ? 57.350  9.515   -3.835   1.00 87.99  ? 589  GLN   A CG   1 
ATOM   9005  C  CD   . GLN   A  1  589 ? 57.193  8.346   -2.882   1.00 88.64  ? 589  GLN   A CD   1 
ATOM   9006  O  OE1  . GLN   A  1  589 ? 56.138  8.161   -2.276   1.00 87.82  ? 589  GLN   A OE1  1 
ATOM   9007  N  NE2  . GLN   A  1  589 ? 58.247  7.552   -2.740   1.00 90.51  ? 589  GLN   A NE2  1 
ATOM   9008  H  H    . GLN   A  1  589 ? 56.706  10.962  -6.226   1.00 101.45 ? 589  GLN   A H    1 
ATOM   9009  H  HA   . GLN   A  1  589 ? 55.833  12.519  -4.179   1.00 105.11 ? 589  GLN   A HA   1 
ATOM   9010  H  HB2  . GLN   A  1  589 ? 56.562  10.944  -2.626   1.00 105.62 ? 589  GLN   A HB2  1 
ATOM   9011  H  HB3  . GLN   A  1  589 ? 55.483  10.268  -3.577   1.00 105.62 ? 589  GLN   A HB3  1 
ATOM   9012  H  HG2  . GLN   A  1  589 ? 57.192  9.195   -4.737   1.00 105.57 ? 589  GLN   A HG2  1 
ATOM   9013  H  HG3  . GLN   A  1  589 ? 58.258  9.850   -3.756   1.00 105.57 ? 589  GLN   A HG3  1 
ATOM   9014  H  HE21 . GLN   A  1  589 ? 58.970  7.715   -3.177   1.00 108.59 ? 589  GLN   A HE21 1 
ATOM   9015  H  HE22 . GLN   A  1  589 ? 58.208  6.875   -2.211   1.00 108.59 ? 589  GLN   A HE22 1 
ATOM   9016  N  N    . ALA   A  1  590 ? 57.957  13.558  -3.681   1.00 89.17  ? 590  ALA   A N    1 
ATOM   9017  C  CA   . ALA   A  1  590 ? 59.224  14.208  -3.385   1.00 90.62  ? 590  ALA   A CA   1 
ATOM   9018  C  C    . ALA   A  1  590 ? 59.676  13.839  -1.975   1.00 90.86  ? 590  ALA   A C    1 
ATOM   9019  O  O    . ALA   A  1  590 ? 58.912  13.302  -1.170   1.00 89.83  ? 590  ALA   A O    1 
ATOM   9020  C  CB   . ALA   A  1  590 ? 59.094  15.727  -3.531   1.00 90.68  ? 590  ALA   A CB   1 
ATOM   9021  H  H    . ALA   A  1  590 ? 57.283  13.962  -3.332   1.00 106.99 ? 590  ALA   A H    1 
ATOM   9022  H  HA   . ALA   A  1  590 ? 59.899  13.907  -4.013   1.00 108.73 ? 590  ALA   A HA   1 
ATOM   9023  H  HB1  . ALA   A  1  590 ? 59.941  16.140  -3.300   1.00 108.79 ? 590  ALA   A HB1  1 
ATOM   9024  H  HB2  . ALA   A  1  590 ? 58.862  15.937  -4.449   1.00 108.79 ? 590  ALA   A HB2  1 
ATOM   9025  H  HB3  . ALA   A  1  590 ? 58.398  16.043  -2.933   1.00 108.79 ? 590  ALA   A HB3  1 
ATOM   9026  N  N    . HIS   A  1  591 ? 60.940  14.137  -1.680   1.00 91.39  ? 591  HIS   A N    1 
ATOM   9027  C  CA   . HIS   A  1  591 ? 61.537  13.791  -0.398   1.00 93.27  ? 591  HIS   A CA   1 
ATOM   9028  C  C    . HIS   A  1  591 ? 62.292  14.980  0.177    1.00 95.13  ? 591  HIS   A C    1 
ATOM   9029  O  O    . HIS   A  1  591 ? 62.775  15.848  -0.555   1.00 95.56  ? 591  HIS   A O    1 
ATOM   9030  C  CB   . HIS   A  1  591 ? 62.486  12.594  -0.527   1.00 97.43  ? 591  HIS   A CB   1 
ATOM   9031  C  CG   . HIS   A  1  591 ? 61.783  11.292  -0.756   1.00 98.60  ? 591  HIS   A CG   1 
ATOM   9032  N  ND1  . HIS   A  1  591 ? 61.225  10.949  -1.968   1.00 96.58  ? 591  HIS   A ND1  1 
ATOM   9033  C  CD2  . HIS   A  1  591 ? 61.539  10.254  0.078    1.00 98.95  ? 591  HIS   A CD2  1 
ATOM   9034  C  CE1  . HIS   A  1  591 ? 60.673  9.753   -1.874   1.00 95.69  ? 591  HIS   A CE1  1 
ATOM   9035  N  NE2  . HIS   A  1  591 ? 60.850  9.308   -0.643   1.00 96.77  ? 591  HIS   A NE2  1 
ATOM   9036  H  H    . HIS   A  1  591 ? 61.477  14.544  -2.215   1.00 109.65 ? 591  HIS   A H    1 
ATOM   9037  H  HA   . HIS   A  1  591 ? 60.829  13.563  0.225    1.00 111.90 ? 591  HIS   A HA   1 
ATOM   9038  H  HB2  . HIS   A  1  591 ? 63.080  12.746  -1.279   1.00 116.90 ? 591  HIS   A HB2  1 
ATOM   9039  H  HB3  . HIS   A  1  591 ? 63.000  12.513  0.291    1.00 116.90 ? 591  HIS   A HB3  1 
ATOM   9040  H  HD2  . HIS   A  1  591 ? 61.791  10.192  0.971    1.00 118.72 ? 591  HIS   A HD2  1 
ATOM   9041  H  HE1  . HIS   A  1  591 ? 60.233  9.301   -2.557   1.00 114.81 ? 591  HIS   A HE1  1 
ATOM   9042  H  HE2  . HIS   A  1  591 ? 60.579  8.550   -0.341   1.00 116.10 ? 591  HIS   A HE2  1 
ATOM   9043  N  N    . ILE   A  1  592 ? 62.390  15.000  1.504    1.00 96.08  ? 592  ILE   A N    1 
ATOM   9044  C  CA   . ILE   A  1  592 ? 63.075  16.065  2.227    1.00 99.69  ? 592  ILE   A CA   1 
ATOM   9045  C  C    . ILE   A  1  592 ? 64.512  15.636  2.492    1.00 99.03  ? 592  ILE   A C    1 
ATOM   9046  O  O    . ILE   A  1  592 ? 64.765  14.518  2.958    1.00 98.61  ? 592  ILE   A O    1 
ATOM   9047  C  CB   . ILE   A  1  592 ? 62.339  16.398  3.538    1.00 102.98 ? 592  ILE   A CB   1 
ATOM   9048  C  CG1  . ILE   A  1  592 ? 60.980  17.034  3.222    1.00 101.47 ? 592  ILE   A CG1  1 
ATOM   9049  C  CG2  . ILE   A  1  592 ? 63.183  17.324  4.414    1.00 108.48 ? 592  ILE   A CG2  1 
ATOM   9050  C  CD1  . ILE   A  1  592 ? 60.143  17.379  4.442    1.00 102.23 ? 592  ILE   A CD1  1 
ATOM   9051  H  H    . ILE   A  1  592 ? 62.061  14.395  2.018    1.00 115.28 ? 592  ILE   A H    1 
ATOM   9052  H  HA   . ILE   A  1  592 ? 63.096  16.864  1.678    1.00 119.61 ? 592  ILE   A HA   1 
ATOM   9053  H  HB   . ILE   A  1  592 ? 62.194  15.575  4.029    1.00 123.55 ? 592  ILE   A HB   1 
ATOM   9054  H  HG12 . ILE   A  1  592 ? 61.132  17.857  2.730    1.00 121.74 ? 592  ILE   A HG12 1 
ATOM   9055  H  HG13 . ILE   A  1  592 ? 60.467  16.414  2.681    1.00 121.74 ? 592  ILE   A HG13 1 
ATOM   9056  H  HG21 . ILE   A  1  592 ? 62.687  17.533  5.221    1.00 130.16 ? 592  ILE   A HG21 1 
ATOM   9057  H  HG22 . ILE   A  1  592 ? 64.011  16.875  4.642    1.00 130.16 ? 592  ILE   A HG22 1 
ATOM   9058  H  HG23 . ILE   A  1  592 ? 63.372  18.138  3.923    1.00 130.16 ? 592  ILE   A HG23 1 
ATOM   9059  H  HD11 . ILE   A  1  592 ? 59.280  17.711  4.149    1.00 122.65 ? 592  ILE   A HD11 1 
ATOM   9060  H  HD12 . ILE   A  1  592 ? 60.025  16.580  4.979    1.00 122.65 ? 592  ILE   A HD12 1 
ATOM   9061  H  HD13 . ILE   A  1  592 ? 60.602  18.060  4.958    1.00 122.65 ? 592  ILE   A HD13 1 
ATOM   9062  N  N    . LEU   A  1  593 ? 65.452  16.528  2.193    1.00 99.48  ? 593  LEU   A N    1 
ATOM   9063  C  CA   . LEU   A  1  593 ? 66.865  16.267  2.430    1.00 100.37 ? 593  LEU   A CA   1 
ATOM   9064  C  C    . LEU   A  1  593 ? 67.149  16.188  3.927    1.00 102.45 ? 593  LEU   A C    1 
ATOM   9065  O  O    . LEU   A  1  593 ? 66.525  16.876  4.739    1.00 106.35 ? 593  LEU   A O    1 
ATOM   9066  C  CB   . LEU   A  1  593 ? 67.705  17.371  1.782    1.00 101.92 ? 593  LEU   A CB   1 
ATOM   9067  C  CG   . LEU   A  1  593 ? 69.204  17.191  1.515    1.00 103.52 ? 593  LEU   A CG   1 
ATOM   9068  C  CD1  . LEU   A  1  593 ? 70.042  17.410  2.769    1.00 106.43 ? 593  LEU   A CD1  1 
ATOM   9069  C  CD2  . LEU   A  1  593 ? 69.494  15.827  0.901    1.00 103.13 ? 593  LEU   A CD2  1 
ATOM   9070  H  H    . LEU   A  1  593 ? 65.295  17.300  1.848    1.00 119.35 ? 593  LEU   A H    1 
ATOM   9071  H  HA   . LEU   A  1  593 ? 67.122  15.419  2.036    1.00 120.42 ? 593  LEU   A HA   1 
ATOM   9072  H  HB2  . LEU   A  1  593 ? 67.305  17.556  0.918    1.00 122.29 ? 593  LEU   A HB2  1 
ATOM   9073  H  HB3  . LEU   A  1  593 ? 67.632  18.150  2.355    1.00 122.29 ? 593  LEU   A HB3  1 
ATOM   9074  H  HG   . LEU   A  1  593 ? 69.470  17.870  0.875    1.00 124.20 ? 593  LEU   A HG   1 
ATOM   9075  H  HD11 . LEU   A  1  593 ? 70.981  17.407  2.526    1.00 127.70 ? 593  LEU   A HD11 1 
ATOM   9076  H  HD12 . LEU   A  1  593 ? 69.804  18.264  3.162    1.00 127.70 ? 593  LEU   A HD12 1 
ATOM   9077  H  HD13 . LEU   A  1  593 ? 69.860  16.695  3.398    1.00 127.70 ? 593  LEU   A HD13 1 
ATOM   9078  H  HD21 . LEU   A  1  593 ? 70.436  15.775  0.678    1.00 123.73 ? 593  LEU   A HD21 1 
ATOM   9079  H  HD22 . LEU   A  1  593 ? 69.268  15.137  1.545    1.00 123.73 ? 593  LEU   A HD22 1 
ATOM   9080  H  HD23 . LEU   A  1  593 ? 68.958  15.720  0.100    1.00 123.73 ? 593  LEU   A HD23 1 
ATOM   9081  N  N    . LEU   A  1  594 ? 68.101  15.328  4.290    1.00 101.58 ? 594  LEU   A N    1 
ATOM   9082  C  CA   . LEU   A  1  594 ? 68.491  15.126  5.678    1.00 103.69 ? 594  LEU   A CA   1 
ATOM   9083  C  C    . LEU   A  1  594 ? 69.990  15.336  5.834    1.00 109.55 ? 594  LEU   A C    1 
ATOM   9084  O  O    . LEU   A  1  594 ? 70.775  14.992  4.944    1.00 111.48 ? 594  LEU   A O    1 
ATOM   9085  C  CB   . LEU   A  1  594 ? 68.110  13.720  6.164    1.00 103.83 ? 594  LEU   A CB   1 
ATOM   9086  C  CG   . LEU   A  1  594 ? 66.642  13.334  5.974    1.00 103.21 ? 594  LEU   A CG   1 
ATOM   9087  C  CD1  . LEU   A  1  594 ? 66.421  11.883  6.370    1.00 101.47 ? 594  LEU   A CD1  1 
ATOM   9088  C  CD2  . LEU   A  1  594 ? 65.726  14.253  6.769    1.00 106.39 ? 594  LEU   A CD2  1 
ATOM   9089  H  H    . LEU   A  1  594 ? 68.542  14.841  3.735    1.00 121.88 ? 594  LEU   A H    1 
ATOM   9090  H  HA   . LEU   A  1  594 ? 68.037  15.778  6.234    1.00 124.40 ? 594  LEU   A HA   1 
ATOM   9091  H  HB2  . LEU   A  1  594 ? 68.645  13.074  5.677    1.00 124.58 ? 594  LEU   A HB2  1 
ATOM   9092  H  HB3  . LEU   A  1  594 ? 68.304  13.664  7.113    1.00 124.58 ? 594  LEU   A HB3  1 
ATOM   9093  H  HG   . LEU   A  1  594 ? 66.413  13.431  5.036    1.00 123.84 ? 594  LEU   A HG   1 
ATOM   9094  H  HD11 . LEU   A  1  594 ? 65.483  11.664  6.255    1.00 121.74 ? 594  LEU   A HD11 1 
ATOM   9095  H  HD12 . LEU   A  1  594 ? 66.965  11.315  5.803    1.00 121.74 ? 594  LEU   A HD12 1 
ATOM   9096  H  HD13 . LEU   A  1  594 ? 66.676  11.767  7.298    1.00 121.74 ? 594  LEU   A HD13 1 
ATOM   9097  H  HD21 . LEU   A  1  594 ? 64.809  13.958  6.659    1.00 127.65 ? 594  LEU   A HD21 1 
ATOM   9098  H  HD22 . LEU   A  1  594 ? 65.976  14.214  7.706    1.00 127.65 ? 594  LEU   A HD22 1 
ATOM   9099  H  HD23 . LEU   A  1  594 ? 65.824  15.159  6.438    1.00 127.65 ? 594  LEU   A HD23 1 
ATOM   9100  N  N    . ASP   A  1  595 ? 70.379  15.895  6.975    1.00 115.05 ? 595  ASP   A N    1 
ATOM   9101  C  CA   . ASP   A  1  595 ? 71.783  16.171  7.258    1.00 122.32 ? 595  ASP   A CA   1 
ATOM   9102  C  C    . ASP   A  1  595 ? 72.109  15.929  8.727    1.00 117.05 ? 595  ASP   A C    1 
ATOM   9103  O  O    . ASP   A  1  595 ? 73.200  16.262  9.192    1.00 113.57 ? 595  ASP   A O    1 
ATOM   9104  C  CB   . ASP   A  1  595 ? 72.131  17.612  6.880    1.00 135.71 ? 595  ASP   A CB   1 
ATOM   9105  C  CG   . ASP   A  1  595 ? 72.017  17.868  5.391    1.00 141.81 ? 595  ASP   A CG   1 
ATOM   9106  O  OD1  . ASP   A  1  595 ? 72.382  16.970  4.603    1.00 142.77 ? 595  ASP   A OD1  1 
ATOM   9107  O  OD2  . ASP   A  1  595 ? 71.563  18.967  5.008    1.00 144.59 ? 595  ASP   A OD2  1 
ATOM   9108  H  H    . ASP   A  1  595 ? 69.844  16.126  7.607    1.00 138.05 ? 595  ASP   A H    1 
ATOM   9109  H  HA   . ASP   A  1  595 ? 72.331  15.574  6.725    1.00 146.77 ? 595  ASP   A HA   1 
ATOM   9110  H  HB2  . ASP   A  1  595 ? 71.522  18.214  7.336    1.00 162.84 ? 595  ASP   A HB2  1 
ATOM   9111  H  HB3  . ASP   A  1  595 ? 73.044  17.798  7.148    1.00 162.84 ? 595  ASP   A HB3  1 
ATOM   9112  N  N    . GLY   B  2  1   ? 54.697  -5.158  17.657   1.00 147.39 ? 5    GLY   B N    1 
ATOM   9113  C  CA   . GLY   B  2  1   ? 53.968  -6.092  16.820   1.00 146.97 ? 5    GLY   B CA   1 
ATOM   9114  C  C    . GLY   B  2  1   ? 52.650  -5.530  16.325   1.00 139.12 ? 5    GLY   B C    1 
ATOM   9115  O  O    . GLY   B  2  1   ? 52.343  -5.606  15.135   1.00 137.91 ? 5    GLY   B O    1 
ATOM   9116  H  HA2  . GLY   B  2  1   ? 54.510  -6.321  16.049   1.00 176.35 ? 5    GLY   B HA2  1 
ATOM   9117  H  HA3  . GLY   B  2  1   ? 53.784  -6.899  17.327   1.00 176.35 ? 5    GLY   B HA3  1 
ATOM   9118  N  N    . CYS   B  2  2   ? 51.866  -4.966  17.245   1.00 135.05 ? 6    CYS   B N    1 
ATOM   9119  C  CA   . CYS   B  2  2   ? 50.582  -4.357  16.920   1.00 130.92 ? 6    CYS   B CA   1 
ATOM   9120  C  C    . CYS   B  2  2   ? 50.659  -2.834  16.890   1.00 130.31 ? 6    CYS   B C    1 
ATOM   9121  O  O    . CYS   B  2  2   ? 49.669  -2.154  17.184   1.00 124.61 ? 6    CYS   B O    1 
ATOM   9122  C  CB   . CYS   B  2  2   ? 49.513  -4.813  17.912   1.00 131.02 ? 6    CYS   B CB   1 
ATOM   9123  S  SG   . CYS   B  2  2   ? 47.828  -4.428  17.379   1.00 129.87 ? 6    CYS   B SG   1 
ATOM   9124  H  H    . CYS   B  2  2   ? 52.063  -4.924  18.081   1.00 162.05 ? 6    CYS   B H    1 
ATOM   9125  H  HA   . CYS   B  2  2   ? 50.318  -4.658  16.037   1.00 157.09 ? 6    CYS   B HA   1 
ATOM   9126  H  HB2  . CYS   B  2  2   ? 49.577  -5.774  18.022   1.00 157.20 ? 6    CYS   B HB2  1 
ATOM   9127  H  HB3  . CYS   B  2  2   ? 49.664  -4.370  18.761   1.00 157.20 ? 6    CYS   B HB3  1 
ATOM   9128  N  N    . ALA   B  2  3   ? 51.821  -2.287  16.547   1.00 137.97 ? 7    ALA   B N    1 
ATOM   9129  C  CA   . ALA   B  2  3   ? 52.023  -0.848  16.418   1.00 138.31 ? 7    ALA   B CA   1 
ATOM   9130  C  C    . ALA   B  2  3   ? 52.297  -0.467  14.966   1.00 139.96 ? 7    ALA   B C    1 
ATOM   9131  O  O    . ALA   B  2  3   ? 53.092  0.430   14.680   1.00 142.17 ? 7    ALA   B O    1 
ATOM   9132  C  CB   . ALA   B  2  3   ? 53.165  -0.382  17.317   1.00 142.65 ? 7    ALA   B CB   1 
ATOM   9133  H  H    . ALA   B  2  3   ? 52.530  -2.744  16.379   1.00 165.55 ? 7    ALA   B H    1 
ATOM   9134  H  HA   . ALA   B  2  3   ? 51.217  -0.392  16.704   1.00 165.95 ? 7    ALA   B HA   1 
ATOM   9135  H  HB1  . ALA   B  2  3   ? 53.269  0.578   17.223   1.00 171.16 ? 7    ALA   B HB1  1 
ATOM   9136  H  HB2  . ALA   B  2  3   ? 52.952  -0.603  18.238   1.00 171.16 ? 7    ALA   B HB2  1 
ATOM   9137  H  HB3  . ALA   B  2  3   ? 53.982  -0.832  17.050   1.00 171.16 ? 7    ALA   B HB3  1 
ATOM   9138  N  N    . LEU   B  2  4   ? 51.636  -1.150  14.035   1.00 139.15 ? 8    LEU   B N    1 
ATOM   9139  C  CA   . LEU   B  2  4   ? 51.884  -0.942  12.619   1.00 144.08 ? 8    LEU   B CA   1 
ATOM   9140  C  C    . LEU   B  2  4   ? 51.142  0.294   12.115   1.00 147.26 ? 8    LEU   B C    1 
ATOM   9141  O  O    . LEU   B  2  4   ? 50.343  0.910   12.825   1.00 143.61 ? 8    LEU   B O    1 
ATOM   9142  C  CB   . LEU   B  2  4   ? 51.467  -2.175  11.819   1.00 143.21 ? 8    LEU   B CB   1 
ATOM   9143  C  CG   . LEU   B  2  4   ? 52.097  -3.503  12.251   1.00 147.09 ? 8    LEU   B CG   1 
ATOM   9144  C  CD1  . LEU   B  2  4   ? 51.764  -4.597  11.246   1.00 149.47 ? 8    LEU   B CD1  1 
ATOM   9145  C  CD2  . LEU   B  2  4   ? 53.603  -3.374  12.431   1.00 152.88 ? 8    LEU   B CD2  1 
ATOM   9146  H  H    . LEU   B  2  4   ? 51.035  -1.742  14.202   1.00 166.97 ? 8    LEU   B H    1 
ATOM   9147  H  HA   . LEU   B  2  4   ? 52.834  -0.798  12.483   1.00 172.88 ? 8    LEU   B HA   1 
ATOM   9148  H  HB2  . LEU   B  2  4   ? 50.505  -2.275  11.897   1.00 171.83 ? 8    LEU   B HB2  1 
ATOM   9149  H  HB3  . LEU   B  2  4   ? 51.711  -2.031  10.891   1.00 171.83 ? 8    LEU   B HB3  1 
ATOM   9150  H  HG   . LEU   B  2  4   ? 51.727  -3.754  13.112   1.00 176.49 ? 8    LEU   B HG   1 
ATOM   9151  H  HD11 . LEU   B  2  4   ? 52.362  -5.347  11.386   1.00 179.35 ? 8    LEU   B HD11 1 
ATOM   9152  H  HD12 . LEU   B  2  4   ? 50.845  -4.878  11.378   1.00 179.35 ? 8    LEU   B HD12 1 
ATOM   9153  H  HD13 . LEU   B  2  4   ? 51.877  -4.246  10.349   1.00 179.35 ? 8    LEU   B HD13 1 
ATOM   9154  H  HD21 . LEU   B  2  4   ? 53.970  -4.243  12.657   1.00 183.43 ? 8    LEU   B HD21 1 
ATOM   9155  H  HD22 . LEU   B  2  4   ? 53.994  -3.056  11.602   1.00 183.43 ? 8    LEU   B HD22 1 
ATOM   9156  H  HD23 . LEU   B  2  4   ? 53.784  -2.743  13.145   1.00 183.43 ? 8    LEU   B HD23 1 
ATOM   9157  N  N    . GLY   B  2  5   ? 51.422  0.650   10.861   1.00 155.18 ? 9    GLY   B N    1 
ATOM   9158  C  CA   . GLY   B  2  5   ? 50.838  1.821   10.236   1.00 155.61 ? 9    GLY   B CA   1 
ATOM   9159  C  C    . GLY   B  2  5   ? 49.360  1.978   10.518   1.00 148.63 ? 9    GLY   B C    1 
ATOM   9160  O  O    . GLY   B  2  5   ? 48.625  0.990   10.608   1.00 145.89 ? 9    GLY   B O    1 
ATOM   9161  H  H    . GLY   B  2  5   ? 51.957  0.217   10.346   1.00 186.20 ? 9    GLY   B H    1 
ATOM   9162  H  HA2  . GLY   B  2  5   ? 51.293  2.613   10.562   1.00 186.71 ? 9    GLY   B HA2  1 
ATOM   9163  H  HA3  . GLY   B  2  5   ? 50.957  1.760   9.276    1.00 186.71 ? 9    GLY   B HA3  1 
ATOM   9164  N  N    . GLY   B  2  6   ? 48.912  3.223   10.656   1.00 143.73 ? 10   GLY   B N    1 
ATOM   9165  C  CA   . GLY   B  2  6   ? 47.561  3.489   11.101   1.00 133.64 ? 10   GLY   B CA   1 
ATOM   9166  C  C    . GLY   B  2  6   ? 47.496  3.481   12.613   1.00 126.04 ? 10   GLY   B C    1 
ATOM   9167  O  O    . GLY   B  2  6   ? 48.430  3.941   13.278   1.00 123.39 ? 10   GLY   B O    1 
ATOM   9168  H  H    . GLY   B  2  6   ? 49.377  3.928   10.496   1.00 172.46 ? 10   GLY   B H    1 
ATOM   9169  H  HA2  . GLY   B  2  6   ? 47.273  4.357   10.778   1.00 160.35 ? 10   GLY   B HA2  1 
ATOM   9170  H  HA3  . GLY   B  2  6   ? 46.961  2.809   10.757   1.00 160.35 ? 10   GLY   B HA3  1 
ATOM   9171  N  N    . ALA   B  2  7   ? 46.406  2.959   13.169   1.00 123.94 ? 11   ALA   B N    1 
ATOM   9172  C  CA   . ALA   B  2  7   ? 46.269  2.781   14.611   1.00 123.39 ? 11   ALA   B CA   1 
ATOM   9173  C  C    . ALA   B  2  7   ? 46.596  4.073   15.359   1.00 121.32 ? 11   ALA   B C    1 
ATOM   9174  O  O    . ALA   B  2  7   ? 47.378  4.093   16.312   1.00 118.61 ? 11   ALA   B O    1 
ATOM   9175  C  CB   . ALA   B  2  7   ? 47.151  1.629   15.098   1.00 128.15 ? 11   ALA   B CB   1 
ATOM   9176  H  H    . ALA   B  2  7   ? 45.719  2.695   12.723   1.00 148.70 ? 11   ALA   B H    1 
ATOM   9177  H  HA   . ALA   B  2  7   ? 45.345  2.559   14.806   1.00 148.05 ? 11   ALA   B HA   1 
ATOM   9178  H  HB1  . ALA   B  2  7   ? 46.704  1.178   15.832   1.00 153.76 ? 11   ALA   B HB1  1 
ATOM   9179  H  HB2  . ALA   B  2  7   ? 47.293  1.009   14.366   1.00 153.76 ? 11   ALA   B HB2  1 
ATOM   9180  H  HB3  . ALA   B  2  7   ? 48.001  1.987   15.398   1.00 153.76 ? 11   ALA   B HB3  1 
ATOM   9181  N  N    . GLU   B  2  8   ? 45.989  5.168   14.908   1.00 121.32 ? 12   GLU   B N    1 
ATOM   9182  C  CA   . GLU   B  2  8   ? 46.105  6.456   15.578   1.00 118.56 ? 12   GLU   B CA   1 
ATOM   9183  C  C    . GLU   B  2  8   ? 44.893  6.773   16.444   1.00 107.57 ? 12   GLU   B C    1 
ATOM   9184  O  O    . GLU   B  2  8   ? 44.853  7.840   17.065   1.00 104.17 ? 12   GLU   B O    1 
ATOM   9185  C  CB   . GLU   B  2  8   ? 46.314  7.571   14.548   1.00 125.91 ? 12   GLU   B CB   1 
ATOM   9186  C  CG   . GLU   B  2  8   ? 47.658  7.505   13.837   1.00 132.81 ? 12   GLU   B CG   1 
ATOM   9187  C  CD   . GLU   B  2  8   ? 47.844  8.619   12.825   1.00 137.74 ? 12   GLU   B CD   1 
ATOM   9188  O  OE1  . GLU   B  2  8   ? 46.858  9.324   12.523   1.00 137.94 ? 12   GLU   B OE1  1 
ATOM   9189  O  OE2  . GLU   B  2  8   ? 48.978  8.789   12.331   1.00 141.94 ? 12   GLU   B OE2  1 
ATOM   9190  H  H    . GLU   B  2  8   ? 45.496  5.189   14.204   1.00 145.57 ? 12   GLU   B H    1 
ATOM   9191  H  HA   . GLU   B  2  8   ? 46.886  6.440   16.153   1.00 142.26 ? 12   GLU   B HA   1 
ATOM   9192  H  HB2  . GLU   B  2  8   ? 45.619  7.508   13.874   1.00 151.07 ? 12   GLU   B HB2  1 
ATOM   9193  H  HB3  . GLU   B  2  8   ? 46.260  8.428   15.000   1.00 151.07 ? 12   GLU   B HB3  1 
ATOM   9194  H  HG2  . GLU   B  2  8   ? 48.367  7.577   14.495   1.00 159.36 ? 12   GLU   B HG2  1 
ATOM   9195  H  HG3  . GLU   B  2  8   ? 47.726  6.659   13.367   1.00 159.36 ? 12   GLU   B HG3  1 
ATOM   9196  N  N    . THR   B  2  9   ? 43.911  5.876   16.499   1.00 103.67 ? 13   THR   B N    1 
ATOM   9197  C  CA   . THR   B  2  9   ? 42.732  6.035   17.338   1.00 103.40 ? 13   THR   B CA   1 
ATOM   9198  C  C    . THR   B  2  9   ? 42.504  4.748   18.118   1.00 100.87 ? 13   THR   B C    1 
ATOM   9199  O  O    . THR   B  2  9   ? 42.908  3.665   17.685   1.00 105.41 ? 13   THR   B O    1 
ATOM   9200  C  CB   . THR   B  2  9   ? 41.482  6.362   16.506   1.00 107.65 ? 13   THR   B CB   1 
ATOM   9201  O  OG1  . THR   B  2  9   ? 41.834  7.233   15.425   1.00 114.89 ? 13   THR   B OG1  1 
ATOM   9202  C  CG2  . THR   B  2  9   ? 40.426  7.040   17.366   1.00 107.94 ? 13   THR   B CG2  1 
ATOM   9203  H  H    . THR   B  2  9   ? 43.907  5.145   16.045   1.00 124.39 ? 13   THR   B H    1 
ATOM   9204  H  HA   . THR   B  2  9   ? 42.873  6.761   17.965   1.00 124.06 ? 13   THR   B HA   1 
ATOM   9205  H  HB   . THR   B  2  9   ? 41.110  5.539   16.153   1.00 129.16 ? 13   THR   B HB   1 
ATOM   9206  H  HG1  . THR   B  2  9   ? 41.146  7.606   15.120   1.00 137.85 ? 13   THR   B HG1  1 
ATOM   9207  H  HG21 . THR   B  2  9   ? 39.772  7.481   16.802   1.00 129.50 ? 13   THR   B HG21 1 
ATOM   9208  H  HG22 . THR   B  2  9   ? 39.974  6.382   17.917   1.00 129.50 ? 13   THR   B HG22 1 
ATOM   9209  H  HG23 . THR   B  2  9   ? 40.842  7.700   17.942   1.00 129.50 ? 13   THR   B HG23 1 
ATOM   9210  N  N    . CYS   B  2  10  ? 41.856  4.872   19.279   1.00 96.23  ? 14   CYS   B N    1 
ATOM   9211  C  CA   . CYS   B  2  10  ? 41.532  3.684   20.063   1.00 96.60  ? 14   CYS   B CA   1 
ATOM   9212  C  C    . CYS   B  2  10  ? 40.693  2.713   19.242   1.00 95.40  ? 14   CYS   B C    1 
ATOM   9213  O  O    . CYS   B  2  10  ? 40.972  1.509   19.201   1.00 92.35  ? 14   CYS   B O    1 
ATOM   9214  C  CB   . CYS   B  2  10  ? 40.803  4.074   21.350   1.00 98.57  ? 14   CYS   B CB   1 
ATOM   9215  S  SG   . CYS   B  2  10  ? 40.714  2.729   22.564   1.00 102.30 ? 14   CYS   B SG   1 
ATOM   9216  H  H    . CYS   B  2  10  ? 41.599  5.616   19.625   1.00 115.45 ? 14   CYS   B H    1 
ATOM   9217  H  HA   . CYS   B  2  10  ? 42.358  3.241   20.316   1.00 115.90 ? 14   CYS   B HA   1 
ATOM   9218  H  HB2  . CYS   B  2  10  ? 41.271  4.817   21.763   1.00 118.26 ? 14   CYS   B HB2  1 
ATOM   9219  H  HB3  . CYS   B  2  10  ? 39.896  4.336   21.129   1.00 118.26 ? 14   CYS   B HB3  1 
ATOM   9220  N  N    . GLU   B  2  11  ? 39.657  3.225   18.573   1.00 98.36  ? 15   GLU   B N    1 
ATOM   9221  C  CA   . GLU   B  2  11  ? 38.855  2.383   17.692   1.00 100.64 ? 15   GLU   B CA   1 
ATOM   9222  C  C    . GLU   B  2  11  ? 39.701  1.809   16.562   1.00 97.86  ? 15   GLU   B C    1 
ATOM   9223  O  O    . GLU   B  2  11  ? 39.580  0.625   16.227   1.00 95.49  ? 15   GLU   B O    1 
ATOM   9224  C  CB   . GLU   B  2  11  ? 37.677  3.189   17.138   1.00 107.87 ? 15   GLU   B CB   1 
ATOM   9225  C  CG   . GLU   B  2  11  ? 36.938  2.525   15.988   1.00 112.64 ? 15   GLU   B CG   1 
ATOM   9226  C  CD   . GLU   B  2  11  ? 35.716  3.310   15.553   1.00 116.50 ? 15   GLU   B CD   1 
ATOM   9227  O  OE1  . GLU   B  2  11  ? 35.218  4.133   16.351   1.00 117.25 ? 15   GLU   B OE1  1 
ATOM   9228  O  OE2  . GLU   B  2  11  ? 35.255  3.104   14.411   1.00 118.41 ? 15   GLU   B OE2  1 
ATOM   9229  H  H    . GLU   B  2  11  ? 39.404  4.046   18.611   1.00 118.01 ? 15   GLU   B H    1 
ATOM   9230  H  HA   . GLU   B  2  11  ? 38.495  1.640   18.201   1.00 120.75 ? 15   GLU   B HA   1 
ATOM   9231  H  HB2  . GLU   B  2  11  ? 37.038  3.331   17.854   1.00 129.43 ? 15   GLU   B HB2  1 
ATOM   9232  H  HB3  . GLU   B  2  11  ? 38.011  4.041   16.818   1.00 129.43 ? 15   GLU   B HB3  1 
ATOM   9233  H  HG2  . GLU   B  2  11  ? 37.535  2.453   15.227   1.00 135.14 ? 15   GLU   B HG2  1 
ATOM   9234  H  HG3  . GLU   B  2  11  ? 36.645  1.643   16.266   1.00 135.14 ? 15   GLU   B HG3  1 
ATOM   9235  N  N    . ASP   B  2  12  ? 40.566  2.632   15.963   1.00 99.38  ? 16   ASP   B N    1 
ATOM   9236  C  CA   . ASP   B  2  12  ? 41.454  2.132   14.918   1.00 101.23 ? 16   ASP   B CA   1 
ATOM   9237  C  C    . ASP   B  2  12  ? 42.433  1.106   15.474   1.00 100.96 ? 16   ASP   B C    1 
ATOM   9238  O  O    . ASP   B  2  12  ? 42.787  0.138   14.791   1.00 103.90 ? 16   ASP   B O    1 
ATOM   9239  C  CB   . ASP   B  2  12  ? 42.211  3.291   14.270   1.00 103.46 ? 16   ASP   B CB   1 
ATOM   9240  C  CG   . ASP   B  2  12  ? 41.343  4.100   13.325   1.00 104.10 ? 16   ASP   B CG   1 
ATOM   9241  O  OD1  . ASP   B  2  12  ? 40.122  3.844   13.268   1.00 102.49 ? 16   ASP   B OD1  1 
ATOM   9242  O  OD2  . ASP   B  2  12  ? 41.884  4.989   12.634   1.00 106.83 ? 16   ASP   B OD2  1 
ATOM   9243  H  H    . ASP   B  2  12  ? 40.656  3.468   16.142   1.00 119.24 ? 16   ASP   B H    1 
ATOM   9244  H  HA   . ASP   B  2  12  ? 40.917  1.702   14.233   1.00 121.46 ? 16   ASP   B HA   1 
ATOM   9245  H  HB2  . ASP   B  2  12  ? 42.533  3.886   14.965   1.00 124.14 ? 16   ASP   B HB2  1 
ATOM   9246  H  HB3  . ASP   B  2  12  ? 42.958  2.938   13.763   1.00 124.14 ? 16   ASP   B HB3  1 
ATOM   9247  N  N    . CYS   B  2  13  ? 42.884  1.304   16.713   1.00 98.44  ? 17   CYS   B N    1 
ATOM   9248  C  CA   . CYS   B  2  13  ? 43.819  0.365   17.322   1.00 100.81 ? 17   CYS   B CA   1 
ATOM   9249  C  C    . CYS   B  2  13  ? 43.156  -0.981  17.583   1.00 104.45 ? 17   CYS   B C    1 
ATOM   9250  O  O    . CYS   B  2  13  ? 43.723  -2.036  17.274   1.00 108.10 ? 17   CYS   B O    1 
ATOM   9251  C  CB   . CYS   B  2  13  ? 44.368  0.953   18.620   1.00 99.08  ? 17   CYS   B CB   1 
ATOM   9252  S  SG   . CYS   B  2  13  ? 45.253  -0.238  19.637   1.00 102.99 ? 17   CYS   B SG   1 
ATOM   9253  H  H    . CYS   B  2  13  ? 42.666  1.967   17.215   1.00 118.11 ? 17   CYS   B H    1 
ATOM   9254  H  HA   . CYS   B  2  13  ? 44.561  0.221   16.714   1.00 120.95 ? 17   CYS   B HA   1 
ATOM   9255  H  HB2  . CYS   B  2  13  ? 44.982  1.671   18.401   1.00 118.87 ? 17   CYS   B HB2  1 
ATOM   9256  H  HB3  . CYS   B  2  13  ? 43.627  1.297   19.143   1.00 118.87 ? 17   CYS   B HB3  1 
ATOM   9257  N  N    . LEU   B  2  14  ? 41.952  -0.964  18.160   1.00 101.87 ? 18   LEU   B N    1 
ATOM   9258  C  CA   . LEU   B  2  14  ? 41.241  -2.208  18.430   1.00 97.69  ? 18   LEU   B CA   1 
ATOM   9259  C  C    . LEU   B  2  14  ? 41.037  -3.028  17.164   1.00 95.97  ? 18   LEU   B C    1 
ATOM   9260  O  O    . LEU   B  2  14  ? 40.993  -4.262  17.223   1.00 97.71  ? 18   LEU   B O    1 
ATOM   9261  C  CB   . LEU   B  2  14  ? 39.889  -1.904  19.073   1.00 95.24  ? 18   LEU   B CB   1 
ATOM   9262  C  CG   . LEU   B  2  14  ? 39.794  -2.004  20.596   1.00 97.65  ? 18   LEU   B CG   1 
ATOM   9263  C  CD1  . LEU   B  2  14  ? 40.909  -1.230  21.273   1.00 102.58 ? 18   LEU   B CD1  1 
ATOM   9264  C  CD2  . LEU   B  2  14  ? 38.433  -1.505  21.063   1.00 93.56  ? 18   LEU   B CD2  1 
ATOM   9265  H  H    . LEU   B  2  14  ? 41.533  -0.253  18.401   1.00 122.22 ? 18   LEU   B H    1 
ATOM   9266  H  HA   . LEU   B  2  14  ? 41.767  -2.737  19.050   1.00 117.21 ? 18   LEU   B HA   1 
ATOM   9267  H  HB2  . LEU   B  2  14  ? 39.645  -0.995  18.836   1.00 114.27 ? 18   LEU   B HB2  1 
ATOM   9268  H  HB3  . LEU   B  2  14  ? 39.240  -2.527  18.710   1.00 114.27 ? 18   LEU   B HB3  1 
ATOM   9269  H  HG   . LEU   B  2  14  ? 39.892  -2.933  20.856   1.00 117.16 ? 18   LEU   B HG   1 
ATOM   9270  H  HD11 . LEU   B  2  14  ? 40.765  -1.244  22.232   1.00 123.08 ? 18   LEU   B HD11 1 
ATOM   9271  H  HD12 . LEU   B  2  14  ? 41.758  -1.649  21.060   1.00 123.08 ? 18   LEU   B HD12 1 
ATOM   9272  H  HD13 . LEU   B  2  14  ? 40.900  -0.316  20.950   1.00 123.08 ? 18   LEU   B HD13 1 
ATOM   9273  H  HD21 . LEU   B  2  14  ? 38.466  -1.345  22.019   1.00 112.26 ? 18   LEU   B HD21 1 
ATOM   9274  H  HD22 . LEU   B  2  14  ? 38.222  -0.680  20.597   1.00 112.26 ? 18   LEU   B HD22 1 
ATOM   9275  H  HD23 . LEU   B  2  14  ? 37.764  -2.178  20.863   1.00 112.26 ? 18   LEU   B HD23 1 
ATOM   9276  N  N    . LEU   B  2  15  ? 40.910  -2.365  16.014   1.00 95.48  ? 19   LEU   B N    1 
ATOM   9277  C  CA   . LEU   B  2  15  ? 40.555  -3.070  14.788   1.00 98.93  ? 19   LEU   B CA   1 
ATOM   9278  C  C    . LEU   B  2  15  ? 41.717  -3.889  14.239   1.00 102.01 ? 19   LEU   B C    1 
ATOM   9279  O  O    . LEU   B  2  15  ? 41.494  -4.932  13.614   1.00 105.96 ? 19   LEU   B O    1 
ATOM   9280  C  CB   . LEU   B  2  15  ? 40.079  -2.067  13.738   1.00 103.10 ? 19   LEU   B CB   1 
ATOM   9281  C  CG   . LEU   B  2  15  ? 39.548  -2.647  12.427   1.00 107.84 ? 19   LEU   B CG   1 
ATOM   9282  C  CD1  . LEU   B  2  15  ? 38.272  -3.439  12.663   1.00 105.92 ? 19   LEU   B CD1  1 
ATOM   9283  C  CD2  . LEU   B  2  15  ? 39.316  -1.532  11.419   1.00 110.54 ? 19   LEU   B CD2  1 
ATOM   9284  H  H    . LEU   B  2  15  ? 41.023  -1.518  15.919   1.00 114.56 ? 19   LEU   B H    1 
ATOM   9285  H  HA   . LEU   B  2  15  ? 39.830  -3.684  14.983   1.00 118.70 ? 19   LEU   B HA   1 
ATOM   9286  H  HB2  . LEU   B  2  15  ? 39.362  -1.543  14.128   1.00 123.71 ? 19   LEU   B HB2  1 
ATOM   9287  H  HB3  . LEU   B  2  15  ? 40.827  -1.492  13.513   1.00 123.71 ? 19   LEU   B HB3  1 
ATOM   9288  H  HG   . LEU   B  2  15  ? 40.207  -3.256  12.058   1.00 129.39 ? 19   LEU   B HG   1 
ATOM   9289  H  HD11 . LEU   B  2  15  ? 37.974  -3.817  11.820   1.00 127.08 ? 19   LEU   B HD11 1 
ATOM   9290  H  HD12 . LEU   B  2  15  ? 38.454  -4.150  13.297   1.00 127.08 ? 19   LEU   B HD12 1 
ATOM   9291  H  HD13 . LEU   B  2  15  ? 37.592  -2.845  13.017   1.00 127.08 ? 19   LEU   B HD13 1 
ATOM   9292  H  HD21 . LEU   B  2  15  ? 39.119  -1.924  10.554   1.00 132.62 ? 19   LEU   B HD21 1 
ATOM   9293  H  HD22 . LEU   B  2  15  ? 38.567  -0.990  11.714   1.00 132.62 ? 19   LEU   B HD22 1 
ATOM   9294  H  HD23 . LEU   B  2  15  ? 40.116  -0.987  11.360   1.00 132.62 ? 19   LEU   B HD23 1 
ATOM   9295  N  N    . ILE   B  2  16  ? 42.954  -3.443  14.458   1.00 102.19 ? 20   ILE   B N    1 
ATOM   9296  C  CA   . ILE   B  2  16  ? 44.090  -4.082  13.801   1.00 107.75 ? 20   ILE   B CA   1 
ATOM   9297  C  C    . ILE   B  2  16  ? 44.351  -5.464  14.388   1.00 110.67 ? 20   ILE   B C    1 
ATOM   9298  O  O    . ILE   B  2  16  ? 44.682  -6.406  13.658   1.00 114.89 ? 20   ILE   B O    1 
ATOM   9299  C  CB   . ILE   B  2  16  ? 45.336  -3.182  13.893   1.00 114.36 ? 20   ILE   B CB   1 
ATOM   9300  C  CG1  . ILE   B  2  16  ? 45.103  -1.856  13.160   1.00 116.84 ? 20   ILE   B CG1  1 
ATOM   9301  C  CG2  . ILE   B  2  16  ? 46.557  -3.896  13.323   1.00 120.16 ? 20   ILE   B CG2  1 
ATOM   9302  C  CD1  . ILE   B  2  16  ? 44.851  -1.991  11.663   1.00 121.52 ? 20   ILE   B CD1  1 
ATOM   9303  H  H    . ILE   B  2  16  ? 43.159  -2.785  14.973   1.00 122.61 ? 20   ILE   B H    1 
ATOM   9304  H  HA   . ILE   B  2  16  ? 43.870  -4.197  12.863   1.00 129.28 ? 20   ILE   B HA   1 
ATOM   9305  H  HB   . ILE   B  2  16  ? 45.499  -2.991  14.830   1.00 137.21 ? 20   ILE   B HB   1 
ATOM   9306  H  HG12 . ILE   B  2  16  ? 44.327  -1.422  13.548   1.00 140.19 ? 20   ILE   B HG12 1 
ATOM   9307  H  HG13 . ILE   B  2  16  ? 45.887  -1.298  13.275   1.00 140.19 ? 20   ILE   B HG13 1 
ATOM   9308  H  HG21 . ILE   B  2  16  ? 47.288  -3.263  13.252   1.00 144.17 ? 20   ILE   B HG21 1 
ATOM   9309  H  HG22 . ILE   B  2  16  ? 46.804  -4.622  13.916   1.00 144.17 ? 20   ILE   B HG22 1 
ATOM   9310  H  HG23 . ILE   B  2  16  ? 46.336  -4.246  12.445   1.00 144.17 ? 20   ILE   B HG23 1 
ATOM   9311  H  HD11 . ILE   B  2  16  ? 44.043  -1.506  11.433   1.00 145.80 ? 20   ILE   B HD11 1 
ATOM   9312  H  HD12 . ILE   B  2  16  ? 45.608  -1.621  11.181   1.00 145.80 ? 20   ILE   B HD12 1 
ATOM   9313  H  HD13 . ILE   B  2  16  ? 44.747  -2.930  11.443   1.00 145.80 ? 20   ILE   B HD13 1 
ATOM   9314  N  N    . GLY   B  2  17  ? 44.213  -5.614  15.704   1.00 108.43 ? 21   GLY   B N    1 
ATOM   9315  C  CA   . GLY   B  2  17  ? 44.510  -6.872  16.347   1.00 107.20 ? 21   GLY   B CA   1 
ATOM   9316  C  C    . GLY   B  2  17  ? 43.568  -7.208  17.486   1.00 100.44 ? 21   GLY   B C    1 
ATOM   9317  O  O    . GLY   B  2  17  ? 42.979  -6.326  18.120   1.00 97.31  ? 21   GLY   B O    1 
ATOM   9318  H  H    . GLY   B  2  17  ? 43.949  -4.995  16.239   1.00 130.10 ? 21   GLY   B H    1 
ATOM   9319  H  HA2  . GLY   B  2  17  ? 44.454  -7.584  15.691   1.00 128.62 ? 21   GLY   B HA2  1 
ATOM   9320  H  HA3  . GLY   B  2  17  ? 45.412  -6.841  16.703   1.00 128.62 ? 21   GLY   B HA3  1 
ATOM   9321  N  N    . PRO   B  2  18  ? 43.400  -8.507  17.764   1.00 101.05 ? 22   PRO   B N    1 
ATOM   9322  C  CA   . PRO   B  2  18  ? 42.557  -8.907  18.902   1.00 96.75  ? 22   PRO   B CA   1 
ATOM   9323  C  C    . PRO   B  2  18  ? 43.217  -8.755  20.264   1.00 95.64  ? 22   PRO   B C    1 
ATOM   9324  O  O    . PRO   B  2  18  ? 42.495  -8.707  21.269   1.00 89.76  ? 22   PRO   B O    1 
ATOM   9325  C  CB   . PRO   B  2  18  ? 42.247  -10.384 18.610   1.00 102.70 ? 22   PRO   B CB   1 
ATOM   9326  C  CG   . PRO   B  2  18  ? 43.358  -10.843 17.731   1.00 111.80 ? 22   PRO   B CG   1 
ATOM   9327  C  CD   . PRO   B  2  18  ? 43.768  -9.655  16.915   1.00 109.79 ? 22   PRO   B CD   1 
ATOM   9328  H  HA   . PRO   B  2  18  ? 41.735  -8.393  18.893   1.00 116.08 ? 22   PRO   B HA   1 
ATOM   9329  H  HB2  . PRO   B  2  18  ? 42.229  -10.888 19.438   1.00 123.21 ? 22   PRO   B HB2  1 
ATOM   9330  H  HB3  . PRO   B  2  18  ? 41.393  -10.459 18.156   1.00 123.21 ? 22   PRO   B HB3  1 
ATOM   9331  H  HG2  . PRO   B  2  18  ? 44.098  -11.154 18.277   1.00 134.14 ? 22   PRO   B HG2  1 
ATOM   9332  H  HG3  . PRO   B  2  18  ? 43.045  -11.560 17.158   1.00 134.14 ? 22   PRO   B HG3  1 
ATOM   9333  H  HD2  . PRO   B  2  18  ? 44.723  -9.666  16.746   1.00 131.73 ? 22   PRO   B HD2  1 
ATOM   9334  H  HD3  . PRO   B  2  18  ? 43.283  -9.631  16.075   1.00 131.73 ? 22   PRO   B HD3  1 
ATOM   9335  N  N    . GLN   B  2  19  ? 44.547  -8.676  20.341   1.00 104.23 ? 23   GLN   B N    1 
ATOM   9336  C  CA   . GLN   B  2  19  ? 45.248  -8.631  21.619   1.00 115.35 ? 23   GLN   B CA   1 
ATOM   9337  C  C    . GLN   B  2  19  ? 45.843  -7.262  21.929   1.00 118.00 ? 23   GLN   B C    1 
ATOM   9338  O  O    . GLN   B  2  19  ? 46.655  -7.148  22.854   1.00 126.52 ? 23   GLN   B O    1 
ATOM   9339  C  CB   . GLN   B  2  19  ? 46.357  -9.689  21.657   1.00 123.38 ? 23   GLN   B CB   1 
ATOM   9340  C  CG   . GLN   B  2  19  ? 47.526  -9.448  20.702   1.00 124.14 ? 23   GLN   B CG   1 
ATOM   9341  C  CD   . GLN   B  2  19  ? 47.264  -9.975  19.306   1.00 119.91 ? 23   GLN   B CD   1 
ATOM   9342  O  OE1  . GLN   B  2  19  ? 46.313  -9.564  18.642   1.00 108.92 ? 23   GLN   B OE1  1 
ATOM   9343  N  NE2  . GLN   B  2  19  ? 48.109  -10.896 18.855   1.00 128.66 ? 23   GLN   B NE2  1 
ATOM   9344  H  H    . GLN   B  2  19  ? 45.068  -8.647  19.657   1.00 125.05 ? 23   GLN   B H    1 
ATOM   9345  H  HA   . GLN   B  2  19  ? 44.604  -8.836  22.314   1.00 138.40 ? 23   GLN   B HA   1 
ATOM   9346  H  HB2  . GLN   B  2  19  ? 46.720  -9.719  22.556   1.00 148.04 ? 23   GLN   B HB2  1 
ATOM   9347  H  HB3  . GLN   B  2  19  ? 45.969  -10.548 21.428   1.00 148.04 ? 23   GLN   B HB3  1 
ATOM   9348  H  HG2  . GLN   B  2  19  ? 47.687  -8.493  20.636   1.00 148.95 ? 23   GLN   B HG2  1 
ATOM   9349  H  HG3  . GLN   B  2  19  ? 48.314  -9.894  21.048   1.00 148.95 ? 23   GLN   B HG3  1 
ATOM   9350  H  HE21 . GLN   B  2  19  ? 48.761  -11.161 19.350   1.00 154.37 ? 23   GLN   B HE21 1 
ATOM   9351  H  HE22 . GLN   B  2  19  ? 48.004  -11.227 18.069   1.00 154.37 ? 23   GLN   B HE22 1 
ATOM   9352  N  N    . CYS   B  2  20  ? 45.466  -6.226  21.191   1.00 112.45 ? 24   CYS   B N    1 
ATOM   9353  C  CA   . CYS   B  2  20  ? 46.062  -4.907  21.338   1.00 112.92 ? 24   CYS   B CA   1 
ATOM   9354  C  C    . CYS   B  2  20  ? 45.213  -4.031  22.253   1.00 105.91 ? 24   CYS   B C    1 
ATOM   9355  O  O    . CYS   B  2  20  ? 44.027  -4.285  22.475   1.00 101.38 ? 24   CYS   B O    1 
ATOM   9356  C  CB   . CYS   B  2  20  ? 46.231  -4.250  19.967   1.00 116.89 ? 24   CYS   B CB   1 
ATOM   9357  S  SG   . CYS   B  2  20  ? 46.661  -5.448  18.684   1.00 126.34 ? 24   CYS   B SG   1 
ATOM   9358  H  H    . CYS   B  2  20  ? 44.855  -6.264  20.587   1.00 134.92 ? 24   CYS   B H    1 
ATOM   9359  H  HA   . CYS   B  2  20  ? 46.939  -4.987  21.745   1.00 135.49 ? 24   CYS   B HA   1 
ATOM   9360  H  HB2  . CYS   B  2  20  ? 45.397  -3.822  19.715   1.00 140.24 ? 24   CYS   B HB2  1 
ATOM   9361  H  HB3  . CYS   B  2  20  ? 46.940  -3.591  20.015   1.00 140.24 ? 24   CYS   B HB3  1 
ATOM   9362  N  N    . ALA   B  2  21  ? 45.846  -2.988  22.792   1.00 107.61 ? 25   ALA   B N    1 
ATOM   9363  C  CA   . ALA   B  2  21  ? 45.224  -2.125  23.786   1.00 107.77 ? 25   ALA   B CA   1 
ATOM   9364  C  C    . ALA   B  2  21  ? 45.563  -0.672  23.476   1.00 111.67 ? 25   ALA   B C    1 
ATOM   9365  O  O    . ALA   B  2  21  ? 46.248  -0.365  22.497   1.00 112.94 ? 25   ALA   B O    1 
ATOM   9366  C  CB   . ALA   B  2  21  ? 45.678  -2.507  25.201   1.00 109.67 ? 25   ALA   B CB   1 
ATOM   9367  H  H    . ALA   B  2  21  ? 46.650  -2.758  22.591   1.00 129.11 ? 25   ALA   B H    1 
ATOM   9368  H  HA   . ALA   B  2  21  ? 44.262  -2.228  23.728   1.00 129.30 ? 25   ALA   B HA   1 
ATOM   9369  H  HB1  . ALA   B  2  21  ? 45.173  -1.986  25.846   1.00 131.59 ? 25   ALA   B HB1  1 
ATOM   9370  H  HB2  . ALA   B  2  21  ? 45.516  -3.453  25.341   1.00 131.59 ? 25   ALA   B HB2  1 
ATOM   9371  H  HB3  . ALA   B  2  21  ? 46.625  -2.316  25.292   1.00 131.59 ? 25   ALA   B HB3  1 
ATOM   9372  N  N    . TRP   B  2  22  ? 45.075  0.229   24.330   1.00 113.84 ? 26   TRP   B N    1 
ATOM   9373  C  CA   . TRP   B  2  22  ? 45.264  1.663   24.158   1.00 111.16 ? 26   TRP   B CA   1 
ATOM   9374  C  C    . TRP   B  2  22  ? 45.607  2.280   25.507   1.00 113.10 ? 26   TRP   B C    1 
ATOM   9375  O  O    . TRP   B  2  22  ? 45.347  1.697   26.563   1.00 116.43 ? 26   TRP   B O    1 
ATOM   9376  C  CB   . TRP   B  2  22  ? 44.009  2.318   23.562   1.00 107.53 ? 26   TRP   B CB   1 
ATOM   9377  C  CG   . TRP   B  2  22  ? 44.236  3.677   22.967   1.00 106.27 ? 26   TRP   B CG   1 
ATOM   9378  C  CD1  . TRP   B  2  22  ? 43.821  4.873   23.475   1.00 105.91 ? 26   TRP   B CD1  1 
ATOM   9379  C  CD2  . TRP   B  2  22  ? 44.924  3.976   21.746   1.00 104.72 ? 26   TRP   B CD2  1 
ATOM   9380  N  NE1  . TRP   B  2  22  ? 44.209  5.899   22.647   1.00 106.14 ? 26   TRP   B NE1  1 
ATOM   9381  C  CE2  . TRP   B  2  22  ? 44.889  5.375   21.579   1.00 103.97 ? 26   TRP   B CE2  1 
ATOM   9382  C  CE3  . TRP   B  2  22  ? 45.567  3.198   20.780   1.00 105.05 ? 26   TRP   B CE3  1 
ATOM   9383  C  CZ2  . TRP   B  2  22  ? 45.473  6.011   20.485   1.00 102.40 ? 26   TRP   B CZ2  1 
ATOM   9384  C  CZ3  . TRP   B  2  22  ? 46.147  3.831   19.694   1.00 103.88 ? 26   TRP   B CZ3  1 
ATOM   9385  C  CH2  . TRP   B  2  22  ? 46.095  5.223   19.556   1.00 102.35 ? 26   TRP   B CH2  1 
ATOM   9386  H  H    . TRP   B  2  22  ? 44.622  0.026   25.032   1.00 136.59 ? 26   TRP   B H    1 
ATOM   9387  H  HA   . TRP   B  2  22  ? 46.006  1.832   23.556   1.00 133.38 ? 26   TRP   B HA   1 
ATOM   9388  H  HB2  . TRP   B  2  22  ? 43.665  1.745   22.859   1.00 129.02 ? 26   TRP   B HB2  1 
ATOM   9389  H  HB3  . TRP   B  2  22  ? 43.348  2.413   24.266   1.00 129.02 ? 26   TRP   B HB3  1 
ATOM   9390  H  HD1  . TRP   B  2  22  ? 43.345  4.980   24.267   1.00 127.07 ? 26   TRP   B HD1  1 
ATOM   9391  H  HE1  . TRP   B  2  22  ? 44.051  6.734   22.778   1.00 127.35 ? 26   TRP   B HE1  1 
ATOM   9392  H  HE3  . TRP   B  2  22  ? 45.605  2.272   20.864   1.00 126.04 ? 26   TRP   B HE3  1 
ATOM   9393  H  HZ2  . TRP   B  2  22  ? 45.440  6.936   20.390   1.00 122.86 ? 26   TRP   B HZ2  1 
ATOM   9394  H  HZ3  . TRP   B  2  22  ? 46.579  3.324   19.046   1.00 124.63 ? 26   TRP   B HZ3  1 
ATOM   9395  H  HH2  . TRP   B  2  22  ? 46.493  5.621   18.815   1.00 122.81 ? 26   TRP   B HH2  1 
ATOM   9396  N  N    . CYS   B  2  23  ? 46.196  3.472   25.461   1.00 114.57 ? 27   CYS   B N    1 
ATOM   9397  C  CA   . CYS   B  2  23  ? 46.680  4.173   26.643   1.00 119.82 ? 27   CYS   B CA   1 
ATOM   9398  C  C    . CYS   B  2  23  ? 46.000  5.533   26.753   1.00 119.36 ? 27   CYS   B C    1 
ATOM   9399  O  O    . CYS   B  2  23  ? 45.380  6.023   25.805   1.00 117.03 ? 27   CYS   B O    1 
ATOM   9400  C  CB   . CYS   B  2  23  ? 48.204  4.342   26.584   1.00 125.15 ? 27   CYS   B CB   1 
ATOM   9401  S  SG   . CYS   B  2  23  ? 48.995  4.966   28.088   1.00 133.42 ? 27   CYS   B SG   1 
ATOM   9402  H  H    . CYS   B  2  23  ? 46.329  3.908   24.732   1.00 137.46 ? 27   CYS   B H    1 
ATOM   9403  H  HA   . CYS   B  2  23  ? 46.458  3.662   27.436   1.00 143.77 ? 27   CYS   B HA   1 
ATOM   9404  H  HB2  . CYS   B  2  23  ? 48.597  3.476   26.393   1.00 150.17 ? 27   CYS   B HB2  1 
ATOM   9405  H  HB3  . CYS   B  2  23  ? 48.413  4.965   25.871   1.00 150.17 ? 27   CYS   B HB3  1 
ATOM   9406  N  N    . ALA   B  2  24  ? 46.122  6.147   27.931   1.00 121.94 ? 28   ALA   B N    1 
ATOM   9407  C  CA   . ALA   B  2  24  ? 45.482  7.431   28.198   1.00 117.36 ? 28   ALA   B CA   1 
ATOM   9408  C  C    . ALA   B  2  24  ? 46.419  8.335   28.984   1.00 119.05 ? 28   ALA   B C    1 
ATOM   9409  O  O    . ALA   B  2  24  ? 46.877  7.970   30.071   1.00 119.31 ? 28   ALA   B O    1 
ATOM   9410  C  CB   . ALA   B  2  24  ? 44.165  7.241   28.960   1.00 114.81 ? 28   ALA   B CB   1 
ATOM   9411  H  H    . ALA   B  2  24  ? 46.573  5.835   28.594   1.00 146.31 ? 28   ALA   B H    1 
ATOM   9412  H  HA   . ALA   B  2  24  ? 45.303  7.864   27.349   1.00 140.81 ? 28   ALA   B HA   1 
ATOM   9413  H  HB1  . ALA   B  2  24  ? 43.740  8.106   29.077   1.00 137.76 ? 28   ALA   B HB1  1 
ATOM   9414  H  HB2  . ALA   B  2  24  ? 43.585  6.655   28.449   1.00 137.76 ? 28   ALA   B HB2  1 
ATOM   9415  H  HB3  . ALA   B  2  24  ? 44.355  6.847   29.826   1.00 137.76 ? 28   ALA   B HB3  1 
ATOM   9416  N  N    . GLN   B  2  25  ? 46.692  9.514   28.427   1.00 121.50 ? 29   GLN   B N    1 
ATOM   9417  C  CA   . GLN   B  2  25  ? 47.282  10.698  29.042   1.00 127.62 ? 29   GLN   B CA   1 
ATOM   9418  C  C    . GLN   B  2  25  ? 48.804  10.625  29.200   1.00 129.11 ? 29   GLN   B C    1 
ATOM   9419  O  O    . GLN   B  2  25  ? 49.408  11.630  29.582   1.00 130.75 ? 29   GLN   B O    1 
ATOM   9420  C  CB   . GLN   B  2  25  ? 46.663  11.025  30.417   1.00 132.92 ? 29   GLN   B CB   1 
ATOM   9421  C  CG   . GLN   B  2  25  ? 46.988  12.419  30.962   1.00 136.01 ? 29   GLN   B CG   1 
ATOM   9422  C  CD   . GLN   B  2  25  ? 46.667  13.540  29.984   1.00 132.03 ? 29   GLN   B CD   1 
ATOM   9423  O  OE1  . GLN   B  2  25  ? 47.262  13.635  28.910   1.00 131.13 ? 29   GLN   B OE1  1 
ATOM   9424  N  NE2  . GLN   B  2  25  ? 45.727  14.399  30.357   1.00 130.18 ? 29   GLN   B NE2  1 
ATOM   9425  H  H    . GLN   B  2  25  ? 46.522  9.663   27.597   1.00 145.78 ? 29   GLN   B H    1 
ATOM   9426  H  HA   . GLN   B  2  25  ? 47.111  11.441  28.441   1.00 153.12 ? 29   GLN   B HA   1 
ATOM   9427  H  HB2  . GLN   B  2  25  ? 45.698  10.961  30.342   1.00 159.48 ? 29   GLN   B HB2  1 
ATOM   9428  H  HB3  . GLN   B  2  25  ? 46.990  10.378  31.062   1.00 159.48 ? 29   GLN   B HB3  1 
ATOM   9429  H  HG2  . GLN   B  2  25  ? 46.470  12.570  31.767   1.00 163.20 ? 29   GLN   B HG2  1 
ATOM   9430  H  HG3  . GLN   B  2  25  ? 47.936  12.463  31.164   1.00 163.20 ? 29   GLN   B HG3  1 
ATOM   9431  H  HE21 . GLN   B  2  25  ? 45.336  14.305  31.117   1.00 156.19 ? 29   GLN   B HE21 1 
ATOM   9432  H  HE22 . GLN   B  2  25  ? 45.509  15.050  29.840   1.00 156.19 ? 29   GLN   B HE22 1 
ATOM   9433  N  N    . GLU   B  2  26  ? 49.448  9.501   28.905   1.00 126.16 ? 30   GLU   B N    1 
ATOM   9434  C  CA   . GLU   B  2  26  ? 50.909  9.411   28.847   1.00 123.88 ? 30   GLU   B CA   1 
ATOM   9435  C  C    . GLU   B  2  26  ? 51.566  10.120  30.033   1.00 128.07 ? 30   GLU   B C    1 
ATOM   9436  O  O    . GLU   B  2  26  ? 52.389  11.023  29.883   1.00 122.60 ? 30   GLU   B O    1 
ATOM   9437  C  CB   . GLU   B  2  26  ? 51.423  9.979   27.521   1.00 118.44 ? 30   GLU   B CB   1 
ATOM   9438  C  CG   . GLU   B  2  26  ? 52.912  9.779   27.280   1.00 119.84 ? 30   GLU   B CG   1 
ATOM   9439  C  CD   . GLU   B  2  26  ? 53.263  9.734   25.803   1.00 118.13 ? 30   GLU   B CD   1 
ATOM   9440  O  OE1  . GLU   B  2  26  ? 52.441  10.187  24.978   1.00 114.63 ? 30   GLU   B OE1  1 
ATOM   9441  O  OE2  . GLU   B  2  26  ? 54.358  9.237   25.467   1.00 121.18 ? 30   GLU   B OE2  1 
ATOM   9442  H  H    . GLU   B  2  26  ? 49.054  8.757   28.731   1.00 151.37 ? 30   GLU   B H    1 
ATOM   9443  H  HA   . GLU   B  2  26  ? 51.154  8.474   28.905   1.00 148.63 ? 30   GLU   B HA   1 
ATOM   9444  H  HB2  . GLU   B  2  26  ? 50.948  9.545   26.795   1.00 142.10 ? 30   GLU   B HB2  1 
ATOM   9445  H  HB3  . GLU   B  2  26  ? 51.250  10.933  27.508   1.00 142.10 ? 30   GLU   B HB3  1 
ATOM   9446  H  HG2  . GLU   B  2  26  ? 53.400  10.514  27.683   1.00 143.79 ? 30   GLU   B HG2  1 
ATOM   9447  H  HG3  . GLU   B  2  26  ? 53.188  8.939   27.679   1.00 143.79 ? 30   GLU   B HG3  1 
ATOM   9448  N  N    . ASN   B  2  27  ? 51.185  9.690   31.232   1.00 138.69 ? 31   ASN   B N    1 
ATOM   9449  C  CA   . ASN   B  2  27  ? 51.766  10.242  32.453   1.00 146.97 ? 31   ASN   B CA   1 
ATOM   9450  C  C    . ASN   B  2  27  ? 53.272  10.004  32.490   1.00 142.94 ? 31   ASN   B C    1 
ATOM   9451  O  O    . ASN   B  2  27  ? 54.018  10.773  33.098   1.00 140.45 ? 31   ASN   B O    1 
ATOM   9452  C  CB   . ASN   B  2  27  ? 51.112  9.629   33.692   1.00 158.11 ? 31   ASN   B CB   1 
ATOM   9453  C  CG   . ASN   B  2  27  ? 49.705  10.142  33.924   1.00 159.98 ? 31   ASN   B CG   1 
ATOM   9454  O  OD1  . ASN   B  2  27  ? 49.337  11.217  33.450   1.00 157.66 ? 31   ASN   B OD1  1 
ATOM   9455  N  ND2  . ASN   B  2  27  ? 48.911  9.377   34.664   1.00 163.31 ? 31   ASN   B ND2  1 
ATOM   9456  H  H    . ASN   B  2  27  ? 50.592  9.081   31.366   1.00 166.40 ? 31   ASN   B H    1 
ATOM   9457  H  HA   . ASN   B  2  27  ? 51.605  11.198  32.473   1.00 176.35 ? 31   ASN   B HA   1 
ATOM   9458  H  HB2  . ASN   B  2  27  ? 51.066  8.666   33.582   1.00 189.72 ? 31   ASN   B HB2  1 
ATOM   9459  H  HB3  . ASN   B  2  27  ? 51.644  9.849   34.473   1.00 189.72 ? 31   ASN   B HB3  1 
ATOM   9460  H  HD21 . ASN   B  2  27  ? 48.103  9.624   34.824   1.00 195.95 ? 31   ASN   B HD21 1 
ATOM   9461  H  HD22 . ASN   B  2  27  ? 49.205  8.634   34.983   1.00 195.95 ? 31   ASN   B HD22 1 
ATOM   9462  N  N    . GLY   B  2  35  ? 52.113  9.563   19.197   1.00 117.69 ? 39   GLY   B N    1 
ATOM   9463  C  CA   . GLY   B  2  35  ? 52.869  8.334   19.348   1.00 120.53 ? 39   GLY   B CA   1 
ATOM   9464  C  C    . GLY   B  2  35  ? 52.081  7.108   18.935   1.00 119.50 ? 39   GLY   B C    1 
ATOM   9465  O  O    . GLY   B  2  35  ? 51.104  7.206   18.191   1.00 115.36 ? 39   GLY   B O    1 
ATOM   9466  H  HA2  . GLY   B  2  35  ? 53.668  8.382   18.799   1.00 144.61 ? 39   GLY   B HA2  1 
ATOM   9467  H  HA3  . GLY   B  2  35  ? 53.129  8.231   20.277   1.00 144.61 ? 39   GLY   B HA3  1 
ATOM   9468  N  N    . GLU   B  2  36  ? 52.509  5.943   19.422   1.00 122.93 ? 40   GLU   B N    1 
ATOM   9469  C  CA   . GLU   B  2  36  ? 51.854  4.668   19.130   1.00 122.91 ? 40   GLU   B CA   1 
ATOM   9470  C  C    . GLU   B  2  36  ? 51.544  3.987   20.460   1.00 120.52 ? 40   GLU   B C    1 
ATOM   9471  O  O    . GLU   B  2  36  ? 52.329  3.171   20.953   1.00 120.31 ? 40   GLU   B O    1 
ATOM   9472  C  CB   . GLU   B  2  36  ? 52.730  3.796   18.232   1.00 132.35 ? 40   GLU   B CB   1 
ATOM   9473  C  CG   . GLU   B  2  36  ? 52.913  4.353   16.829   1.00 140.08 ? 40   GLU   B CG   1 
ATOM   9474  C  CD   . GLU   B  2  36  ? 53.809  3.485   15.964   1.00 150.70 ? 40   GLU   B CD   1 
ATOM   9475  O  OE1  . GLU   B  2  36  ? 54.433  2.546   16.501   1.00 155.86 ? 40   GLU   B OE1  1 
ATOM   9476  O  OE2  . GLU   B  2  36  ? 53.890  3.744   14.745   1.00 153.90 ? 40   GLU   B OE2  1 
ATOM   9477  H  H    . GLU   B  2  36  ? 53.194  5.865   19.935   1.00 147.50 ? 40   GLU   B H    1 
ATOM   9478  H  HA   . GLU   B  2  36  ? 51.015  4.836   18.673   1.00 147.47 ? 40   GLU   B HA   1 
ATOM   9479  H  HB2  . GLU   B  2  36  ? 53.608  3.716   18.636   1.00 158.81 ? 40   GLU   B HB2  1 
ATOM   9480  H  HB3  . GLU   B  2  36  ? 52.320  2.921   18.152   1.00 158.81 ? 40   GLU   B HB3  1 
ATOM   9481  H  HG2  . GLU   B  2  36  ? 52.047  4.413   16.397   1.00 168.08 ? 40   GLU   B HG2  1 
ATOM   9482  H  HG3  . GLU   B  2  36  ? 53.316  5.234   16.889   1.00 168.08 ? 40   GLU   B HG3  1 
ATOM   9483  N  N    . ARG   B  2  37  ? 50.391  4.328   21.040   1.00 120.43 ? 41   ARG   B N    1 
ATOM   9484  C  CA   . ARG   B  2  37  ? 49.932  3.656   22.247   1.00 122.49 ? 41   ARG   B CA   1 
ATOM   9485  C  C    . ARG   B  2  37  ? 49.440  2.246   21.958   1.00 126.83 ? 41   ARG   B C    1 
ATOM   9486  O  O    . ARG   B  2  37  ? 49.410  1.412   22.869   1.00 135.34 ? 41   ARG   B O    1 
ATOM   9487  C  CB   . ARG   B  2  37  ? 48.808  4.457   22.902   1.00 114.29 ? 41   ARG   B CB   1 
ATOM   9488  C  CG   . ARG   B  2  37  ? 49.142  5.911   23.180   1.00 110.17 ? 41   ARG   B CG   1 
ATOM   9489  C  CD   . ARG   B  2  37  ? 47.870  6.735   23.314   1.00 105.17 ? 41   ARG   B CD   1 
ATOM   9490  N  NE   . ARG   B  2  37  ? 47.930  7.669   24.434   1.00 105.74 ? 41   ARG   B NE   1 
ATOM   9491  C  CZ   . ARG   B  2  37  ? 48.530  8.854   24.394   1.00 108.14 ? 41   ARG   B CZ   1 
ATOM   9492  N  NH1  . ARG   B  2  37  ? 49.136  9.265   23.287   1.00 108.81 ? 41   ARG   B NH1  1 
ATOM   9493  N  NH2  . ARG   B  2  37  ? 48.527  9.630   25.469   1.00 111.00 ? 41   ARG   B NH2  1 
ATOM   9494  H  H    . ARG   B  2  37  ? 49.862  4.943   20.753   1.00 144.49 ? 41   ARG   B H    1 
ATOM   9495  H  HA   . ARG   B  2  37  ? 50.671  3.604   22.873   1.00 146.97 ? 41   ARG   B HA   1 
ATOM   9496  H  HB2  . ARG   B  2  37  ? 48.037  4.442   22.314   1.00 137.13 ? 41   ARG   B HB2  1 
ATOM   9497  H  HB3  . ARG   B  2  37  ? 48.587  4.041   23.750   1.00 137.13 ? 41   ARG   B HB3  1 
ATOM   9498  H  HG2  . ARG   B  2  37  ? 49.641  5.977   24.009   1.00 132.18 ? 41   ARG   B HG2  1 
ATOM   9499  H  HG3  . ARG   B  2  37  ? 49.666  6.270   22.448   1.00 132.18 ? 41   ARG   B HG3  1 
ATOM   9500  H  HD2  . ARG   B  2  37  ? 47.735  7.246   22.501   1.00 126.18 ? 41   ARG   B HD2  1 
ATOM   9501  H  HD3  . ARG   B  2  37  ? 47.118  6.138   23.459   1.00 126.18 ? 41   ARG   B HD3  1 
ATOM   9502  H  HE   . ARG   B  2  37  ? 47.552  7.436   25.170   1.00 126.87 ? 41   ARG   B HE   1 
ATOM   9503  H  HH11 . ARG   B  2  37  ? 49.143  8.763   22.589   1.00 130.55 ? 41   ARG   B HH11 1 
ATOM   9504  H  HH12 . ARG   B  2  37  ? 49.522  10.033  23.268   1.00 130.55 ? 41   ARG   B HH12 1 
ATOM   9505  H  HH21 . ARG   B  2  37  ? 48.138  9.365   26.189   1.00 133.18 ? 41   ARG   B HH21 1 
ATOM   9506  H  HH22 . ARG   B  2  37  ? 48.915  10.397  25.446   1.00 133.18 ? 41   ARG   B HH22 1 
ATOM   9507  N  N    . CYS   B  2  38  ? 49.046  1.969   20.717   1.00 120.12 ? 42   CYS   B N    1 
ATOM   9508  C  CA   . CYS   B  2  38  ? 48.554  0.651   20.343   1.00 115.81 ? 42   CYS   B CA   1 
ATOM   9509  C  C    . CYS   B  2  38  ? 49.656  -0.390  20.478   1.00 118.52 ? 42   CYS   B C    1 
ATOM   9510  O  O    . CYS   B  2  38  ? 50.623  -0.381  19.710   1.00 121.63 ? 42   CYS   B O    1 
ATOM   9511  C  CB   . CYS   B  2  38  ? 48.023  0.670   18.910   1.00 112.87 ? 42   CYS   B CB   1 
ATOM   9512  S  SG   . CYS   B  2  38  ? 46.892  -0.677  18.525   1.00 109.92 ? 42   CYS   B SG   1 
ATOM   9513  H  H    . CYS   B  2  38  ? 49.054  2.534   20.069   1.00 144.12 ? 42   CYS   B H    1 
ATOM   9514  H  HA   . CYS   B  2  38  ? 47.826  0.403   20.934   1.00 138.95 ? 42   CYS   B HA   1 
ATOM   9515  H  HB2  . CYS   B  2  38  ? 47.547  1.503   18.766   1.00 135.43 ? 42   CYS   B HB2  1 
ATOM   9516  H  HB3  . CYS   B  2  38  ? 48.774  0.607   18.299   1.00 135.43 ? 42   CYS   B HB3  1 
ATOM   9517  N  N    . ASP   B  2  39  ? 49.522  -1.289  21.445   1.00 117.83 ? 43   ASP   B N    1 
ATOM   9518  C  CA   . ASP   B  2  39  ? 50.512  -2.338  21.661   1.00 123.40 ? 43   ASP   B CA   1 
ATOM   9519  C  C    . ASP   B  2  39  ? 49.931  -3.336  22.655   1.00 122.55 ? 43   ASP   B C    1 
ATOM   9520  O  O    . ASP   B  2  39  ? 48.790  -3.203  23.107   1.00 119.69 ? 43   ASP   B O    1 
ATOM   9521  C  CB   . ASP   B  2  39  ? 51.838  -1.756  22.155   1.00 127.25 ? 43   ASP   B CB   1 
ATOM   9522  C  CG   . ASP   B  2  39  ? 53.039  -2.444  21.542   1.00 132.14 ? 43   ASP   B CG   1 
ATOM   9523  O  OD1  . ASP   B  2  39  ? 53.046  -3.691  21.486   1.00 134.60 ? 43   ASP   B OD1  1 
ATOM   9524  O  OD2  . ASP   B  2  39  ? 53.972  -1.736  21.107   1.00 134.19 ? 43   ASP   B OD2  1 
ATOM   9525  H  H    . ASP   B  2  39  ? 48.861  -1.312  21.995   1.00 141.38 ? 43   ASP   B H    1 
ATOM   9526  H  HA   . ASP   B  2  39  ? 50.672  -2.802  20.825   1.00 148.07 ? 43   ASP   B HA   1 
ATOM   9527  H  HB2  . ASP   B  2  39  ? 51.878  -0.815  21.921   1.00 152.68 ? 43   ASP   B HB2  1 
ATOM   9528  H  HB3  . ASP   B  2  39  ? 51.891  -1.860  23.118   1.00 152.68 ? 43   ASP   B HB3  1 
ATOM   9529  N  N    . THR   B  2  40  ? 50.730  -4.342  22.988   1.00 124.84 ? 44   THR   B N    1 
ATOM   9530  C  CA   . THR   B  2  40  ? 50.286  -5.362  23.925   1.00 124.23 ? 44   THR   B CA   1 
ATOM   9531  C  C    . THR   B  2  40  ? 50.030  -4.733  25.293   1.00 126.61 ? 44   THR   B C    1 
ATOM   9532  O  O    . THR   B  2  40  ? 50.796  -3.864  25.728   1.00 130.93 ? 44   THR   B O    1 
ATOM   9533  C  CB   . THR   B  2  40  ? 51.334  -6.470  24.038   1.00 129.10 ? 44   THR   B CB   1 
ATOM   9534  O  OG1  . THR   B  2  40  ? 51.709  -6.909  22.725   1.00 126.56 ? 44   THR   B OG1  1 
ATOM   9535  C  CG2  . THR   B  2  40  ? 50.787  -7.651  24.823   1.00 133.12 ? 44   THR   B CG2  1 
ATOM   9536  H  H    . THR   B  2  40  ? 51.528  -4.456  22.689   1.00 149.79 ? 44   THR   B H    1 
ATOM   9537  H  HA   . THR   B  2  40  ? 49.457  -5.759  23.611   1.00 149.06 ? 44   THR   B HA   1 
ATOM   9538  H  HB   . THR   B  2  40  ? 52.114  -6.130  24.503   1.00 154.90 ? 44   THR   B HB   1 
ATOM   9539  H  HG1  . THR   B  2  40  ? 51.762  -7.747  22.707   1.00 151.85 ? 44   THR   B HG1  1 
ATOM   9540  H  HG21 . THR   B  2  40  ? 51.443  -8.365  24.848   1.00 159.73 ? 44   THR   B HG21 1 
ATOM   9541  H  HG22 . THR   B  2  40  ? 50.583  -7.379  25.731   1.00 159.73 ? 44   THR   B HG22 1 
ATOM   9542  H  HG23 . THR   B  2  40  ? 49.977  -7.981  24.403   1.00 159.73 ? 44   THR   B HG23 1 
ATOM   9543  N  N    . PRO   B  2  41  ? 48.962  -5.133  25.994   1.00 125.27 ? 45   PRO   B N    1 
ATOM   9544  C  CA   . PRO   B  2  41  ? 48.691  -4.526  27.309   1.00 127.15 ? 45   PRO   B CA   1 
ATOM   9545  C  C    . PRO   B  2  41  ? 49.884  -4.536  28.253   1.00 137.46 ? 45   PRO   B C    1 
ATOM   9546  O  O    . PRO   B  2  41  ? 50.100  -3.554  28.973   1.00 141.95 ? 45   PRO   B O    1 
ATOM   9547  C  CB   . PRO   B  2  41  ? 47.529  -5.371  27.862   1.00 123.19 ? 45   PRO   B CB   1 
ATOM   9548  C  CG   . PRO   B  2  41  ? 47.153  -6.354  26.786   1.00 120.56 ? 45   PRO   B CG   1 
ATOM   9549  C  CD   . PRO   B  2  41  ? 47.833  -5.952  25.524   1.00 120.01 ? 45   PRO   B CD   1 
ATOM   9550  H  HA   . PRO   B  2  41  ? 48.392  -3.612  27.179   1.00 152.57 ? 45   PRO   B HA   1 
ATOM   9551  H  HB2  . PRO   B  2  41  ? 47.821  -5.836  28.661   1.00 147.80 ? 45   PRO   B HB2  1 
ATOM   9552  H  HB3  . PRO   B  2  41  ? 46.780  -4.792  28.070   1.00 147.80 ? 45   PRO   B HB3  1 
ATOM   9553  H  HG2  . PRO   B  2  41  ? 47.441  -7.241  27.053   1.00 144.65 ? 45   PRO   B HG2  1 
ATOM   9554  H  HG3  . PRO   B  2  41  ? 46.191  -6.340  26.666   1.00 144.65 ? 45   PRO   B HG3  1 
ATOM   9555  H  HD2  . PRO   B  2  41  ? 48.149  -6.731  25.039   1.00 143.99 ? 45   PRO   B HD2  1 
ATOM   9556  H  HD3  . PRO   B  2  41  ? 47.238  -5.431  24.962   1.00 143.99 ? 45   PRO   B HD3  1 
ATOM   9557  N  N    . ALA   B  2  42  ? 50.665  -5.619  28.275   1.00 139.29 ? 46   ALA   B N    1 
ATOM   9558  C  CA   . ALA   B  2  42  ? 51.820  -5.669  29.166   1.00 141.47 ? 46   ALA   B CA   1 
ATOM   9559  C  C    . ALA   B  2  42  ? 52.814  -4.562  28.837   1.00 142.71 ? 46   ALA   B C    1 
ATOM   9560  O  O    . ALA   B  2  42  ? 53.397  -3.951  29.741   1.00 147.57 ? 46   ALA   B O    1 
ATOM   9561  C  CB   . ALA   B  2  42  ? 52.495  -7.038  29.080   1.00 142.74 ? 46   ALA   B CB   1 
ATOM   9562  H  H    . ALA   B  2  42  ? 50.549  -6.323  27.794   1.00 167.13 ? 46   ALA   B H    1 
ATOM   9563  H  HA   . ALA   B  2  42  ? 51.516  -5.542  30.079   1.00 169.75 ? 46   ALA   B HA   1 
ATOM   9564  H  HB1  . ALA   B  2  42  ? 53.261  -7.050  29.674   1.00 171.27 ? 46   ALA   B HB1  1 
ATOM   9565  H  HB2  . ALA   B  2  42  ? 51.859  -7.721  29.345   1.00 171.27 ? 46   ALA   B HB2  1 
ATOM   9566  H  HB3  . ALA   B  2  42  ? 52.783  -7.191  28.166   1.00 171.27 ? 46   ALA   B HB3  1 
ATOM   9567  N  N    . ASN   B  2  43  ? 53.018  -4.289  27.547   1.00 137.79 ? 47   ASN   B N    1 
ATOM   9568  C  CA   . ASN   B  2  43  ? 53.942  -3.230  27.153   1.00 136.33 ? 47   ASN   B CA   1 
ATOM   9569  C  C    . ASN   B  2  43  ? 53.458  -1.871  27.642   1.00 133.04 ? 47   ASN   B C    1 
ATOM   9570  O  O    . ASN   B  2  43  ? 54.260  -1.041  28.088   1.00 133.72 ? 47   ASN   B O    1 
ATOM   9571  C  CB   . ASN   B  2  43  ? 54.110  -3.223  25.634   1.00 130.78 ? 47   ASN   B CB   1 
ATOM   9572  C  CG   . ASN   B  2  43  ? 54.490  -4.584  25.084   1.00 134.96 ? 47   ASN   B CG   1 
ATOM   9573  O  OD1  . ASN   B  2  43  ? 54.331  -5.603  25.756   1.00 139.32 ? 47   ASN   B OD1  1 
ATOM   9574  N  ND2  . ASN   B  2  43  ? 54.992  -4.608  23.855   1.00 135.20 ? 47   ASN   B ND2  1 
ATOM   9575  H  H    . ASN   B  2  43  ? 52.640  -4.696  26.891   1.00 165.33 ? 47   ASN   B H    1 
ATOM   9576  H  HA   . ASN   B  2  43  ? 54.809  -3.404  27.553   1.00 163.58 ? 47   ASN   B HA   1 
ATOM   9577  H  HB2  . ASN   B  2  43  ? 53.273  -2.956  25.223   1.00 156.91 ? 47   ASN   B HB2  1 
ATOM   9578  H  HB3  . ASN   B  2  43  ? 54.811  -2.597  25.396   1.00 156.91 ? 47   ASN   B HB3  1 
ATOM   9579  H  HD21 . ASN   B  2  43  ? 55.223  -5.357  23.499   1.00 162.22 ? 47   ASN   B HD21 1 
ATOM   9580  H  HD22 . ASN   B  2  43  ? 55.087  -3.876  23.415   1.00 162.22 ? 47   ASN   B HD22 1 
ATOM   9581  N  N    . LEU   B  2  44  ? 52.149  -1.624  27.569   1.00 131.64 ? 48   LEU   B N    1 
ATOM   9582  C  CA   . LEU   B  2  44  ? 51.616  -0.346  28.026   1.00 133.28 ? 48   LEU   B CA   1 
ATOM   9583  C  C    . LEU   B  2  44  ? 51.816  -0.177  29.527   1.00 141.33 ? 48   LEU   B C    1 
ATOM   9584  O  O    . LEU   B  2  44  ? 52.192  0.905   29.994   1.00 143.72 ? 48   LEU   B O    1 
ATOM   9585  C  CB   . LEU   B  2  44  ? 50.137  -0.234  27.661   1.00 126.62 ? 48   LEU   B CB   1 
ATOM   9586  C  CG   . LEU   B  2  44  ? 49.770  -0.558  26.210   1.00 122.07 ? 48   LEU   B CG   1 
ATOM   9587  C  CD1  . LEU   B  2  44  ? 48.388  -0.009  25.878   1.00 117.32 ? 48   LEU   B CD1  1 
ATOM   9588  C  CD2  . LEU   B  2  44  ? 50.808  -0.026  25.230   1.00 121.17 ? 48   LEU   B CD2  1 
ATOM   9589  H  H    . LEU   B  2  44  ? 51.560  -2.172  27.263   1.00 157.95 ? 48   LEU   B H    1 
ATOM   9590  H  HA   . LEU   B  2  44  ? 52.088  0.373   27.577   1.00 159.91 ? 48   LEU   B HA   1 
ATOM   9591  H  HB2  . LEU   B  2  44  ? 49.640  -0.847  28.225   1.00 151.92 ? 48   LEU   B HB2  1 
ATOM   9592  H  HB3  . LEU   B  2  44  ? 49.852  0.677   27.832   1.00 151.92 ? 48   LEU   B HB3  1 
ATOM   9593  H  HG   . LEU   B  2  44  ? 49.753  -1.523  26.109   1.00 146.46 ? 48   LEU   B HG   1 
ATOM   9594  H  HD11 . LEU   B  2  44  ? 48.143  -0.292  24.983   1.00 140.77 ? 48   LEU   B HD11 1 
ATOM   9595  H  HD12 . LEU   B  2  44  ? 47.749  -0.355  26.521   1.00 140.77 ? 48   LEU   B HD12 1 
ATOM   9596  H  HD13 . LEU   B  2  44  ? 48.414  0.959   25.924   1.00 140.77 ? 48   LEU   B HD13 1 
ATOM   9597  H  HD21 . LEU   B  2  44  ? 50.478  -0.143  24.325   1.00 145.39 ? 48   LEU   B HD21 1 
ATOM   9598  H  HD22 . LEU   B  2  44  ? 50.957  0.916   25.408   1.00 145.39 ? 48   LEU   B HD22 1 
ATOM   9599  H  HD23 . LEU   B  2  44  ? 51.635  -0.520  25.346   1.00 145.39 ? 48   LEU   B HD23 1 
ATOM   9600  N  N    . LEU   B  2  45  ? 51.568  -1.237  30.301   1.00 142.72 ? 49   LEU   B N    1 
ATOM   9601  C  CA   . LEU   B  2  45  ? 51.877  -1.190  31.726   1.00 142.57 ? 49   LEU   B CA   1 
ATOM   9602  C  C    . LEU   B  2  45  ? 53.370  -0.993  31.952   1.00 145.55 ? 49   LEU   B C    1 
ATOM   9603  O  O    . LEU   B  2  45  ? 53.779  -0.277  32.874   1.00 145.81 ? 49   LEU   B O    1 
ATOM   9604  C  CB   . LEU   B  2  45  ? 51.402  -2.472  32.411   1.00 142.93 ? 49   LEU   B CB   1 
ATOM   9605  C  CG   . LEU   B  2  45  ? 50.020  -2.444  33.067   1.00 134.83 ? 49   LEU   B CG   1 
ATOM   9606  C  CD1  . LEU   B  2  45  ? 49.596  -3.851  33.461   1.00 135.58 ? 49   LEU   B CD1  1 
ATOM   9607  C  CD2  . LEU   B  2  45  ? 50.018  -1.532  34.285   1.00 136.05 ? 49   LEU   B CD2  1 
ATOM   9608  H  H    . LEU   B  2  45  ? 51.229  -1.979  30.030   1.00 171.24 ? 49   LEU   B H    1 
ATOM   9609  H  HA   . LEU   B  2  45  ? 51.404  -0.444  32.126   1.00 171.07 ? 49   LEU   B HA   1 
ATOM   9610  H  HB2  . LEU   B  2  45  ? 51.384  -3.176  31.745   1.00 171.49 ? 49   LEU   B HB2  1 
ATOM   9611  H  HB3  . LEU   B  2  45  ? 52.040  -2.691  33.108   1.00 171.49 ? 49   LEU   B HB3  1 
ATOM   9612  H  HG   . LEU   B  2  45  ? 49.377  -2.094  32.430   1.00 161.77 ? 49   LEU   B HG   1 
ATOM   9613  H  HD11 . LEU   B  2  45  ? 48.662  -3.839  33.721   1.00 162.67 ? 49   LEU   B HD11 1 
ATOM   9614  H  HD12 . LEU   B  2  45  ? 49.721  -4.442  32.702   1.00 162.67 ? 49   LEU   B HD12 1 
ATOM   9615  H  HD13 . LEU   B  2  45  ? 50.143  -4.149  34.205   1.00 162.67 ? 49   LEU   B HD13 1 
ATOM   9616  H  HD21 . LEU   B  2  45  ? 49.111  -1.456  34.621   1.00 163.24 ? 49   LEU   B HD21 1 
ATOM   9617  H  HD22 . LEU   B  2  45  ? 50.593  -1.913  34.966   1.00 163.24 ? 49   LEU   B HD22 1 
ATOM   9618  H  HD23 . LEU   B  2  45  ? 50.348  -0.657  34.025   1.00 163.24 ? 49   LEU   B HD23 1 
ATOM   9619  N  N    . ALA   B  2  46  ? 54.200  -1.622  31.118   1.00 148.16 ? 50   ALA   B N    1 
ATOM   9620  C  CA   . ALA   B  2  46  ? 55.642  -1.459  31.251   1.00 157.48 ? 50   ALA   B CA   1 
ATOM   9621  C  C    . ALA   B  2  46  ? 56.072  -0.024  30.977   1.00 160.45 ? 50   ALA   B C    1 
ATOM   9622  O  O    . ALA   B  2  46  ? 57.054  0.449   31.560   1.00 163.38 ? 50   ALA   B O    1 
ATOM   9623  C  CB   . ALA   B  2  46  ? 56.367  -2.415  30.303   1.00 159.09 ? 50   ALA   B CB   1 
ATOM   9624  H  H    . ALA   B  2  46  ? 53.956  -2.141  30.477   1.00 177.77 ? 50   ALA   B H    1 
ATOM   9625  H  HA   . ALA   B  2  46  ? 55.898  -1.681  32.159   1.00 188.95 ? 50   ALA   B HA   1 
ATOM   9626  H  HB1  . ALA   B  2  46  ? 57.324  -2.303  30.413   1.00 190.89 ? 50   ALA   B HB1  1 
ATOM   9627  H  HB2  . ALA   B  2  46  ? 56.113  -3.326  30.519   1.00 190.89 ? 50   ALA   B HB2  1 
ATOM   9628  H  HB3  . ALA   B  2  46  ? 56.113  -2.208  29.390   1.00 190.89 ? 50   ALA   B HB3  1 
ATOM   9629  N  N    . LYS   B  2  47  ? 55.353  0.685   30.104   1.00 128.42 ? 51   LYS   B N    1 
ATOM   9630  C  CA   . LYS   B  2  47  ? 55.728  2.033   29.703   1.00 134.87 ? 51   LYS   B CA   1 
ATOM   9631  C  C    . LYS   B  2  47  ? 54.889  3.110   30.384   1.00 142.13 ? 51   LYS   B C    1 
ATOM   9632  O  O    . LYS   B  2  47  ? 54.773  4.220   29.853   1.00 146.10 ? 51   LYS   B O    1 
ATOM   9633  C  CB   . LYS   B  2  47  ? 55.631  2.185   28.183   1.00 129.74 ? 51   LYS   B CB   1 
ATOM   9634  C  CG   . LYS   B  2  47  ? 56.556  1.273   27.379   1.00 125.69 ? 51   LYS   B CG   1 
ATOM   9635  C  CD   . LYS   B  2  47  ? 57.981  1.220   27.929   1.00 128.77 ? 51   LYS   B CD   1 
ATOM   9636  C  CE   . LYS   B  2  47  ? 58.602  2.603   28.113   1.00 135.63 ? 51   LYS   B CE   1 
ATOM   9637  N  NZ   . LYS   B  2  47  ? 58.607  3.416   26.868   1.00 139.04 ? 51   LYS   B NZ   1 
ATOM   9638  H  H    . LYS   B  2  47  ? 54.635  0.398   29.728   1.00 154.08 ? 51   LYS   B H    1 
ATOM   9639  H  HA   . LYS   B  2  47  ? 56.653  2.170   29.963   1.00 161.82 ? 51   LYS   B HA   1 
ATOM   9640  H  HB2  . LYS   B  2  47  ? 54.721  1.986   27.913   1.00 155.67 ? 51   LYS   B HB2  1 
ATOM   9641  H  HB3  . LYS   B  2  47  ? 55.854  3.100   27.952   1.00 155.67 ? 51   LYS   B HB3  1 
ATOM   9642  H  HG2  . LYS   B  2  47  ? 56.198  0.371   27.393   1.00 150.80 ? 51   LYS   B HG2  1 
ATOM   9643  H  HG3  . LYS   B  2  47  ? 56.602  1.597   26.466   1.00 150.80 ? 51   LYS   B HG3  1 
ATOM   9644  H  HD2  . LYS   B  2  47  ? 57.969  0.781   28.794   1.00 154.51 ? 51   LYS   B HD2  1 
ATOM   9645  H  HD3  . LYS   B  2  47  ? 58.539  0.722   27.312   1.00 154.51 ? 51   LYS   B HD3  1 
ATOM   9646  H  HE2  . LYS   B  2  47  ? 58.096  3.088   28.783   1.00 162.74 ? 51   LYS   B HE2  1 
ATOM   9647  H  HE3  . LYS   B  2  47  ? 59.522  2.497   28.403   1.00 162.74 ? 51   LYS   B HE3  1 
ATOM   9648  H  HZ1  . LYS   B  2  47  ? 59.258  4.022   26.904   1.00 166.83 ? 51   LYS   B HZ1  1 
ATOM   9649  H  HZ2  . LYS   B  2  47  ? 58.739  2.891   26.162   1.00 166.83 ? 51   LYS   B HZ2  1 
ATOM   9650  H  HZ3  . LYS   B  2  47  ? 57.828  3.835   26.775   1.00 166.83 ? 51   LYS   B HZ3  1 
ATOM   9651  N  N    . GLY   B  2  48  ? 54.299  2.811   31.544   1.00 142.85 ? 52   GLY   B N    1 
ATOM   9652  C  CA   . GLY   B  2  48  ? 53.669  3.805   32.388   1.00 143.28 ? 52   GLY   B CA   1 
ATOM   9653  C  C    . GLY   B  2  48  ? 52.159  3.697   32.474   1.00 138.78 ? 52   GLY   B C    1 
ATOM   9654  O  O    . GLY   B  2  48  ? 51.585  4.018   33.522   1.00 138.65 ? 52   GLY   B O    1 
ATOM   9655  H  H    . GLY   B  2  48  ? 54.254  2.014   31.864   1.00 171.40 ? 52   GLY   B H    1 
ATOM   9656  H  HA2  . GLY   B  2  48  ? 54.024  3.720   33.287   1.00 171.92 ? 52   GLY   B HA2  1 
ATOM   9657  H  HA3  . GLY   B  2  48  ? 53.885  4.687   32.046   1.00 171.92 ? 52   GLY   B HA3  1 
ATOM   9658  N  N    . CYS   B  2  49  ? 51.502  3.258   31.400   1.00 135.41 ? 53   CYS   B N    1 
ATOM   9659  C  CA   . CYS   B  2  49  ? 50.044  3.256   31.369   1.00 136.46 ? 53   CYS   B CA   1 
ATOM   9660  C  C    . CYS   B  2  49  ? 49.492  2.459   32.543   1.00 134.99 ? 53   CYS   B C    1 
ATOM   9661  O  O    . CYS   B  2  49  ? 49.633  1.233   32.595   1.00 134.57 ? 53   CYS   B O    1 
ATOM   9662  C  CB   . CYS   B  2  49  ? 49.541  2.688   30.043   1.00 135.58 ? 53   CYS   B CB   1 
ATOM   9663  S  SG   . CYS   B  2  49  ? 50.294  3.492   28.610   1.00 139.13 ? 53   CYS   B SG   1 
ATOM   9664  H  H    . CYS   B  2  49  ? 51.876  2.959   30.686   1.00 162.48 ? 53   CYS   B H    1 
ATOM   9665  H  HA   . CYS   B  2  49  ? 49.717  4.167   31.443   1.00 163.73 ? 53   CYS   B HA   1 
ATOM   9666  H  HB2  . CYS   B  2  49  ? 49.754  1.742   30.003   1.00 162.68 ? 53   CYS   B HB2  1 
ATOM   9667  H  HB3  . CYS   B  2  49  ? 48.580  2.814   29.989   1.00 162.68 ? 53   CYS   B HB3  1 
ATOM   9668  N  N    . GLN   B  2  50  ? 48.858  3.151   33.484   1.00 133.06 ? 54   GLN   B N    1 
ATOM   9669  C  CA   . GLN   B  2  50  ? 48.381  2.516   34.700   1.00 128.77 ? 54   GLN   B CA   1 
ATOM   9670  C  C    . GLN   B  2  50  ? 47.179  1.622   34.399   1.00 126.01 ? 54   GLN   B C    1 
ATOM   9671  O  O    . GLN   B  2  50  ? 46.604  1.645   33.306   1.00 120.85 ? 54   GLN   B O    1 
ATOM   9672  C  CB   . GLN   B  2  50  ? 48.023  3.575   35.743   1.00 128.23 ? 54   GLN   B CB   1 
ATOM   9673  C  CG   . GLN   B  2  50  ? 49.174  4.518   36.075   1.00 129.15 ? 54   GLN   B CG   1 
ATOM   9674  C  CD   . GLN   B  2  50  ? 48.765  5.648   36.999   1.00 130.73 ? 54   GLN   B CD   1 
ATOM   9675  O  OE1  . GLN   B  2  50  ? 47.672  5.640   37.564   1.00 133.18 ? 54   GLN   B OE1  1 
ATOM   9676  N  NE2  . GLN   B  2  50  ? 49.645  6.632   37.156   1.00 128.99 ? 54   GLN   B NE2  1 
ATOM   9677  H  H    . GLN   B  2  50  ? 48.691  3.994   33.440   1.00 159.66 ? 54   GLN   B H    1 
ATOM   9678  H  HA   . GLN   B  2  50  ? 49.081  1.956   35.070   1.00 154.51 ? 54   GLN   B HA   1 
ATOM   9679  H  HB2  . GLN   B  2  50  ? 47.288  4.110   35.405   1.00 153.86 ? 54   GLN   B HB2  1 
ATOM   9680  H  HB3  . GLN   B  2  50  ? 47.758  3.129   36.563   1.00 153.86 ? 54   GLN   B HB3  1 
ATOM   9681  H  HG2  . GLN   B  2  50  ? 49.879  4.014   36.511   1.00 154.96 ? 54   GLN   B HG2  1 
ATOM   9682  H  HG3  . GLN   B  2  50  ? 49.507  4.910   35.252   1.00 154.96 ? 54   GLN   B HG3  1 
ATOM   9683  H  HE21 . GLN   B  2  50  ? 50.399  6.604   36.743   1.00 154.77 ? 54   GLN   B HE21 1 
ATOM   9684  H  HE22 . GLN   B  2  50  ? 49.461  7.296   37.670   1.00 154.77 ? 54   GLN   B HE22 1 
ATOM   9685  N  N    . LEU   B  2  51  ? 46.802  0.820   35.396   1.00 128.49 ? 55   LEU   B N    1 
ATOM   9686  C  CA   . LEU   B  2  51  ? 45.700  -0.120  35.219   1.00 127.14 ? 55   LEU   B CA   1 
ATOM   9687  C  C    . LEU   B  2  51  ? 44.381  0.610   35.001   1.00 121.96 ? 55   LEU   B C    1 
ATOM   9688  O  O    . LEU   B  2  51  ? 43.611  0.267   34.096   1.00 114.28 ? 55   LEU   B O    1 
ATOM   9689  C  CB   . LEU   B  2  51  ? 45.603  -1.043  36.433   1.00 129.70 ? 55   LEU   B CB   1 
ATOM   9690  C  CG   . LEU   B  2  51  ? 46.752  -2.032  36.623   1.00 128.88 ? 55   LEU   B CG   1 
ATOM   9691  C  CD1  . LEU   B  2  51  ? 46.664  -2.696  37.988   1.00 130.52 ? 55   LEU   B CD1  1 
ATOM   9692  C  CD2  . LEU   B  2  51  ? 46.745  -3.076  35.518   1.00 123.83 ? 55   LEU   B CD2  1 
ATOM   9693  H  H    . LEU   B  2  51  ? 47.165  0.801   36.175   1.00 154.17 ? 55   LEU   B H    1 
ATOM   9694  H  HA   . LEU   B  2  51  ? 45.878  -0.662  34.434   1.00 152.55 ? 55   LEU   B HA   1 
ATOM   9695  H  HB2  . LEU   B  2  51  ? 45.565  -0.491  37.229   1.00 155.62 ? 55   LEU   B HB2  1 
ATOM   9696  H  HB3  . LEU   B  2  51  ? 44.788  -1.564  36.351   1.00 155.62 ? 55   LEU   B HB3  1 
ATOM   9697  H  HG   . LEU   B  2  51  ? 47.594  -1.552  36.577   1.00 154.63 ? 55   LEU   B HG   1 
ATOM   9698  H  HD11 . LEU   B  2  51  ? 47.396  -3.325  38.082   1.00 156.60 ? 55   LEU   B HD11 1 
ATOM   9699  H  HD12 . LEU   B  2  51  ? 46.723  -2.014  38.676   1.00 156.60 ? 55   LEU   B HD12 1 
ATOM   9700  H  HD13 . LEU   B  2  51  ? 45.816  -3.163  38.058   1.00 156.60 ? 55   LEU   B HD13 1 
ATOM   9701  H  HD21 . LEU   B  2  51  ? 47.441  -3.728  35.695   1.00 148.58 ? 55   LEU   B HD21 1 
ATOM   9702  H  HD22 . LEU   B  2  51  ? 45.879  -3.512  35.502   1.00 148.58 ? 55   LEU   B HD22 1 
ATOM   9703  H  HD23 . LEU   B  2  51  ? 46.910  -2.638  34.669   1.00 148.58 ? 55   LEU   B HD23 1 
ATOM   9704  N  N    . ASN   B  2  52  ? 44.097  1.617   35.827   1.00 125.31 ? 56   ASN   B N    1 
ATOM   9705  C  CA   . ASN   B  2  52  ? 42.823  2.318   35.741   1.00 126.42 ? 56   ASN   B CA   1 
ATOM   9706  C  C    . ASN   B  2  52  ? 42.659  3.088   34.437   1.00 124.29 ? 56   ASN   B C    1 
ATOM   9707  O  O    . ASN   B  2  52  ? 41.535  3.488   34.115   1.00 124.68 ? 56   ASN   B O    1 
ATOM   9708  C  CB   . ASN   B  2  52  ? 42.674  3.274   36.927   1.00 132.50 ? 56   ASN   B CB   1 
ATOM   9709  C  CG   . ASN   B  2  52  ? 43.061  2.631   38.244   1.00 136.17 ? 56   ASN   B CG   1 
ATOM   9710  O  OD1  . ASN   B  2  52  ? 44.103  1.984   38.347   1.00 135.91 ? 56   ASN   B OD1  1 
ATOM   9711  N  ND2  . ASN   B  2  52  ? 42.218  2.795   39.257   1.00 139.11 ? 56   ASN   B ND2  1 
ATOM   9712  H  H    . ASN   B  2  52  ? 44.624  1.910   36.441   1.00 150.36 ? 56   ASN   B H    1 
ATOM   9713  H  HA   . ASN   B  2  52  ? 42.107  1.666   35.790   1.00 151.68 ? 56   ASN   B HA   1 
ATOM   9714  H  HB2  . ASN   B  2  52  ? 43.248  4.044   36.788   1.00 158.99 ? 56   ASN   B HB2  1 
ATOM   9715  H  HB3  . ASN   B  2  52  ? 41.749  3.558   36.991   1.00 158.99 ? 56   ASN   B HB3  1 
ATOM   9716  H  HD21 . ASN   B  2  52  ? 42.394  2.449   40.024   1.00 166.91 ? 56   ASN   B HD21 1 
ATOM   9717  H  HD22 . ASN   B  2  52  ? 41.495  3.248   39.146   1.00 166.91 ? 56   ASN   B HD22 1 
ATOM   9718  N  N    . PHE   B  2  53  ? 43.740  3.296   33.681   1.00 121.84 ? 57   PHE   B N    1 
ATOM   9719  C  CA   . PHE   B  2  53  ? 43.690  4.064   32.445   1.00 120.18 ? 57   PHE   B CA   1 
ATOM   9720  C  C    . PHE   B  2  53  ? 43.811  3.218   31.185   1.00 119.28 ? 57   PHE   B C    1 
ATOM   9721  O  O    . PHE   B  2  53  ? 43.342  3.650   30.128   1.00 117.47 ? 57   PHE   B O    1 
ATOM   9722  C  CB   . PHE   B  2  53  ? 44.805  5.120   32.434   1.00 118.68 ? 57   PHE   B CB   1 
ATOM   9723  C  CG   . PHE   B  2  53  ? 44.588  6.237   33.413   1.00 120.56 ? 57   PHE   B CG   1 
ATOM   9724  C  CD1  . PHE   B  2  53  ? 44.892  6.071   34.753   1.00 122.46 ? 57   PHE   B CD1  1 
ATOM   9725  C  CD2  . PHE   B  2  53  ? 44.081  7.455   32.993   1.00 122.27 ? 57   PHE   B CD2  1 
ATOM   9726  C  CE1  . PHE   B  2  53  ? 44.693  7.097   35.655   1.00 126.79 ? 57   PHE   B CE1  1 
ATOM   9727  C  CE2  . PHE   B  2  53  ? 43.880  8.484   33.890   1.00 127.45 ? 57   PHE   B CE2  1 
ATOM   9728  C  CZ   . PHE   B  2  53  ? 44.186  8.306   35.222   1.00 129.96 ? 57   PHE   B CZ   1 
ATOM   9729  H  H    . PHE   B  2  53  ? 44.524  2.997   33.870   1.00 146.19 ? 57   PHE   B H    1 
ATOM   9730  H  HA   . PHE   B  2  53  ? 42.837  4.524   32.404   1.00 144.20 ? 57   PHE   B HA   1 
ATOM   9731  H  HB2  . PHE   B  2  53  ? 45.645  4.690   32.657   1.00 142.40 ? 57   PHE   B HB2  1 
ATOM   9732  H  HB3  . PHE   B  2  53  ? 44.857  5.510   31.547   1.00 142.40 ? 57   PHE   B HB3  1 
ATOM   9733  H  HD1  . PHE   B  2  53  ? 45.235  5.258   35.049   1.00 146.93 ? 57   PHE   B HD1  1 
ATOM   9734  H  HD2  . PHE   B  2  53  ? 43.873  7.581   32.095   1.00 146.71 ? 57   PHE   B HD2  1 
ATOM   9735  H  HE1  . PHE   B  2  53  ? 44.899  6.974   36.553   1.00 152.13 ? 57   PHE   B HE1  1 
ATOM   9736  H  HE2  . PHE   B  2  53  ? 43.538  9.298   33.596   1.00 152.92 ? 57   PHE   B HE2  1 
ATOM   9737  H  HZ   . PHE   B  2  53  ? 44.051  8.998   35.828   1.00 155.94 ? 57   PHE   B HZ   1 
ATOM   9738  N  N    . ILE   B  2  54  ? 44.426  2.035   31.266   1.00 121.81 ? 58   ILE   B N    1 
ATOM   9739  C  CA   . ILE   B  2  54  ? 44.573  1.202   30.081   1.00 125.09 ? 58   ILE   B CA   1 
ATOM   9740  C  C    . ILE   B  2  54  ? 43.196  0.779   29.576   1.00 123.03 ? 58   ILE   B C    1 
ATOM   9741  O  O    . ILE   B  2  54  ? 42.258  0.562   30.355   1.00 125.71 ? 58   ILE   B O    1 
ATOM   9742  C  CB   . ILE   B  2  54  ? 45.459  -0.019  30.386   1.00 127.99 ? 58   ILE   B CB   1 
ATOM   9743  C  CG1  . ILE   B  2  54  ? 45.914  -0.689  29.088   1.00 127.75 ? 58   ILE   B CG1  1 
ATOM   9744  C  CG2  . ILE   B  2  54  ? 44.716  -1.018  31.263   1.00 127.08 ? 58   ILE   B CG2  1 
ATOM   9745  C  CD1  . ILE   B  2  54  ? 47.178  -1.506  29.244   1.00 126.92 ? 58   ILE   B CD1  1 
ATOM   9746  H  H    . ILE   B  2  54  ? 44.760  1.701   31.984   1.00 146.15 ? 58   ILE   B H    1 
ATOM   9747  H  HA   . ILE   B  2  54  ? 45.004  1.715   29.380   1.00 150.09 ? 58   ILE   B HA   1 
ATOM   9748  H  HB   . ILE   B  2  54  ? 46.242  0.292   30.866   1.00 153.56 ? 58   ILE   B HB   1 
ATOM   9749  H  HG12 . ILE   B  2  54  ? 45.212  -1.284  28.780   1.00 153.28 ? 58   ILE   B HG12 1 
ATOM   9750  H  HG13 . ILE   B  2  54  ? 46.083  -0.003  28.424   1.00 153.28 ? 58   ILE   B HG13 1 
ATOM   9751  H  HG21 . ILE   B  2  54  ? 45.342  -1.691  31.574   1.00 152.47 ? 58   ILE   B HG21 1 
ATOM   9752  H  HG22 . ILE   B  2  54  ? 44.332  -0.548  32.020   1.00 152.47 ? 58   ILE   B HG22 1 
ATOM   9753  H  HG23 . ILE   B  2  54  ? 44.013  -1.435  30.741   1.00 152.47 ? 58   ILE   B HG23 1 
ATOM   9754  H  HD11 . ILE   B  2  54  ? 47.472  -1.803  28.369   1.00 152.28 ? 58   ILE   B HD11 1 
ATOM   9755  H  HD12 . ILE   B  2  54  ? 47.862  -0.953  29.653   1.00 152.28 ? 58   ILE   B HD12 1 
ATOM   9756  H  HD13 . ILE   B  2  54  ? 46.991  -2.272  29.809   1.00 152.28 ? 58   ILE   B HD13 1 
ATOM   9757  N  N    . GLU   B  2  55  ? 43.073  0.665   28.255   1.00 118.19 ? 59   GLU   B N    1 
ATOM   9758  C  CA   . GLU   B  2  55  ? 41.812  0.342   27.596   1.00 115.33 ? 59   GLU   B CA   1 
ATOM   9759  C  C    . GLU   B  2  55  ? 41.997  -0.910  26.753   1.00 113.67 ? 59   GLU   B C    1 
ATOM   9760  O  O    . GLU   B  2  55  ? 42.809  -0.921  25.822   1.00 114.79 ? 59   GLU   B O    1 
ATOM   9761  C  CB   . GLU   B  2  55  ? 41.340  1.507   26.722   1.00 116.88 ? 59   GLU   B CB   1 
ATOM   9762  C  CG   . GLU   B  2  55  ? 40.603  2.596   27.481   1.00 122.32 ? 59   GLU   B CG   1 
ATOM   9763  C  CD   . GLU   B  2  55  ? 39.143  2.255   27.711   1.00 125.17 ? 59   GLU   B CD   1 
ATOM   9764  O  OE1  . GLU   B  2  55  ? 38.363  2.284   26.735   1.00 125.69 ? 59   GLU   B OE1  1 
ATOM   9765  O  OE2  . GLU   B  2  55  ? 38.776  1.947   28.864   1.00 127.27 ? 59   GLU   B OE2  1 
ATOM   9766  H  H    . GLU   B  2  55  ? 43.725  0.774   27.705   1.00 141.81 ? 59   GLU   B H    1 
ATOM   9767  H  HA   . GLU   B  2  55  ? 41.136  0.161   28.267   1.00 138.38 ? 59   GLU   B HA   1 
ATOM   9768  H  HB2  . GLU   B  2  55  ? 42.114  1.914   26.303   1.00 140.23 ? 59   GLU   B HB2  1 
ATOM   9769  H  HB3  . GLU   B  2  55  ? 40.738  1.162   26.044   1.00 140.23 ? 59   GLU   B HB3  1 
ATOM   9770  H  HG2  . GLU   B  2  55  ? 41.023  2.719   28.347   1.00 146.77 ? 59   GLU   B HG2  1 
ATOM   9771  H  HG3  . GLU   B  2  55  ? 40.643  3.420   26.972   1.00 146.77 ? 59   GLU   B HG3  1 
ATOM   9772  N  N    . ASN   B  2  56  ? 41.247  -1.963  27.080   1.00 109.95 ? 60   ASN   B N    1 
ATOM   9773  C  CA   . ASN   B  2  56  ? 41.309  -3.198  26.310   1.00 105.69 ? 60   ASN   B CA   1 
ATOM   9774  C  C    . ASN   B  2  56  ? 40.034  -4.020  26.467   1.00 100.24 ? 60   ASN   B C    1 
ATOM   9775  O  O    . ASN   B  2  56  ? 39.899  -4.768  27.444   1.00 97.47  ? 60   ASN   B O    1 
ATOM   9776  C  CB   . ASN   B  2  56  ? 42.516  -4.037  26.737   1.00 105.75 ? 60   ASN   B CB   1 
ATOM   9777  C  CG   . ASN   B  2  56  ? 42.630  -5.333  25.956   1.00 99.81  ? 60   ASN   B CG   1 
ATOM   9778  O  OD1  . ASN   B  2  56  ? 41.995  -5.501  24.915   1.00 96.29  ? 60   ASN   B OD1  1 
ATOM   9779  N  ND2  . ASN   B  2  56  ? 43.443  -6.257  26.455   1.00 97.37  ? 60   ASN   B ND2  1 
ATOM   9780  H  H    . ASN   B  2  56  ? 40.697  -1.984  27.741   1.00 131.93 ? 60   ASN   B H    1 
ATOM   9781  H  HA   . ASN   B  2  56  ? 41.395  -2.963  25.373   1.00 126.80 ? 60   ASN   B HA   1 
ATOM   9782  H  HB2  . ASN   B  2  56  ? 43.326  -3.524  26.589   1.00 126.87 ? 60   ASN   B HB2  1 
ATOM   9783  H  HB3  . ASN   B  2  56  ? 42.432  -4.258  27.678   1.00 126.87 ? 60   ASN   B HB3  1 
ATOM   9784  H  HD21 . ASN   B  2  56  ? 43.541  -7.008  26.048   1.00 116.83 ? 60   ASN   B HD21 1 
ATOM   9785  H  HD22 . ASN   B  2  56  ? 43.871  -6.103  27.184   1.00 116.83 ? 60   ASN   B HD22 1 
ATOM   9786  N  N    . PRO   B  2  57  ? 39.086  -3.926  25.539   1.00 97.77  ? 61   PRO   B N    1 
ATOM   9787  C  CA   . PRO   B  2  57  ? 37.941  -4.839  25.567   1.00 94.41  ? 61   PRO   B CA   1 
ATOM   9788  C  C    . PRO   B  2  57  ? 38.315  -6.194  24.988   1.00 89.61  ? 61   PRO   B C    1 
ATOM   9789  O  O    . PRO   B  2  57  ? 39.145  -6.303  24.083   1.00 83.72  ? 61   PRO   B O    1 
ATOM   9790  C  CB   . PRO   B  2  57  ? 36.903  -4.125  24.694   1.00 95.68  ? 61   PRO   B CB   1 
ATOM   9791  C  CG   . PRO   B  2  57  ? 37.723  -3.377  23.703   1.00 96.99  ? 61   PRO   B CG   1 
ATOM   9792  C  CD   . PRO   B  2  57  ? 39.009  -2.987  24.403   1.00 99.48  ? 61   PRO   B CD   1 
ATOM   9793  H  HA   . PRO   B  2  57  ? 37.586  -4.946  26.463   1.00 113.27 ? 61   PRO   B HA   1 
ATOM   9794  H  HB2  . PRO   B  2  57  ? 36.330  -4.775  24.258   1.00 114.80 ? 61   PRO   B HB2  1 
ATOM   9795  H  HB3  . PRO   B  2  57  ? 36.370  -3.522  25.235   1.00 114.80 ? 61   PRO   B HB3  1 
ATOM   9796  H  HG2  . PRO   B  2  57  ? 37.910  -3.949  22.941   1.00 116.37 ? 61   PRO   B HG2  1 
ATOM   9797  H  HG3  . PRO   B  2  57  ? 37.240  -2.588  23.414   1.00 116.37 ? 61   PRO   B HG3  1 
ATOM   9798  H  HD2  . PRO   B  2  57  ? 39.770  -3.099  23.812   1.00 119.36 ? 61   PRO   B HD2  1 
ATOM   9799  H  HD3  . PRO   B  2  57  ? 38.965  -2.070  24.717   1.00 119.36 ? 61   PRO   B HD3  1 
ATOM   9800  N  N    . VAL   B  2  58  ? 37.695  -7.239  25.532   1.00 92.45  ? 62   VAL   B N    1 
ATOM   9801  C  CA   . VAL   B  2  58  ? 37.991  -8.606  25.125   1.00 93.64  ? 62   VAL   B CA   1 
ATOM   9802  C  C    . VAL   B  2  58  ? 36.688  -9.353  24.886   1.00 89.34  ? 62   VAL   B C    1 
ATOM   9803  O  O    . VAL   B  2  58  ? 35.646  -9.031  25.467   1.00 90.48  ? 62   VAL   B O    1 
ATOM   9804  C  CB   . VAL   B  2  58  ? 38.854  -9.345  26.173   1.00 98.47  ? 62   VAL   B CB   1 
ATOM   9805  C  CG1  . VAL   B  2  58  ? 38.009  -9.755  27.376   1.00 96.49  ? 62   VAL   B CG1  1 
ATOM   9806  C  CG2  . VAL   B  2  58  ? 39.534  -10.553 25.542   1.00 100.92 ? 62   VAL   B CG2  1 
ATOM   9807  H  H    . VAL   B  2  58  ? 37.094  -7.179  26.145   1.00 110.92 ? 62   VAL   B H    1 
ATOM   9808  H  HA   . VAL   B  2  58  ? 38.479  -8.581  24.287   1.00 112.35 ? 62   VAL   B HA   1 
ATOM   9809  H  HB   . VAL   B  2  58  ? 39.546  -8.745  26.492   1.00 118.15 ? 62   VAL   B HB   1 
ATOM   9810  H  HG11 . VAL   B  2  58  ? 38.598  -10.040 28.093   1.00 115.76 ? 62   VAL   B HG11 1 
ATOM   9811  H  HG12 . VAL   B  2  58  ? 37.480  -8.995  27.664   1.00 115.76 ? 62   VAL   B HG12 1 
ATOM   9812  H  HG13 . VAL   B  2  58  ? 37.426  -10.486 27.118   1.00 115.76 ? 62   VAL   B HG13 1 
ATOM   9813  H  HG21 . VAL   B  2  58  ? 40.209  -10.890 26.152   1.00 121.08 ? 62   VAL   B HG21 1 
ATOM   9814  H  HG22 . VAL   B  2  58  ? 38.868  -11.239 25.374   1.00 121.08 ? 62   VAL   B HG22 1 
ATOM   9815  H  HG23 . VAL   B  2  58  ? 39.948  -10.283 24.707   1.00 121.08 ? 62   VAL   B HG23 1 
ATOM   9816  N  N    . SER   B  2  59  ? 36.756  -10.362 24.021   1.00 86.12  ? 63   SER   B N    1 
ATOM   9817  C  CA   . SER   B  2  59  ? 35.593  -11.196 23.754   1.00 83.97  ? 63   SER   B CA   1 
ATOM   9818  C  C    . SER   B  2  59  ? 35.130  -11.879 25.035   1.00 82.47  ? 63   SER   B C    1 
ATOM   9819  O  O    . SER   B  2  59  ? 35.941  -12.294 25.866   1.00 80.10  ? 63   SER   B O    1 
ATOM   9820  C  CB   . SER   B  2  59  ? 35.930  -12.240 22.690   1.00 84.60  ? 63   SER   B CB   1 
ATOM   9821  O  OG   . SER   B  2  59  ? 36.518  -11.631 21.555   1.00 87.90  ? 63   SER   B OG   1 
ATOM   9822  H  H    . SER   B  2  59  ? 37.460  -10.583 23.580   1.00 103.33 ? 63   SER   B H    1 
ATOM   9823  H  HA   . SER   B  2  59  ? 34.867  -10.647 23.419   1.00 100.74 ? 63   SER   B HA   1 
ATOM   9824  H  HB2  . SER   B  2  59  ? 36.554  -12.881 23.064   1.00 101.50 ? 63   SER   B HB2  1 
ATOM   9825  H  HB3  . SER   B  2  59  ? 35.114  -12.690 22.420   1.00 101.50 ? 63   SER   B HB3  1 
ATOM   9826  H  HG   . SER   B  2  59  ? 36.715  -12.216 20.985   1.00 105.46 ? 63   SER   B HG   1 
ATOM   9827  N  N    . GLN   B  2  60  ? 33.812  -11.996 25.191   1.00 84.37  ? 64   GLN   B N    1 
ATOM   9828  C  CA   . GLN   B  2  60  ? 33.237  -12.570 26.398   1.00 87.34  ? 64   GLN   B CA   1 
ATOM   9829  C  C    . GLN   B  2  60  ? 31.908  -13.229 26.063   1.00 87.78  ? 64   GLN   B C    1 
ATOM   9830  O  O    . GLN   B  2  60  ? 31.237  -12.852 25.099   1.00 91.04  ? 64   GLN   B O    1 
ATOM   9831  C  CB   . GLN   B  2  60  ? 33.042  -11.504 27.484   1.00 91.36  ? 64   GLN   B CB   1 
ATOM   9832  C  CG   . GLN   B  2  60  ? 32.222  -10.304 27.035   1.00 97.71  ? 64   GLN   B CG   1 
ATOM   9833  C  CD   . GLN   B  2  60  ? 32.202  -9.192  28.066   1.00 105.98 ? 64   GLN   B CD   1 
ATOM   9834  O  OE1  . GLN   B  2  60  ? 32.222  -9.446  29.270   1.00 111.47 ? 64   GLN   B OE1  1 
ATOM   9835  N  NE2  . GLN   B  2  60  ? 32.170  -7.950  27.595   1.00 105.76 ? 64   GLN   B NE2  1 
ATOM   9836  H  H    . GLN   B  2  60  ? 33.231  -11.749 24.607   1.00 101.22 ? 64   GLN   B H    1 
ATOM   9837  H  HA   . GLN   B  2  60  ? 33.831  -13.256 26.742   1.00 104.78 ? 64   GLN   B HA   1 
ATOM   9838  H  HB2  . GLN   B  2  60  ? 32.584  -11.909 28.237   1.00 109.61 ? 64   GLN   B HB2  1 
ATOM   9839  H  HB3  . GLN   B  2  60  ? 33.913  -11.179 27.761   1.00 109.61 ? 64   GLN   B HB3  1 
ATOM   9840  H  HG2  . GLN   B  2  60  ? 32.603  -9.949  26.217   1.00 117.24 ? 64   GLN   B HG2  1 
ATOM   9841  H  HG3  . GLN   B  2  60  ? 31.307  -10.586 26.880   1.00 117.24 ? 64   GLN   B HG3  1 
ATOM   9842  H  HE21 . GLN   B  2  60  ? 32.161  -7.812  26.746   1.00 126.89 ? 64   GLN   B HE21 1 
ATOM   9843  H  HE22 . GLN   B  2  60  ? 32.157  -7.285  28.139   1.00 126.89 ? 64   GLN   B HE22 1 
ATOM   9844  N  N    . VAL   B  2  61  ? 31.539  -14.220 26.872   1.00 84.88  ? 65   VAL   B N    1 
ATOM   9845  C  CA   . VAL   B  2  61  ? 30.287  -14.949 26.719   1.00 81.68  ? 65   VAL   B CA   1 
ATOM   9846  C  C    . VAL   B  2  61  ? 29.441  -14.724 27.964   1.00 82.89  ? 65   VAL   B C    1 
ATOM   9847  O  O    . VAL   B  2  61  ? 29.957  -14.738 29.087   1.00 87.92  ? 65   VAL   B O    1 
ATOM   9848  C  CB   . VAL   B  2  61  ? 30.520  -16.459 26.498   1.00 79.39  ? 65   VAL   B CB   1 
ATOM   9849  C  CG1  . VAL   B  2  61  ? 29.202  -17.161 26.182   1.00 78.55  ? 65   VAL   B CG1  1 
ATOM   9850  C  CG2  . VAL   B  2  61  ? 31.535  -16.692 25.394   1.00 79.00  ? 65   VAL   B CG2  1 
ATOM   9851  H  H    . VAL   B  2  61  ? 32.013  -14.495 27.535   1.00 101.84 ? 65   VAL   B H    1 
ATOM   9852  H  HA   . VAL   B  2  61  ? 29.812  -14.598 25.949   1.00 98.00  ? 65   VAL   B HA   1 
ATOM   9853  H  HB   . VAL   B  2  61  ? 30.877  -16.842 27.315   1.00 95.24  ? 65   VAL   B HB   1 
ATOM   9854  H  HG11 . VAL   B  2  61  ? 29.376  -18.102 26.023   1.00 94.24  ? 65   VAL   B HG11 1 
ATOM   9855  H  HG12 . VAL   B  2  61  ? 28.601  -17.060 26.937   1.00 94.24  ? 65   VAL   B HG12 1 
ATOM   9856  H  HG13 . VAL   B  2  61  ? 28.811  -16.758 25.392   1.00 94.24  ? 65   VAL   B HG13 1 
ATOM   9857  H  HG21 . VAL   B  2  61  ? 31.632  -17.646 25.250   1.00 94.78  ? 65   VAL   B HG21 1 
ATOM   9858  H  HG22 . VAL   B  2  61  ? 31.221  -16.265 24.581   1.00 94.78  ? 65   VAL   B HG22 1 
ATOM   9859  H  HG23 . VAL   B  2  61  ? 32.385  -16.309 25.661   1.00 94.78  ? 65   VAL   B HG23 1 
ATOM   9860  N  N    . GLU   B  2  62  ? 28.142  -14.520 27.761   1.00 79.94  ? 66   GLU   B N    1 
ATOM   9861  C  CA   . GLU   B  2  62  ? 27.174  -14.423 28.847   1.00 81.37  ? 66   GLU   B CA   1 
ATOM   9862  C  C    . GLU   B  2  62  ? 26.153  -15.536 28.672   1.00 81.33  ? 66   GLU   B C    1 
ATOM   9863  O  O    . GLU   B  2  62  ? 25.500  -15.626 27.626   1.00 79.46  ? 66   GLU   B O    1 
ATOM   9864  C  CB   . GLU   B  2  62  ? 26.484  -13.058 28.866   1.00 85.52  ? 66   GLU   B CB   1 
ATOM   9865  C  CG   . GLU   B  2  62  ? 25.502  -12.885 30.016   1.00 93.25  ? 66   GLU   B CG   1 
ATOM   9866  C  CD   . GLU   B  2  62  ? 24.794  -11.548 29.986   1.00 100.79 ? 66   GLU   B CD   1 
ATOM   9867  O  OE1  . GLU   B  2  62  ? 25.069  -10.749 29.066   1.00 102.31 ? 66   GLU   B OE1  1 
ATOM   9868  O  OE2  . GLU   B  2  62  ? 23.961  -11.299 30.882   1.00 104.15 ? 66   GLU   B OE2  1 
ATOM   9869  H  H    . GLU   B  2  62  ? 27.789  -14.431 26.982   1.00 95.91  ? 66   GLU   B H    1 
ATOM   9870  H  HA   . GLU   B  2  62  ? 27.627  -14.539 29.697   1.00 97.63  ? 66   GLU   B HA   1 
ATOM   9871  H  HB2  . GLU   B  2  62  ? 27.161  -12.367 28.947   1.00 102.61 ? 66   GLU   B HB2  1 
ATOM   9872  H  HB3  . GLU   B  2  62  ? 25.993  -12.945 28.037   1.00 102.61 ? 66   GLU   B HB3  1 
ATOM   9873  H  HG2  . GLU   B  2  62  ? 24.829  -13.582 29.965   1.00 111.88 ? 66   GLU   B HG2  1 
ATOM   9874  H  HG3  . GLU   B  2  62  ? 25.984  -12.950 30.856   1.00 111.88 ? 66   GLU   B HG3  1 
ATOM   9875  N  N    . ILE   B  2  63  ? 26.019  -16.379 29.689   1.00 80.93  ? 67   ILE   B N    1 
ATOM   9876  C  CA   . ILE   B  2  63  ? 25.081  -17.495 29.661   1.00 76.80  ? 67   ILE   B CA   1 
ATOM   9877  C  C    . ILE   B  2  63  ? 23.743  -17.007 30.199   1.00 79.01  ? 67   ILE   B C    1 
ATOM   9878  O  O    . ILE   B  2  63  ? 23.644  -16.592 31.359   1.00 81.63  ? 67   ILE   B O    1 
ATOM   9879  C  CB   . ILE   B  2  63  ? 25.610  -18.685 30.476   1.00 72.49  ? 67   ILE   B CB   1 
ATOM   9880  C  CG1  . ILE   B  2  63  ? 26.938  -19.170 29.885   1.00 69.93  ? 67   ILE   B CG1  1 
ATOM   9881  C  CG2  . ILE   B  2  63  ? 24.587  -19.811 30.500   1.00 70.61  ? 67   ILE   B CG2  1 
ATOM   9882  C  CD1  . ILE   B  2  63  ? 27.591  -20.294 30.658   1.00 71.06  ? 67   ILE   B CD1  1 
ATOM   9883  H  H    . ILE   B  2  63  ? 26.469  -16.325 30.421   1.00 97.09  ? 67   ILE   B H    1 
ATOM   9884  H  HA   . ILE   B  2  63  ? 24.954  -17.788 28.745   1.00 92.14  ? 67   ILE   B HA   1 
ATOM   9885  H  HB   . ILE   B  2  63  ? 25.763  -18.395 31.389   1.00 86.97  ? 67   ILE   B HB   1 
ATOM   9886  H  HG12 . ILE   B  2  63  ? 26.777  -19.490 28.983   1.00 83.90  ? 67   ILE   B HG12 1 
ATOM   9887  H  HG13 . ILE   B  2  63  ? 27.560  -18.426 29.867   1.00 83.90  ? 67   ILE   B HG13 1 
ATOM   9888  H  HG21 . ILE   B  2  63  ? 24.939  -20.546 31.028   1.00 84.71  ? 67   ILE   B HG21 1 
ATOM   9889  H  HG22 . ILE   B  2  63  ? 23.765  -19.483 30.896   1.00 84.71  ? 67   ILE   B HG22 1 
ATOM   9890  H  HG23 . ILE   B  2  63  ? 24.422  -20.107 29.591   1.00 84.71  ? 67   ILE   B HG23 1 
ATOM   9891  H  HD11 . ILE   B  2  63  ? 28.458  -20.485 30.267   1.00 85.25  ? 67   ILE   B HD11 1 
ATOM   9892  H  HD12 . ILE   B  2  63  ? 27.698  -20.021 31.583   1.00 85.25  ? 67   ILE   B HD12 1 
ATOM   9893  H  HD13 . ILE   B  2  63  ? 27.026  -21.081 30.610   1.00 85.25  ? 67   ILE   B HD13 1 
ATOM   9894  N  N    . LEU   B  2  64  ? 22.713  -17.053 29.355   1.00 78.36  ? 68   LEU   B N    1 
ATOM   9895  C  CA   . LEU   B  2  64  ? 21.373  -16.619 29.730   1.00 82.27  ? 68   LEU   B CA   1 
ATOM   9896  C  C    . LEU   B  2  64  ? 20.477  -17.782 30.139   1.00 84.76  ? 68   LEU   B C    1 
ATOM   9897  O  O    . LEU   B  2  64  ? 19.792  -17.706 31.162   1.00 91.42  ? 68   LEU   B O    1 
ATOM   9898  C  CB   . LEU   B  2  64  ? 20.729  -15.847 28.571   1.00 81.72  ? 68   LEU   B CB   1 
ATOM   9899  C  CG   . LEU   B  2  64  ? 21.471  -14.601 28.079   1.00 82.27  ? 68   LEU   B CG   1 
ATOM   9900  C  CD1  . LEU   B  2  64  ? 20.654  -13.901 27.002   1.00 79.87  ? 68   LEU   B CD1  1 
ATOM   9901  C  CD2  . LEU   B  2  64  ? 21.780  -13.646 29.222   1.00 86.02  ? 68   LEU   B CD2  1 
ATOM   9902  H  H    . LEU   B  2  64  ? 22.769  -17.337 28.545   1.00 94.02  ? 68   LEU   B H    1 
ATOM   9903  H  HA   . LEU   B  2  64  ? 21.442  -16.017 30.488   1.00 98.71  ? 68   LEU   B HA   1 
ATOM   9904  H  HB2  . LEU   B  2  64  ? 20.653  -16.450 27.815   1.00 98.04  ? 68   LEU   B HB2  1 
ATOM   9905  H  HB3  . LEU   B  2  64  ? 19.848  -15.559 28.856   1.00 98.04  ? 68   LEU   B HB3  1 
ATOM   9906  H  HG   . LEU   B  2  64  ? 22.320  -14.875 27.699   1.00 98.71  ? 68   LEU   B HG   1 
ATOM   9907  H  HD11 . LEU   B  2  64  ? 21.118  -13.095 26.729   1.00 95.82  ? 68   LEU   B HD11 1 
ATOM   9908  H  HD12 . LEU   B  2  64  ? 20.553  -14.498 26.245   1.00 95.82  ? 68   LEU   B HD12 1 
ATOM   9909  H  HD13 . LEU   B  2  64  ? 19.782  -13.676 27.364   1.00 95.82  ? 68   LEU   B HD13 1 
ATOM   9910  H  HD21 . LEU   B  2  64  ? 22.186  -12.842 28.861   1.00 103.21 ? 68   LEU   B HD21 1 
ATOM   9911  H  HD22 . LEU   B  2  64  ? 20.954  -13.422 29.679   1.00 103.21 ? 68   LEU   B HD22 1 
ATOM   9912  H  HD23 . LEU   B  2  64  ? 22.392  -14.078 29.838   1.00 103.21 ? 68   LEU   B HD23 1 
ATOM   9913  N  N    . LYS   B  2  65  ? 20.469  -18.862 29.359   1.00 79.23  ? 69   LYS   B N    1 
ATOM   9914  C  CA   . LYS   B  2  65  ? 19.660  -20.040 29.650   1.00 76.02  ? 69   LYS   B CA   1 
ATOM   9915  C  C    . LYS   B  2  65  ? 20.528  -21.279 29.494   1.00 70.34  ? 69   LYS   B C    1 
ATOM   9916  O  O    . LYS   B  2  65  ? 20.991  -21.580 28.389   1.00 69.85  ? 69   LYS   B O    1 
ATOM   9917  C  CB   . LYS   B  2  65  ? 18.438  -20.113 28.729   1.00 80.27  ? 69   LYS   B CB   1 
ATOM   9918  C  CG   . LYS   B  2  65  ? 17.402  -19.024 28.996   1.00 91.20  ? 69   LYS   B CG   1 
ATOM   9919  C  CD   . LYS   B  2  65  ? 16.109  -19.252 28.216   1.00 99.42  ? 69   LYS   B CD   1 
ATOM   9920  C  CE   . LYS   B  2  65  ? 16.006  -18.338 27.004   1.00 104.41 ? 69   LYS   B CE   1 
ATOM   9921  N  NZ   . LYS   B  2  65  ? 14.744  -18.554 26.240   1.00 107.12 ? 69   LYS   B NZ   1 
ATOM   9922  H  H    . LYS   B  2  65  ? 20.935  -18.935 28.639   1.00 95.05  ? 69   LYS   B H    1 
ATOM   9923  H  HA   . LYS   B  2  65  ? 19.349  -20.001 30.568   1.00 91.21  ? 69   LYS   B HA   1 
ATOM   9924  H  HB2  . LYS   B  2  65  ? 18.734  -20.021 27.810   1.00 96.30  ? 69   LYS   B HB2  1 
ATOM   9925  H  HB3  . LYS   B  2  65  ? 18.004  -20.971 28.854   1.00 96.30  ? 69   LYS   B HB3  1 
ATOM   9926  H  HG2  . LYS   B  2  65  ? 17.186  -19.015 29.942   1.00 109.42 ? 69   LYS   B HG2  1 
ATOM   9927  H  HG3  . LYS   B  2  65  ? 17.767  -18.165 28.731   1.00 109.42 ? 69   LYS   B HG3  1 
ATOM   9928  H  HD2  . LYS   B  2  65  ? 16.081  -20.170 27.906   1.00 119.29 ? 69   LYS   B HD2  1 
ATOM   9929  H  HD3  . LYS   B  2  65  ? 15.351  -19.074 28.795   1.00 119.29 ? 69   LYS   B HD3  1 
ATOM   9930  H  HE2  . LYS   B  2  65  ? 16.026  -17.414 27.299   1.00 125.28 ? 69   LYS   B HE2  1 
ATOM   9931  H  HE3  . LYS   B  2  65  ? 16.753  -18.512 26.410   1.00 125.28 ? 69   LYS   B HE3  1 
ATOM   9932  H  HZ1  . LYS   B  2  65  ? 14.716  -18.007 25.538   1.00 128.53 ? 69   LYS   B HZ1  1 
ATOM   9933  H  HZ2  . LYS   B  2  65  ? 14.703  -19.395 25.953   1.00 128.53 ? 69   LYS   B HZ2  1 
ATOM   9934  H  HZ3  . LYS   B  2  65  ? 14.041  -18.392 26.761   1.00 128.53 ? 69   LYS   B HZ3  1 
ATOM   9935  N  N    . ASN   B  2  66  ? 20.752  -21.988 30.599   1.00 68.57  ? 70   ASN   B N    1 
ATOM   9936  C  CA   . ASN   B  2  66  ? 21.577  -23.192 30.611   1.00 69.63  ? 70   ASN   B CA   1 
ATOM   9937  C  C    . ASN   B  2  66  ? 20.901  -24.283 31.437   1.00 70.82  ? 70   ASN   B C    1 
ATOM   9938  O  O    . ASN   B  2  66  ? 21.507  -24.897 32.316   1.00 72.51  ? 70   ASN   B O    1 
ATOM   9939  C  CB   . ASN   B  2  66  ? 22.976  -22.890 31.149   1.00 70.28  ? 70   ASN   B CB   1 
ATOM   9940  C  CG   . ASN   B  2  66  ? 23.940  -24.043 30.948   1.00 72.21  ? 70   ASN   B CG   1 
ATOM   9941  O  OD1  . ASN   B  2  66  ? 23.769  -24.858 30.040   1.00 72.35  ? 70   ASN   B OD1  1 
ATOM   9942  N  ND2  . ASN   B  2  66  ? 24.961  -24.118 31.795   1.00 74.40  ? 70   ASN   B ND2  1 
ATOM   9943  H  H    . ASN   B  2  66  ? 20.429  -21.786 31.370   1.00 82.27  ? 70   ASN   B H    1 
ATOM   9944  H  HA   . ASN   B  2  66  ? 21.660  -23.514 29.700   1.00 83.54  ? 70   ASN   B HA   1 
ATOM   9945  H  HB2  . ASN   B  2  66  ? 23.333  -22.116 30.686   1.00 84.31  ? 70   ASN   B HB2  1 
ATOM   9946  H  HB3  . ASN   B  2  66  ? 22.917  -22.710 32.100   1.00 84.31  ? 70   ASN   B HB3  1 
ATOM   9947  H  HD21 . ASN   B  2  66  ? 25.535  -24.754 31.722   1.00 89.26  ? 70   ASN   B HD21 1 
ATOM   9948  H  HD22 . ASN   B  2  66  ? 25.047  -23.530 32.417   1.00 89.26  ? 70   ASN   B HD22 1 
ATOM   9949  N  N    . LYS   B  2  67  ? 19.621  -24.521 31.175   1.00 69.81  ? 71   LYS   B N    1 
ATOM   9950  C  CA   . LYS   B  2  67  ? 18.914  -25.573 31.893   1.00 73.54  ? 71   LYS   B CA   1 
ATOM   9951  C  C    . LYS   B  2  67  ? 19.615  -26.912 31.666   1.00 73.44  ? 71   LYS   B C    1 
ATOM   9952  O  O    . LYS   B  2  67  ? 20.010  -27.221 30.535   1.00 70.81  ? 71   LYS   B O    1 
ATOM   9953  C  CB   . LYS   B  2  67  ? 17.458  -25.652 31.430   1.00 75.37  ? 71   LYS   B CB   1 
ATOM   9954  C  CG   . LYS   B  2  67  ? 16.589  -26.581 32.269   1.00 83.10  ? 71   LYS   B CG   1 
ATOM   9955  C  CD   . LYS   B  2  67  ? 15.145  -26.588 31.785   1.00 90.07  ? 71   LYS   B CD   1 
ATOM   9956  C  CE   . LYS   B  2  67  ? 14.289  -27.543 32.605   1.00 98.82  ? 71   LYS   B CE   1 
ATOM   9957  N  NZ   . LYS   B  2  67  ? 12.899  -27.654 32.081   1.00 104.23 ? 71   LYS   B NZ   1 
ATOM   9958  H  H    . LYS   B  2  67  ? 19.147  -24.096 30.597   1.00 83.75  ? 71   LYS   B H    1 
ATOM   9959  H  HA   . LYS   B  2  67  ? 18.917  -25.380 32.843   1.00 88.23  ? 71   LYS   B HA   1 
ATOM   9960  H  HB2  . LYS   B  2  67  ? 17.069  -24.765 31.474   1.00 90.42  ? 71   LYS   B HB2  1 
ATOM   9961  H  HB3  . LYS   B  2  67  ? 17.440  -25.977 30.516   1.00 90.42  ? 71   LYS   B HB3  1 
ATOM   9962  H  HG2  . LYS   B  2  67  ? 16.935  -27.485 32.208   1.00 99.70  ? 71   LYS   B HG2  1 
ATOM   9963  H  HG3  . LYS   B  2  67  ? 16.600  -26.283 33.192   1.00 99.70  ? 71   LYS   B HG3  1 
ATOM   9964  H  HD2  . LYS   B  2  67  ? 14.773  -25.696 31.869   1.00 108.06 ? 71   LYS   B HD2  1 
ATOM   9965  H  HD3  . LYS   B  2  67  ? 15.117  -26.873 30.858   1.00 108.06 ? 71   LYS   B HD3  1 
ATOM   9966  H  HE2  . LYS   B  2  67  ? 14.690  -28.426 32.584   1.00 118.56 ? 71   LYS   B HE2  1 
ATOM   9967  H  HE3  . LYS   B  2  67  ? 14.242  -27.222 33.519   1.00 118.56 ? 71   LYS   B HE3  1 
ATOM   9968  H  HZ1  . LYS   B  2  67  ? 12.436  -28.238 32.567   1.00 125.06 ? 71   LYS   B HZ1  1 
ATOM   9969  H  HZ2  . LYS   B  2  67  ? 12.496  -26.862 32.119   1.00 125.06 ? 71   LYS   B HZ2  1 
ATOM   9970  H  HZ3  . LYS   B  2  67  ? 12.914  -27.930 31.235   1.00 125.06 ? 71   LYS   B HZ3  1 
ATOM   9971  N  N    . PRO   B  2  68  ? 19.792  -27.730 32.708   1.00 73.90  ? 72   PRO   B N    1 
ATOM   9972  C  CA   . PRO   B  2  68  ? 20.515  -28.995 32.525   1.00 70.00  ? 72   PRO   B CA   1 
ATOM   9973  C  C    . PRO   B  2  68  ? 19.799  -29.928 31.560   1.00 66.75  ? 72   PRO   B C    1 
ATOM   9974  O  O    . PRO   B  2  68  ? 18.574  -29.899 31.421   1.00 67.07  ? 72   PRO   B O    1 
ATOM   9975  C  CB   . PRO   B  2  68  ? 20.565  -29.590 33.940   1.00 72.99  ? 72   PRO   B CB   1 
ATOM   9976  C  CG   . PRO   B  2  68  ? 20.328  -28.441 34.858   1.00 76.45  ? 72   PRO   B CG   1 
ATOM   9977  C  CD   . PRO   B  2  68  ? 19.409  -27.520 34.117   1.00 76.01  ? 72   PRO   B CD   1 
ATOM   9978  H  HA   . PRO   B  2  68  ? 21.415  -28.826 32.204   1.00 83.98  ? 72   PRO   B HA   1 
ATOM   9979  H  HB2  . PRO   B  2  68  ? 19.871  -30.261 34.040   1.00 87.57  ? 72   PRO   B HB2  1 
ATOM   9980  H  HB3  . PRO   B  2  68  ? 21.435  -29.986 34.100   1.00 87.57  ? 72   PRO   B HB3  1 
ATOM   9981  H  HG2  . PRO   B  2  68  ? 19.914  -28.755 35.677   1.00 91.72  ? 72   PRO   B HG2  1 
ATOM   9982  H  HG3  . PRO   B  2  68  ? 21.169  -28.002 35.059   1.00 91.72  ? 72   PRO   B HG3  1 
ATOM   9983  H  HD2  . PRO   B  2  68  ? 18.482  -27.764 34.263   1.00 91.19  ? 72   PRO   B HD2  1 
ATOM   9984  H  HD3  . PRO   B  2  68  ? 19.555  -26.599 34.381   1.00 91.19  ? 72   PRO   B HD3  1 
ATOM   9985  N  N    . LEU   B  2  69  ? 20.587  -30.764 30.886   1.00 66.77  ? 73   LEU   B N    1 
ATOM   9986  C  CA   . LEU   B  2  69  ? 20.025  -31.759 29.982   1.00 68.79  ? 73   LEU   B CA   1 
ATOM   9987  C  C    . LEU   B  2  69  ? 19.155  -32.743 30.754   1.00 71.13  ? 73   LEU   B C    1 
ATOM   9988  O  O    . LEU   B  2  69  ? 19.521  -33.205 31.839   1.00 75.62  ? 73   LEU   B O    1 
ATOM   9989  C  CB   . LEU   B  2  69  ? 21.147  -32.506 29.260   1.00 67.49  ? 73   LEU   B CB   1 
ATOM   9990  C  CG   . LEU   B  2  69  ? 21.976  -31.691 28.266   1.00 66.61  ? 73   LEU   B CG   1 
ATOM   9991  C  CD1  . LEU   B  2  69  ? 23.253  -32.437 27.914   1.00 66.57  ? 73   LEU   B CD1  1 
ATOM   9992  C  CD2  . LEU   B  2  69  ? 21.168  -31.393 27.014   1.00 64.32  ? 73   LEU   B CD2  1 
ATOM   9993  H  H    . LEU   B  2  69  ? 21.445  -30.775 30.936   1.00 80.10  ? 73   LEU   B H    1 
ATOM   9994  H  HA   . LEU   B  2  69  ? 19.475  -31.319 29.316   1.00 82.53  ? 73   LEU   B HA   1 
ATOM   9995  H  HB2  . LEU   B  2  69  ? 21.760  -32.849 29.929   1.00 80.97  ? 73   LEU   B HB2  1 
ATOM   9996  H  HB3  . LEU   B  2  69  ? 20.750  -33.240 28.766   1.00 80.97  ? 73   LEU   B HB3  1 
ATOM   9997  H  HG   . LEU   B  2  69  ? 22.220  -30.844 28.671   1.00 79.91  ? 73   LEU   B HG   1 
ATOM   9998  H  HD11 . LEU   B  2  69  ? 23.760  -31.912 27.275   1.00 79.86  ? 73   LEU   B HD11 1 
ATOM   9999  H  HD12 . LEU   B  2  69  ? 23.775  -32.569 28.721   1.00 79.86  ? 73   LEU   B HD12 1 
ATOM   10000 H  HD13 . LEU   B  2  69  ? 23.021  -33.295 27.527   1.00 79.86  ? 73   LEU   B HD13 1 
ATOM   10001 H  HD21 . LEU   B  2  69  ? 21.718  -30.888 26.395   1.00 77.17  ? 73   LEU   B HD21 1 
ATOM   10002 H  HD22 . LEU   B  2  69  ? 20.896  -32.231 26.608   1.00 77.17  ? 73   LEU   B HD22 1 
ATOM   10003 H  HD23 . LEU   B  2  69  ? 20.385  -30.876 27.260   1.00 77.17  ? 73   LEU   B HD23 1 
ATOM   10004 N  N    . SER   B  2  70  ? 17.995  -33.067 30.188   1.00 68.11  ? 74   SER   B N    1 
ATOM   10005 C  CA   . SER   B  2  70  ? 17.066  -33.962 30.866   1.00 73.47  ? 74   SER   B CA   1 
ATOM   10006 C  C    . SER   B  2  70  ? 17.596  -35.389 30.827   1.00 80.35  ? 74   SER   B C    1 
ATOM   10007 O  O    . SER   B  2  70  ? 18.051  -35.868 29.784   1.00 83.11  ? 74   SER   B O    1 
ATOM   10008 C  CB   . SER   B  2  70  ? 15.685  -33.894 30.219   1.00 74.30  ? 74   SER   B CB   1 
ATOM   10009 O  OG   . SER   B  2  70  ? 15.653  -34.613 28.998   1.00 76.09  ? 74   SER   B OG   1 
ATOM   10010 H  H    . SER   B  2  70  ? 17.726  -32.786 29.421   1.00 81.72  ? 74   SER   B H    1 
ATOM   10011 H  HA   . SER   B  2  70  ? 16.977  -33.687 31.792   1.00 88.15  ? 74   SER   B HA   1 
ATOM   10012 H  HB2  . SER   B  2  70  ? 15.034  -34.279 30.827   1.00 89.14  ? 74   SER   B HB2  1 
ATOM   10013 H  HB3  . SER   B  2  70  ? 15.466  -32.966 30.042   1.00 89.14  ? 74   SER   B HB3  1 
ATOM   10014 H  HG   . SER   B  2  70  ? 14.864  -34.660 28.713   1.00 91.29  ? 74   SER   B HG   1 
ATOM   10015 N  N    . VAL   B  2  71  ? 17.533  -36.066 31.969   1.00 83.37  ? 75   VAL   B N    1 
ATOM   10016 C  CA   . VAL   B  2  71  ? 18.020  -37.431 32.119   1.00 79.91  ? 75   VAL   B CA   1 
ATOM   10017 C  C    . VAL   B  2  71  ? 16.819  -38.359 32.235   1.00 79.79  ? 75   VAL   B C    1 
ATOM   10018 O  O    . VAL   B  2  71  ? 15.891  -38.091 33.007   1.00 81.06  ? 75   VAL   B O    1 
ATOM   10019 C  CB   . VAL   B  2  71  ? 18.947  -37.566 33.342   1.00 79.06  ? 75   VAL   B CB   1 
ATOM   10020 C  CG1  . VAL   B  2  71  ? 18.248  -37.082 34.611   1.00 85.13  ? 75   VAL   B CG1  1 
ATOM   10021 C  CG2  . VAL   B  2  71  ? 19.416  -39.006 33.501   1.00 77.53  ? 75   VAL   B CG2  1 
ATOM   10022 H  H    . VAL   B  2  71  ? 17.201  -35.744 32.694   1.00 100.03 ? 75   VAL   B H    1 
ATOM   10023 H  HA   . VAL   B  2  71  ? 18.522  -37.683 31.328   1.00 95.87  ? 75   VAL   B HA   1 
ATOM   10024 H  HB   . VAL   B  2  71  ? 19.727  -37.007 33.202   1.00 94.86  ? 75   VAL   B HB   1 
ATOM   10025 H  HG11 . VAL   B  2  71  ? 18.849  -37.194 35.364   1.00 102.14 ? 75   VAL   B HG11 1 
ATOM   10026 H  HG12 . VAL   B  2  71  ? 18.020  -36.145 34.508   1.00 102.14 ? 75   VAL   B HG12 1 
ATOM   10027 H  HG13 . VAL   B  2  71  ? 17.444  -37.606 34.748   1.00 102.14 ? 75   VAL   B HG13 1 
ATOM   10028 H  HG21 . VAL   B  2  71  ? 20.063  -39.049 34.221   1.00 93.02  ? 75   VAL   B HG21 1 
ATOM   10029 H  HG22 . VAL   B  2  71  ? 18.651  -39.566 33.709   1.00 93.02  ? 75   VAL   B HG22 1 
ATOM   10030 H  HG23 . VAL   B  2  71  ? 19.824  -39.299 32.671   1.00 93.02  ? 75   VAL   B HG23 1 
ATOM   10031 N  N    . GLY   B  2  72  ? 16.834  -39.442 31.463   1.00 77.28  ? 76   GLY   B N    1 
ATOM   10032 C  CA   . GLY   B  2  72  ? 15.795  -40.446 31.533   1.00 79.03  ? 76   GLY   B CA   1 
ATOM   10033 C  C    . GLY   B  2  72  ? 14.537  -40.048 30.783   1.00 78.65  ? 76   GLY   B C    1 
ATOM   10034 O  O    . GLY   B  2  72  ? 14.373  -38.923 30.308   1.00 80.33  ? 76   GLY   B O    1 
ATOM   10035 H  H    . GLY   B  2  72  ? 17.447  -39.615 30.885   1.00 92.71  ? 76   GLY   B H    1 
ATOM   10036 H  HA2  . GLY   B  2  72  ? 16.126  -41.274 31.153   1.00 94.81  ? 76   GLY   B HA2  1 
ATOM   10037 H  HA3  . GLY   B  2  72  ? 15.560  -40.596 32.462   1.00 94.81  ? 76   GLY   B HA3  1 
ATOM   10038 N  N    . ARG   B  2  73  ? 13.625  -41.012 30.678   1.00 77.38  ? 77   ARG   B N    1 
ATOM   10039 C  CA   . ARG   B  2  73  ? 12.352  -40.766 30.017   1.00 80.47  ? 77   ARG   B CA   1 
ATOM   10040 C  C    . ARG   B  2  73  ? 11.542  -39.737 30.796   1.00 82.13  ? 77   ARG   B C    1 
ATOM   10041 O  O    . ARG   B  2  73  ? 11.444  -39.797 32.024   1.00 84.81  ? 77   ARG   B O    1 
ATOM   10042 C  CB   . ARG   B  2  73  ? 11.566  -42.070 29.889   1.00 86.14  ? 77   ARG   B CB   1 
ATOM   10043 C  CG   . ARG   B  2  73  ? 10.277  -41.933 29.102   1.00 89.93  ? 77   ARG   B CG   1 
ATOM   10044 C  CD   . ARG   B  2  73  ? 9.514   -43.244 29.036   1.00 96.03  ? 77   ARG   B CD   1 
ATOM   10045 N  NE   . ARG   B  2  73  ? 8.267   -43.095 28.291   1.00 99.63  ? 77   ARG   B NE   1 
ATOM   10046 C  CZ   . ARG   B  2  73  ? 7.146   -42.591 28.797   1.00 106.70 ? 77   ARG   B CZ   1 
ATOM   10047 N  NH1  . ARG   B  2  73  ? 7.103   -42.182 30.059   1.00 109.36 ? 77   ARG   B NH1  1 
ATOM   10048 N  NH2  . ARG   B  2  73  ? 6.063   -42.493 28.039   1.00 110.34 ? 77   ARG   B NH2  1 
ATOM   10049 H  H    . ARG   B  2  73  ? 13.721  -41.812 30.979   1.00 92.84  ? 77   ARG   B H    1 
ATOM   10050 H  HA   . ARG   B  2  73  ? 12.511  -40.419 29.125   1.00 96.54  ? 77   ARG   B HA   1 
ATOM   10051 H  HB2  . ARG   B  2  73  ? 12.120  -42.725 29.438   1.00 103.35 ? 77   ARG   B HB2  1 
ATOM   10052 H  HB3  . ARG   B  2  73  ? 11.338  -42.385 30.778   1.00 103.35 ? 77   ARG   B HB3  1 
ATOM   10053 H  HG2  . ARG   B  2  73  ? 9.709   -41.273 29.530   1.00 107.90 ? 77   ARG   B HG2  1 
ATOM   10054 H  HG3  . ARG   B  2  73  ? 10.483  -41.656 28.196   1.00 107.90 ? 77   ARG   B HG3  1 
ATOM   10055 H  HD2  . ARG   B  2  73  ? 10.059  -43.912 28.590   1.00 115.22 ? 77   ARG   B HD2  1 
ATOM   10056 H  HD3  . ARG   B  2  73  ? 9.300   -43.538 29.935   1.00 115.22 ? 77   ARG   B HD3  1 
ATOM   10057 H  HE   . ARG   B  2  73  ? 8.257   -43.351 27.470   1.00 119.53 ? 77   ARG   B HE   1 
ATOM   10058 H  HH11 . ARG   B  2  73  ? 7.804   -42.242 30.554   1.00 131.22 ? 77   ARG   B HH11 1 
ATOM   10059 H  HH12 . ARG   B  2  73  ? 6.375   -41.856 30.381   1.00 131.22 ? 77   ARG   B HH12 1 
ATOM   10060 H  HH21 . ARG   B  2  73  ? 6.086   -42.755 27.220   1.00 132.39 ? 77   ARG   B HH21 1 
ATOM   10061 H  HH22 . ARG   B  2  73  ? 5.337   -42.167 28.365   1.00 132.39 ? 77   ARG   B HH22 1 
ATOM   10062 N  N    . GLN   B  2  74  ? 10.958  -38.787 30.070   1.00 82.34  ? 78   GLN   B N    1 
ATOM   10063 C  CA   . GLN   B  2  74  ? 10.168  -37.711 30.654   1.00 86.61  ? 78   GLN   B CA   1 
ATOM   10064 C  C    . GLN   B  2  74  ? 8.700   -37.932 30.315   1.00 90.47  ? 78   GLN   B C    1 
ATOM   10065 O  O    . GLN   B  2  74  ? 8.344   -38.063 29.139   1.00 87.51  ? 78   GLN   B O    1 
ATOM   10066 C  CB   . GLN   B  2  74  ? 10.637  -36.350 30.138   1.00 85.88  ? 78   GLN   B CB   1 
ATOM   10067 C  CG   . GLN   B  2  74  ? 12.117  -36.085 30.355   1.00 84.64  ? 78   GLN   B CG   1 
ATOM   10068 C  CD   . GLN   B  2  74  ? 12.498  -36.072 31.822   1.00 86.68  ? 78   GLN   B CD   1 
ATOM   10069 O  OE1  . GLN   B  2  74  ? 11.853  -35.413 32.637   1.00 86.55  ? 78   GLN   B OE1  1 
ATOM   10070 N  NE2  . GLN   B  2  74  ? 13.548  -36.808 32.168   1.00 88.52  ? 78   GLN   B NE2  1 
ATOM   10071 H  H    . GLN   B  2  74  ? 11.008  -38.745 29.212   1.00 98.79  ? 78   GLN   B H    1 
ATOM   10072 H  HA   . GLN   B  2  74  ? 10.265  -37.726 31.619   1.00 103.91 ? 78   GLN   B HA   1 
ATOM   10073 H  HB2  . GLN   B  2  74  ? 10.465  -36.302 29.184   1.00 103.04 ? 78   GLN   B HB2  1 
ATOM   10074 H  HB3  . GLN   B  2  74  ? 10.142  -35.655 30.599   1.00 103.04 ? 78   GLN   B HB3  1 
ATOM   10075 H  HG2  . GLN   B  2  74  ? 12.631  -36.782 29.917   1.00 101.55 ? 78   GLN   B HG2  1 
ATOM   10076 H  HG3  . GLN   B  2  74  ? 12.343  -35.220 29.978   1.00 101.55 ? 78   GLN   B HG3  1 
ATOM   10077 H  HE21 . GLN   B  2  74  ? 13.972  -37.259 31.571   1.00 106.21 ? 78   GLN   B HE21 1 
ATOM   10078 H  HE22 . GLN   B  2  74  ? 13.804  -36.834 32.988   1.00 106.21 ? 78   GLN   B HE22 1 
ATOM   10079 N  N    . LYS   B  2  75  ? 7.854   -37.979 31.346   1.00 97.50  ? 79   LYS   B N    1 
ATOM   10080 C  CA   . LYS   B  2  75  ? 6.418   -38.089 31.123   1.00 102.53 ? 79   LYS   B CA   1 
ATOM   10081 C  C    . LYS   B  2  75  ? 5.817   -36.788 30.608   1.00 106.95 ? 79   LYS   B C    1 
ATOM   10082 O  O    . LYS   B  2  75  ? 4.729   -36.810 30.022   1.00 109.05 ? 79   LYS   B O    1 
ATOM   10083 C  CB   . LYS   B  2  75  ? 5.714   -38.504 32.417   1.00 104.55 ? 79   LYS   B CB   1 
ATOM   10084 C  CG   . LYS   B  2  75  ? 6.117   -39.877 32.940   1.00 104.82 ? 79   LYS   B CG   1 
ATOM   10085 C  CD   . LYS   B  2  75  ? 5.395   -40.208 34.240   1.00 106.43 ? 79   LYS   B CD   1 
ATOM   10086 C  CE   . LYS   B  2  75  ? 5.746   -41.601 34.738   1.00 105.03 ? 79   LYS   B CE   1 
ATOM   10087 N  NZ   . LYS   B  2  75  ? 5.054   -41.935 36.016   1.00 107.00 ? 79   LYS   B NZ   1 
ATOM   10088 H  H    . LYS   B  2  75  ? 8.086   -37.948 32.174   1.00 116.98 ? 79   LYS   B H    1 
ATOM   10089 H  HA   . LYS   B  2  75  ? 6.259   -38.779 30.460   1.00 123.01 ? 79   LYS   B HA   1 
ATOM   10090 H  HB2  . LYS   B  2  75  ? 5.925   -37.854 33.105   1.00 125.44 ? 79   LYS   B HB2  1 
ATOM   10091 H  HB3  . LYS   B  2  75  ? 4.758   -38.520 32.257   1.00 125.44 ? 79   LYS   B HB3  1 
ATOM   10092 H  HG2  . LYS   B  2  75  ? 5.888   -40.552 32.283   1.00 125.76 ? 79   LYS   B HG2  1 
ATOM   10093 H  HG3  . LYS   B  2  75  ? 7.072   -39.890 33.110   1.00 125.76 ? 79   LYS   B HG3  1 
ATOM   10094 H  HD2  . LYS   B  2  75  ? 5.652   -39.567 34.921   1.00 127.70 ? 79   LYS   B HD2  1 
ATOM   10095 H  HD3  . LYS   B  2  75  ? 4.437   -40.169 34.093   1.00 127.70 ? 79   LYS   B HD3  1 
ATOM   10096 H  HE2  . LYS   B  2  75  ? 5.480   -42.253 34.071   1.00 126.02 ? 79   LYS   B HE2  1 
ATOM   10097 H  HE3  . LYS   B  2  75  ? 6.702   -41.653 34.890   1.00 126.02 ? 79   LYS   B HE3  1 
ATOM   10098 H  HZ1  . LYS   B  2  75  ? 5.279   -42.754 36.279   1.00 128.38 ? 79   LYS   B HZ1  1 
ATOM   10099 H  HZ2  . LYS   B  2  75  ? 5.287   -41.354 36.649   1.00 128.38 ? 79   LYS   B HZ2  1 
ATOM   10100 H  HZ3  . LYS   B  2  75  ? 4.172   -41.899 35.903   1.00 128.38 ? 79   LYS   B HZ3  1 
ATOM   10101 N  N    . ASN   B  2  76  ? 6.500   -35.663 30.808   1.00 107.88 ? 80   ASN   B N    1 
ATOM   10102 C  CA   . ASN   B  2  76  ? 6.008   -34.346 30.423   1.00 108.41 ? 80   ASN   B CA   1 
ATOM   10103 C  C    . ASN   B  2  76  ? 6.918   -33.785 29.340   1.00 102.68 ? 80   ASN   B C    1 
ATOM   10104 O  O    . ASN   B  2  76  ? 8.133   -33.681 29.537   1.00 99.99  ? 80   ASN   B O    1 
ATOM   10105 C  CB   . ASN   B  2  76  ? 5.958   -33.417 31.638   1.00 114.45 ? 80   ASN   B CB   1 
ATOM   10106 C  CG   . ASN   B  2  76  ? 5.603   -31.994 31.271   1.00 117.05 ? 80   ASN   B CG   1 
ATOM   10107 O  OD1  . ASN   B  2  76  ? 6.463   -31.116 31.262   1.00 119.09 ? 80   ASN   B OD1  1 
ATOM   10108 N  ND2  . ASN   B  2  76  ? 4.333   -31.757 30.965   1.00 117.11 ? 80   ASN   B ND2  1 
ATOM   10109 H  H    . ASN   B  2  76  ? 7.276   -35.639 31.177   1.00 129.43 ? 80   ASN   B H    1 
ATOM   10110 H  HA   . ASN   B  2  76  ? 5.113   -34.417 30.055   1.00 130.08 ? 80   ASN   B HA   1 
ATOM   10111 H  HB2  . ASN   B  2  76  ? 5.287   -33.744 32.258   1.00 137.32 ? 80   ASN   B HB2  1 
ATOM   10112 H  HB3  . ASN   B  2  76  ? 6.829   -33.409 32.065   1.00 137.32 ? 80   ASN   B HB3  1 
ATOM   10113 H  HD21 . ASN   B  2  76  ? 4.083   -30.962 30.750   1.00 140.51 ? 80   ASN   B HD21 1 
ATOM   10114 H  HD22 . ASN   B  2  76  ? 3.759   -32.398 30.982   1.00 140.51 ? 80   ASN   B HD22 1 
ATOM   10115 N  N    . SER   B  2  77  ? 6.328   -33.428 28.195   1.00 99.94  ? 81   SER   B N    1 
ATOM   10116 C  CA   . SER   B  2  77  ? 7.117   -32.964 27.060   1.00 96.21  ? 81   SER   B CA   1 
ATOM   10117 C  C    . SER   B  2  77  ? 7.836   -31.651 27.345   1.00 95.55  ? 81   SER   B C    1 
ATOM   10118 O  O    . SER   B  2  77  ? 8.812   -31.332 26.656   1.00 92.24  ? 81   SER   B O    1 
ATOM   10119 C  CB   . SER   B  2  77  ? 6.221   -32.803 25.830   1.00 96.90  ? 81   SER   B CB   1 
ATOM   10120 O  OG   . SER   B  2  77  ? 5.642   -34.041 25.456   1.00 100.79 ? 81   SER   B OG   1 
ATOM   10121 H  H    . SER   B  2  77  ? 5.480   -33.445 28.055   1.00 119.91 ? 81   SER   B H    1 
ATOM   10122 H  HA   . SER   B  2  77  ? 7.790   -33.634 26.863   1.00 115.43 ? 81   SER   B HA   1 
ATOM   10123 H  HB2  . SER   B  2  77  ? 5.512   -32.173 26.037   1.00 116.26 ? 81   SER   B HB2  1 
ATOM   10124 H  HB3  . SER   B  2  77  ? 6.756   -32.469 25.092   1.00 116.26 ? 81   SER   B HB3  1 
ATOM   10125 H  HG   . SER   B  2  77  ? 5.174   -33.942 24.766   1.00 120.93 ? 81   SER   B HG   1 
ATOM   10126 N  N    . SER   B  2  78  ? 7.383   -30.885 28.337   1.00 98.11  ? 82   SER   B N    1 
ATOM   10127 C  CA   . SER   B  2  78  ? 7.990   -29.592 28.630   1.00 99.43  ? 82   SER   B CA   1 
ATOM   10128 C  C    . SER   B  2  78  ? 9.263   -29.705 29.457   1.00 97.96  ? 82   SER   B C    1 
ATOM   10129 O  O    . SER   B  2  78  ? 9.974   -28.704 29.605   1.00 99.29  ? 82   SER   B O    1 
ATOM   10130 C  CB   . SER   B  2  78  ? 6.988   -28.696 29.361   1.00 105.56 ? 82   SER   B CB   1 
ATOM   10131 O  OG   . SER   B  2  78  ? 5.755   -28.639 28.666   1.00 107.87 ? 82   SER   B OG   1 
ATOM   10132 H  H    . SER   B  2  78  ? 6.727   -31.092 28.852   1.00 117.71 ? 82   SER   B H    1 
ATOM   10133 H  HA   . SER   B  2  78  ? 8.219   -29.165 27.790   1.00 119.30 ? 82   SER   B HA   1 
ATOM   10134 H  HB2  . SER   B  2  78  ? 6.833   -29.055 30.249   1.00 126.65 ? 82   SER   B HB2  1 
ATOM   10135 H  HB3  . SER   B  2  78  ? 7.355   -27.800 29.425   1.00 126.65 ? 82   SER   B HB3  1 
ATOM   10136 H  HG   . SER   B  2  78  ? 5.197   -28.194 29.108   1.00 129.43 ? 82   SER   B HG   1 
ATOM   10137 N  N    . ASP   B  2  79  ? 9.567   -30.883 30.000   1.00 95.61  ? 83   ASP   B N    1 
ATOM   10138 C  CA   . ASP   B  2  79  ? 10.783  -31.100 30.770   1.00 92.90  ? 83   ASP   B CA   1 
ATOM   10139 C  C    . ASP   B  2  79  ? 11.882  -31.779 29.961   1.00 86.67  ? 83   ASP   B C    1 
ATOM   10140 O  O    . ASP   B  2  79  ? 12.933  -32.106 30.521   1.00 86.11  ? 83   ASP   B O    1 
ATOM   10141 C  CB   . ASP   B  2  79  ? 10.474  -31.929 32.021   1.00 99.72  ? 83   ASP   B CB   1 
ATOM   10142 C  CG   . ASP   B  2  79  ? 9.623   -31.174 33.024   1.00 108.17 ? 83   ASP   B CG   1 
ATOM   10143 O  OD1  . ASP   B  2  79  ? 9.725   -29.930 33.075   1.00 110.38 ? 83   ASP   B OD1  1 
ATOM   10144 O  OD2  . ASP   B  2  79  ? 8.851   -31.823 33.763   1.00 112.27 ? 83   ASP   B OD2  1 
ATOM   10145 H  H    . ASP   B  2  79  ? 9.073   -31.583 29.932   1.00 114.71 ? 83   ASP   B H    1 
ATOM   10146 H  HA   . ASP   B  2  79  ? 11.119  -30.236 31.057   1.00 111.46 ? 83   ASP   B HA   1 
ATOM   10147 H  HB2  . ASP   B  2  79  ? 9.993   -32.729 31.760   1.00 119.65 ? 83   ASP   B HB2  1 
ATOM   10148 H  HB3  . ASP   B  2  79  ? 11.308  -32.170 32.455   1.00 119.65 ? 83   ASP   B HB3  1 
ATOM   10149 N  N    . ILE   B  2  80  ? 11.667  -31.998 28.666   1.00 82.92  ? 84   ILE   B N    1 
ATOM   10150 C  CA   . ILE   B  2  80  ? 12.695  -32.578 27.807   1.00 79.68  ? 84   ILE   B CA   1 
ATOM   10151 C  C    . ILE   B  2  80  ? 13.693  -31.491 27.432   1.00 77.49  ? 84   ILE   B C    1 
ATOM   10152 O  O    . ILE   B  2  80  ? 13.315  -30.437 26.906   1.00 78.28  ? 84   ILE   B O    1 
ATOM   10153 C  CB   . ILE   B  2  80  ? 12.068  -33.213 26.554   1.00 77.81  ? 84   ILE   B CB   1 
ATOM   10154 C  CG1  . ILE   B  2  80  ? 11.247  -34.448 26.940   1.00 77.25  ? 84   ILE   B CG1  1 
ATOM   10155 C  CG2  . ILE   B  2  80  ? 13.152  -33.579 25.538   1.00 75.14  ? 84   ILE   B CG2  1 
ATOM   10156 C  CD1  . ILE   B  2  80  ? 10.528  -35.108 25.775   1.00 74.23  ? 84   ILE   B CD1  1 
ATOM   10157 H  H    . ILE   B  2  80  ? 10.931  -31.819 28.260   1.00 99.48  ? 84   ILE   B H    1 
ATOM   10158 H  HA   . ILE   B  2  80  ? 13.164  -33.272 28.295   1.00 95.59  ? 84   ILE   B HA   1 
ATOM   10159 H  HB   . ILE   B  2  80  ? 11.474  -32.564 26.145   1.00 93.36  ? 84   ILE   B HB   1 
ATOM   10160 H  HG12 . ILE   B  2  80  ? 11.843  -35.107 27.329   1.00 92.68  ? 84   ILE   B HG12 1 
ATOM   10161 H  HG13 . ILE   B  2  80  ? 10.576  -34.184 27.589   1.00 92.68  ? 84   ILE   B HG13 1 
ATOM   10162 H  HG21 . ILE   B  2  80  ? 12.738  -34.019 24.779   1.00 90.15  ? 84   ILE   B HG21 1 
ATOM   10163 H  HG22 . ILE   B  2  80  ? 13.598  -32.768 25.246   1.00 90.15  ? 84   ILE   B HG22 1 
ATOM   10164 H  HG23 . ILE   B  2  80  ? 13.791  -34.175 25.958   1.00 90.15  ? 84   ILE   B HG23 1 
ATOM   10165 H  HD11 . ILE   B  2  80  ? 9.974   -35.828 26.114   1.00 89.06  ? 84   ILE   B HD11 1 
ATOM   10166 H  HD12 . ILE   B  2  80  ? 9.976   -34.446 25.330   1.00 89.06  ? 84   ILE   B HD12 1 
ATOM   10167 H  HD13 . ILE   B  2  80  ? 11.187  -35.460 25.156   1.00 89.06  ? 84   ILE   B HD13 1 
ATOM   10168 N  N    . VAL   B  2  81  ? 14.970  -31.748 27.698   1.00 74.68  ? 85   VAL   B N    1 
ATOM   10169 C  CA   . VAL   B  2  81  ? 16.059  -30.839 27.358   1.00 70.93  ? 85   VAL   B CA   1 
ATOM   10170 C  C    . VAL   B  2  81  ? 17.112  -31.668 26.637   1.00 69.09  ? 85   VAL   B C    1 
ATOM   10171 O  O    . VAL   B  2  81  ? 17.773  -32.512 27.257   1.00 72.24  ? 85   VAL   B O    1 
ATOM   10172 C  CB   . VAL   B  2  81  ? 16.653  -30.153 28.596   1.00 70.29  ? 85   VAL   B CB   1 
ATOM   10173 C  CG1  . VAL   B  2  81  ? 17.748  -29.173 28.192   1.00 71.54  ? 85   VAL   B CG1  1 
ATOM   10174 C  CG2  . VAL   B  2  81  ? 15.563  -29.445 29.388   1.00 66.75  ? 85   VAL   B CG2  1 
ATOM   10175 H  H    . VAL   B  2  81  ? 15.238  -32.466 28.089   1.00 89.59  ? 85   VAL   B H    1 
ATOM   10176 H  HA   . VAL   B  2  81  ? 15.736  -30.150 26.756   1.00 85.10  ? 85   VAL   B HA   1 
ATOM   10177 H  HB   . VAL   B  2  81  ? 17.052  -30.828 29.167   1.00 84.33  ? 85   VAL   B HB   1 
ATOM   10178 H  HG11 . VAL   B  2  81  ? 18.080  -28.726 28.987   1.00 85.83  ? 85   VAL   B HG11 1 
ATOM   10179 H  HG12 . VAL   B  2  81  ? 18.467  -29.662 27.764   1.00 85.83  ? 85   VAL   B HG12 1 
ATOM   10180 H  HG13 . VAL   B  2  81  ? 17.378  -28.522 27.576   1.00 85.83  ? 85   VAL   B HG13 1 
ATOM   10181 H  HG21 . VAL   B  2  81  ? 15.963  -29.009 30.156   1.00 80.08  ? 85   VAL   B HG21 1 
ATOM   10182 H  HG22 . VAL   B  2  81  ? 15.136  -28.785 28.818   1.00 80.08  ? 85   VAL   B HG22 1 
ATOM   10183 H  HG23 . VAL   B  2  81  ? 14.910  -30.099 29.682   1.00 80.08  ? 85   VAL   B HG23 1 
ATOM   10184 N  N    . GLN   B  2  82  ? 17.268  -31.436 25.332   1.00 66.28  ? 86   GLN   B N    1 
ATOM   10185 C  CA   . GLN   B  2  82  ? 18.201  -32.201 24.518   1.00 64.65  ? 86   GLN   B CA   1 
ATOM   10186 C  C    . GLN   B  2  82  ? 19.439  -31.415 24.113   1.00 63.58  ? 86   GLN   B C    1 
ATOM   10187 O  O    . GLN   B  2  82  ? 20.407  -32.023 23.643   1.00 64.46  ? 86   GLN   B O    1 
ATOM   10188 C  CB   . GLN   B  2  82  ? 17.499  -32.720 23.252   1.00 64.41  ? 86   GLN   B CB   1 
ATOM   10189 C  CG   . GLN   B  2  82  ? 16.182  -33.430 23.525   1.00 66.29  ? 86   GLN   B CG   1 
ATOM   10190 C  CD   . GLN   B  2  82  ? 15.709  -34.265 22.351   1.00 62.91  ? 86   GLN   B CD   1 
ATOM   10191 O  OE1  . GLN   B  2  82  ? 15.999  -35.458 22.269   1.00 60.54  ? 86   GLN   B OE1  1 
ATOM   10192 N  NE2  . GLN   B  2  82  ? 14.974  -33.642 21.436   1.00 59.49  ? 86   GLN   B NE2  1 
ATOM   10193 H  H    . GLN   B  2  82  ? 16.838  -30.833 24.895   1.00 79.51  ? 86   GLN   B H    1 
ATOM   10194 H  HA   . GLN   B  2  82  ? 18.496  -32.970 25.030   1.00 77.56  ? 86   GLN   B HA   1 
ATOM   10195 H  HB2  . GLN   B  2  82  ? 17.314  -31.968 22.668   1.00 77.27  ? 86   GLN   B HB2  1 
ATOM   10196 H  HB3  . GLN   B  2  82  ? 18.087  -33.349 22.806   1.00 77.27  ? 86   GLN   B HB3  1 
ATOM   10197 H  HG2  . GLN   B  2  82  ? 16.293  -34.020 24.287   1.00 79.53  ? 86   GLN   B HG2  1 
ATOM   10198 H  HG3  . GLN   B  2  82  ? 15.499  -32.767 23.715   1.00 79.53  ? 86   GLN   B HG3  1 
ATOM   10199 H  HE21 . GLN   B  2  82  ? 14.790  -32.807 21.528   1.00 71.37  ? 86   GLN   B HE21 1 
ATOM   10200 H  HE22 . GLN   B  2  82  ? 14.683  -34.073 20.751   1.00 71.37  ? 86   GLN   B HE22 1 
ATOM   10201 N  N    . ILE   B  2  83  ? 19.440  -30.093 24.274   1.00 61.56  ? 87   ILE   B N    1 
ATOM   10202 C  CA   . ILE   B  2  83  ? 20.605  -29.263 23.996   1.00 62.02  ? 87   ILE   B CA   1 
ATOM   10203 C  C    . ILE   B  2  83  ? 20.796  -28.296 25.156   1.00 66.52  ? 87   ILE   B C    1 
ATOM   10204 O  O    . ILE   B  2  83  ? 19.831  -27.697 25.644   1.00 68.08  ? 87   ILE   B O    1 
ATOM   10205 C  CB   . ILE   B  2  83  ? 20.467  -28.493 22.666   1.00 60.61  ? 87   ILE   B CB   1 
ATOM   10206 C  CG1  . ILE   B  2  83  ? 21.809  -27.866 22.279   1.00 60.39  ? 87   ILE   B CG1  1 
ATOM   10207 C  CG2  . ILE   B  2  83  ? 19.402  -27.415 22.784   1.00 57.78  ? 87   ILE   B CG2  1 
ATOM   10208 C  CD1  . ILE   B  2  83  ? 21.842  -27.281 20.882   1.00 58.87  ? 87   ILE   B CD1  1 
ATOM   10209 H  H    . ILE   B  2  83  ? 18.759  -29.645 24.549   1.00 73.85  ? 87   ILE   B H    1 
ATOM   10210 H  HA   . ILE   B  2  83  ? 21.389  -29.831 23.934   1.00 74.41  ? 87   ILE   B HA   1 
ATOM   10211 H  HB   . ILE   B  2  83  ? 20.200  -29.120 21.976   1.00 72.71  ? 87   ILE   B HB   1 
ATOM   10212 H  HG12 . ILE   B  2  83  ? 22.008  -27.150 22.902   1.00 72.45  ? 87   ILE   B HG12 1 
ATOM   10213 H  HG13 . ILE   B  2  83  ? 22.497  -28.549 22.329   1.00 72.45  ? 87   ILE   B HG13 1 
ATOM   10214 H  HG21 . ILE   B  2  83  ? 19.089  -27.182 21.896   1.00 69.32  ? 87   ILE   B HG21 1 
ATOM   10215 H  HG22 . ILE   B  2  83  ? 18.665  -27.756 23.315   1.00 69.32  ? 87   ILE   B HG22 1 
ATOM   10216 H  HG23 . ILE   B  2  83  ? 19.788  -26.636 23.214   1.00 69.32  ? 87   ILE   B HG23 1 
ATOM   10217 H  HD11 . ILE   B  2  83  ? 22.629  -26.721 20.792   1.00 70.62  ? 87   ILE   B HD11 1 
ATOM   10218 H  HD12 . ILE   B  2  83  ? 21.877  -28.005 20.237   1.00 70.62  ? 87   ILE   B HD12 1 
ATOM   10219 H  HD13 . ILE   B  2  83  ? 21.041  -26.752 20.742   1.00 70.62  ? 87   ILE   B HD13 1 
ATOM   10220 N  N    . ALA   B  2  84  ? 22.045  -28.150 25.601   1.00 68.37  ? 88   ALA   B N    1 
ATOM   10221 C  CA   . ALA   B  2  84  ? 22.394  -27.244 26.681   1.00 70.83  ? 88   ALA   B CA   1 
ATOM   10222 C  C    . ALA   B  2  84  ? 23.738  -26.618 26.321   1.00 70.46  ? 88   ALA   B C    1 
ATOM   10223 O  O    . ALA   B  2  84  ? 24.659  -27.342 25.900   1.00 72.31  ? 88   ALA   B O    1 
ATOM   10224 C  CB   . ALA   B  2  84  ? 22.481  -27.967 28.028   1.00 74.79  ? 88   ALA   B CB   1 
ATOM   10225 H  H    . ALA   B  2  84  ? 22.720  -28.578 25.281   1.00 82.03  ? 88   ALA   B H    1 
ATOM   10226 H  HA   . ALA   B  2  84  ? 21.720  -26.552 26.758   1.00 84.98  ? 88   ALA   B HA   1 
ATOM   10227 H  HB1  . ALA   B  2  84  ? 22.730  -27.327 28.713   1.00 89.73  ? 88   ALA   B HB1  1 
ATOM   10228 H  HB2  . ALA   B  2  84  ? 21.616  -28.354 28.235   1.00 89.73  ? 88   ALA   B HB2  1 
ATOM   10229 H  HB3  . ALA   B  2  84  ? 23.151  -28.666 27.968   1.00 89.73  ? 88   ALA   B HB3  1 
ATOM   10230 N  N    . PRO   B  2  85  ? 23.897  -25.291 26.462   1.00 70.14  ? 89   PRO   B N    1 
ATOM   10231 C  CA   . PRO   B  2  85  ? 22.924  -24.280 26.902   1.00 71.77  ? 89   PRO   B CA   1 
ATOM   10232 C  C    . PRO   B  2  85  ? 21.812  -24.042 25.887   1.00 68.55  ? 89   PRO   B C    1 
ATOM   10233 O  O    . PRO   B  2  85  ? 21.791  -24.690 24.841   1.00 68.29  ? 89   PRO   B O    1 
ATOM   10234 C  CB   . PRO   B  2  85  ? 23.778  -23.014 27.068   1.00 73.85  ? 89   PRO   B CB   1 
ATOM   10235 C  CG   . PRO   B  2  85  ? 25.192  -23.490 27.124   1.00 73.60  ? 89   PRO   B CG   1 
ATOM   10236 C  CD   . PRO   B  2  85  ? 25.231  -24.704 26.262   1.00 72.83  ? 89   PRO   B CD   1 
ATOM   10237 H  HA   . PRO   B  2  85  ? 22.537  -24.532 27.755   1.00 86.11  ? 89   PRO   B HA   1 
ATOM   10238 H  HB2  . PRO   B  2  85  ? 23.642  -22.424 26.310   1.00 88.59  ? 89   PRO   B HB2  1 
ATOM   10239 H  HB3  . PRO   B  2  85  ? 23.534  -22.559 27.890   1.00 88.59  ? 89   PRO   B HB3  1 
ATOM   10240 H  HG2  . PRO   B  2  85  ? 25.785  -22.803 26.782   1.00 88.30  ? 89   PRO   B HG2  1 
ATOM   10241 H  HG3  . PRO   B  2  85  ? 25.431  -23.708 28.039   1.00 88.30  ? 89   PRO   B HG3  1 
ATOM   10242 H  HD2  . PRO   B  2  85  ? 25.370  -24.465 25.332   1.00 87.38  ? 89   PRO   B HD2  1 
ATOM   10243 H  HD3  . PRO   B  2  85  ? 25.926  -25.315 26.555   1.00 87.38  ? 89   PRO   B HD3  1 
ATOM   10244 N  N    . GLN   B  2  86  ? 20.898  -23.118 26.199   1.00 69.27  ? 90   GLN   B N    1 
ATOM   10245 C  CA   . GLN   B  2  86  ? 19.794  -22.787 25.312   1.00 68.09  ? 90   GLN   B CA   1 
ATOM   10246 C  C    . GLN   B  2  86  ? 19.782  -21.333 24.862   1.00 65.88  ? 90   GLN   B C    1 
ATOM   10247 O  O    . GLN   B  2  86  ? 19.044  -21.005 23.926   1.00 63.63  ? 90   GLN   B O    1 
ATOM   10248 C  CB   . GLN   B  2  86  ? 18.447  -23.106 25.985   1.00 70.36  ? 90   GLN   B CB   1 
ATOM   10249 C  CG   . GLN   B  2  86  ? 18.259  -24.574 26.349   1.00 72.00  ? 90   GLN   B CG   1 
ATOM   10250 C  CD   . GLN   B  2  86  ? 18.780  -24.910 27.732   1.00 74.60  ? 90   GLN   B CD   1 
ATOM   10251 O  OE1  . GLN   B  2  86  ? 18.798  -24.063 28.626   1.00 74.04  ? 90   GLN   B OE1  1 
ATOM   10252 N  NE2  . GLN   B  2  86  ? 19.205  -26.154 27.917   1.00 76.67  ? 90   GLN   B NE2  1 
ATOM   10253 H  H    . GLN   B  2  86  ? 20.902  -22.666 26.930   1.00 83.10  ? 90   GLN   B H    1 
ATOM   10254 H  HA   . GLN   B  2  86  ? 19.866  -23.341 24.519   1.00 81.69  ? 90   GLN   B HA   1 
ATOM   10255 H  HB2  . GLN   B  2  86  ? 18.380  -22.590 26.803   1.00 84.42  ? 90   GLN   B HB2  1 
ATOM   10256 H  HB3  . GLN   B  2  86  ? 17.732  -22.860 25.377   1.00 84.42  ? 90   GLN   B HB3  1 
ATOM   10257 H  HG2  . GLN   B  2  86  ? 17.312  -24.786 26.325   1.00 86.38  ? 90   GLN   B HG2  1 
ATOM   10258 H  HG3  . GLN   B  2  86  ? 18.737  -25.122 25.707   1.00 86.38  ? 90   GLN   B HG3  1 
ATOM   10259 H  HE21 . GLN   B  2  86  ? 19.175  -26.719 27.269   1.00 91.98  ? 90   GLN   B HE21 1 
ATOM   10260 H  HE22 . GLN   B  2  86  ? 19.510  -26.395 28.684   1.00 91.98  ? 90   GLN   B HE22 1 
ATOM   10261 N  N    . SER   B  2  87  ? 20.566  -20.455 25.488   1.00 67.79  ? 91   SER   B N    1 
ATOM   10262 C  CA   . SER   B  2  87  ? 20.618  -19.058 25.072   1.00 73.32  ? 91   SER   B CA   1 
ATOM   10263 C  C    . SER   B  2  87  ? 21.903  -18.432 25.590   1.00 72.84  ? 91   SER   B C    1 
ATOM   10264 O  O    . SER   B  2  87  ? 22.190  -18.505 26.788   1.00 72.23  ? 91   SER   B O    1 
ATOM   10265 C  CB   . SER   B  2  87  ? 19.398  -18.286 25.586   1.00 81.42  ? 91   SER   B CB   1 
ATOM   10266 O  OG   . SER   B  2  87  ? 19.408  -16.948 25.120   1.00 86.89  ? 91   SER   B OG   1 
ATOM   10267 H  H    . SER   B  2  87  ? 21.075  -20.646 26.154   1.00 81.32  ? 91   SER   B H    1 
ATOM   10268 H  HA   . SER   B  2  87  ? 20.627  -19.011 24.103   1.00 87.97  ? 91   SER   B HA   1 
ATOM   10269 H  HB2  . SER   B  2  87  ? 18.592  -18.723 25.269   1.00 97.68  ? 91   SER   B HB2  1 
ATOM   10270 H  HB3  . SER   B  2  87  ? 19.414  -18.281 26.555   1.00 97.68  ? 91   SER   B HB3  1 
ATOM   10271 H  HG   . SER   B  2  87  ? 18.730  -16.540 25.402   1.00 104.25 ? 91   SER   B HG   1 
ATOM   10272 N  N    . LEU   B  2  88  ? 22.669  -17.819 24.687   1.00 72.42  ? 92   LEU   B N    1 
ATOM   10273 C  CA   . LEU   B  2  88  ? 23.928  -17.182 25.041   1.00 72.38  ? 92   LEU   B CA   1 
ATOM   10274 C  C    . LEU   B  2  88  ? 24.062  -15.859 24.302   1.00 72.62  ? 92   LEU   B C    1 
ATOM   10275 O  O    . LEU   B  2  88  ? 23.534  -15.688 23.200   1.00 71.36  ? 92   LEU   B O    1 
ATOM   10276 C  CB   . LEU   B  2  88  ? 25.139  -18.057 24.688   1.00 71.62  ? 92   LEU   B CB   1 
ATOM   10277 C  CG   . LEU   B  2  88  ? 25.125  -19.531 25.088   1.00 74.84  ? 92   LEU   B CG   1 
ATOM   10278 C  CD1  . LEU   B  2  88  ? 26.229  -20.264 24.335   1.00 72.28  ? 92   LEU   B CD1  1 
ATOM   10279 C  CD2  . LEU   B  2  88  ? 25.296  -19.697 26.588   1.00 81.65  ? 92   LEU   B CD2  1 
ATOM   10280 H  H    . LEU   B  2  88  ? 22.474  -17.759 23.852   1.00 86.89  ? 92   LEU   B H    1 
ATOM   10281 H  HA   . LEU   B  2  88  ? 23.926  -17.013 25.996   1.00 86.84  ? 92   LEU   B HA   1 
ATOM   10282 H  HB2  . LEU   B  2  88  ? 25.242  -18.036 23.724   1.00 85.93  ? 92   LEU   B HB2  1 
ATOM   10283 H  HB3  . LEU   B  2  88  ? 25.916  -17.664 25.114   1.00 85.93  ? 92   LEU   B HB3  1 
ATOM   10284 H  HG   . LEU   B  2  88  ? 24.268  -19.922 24.857   1.00 89.79  ? 92   LEU   B HG   1 
ATOM   10285 H  HD11 . LEU   B  2  88  ? 26.302  -21.167 24.681   1.00 86.72  ? 92   LEU   B HD11 1 
ATOM   10286 H  HD12 . LEU   B  2  88  ? 26.005  -20.288 23.392   1.00 86.72  ? 92   LEU   B HD12 1 
ATOM   10287 H  HD13 . LEU   B  2  88  ? 27.067  -19.792 24.465   1.00 86.72  ? 92   LEU   B HD13 1 
ATOM   10288 H  HD21 . LEU   B  2  88  ? 25.685  -20.567 26.767   1.00 97.96  ? 92   LEU   B HD21 1 
ATOM   10289 H  HD22 . LEU   B  2  88  ? 25.882  -18.998 26.918   1.00 97.96  ? 92   LEU   B HD22 1 
ATOM   10290 H  HD23 . LEU   B  2  88  ? 24.427  -19.630 27.014   1.00 97.96  ? 92   LEU   B HD23 1 
ATOM   10291 N  N    . ILE   B  2  89  ? 24.783  -14.926 24.919   1.00 75.50  ? 93   ILE   B N    1 
ATOM   10292 C  CA   . ILE   B  2  89  ? 25.249  -13.711 24.262   1.00 77.73  ? 93   ILE   B CA   1 
ATOM   10293 C  C    . ILE   B  2  89  ? 26.747  -13.858 24.043   1.00 74.25  ? 93   ILE   B C    1 
ATOM   10294 O  O    . ILE   B  2  89  ? 27.482  -14.215 24.973   1.00 72.55  ? 93   ILE   B O    1 
ATOM   10295 C  CB   . ILE   B  2  89  ? 24.956  -12.447 25.090   1.00 88.52  ? 93   ILE   B CB   1 
ATOM   10296 C  CG1  . ILE   B  2  89  ? 23.466  -12.334 25.428   1.00 93.49  ? 93   ILE   B CG1  1 
ATOM   10297 C  CG2  . ILE   B  2  89  ? 25.451  -11.210 24.340   1.00 91.20  ? 93   ILE   B CG2  1 
ATOM   10298 C  CD1  . ILE   B  2  89  ? 22.573  -11.924 24.271   1.00 94.83  ? 93   ILE   B CD1  1 
ATOM   10299 H  H    . ILE   B  2  89  ? 25.021  -14.978 25.744   1.00 90.58  ? 93   ILE   B H    1 
ATOM   10300 H  HA   . ILE   B  2  89  ? 24.798  -13.620 23.409   1.00 93.25  ? 93   ILE   B HA   1 
ATOM   10301 H  HB   . ILE   B  2  89  ? 25.434  -12.515 25.931   1.00 106.21 ? 93   ILE   B HB   1 
ATOM   10302 H  HG12 . ILE   B  2  89  ? 23.156  -13.199 25.741   1.00 112.17 ? 93   ILE   B HG12 1 
ATOM   10303 H  HG13 . ILE   B  2  89  ? 23.360  -11.670 26.127   1.00 112.17 ? 93   ILE   B HG13 1 
ATOM   10304 H  HG21 . ILE   B  2  89  ? 25.105  -10.416 24.777   1.00 109.42 ? 93   ILE   B HG21 1 
ATOM   10305 H  HG22 . ILE   B  2  89  ? 26.421  -11.199 24.354   1.00 109.42 ? 93   ILE   B HG22 1 
ATOM   10306 H  HG23 . ILE   B  2  89  ? 25.134  -11.248 23.424   1.00 109.42 ? 93   ILE   B HG23 1 
ATOM   10307 H  HD11 . ILE   B  2  89  ? 21.678  -11.760 24.606   1.00 113.78 ? 93   ILE   B HD11 1 
ATOM   10308 H  HD12 . ILE   B  2  89  ? 22.929  -11.117 23.869   1.00 113.78 ? 93   ILE   B HD12 1 
ATOM   10309 H  HD13 . ILE   B  2  89  ? 22.556  -12.640 23.617   1.00 113.78 ? 93   ILE   B HD13 1 
ATOM   10310 N  N    . LEU   B  2  90  ? 27.200  -13.583 22.825   1.00 73.86  ? 94   LEU   B N    1 
ATOM   10311 C  CA   . LEU   B  2  90  ? 28.617  -13.648 22.479   1.00 73.54  ? 94   LEU   B CA   1 
ATOM   10312 C  C    . LEU   B  2  90  ? 29.064  -12.255 22.046   1.00 74.30  ? 94   LEU   B C    1 
ATOM   10313 O  O    . LEU   B  2  90  ? 28.772  -11.819 20.928   1.00 74.58  ? 94   LEU   B O    1 
ATOM   10314 C  CB   . LEU   B  2  90  ? 28.867  -14.685 21.387   1.00 76.05  ? 94   LEU   B CB   1 
ATOM   10315 C  CG   . LEU   B  2  90  ? 30.314  -14.794 20.904   1.00 80.46  ? 94   LEU   B CG   1 
ATOM   10316 C  CD1  . LEU   B  2  90  ? 31.247  -15.260 22.017   1.00 83.54  ? 94   LEU   B CD1  1 
ATOM   10317 C  CD2  . LEU   B  2  90  ? 30.406  -15.726 19.705   1.00 78.62  ? 94   LEU   B CD2  1 
ATOM   10318 H  H    . LEU   B  2  90  ? 26.695  -13.351 22.169   1.00 88.61  ? 94   LEU   B H    1 
ATOM   10319 H  HA   . LEU   B  2  90  ? 29.128  -13.901 23.264   1.00 88.23  ? 94   LEU   B HA   1 
ATOM   10320 H  HB2  . LEU   B  2  90  ? 28.609  -15.555 21.729   1.00 91.24  ? 94   LEU   B HB2  1 
ATOM   10321 H  HB3  . LEU   B  2  90  ? 28.321  -14.455 20.619   1.00 91.24  ? 94   LEU   B HB3  1 
ATOM   10322 H  HG   . LEU   B  2  90  ? 30.611  -13.912 20.631   1.00 96.53  ? 94   LEU   B HG   1 
ATOM   10323 H  HD11 . LEU   B  2  90  ? 32.165  -15.181 21.714   1.00 100.23 ? 94   LEU   B HD11 1 
ATOM   10324 H  HD12 . LEU   B  2  90  ? 31.107  -14.704 22.799   1.00 100.23 ? 94   LEU   B HD12 1 
ATOM   10325 H  HD13 . LEU   B  2  90  ? 31.047  -16.185 22.229   1.00 100.23 ? 94   LEU   B HD13 1 
ATOM   10326 H  HD21 . LEU   B  2  90  ? 31.335  -15.810 19.441   1.00 94.33  ? 94   LEU   B HD21 1 
ATOM   10327 H  HD22 . LEU   B  2  90  ? 30.053  -16.595 19.953   1.00 94.33  ? 94   LEU   B HD22 1 
ATOM   10328 H  HD23 . LEU   B  2  90  ? 29.886  -15.354 18.976   1.00 94.33  ? 94   LEU   B HD23 1 
ATOM   10329 N  N    . LYS   B  2  91  ? 29.764  -11.559 22.938   1.00 77.17  ? 95   LYS   B N    1 
ATOM   10330 C  CA   . LYS   B  2  91  ? 30.386  -10.277 22.622   1.00 82.03  ? 95   LYS   B CA   1 
ATOM   10331 C  C    . LYS   B  2  91  ? 31.771  -10.560 22.055   1.00 82.50  ? 95   LYS   B C    1 
ATOM   10332 O  O    . LYS   B  2  91  ? 32.641  -11.078 22.762   1.00 85.08  ? 95   LYS   B O    1 
ATOM   10333 C  CB   . LYS   B  2  91  ? 30.468  -9.393  23.864   1.00 85.81  ? 95   LYS   B CB   1 
ATOM   10334 C  CG   . LYS   B  2  91  ? 29.198  -8.611  24.159   1.00 89.16  ? 95   LYS   B CG   1 
ATOM   10335 C  CD   . LYS   B  2  91  ? 29.223  -8.025  25.563   1.00 94.30  ? 95   LYS   B CD   1 
ATOM   10336 C  CE   . LYS   B  2  91  ? 27.828  -7.960  26.162   1.00 96.88  ? 95   LYS   B CE   1 
ATOM   10337 N  NZ   . LYS   B  2  91  ? 27.862  -7.661  27.621   1.00 100.67 ? 95   LYS   B NZ   1 
ATOM   10338 H  H    . LYS   B  2  91  ? 29.896  -11.813 23.748   1.00 92.59  ? 95   LYS   B H    1 
ATOM   10339 H  HA   . LYS   B  2  91  ? 29.858  -9.808  21.957   1.00 98.41  ? 95   LYS   B HA   1 
ATOM   10340 H  HB2  . LYS   B  2  91  ? 30.652  -9.956  24.632   1.00 102.95 ? 95   LYS   B HB2  1 
ATOM   10341 H  HB3  . LYS   B  2  91  ? 31.186  -8.753  23.741   1.00 102.95 ? 95   LYS   B HB3  1 
ATOM   10342 H  HG2  . LYS   B  2  91  ? 29.114  -7.882  23.524   1.00 106.97 ? 95   LYS   B HG2  1 
ATOM   10343 H  HG3  . LYS   B  2  91  ? 28.432  -9.202  24.088   1.00 106.97 ? 95   LYS   B HG3  1 
ATOM   10344 H  HD2  . LYS   B  2  91  ? 29.775  -8.581  26.134   1.00 113.14 ? 95   LYS   B HD2  1 
ATOM   10345 H  HD3  . LYS   B  2  91  ? 29.582  -7.124  25.529   1.00 113.14 ? 95   LYS   B HD3  1 
ATOM   10346 H  HE2  . LYS   B  2  91  ? 27.322  -7.260  25.721   1.00 116.23 ? 95   LYS   B HE2  1 
ATOM   10347 H  HE3  . LYS   B  2  91  ? 27.387  -8.816  26.038   1.00 116.23 ? 95   LYS   B HE3  1 
ATOM   10348 H  HZ1  . LYS   B  2  91  ? 27.042  -7.716  27.963   1.00 120.79 ? 95   LYS   B HZ1  1 
ATOM   10349 H  HZ2  . LYS   B  2  91  ? 28.389  -8.244  28.039   1.00 120.79 ? 95   LYS   B HZ2  1 
ATOM   10350 H  HZ3  . LYS   B  2  91  ? 28.176  -6.839  27.756   1.00 120.79 ? 95   LYS   B HZ3  1 
ATOM   10351 N  N    . LEU   B  2  92  ? 31.977  -10.227 20.784   1.00 81.64  ? 96   LEU   B N    1 
ATOM   10352 C  CA   . LEU   B  2  92  ? 33.205  -10.564 20.080   1.00 81.33  ? 96   LEU   B CA   1 
ATOM   10353 C  C    . LEU   B  2  92  ? 33.976  -9.307  19.711   1.00 85.78  ? 96   LEU   B C    1 
ATOM   10354 O  O    . LEU   B  2  92  ? 33.428  -8.392  19.087   1.00 87.75  ? 96   LEU   B O    1 
ATOM   10355 C  CB   . LEU   B  2  92  ? 32.915  -11.370 18.811   1.00 78.02  ? 96   LEU   B CB   1 
ATOM   10356 C  CG   . LEU   B  2  92  ? 32.899  -12.895 18.933   1.00 76.83  ? 96   LEU   B CG   1 
ATOM   10357 C  CD1  . LEU   B  2  92  ? 32.552  -13.507 17.580   1.00 74.96  ? 96   LEU   B CD1  1 
ATOM   10358 C  CD2  . LEU   B  2  92  ? 34.220  -13.461 19.455   1.00 78.60  ? 96   LEU   B CD2  1 
ATOM   10359 H  H    . LEU   B  2  92  ? 31.408  -9.798  20.303   1.00 97.95  ? 96   LEU   B H    1 
ATOM   10360 H  HA   . LEU   B  2  92  ? 33.756  -11.095 20.675   1.00 97.58  ? 96   LEU   B HA   1 
ATOM   10361 H  HB2  . LEU   B  2  92  ? 32.042  -11.104 18.483   1.00 93.60  ? 96   LEU   B HB2  1 
ATOM   10362 H  HB3  . LEU   B  2  92  ? 33.596  -11.148 18.156   1.00 93.60  ? 96   LEU   B HB3  1 
ATOM   10363 H  HG   . LEU   B  2  92  ? 32.224  -13.140 19.586   1.00 92.18  ? 96   LEU   B HG   1 
ATOM   10364 H  HD11 . LEU   B  2  92  ? 32.106  -14.356 17.722   1.00 89.93  ? 96   LEU   B HD11 1 
ATOM   10365 H  HD12 . LEU   B  2  92  ? 31.965  -12.901 17.101   1.00 89.93  ? 96   LEU   B HD12 1 
ATOM   10366 H  HD13 . LEU   B  2  92  ? 33.370  -13.643 17.076   1.00 89.93  ? 96   LEU   B HD13 1 
ATOM   10367 H  HD21 . LEU   B  2  92  ? 34.035  -14.237 20.007   1.00 94.30  ? 96   LEU   B HD21 1 
ATOM   10368 H  HD22 . LEU   B  2  92  ? 34.774  -13.717 18.701   1.00 94.30  ? 96   LEU   B HD22 1 
ATOM   10369 H  HD23 . LEU   B  2  92  ? 34.670  -12.781 19.980   1.00 94.30  ? 96   LEU   B HD23 1 
ATOM   10370 N  N    . ARG   B  2  93  ? 35.236  -9.276  20.092   1.00 86.59  ? 97   ARG   B N    1 
ATOM   10371 C  CA   . ARG   B  2  93  ? 36.166  -8.293  19.563   1.00 87.38  ? 97   ARG   B CA   1 
ATOM   10372 C  C    . ARG   B  2  93  ? 36.555  -8.686  18.138   1.00 93.81  ? 97   ARG   B C    1 
ATOM   10373 O  O    . ARG   B  2  93  ? 36.730  -9.873  17.853   1.00 94.61  ? 97   ARG   B O    1 
ATOM   10374 C  CB   . ARG   B  2  93  ? 37.409  -8.218  20.443   1.00 82.28  ? 97   ARG   B CB   1 
ATOM   10375 C  CG   . ARG   B  2  93  ? 38.326  -7.047  20.160   1.00 83.32  ? 97   ARG   B CG   1 
ATOM   10376 C  CD   . ARG   B  2  93  ? 39.630  -7.201  20.930   1.00 84.62  ? 97   ARG   B CD   1 
ATOM   10377 N  NE   . ARG   B  2  93  ? 40.704  -6.382  20.371   1.00 88.39  ? 97   ARG   B NE   1 
ATOM   10378 C  CZ   . ARG   B  2  93  ? 41.392  -5.456  21.038   1.00 96.43  ? 97   ARG   B CZ   1 
ATOM   10379 N  NH1  . ARG   B  2  93  ? 41.151  -5.206  22.320   1.00 99.65  ? 97   ARG   B NH1  1 
ATOM   10380 N  NH2  . ARG   B  2  93  ? 42.345  -4.780  20.413   1.00 103.18 ? 97   ARG   B NH2  1 
ATOM   10381 H  H    . ARG   B  2  93  ? 35.586  -9.816  20.662   1.00 103.89 ? 97   ARG   B H    1 
ATOM   10382 H  HA   . ARG   B  2  93  ? 35.758  -7.413  19.544   1.00 104.84 ? 97   ARG   B HA   1 
ATOM   10383 H  HB2  . ARG   B  2  93  ? 37.126  -8.149  21.369   1.00 98.71  ? 97   ARG   B HB2  1 
ATOM   10384 H  HB3  . ARG   B  2  93  ? 37.925  -9.029  20.314   1.00 98.71  ? 97   ARG   B HB3  1 
ATOM   10385 H  HG2  . ARG   B  2  93  ? 38.528  -7.012  19.212   1.00 99.96  ? 97   ARG   B HG2  1 
ATOM   10386 H  HG3  . ARG   B  2  93  ? 37.897  -6.222  20.438   1.00 99.96  ? 97   ARG   B HG3  1 
ATOM   10387 H  HD2  . ARG   B  2  93  ? 39.490  -6.928  21.850   1.00 101.53 ? 97   ARG   B HD2  1 
ATOM   10388 H  HD3  . ARG   B  2  93  ? 39.910  -8.129  20.898   1.00 101.53 ? 97   ARG   B HD3  1 
ATOM   10389 H  HE   . ARG   B  2  93  ? 40.908  -6.508  19.545   1.00 106.05 ? 97   ARG   B HE   1 
ATOM   10390 H  HH11 . ARG   B  2  93  ? 40.540  -5.646  22.736   1.00 119.56 ? 97   ARG   B HH11 1 
ATOM   10391 H  HH12 . ARG   B  2  93  ? 41.606  -4.605  22.733   1.00 119.56 ? 97   ARG   B HH12 1 
ATOM   10392 H  HH21 . ARG   B  2  93  ? 42.514  -4.941  19.585   1.00 123.79 ? 97   ARG   B HH21 1 
ATOM   10393 H  HH22 . ARG   B  2  93  ? 42.794  -4.181  20.835   1.00 123.79 ? 97   ARG   B HH22 1 
ATOM   10394 N  N    . PRO   B  2  94  ? 36.681  -7.727  17.222   1.00 97.87  ? 98   PRO   B N    1 
ATOM   10395 C  CA   . PRO   B  2  94  ? 37.044  -8.085  15.844   1.00 96.69  ? 98   PRO   B CA   1 
ATOM   10396 C  C    . PRO   B  2  94  ? 38.356  -8.855  15.797   1.00 97.23  ? 98   PRO   B C    1 
ATOM   10397 O  O    . PRO   B  2  94  ? 39.348  -8.470  16.421   1.00 98.20  ? 98   PRO   B O    1 
ATOM   10398 C  CB   . PRO   B  2  94  ? 37.152  -6.728  15.135   1.00 100.19 ? 98   PRO   B CB   1 
ATOM   10399 C  CG   . PRO   B  2  94  ? 37.247  -5.712  16.228   1.00 103.87 ? 98   PRO   B CG   1 
ATOM   10400 C  CD   . PRO   B  2  94  ? 36.477  -6.277  17.376   1.00 102.24 ? 98   PRO   B CD   1 
ATOM   10401 H  HA   . PRO   B  2  94  ? 36.342  -8.613  15.432   1.00 116.01 ? 98   PRO   B HA   1 
ATOM   10402 H  HB2  . PRO   B  2  94  ? 37.945  -6.711  14.578   1.00 120.21 ? 98   PRO   B HB2  1 
ATOM   10403 H  HB3  . PRO   B  2  94  ? 36.361  -6.578  14.593   1.00 120.21 ? 98   PRO   B HB3  1 
ATOM   10404 H  HG2  . PRO   B  2  94  ? 38.177  -5.578  16.470   1.00 124.63 ? 98   PRO   B HG2  1 
ATOM   10405 H  HG3  . PRO   B  2  94  ? 36.858  -4.874  15.931   1.00 124.63 ? 98   PRO   B HG3  1 
ATOM   10406 H  HD2  . PRO   B  2  94  ? 36.834  -5.964  18.221   1.00 122.67 ? 98   PRO   B HD2  1 
ATOM   10407 H  HD3  . PRO   B  2  94  ? 35.536  -6.050  17.308   1.00 122.67 ? 98   PRO   B HD3  1 
ATOM   10408 N  N    . GLY   B  2  95  ? 38.351  -9.958  15.050   1.00 95.57  ? 99   GLY   B N    1 
ATOM   10409 C  CA   . GLY   B  2  95  ? 39.517  -10.806 14.932   1.00 94.52  ? 99   GLY   B CA   1 
ATOM   10410 C  C    . GLY   B  2  95  ? 39.753  -11.735 16.101   1.00 90.21  ? 99   GLY   B C    1 
ATOM   10411 O  O    . GLY   B  2  95  ? 40.685  -12.547 16.044   1.00 87.54  ? 99   GLY   B O    1 
ATOM   10412 H  H    . GLY   B  2  95  ? 37.673  -10.234 14.600   1.00 114.67 ? 99   GLY   B H    1 
ATOM   10413 H  HA2  . GLY   B  2  95  ? 39.425  -11.351 14.135   1.00 113.41 ? 99   GLY   B HA2  1 
ATOM   10414 H  HA3  . GLY   B  2  95  ? 40.301  -10.242 14.840   1.00 113.41 ? 99   GLY   B HA3  1 
ATOM   10415 N  N    . GLY   B  2  96  ? 38.944  -11.650 17.151   1.00 88.58  ? 100  GLY   B N    1 
ATOM   10416 C  CA   . GLY   B  2  96  ? 39.068  -12.529 18.301   1.00 87.84  ? 100  GLY   B CA   1 
ATOM   10417 C  C    . GLY   B  2  96  ? 38.051  -13.654 18.214   1.00 86.40  ? 100  GLY   B C    1 
ATOM   10418 O  O    . GLY   B  2  96  ? 36.920  -13.449 17.772   1.00 91.97  ? 100  GLY   B O    1 
ATOM   10419 H  H    . GLY   B  2  96  ? 38.304  -11.079 17.220   1.00 106.27 ? 100  GLY   B H    1 
ATOM   10420 H  HA2  . GLY   B  2  96  ? 39.958  -12.912 18.328   1.00 105.39 ? 100  GLY   B HA2  1 
ATOM   10421 H  HA3  . GLY   B  2  96  ? 38.914  -12.028 19.117   1.00 105.39 ? 100  GLY   B HA3  1 
ATOM   10422 N  N    . ALA   B  2  97  ? 38.468  -14.843 18.631   1.00 78.18  ? 101  ALA   B N    1 
ATOM   10423 C  CA   . ALA   B  2  97  ? 37.627  -16.028 18.572   1.00 73.88  ? 101  ALA   B CA   1 
ATOM   10424 C  C    . ALA   B  2  97  ? 37.261  -16.478 19.978   1.00 68.99  ? 101  ALA   B C    1 
ATOM   10425 O  O    . ALA   B  2  97  ? 38.072  -16.381 20.905   1.00 68.71  ? 101  ALA   B O    1 
ATOM   10426 C  CB   . ALA   B  2  97  ? 38.328  -17.166 17.829   1.00 75.06  ? 101  ALA   B CB   1 
ATOM   10427 H  H    . ALA   B  2  97  ? 39.250  -14.990 18.958   1.00 93.79  ? 101  ALA   B H    1 
ATOM   10428 H  HA   . ALA   B  2  97  ? 36.807  -15.815 18.099   1.00 88.64  ? 101  ALA   B HA   1 
ATOM   10429 H  HB1  . ALA   B  2  97  ? 37.688  -17.876 17.663   1.00 90.05  ? 101  ALA   B HB1  1 
ATOM   10430 H  HB2  . ALA   B  2  97  ? 38.674  -16.829 16.988   1.00 90.05  ? 101  ALA   B HB2  1 
ATOM   10431 H  HB3  . ALA   B  2  97  ? 39.057  -17.499 18.376   1.00 90.05  ? 101  ALA   B HB3  1 
ATOM   10432 N  N    . GLN   B  2  98  ? 36.032  -16.962 20.130   1.00 64.54  ? 102  GLN   B N    1 
ATOM   10433 C  CA   . GLN   B  2  98  ? 35.557  -17.536 21.379   1.00 66.19  ? 102  GLN   B CA   1 
ATOM   10434 C  C    . GLN   B  2  98  ? 35.022  -18.929 21.094   1.00 65.12  ? 102  GLN   B C    1 
ATOM   10435 O  O    . GLN   B  2  98  ? 34.371  -19.154 20.069   1.00 63.62  ? 102  GLN   B O    1 
ATOM   10436 C  CB   . GLN   B  2  98  ? 34.469  -16.667 22.014   1.00 69.19  ? 102  GLN   B CB   1 
ATOM   10437 C  CG   . GLN   B  2  98  ? 34.624  -16.477 23.513   1.00 70.71  ? 102  GLN   B CG   1 
ATOM   10438 C  CD   . GLN   B  2  98  ? 35.884  -15.720 23.872   1.00 71.95  ? 102  GLN   B CD   1 
ATOM   10439 O  OE1  . GLN   B  2  98  ? 36.659  -15.332 22.998   1.00 74.15  ? 102  GLN   B OE1  1 
ATOM   10440 N  NE2  . GLN   B  2  98  ? 36.098  -15.507 25.163   1.00 73.10  ? 102  GLN   B NE2  1 
ATOM   10441 H  H    . GLN   B  2  98  ? 35.441  -16.968 19.505   1.00 77.43  ? 102  GLN   B H    1 
ATOM   10442 H  HA   . GLN   B  2  98  ? 36.285  -17.605 22.016   1.00 79.41  ? 102  GLN   B HA   1 
ATOM   10443 H  HB2  . GLN   B  2  98  ? 34.492  -15.789 21.602   1.00 83.01  ? 102  GLN   B HB2  1 
ATOM   10444 H  HB3  . GLN   B  2  98  ? 33.608  -17.085 21.858   1.00 83.01  ? 102  GLN   B HB3  1 
ATOM   10445 H  HG2  . GLN   B  2  98  ? 33.865  -15.975 23.849   1.00 84.83  ? 102  GLN   B HG2  1 
ATOM   10446 H  HG3  . GLN   B  2  98  ? 34.663  -17.347 23.941   1.00 84.83  ? 102  GLN   B HG3  1 
ATOM   10447 H  HE21 . GLN   B  2  98  ? 35.534  -15.795 25.745   1.00 87.70  ? 102  GLN   B HE21 1 
ATOM   10448 H  HE22 . GLN   B  2  98  ? 36.800  -15.081 25.418   1.00 87.70  ? 102  GLN   B HE22 1 
ATOM   10449 N  N    . THR   B  2  99  ? 35.303  -19.863 21.999   1.00 64.93  ? 103  THR   B N    1 
ATOM   10450 C  CA   . THR   B  2  99  ? 34.922  -21.262 21.835   1.00 62.88  ? 103  THR   B CA   1 
ATOM   10451 C  C    . THR   B  2  99  ? 33.767  -21.568 22.781   1.00 62.57  ? 103  THR   B C    1 
ATOM   10452 O  O    . THR   B  2  99  ? 33.931  -21.525 24.005   1.00 63.19  ? 103  THR   B O    1 
ATOM   10453 C  CB   . THR   B  2  99  ? 36.106  -22.189 22.102   1.00 62.62  ? 103  THR   B CB   1 
ATOM   10454 O  OG1  . THR   B  2  99  ? 37.190  -21.850 21.229   1.00 63.81  ? 103  THR   B OG1  1 
ATOM   10455 C  CG2  . THR   B  2  99  ? 35.712  -23.643 21.867   1.00 60.16  ? 103  THR   B CG2  1 
ATOM   10456 H  H    . THR   B  2  99  ? 35.723  -19.706 22.733   1.00 77.89  ? 103  THR   B H    1 
ATOM   10457 H  HA   . THR   B  2  99  ? 34.619  -21.403 20.925   1.00 75.44  ? 103  THR   B HA   1 
ATOM   10458 H  HB   . THR   B  2  99  ? 36.389  -22.092 23.025   1.00 75.12  ? 103  THR   B HB   1 
ATOM   10459 H  HG1  . THR   B  2  99  ? 36.982  -22.022 20.433   1.00 76.56  ? 103  THR   B HG1  1 
ATOM   10460 H  HG21 . THR   B  2  99  ? 36.487  -24.218 21.969   1.00 72.17  ? 103  THR   B HG21 1 
ATOM   10461 H  HG22 . THR   B  2  99  ? 35.034  -23.911 22.507   1.00 72.17  ? 103  THR   B HG22 1 
ATOM   10462 H  HG23 . THR   B  2  99  ? 35.358  -23.749 20.970   1.00 72.17  ? 103  THR   B HG23 1 
ATOM   10463 N  N    . LEU   B  2  100 ? 32.607  -21.877 22.211   1.00 63.70  ? 104  LEU   B N    1 
ATOM   10464 C  CA   . LEU   B  2  100 ? 31.432  -22.248 22.984   1.00 66.07  ? 104  LEU   B CA   1 
ATOM   10465 C  C    . LEU   B  2  100 ? 31.368  -23.760 23.145   1.00 67.74  ? 104  LEU   B C    1 
ATOM   10466 O  O    . LEU   B  2  100 ? 31.690  -24.510 22.218   1.00 68.00  ? 104  LEU   B O    1 
ATOM   10467 C  CB   . LEU   B  2  100 ? 30.157  -21.752 22.300   1.00 66.46  ? 104  LEU   B CB   1 
ATOM   10468 C  CG   . LEU   B  2  100 ? 30.139  -20.296 21.835   1.00 69.32  ? 104  LEU   B CG   1 
ATOM   10469 C  CD1  . LEU   B  2  100 ? 28.919  -20.051 20.961   1.00 66.02  ? 104  LEU   B CD1  1 
ATOM   10470 C  CD2  . LEU   B  2  100 ? 30.153  -19.346 23.019   1.00 75.18  ? 104  LEU   B CD2  1 
ATOM   10471 H  H    . LEU   B  2  100 ? 32.474  -21.880 21.361   1.00 76.42  ? 104  LEU   B H    1 
ATOM   10472 H  HA   . LEU   B  2  100 ? 31.485  -21.842 23.864   1.00 79.27  ? 104  LEU   B HA   1 
ATOM   10473 H  HB2  . LEU   B  2  100 ? 30.007  -22.302 21.515   1.00 79.73  ? 104  LEU   B HB2  1 
ATOM   10474 H  HB3  . LEU   B  2  100 ? 29.423  -21.859 22.925   1.00 79.73  ? 104  LEU   B HB3  1 
ATOM   10475 H  HG   . LEU   B  2  100 ? 30.936  -20.118 21.312   1.00 83.16  ? 104  LEU   B HG   1 
ATOM   10476 H  HD11 . LEU   B  2  100 ? 28.921  -19.126 20.668   1.00 79.20  ? 104  LEU   B HD11 1 
ATOM   10477 H  HD12 . LEU   B  2  100 ? 28.957  -20.641 20.192   1.00 79.20  ? 104  LEU   B HD12 1 
ATOM   10478 H  HD13 . LEU   B  2  100 ? 28.119  -20.233 21.478   1.00 79.20  ? 104  LEU   B HD13 1 
ATOM   10479 H  HD21 . LEU   B  2  100 ? 30.131  -18.433 22.692   1.00 90.19  ? 104  LEU   B HD21 1 
ATOM   10480 H  HD22 . LEU   B  2  100 ? 29.375  -19.518 23.572   1.00 90.19  ? 104  LEU   B HD22 1 
ATOM   10481 H  HD23 . LEU   B  2  100 ? 30.963  -19.493 23.533   1.00 90.19  ? 104  LEU   B HD23 1 
ATOM   10482 N  N    . GLN   B  2  101 ? 30.949  -24.204 24.325   1.00 69.48  ? 105  GLN   B N    1 
ATOM   10483 C  CA   . GLN   B  2  101 ? 30.739  -25.620 24.600   1.00 72.96  ? 105  GLN   B CA   1 
ATOM   10484 C  C    . GLN   B  2  101 ? 29.247  -25.917 24.511   1.00 70.21  ? 105  GLN   B C    1 
ATOM   10485 O  O    . GLN   B  2  101 ? 28.448  -25.331 25.251   1.00 70.28  ? 105  GLN   B O    1 
ATOM   10486 C  CB   . GLN   B  2  101 ? 31.288  -26.000 25.974   1.00 81.59  ? 105  GLN   B CB   1 
ATOM   10487 C  CG   . GLN   B  2  101 ? 32.807  -25.939 26.070   1.00 88.78  ? 105  GLN   B CG   1 
ATOM   10488 C  CD   . GLN   B  2  101 ? 33.495  -26.909 25.127   1.00 95.09  ? 105  GLN   B CD   1 
ATOM   10489 O  OE1  . GLN   B  2  101 ? 34.397  -26.530 24.380   1.00 98.97  ? 105  GLN   B OE1  1 
ATOM   10490 N  NE2  . GLN   B  2  101 ? 33.076  -28.168 25.163   1.00 96.34  ? 105  GLN   B NE2  1 
ATOM   10491 H  H    . GLN   B  2  101 ? 30.777  -23.694 24.996   1.00 83.36  ? 105  GLN   B H    1 
ATOM   10492 H  HA   . GLN   B  2  101 ? 31.201  -26.154 23.935   1.00 87.53  ? 105  GLN   B HA   1 
ATOM   10493 H  HB2  . GLN   B  2  101 ? 30.925  -25.389 26.634   1.00 97.88  ? 105  GLN   B HB2  1 
ATOM   10494 H  HB3  . GLN   B  2  101 ? 31.016  -26.909 26.177   1.00 97.88  ? 105  GLN   B HB3  1 
ATOM   10495 H  HG2  . GLN   B  2  101 ? 33.102  -25.043 25.846   1.00 106.51 ? 105  GLN   B HG2  1 
ATOM   10496 H  HG3  . GLN   B  2  101 ? 33.076  -26.160 26.975   1.00 106.51 ? 105  GLN   B HG3  1 
ATOM   10497 H  HE21 . GLN   B  2  101 ? 32.446  -28.396 25.702   1.00 115.59 ? 105  GLN   B HE21 1 
ATOM   10498 H  HE22 . GLN   B  2  101 ? 33.435  -28.756 24.647   1.00 115.59 ? 105  GLN   B HE22 1 
ATOM   10499 N  N    . VAL   B  2  102 ? 28.878  -26.819 23.606   1.00 67.45  ? 106  VAL   B N    1 
ATOM   10500 C  CA   . VAL   B  2  102 ? 27.489  -27.189 23.367   1.00 66.03  ? 106  VAL   B CA   1 
ATOM   10501 C  C    . VAL   B  2  102 ? 27.349  -28.683 23.620   1.00 66.82  ? 106  VAL   B C    1 
ATOM   10502 O  O    . VAL   B  2  102 ? 28.119  -29.484 23.078   1.00 69.08  ? 106  VAL   B O    1 
ATOM   10503 C  CB   . VAL   B  2  102 ? 27.044  -26.831 21.937   1.00 65.26  ? 106  VAL   B CB   1 
ATOM   10504 C  CG1  . VAL   B  2  102 ? 25.575  -27.172 21.730   1.00 65.07  ? 106  VAL   B CG1  1 
ATOM   10505 C  CG2  . VAL   B  2  102 ? 27.299  -25.357 21.656   1.00 67.80  ? 106  VAL   B CG2  1 
ATOM   10506 H  H    . VAL   B  2  102 ? 29.433  -27.241 23.103   1.00 80.92  ? 106  VAL   B H    1 
ATOM   10507 H  HA   . VAL   B  2  102 ? 26.915  -26.717 23.990   1.00 79.21  ? 106  VAL   B HA   1 
ATOM   10508 H  HB   . VAL   B  2  102 ? 27.564  -27.354 21.306   1.00 78.29  ? 106  VAL   B HB   1 
ATOM   10509 H  HG11 . VAL   B  2  102 ? 25.308  -26.891 20.841   1.00 78.07  ? 106  VAL   B HG11 1 
ATOM   10510 H  HG12 . VAL   B  2  102 ? 25.457  -28.131 21.823   1.00 78.07  ? 106  VAL   B HG12 1 
ATOM   10511 H  HG13 . VAL   B  2  102 ? 25.046  -26.708 22.397   1.00 78.07  ? 106  VAL   B HG13 1 
ATOM   10512 H  HG21 . VAL   B  2  102 ? 26.982  -25.145 20.765   1.00 81.34  ? 106  VAL   B HG21 1 
ATOM   10513 H  HG22 . VAL   B  2  102 ? 26.824  -24.824 22.312   1.00 81.34  ? 106  VAL   B HG22 1 
ATOM   10514 H  HG23 . VAL   B  2  102 ? 28.252  -25.184 21.718   1.00 81.34  ? 106  VAL   B HG23 1 
ATOM   10515 N  N    . HIS   B  2  103 ? 26.368  -29.052 24.438   1.00 67.57  ? 107  HIS   B N    1 
ATOM   10516 C  CA   . HIS   B  2  103 ? 26.136  -30.436 24.825   1.00 68.86  ? 107  HIS   B CA   1 
ATOM   10517 C  C    . HIS   B  2  103 ? 24.770  -30.872 24.318   1.00 68.71  ? 107  HIS   B C    1 
ATOM   10518 O  O    . HIS   B  2  103 ? 23.779  -30.157 24.502   1.00 66.62  ? 107  HIS   B O    1 
ATOM   10519 C  CB   . HIS   B  2  103 ? 26.218  -30.596 26.344   1.00 70.72  ? 107  HIS   B CB   1 
ATOM   10520 C  CG   . HIS   B  2  103 ? 27.448  -29.989 26.944   1.00 73.03  ? 107  HIS   B CG   1 
ATOM   10521 N  ND1  . HIS   B  2  103 ? 28.616  -30.698 27.124   1.00 72.52  ? 107  HIS   B ND1  1 
ATOM   10522 C  CD2  . HIS   B  2  103 ? 27.694  -28.737 27.397   1.00 73.13  ? 107  HIS   B CD2  1 
ATOM   10523 C  CE1  . HIS   B  2  103 ? 29.528  -29.910 27.665   1.00 73.77  ? 107  HIS   B CE1  1 
ATOM   10524 N  NE2  . HIS   B  2  103 ? 28.993  -28.715 27.842   1.00 73.48  ? 107  HIS   B NE2  1 
ATOM   10525 H  H    . HIS   B  2  103 ? 25.810  -28.501 24.791   1.00 81.07  ? 107  HIS   B H    1 
ATOM   10526 H  HA   . HIS   B  2  103 ? 26.806  -31.009 24.421   1.00 82.61  ? 107  HIS   B HA   1 
ATOM   10527 H  HB2  . HIS   B  2  103 ? 25.448  -30.165 26.746   1.00 84.84  ? 107  HIS   B HB2  1 
ATOM   10528 H  HB3  . HIS   B  2  103 ? 26.219  -31.542 26.559   1.00 84.84  ? 107  HIS   B HB3  1 
ATOM   10529 H  HD2  . HIS   B  2  103 ? 27.095  -28.025 27.405   1.00 87.74  ? 107  HIS   B HD2  1 
ATOM   10530 H  HE1  . HIS   B  2  103 ? 30.397  -30.155 27.885   1.00 88.50  ? 107  HIS   B HE1  1 
ATOM   10531 H  HE2  . HIS   B  2  103 ? 29.394  -28.033 28.181   1.00 88.16  ? 107  HIS   B HE2  1 
ATOM   10532 N  N    . VAL   B  2  104 ? 24.721  -32.040 23.683   1.00 69.63  ? 108  VAL   B N    1 
ATOM   10533 C  CA   . VAL   B  2  104 ? 23.491  -32.580 23.121   1.00 68.11  ? 108  VAL   B CA   1 
ATOM   10534 C  C    . VAL   B  2  104 ? 23.267  -33.976 23.682   1.00 68.35  ? 108  VAL   B C    1 
ATOM   10535 O  O    . VAL   B  2  104 ? 24.215  -34.753 23.846   1.00 66.81  ? 108  VAL   B O    1 
ATOM   10536 C  CB   . VAL   B  2  104 ? 23.533  -32.617 21.579   1.00 67.15  ? 108  VAL   B CB   1 
ATOM   10537 C  CG1  . VAL   B  2  104 ? 22.221  -33.158 21.020   1.00 66.51  ? 108  VAL   B CG1  1 
ATOM   10538 C  CG2  . VAL   B  2  104 ? 23.818  -31.232 21.022   1.00 65.90  ? 108  VAL   B CG2  1 
ATOM   10539 H  H    . VAL   B  2  104 ? 25.405  -32.548 23.564   1.00 83.54  ? 108  VAL   B H    1 
ATOM   10540 H  HA   . VAL   B  2  104 ? 22.748  -32.019 23.393   1.00 81.71  ? 108  VAL   B HA   1 
ATOM   10541 H  HB   . VAL   B  2  104 ? 24.248  -33.210 21.299   1.00 80.56  ? 108  VAL   B HB   1 
ATOM   10542 H  HG11 . VAL   B  2  104 ? 22.241  -33.096 20.052   1.00 79.80  ? 108  VAL   B HG11 1 
ATOM   10543 H  HG12 . VAL   B  2  104 ? 22.122  -34.085 21.290   1.00 79.80  ? 108  VAL   B HG12 1 
ATOM   10544 H  HG13 . VAL   B  2  104 ? 21.487  -32.631 21.370   1.00 79.80  ? 108  VAL   B HG13 1 
ATOM   10545 H  HG21 . VAL   B  2  104 ? 23.805  -31.272 20.053   1.00 79.06  ? 108  VAL   B HG21 1 
ATOM   10546 H  HG22 . VAL   B  2  104 ? 23.135  -30.618 21.337   1.00 79.06  ? 108  VAL   B HG22 1 
ATOM   10547 H  HG23 . VAL   B  2  104 ? 24.691  -30.941 21.330   1.00 79.06  ? 108  VAL   B HG23 1 
ATOM   10548 N  N    . ARG   B  2  105 ? 22.007  -34.290 23.972   1.00 69.04  ? 109  ARG   B N    1 
ATOM   10549 C  CA   . ARG   B  2  105 ? 21.617  -35.605 24.461   1.00 67.65  ? 109  ARG   B CA   1 
ATOM   10550 C  C    . ARG   B  2  105 ? 20.192  -35.866 24.003   1.00 64.74  ? 109  ARG   B C    1 
ATOM   10551 O  O    . ARG   B  2  105 ? 19.309  -35.033 24.226   1.00 62.35  ? 109  ARG   B O    1 
ATOM   10552 C  CB   . ARG   B  2  105 ? 21.712  -35.685 25.988   1.00 71.98  ? 109  ARG   B CB   1 
ATOM   10553 C  CG   . ARG   B  2  105 ? 21.333  -37.041 26.569   1.00 77.41  ? 109  ARG   B CG   1 
ATOM   10554 C  CD   . ARG   B  2  105 ? 21.243  -36.987 28.086   1.00 85.85  ? 109  ARG   B CD   1 
ATOM   10555 N  NE   . ARG   B  2  105 ? 20.817  -38.262 28.656   1.00 94.51  ? 109  ARG   B NE   1 
ATOM   10556 C  CZ   . ARG   B  2  105 ? 19.555  -38.678 28.711   1.00 98.05  ? 109  ARG   B CZ   1 
ATOM   10557 N  NH1  . ARG   B  2  105 ? 18.577  -37.925 28.224   1.00 99.45  ? 109  ARG   B NH1  1 
ATOM   10558 N  NH2  . ARG   B  2  105 ? 19.270  -39.855 29.251   1.00 97.76  ? 109  ARG   B NH2  1 
ATOM   10559 H  H    . ARG   B  2  105 ? 21.347  -33.745 23.892   1.00 82.83  ? 109  ARG   B H    1 
ATOM   10560 H  HA   . ARG   B  2  105 ? 22.201  -36.286 24.091   1.00 81.16  ? 109  ARG   B HA   1 
ATOM   10561 H  HB2  . ARG   B  2  105 ? 22.627  -35.498 26.251   1.00 86.35  ? 109  ARG   B HB2  1 
ATOM   10562 H  HB3  . ARG   B  2  105 ? 21.115  -35.024 26.371   1.00 86.35  ? 109  ARG   B HB3  1 
ATOM   10563 H  HG2  . ARG   B  2  105 ? 20.468  -37.310 26.221   1.00 92.87  ? 109  ARG   B HG2  1 
ATOM   10564 H  HG3  . ARG   B  2  105 ? 22.007  -37.695 26.326   1.00 92.87  ? 109  ARG   B HG3  1 
ATOM   10565 H  HD2  . ARG   B  2  105 ? 22.115  -36.769 28.449   1.00 103.00 ? 109  ARG   B HD2  1 
ATOM   10566 H  HD3  . ARG   B  2  105 ? 20.598  -36.310 28.343   1.00 103.00 ? 109  ARG   B HD3  1 
ATOM   10567 H  HE   . ARG   B  2  105 ? 21.424  -38.780 28.977   1.00 113.40 ? 109  ARG   B HE   1 
ATOM   10568 H  HH11 . ARG   B  2  105 ? 18.758  -37.163 27.869   1.00 119.32 ? 109  ARG   B HH11 1 
ATOM   10569 H  HH12 . ARG   B  2  105 ? 17.763  -38.200 28.263   1.00 119.32 ? 109  ARG   B HH12 1 
ATOM   10570 H  HH21 . ARG   B  2  105 ? 19.901  -40.348 29.564   1.00 117.29 ? 109  ARG   B HH21 1 
ATOM   10571 H  HH22 . ARG   B  2  105 ? 18.455  -40.125 29.287   1.00 117.29 ? 109  ARG   B HH22 1 
ATOM   10572 N  N    . GLN   B  2  106 ? 19.972  -37.009 23.362   1.00 67.53  ? 110  GLN   B N    1 
ATOM   10573 C  CA   . GLN   B  2  106 ? 18.650  -37.368 22.869   1.00 68.11  ? 110  GLN   B CA   1 
ATOM   10574 C  C    . GLN   B  2  106 ? 17.863  -38.061 23.973   1.00 66.97  ? 110  GLN   B C    1 
ATOM   10575 O  O    . GLN   B  2  106 ? 18.366  -38.988 24.616   1.00 69.08  ? 110  GLN   B O    1 
ATOM   10576 C  CB   . GLN   B  2  106 ? 18.753  -38.272 21.641   1.00 69.24  ? 110  GLN   B CB   1 
ATOM   10577 C  CG   . GLN   B  2  106 ? 19.362  -37.588 20.428   1.00 69.81  ? 110  GLN   B CG   1 
ATOM   10578 C  CD   . GLN   B  2  106 ? 19.118  -38.353 19.141   1.00 70.95  ? 110  GLN   B CD   1 
ATOM   10579 O  OE1  . GLN   B  2  106 ? 20.056  -38.818 18.494   1.00 69.77  ? 110  GLN   B OE1  1 
ATOM   10580 N  NE2  . GLN   B  2  106 ? 17.852  -38.478 18.759   1.00 70.97  ? 110  GLN   B NE2  1 
ATOM   10581 H  H    . GLN   B  2  106 ? 20.578  -37.598 23.200   1.00 81.01  ? 110  GLN   B H    1 
ATOM   10582 H  HA   . GLN   B  2  106 ? 18.173  -36.564 22.609   1.00 81.71  ? 110  GLN   B HA   1 
ATOM   10583 H  HB2  . GLN   B  2  106 ? 19.309  -39.035 21.861   1.00 83.07  ? 110  GLN   B HB2  1 
ATOM   10584 H  HB3  . GLN   B  2  106 ? 17.862  -38.569 21.397   1.00 83.07  ? 110  GLN   B HB3  1 
ATOM   10585 H  HG2  . GLN   B  2  106 ? 18.970  -36.706 20.332   1.00 83.75  ? 110  GLN   B HG2  1 
ATOM   10586 H  HG3  . GLN   B  2  106 ? 20.320  -37.513 20.555   1.00 83.75  ? 110  GLN   B HG3  1 
ATOM   10587 H  HE21 . GLN   B  2  106 ? 17.224  -38.134 19.234   1.00 85.14  ? 110  GLN   B HE21 1 
ATOM   10588 H  HE22 . GLN   B  2  106 ? 17.662  -38.903 18.036   1.00 85.14  ? 110  GLN   B HE22 1 
ATOM   10589 N  N    . THR   B  2  107 ? 16.634  -37.604 24.192   1.00 63.31  ? 111  THR   B N    1 
ATOM   10590 C  CA   . THR   B  2  107 ? 15.790  -38.187 25.222   1.00 66.49  ? 111  THR   B CA   1 
ATOM   10591 C  C    . THR   B  2  107 ? 15.343  -39.589 24.816   1.00 66.48  ? 111  THR   B C    1 
ATOM   10592 O  O    . THR   B  2  107 ? 15.273  -39.931 23.631   1.00 65.16  ? 111  THR   B O    1 
ATOM   10593 C  CB   . THR   B  2  107 ? 14.574  -37.296 25.487   1.00 71.15  ? 111  THR   B CB   1 
ATOM   10594 O  OG1  . THR   B  2  107 ? 13.783  -37.861 26.540   1.00 80.02  ? 111  THR   B OG1  1 
ATOM   10595 C  CG2  . THR   B  2  107 ? 13.719  -37.150 24.234   1.00 69.41  ? 111  THR   B CG2  1 
ATOM   10596 H  H    . THR   B  2  107 ? 16.268  -36.958 23.757   1.00 75.95  ? 111  THR   B H    1 
ATOM   10597 H  HA   . THR   B  2  107 ? 16.291  -38.259 26.050   1.00 79.77  ? 111  THR   B HA   1 
ATOM   10598 H  HB   . THR   B  2  107 ? 14.879  -36.413 25.748   1.00 85.36  ? 111  THR   B HB   1 
ATOM   10599 H  HG1  . THR   B  2  107 ? 13.120  -37.370 26.696   1.00 96.00  ? 111  THR   B HG1  1 
ATOM   10600 H  HG21 . THR   B  2  107 ? 12.970  -36.560 24.411   1.00 83.27  ? 111  THR   B HG21 1 
ATOM   10601 H  HG22 . THR   B  2  107 ? 14.249  -36.778 23.512   1.00 83.27  ? 111  THR   B HG22 1 
ATOM   10602 H  HG23 . THR   B  2  107 ? 13.380  -38.017 23.961   1.00 83.27  ? 111  THR   B HG23 1 
ATOM   10603 N  N    . GLU   B  2  108 ? 15.034  -40.405 25.824   1.00 69.25  ? 112  GLU   B N    1 
ATOM   10604 C  CA   . GLU   B  2  108 ? 14.717  -41.805 25.565   1.00 71.62  ? 112  GLU   B CA   1 
ATOM   10605 C  C    . GLU   B  2  108 ? 13.437  -41.948 24.750   1.00 71.55  ? 112  GLU   B C    1 
ATOM   10606 O  O    . GLU   B  2  108 ? 13.357  -42.802 23.859   1.00 74.13  ? 112  GLU   B O    1 
ATOM   10607 C  CB   . GLU   B  2  108 ? 14.597  -42.569 26.884   1.00 76.45  ? 112  GLU   B CB   1 
ATOM   10608 C  CG   . GLU   B  2  108 ? 15.919  -42.792 27.606   1.00 83.72  ? 112  GLU   B CG   1 
ATOM   10609 C  CD   . GLU   B  2  108 ? 16.468  -41.531 28.242   1.00 90.89  ? 112  GLU   B CD   1 
ATOM   10610 O  OE1  . GLU   B  2  108 ? 15.817  -40.471 28.127   1.00 93.53  ? 112  GLU   B OE1  1 
ATOM   10611 O  OE2  . GLU   B  2  108 ? 17.552  -41.599 28.859   1.00 94.05  ? 112  GLU   B OE2  1 
ATOM   10612 H  H    . GLU   B  2  108 ? 15.002  -40.176 26.652   1.00 83.08  ? 112  GLU   B H    1 
ATOM   10613 H  HA   . GLU   B  2  108 ? 15.443  -42.195 25.054   1.00 85.93  ? 112  GLU   B HA   1 
ATOM   10614 H  HB2  . GLU   B  2  108 ? 14.018  -42.067 27.480   1.00 91.72  ? 112  GLU   B HB2  1 
ATOM   10615 H  HB3  . GLU   B  2  108 ? 14.210  -43.440 26.703   1.00 91.72  ? 112  GLU   B HB3  1 
ATOM   10616 H  HG2  . GLU   B  2  108 ? 15.788  -43.448 28.309   1.00 100.45 ? 112  GLU   B HG2  1 
ATOM   10617 H  HG3  . GLU   B  2  108 ? 16.575  -43.116 26.969   1.00 100.45 ? 112  GLU   B HG3  1 
ATOM   10618 N  N    . ASP   B  2  109 ? 12.426  -41.130 25.039   1.00 70.35  ? 113  ASP   B N    1 
ATOM   10619 C  CA   . ASP   B  2  109 ? 11.140  -41.184 24.349   1.00 68.61  ? 113  ASP   B CA   1 
ATOM   10620 C  C    . ASP   B  2  109 ? 10.910  -39.844 23.662   1.00 64.70  ? 113  ASP   B C    1 
ATOM   10621 O  O    . ASP   B  2  109 ? 10.766  -38.815 24.331   1.00 65.51  ? 113  ASP   B O    1 
ATOM   10622 C  CB   . ASP   B  2  109 ? 10.006  -41.503 25.324   1.00 74.82  ? 113  ASP   B CB   1 
ATOM   10623 C  CG   . ASP   B  2  109 ? 8.743   -41.965 24.619   1.00 76.05  ? 113  ASP   B CG   1 
ATOM   10624 O  OD1  . ASP   B  2  109 ? 8.572   -41.642 23.426   1.00 73.81  ? 113  ASP   B OD1  1 
ATOM   10625 O  OD2  . ASP   B  2  109 ? 7.918   -42.650 25.261   1.00 80.54  ? 113  ASP   B OD2  1 
ATOM   10626 H  H    . ASP   B  2  109 ? 12.463  -40.521 25.646   1.00 84.40  ? 113  ASP   B H    1 
ATOM   10627 H  HA   . ASP   B  2  109 ? 11.166  -41.877 23.672   1.00 82.31  ? 113  ASP   B HA   1 
ATOM   10628 H  HB2  . ASP   B  2  109 ? 10.292  -42.210 25.922   1.00 89.76  ? 113  ASP   B HB2  1 
ATOM   10629 H  HB3  . ASP   B  2  109 ? 9.791   -40.705 25.832   1.00 89.76  ? 113  ASP   B HB3  1 
ATOM   10630 N  N    . TYR   B  2  110 ? 10.875  -39.857 22.327   1.00 62.35  ? 114  TYR   B N    1 
ATOM   10631 C  CA   . TYR   B  2  110 ? 10.695  -38.645 21.547   1.00 61.79  ? 114  TYR   B CA   1 
ATOM   10632 C  C    . TYR   B  2  110 ? 9.709   -38.935 20.420   1.00 64.08  ? 114  TYR   B C    1 
ATOM   10633 O  O    . TYR   B  2  110 ? 9.866   -39.944 19.709   1.00 66.45  ? 114  TYR   B O    1 
ATOM   10634 C  CB   . TYR   B  2  110 ? 12.033  -38.149 20.986   1.00 56.93  ? 114  TYR   B CB   1 
ATOM   10635 C  CG   . TYR   B  2  110 ? 12.025  -36.689 20.594   1.00 53.34  ? 114  TYR   B CG   1 
ATOM   10636 C  CD1  . TYR   B  2  110 ? 11.822  -35.699 21.546   1.00 55.80  ? 114  TYR   B CD1  1 
ATOM   10637 C  CD2  . TYR   B  2  110 ? 12.226  -36.300 19.276   1.00 53.07  ? 114  TYR   B CD2  1 
ATOM   10638 C  CE1  . TYR   B  2  110 ? 11.810  -34.362 21.198   1.00 56.50  ? 114  TYR   B CE1  1 
ATOM   10639 C  CE2  . TYR   B  2  110 ? 12.219  -34.963 18.917   1.00 54.42  ? 114  TYR   B CE2  1 
ATOM   10640 C  CZ   . TYR   B  2  110 ? 12.010  -33.998 19.882   1.00 56.60  ? 114  TYR   B CZ   1 
ATOM   10641 O  OH   . TYR   B  2  110 ? 12.001  -32.667 19.532   1.00 58.15  ? 114  TYR   B OH   1 
ATOM   10642 H  H    . TYR   B  2  110 ? 10.954  -40.569 21.850   1.00 74.80  ? 114  TYR   B H    1 
ATOM   10643 H  HA   . TYR   B  2  110 ? 10.315  -37.953 22.112   1.00 74.13  ? 114  TYR   B HA   1 
ATOM   10644 H  HB2  . TYR   B  2  110 ? 12.719  -38.271 21.661   1.00 68.29  ? 114  TYR   B HB2  1 
ATOM   10645 H  HB3  . TYR   B  2  110 ? 12.250  -38.667 20.195   1.00 68.29  ? 114  TYR   B HB3  1 
ATOM   10646 H  HD1  . TYR   B  2  110 ? 11.693  -35.940 22.435   1.00 66.95  ? 114  TYR   B HD1  1 
ATOM   10647 H  HD2  . TYR   B  2  110 ? 12.366  -36.948 18.624   1.00 63.66  ? 114  TYR   B HD2  1 
ATOM   10648 H  HE1  . TYR   B  2  110 ? 11.668  -33.711 21.847   1.00 67.78  ? 114  TYR   B HE1  1 
ATOM   10649 H  HE2  . TYR   B  2  110 ? 12.355  -34.716 18.031   1.00 65.29  ? 114  TYR   B HE2  1 
ATOM   10650 H  HH   . TYR   B  2  110 ? 12.134  -32.586 18.706   1.00 69.76  ? 114  TYR   B HH   1 
ATOM   10651 N  N    . PRO   B  2  111 ? 8.691   -38.094 20.226   1.00 64.88  ? 115  PRO   B N    1 
ATOM   10652 C  CA   . PRO   B  2  111 ? 7.708   -38.366 19.171   1.00 62.21  ? 115  PRO   B CA   1 
ATOM   10653 C  C    . PRO   B  2  111 ? 8.349   -38.374 17.792   1.00 57.53  ? 115  PRO   B C    1 
ATOM   10654 O  O    . PRO   B  2  111 ? 9.390   -37.760 17.552   1.00 57.18  ? 115  PRO   B O    1 
ATOM   10655 C  CB   . PRO   B  2  111 ? 6.697   -37.220 19.313   1.00 61.31  ? 115  PRO   B CB   1 
ATOM   10656 C  CG   . PRO   B  2  111 ? 7.408   -36.158 20.076   1.00 64.17  ? 115  PRO   B CG   1 
ATOM   10657 C  CD   . PRO   B  2  111 ? 8.374   -36.863 20.973   1.00 66.22  ? 115  PRO   B CD   1 
ATOM   10658 H  HA   . PRO   B  2  111 ? 7.264   -39.214 19.328   1.00 74.64  ? 115  PRO   B HA   1 
ATOM   10659 H  HB2  . PRO   B  2  111 ? 6.437   -36.900 18.435   1.00 73.55  ? 115  PRO   B HB2  1 
ATOM   10660 H  HB3  . PRO   B  2  111 ? 5.915   -37.529 19.798   1.00 73.55  ? 115  PRO   B HB3  1 
ATOM   10661 H  HG2  . PRO   B  2  111 ? 7.878   -35.574 19.460   1.00 76.99  ? 115  PRO   B HG2  1 
ATOM   10662 H  HG3  . PRO   B  2  111 ? 6.769   -35.647 20.597   1.00 76.99  ? 115  PRO   B HG3  1 
ATOM   10663 H  HD2  . PRO   B  2  111 ? 9.171   -36.328 21.111   1.00 79.44  ? 115  PRO   B HD2  1 
ATOM   10664 H  HD3  . PRO   B  2  111 ? 7.963   -37.073 21.826   1.00 79.44  ? 115  PRO   B HD3  1 
ATOM   10665 N  N    . VAL   B  2  112 ? 7.701   -39.090 16.874   1.00 58.73  ? 116  VAL   B N    1 
ATOM   10666 C  CA   . VAL   B  2  112 ? 8.212   -39.286 15.522   1.00 59.19  ? 116  VAL   B CA   1 
ATOM   10667 C  C    . VAL   B  2  112 ? 7.061   -39.114 14.541   1.00 61.59  ? 116  VAL   B C    1 
ATOM   10668 O  O    . VAL   B  2  112 ? 6.049   -39.819 14.636   1.00 66.04  ? 116  VAL   B O    1 
ATOM   10669 C  CB   . VAL   B  2  112 ? 8.857   -40.672 15.340   1.00 59.72  ? 116  VAL   B CB   1 
ATOM   10670 C  CG1  . VAL   B  2  112 ? 9.395   -40.832 13.922   1.00 58.80  ? 116  VAL   B CG1  1 
ATOM   10671 C  CG2  . VAL   B  2  112 ? 9.961   -40.888 16.363   1.00 59.80  ? 116  VAL   B CG2  1 
ATOM   10672 H  H    . VAL   B  2  112 ? 6.947   -39.480 17.015   1.00 70.45  ? 116  VAL   B H    1 
ATOM   10673 H  HA   . VAL   B  2  112 ? 8.876   -38.604 15.333   1.00 71.01  ? 116  VAL   B HA   1 
ATOM   10674 H  HB   . VAL   B  2  112 ? 8.180   -41.352 15.483   1.00 71.64  ? 116  VAL   B HB   1 
ATOM   10675 H  HG11 . VAL   B  2  112 ? 9.882   -41.669 13.862   1.00 70.53  ? 116  VAL   B HG11 1 
ATOM   10676 H  HG12 . VAL   B  2  112 ? 8.651   -40.837 13.301   1.00 70.53  ? 116  VAL   B HG12 1 
ATOM   10677 H  HG13 . VAL   B  2  112 ? 9.987   -40.090 13.724   1.00 70.53  ? 116  VAL   B HG13 1 
ATOM   10678 H  HG21 . VAL   B  2  112 ? 10.346  -41.769 16.232   1.00 71.74  ? 116  VAL   B HG21 1 
ATOM   10679 H  HG22 . VAL   B  2  112 ? 10.642  -40.208 16.241   1.00 71.74  ? 116  VAL   B HG22 1 
ATOM   10680 H  HG23 . VAL   B  2  112 ? 9.584   -40.821 17.254   1.00 71.74  ? 116  VAL   B HG23 1 
ATOM   10681 N  N    . ASP   B  2  113 ? 7.212   -38.184 13.602   1.00 57.79  ? 117  ASP   B N    1 
ATOM   10682 C  CA   . ASP   B  2  113 ? 6.314   -38.058 12.464   1.00 56.62  ? 117  ASP   B CA   1 
ATOM   10683 C  C    . ASP   B  2  113 ? 6.971   -38.685 11.242   1.00 57.24  ? 117  ASP   B C    1 
ATOM   10684 O  O    . ASP   B  2  113 ? 8.165   -38.490 11.000   1.00 59.53  ? 117  ASP   B O    1 
ATOM   10685 C  CB   . ASP   B  2  113 ? 5.984   -36.595 12.168   1.00 59.99  ? 117  ASP   B CB   1 
ATOM   10686 C  CG   . ASP   B  2  113 ? 5.161   -35.949 13.258   1.00 66.25  ? 117  ASP   B CG   1 
ATOM   10687 O  OD1  . ASP   B  2  113 ? 4.459   -36.674 13.995   1.00 69.59  ? 117  ASP   B OD1  1 
ATOM   10688 O  OD2  . ASP   B  2  113 ? 5.213   -34.707 13.368   1.00 65.81  ? 117  ASP   B OD2  1 
ATOM   10689 H  H    . ASP   B  2  113 ? 7.843   -37.600 13.606   1.00 69.33  ? 117  ASP   B H    1 
ATOM   10690 H  HA   . ASP   B  2  113 ? 5.482   -38.518 12.657   1.00 67.92  ? 117  ASP   B HA   1 
ATOM   10691 H  HB2  . ASP   B  2  113 ? 6.811   -36.096 12.080   1.00 71.97  ? 117  ASP   B HB2  1 
ATOM   10692 H  HB3  . ASP   B  2  113 ? 5.478   -36.547 11.342   1.00 71.97  ? 117  ASP   B HB3  1 
ATOM   10693 N  N    . LEU   B  2  114 ? 6.188   -39.438 10.473   1.00 58.40  ? 118  LEU   B N    1 
ATOM   10694 C  CA   . LEU   B  2  114 ? 6.689   -40.076 9.261    1.00 54.86  ? 118  LEU   B CA   1 
ATOM   10695 C  C    . LEU   B  2  114 ? 5.677   -39.887 8.144    1.00 52.13  ? 118  LEU   B C    1 
ATOM   10696 O  O    . LEU   B  2  114 ? 4.557   -40.398 8.226    1.00 52.04  ? 118  LEU   B O    1 
ATOM   10697 C  CB   . LEU   B  2  114 ? 6.964   -41.565 9.494    1.00 56.46  ? 118  LEU   B CB   1 
ATOM   10698 C  CG   . LEU   B  2  114 ? 7.691   -42.284 8.355    1.00 57.39  ? 118  LEU   B CG   1 
ATOM   10699 C  CD1  . LEU   B  2  114 ? 8.626   -43.346 8.911    1.00 60.23  ? 118  LEU   B CD1  1 
ATOM   10700 C  CD2  . LEU   B  2  114 ? 6.703   -42.908 7.383    1.00 58.49  ? 118  LEU   B CD2  1 
ATOM   10701 H  H    . LEU   B  2  114 ? 5.358   -39.595 10.634   1.00 70.07  ? 118  LEU   B H    1 
ATOM   10702 H  HA   . LEU   B  2  114 ? 7.517   -39.648 8.993    1.00 65.81  ? 118  LEU   B HA   1 
ATOM   10703 H  HB2  . LEU   B  2  114 ? 7.513   -41.654 10.289   1.00 67.73  ? 118  LEU   B HB2  1 
ATOM   10704 H  HB3  . LEU   B  2  114 ? 6.115   -42.015 9.625    1.00 67.73  ? 118  LEU   B HB3  1 
ATOM   10705 H  HG   . LEU   B  2  114 ? 8.218   -41.633 7.866    1.00 68.85  ? 118  LEU   B HG   1 
ATOM   10706 H  HD11 . LEU   B  2  114 ? 9.061   -43.801 8.173    1.00 72.25  ? 118  LEU   B HD11 1 
ATOM   10707 H  HD12 . LEU   B  2  114 ? 9.291   -42.918 9.473    1.00 72.25  ? 118  LEU   B HD12 1 
ATOM   10708 H  HD13 . LEU   B  2  114 ? 8.110   -43.979 9.433    1.00 72.25  ? 118  LEU   B HD13 1 
ATOM   10709 H  HD21 . LEU   B  2  114 ? 7.195   -43.388 6.698    1.00 70.16  ? 118  LEU   B HD21 1 
ATOM   10710 H  HD22 . LEU   B  2  114 ? 6.127   -43.520 7.867    1.00 70.16  ? 118  LEU   B HD22 1 
ATOM   10711 H  HD23 . LEU   B  2  114 ? 6.172   -42.205 6.977    1.00 70.16  ? 118  LEU   B HD23 1 
ATOM   10712 N  N    . TYR   B  2  115 ? 6.071   -39.161 7.103    1.00 53.85  ? 119  TYR   B N    1 
ATOM   10713 C  CA   . TYR   B  2  115 ? 5.240   -38.970 5.921    1.00 55.79  ? 119  TYR   B CA   1 
ATOM   10714 C  C    . TYR   B  2  115 ? 5.755   -39.881 4.813    1.00 57.91  ? 119  TYR   B C    1 
ATOM   10715 O  O    . TYR   B  2  115 ? 6.916   -39.770 4.402    1.00 59.11  ? 119  TYR   B O    1 
ATOM   10716 C  CB   . TYR   B  2  115 ? 5.249   -37.508 5.476    1.00 52.89  ? 119  TYR   B CB   1 
ATOM   10717 C  CG   . TYR   B  2  115 ? 4.189   -37.182 4.449    1.00 54.34  ? 119  TYR   B CG   1 
ATOM   10718 C  CD1  . TYR   B  2  115 ? 2.852   -37.085 4.813    1.00 59.55  ? 119  TYR   B CD1  1 
ATOM   10719 C  CD2  . TYR   B  2  115 ? 4.522   -36.968 3.119    1.00 54.90  ? 119  TYR   B CD2  1 
ATOM   10720 C  CE1  . TYR   B  2  115 ? 1.878   -36.789 3.880    1.00 61.24  ? 119  TYR   B CE1  1 
ATOM   10721 C  CE2  . TYR   B  2  115 ? 3.554   -36.669 2.178    1.00 59.39  ? 119  TYR   B CE2  1 
ATOM   10722 C  CZ   . TYR   B  2  115 ? 2.235   -36.579 2.565    1.00 62.01  ? 119  TYR   B CZ   1 
ATOM   10723 O  OH   . TYR   B  2  115 ? 1.269   -36.284 1.631    1.00 62.13  ? 119  TYR   B OH   1 
ATOM   10724 H  H    . TYR   B  2  115 ? 6.831   -38.762 7.057    1.00 64.60  ? 119  TYR   B H    1 
ATOM   10725 H  HA   . TYR   B  2  115 ? 4.323   -39.214 6.121    1.00 66.93  ? 119  TYR   B HA   1 
ATOM   10726 H  HB2  . TYR   B  2  115 ? 5.096   -36.945 6.250    1.00 63.45  ? 119  TYR   B HB2  1 
ATOM   10727 H  HB3  . TYR   B  2  115 ? 6.113   -37.306 5.084    1.00 63.45  ? 119  TYR   B HB3  1 
ATOM   10728 H  HD1  . TYR   B  2  115 ? 2.609   -37.222 5.700    1.00 71.44  ? 119  TYR   B HD1  1 
ATOM   10729 H  HD2  . TYR   B  2  115 ? 5.412   -37.027 2.856    1.00 65.87  ? 119  TYR   B HD2  1 
ATOM   10730 H  HE1  . TYR   B  2  115 ? 0.986   -36.731 4.137    1.00 73.47  ? 119  TYR   B HE1  1 
ATOM   10731 H  HE2  . TYR   B  2  115 ? 3.791   -36.530 1.290    1.00 71.25  ? 119  TYR   B HE2  1 
ATOM   10732 H  HH   . TYR   B  2  115 ? 0.535   -36.623 1.861    1.00 74.53  ? 119  TYR   B HH   1 
ATOM   10733 N  N    . TYR   B  2  116 ? 4.895   -40.780 4.340    1.00 56.97  ? 120  TYR   B N    1 
ATOM   10734 C  CA   . TYR   B  2  116 ? 5.257   -41.768 3.324    1.00 58.60  ? 120  TYR   B CA   1 
ATOM   10735 C  C    . TYR   B  2  116 ? 4.901   -41.190 1.959    1.00 64.48  ? 120  TYR   B C    1 
ATOM   10736 O  O    . TYR   B  2  116 ? 3.732   -41.159 1.569    1.00 70.19  ? 120  TYR   B O    1 
ATOM   10737 C  CB   . TYR   B  2  116 ? 4.536   -43.086 3.592    1.00 57.06  ? 120  TYR   B CB   1 
ATOM   10738 C  CG   . TYR   B  2  116 ? 5.081   -44.289 2.849    1.00 54.62  ? 120  TYR   B CG   1 
ATOM   10739 C  CD1  . TYR   B  2  116 ? 6.116   -45.049 3.382    1.00 56.41  ? 120  TYR   B CD1  1 
ATOM   10740 C  CD2  . TYR   B  2  116 ? 4.544   -44.681 1.629    1.00 55.24  ? 120  TYR   B CD2  1 
ATOM   10741 C  CE1  . TYR   B  2  116 ? 6.609   -46.155 2.714    1.00 56.94  ? 120  TYR   B CE1  1 
ATOM   10742 C  CE2  . TYR   B  2  116 ? 5.031   -45.785 0.954    1.00 56.03  ? 120  TYR   B CE2  1 
ATOM   10743 C  CZ   . TYR   B  2  116 ? 6.063   -46.519 1.501    1.00 56.81  ? 120  TYR   B CZ   1 
ATOM   10744 O  OH   . TYR   B  2  116 ? 6.553   -47.619 0.835    1.00 56.32  ? 120  TYR   B OH   1 
ATOM   10745 H  H    . TYR   B  2  116 ? 4.076   -40.840 4.598    1.00 68.34  ? 120  TYR   B H    1 
ATOM   10746 H  HA   . TYR   B  2  116 ? 6.213   -41.933 3.344    1.00 70.30  ? 120  TYR   B HA   1 
ATOM   10747 H  HB2  . TYR   B  2  116 ? 4.596   -43.280 4.540    1.00 68.45  ? 120  TYR   B HB2  1 
ATOM   10748 H  HB3  . TYR   B  2  116 ? 3.607   -42.983 3.333    1.00 68.45  ? 120  TYR   B HB3  1 
ATOM   10749 H  HD1  . TYR   B  2  116 ? 6.483   -44.810 4.202    1.00 67.68  ? 120  TYR   B HD1  1 
ATOM   10750 H  HD2  . TYR   B  2  116 ? 3.844   -44.192 1.260    1.00 66.27  ? 120  TYR   B HD2  1 
ATOM   10751 H  HE1  . TYR   B  2  116 ? 7.305   -46.651 3.080    1.00 68.31  ? 120  TYR   B HE1  1 
ATOM   10752 H  HE2  . TYR   B  2  116 ? 4.666   -46.032 0.135    1.00 67.22  ? 120  TYR   B HE2  1 
ATOM   10753 H  HH   . TYR   B  2  116 ? 6.148   -47.716 0.105    1.00 67.56  ? 120  TYR   B HH   1 
ATOM   10754 N  N    . LEU   B  2  117 ? 5.915   -40.721 1.234    1.00 63.71  ? 121  LEU   B N    1 
ATOM   10755 C  CA   . LEU   B  2  117 ? 5.741   -40.106 -0.077   1.00 59.82  ? 121  LEU   B CA   1 
ATOM   10756 C  C    . LEU   B  2  117 ? 6.196   -41.097 -1.139   1.00 59.10  ? 121  LEU   B C    1 
ATOM   10757 O  O    . LEU   B  2  117 ? 7.378   -41.453 -1.193   1.00 57.79  ? 121  LEU   B O    1 
ATOM   10758 C  CB   . LEU   B  2  117 ? 6.534   -38.803 -0.169   1.00 56.23  ? 121  LEU   B CB   1 
ATOM   10759 C  CG   . LEU   B  2  117 ? 6.437   -38.024 -1.480   1.00 59.48  ? 121  LEU   B CG   1 
ATOM   10760 C  CD1  . LEU   B  2  117 ? 4.987   -37.742 -1.843   1.00 59.93  ? 121  LEU   B CD1  1 
ATOM   10761 C  CD2  . LEU   B  2  117 ? 7.225   -36.727 -1.364   1.00 58.54  ? 121  LEU   B CD2  1 
ATOM   10762 H  H    . LEU   B  2  117 ? 6.736   -40.750 1.489    1.00 76.43  ? 121  LEU   B H    1 
ATOM   10763 H  HA   . LEU   B  2  117 ? 4.805   -39.900 -0.228   1.00 71.76  ? 121  LEU   B HA   1 
ATOM   10764 H  HB2  . LEU   B  2  117 ? 6.221   -38.213 0.535    1.00 67.45  ? 121  LEU   B HB2  1 
ATOM   10765 H  HB3  . LEU   B  2  117 ? 7.471   -39.013 -0.033   1.00 67.45  ? 121  LEU   B HB3  1 
ATOM   10766 H  HG   . LEU   B  2  117 ? 6.816   -38.556 -2.198   1.00 71.35  ? 121  LEU   B HG   1 
ATOM   10767 H  HD11 . LEU   B  2  117 ? 4.962   -37.221 -2.661   1.00 71.89  ? 121  LEU   B HD11 1 
ATOM   10768 H  HD12 . LEU   B  2  117 ? 4.525   -38.585 -1.973   1.00 71.89  ? 121  LEU   B HD12 1 
ATOM   10769 H  HD13 . LEU   B  2  117 ? 4.572   -37.245 -1.121   1.00 71.89  ? 121  LEU   B HD13 1 
ATOM   10770 H  HD21 . LEU   B  2  117 ? 7.174   -36.249 -2.207   1.00 70.23  ? 121  LEU   B HD21 1 
ATOM   10771 H  HD22 . LEU   B  2  117 ? 6.842   -36.187 -0.655   1.00 70.23  ? 121  LEU   B HD22 1 
ATOM   10772 H  HD23 . LEU   B  2  117 ? 8.150   -36.936 -1.158   1.00 70.23  ? 121  LEU   B HD23 1 
ATOM   10773 N  N    . MET   B  2  118 ? 5.265   -41.533 -1.985   1.00 58.55  ? 122  MET   B N    1 
ATOM   10774 C  CA   . MET   B  2  118 ? 5.477   -42.686 -2.848   1.00 60.16  ? 122  MET   B CA   1 
ATOM   10775 C  C    . MET   B  2  118 ? 5.265   -42.336 -4.314   1.00 60.46  ? 122  MET   B C    1 
ATOM   10776 O  O    . MET   B  2  118 ? 4.273   -41.691 -4.672   1.00 60.69  ? 122  MET   B O    1 
ATOM   10777 C  CB   . MET   B  2  118 ? 4.540   -43.830 -2.450   1.00 57.00  ? 122  MET   B CB   1 
ATOM   10778 C  CG   . MET   B  2  118 ? 4.686   -45.068 -3.311   1.00 53.40  ? 122  MET   B CG   1 
ATOM   10779 S  SD   . MET   B  2  118 ? 3.725   -46.462 -2.703   1.00 56.67  ? 122  MET   B SD   1 
ATOM   10780 C  CE   . MET   B  2  118 ? 4.011   -47.644 -4.017   1.00 59.03  ? 122  MET   B CE   1 
ATOM   10781 H  H    . MET   B  2  118 ? 4.490   -41.170 -2.076   1.00 70.25  ? 122  MET   B H    1 
ATOM   10782 H  HA   . MET   B  2  118 ? 6.400   -42.969 -2.746   1.00 72.17  ? 122  MET   B HA   1 
ATOM   10783 H  HB2  . MET   B  2  118 ? 4.729   -44.084 -1.533   1.00 68.38  ? 122  MET   B HB2  1 
ATOM   10784 H  HB3  . MET   B  2  118 ? 3.623   -43.523 -2.527   1.00 68.38  ? 122  MET   B HB3  1 
ATOM   10785 H  HG2  . MET   B  2  118 ? 4.383   -44.864 -4.210   1.00 64.07  ? 122  MET   B HG2  1 
ATOM   10786 H  HG3  . MET   B  2  118 ? 5.619   -45.332 -3.328   1.00 64.07  ? 122  MET   B HG3  1 
ATOM   10787 H  HE1  . MET   B  2  118 ? 3.474   -48.435 -3.853   1.00 70.81  ? 122  MET   B HE1  1 
ATOM   10788 H  HE2  . MET   B  2  118 ? 3.760   -47.243 -4.863   1.00 70.81  ? 122  MET   B HE2  1 
ATOM   10789 H  HE3  . MET   B  2  118 ? 4.952   -47.881 -4.030   1.00 70.81  ? 122  MET   B HE3  1 
ATOM   10790 N  N    . ASP   B  2  119 ? 6.207   -42.767 -5.149   1.00 58.77  ? 123  ASP   B N    1 
ATOM   10791 C  CA   . ASP   B  2  119 ? 6.009   -42.795 -6.592   1.00 58.22  ? 123  ASP   B CA   1 
ATOM   10792 C  C    . ASP   B  2  119 ? 4.850   -43.724 -6.934   1.00 60.35  ? 123  ASP   B C    1 
ATOM   10793 O  O    . ASP   B  2  119 ? 4.830   -44.885 -6.517   1.00 60.42  ? 123  ASP   B O    1 
ATOM   10794 C  CB   . ASP   B  2  119 ? 7.301   -43.270 -7.261   1.00 57.92  ? 123  ASP   B CB   1 
ATOM   10795 C  CG   . ASP   B  2  119 ? 7.224   -43.280 -8.775   1.00 57.42  ? 123  ASP   B CG   1 
ATOM   10796 O  OD1  . ASP   B  2  119 ? 6.113   -43.387 -9.335   1.00 56.92  ? 123  ASP   B OD1  1 
ATOM   10797 O  OD2  . ASP   B  2  119 ? 8.296   -43.188 -9.411   1.00 57.46  ? 123  ASP   B OD2  1 
ATOM   10798 H  H    . ASP   B  2  119 ? 6.980   -43.051 -4.902   1.00 70.50  ? 123  ASP   B H    1 
ATOM   10799 H  HA   . ASP   B  2  119 ? 5.795   -41.910 -6.926   1.00 69.84  ? 123  ASP   B HA   1 
ATOM   10800 H  HB2  . ASP   B  2  119 ? 8.025   -42.677 -7.004   1.00 69.48  ? 123  ASP   B HB2  1 
ATOM   10801 H  HB3  . ASP   B  2  119 ? 7.493   -44.174 -6.967   1.00 69.48  ? 123  ASP   B HB3  1 
ATOM   10802 N  N    . LEU   B  2  120 ? 3.876   -43.212 -7.690   1.00 60.97  ? 124  LEU   B N    1 
ATOM   10803 C  CA   . LEU   B  2  120 ? 2.732   -44.010 -8.118   1.00 62.59  ? 124  LEU   B CA   1 
ATOM   10804 C  C    . LEU   B  2  120 ? 2.659   -44.128 -9.638   1.00 59.81  ? 124  LEU   B C    1 
ATOM   10805 O  O    . LEU   B  2  120 ? 1.581   -44.337 -10.200  1.00 57.07  ? 124  LEU   B O    1 
ATOM   10806 C  CB   . LEU   B  2  120 ? 1.423   -43.440 -7.569   1.00 65.49  ? 124  LEU   B CB   1 
ATOM   10807 C  CG   . LEU   B  2  120 ? 1.007   -43.834 -6.147   1.00 69.83  ? 124  LEU   B CG   1 
ATOM   10808 C  CD1  . LEU   B  2  120 ? -0.442  -43.431 -5.899   1.00 71.41  ? 124  LEU   B CD1  1 
ATOM   10809 C  CD2  . LEU   B  2  120 ? 1.185   -45.323 -5.879   1.00 74.21  ? 124  LEU   B CD2  1 
ATOM   10810 H  H    . LEU   B  2  120 ? 3.859   -42.399 -7.968   1.00 73.15  ? 124  LEU   B H    1 
ATOM   10811 H  HA   . LEU   B  2  120 ? 2.843   -44.903 -7.756   1.00 75.09  ? 124  LEU   B HA   1 
ATOM   10812 H  HB2  . LEU   B  2  120 ? 1.495   -42.473 -7.580   1.00 78.57  ? 124  LEU   B HB2  1 
ATOM   10813 H  HB3  . LEU   B  2  120 ? 0.707   -43.726 -8.158   1.00 78.57  ? 124  LEU   B HB3  1 
ATOM   10814 H  HG   . LEU   B  2  120 ? 1.587   -43.364 -5.528   1.00 83.77  ? 124  LEU   B HG   1 
ATOM   10815 H  HD11 . LEU   B  2  120 ? -0.697  -43.704 -5.004   1.00 85.67  ? 124  LEU   B HD11 1 
ATOM   10816 H  HD12 . LEU   B  2  120 ? -0.522  -42.469 -5.987   1.00 85.67  ? 124  LEU   B HD12 1 
ATOM   10817 H  HD13 . LEU   B  2  120 ? -1.008  -43.871 -6.553   1.00 85.67  ? 124  LEU   B HD13 1 
ATOM   10818 H  HD21 . LEU   B  2  120 ? 0.726   -45.553 -5.056   1.00 89.03  ? 124  LEU   B HD21 1 
ATOM   10819 H  HD22 . LEU   B  2  120 ? 0.807   -45.824 -6.619   1.00 89.03  ? 124  LEU   B HD22 1 
ATOM   10820 H  HD23 . LEU   B  2  120 ? 2.131   -45.518 -5.797   1.00 89.03  ? 124  LEU   B HD23 1 
ATOM   10821 N  N    . SER   B  2  121 ? 3.793   -44.002 -10.321  1.00 55.90  ? 125  SER   B N    1 
ATOM   10822 C  CA   . SER   B  2  121 ? 3.824   -44.330 -11.736  1.00 57.06  ? 125  SER   B CA   1 
ATOM   10823 C  C    . SER   B  2  121 ? 3.588   -45.830 -11.917  1.00 58.59  ? 125  SER   B C    1 
ATOM   10824 O  O    . SER   B  2  121 ? 3.506   -46.598 -10.954  1.00 57.25  ? 125  SER   B O    1 
ATOM   10825 C  CB   . SER   B  2  121 ? 5.147   -43.896 -12.359  1.00 60.83  ? 125  SER   B CB   1 
ATOM   10826 O  OG   . SER   B  2  121 ? 6.249   -44.417 -11.638  1.00 70.06  ? 125  SER   B OG   1 
ATOM   10827 H  H    . SER   B  2  121 ? 4.541   -43.734 -9.992   1.00 67.07  ? 125  SER   B H    1 
ATOM   10828 H  HA   . SER   B  2  121 ? 3.116   -43.848 -12.191  1.00 68.45  ? 125  SER   B HA   1 
ATOM   10829 H  HB2  . SER   B  2  121 ? 5.186   -44.223 -13.272  1.00 72.98  ? 125  SER   B HB2  1 
ATOM   10830 H  HB3  . SER   B  2  121 ? 5.196   -42.927 -12.351  1.00 72.98  ? 125  SER   B HB3  1 
ATOM   10831 N  N    . ALA   B  2  122 ? 3.489   -46.255 -13.179  1.00 62.48  ? 126  ALA   B N    1 
ATOM   10832 C  CA   . ALA   B  2  122 ? 3.000   -47.600 -13.466  1.00 66.50  ? 126  ALA   B CA   1 
ATOM   10833 C  C    . ALA   B  2  122 ? 3.917   -48.684 -12.909  1.00 64.03  ? 126  ALA   B C    1 
ATOM   10834 O  O    . ALA   B  2  122 ? 3.454   -49.794 -12.622  1.00 64.46  ? 126  ALA   B O    1 
ATOM   10835 C  CB   . ALA   B  2  122 ? 2.819   -47.778 -14.974  1.00 67.83  ? 126  ALA   B CB   1 
ATOM   10836 H  H    . ALA   B  2  122 ? 3.695   -45.791 -13.874  1.00 74.95  ? 126  ALA   B H    1 
ATOM   10837 H  HA   . ALA   B  2  122 ? 2.135   -47.706 -13.039  1.00 79.78  ? 126  ALA   B HA   1 
ATOM   10838 H  HB1  . ALA   B  2  122 ? 2.569   -48.698 -15.155  1.00 81.38  ? 126  ALA   B HB1  1 
ATOM   10839 H  HB2  . ALA   B  2  122 ? 2.120   -47.179 -15.281  1.00 81.38  ? 126  ALA   B HB2  1 
ATOM   10840 H  HB3  . ALA   B  2  122 ? 3.654   -47.567 -15.419  1.00 81.38  ? 126  ALA   B HB3  1 
ATOM   10841 N  N    . SER   B  2  123 ? 5.208   -48.394 -12.745  1.00 61.24  ? 127  SER   B N    1 
ATOM   10842 C  CA   . SER   B  2  123 ? 6.143   -49.401 -12.250  1.00 58.52  ? 127  SER   B CA   1 
ATOM   10843 C  C    . SER   B  2  123 ? 6.003   -49.669 -10.756  1.00 58.56  ? 127  SER   B C    1 
ATOM   10844 O  O    . SER   B  2  123 ? 6.740   -50.512 -10.227  1.00 56.44  ? 127  SER   B O    1 
ATOM   10845 C  CB   . SER   B  2  123 ? 7.580   -48.974 -12.556  1.00 60.01  ? 127  SER   B CB   1 
ATOM   10846 O  OG   . SER   B  2  123 ? 7.894   -47.751 -11.913  1.00 60.69  ? 127  SER   B OG   1 
ATOM   10847 H  H    . SER   B  2  123 ? 5.563   -47.629 -12.912  1.00 73.47  ? 127  SER   B H    1 
ATOM   10848 H  HA   . SER   B  2  123 ? 5.966   -50.233 -12.717  1.00 70.20  ? 127  SER   B HA   1 
ATOM   10849 H  HB2  . SER   B  2  123 ? 8.187   -49.661 -12.239  1.00 71.99  ? 127  SER   B HB2  1 
ATOM   10850 H  HB3  . SER   B  2  123 ? 7.678   -48.860 -13.514  1.00 71.99  ? 127  SER   B HB3  1 
ATOM   10851 H  HG   . SER   B  2  123 ? 8.545   -47.858 -11.393  1.00 72.81  ? 127  SER   B HG   1 
ATOM   10852 N  N    . MET   B  2  124 ? 5.087   -48.988 -10.065  1.00 61.30  ? 128  MET   B N    1 
ATOM   10853 C  CA   . MET   B  2  124 ? 4.913   -49.140 -8.626   1.00 63.75  ? 128  MET   B CA   1 
ATOM   10854 C  C    . MET   B  2  124 ? 3.615   -49.863 -8.276   1.00 65.06  ? 128  MET   B C    1 
ATOM   10855 O  O    . MET   B  2  124 ? 3.170   -49.809 -7.125   1.00 64.14  ? 128  MET   B O    1 
ATOM   10856 C  CB   . MET   B  2  124 ? 4.965   -47.768 -7.952   1.00 62.42  ? 128  MET   B CB   1 
ATOM   10857 C  CG   . MET   B  2  124 ? 6.230   -46.979 -8.276   1.00 61.44  ? 128  MET   B CG   1 
ATOM   10858 S  SD   . MET   B  2  124 ? 7.720   -47.713 -7.573   1.00 62.55  ? 128  MET   B SD   1 
ATOM   10859 C  CE   . MET   B  2  124 ? 7.438   -47.452 -5.823   1.00 58.86  ? 128  MET   B CE   1 
ATOM   10860 H  H    . MET   B  2  124 ? 4.546   -48.421 -10.418  1.00 73.54  ? 128  MET   B H    1 
ATOM   10861 H  HA   . MET   B  2  124 ? 5.649   -49.669 -8.280   1.00 76.48  ? 128  MET   B HA   1 
ATOM   10862 H  HB2  . MET   B  2  124 ? 4.204   -47.245 -8.247   1.00 74.88  ? 128  MET   B HB2  1 
ATOM   10863 H  HB3  . MET   B  2  124 ? 4.930   -47.891 -6.990   1.00 74.88  ? 128  MET   B HB3  1 
ATOM   10864 H  HG2  . MET   B  2  124 ? 6.340   -46.944 -9.239   1.00 73.71  ? 128  MET   B HG2  1 
ATOM   10865 H  HG3  . MET   B  2  124 ? 6.141   -46.082 -7.919   1.00 73.71  ? 128  MET   B HG3  1 
ATOM   10866 H  HE1  . MET   B  2  124 ? 8.219   -47.748 -5.330   1.00 70.61  ? 128  MET   B HE1  1 
ATOM   10867 H  HE2  . MET   B  2  124 ? 7.285   -46.507 -5.665   1.00 70.61  ? 128  MET   B HE2  1 
ATOM   10868 H  HE3  . MET   B  2  124 ? 6.660   -47.963 -5.549   1.00 70.61  ? 128  MET   B HE3  1 
ATOM   10869 N  N    . ASP   B  2  125 ? 3.001   -50.541 -9.247   1.00 64.43  ? 129  ASP   B N    1 
ATOM   10870 C  CA   . ASP   B  2  125 ? 1.801   -51.321 -8.964   1.00 67.81  ? 129  ASP   B CA   1 
ATOM   10871 C  C    . ASP   B  2  125 ? 2.113   -52.471 -8.016   1.00 67.87  ? 129  ASP   B C    1 
ATOM   10872 O  O    . ASP   B  2  125 ? 1.401   -52.692 -7.028   1.00 67.70  ? 129  ASP   B O    1 
ATOM   10873 C  CB   . ASP   B  2  125 ? 1.204   -51.849 -10.268  1.00 75.69  ? 129  ASP   B CB   1 
ATOM   10874 C  CG   . ASP   B  2  125 ? -0.163  -52.479 -10.074  1.00 89.82  ? 129  ASP   B CG   1 
ATOM   10875 O  OD1  . ASP   B  2  125 ? -1.149  -51.728 -9.918   1.00 93.40  ? 129  ASP   B OD1  1 
ATOM   10876 O  OD2  . ASP   B  2  125 ? -0.252  -53.724 -10.079  1.00 96.68  ? 129  ASP   B OD2  1 
ATOM   10877 H  H    . ASP   B  2  125 ? 3.258   -50.565 -10.068  1.00 77.29  ? 129  ASP   B H    1 
ATOM   10878 H  HA   . ASP   B  2  125 ? 1.144   -50.746 -8.541   1.00 81.36  ? 129  ASP   B HA   1 
ATOM   10879 H  HB2  . ASP   B  2  125 ? 1.110   -51.114 -10.894  1.00 90.81  ? 129  ASP   B HB2  1 
ATOM   10880 H  HB3  . ASP   B  2  125 ? 1.796   -52.524 -10.636  1.00 90.81  ? 129  ASP   B HB3  1 
ATOM   10881 N  N    . ASP   B  2  126 ? 3.174   -53.224 -8.308   1.00 67.40  ? 130  ASP   B N    1 
ATOM   10882 C  CA   . ASP   B  2  126 ? 3.587   -54.298 -7.413   1.00 68.46  ? 130  ASP   B CA   1 
ATOM   10883 C  C    . ASP   B  2  126 ? 3.908   -53.760 -6.025   1.00 70.07  ? 130  ASP   B C    1 
ATOM   10884 O  O    . ASP   B  2  126 ? 3.610   -54.407 -5.014   1.00 74.15  ? 130  ASP   B O    1 
ATOM   10885 C  CB   . ASP   B  2  126 ? 4.799   -55.023 -7.997   1.00 68.40  ? 130  ASP   B CB   1 
ATOM   10886 C  CG   . ASP   B  2  126 ? 5.922   -54.069 -8.366   1.00 68.93  ? 130  ASP   B CG   1 
ATOM   10887 O  OD1  . ASP   B  2  126 ? 5.619   -52.969 -8.873   1.00 68.94  ? 130  ASP   B OD1  1 
ATOM   10888 O  OD2  . ASP   B  2  126 ? 7.104   -54.407 -8.141   1.00 71.86  ? 130  ASP   B OD2  1 
ATOM   10889 H  H    . ASP   B  2  126 ? 3.664   -53.134 -9.009   1.00 80.87  ? 130  ASP   B H    1 
ATOM   10890 H  HA   . ASP   B  2  126 ? 2.862   -54.937 -7.330   1.00 82.13  ? 130  ASP   B HA   1 
ATOM   10891 H  HB2  . ASP   B  2  126 ? 5.140   -55.650 -7.340   1.00 82.06  ? 130  ASP   B HB2  1 
ATOM   10892 H  HB3  . ASP   B  2  126 ? 4.530   -55.496 -8.799   1.00 82.06  ? 130  ASP   B HB3  1 
ATOM   10893 N  N    . ASP   B  2  127 ? 4.516   -52.574 -5.957   1.00 66.19  ? 131  ASP   B N    1 
ATOM   10894 C  CA   . ASP   B  2  127 ? 4.860   -51.991 -4.665   1.00 65.82  ? 131  ASP   B CA   1 
ATOM   10895 C  C    . ASP   B  2  127 ? 3.616   -51.762 -3.816   1.00 64.83  ? 131  ASP   B C    1 
ATOM   10896 O  O    . ASP   B  2  127 ? 3.608   -52.072 -2.619   1.00 62.95  ? 131  ASP   B O    1 
ATOM   10897 C  CB   . ASP   B  2  127 ? 5.621   -50.683 -4.874   1.00 66.60  ? 131  ASP   B CB   1 
ATOM   10898 C  CG   . ASP   B  2  127 ? 6.930   -50.884 -5.612   1.00 66.99  ? 131  ASP   B CG   1 
ATOM   10899 O  OD1  . ASP   B  2  127 ? 6.893   -51.257 -6.804   1.00 66.67  ? 131  ASP   B OD1  1 
ATOM   10900 O  OD2  . ASP   B  2  127 ? 7.997   -50.672 -4.999   1.00 64.37  ? 131  ASP   B OD2  1 
ATOM   10901 H  H    . ASP   B  2  127 ? 4.736   -52.094 -6.636   1.00 79.41  ? 131  ASP   B H    1 
ATOM   10902 H  HA   . ASP   B  2  127 ? 5.439   -52.604 -4.185   1.00 78.96  ? 131  ASP   B HA   1 
ATOM   10903 H  HB2  . ASP   B  2  127 ? 5.072   -50.076 -5.394   1.00 79.91  ? 131  ASP   B HB2  1 
ATOM   10904 H  HB3  . ASP   B  2  127 ? 5.821   -50.291 -4.009   1.00 79.91  ? 131  ASP   B HB3  1 
ATOM   10905 N  N    . LEU   B  2  128 ? 2.552   -51.221 -4.417   1.00 63.41  ? 132  LEU   B N    1 
ATOM   10906 C  CA   . LEU   B  2  128 ? 1.310   -51.015 -3.679   1.00 64.52  ? 132  LEU   B CA   1 
ATOM   10907 C  C    . LEU   B  2  128 ? 0.786   -52.317 -3.087   1.00 65.80  ? 132  LEU   B C    1 
ATOM   10908 O  O    . LEU   B  2  128 ? 0.175   -52.308 -2.013   1.00 63.78  ? 132  LEU   B O    1 
ATOM   10909 C  CB   . LEU   B  2  128 ? 0.244   -50.398 -4.588   1.00 63.59  ? 132  LEU   B CB   1 
ATOM   10910 C  CG   . LEU   B  2  128 ? 0.197   -48.875 -4.733   1.00 62.87  ? 132  LEU   B CG   1 
ATOM   10911 C  CD1  . LEU   B  2  128 ? -0.979  -48.497 -5.624   1.00 63.61  ? 132  LEU   B CD1  1 
ATOM   10912 C  CD2  . LEU   B  2  128 ? 0.089   -48.176 -3.387   1.00 63.82  ? 132  LEU   B CD2  1 
ATOM   10913 H  H    . LEU   B  2  128 ? 2.526   -50.968 -5.239   1.00 76.07  ? 132  LEU   B H    1 
ATOM   10914 H  HA   . LEU   B  2  128 ? 1.488   -50.396 -2.953   1.00 77.41  ? 132  LEU   B HA   1 
ATOM   10915 H  HB2  . LEU   B  2  128 ? 0.377   -50.756 -5.479   1.00 76.28  ? 132  LEU   B HB2  1 
ATOM   10916 H  HB3  . LEU   B  2  128 ? -0.623  -50.669 -4.247   1.00 76.28  ? 132  LEU   B HB3  1 
ATOM   10917 H  HG   . LEU   B  2  128 ? 1.024   -48.572 -5.138   1.00 75.43  ? 132  LEU   B HG   1 
ATOM   10918 H  HD11 . LEU   B  2  128 ? -1.002  -47.532 -5.722   1.00 76.31  ? 132  LEU   B HD11 1 
ATOM   10919 H  HD12 . LEU   B  2  128 ? -0.865  -48.915 -6.492   1.00 76.31  ? 132  LEU   B HD12 1 
ATOM   10920 H  HD13 . LEU   B  2  128 ? -1.800  -48.808 -5.213   1.00 76.31  ? 132  LEU   B HD13 1 
ATOM   10921 H  HD21 . LEU   B  2  128 ? -0.037  -47.226 -3.533   1.00 76.57  ? 132  LEU   B HD21 1 
ATOM   10922 H  HD22 . LEU   B  2  128 ? -0.669  -48.540 -2.902   1.00 76.57  ? 132  LEU   B HD22 1 
ATOM   10923 H  HD23 . LEU   B  2  128 ? 0.906   -48.328 -2.886   1.00 76.57  ? 132  LEU   B HD23 1 
ATOM   10924 N  N    . ASN   B  2  129 ? 1.014   -53.443 -3.767   1.00 71.33  ? 133  ASN   B N    1 
ATOM   10925 C  CA   . ASN   B  2  129 ? 0.425   -54.702 -3.324   1.00 76.64  ? 133  ASN   B CA   1 
ATOM   10926 C  C    . ASN   B  2  129 ? 1.113   -55.254 -2.082   1.00 76.41  ? 133  ASN   B C    1 
ATOM   10927 O  O    . ASN   B  2  129 ? 0.481   -55.973 -1.299   1.00 80.11  ? 133  ASN   B O    1 
ATOM   10928 C  CB   . ASN   B  2  129 ? 0.475   -55.729 -4.456   1.00 82.87  ? 133  ASN   B CB   1 
ATOM   10929 C  CG   . ASN   B  2  129 ? -0.746  -55.667 -5.355   1.00 89.28  ? 133  ASN   B CG   1 
ATOM   10930 O  OD1  . ASN   B  2  129 ? -1.875  -55.553 -4.880   1.00 92.23  ? 133  ASN   B OD1  1 
ATOM   10931 N  ND2  . ASN   B  2  129 ? -0.523  -55.740 -6.662   1.00 92.89  ? 133  ASN   B ND2  1 
ATOM   10932 H  H    . ASN   B  2  129 ? 1.497   -53.502 -4.477   1.00 85.58  ? 133  ASN   B H    1 
ATOM   10933 H  HA   . ASN   B  2  129 ? -0.504  -54.541 -3.098   1.00 91.95  ? 133  ASN   B HA   1 
ATOM   10934 H  HB2  . ASN   B  2  129 ? 1.260   -55.562 -5.002   1.00 99.42  ? 133  ASN   B HB2  1 
ATOM   10935 H  HB3  . ASN   B  2  129 ? 0.522   -56.620 -4.074   1.00 99.42  ? 133  ASN   B HB3  1 
ATOM   10936 H  HD21 . ASN   B  2  129 ? -1.183  -55.709 -7.213   1.00 111.45 ? 133  ASN   B HD21 1 
ATOM   10937 H  HD22 . ASN   B  2  129 ? 0.280   -55.818 -6.958   1.00 111.45 ? 133  ASN   B HD22 1 
ATOM   10938 N  N    . THR   B  2  130 ? 2.388   -54.937 -1.873   1.00 72.97  ? 134  THR   B N    1 
ATOM   10939 C  CA   . THR   B  2  130 ? 3.140   -55.508 -0.764   1.00 77.89  ? 134  THR   B CA   1 
ATOM   10940 C  C    . THR   B  2  130 ? 3.163   -54.622 0.476    1.00 75.08  ? 134  THR   B C    1 
ATOM   10941 O  O    . THR   B  2  130 ? 3.730   -55.030 1.495    1.00 77.08  ? 134  THR   B O    1 
ATOM   10942 C  CB   . THR   B  2  130 ? 4.580   -55.809 -1.200   1.00 81.03  ? 134  THR   B CB   1 
ATOM   10943 O  OG1  . THR   B  2  130 ? 5.227   -54.593 -1.594   1.00 82.89  ? 134  THR   B OG1  1 
ATOM   10944 C  CG2  . THR   B  2  130 ? 4.599   -56.793 -2.364   1.00 85.45  ? 134  THR   B CG2  1 
ATOM   10945 H  H    . THR   B  2  130 ? 2.839   -54.392 -2.362   1.00 87.54  ? 134  THR   B H    1 
ATOM   10946 H  HA   . THR   B  2  130 ? 2.717   -56.345 -0.517   1.00 93.44  ? 134  THR   B HA   1 
ATOM   10947 H  HB   . THR   B  2  130 ? 5.062   -56.207 -0.458   1.00 97.21  ? 134  THR   B HB   1 
ATOM   10948 H  HG1  . THR   B  2  130 ? 5.654   -54.714 -2.307   1.00 99.45  ? 134  THR   B HG1  1 
ATOM   10949 H  HG21 . THR   B  2  130 ? 5.470   -57.214 -2.428   1.00 102.52 ? 134  THR   B HG21 1 
ATOM   10950 H  HG22 . THR   B  2  130 ? 3.927   -57.479 -2.230   1.00 102.52 ? 134  THR   B HG22 1 
ATOM   10951 H  HG23 . THR   B  2  130 ? 4.412   -56.327 -3.194   1.00 102.52 ? 134  THR   B HG23 1 
ATOM   10952 N  N    . ILE   B  2  131 ? 2.566   -53.429 0.425    1.00 68.20  ? 135  ILE   B N    1 
ATOM   10953 C  CA   . ILE   B  2  131 ? 2.541   -52.541 1.584    1.00 67.07  ? 135  ILE   B CA   1 
ATOM   10954 C  C    . ILE   B  2  131 ? 1.109   -52.334 2.062    1.00 66.82  ? 135  ILE   B C    1 
ATOM   10955 O  O    . ILE   B  2  131 ? 0.793   -51.307 2.673    1.00 63.31  ? 135  ILE   B O    1 
ATOM   10956 C  CB   . ILE   B  2  131 ? 3.203   -51.185 1.269    1.00 66.14  ? 135  ILE   B CB   1 
ATOM   10957 C  CG1  . ILE   B  2  131 ? 2.492   -50.490 0.105    1.00 63.78  ? 135  ILE   B CG1  1 
ATOM   10958 C  CG2  . ILE   B  2  131 ? 4.678   -51.373 0.955    1.00 65.00  ? 135  ILE   B CG2  1 
ATOM   10959 C  CD1  . ILE   B  2  131 ? 2.793   -49.013 0.013    1.00 60.27  ? 135  ILE   B CD1  1 
ATOM   10960 H  H    . ILE   B  2  131 ? 2.168   -53.114 -0.269   1.00 81.82  ? 135  ILE   B H    1 
ATOM   10961 H  HA   . ILE   B  2  131 ? 3.037   -52.973 2.297    1.00 80.47  ? 135  ILE   B HA   1 
ATOM   10962 H  HB   . ILE   B  2  131 ? 3.122   -50.622 2.055    1.00 79.34  ? 135  ILE   B HB   1 
ATOM   10963 H  HG12 . ILE   B  2  131 ? 2.774   -50.903 -0.726   1.00 76.51  ? 135  ILE   B HG12 1 
ATOM   10964 H  HG13 . ILE   B  2  131 ? 1.534   -50.592 0.218    1.00 76.51  ? 135  ILE   B HG13 1 
ATOM   10965 H  HG21 . ILE   B  2  131 ? 5.079   -50.505 0.790    1.00 77.98  ? 135  ILE   B HG21 1 
ATOM   10966 H  HG22 . ILE   B  2  131 ? 5.111   -51.798 1.712    1.00 77.98  ? 135  ILE   B HG22 1 
ATOM   10967 H  HG23 . ILE   B  2  131 ? 4.764   -51.933 0.168    1.00 77.98  ? 135  ILE   B HG23 1 
ATOM   10968 H  HD11 . ILE   B  2  131 ? 2.257   -48.625 -0.697   1.00 72.30  ? 135  ILE   B HD11 1 
ATOM   10969 H  HD12 . ILE   B  2  131 ? 2.574   -48.593 0.860    1.00 72.30  ? 135  ILE   B HD12 1 
ATOM   10970 H  HD13 . ILE   B  2  131 ? 3.735   -48.894 -0.182   1.00 72.30  ? 135  ILE   B HD13 1 
ATOM   10971 N  N    . LYS   B  2  132 ? 0.232   -53.304 1.791    1.00 73.35  ? 136  LYS   B N    1 
ATOM   10972 C  CA   . LYS   B  2  132 ? -1.163  -53.162 2.197    1.00 79.89  ? 136  LYS   B CA   1 
ATOM   10973 C  C    . LYS   B  2  132 ? -1.305  -53.086 3.712    1.00 78.86  ? 136  LYS   B C    1 
ATOM   10974 O  O    . LYS   B  2  132 ? -2.286  -52.525 4.214    1.00 82.92  ? 136  LYS   B O    1 
ATOM   10975 C  CB   . LYS   B  2  132 ? -1.993  -54.324 1.651    1.00 88.92  ? 136  LYS   B CB   1 
ATOM   10976 C  CG   . LYS   B  2  132 ? -2.227  -54.278 0.151    1.00 93.21  ? 136  LYS   B CG   1 
ATOM   10977 C  CD   . LYS   B  2  132 ? -2.888  -55.560 -0.333   1.00 97.99  ? 136  LYS   B CD   1 
ATOM   10978 C  CE   . LYS   B  2  132 ? -3.172  -55.523 -1.826   1.00 97.97  ? 136  LYS   B CE   1 
ATOM   10979 N  NZ   . LYS   B  2  132 ? -3.615  -56.847 -2.343   1.00 102.10 ? 136  LYS   B NZ   1 
ATOM   10980 H  H    . LYS   B  2  132 ? 0.417   -54.038 1.382    1.00 88.00  ? 136  LYS   B H    1 
ATOM   10981 H  HA   . LYS   B  2  132 ? -1.510  -52.339 1.820    1.00 95.85  ? 136  LYS   B HA   1 
ATOM   10982 H  HB2  . LYS   B  2  132 ? -1.532  -55.154 1.851    1.00 106.68 ? 136  LYS   B HB2  1 
ATOM   10983 H  HB3  . LYS   B  2  132 ? -2.861  -54.314 2.084    1.00 106.68 ? 136  LYS   B HB3  1 
ATOM   10984 H  HG2  . LYS   B  2  132 ? -2.808  -53.532 -0.064   1.00 111.83 ? 136  LYS   B HG2  1 
ATOM   10985 H  HG3  . LYS   B  2  132 ? -1.377  -54.179 -0.306   1.00 111.83 ? 136  LYS   B HG3  1 
ATOM   10986 H  HD2  . LYS   B  2  132 ? -2.299  -56.310 -0.155   1.00 117.56 ? 136  LYS   B HD2  1 
ATOM   10987 H  HD3  . LYS   B  2  132 ? -3.730  -55.681 0.133    1.00 117.56 ? 136  LYS   B HD3  1 
ATOM   10988 H  HE2  . LYS   B  2  132 ? -3.875  -54.878 -2.001   1.00 117.54 ? 136  LYS   B HE2  1 
ATOM   10989 H  HE3  . LYS   B  2  132 ? -2.364  -55.268 -2.298   1.00 117.54 ? 136  LYS   B HE3  1 
ATOM   10990 H  HZ1  . LYS   B  2  132 ? -3.765  -56.797 -3.219   1.00 122.50 ? 136  LYS   B HZ1  1 
ATOM   10991 H  HZ2  . LYS   B  2  132 ? -2.986  -57.459 -2.192   1.00 122.50 ? 136  LYS   B HZ2  1 
ATOM   10992 H  HZ3  . LYS   B  2  132 ? -4.365  -57.098 -1.935   1.00 122.50 ? 136  LYS   B HZ3  1 
ATOM   10993 N  N    . GLU   B  2  133 ? -0.347  -53.642 4.454    1.00 74.69  ? 137  GLU   B N    1 
ATOM   10994 C  CA   . GLU   B  2  133 ? -0.376  -53.642 5.912    1.00 75.43  ? 137  GLU   B CA   1 
ATOM   10995 C  C    . GLU   B  2  133 ? 0.881   -53.001 6.492    1.00 67.02  ? 137  GLU   B C    1 
ATOM   10996 O  O    . GLU   B  2  133 ? 1.271   -53.293 7.624    1.00 64.63  ? 137  GLU   B O    1 
ATOM   10997 C  CB   . GLU   B  2  133 ? -0.550  -55.064 6.444    1.00 84.62  ? 137  GLU   B CB   1 
ATOM   10998 C  CG   . GLU   B  2  133 ? -1.882  -55.697 6.078    1.00 95.45  ? 137  GLU   B CG   1 
ATOM   10999 C  CD   . GLU   B  2  133 ? -1.997  -57.132 6.551    1.00 109.28 ? 137  GLU   B CD   1 
ATOM   11000 O  OE1  . GLU   B  2  133 ? -1.034  -57.637 7.166    1.00 113.98 ? 137  GLU   B OE1  1 
ATOM   11001 O  OE2  . GLU   B  2  133 ? -3.051  -57.755 6.306    1.00 115.48 ? 137  GLU   B OE2  1 
ATOM   11002 H  H    . GLU   B  2  133 ? 0.344   -54.034 4.126    1.00 89.60  ? 137  GLU   B H    1 
ATOM   11003 H  HA   . GLU   B  2  133 ? -1.136  -53.116 6.208    1.00 90.49  ? 137  GLU   B HA   1 
ATOM   11004 H  HB2  . GLU   B  2  133 ? 0.154   -55.622 6.078    1.00 101.53 ? 137  GLU   B HB2  1 
ATOM   11005 H  HB3  . GLU   B  2  133 ? -0.487  -55.044 7.412    1.00 101.53 ? 137  GLU   B HB3  1 
ATOM   11006 H  HG2  . GLU   B  2  133 ? -2.598  -55.187 6.489    1.00 114.52 ? 137  GLU   B HG2  1 
ATOM   11007 H  HG3  . GLU   B  2  133 ? -1.981  -55.690 5.114    1.00 114.52 ? 137  GLU   B HG3  1 
ATOM   11008 N  N    . LEU   B  2  134 ? 1.524   -52.119 5.722    1.00 65.11  ? 138  LEU   B N    1 
ATOM   11009 C  CA   . LEU   B  2  134 ? 2.713   -51.436 6.221    1.00 66.99  ? 138  LEU   B CA   1 
ATOM   11010 C  C    . LEU   B  2  134 ? 2.374   -50.534 7.402    1.00 65.00  ? 138  LEU   B C    1 
ATOM   11011 O  O    . LEU   B  2  134 ? 3.144   -50.445 8.365    1.00 65.99  ? 138  LEU   B O    1 
ATOM   11012 C  CB   . LEU   B  2  134 ? 3.361   -50.622 5.101    1.00 65.47  ? 138  LEU   B CB   1 
ATOM   11013 C  CG   . LEU   B  2  134 ? 4.593   -49.798 5.486    1.00 63.67  ? 138  LEU   B CG   1 
ATOM   11014 C  CD1  . LEU   B  2  134 ? 5.713   -50.701 5.980    1.00 67.31  ? 138  LEU   B CD1  1 
ATOM   11015 C  CD2  . LEU   B  2  134 ? 5.064   -48.952 4.312    1.00 62.33  ? 138  LEU   B CD2  1 
ATOM   11016 H  H    . LEU   B  2  134 ? 1.295   -51.904 4.922    1.00 78.12  ? 138  LEU   B H    1 
ATOM   11017 H  HA   . LEU   B  2  134 ? 3.352   -52.102 6.521    1.00 80.37  ? 138  LEU   B HA   1 
ATOM   11018 H  HB2  . LEU   B  2  134 ? 3.636   -51.237 4.402    1.00 78.55  ? 138  LEU   B HB2  1 
ATOM   11019 H  HB3  . LEU   B  2  134 ? 2.699   -50.003 4.756    1.00 78.55  ? 138  LEU   B HB3  1 
ATOM   11020 H  HG   . LEU   B  2  134 ? 4.353   -49.198 6.209    1.00 76.38  ? 138  LEU   B HG   1 
ATOM   11021 H  HD11 . LEU   B  2  134 ? 6.492   -50.158 6.179    1.00 80.76  ? 138  LEU   B HD11 1 
ATOM   11022 H  HD12 . LEU   B  2  134 ? 5.417   -51.161 6.781    1.00 80.76  ? 138  LEU   B HD12 1 
ATOM   11023 H  HD13 . LEU   B  2  134 ? 5.928   -51.345 5.288    1.00 80.76  ? 138  LEU   B HD13 1 
ATOM   11024 H  HD21 . LEU   B  2  134 ? 5.849   -48.449 4.580    1.00 74.77  ? 138  LEU   B HD21 1 
ATOM   11025 H  HD22 . LEU   B  2  134 ? 5.283   -49.537 3.570    1.00 74.77  ? 138  LEU   B HD22 1 
ATOM   11026 H  HD23 . LEU   B  2  134 ? 4.353   -48.345 4.055    1.00 74.77  ? 138  LEU   B HD23 1 
ATOM   11027 N  N    . GLY   B  2  135 ? 1.228   -49.854 7.343    1.00 63.30  ? 139  GLY   B N    1 
ATOM   11028 C  CA   . GLY   B  2  135 ? 0.868   -48.936 8.412    1.00 61.79  ? 139  GLY   B CA   1 
ATOM   11029 C  C    . GLY   B  2  135 ? 0.860   -49.603 9.774    1.00 61.48  ? 139  GLY   B C    1 
ATOM   11030 O  O    . GLY   B  2  135 ? 1.405   -49.071 10.744   1.00 65.33  ? 139  GLY   B O    1 
ATOM   11031 H  H    . GLY   B  2  135 ? 0.653   -49.907 6.705    1.00 75.94  ? 139  GLY   B H    1 
ATOM   11032 H  HA2  . GLY   B  2  135 ? 1.505   -48.205 8.434    1.00 74.13  ? 139  GLY   B HA2  1 
ATOM   11033 H  HA3  . GLY   B  2  135 ? -0.018  -48.579 8.243    1.00 74.13  ? 139  GLY   B HA3  1 
ATOM   11034 N  N    . SER   B  2  136 ? 0.240   -50.781 9.865    1.00 59.16  ? 140  SER   B N    1 
ATOM   11035 C  CA   . SER   B  2  136 ? 0.192   -51.488 11.140   1.00 64.08  ? 140  SER   B CA   1 
ATOM   11036 C  C    . SER   B  2  136 ? 1.552   -52.075 11.498   1.00 66.00  ? 140  SER   B C    1 
ATOM   11037 O  O    . SER   B  2  136 ? 1.998   -51.966 12.646   1.00 69.85  ? 140  SER   B O    1 
ATOM   11038 C  CB   . SER   B  2  136 ? -0.872  -52.585 11.091   1.00 67.26  ? 140  SER   B CB   1 
ATOM   11039 O  OG   . SER   B  2  136 ? -0.721  -53.393 9.937    1.00 69.81  ? 140  SER   B OG   1 
ATOM   11040 H  H    . SER   B  2  136 ? -0.154  -51.183 9.215    1.00 70.97  ? 140  SER   B H    1 
ATOM   11041 H  HA   . SER   B  2  136 ? -0.055  -50.861 11.837   1.00 76.88  ? 140  SER   B HA   1 
ATOM   11042 H  HB2  . SER   B  2  136 ? -0.785  -53.144 11.879   1.00 80.69  ? 140  SER   B HB2  1 
ATOM   11043 H  HB3  . SER   B  2  136 ? -1.749  -52.172 11.073   1.00 80.69  ? 140  SER   B HB3  1 
ATOM   11044 H  HG   . SER   B  2  136 ? -1.194  -54.084 10.005   1.00 83.75  ? 140  SER   B HG   1 
ATOM   11045 N  N    . ARG   B  2  137 ? 2.227   -52.702 10.531   1.00 66.77  ? 141  ARG   B N    1 
ATOM   11046 C  CA   . ARG   B  2  137 ? 3.537   -53.285 10.802   1.00 68.16  ? 141  ARG   B CA   1 
ATOM   11047 C  C    . ARG   B  2  137 ? 4.527   -52.218 11.253   1.00 63.32  ? 141  ARG   B C    1 
ATOM   11048 O  O    . ARG   B  2  137 ? 5.251   -52.401 12.239   1.00 60.23  ? 141  ARG   B O    1 
ATOM   11049 C  CB   . ARG   B  2  137 ? 4.056   -54.011 9.558    1.00 70.98  ? 141  ARG   B CB   1 
ATOM   11050 C  CG   . ARG   B  2  137 ? 3.338   -55.318 9.264    1.00 79.11  ? 141  ARG   B CG   1 
ATOM   11051 C  CD   . ARG   B  2  137 ? 3.685   -55.880 7.887    1.00 87.97  ? 141  ARG   B CD   1 
ATOM   11052 N  NE   . ARG   B  2  137 ? 5.098   -56.238 7.760    1.00 95.62  ? 141  ARG   B NE   1 
ATOM   11053 C  CZ   . ARG   B  2  137 ? 5.925   -55.781 6.818    1.00 96.67  ? 141  ARG   B CZ   1 
ATOM   11054 N  NH1  . ARG   B  2  137 ? 5.503   -54.939 5.882    1.00 92.81  ? 141  ARG   B NH1  1 
ATOM   11055 N  NH2  . ARG   B  2  137 ? 7.188   -56.182 6.808    1.00 98.80  ? 141  ARG   B NH2  1 
ATOM   11056 H  H    . ARG   B  2  137 ? 1.951   -52.800 9.722    1.00 80.10  ? 141  ARG   B H    1 
ATOM   11057 H  HA   . ARG   B  2  137 ? 3.448   -53.937 11.515   1.00 81.77  ? 141  ARG   B HA   1 
ATOM   11058 H  HB2  . ARG   B  2  137 ? 3.941   -53.431 8.789    1.00 85.16  ? 141  ARG   B HB2  1 
ATOM   11059 H  HB3  . ARG   B  2  137 ? 4.997   -54.212 9.685    1.00 85.16  ? 141  ARG   B HB3  1 
ATOM   11060 H  HG2  . ARG   B  2  137 ? 3.592   -55.976 9.930    1.00 94.91  ? 141  ARG   B HG2  1 
ATOM   11061 H  HG3  . ARG   B  2  137 ? 2.381   -55.168 9.295    1.00 94.91  ? 141  ARG   B HG3  1 
ATOM   11062 H  HD2  . ARG   B  2  137 ? 3.159   -56.679 7.730    1.00 105.54 ? 141  ARG   B HD2  1 
ATOM   11063 H  HD3  . ARG   B  2  137 ? 3.484   -55.212 7.213    1.00 105.54 ? 141  ARG   B HD3  1 
ATOM   11064 H  HE   . ARG   B  2  137 ? 5.422   -56.786 8.338    1.00 114.72 ? 141  ARG   B HE   1 
ATOM   11065 H  HH11 . ARG   B  2  137 ? 4.683   -54.679 5.875    1.00 111.35 ? 141  ARG   B HH11 1 
ATOM   11066 H  HH12 . ARG   B  2  137 ? 6.049   -54.654 5.282    1.00 111.35 ? 141  ARG   B HH12 1 
ATOM   11067 H  HH21 . ARG   B  2  137 ? 7.469   -56.733 7.405    1.00 118.54 ? 141  ARG   B HH21 1 
ATOM   11068 H  HH22 . ARG   B  2  137 ? 7.726   -55.891 6.203    1.00 118.54 ? 141  ARG   B HH22 1 
ATOM   11069 N  N    . LEU   B  2  138 ? 4.569   -51.090 10.542   1.00 63.33  ? 142  LEU   B N    1 
ATOM   11070 C  CA   . LEU   B  2  138 ? 5.514   -50.034 10.888   1.00 64.14  ? 142  LEU   B CA   1 
ATOM   11071 C  C    . LEU   B  2  138 ? 5.191   -49.432 12.250   1.00 66.92  ? 142  LEU   B C    1 
ATOM   11072 O  O    . LEU   B  2  138 ? 6.083   -49.253 13.088   1.00 67.90  ? 142  LEU   B O    1 
ATOM   11073 C  CB   . LEU   B  2  138 ? 5.508   -48.953 9.807    1.00 63.07  ? 142  LEU   B CB   1 
ATOM   11074 C  CG   . LEU   B  2  138 ? 6.411   -47.746 10.067   1.00 66.35  ? 142  LEU   B CG   1 
ATOM   11075 C  CD1  . LEU   B  2  138 ? 7.862   -48.168 10.241   1.00 65.39  ? 142  LEU   B CD1  1 
ATOM   11076 C  CD2  . LEU   B  2  138 ? 6.272   -46.745 8.934    1.00 66.43  ? 142  LEU   B CD2  1 
ATOM   11077 H  H    . LEU   B  2  138 ? 4.068   -50.916 9.865    1.00 75.97  ? 142  LEU   B H    1 
ATOM   11078 H  HA   . LEU   B  2  138 ? 6.405   -50.414 10.930   1.00 76.95  ? 142  LEU   B HA   1 
ATOM   11079 H  HB2  . LEU   B  2  138 ? 5.799   -49.356 8.974    1.00 75.66  ? 142  LEU   B HB2  1 
ATOM   11080 H  HB3  . LEU   B  2  138 ? 4.601   -48.621 9.716    1.00 75.66  ? 142  LEU   B HB3  1 
ATOM   11081 H  HG   . LEU   B  2  138 ? 6.136   -47.319 10.894   1.00 79.60  ? 142  LEU   B HG   1 
ATOM   11082 H  HD11 . LEU   B  2  138 ? 8.410   -47.376 10.353   1.00 78.45  ? 142  LEU   B HD11 1 
ATOM   11083 H  HD12 . LEU   B  2  138 ? 7.934   -48.735 11.025   1.00 78.45  ? 142  LEU   B HD12 1 
ATOM   11084 H  HD13 . LEU   B  2  138 ? 8.145   -48.657 9.452    1.00 78.45  ? 142  LEU   B HD13 1 
ATOM   11085 H  HD21 . LEU   B  2  138 ? 6.859   -45.992 9.105    1.00 79.70  ? 142  LEU   B HD21 1 
ATOM   11086 H  HD22 . LEU   B  2  138 ? 6.521   -47.175 8.101    1.00 79.70  ? 142  LEU   B HD22 1 
ATOM   11087 H  HD23 . LEU   B  2  138 ? 5.351   -46.444 8.889    1.00 79.70  ? 142  LEU   B HD23 1 
ATOM   11088 N  N    . SER   B  2  139 ? 3.919   -49.109 12.490   1.00 67.72  ? 143  SER   B N    1 
ATOM   11089 C  CA   . SER   B  2  139 ? 3.548   -48.497 13.762   1.00 68.69  ? 143  SER   B CA   1 
ATOM   11090 C  C    . SER   B  2  139 ? 3.765   -49.450 14.931   1.00 64.37  ? 143  SER   B C    1 
ATOM   11091 O  O    . SER   B  2  139 ? 4.057   -49.000 16.045   1.00 62.90  ? 143  SER   B O    1 
ATOM   11092 C  CB   . SER   B  2  139 ? 2.092   -48.032 13.715   1.00 74.69  ? 143  SER   B CB   1 
ATOM   11093 O  OG   . SER   B  2  139 ? 1.228   -49.084 13.325   1.00 83.66  ? 143  SER   B OG   1 
ATOM   11094 H  H    . SER   B  2  139 ? 3.266   -49.231 11.944   1.00 81.25  ? 143  SER   B H    1 
ATOM   11095 H  HA   . SER   B  2  139 ? 4.106   -47.718 13.907   1.00 82.41  ? 143  SER   B HA   1 
ATOM   11096 H  HB2  . SER   B  2  139 ? 1.833   -47.723 14.597   1.00 89.61  ? 143  SER   B HB2  1 
ATOM   11097 H  HB3  . SER   B  2  139 ? 2.014   -47.308 13.073   1.00 89.61  ? 143  SER   B HB3  1 
ATOM   11098 H  HG   . SER   B  2  139 ? 1.384   -49.304 12.529   1.00 100.37 ? 143  SER   B HG   1 
ATOM   11099 N  N    . LYS   B  2  140 ? 3.630   -50.759 14.706   1.00 62.06  ? 144  LYS   B N    1 
ATOM   11100 C  CA   . LYS   B  2  140 ? 3.870   -51.714 15.784   1.00 66.09  ? 144  LYS   B CA   1 
ATOM   11101 C  C    . LYS   B  2  140 ? 5.350   -51.775 16.144   1.00 68.82  ? 144  LYS   B C    1 
ATOM   11102 O  O    . LYS   B  2  140 ? 5.701   -51.870 17.326   1.00 70.13  ? 144  LYS   B O    1 
ATOM   11103 C  CB   . LYS   B  2  140 ? 3.354   -53.100 15.393   1.00 73.44  ? 144  LYS   B CB   1 
ATOM   11104 C  CG   . LYS   B  2  140 ? 3.579   -54.162 16.471   1.00 86.40  ? 144  LYS   B CG   1 
ATOM   11105 C  CD   . LYS   B  2  140 ? 2.528   -55.269 16.429   1.00 98.30  ? 144  LYS   B CD   1 
ATOM   11106 C  CE   . LYS   B  2  140 ? 3.120   -56.607 16.006   1.00 103.61 ? 144  LYS   B CE   1 
ATOM   11107 N  NZ   . LYS   B  2  140 ? 4.103   -57.138 16.993   1.00 105.00 ? 144  LYS   B NZ   1 
ATOM   11108 H  H    . LYS   B  2  140 ? 3.405   -51.111 13.954   1.00 74.45  ? 144  LYS   B H    1 
ATOM   11109 H  HA   . LYS   B  2  140 ? 3.378   -51.425 16.568   1.00 79.29  ? 144  LYS   B HA   1 
ATOM   11110 H  HB2  . LYS   B  2  140 ? 2.400   -53.043 15.227   1.00 88.11  ? 144  LYS   B HB2  1 
ATOM   11111 H  HB3  . LYS   B  2  140 ? 3.814   -53.390 14.590   1.00 88.11  ? 144  LYS   B HB3  1 
ATOM   11112 H  HG2  . LYS   B  2  140 ? 4.449   -54.569 16.338   1.00 103.66 ? 144  LYS   B HG2  1 
ATOM   11113 H  HG3  . LYS   B  2  140 ? 3.538   -53.742 17.344   1.00 103.66 ? 144  LYS   B HG3  1 
ATOM   11114 H  HD2  . LYS   B  2  140 ? 2.142   -55.375 17.312   1.00 117.94 ? 144  LYS   B HD2  1 
ATOM   11115 H  HD3  . LYS   B  2  140 ? 1.838   -55.029 15.792   1.00 117.94 ? 144  LYS   B HD3  1 
ATOM   11116 H  HE2  . LYS   B  2  140 ? 2.405   -57.255 15.916   1.00 124.32 ? 144  LYS   B HE2  1 
ATOM   11117 H  HE3  . LYS   B  2  140 ? 3.577   -56.497 15.157   1.00 124.32 ? 144  LYS   B HE3  1 
ATOM   11118 H  HZ1  . LYS   B  2  140 ? 4.295   -57.987 16.804   1.00 125.98 ? 144  LYS   B HZ1  1 
ATOM   11119 H  HZ2  . LYS   B  2  140 ? 4.852   -56.659 16.965   1.00 125.98 ? 144  LYS   B HZ2  1 
ATOM   11120 H  HZ3  . LYS   B  2  140 ? 3.763   -57.095 17.814   1.00 125.98 ? 144  LYS   B HZ3  1 
ATOM   11121 N  N    . GLU   B  2  141 ? 6.232   -51.720 15.143   1.00 69.45  ? 145  GLU   B N    1 
ATOM   11122 C  CA   . GLU   B  2  141 ? 7.663   -51.726 15.428   1.00 71.44  ? 145  GLU   B CA   1 
ATOM   11123 C  C    . GLU   B  2  141 ? 8.123   -50.399 16.017   1.00 74.97  ? 145  GLU   B C    1 
ATOM   11124 O  O    . GLU   B  2  141 ? 9.023   -50.378 16.864   1.00 77.57  ? 145  GLU   B O    1 
ATOM   11125 C  CB   . GLU   B  2  141 ? 8.454   -52.045 14.159   1.00 71.08  ? 145  GLU   B CB   1 
ATOM   11126 C  CG   . GLU   B  2  141 ? 8.433   -53.513 13.773   1.00 76.26  ? 145  GLU   B CG   1 
ATOM   11127 C  CD   . GLU   B  2  141 ? 9.067   -54.397 14.827   1.00 83.90  ? 145  GLU   B CD   1 
ATOM   11128 O  OE1  . GLU   B  2  141 ? 9.931   -53.900 15.580   1.00 86.10  ? 145  GLU   B OE1  1 
ATOM   11129 O  OE2  . GLU   B  2  141 ? 8.695   -55.586 14.907   1.00 88.65  ? 145  GLU   B OE2  1 
ATOM   11130 H  H    . GLU   B  2  141 ? 6.030   -51.678 14.308   1.00 83.32  ? 145  GLU   B H    1 
ATOM   11131 H  HA   . GLU   B  2  141 ? 7.847   -52.424 16.076   1.00 85.71  ? 145  GLU   B HA   1 
ATOM   11132 H  HB2  . GLU   B  2  141 ? 8.076   -51.541 13.421   1.00 85.28  ? 145  GLU   B HB2  1 
ATOM   11133 H  HB3  . GLU   B  2  141 ? 9.380   -51.789 14.296   1.00 85.28  ? 145  GLU   B HB3  1 
ATOM   11134 H  HG2  . GLU   B  2  141 ? 7.513   -53.797 13.656   1.00 91.49  ? 145  GLU   B HG2  1 
ATOM   11135 H  HG3  . GLU   B  2  141 ? 8.925   -53.631 12.946   1.00 91.49  ? 145  GLU   B HG3  1 
ATOM   11136 N  N    . MET   B  2  142 ? 7.523   -49.287 15.585   1.00 72.81  ? 146  MET   B N    1 
ATOM   11137 C  CA   . MET   B  2  142 ? 7.865   -47.989 16.155   1.00 68.19  ? 146  MET   B CA   1 
ATOM   11138 C  C    . MET   B  2  142 ? 7.330   -47.825 17.571   1.00 70.97  ? 146  MET   B C    1 
ATOM   11139 O  O    . MET   B  2  142 ? 7.850   -46.993 18.323   1.00 72.31  ? 146  MET   B O    1 
ATOM   11140 C  CB   . MET   B  2  142 ? 7.329   -46.868 15.262   1.00 63.54  ? 146  MET   B CB   1 
ATOM   11141 C  CG   . MET   B  2  142 ? 8.003   -46.786 13.898   1.00 62.14  ? 146  MET   B CG   1 
ATOM   11142 S  SD   . MET   B  2  142 ? 9.768   -46.419 13.991   1.00 62.91  ? 146  MET   B SD   1 
ATOM   11143 C  CE   . MET   B  2  142 ? 9.749   -44.805 14.766   1.00 62.19  ? 146  MET   B CE   1 
ATOM   11144 H  H    . MET   B  2  142 ? 6.922   -49.260 14.971   1.00 87.35  ? 146  MET   B H    1 
ATOM   11145 H  HA   . MET   B  2  142 ? 8.831   -47.909 16.179   1.00 81.81  ? 146  MET   B HA   1 
ATOM   11146 H  HB2  . MET   B  2  142 ? 6.382   -47.013 15.115   1.00 76.23  ? 146  MET   B HB2  1 
ATOM   11147 H  HB3  . MET   B  2  142 ? 7.469   -46.019 15.712   1.00 76.23  ? 146  MET   B HB3  1 
ATOM   11148 H  HG2  . MET   B  2  142 ? 7.900   -47.638 13.446   1.00 74.55  ? 146  MET   B HG2  1 
ATOM   11149 H  HG3  . MET   B  2  142 ? 7.580   -46.082 13.381   1.00 74.55  ? 146  MET   B HG3  1 
ATOM   11150 H  HE1  . MET   B  2  142 ? 10.659  -44.479 14.840   1.00 74.61  ? 146  MET   B HE1  1 
ATOM   11151 H  HE2  . MET   B  2  142 ? 9.224   -44.198 14.220   1.00 74.61  ? 146  MET   B HE2  1 
ATOM   11152 H  HE3  . MET   B  2  142 ? 9.352   -44.882 15.648   1.00 74.61  ? 146  MET   B HE3  1 
ATOM   11153 N  N    . SER   B  2  143 ? 6.311   -48.598 17.954   1.00 72.66  ? 147  SER   B N    1 
ATOM   11154 C  CA   . SER   B  2  143 ? 5.795   -48.513 19.316   1.00 79.81  ? 147  SER   B CA   1 
ATOM   11155 C  C    . SER   B  2  143 ? 6.834   -48.961 20.334   1.00 79.74  ? 147  SER   B C    1 
ATOM   11156 O  O    . SER   B  2  143 ? 6.805   -48.516 21.487   1.00 83.36  ? 147  SER   B O    1 
ATOM   11157 C  CB   . SER   B  2  143 ? 4.528   -49.356 19.453   1.00 92.41  ? 147  SER   B CB   1 
ATOM   11158 O  OG   . SER   B  2  143 ? 3.493   -48.870 18.615   1.00 100.76 ? 147  SER   B OG   1 
ATOM   11159 H  H    . SER   B  2  143 ? 5.909   -49.170 17.452   1.00 87.17  ? 147  SER   B H    1 
ATOM   11160 H  HA   . SER   B  2  143 ? 5.565   -47.590 19.503   1.00 95.76  ? 147  SER   B HA   1 
ATOM   11161 H  HB2  . SER   B  2  143 ? 4.731   -50.271 19.202   1.00 110.87 ? 147  SER   B HB2  1 
ATOM   11162 H  HB3  . SER   B  2  143 ? 4.227   -49.324 20.375   1.00 110.87 ? 147  SER   B HB3  1 
ATOM   11163 H  HG   . SER   B  2  143 ? 3.723   -48.930 17.810   1.00 120.89 ? 147  SER   B HG   1 
ATOM   11164 N  N    . LYS   B  2  144 ? 7.754   -49.841 19.932   1.00 76.25  ? 148  LYS   B N    1 
ATOM   11165 C  CA   . LYS   B  2  144 ? 8.812   -50.279 20.833   1.00 78.05  ? 148  LYS   B CA   1 
ATOM   11166 C  C    . LYS   B  2  144 ? 9.859   -49.197 21.056   1.00 76.08  ? 148  LYS   B C    1 
ATOM   11167 O  O    . LYS   B  2  144 ? 10.614  -49.273 22.031   1.00 77.80  ? 148  LYS   B O    1 
ATOM   11168 C  CB   . LYS   B  2  144 ? 9.484   -51.538 20.278   1.00 83.19  ? 148  LYS   B CB   1 
ATOM   11169 C  CG   . LYS   B  2  144 ? 8.520   -52.671 19.948   1.00 88.95  ? 148  LYS   B CG   1 
ATOM   11170 C  CD   . LYS   B  2  144 ? 9.224   -53.816 19.231   1.00 89.48  ? 148  LYS   B CD   1 
ATOM   11171 C  CE   . LYS   B  2  144 ? 8.245   -54.910 18.827   1.00 89.94  ? 148  LYS   B CE   1 
ATOM   11172 N  NZ   . LYS   B  2  144 ? 8.902   -55.997 18.048   1.00 90.49  ? 148  LYS   B NZ   1 
ATOM   11173 H  H    . LYS   B  2  144 ? 7.785   -50.194 19.149   1.00 91.48  ? 148  LYS   B H    1 
ATOM   11174 H  HA   . LYS   B  2  144 ? 8.418   -50.501 21.692   1.00 93.65  ? 148  LYS   B HA   1 
ATOM   11175 H  HB2  . LYS   B  2  144 ? 9.953   -51.304 19.462   1.00 99.81  ? 148  LYS   B HB2  1 
ATOM   11176 H  HB3  . LYS   B  2  144 ? 10.112  -51.870 20.938   1.00 99.81  ? 148  LYS   B HB3  1 
ATOM   11177 H  HG2  . LYS   B  2  144 ? 8.137   -53.016 20.770   1.00 106.72 ? 148  LYS   B HG2  1 
ATOM   11178 H  HG3  . LYS   B  2  144 ? 7.818   -52.336 19.370   1.00 106.72 ? 148  LYS   B HG3  1 
ATOM   11179 H  HD2  . LYS   B  2  144 ? 9.651   -53.478 18.429   1.00 107.35 ? 148  LYS   B HD2  1 
ATOM   11180 H  HD3  . LYS   B  2  144 ? 9.888   -54.205 19.822   1.00 107.35 ? 148  LYS   B HD3  1 
ATOM   11181 H  HE2  . LYS   B  2  144 ? 7.858   -55.302 19.626   1.00 107.91 ? 148  LYS   B HE2  1 
ATOM   11182 H  HE3  . LYS   B  2  144 ? 7.546   -54.524 18.276   1.00 107.91 ? 148  LYS   B HE3  1 
ATOM   11183 H  HZ1  . LYS   B  2  144 ? 8.503   -56.775 18.214   1.00 108.57 ? 148  LYS   B HZ1  1 
ATOM   11184 H  HZ2  . LYS   B  2  144 ? 8.847   -55.824 17.177   1.00 108.57 ? 148  LYS   B HZ2  1 
ATOM   11185 H  HZ3  . LYS   B  2  144 ? 9.761   -56.059 18.276   1.00 108.57 ? 148  LYS   B HZ3  1 
ATOM   11186 N  N    . LEU   B  2  145 ? 9.910   -48.189 20.185   1.00 75.51  ? 149  LEU   B N    1 
ATOM   11187 C  CA   . LEU   B  2  145 ? 10.949  -47.168 20.213   1.00 73.92  ? 149  LEU   B CA   1 
ATOM   11188 C  C    . LEU   B  2  145 ? 10.454  -45.807 20.674   1.00 75.58  ? 149  LEU   B C    1 
ATOM   11189 O  O    . LEU   B  2  145 ? 11.208  -45.079 21.323   1.00 74.93  ? 149  LEU   B O    1 
ATOM   11190 C  CB   . LEU   B  2  145 ? 11.572  -47.018 18.820   1.00 69.44  ? 149  LEU   B CB   1 
ATOM   11191 C  CG   . LEU   B  2  145 ? 11.988  -48.331 18.155   1.00 73.79  ? 149  LEU   B CG   1 
ATOM   11192 C  CD1  . LEU   B  2  145 ? 12.355  -48.105 16.698   1.00 73.95  ? 149  LEU   B CD1  1 
ATOM   11193 C  CD2  . LEU   B  2  145 ? 13.144  -48.967 18.908   1.00 76.73  ? 149  LEU   B CD2  1 
ATOM   11194 H  H    . LEU   B  2  145 ? 9.338   -48.074 19.554   1.00 90.59  ? 149  LEU   B H    1 
ATOM   11195 H  HA   . LEU   B  2  145 ? 11.646  -47.449 20.826   1.00 88.68  ? 149  LEU   B HA   1 
ATOM   11196 H  HB2  . LEU   B  2  145 ? 10.925  -46.588 18.239   1.00 83.31  ? 149  LEU   B HB2  1 
ATOM   11197 H  HB3  . LEU   B  2  145 ? 12.366  -46.465 18.897   1.00 83.31  ? 149  LEU   B HB3  1 
ATOM   11198 H  HG   . LEU   B  2  145 ? 11.238  -48.945 18.179   1.00 88.52  ? 149  LEU   B HG   1 
ATOM   11199 H  HD11 . LEU   B  2  145 ? 12.582  -48.957 16.294   1.00 88.71  ? 149  LEU   B HD11 1 
ATOM   11200 H  HD12 . LEU   B  2  145 ? 11.597  -47.713 16.238   1.00 88.71  ? 149  LEU   B HD12 1 
ATOM   11201 H  HD13 . LEU   B  2  145 ? 13.116  -47.505 16.654   1.00 88.71  ? 149  LEU   B HD13 1 
ATOM   11202 H  HD21 . LEU   B  2  145 ? 13.396  -49.791 18.461   1.00 92.05  ? 149  LEU   B HD21 1 
ATOM   11203 H  HD22 . LEU   B  2  145 ? 13.893  -48.352 18.915   1.00 92.05  ? 149  LEU   B HD22 1 
ATOM   11204 H  HD23 . LEU   B  2  145 ? 12.862  -49.157 19.816   1.00 92.05  ? 149  LEU   B HD23 1 
ATOM   11205 N  N    . THR   B  2  146 ? 9.215   -45.446 20.349   1.00 77.52  ? 150  THR   B N    1 
ATOM   11206 C  CA   . THR   B  2  146 ? 8.626   -44.185 20.773   1.00 76.53  ? 150  THR   B CA   1 
ATOM   11207 C  C    . THR   B  2  146 ? 7.150   -44.406 21.060   1.00 78.93  ? 150  THR   B C    1 
ATOM   11208 O  O    . THR   B  2  146 ? 6.488   -45.191 20.376   1.00 79.99  ? 150  THR   B O    1 
ATOM   11209 C  CB   . THR   B  2  146 ? 8.790   -43.090 19.708   1.00 71.20  ? 150  THR   B CB   1 
ATOM   11210 O  OG1  . THR   B  2  146 ? 8.169   -41.879 20.161   1.00 70.08  ? 150  THR   B OG1  1 
ATOM   11211 C  CG2  . THR   B  2  146 ? 8.161   -43.523 18.389   1.00 68.56  ? 150  THR   B CG2  1 
ATOM   11212 H  H    . THR   B  2  146 ? 8.685   -45.928 19.872   1.00 93.00  ? 150  THR   B H    1 
ATOM   11213 H  HA   . THR   B  2  146 ? 9.063   -43.880 21.584   1.00 91.82  ? 150  THR   B HA   1 
ATOM   11214 H  HB   . THR   B  2  146 ? 9.734   -42.929 19.555   1.00 85.43  ? 150  THR   B HB   1 
ATOM   11215 H  HG1  . THR   B  2  146 ? 8.395   -41.238 19.667   1.00 84.07  ? 150  THR   B HG1  1 
ATOM   11216 H  HG21 . THR   B  2  146 ? 8.306   -42.842 17.713   1.00 82.25  ? 150  THR   B HG21 1 
ATOM   11217 H  HG22 . THR   B  2  146 ? 8.560   -44.355 18.088   1.00 82.25  ? 150  THR   B HG22 1 
ATOM   11218 H  HG23 . THR   B  2  146 ? 7.207   -43.655 18.504   1.00 82.25  ? 150  THR   B HG23 1 
ATOM   11219 N  N    . SER   B  2  147 ? 6.641   -43.710 22.072   1.00 78.73  ? 151  SER   B N    1 
ATOM   11220 C  CA   . SER   B  2  147 ? 5.236   -43.813 22.438   1.00 78.48  ? 151  SER   B CA   1 
ATOM   11221 C  C    . SER   B  2  147 ? 4.347   -42.865 21.644   1.00 74.05  ? 151  SER   B C    1 
ATOM   11222 O  O    . SER   B  2  147 ? 3.121   -42.932 21.782   1.00 73.37  ? 151  SER   B O    1 
ATOM   11223 C  CB   . SER   B  2  147 ? 5.063   -43.542 23.936   1.00 82.10  ? 151  SER   B CB   1 
ATOM   11224 O  OG   . SER   B  2  147 ? 5.573   -42.268 24.288   1.00 84.54  ? 151  SER   B OG   1 
ATOM   11225 H  H    . SER   B  2  147 ? 7.093   -43.168 22.564   1.00 94.46  ? 151  SER   B H    1 
ATOM   11226 H  HA   . SER   B  2  147 ? 4.933   -44.717 22.263   1.00 94.16  ? 151  SER   B HA   1 
ATOM   11227 H  HB2  . SER   B  2  147 ? 4.118   -43.573 24.154   1.00 98.50  ? 151  SER   B HB2  1 
ATOM   11228 H  HB3  . SER   B  2  147 ? 5.542   -44.221 24.436   1.00 98.50  ? 151  SER   B HB3  1 
ATOM   11229 H  HG   . SER   B  2  147 ? 5.744   -42.245 25.110   1.00 101.43 ? 151  SER   B HG   1 
ATOM   11230 N  N    . ASN   B  2  148 ? 4.929   -41.995 20.817   1.00 72.34  ? 152  ASN   B N    1 
ATOM   11231 C  CA   . ASN   B  2  148 ? 4.182   -41.042 19.995   1.00 71.32  ? 152  ASN   B CA   1 
ATOM   11232 C  C    . ASN   B  2  148 ? 4.671   -41.174 18.556   1.00 70.75  ? 152  ASN   B C    1 
ATOM   11233 O  O    . ASN   B  2  148 ? 5.555   -40.431 18.123   1.00 74.01  ? 152  ASN   B O    1 
ATOM   11234 C  CB   . ASN   B  2  148 ? 4.359   -39.617 20.509   1.00 71.61  ? 152  ASN   B CB   1 
ATOM   11235 C  CG   . ASN   B  2  148 ? 3.570   -39.347 21.768   1.00 75.52  ? 152  ASN   B CG   1 
ATOM   11236 O  OD1  . ASN   B  2  148 ? 4.000   -39.684 22.871   1.00 77.91  ? 152  ASN   B OD1  1 
ATOM   11237 N  ND2  . ASN   B  2  148 ? 2.410   -38.722 21.613   1.00 79.36  ? 152  ASN   B ND2  1 
ATOM   11238 H  H    . ASN   B  2  148 ? 5.780   -41.937 20.713   1.00 86.79  ? 152  ASN   B H    1 
ATOM   11239 H  HA   . ASN   B  2  148 ? 3.241   -41.274 20.026   1.00 85.56  ? 152  ASN   B HA   1 
ATOM   11240 H  HB2  . ASN   B  2  148 ? 5.297   -39.466 20.705   1.00 85.92  ? 152  ASN   B HB2  1 
ATOM   11241 H  HB3  . ASN   B  2  148 ? 4.058   -38.995 19.828   1.00 85.92  ? 152  ASN   B HB3  1 
ATOM   11242 H  HD21 . ASN   B  2  148 ? 1.922   -38.545 22.298   1.00 95.21  ? 152  ASN   B HD21 1 
ATOM   11243 H  HD22 . ASN   B  2  148 ? 2.147   -38.495 20.826   1.00 95.21  ? 152  ASN   B HD22 1 
ATOM   11244 N  N    . PHE   B  2  149 ? 4.087   -42.109 17.815   1.00 69.61  ? 153  PHE   B N    1 
ATOM   11245 C  CA   . PHE   B  2  149 ? 4.377   -42.286 16.399   1.00 66.15  ? 153  PHE   B CA   1 
ATOM   11246 C  C    . PHE   B  2  149 ? 3.128   -41.965 15.591   1.00 67.93  ? 153  PHE   B C    1 
ATOM   11247 O  O    . PHE   B  2  149 ? 2.044   -42.482 15.882   1.00 69.45  ? 153  PHE   B O    1 
ATOM   11248 C  CB   . PHE   B  2  149 ? 4.849   -43.710 16.100   1.00 65.07  ? 153  PHE   B CB   1 
ATOM   11249 C  CG   . PHE   B  2  149 ? 5.061   -43.981 14.636   1.00 61.61  ? 153  PHE   B CG   1 
ATOM   11250 C  CD1  . PHE   B  2  149 ? 6.096   -43.370 13.947   1.00 61.35  ? 153  PHE   B CD1  1 
ATOM   11251 C  CD2  . PHE   B  2  149 ? 4.226   -44.847 13.950   1.00 61.42  ? 153  PHE   B CD2  1 
ATOM   11252 C  CE1  . PHE   B  2  149 ? 6.293   -43.616 12.599   1.00 60.77  ? 153  PHE   B CE1  1 
ATOM   11253 C  CE2  . PHE   B  2  149 ? 4.420   -45.097 12.603   1.00 60.89  ? 153  PHE   B CE2  1 
ATOM   11254 C  CZ   . PHE   B  2  149 ? 5.455   -44.480 11.928   1.00 59.48  ? 153  PHE   B CZ   1 
ATOM   11255 H  H    . PHE   B  2  149 ? 3.506   -42.666 18.118   1.00 83.51  ? 153  PHE   B H    1 
ATOM   11256 H  HA   . PHE   B  2  149 ? 5.083   -41.675 16.136   1.00 79.36  ? 153  PHE   B HA   1 
ATOM   11257 H  HB2  . PHE   B  2  149 ? 5.693   -43.861 16.555   1.00 78.06  ? 153  PHE   B HB2  1 
ATOM   11258 H  HB3  . PHE   B  2  149 ? 4.181   -44.335 16.424   1.00 78.06  ? 153  PHE   B HB3  1 
ATOM   11259 H  HD1  . PHE   B  2  149 ? 6.666   -42.788 14.395   1.00 73.60  ? 153  PHE   B HD1  1 
ATOM   11260 H  HD2  . PHE   B  2  149 ? 3.528   -45.265 14.400   1.00 73.69  ? 153  PHE   B HD2  1 
ATOM   11261 H  HE1  . PHE   B  2  149 ? 6.991   -43.199 12.147   1.00 72.90  ? 153  PHE   B HE1  1 
ATOM   11262 H  HE2  . PHE   B  2  149 ? 3.853   -45.680 12.153   1.00 73.05  ? 153  PHE   B HE2  1 
ATOM   11263 H  HZ   . PHE   B  2  149 ? 5.586   -44.647 11.023   1.00 71.36  ? 153  PHE   B HZ   1 
ATOM   11264 N  N    . ARG   B  2  150 ? 3.284   -41.105 14.590   1.00 66.16  ? 154  ARG   B N    1 
ATOM   11265 C  CA   . ARG   B  2  150 ? 2.214   -40.761 13.669   1.00 65.19  ? 154  ARG   B CA   1 
ATOM   11266 C  C    . ARG   B  2  150 ? 2.741   -40.890 12.249   1.00 63.61  ? 154  ARG   B C    1 
ATOM   11267 O  O    . ARG   B  2  150 ? 3.926   -40.656 11.991   1.00 62.17  ? 154  ARG   B O    1 
ATOM   11268 C  CB   . ARG   B  2  150 ? 1.696   -39.339 13.905   1.00 64.39  ? 154  ARG   B CB   1 
ATOM   11269 C  CG   . ARG   B  2  150 ? 1.147   -39.089 15.300   1.00 66.98  ? 154  ARG   B CG   1 
ATOM   11270 C  CD   . ARG   B  2  150 ? 0.404   -37.765 15.344   1.00 70.57  ? 154  ARG   B CD   1 
ATOM   11271 N  NE   . ARG   B  2  150 ? 1.223   -36.677 14.816   1.00 77.72  ? 154  ARG   B NE   1 
ATOM   11272 C  CZ   . ARG   B  2  150 ? 0.743   -35.575 14.247   1.00 83.59  ? 154  ARG   B CZ   1 
ATOM   11273 N  NH1  . ARG   B  2  150 ? -0.566  -35.398 14.112   1.00 87.88  ? 154  ARG   B NH1  1 
ATOM   11274 N  NH2  . ARG   B  2  150 ? 1.578   -34.648 13.801   1.00 82.78  ? 154  ARG   B NH2  1 
ATOM   11275 H  H    . ARG   B  2  150 ? 4.023   -40.698 14.421   1.00 79.37  ? 154  ARG   B H    1 
ATOM   11276 H  HA   . ARG   B  2  150 ? 1.467   -41.368 13.785   1.00 78.21  ? 154  ARG   B HA   1 
ATOM   11277 H  HB2  . ARG   B  2  150 ? 2.426   -38.717 13.762   1.00 77.24  ? 154  ARG   B HB2  1 
ATOM   11278 H  HB3  . ARG   B  2  150 ? 0.981   -39.162 13.273   1.00 77.24  ? 154  ARG   B HB3  1 
ATOM   11279 H  HG2  . ARG   B  2  150 ? 0.530   -39.799 15.539   1.00 80.35  ? 154  ARG   B HG2  1 
ATOM   11280 H  HG3  . ARG   B  2  150 ? 1.878   -39.056 15.937   1.00 80.35  ? 154  ARG   B HG3  1 
ATOM   11281 H  HD2  . ARG   B  2  150 ? -0.401  -37.830 14.807   1.00 84.67  ? 154  ARG   B HD2  1 
ATOM   11282 H  HD3  . ARG   B  2  150 ? 0.174   -37.556 16.263   1.00 84.67  ? 154  ARG   B HD3  1 
ATOM   11283 H  HE   . ARG   B  2  150 ? 2.077   -36.755 14.878   1.00 93.25  ? 154  ARG   B HE   1 
ATOM   11284 H  HH11 . ARG   B  2  150 ? -1.112  -36.000 14.393   1.00 105.44 ? 154  ARG   B HH11 1 
ATOM   11285 H  HH12 . ARG   B  2  150 ? -0.867  -34.682 13.743   1.00 105.44 ? 154  ARG   B HH12 1 
ATOM   11286 H  HH21 . ARG   B  2  150 ? 2.427   -34.761 13.880   1.00 99.32  ? 154  ARG   B HH21 1 
ATOM   11287 H  HH22 . ARG   B  2  150 ? 1.272   -33.934 13.433   1.00 99.32  ? 154  ARG   B HH22 1 
ATOM   11288 N  N    . LEU   B  2  151 ? 1.860   -41.269 11.327   1.00 61.35  ? 155  LEU   B N    1 
ATOM   11289 C  CA   . LEU   B  2  151 ? 2.268   -41.465 9.945    1.00 62.39  ? 155  LEU   B CA   1 
ATOM   11290 C  C    . LEU   B  2  151 ? 1.191   -40.954 9.002    1.00 61.72  ? 155  LEU   B C    1 
ATOM   11291 O  O    . LEU   B  2  151 ? -0.007  -41.031 9.294    1.00 63.93  ? 155  LEU   B O    1 
ATOM   11292 C  CB   . LEU   B  2  151 ? 2.572   -42.943 9.652    1.00 64.29  ? 155  LEU   B CB   1 
ATOM   11293 C  CG   . LEU   B  2  151 ? 1.402   -43.889 9.378    1.00 70.06  ? 155  LEU   B CG   1 
ATOM   11294 C  CD1  . LEU   B  2  151 ? 1.938   -45.262 8.993    1.00 69.18  ? 155  LEU   B CD1  1 
ATOM   11295 C  CD2  . LEU   B  2  151 ? 0.469   -43.994 10.572   1.00 77.16  ? 155  LEU   B CD2  1 
ATOM   11296 H  H    . LEU   B  2  151 ? 1.026   -41.416 11.479   1.00 73.60  ? 155  LEU   B H    1 
ATOM   11297 H  HA   . LEU   B  2  151 ? 3.070   -40.948 9.775    1.00 74.85  ? 155  LEU   B HA   1 
ATOM   11298 H  HB2  . LEU   B  2  151 ? 3.142   -42.974 8.868    1.00 77.13  ? 155  LEU   B HB2  1 
ATOM   11299 H  HB3  . LEU   B  2  151 ? 3.043   -43.302 10.420   1.00 77.13  ? 155  LEU   B HB3  1 
ATOM   11300 H  HG   . LEU   B  2  151 ? 0.877   -43.534 8.644    1.00 84.05  ? 155  LEU   B HG   1 
ATOM   11301 H  HD11 . LEU   B  2  151 ? 1.191   -45.858 8.824    1.00 83.00  ? 155  LEU   B HD11 1 
ATOM   11302 H  HD12 . LEU   B  2  151 ? 2.479   -45.177 8.192    1.00 83.00  ? 155  LEU   B HD12 1 
ATOM   11303 H  HD13 . LEU   B  2  151 ? 2.477   -45.607 9.721    1.00 83.00  ? 155  LEU   B HD13 1 
ATOM   11304 H  HD21 . LEU   B  2  151 ? -0.230  -44.636 10.371   1.00 92.58  ? 155  LEU   B HD21 1 
ATOM   11305 H  HD22 . LEU   B  2  151 ? 0.976   -44.289 11.344   1.00 92.58  ? 155  LEU   B HD22 1 
ATOM   11306 H  HD23 . LEU   B  2  151 ? 0.078   -43.123 10.745   1.00 92.58  ? 155  LEU   B HD23 1 
ATOM   11307 N  N    . GLY   B  2  152 ? 1.638   -40.428 7.863    1.00 59.28  ? 156  GLY   B N    1 
ATOM   11308 C  CA   . GLY   B  2  152 ? 0.746   -39.960 6.823    1.00 58.23  ? 156  GLY   B CA   1 
ATOM   11309 C  C    . GLY   B  2  152 ? 1.215   -40.461 5.467    1.00 56.09  ? 156  GLY   B C    1 
ATOM   11310 O  O    . GLY   B  2  152 ? 2.270   -41.085 5.350    1.00 55.11  ? 156  GLY   B O    1 
ATOM   11311 H  H    . GLY   B  2  152 ? 2.471   -40.332 7.671    1.00 71.12  ? 156  GLY   B H    1 
ATOM   11312 H  HA2  . GLY   B  2  152 ? -0.153  -40.287 6.986    1.00 69.86  ? 156  GLY   B HA2  1 
ATOM   11313 H  HA3  . GLY   B  2  152 ? 0.731   -38.990 6.812    1.00 69.86  ? 156  GLY   B HA3  1 
ATOM   11314 N  N    . PHE   B  2  153 ? 0.410   -40.167 4.450    1.00 58.13  ? 157  PHE   B N    1 
ATOM   11315 C  CA   . PHE   B  2  153 ? 0.661   -40.707 3.121    1.00 57.95  ? 157  PHE   B CA   1 
ATOM   11316 C  C    . PHE   B  2  153 ? 0.434   -39.648 2.054    1.00 57.01  ? 157  PHE   B C    1 
ATOM   11317 O  O    . PHE   B  2  153 ? -0.481  -38.827 2.160    1.00 58.54  ? 157  PHE   B O    1 
ATOM   11318 C  CB   . PHE   B  2  153 ? -0.238  -41.919 2.836    1.00 60.10  ? 157  PHE   B CB   1 
ATOM   11319 C  CG   . PHE   B  2  153 ? 0.042   -42.581 1.518    1.00 59.47  ? 157  PHE   B CG   1 
ATOM   11320 C  CD1  . PHE   B  2  153 ? -0.580  -42.143 0.361    1.00 58.76  ? 157  PHE   B CD1  1 
ATOM   11321 C  CD2  . PHE   B  2  153 ? 0.933   -43.638 1.434    1.00 60.93  ? 157  PHE   B CD2  1 
ATOM   11322 C  CE1  . PHE   B  2  153 ? -0.321  -42.747 -0.855   1.00 62.49  ? 157  PHE   B CE1  1 
ATOM   11323 C  CE2  . PHE   B  2  153 ? 1.195   -44.247 0.221    1.00 59.26  ? 157  PHE   B CE2  1 
ATOM   11324 C  CZ   . PHE   B  2  153 ? 0.567   -43.801 -0.925   1.00 60.22  ? 157  PHE   B CZ   1 
ATOM   11325 H  H    . PHE   B  2  153 ? -0.283  -39.661 4.506    1.00 69.73  ? 157  PHE   B H    1 
ATOM   11326 H  HA   . PHE   B  2  153 ? 1.591   -40.978 3.068    1.00 69.52  ? 157  PHE   B HA   1 
ATOM   11327 H  HB2  . PHE   B  2  153 ? -0.102  -42.579 3.534    1.00 72.10  ? 157  PHE   B HB2  1 
ATOM   11328 H  HB3  . PHE   B  2  153 ? -1.163  -41.627 2.831    1.00 72.10  ? 157  PHE   B HB3  1 
ATOM   11329 H  HD1  . PHE   B  2  153 ? -1.180  -41.433 0.402    1.00 70.49  ? 157  PHE   B HD1  1 
ATOM   11330 H  HD2  . PHE   B  2  153 ? 1.359   -43.942 2.202    1.00 73.10  ? 157  PHE   B HD2  1 
ATOM   11331 H  HE1  . PHE   B  2  153 ? -0.745  -42.444 -1.625   1.00 74.97  ? 157  PHE   B HE1  1 
ATOM   11332 H  HE2  . PHE   B  2  153 ? 1.795   -44.956 0.177    1.00 71.10  ? 157  PHE   B HE2  1 
ATOM   11333 H  HZ   . PHE   B  2  153 ? 0.743   -44.209 -1.742   1.00 72.25  ? 157  PHE   B HZ   1 
ATOM   11334 N  N    . GLY   B  2  154 ? 1.276   -39.686 1.025    1.00 54.38  ? 158  GLY   B N    1 
ATOM   11335 C  CA   . GLY   B  2  154 ? 1.105   -38.846 -0.145   1.00 56.10  ? 158  GLY   B CA   1 
ATOM   11336 C  C    . GLY   B  2  154 ? 1.727   -39.532 -1.342   1.00 57.34  ? 158  GLY   B C    1 
ATOM   11337 O  O    . GLY   B  2  154 ? 2.560   -40.433 -1.202   1.00 57.12  ? 158  GLY   B O    1 
ATOM   11338 H  H    . GLY   B  2  154 ? 1.964   -40.200 0.982    1.00 65.24  ? 158  GLY   B H    1 
ATOM   11339 H  HA2  . GLY   B  2  154 ? 0.162   -38.699 -0.316   1.00 67.30  ? 158  GLY   B HA2  1 
ATOM   11340 H  HA3  . GLY   B  2  154 ? 1.539   -37.989 -0.007   1.00 67.30  ? 158  GLY   B HA3  1 
ATOM   11341 N  N    . SER   B  2  155 ? 1.310   -39.097 -2.529   1.00 56.76  ? 159  SER   B N    1 
ATOM   11342 C  CA   . SER   B  2  155 ? 1.746   -39.725 -3.767   1.00 55.87  ? 159  SER   B CA   1 
ATOM   11343 C  C    . SER   B  2  155 ? 2.088   -38.659 -4.796   1.00 54.84  ? 159  SER   B C    1 
ATOM   11344 O  O    . SER   B  2  155 ? 1.595   -37.529 -4.743   1.00 57.59  ? 159  SER   B O    1 
ATOM   11345 C  CB   . SER   B  2  155 ? 0.670   -40.669 -4.321   1.00 56.58  ? 159  SER   B CB   1 
ATOM   11346 O  OG   . SER   B  2  155 ? -0.562  -39.991 -4.493   1.00 59.34  ? 159  SER   B OG   1 
ATOM   11347 H  H    . SER   B  2  155 ? 0.772   -38.435 -2.641   1.00 68.10  ? 159  SER   B H    1 
ATOM   11348 H  HA   . SER   B  2  155 ? 2.552   -40.237 -3.596   1.00 67.02  ? 159  SER   B HA   1 
ATOM   11349 H  HB2  . SER   B  2  155 ? 0.964   -41.012 -5.180   1.00 67.88  ? 159  SER   B HB2  1 
ATOM   11350 H  HB3  . SER   B  2  155 ? 0.543   -41.402 -3.698   1.00 67.88  ? 159  SER   B HB3  1 
ATOM   11351 H  HG   . SER   B  2  155 ? -0.540  -39.529 -5.194   1.00 71.19  ? 159  SER   B HG   1 
ATOM   11352 N  N    . PHE   B  2  156 ? 2.946   -39.040 -5.741   1.00 50.54  ? 160  PHE   B N    1 
ATOM   11353 C  CA   . PHE   B  2  156 ? 3.354   -38.163 -6.828   1.00 49.19  ? 160  PHE   B CA   1 
ATOM   11354 C  C    . PHE   B  2  156 ? 3.585   -39.003 -8.073   1.00 48.56  ? 160  PHE   B C    1 
ATOM   11355 O  O    . PHE   B  2  156 ? 3.976   -40.170 -7.982   1.00 47.37  ? 160  PHE   B O    1 
ATOM   11356 C  CB   . PHE   B  2  156 ? 4.634   -37.388 -6.486   1.00 50.16  ? 160  PHE   B CB   1 
ATOM   11357 C  CG   . PHE   B  2  156 ? 5.873   -38.245 -6.459   1.00 51.84  ? 160  PHE   B CG   1 
ATOM   11358 C  CD1  . PHE   B  2  156 ? 6.604   -38.469 -7.617   1.00 56.23  ? 160  PHE   B CD1  1 
ATOM   11359 C  CD2  . PHE   B  2  156 ? 6.306   -38.827 -5.279   1.00 51.98  ? 160  PHE   B CD2  1 
ATOM   11360 C  CE1  . PHE   B  2  156 ? 7.739   -39.257 -7.597   1.00 58.45  ? 160  PHE   B CE1  1 
ATOM   11361 C  CE2  . PHE   B  2  156 ? 7.443   -39.615 -5.254   1.00 57.63  ? 160  PHE   B CE2  1 
ATOM   11362 C  CZ   . PHE   B  2  156 ? 8.160   -39.830 -6.414   1.00 59.44  ? 160  PHE   B CZ   1 
ATOM   11363 H  H    . PHE   B  2  156 ? 3.312   -39.818 -5.772   1.00 60.62  ? 160  PHE   B H    1 
ATOM   11364 H  HA   . PHE   B  2  156 ? 2.646   -37.523 -7.005   1.00 59.01  ? 160  PHE   B HA   1 
ATOM   11365 H  HB2  . PHE   B  2  156 ? 4.767   -36.696 -7.152   1.00 60.17  ? 160  PHE   B HB2  1 
ATOM   11366 H  HB3  . PHE   B  2  156 ? 4.532   -36.989 -5.608   1.00 60.17  ? 160  PHE   B HB3  1 
ATOM   11367 H  HD1  . PHE   B  2  156 ? 6.326   -38.084 -8.417   1.00 67.46  ? 160  PHE   B HD1  1 
ATOM   11368 H  HD2  . PHE   B  2  156 ? 5.828   -38.686 -4.495   1.00 62.36  ? 160  PHE   B HD2  1 
ATOM   11369 H  HE1  . PHE   B  2  156 ? 8.219   -39.400 -8.381   1.00 70.12  ? 160  PHE   B HE1  1 
ATOM   11370 H  HE2  . PHE   B  2  156 ? 7.724   -40.001 -4.456   1.00 69.14  ? 160  PHE   B HE2  1 
ATOM   11371 H  HZ   . PHE   B  2  156 ? 8.925   -40.359 -6.399   1.00 71.30  ? 160  PHE   B HZ   1 
ATOM   11372 N  N    . VAL   B  2  157 ? 3.326   -38.409 -9.239   1.00 54.02  ? 161  VAL   B N    1 
ATOM   11373 C  CA   . VAL   B  2  157 ? 3.751   -39.025 -10.490  1.00 56.50  ? 161  VAL   B CA   1 
ATOM   11374 C  C    . VAL   B  2  157 ? 4.583   -38.054 -11.320  1.00 52.02  ? 161  VAL   B C    1 
ATOM   11375 O  O    . VAL   B  2  157 ? 5.782   -38.274 -11.529  1.00 50.74  ? 161  VAL   B O    1 
ATOM   11376 C  CB   . VAL   B  2  157 ? 2.543   -39.532 -11.298  1.00 59.63  ? 161  VAL   B CB   1 
ATOM   11377 C  CG1  . VAL   B  2  157 ? 2.977   -39.925 -12.704  1.00 59.28  ? 161  VAL   B CG1  1 
ATOM   11378 C  CG2  . VAL   B  2  157 ? 1.894   -40.707 -10.585  1.00 62.83  ? 161  VAL   B CG2  1 
ATOM   11379 H  H    . VAL   B  2  157 ? 2.910   -37.662 -9.327   1.00 64.81  ? 161  VAL   B H    1 
ATOM   11380 H  HA   . VAL   B  2  157 ? 4.323   -39.776 -10.269  1.00 67.78  ? 161  VAL   B HA   1 
ATOM   11381 H  HB   . VAL   B  2  157 ? 1.886   -38.822 -11.373  1.00 71.54  ? 161  VAL   B HB   1 
ATOM   11382 H  HG11 . VAL   B  2  157 ? 2.286   -40.474 -13.106  1.00 71.12  ? 161  VAL   B HG11 1 
ATOM   11383 H  HG12 . VAL   B  2  157 ? 3.107   -39.120 -13.231  1.00 71.12  ? 161  VAL   B HG12 1 
ATOM   11384 H  HG13 . VAL   B  2  157 ? 3.807   -40.423 -12.651  1.00 71.12  ? 161  VAL   B HG13 1 
ATOM   11385 H  HG21 . VAL   B  2  157 ? 0.999   -40.454 -10.310  1.00 75.37  ? 161  VAL   B HG21 1 
ATOM   11386 H  HG22 . VAL   B  2  157 ? 1.852   -41.462 -11.193  1.00 75.37  ? 161  VAL   B HG22 1 
ATOM   11387 H  HG23 . VAL   B  2  157 ? 2.426   -40.938 -9.808   1.00 75.37  ? 161  VAL   B HG23 1 
ATOM   11388 N  N    . GLU   B  2  158 ? 3.969   -36.965 -11.778  1.00 51.60  ? 162  GLU   B N    1 
ATOM   11389 C  CA   . GLU   B  2  158 ? 4.622   -36.112 -12.766  1.00 52.02  ? 162  GLU   B CA   1 
ATOM   11390 C  C    . GLU   B  2  158 ? 3.747   -34.899 -13.047  1.00 52.44  ? 162  GLU   B C    1 
ATOM   11391 O  O    . GLU   B  2  158 ? 2.527   -34.937 -12.864  1.00 50.48  ? 162  GLU   B O    1 
ATOM   11392 C  CB   . GLU   B  2  158 ? 4.888   -36.886 -14.066  1.00 55.46  ? 162  GLU   B CB   1 
ATOM   11393 C  CG   . GLU   B  2  158 ? 5.689   -36.130 -15.110  1.00 63.04  ? 162  GLU   B CG   1 
ATOM   11394 C  CD   . GLU   B  2  158 ? 7.057   -35.720 -14.606  1.00 67.62  ? 162  GLU   B CD   1 
ATOM   11395 O  OE1  . GLU   B  2  158 ? 7.152   -34.678 -13.925  1.00 68.33  ? 162  GLU   B OE1  1 
ATOM   11396 O  OE2  . GLU   B  2  158 ? 8.035   -36.448 -14.880  1.00 68.32  ? 162  GLU   B OE2  1 
ATOM   11397 H  H    . GLU   B  2  158 ? 3.187   -36.703 -11.535  1.00 61.91  ? 162  GLU   B H    1 
ATOM   11398 H  HA   . GLU   B  2  158 ? 5.461   -35.786 -12.403  1.00 62.40  ? 162  GLU   B HA   1 
ATOM   11399 H  HB2  . GLU   B  2  158 ? 5.382   -37.692 -13.848  1.00 66.54  ? 162  GLU   B HB2  1 
ATOM   11400 H  HB3  . GLU   B  2  158 ? 4.035   -37.117 -14.465  1.00 66.54  ? 162  GLU   B HB3  1 
ATOM   11401 H  HG2  . GLU   B  2  158 ? 5.812   -36.697 -15.888  1.00 75.63  ? 162  GLU   B HG2  1 
ATOM   11402 H  HG3  . GLU   B  2  158 ? 5.207   -35.325 -15.359  1.00 75.63  ? 162  GLU   B HG3  1 
ATOM   11403 N  N    . LYS   B  2  159 ? 4.387   -33.824 -13.500  1.00 52.61  ? 163  LYS   B N    1 
ATOM   11404 C  CA   . LYS   B  2  159 ? 3.655   -32.667 -13.998  1.00 54.31  ? 163  LYS   B CA   1 
ATOM   11405 C  C    . LYS   B  2  159 ? 2.766   -33.111 -15.157  1.00 53.57  ? 163  LYS   B C    1 
ATOM   11406 O  O    . LYS   B  2  159 ? 3.288   -33.599 -16.172  1.00 54.96  ? 163  LYS   B O    1 
ATOM   11407 C  CB   . LYS   B  2  159 ? 4.608   -31.568 -14.465  1.00 58.29  ? 163  LYS   B CB   1 
ATOM   11408 C  CG   . LYS   B  2  159 ? 5.367   -30.852 -13.356  1.00 58.30  ? 163  LYS   B CG   1 
ATOM   11409 C  CD   . LYS   B  2  159 ? 6.238   -29.735 -13.929  1.00 58.83  ? 163  LYS   B CD   1 
ATOM   11410 C  CE   . LYS   B  2  159 ? 6.988   -28.971 -12.845  1.00 55.33  ? 163  LYS   B CE   1 
ATOM   11411 N  NZ   . LYS   B  2  159 ? 6.075   -28.302 -11.875  1.00 54.39  ? 163  LYS   B NZ   1 
ATOM   11412 H  H    . LYS   B  2  159 ? 5.242   -33.742 -13.529  1.00 63.11  ? 163  LYS   B H    1 
ATOM   11413 H  HA   . LYS   B  2  159 ? 3.111   -32.297 -13.285  1.00 65.15  ? 163  LYS   B HA   1 
ATOM   11414 H  HB2  . LYS   B  2  159 ? 5.265   -31.964 -15.057  1.00 69.93  ? 163  LYS   B HB2  1 
ATOM   11415 H  HB3  . LYS   B  2  159 ? 4.092   -30.899 -14.941  1.00 69.93  ? 163  LYS   B HB3  1 
ATOM   11416 H  HG2  . LYS   B  2  159 ? 4.737   -30.462 -12.731  1.00 69.94  ? 163  LYS   B HG2  1 
ATOM   11417 H  HG3  . LYS   B  2  159 ? 5.942   -31.485 -12.896  1.00 69.94  ? 163  LYS   B HG3  1 
ATOM   11418 H  HD2  . LYS   B  2  159 ? 6.891   -30.120 -14.534  1.00 70.57  ? 163  LYS   B HD2  1 
ATOM   11419 H  HD3  . LYS   B  2  159 ? 5.674   -29.106 -14.407  1.00 70.57  ? 163  LYS   B HD3  1 
ATOM   11420 H  HE2  . LYS   B  2  159 ? 7.548   -29.590 -12.351  1.00 66.38  ? 163  LYS   B HE2  1 
ATOM   11421 H  HE3  . LYS   B  2  159 ? 7.536   -28.287 -13.261  1.00 66.38  ? 163  LYS   B HE3  1 
ATOM   11422 H  HZ1  . LYS   B  2  159 ? 6.278   -27.438 -11.813  1.00 65.25  ? 163  LYS   B HZ1  1 
ATOM   11423 H  HZ2  . LYS   B  2  159 ? 5.231   -28.382 -12.147  1.00 65.25  ? 163  LYS   B HZ2  1 
ATOM   11424 H  HZ3  . LYS   B  2  159 ? 6.157   -28.677 -11.072  1.00 65.25  ? 163  LYS   B HZ3  1 
ATOM   11425 N  N    . PRO   B  2  160 ? 1.439   -32.967 -15.062  1.00 53.01  ? 164  PRO   B N    1 
ATOM   11426 C  CA   . PRO   B  2  160 ? 0.551   -33.499 -16.113  1.00 52.62  ? 164  PRO   B CA   1 
ATOM   11427 C  C    . PRO   B  2  160 ? 0.461   -32.585 -17.332  1.00 54.58  ? 164  PRO   B C    1 
ATOM   11428 O  O    . PRO   B  2  160 ? -0.609  -32.091 -17.700  1.00 59.12  ? 164  PRO   B O    1 
ATOM   11429 C  CB   . PRO   B  2  160 ? -0.786  -33.626 -15.370  1.00 51.19  ? 164  PRO   B CB   1 
ATOM   11430 C  CG   . PRO   B  2  160 ? -0.764  -32.496 -14.401  1.00 52.05  ? 164  PRO   B CG   1 
ATOM   11431 C  CD   . PRO   B  2  160 ? 0.674   -32.351 -13.961  1.00 54.27  ? 164  PRO   B CD   1 
ATOM   11432 H  HA   . PRO   B  2  160 ? 0.855   -34.376 -16.393  1.00 63.12  ? 164  PRO   B HA   1 
ATOM   11433 H  HB2  . PRO   B  2  160 ? -1.524  -33.540 -15.993  1.00 61.40  ? 164  PRO   B HB2  1 
ATOM   11434 H  HB3  . PRO   B  2  160 ? -0.835  -34.480 -14.913  1.00 61.40  ? 164  PRO   B HB3  1 
ATOM   11435 H  HG2  . PRO   B  2  160 ? -1.072  -31.686 -14.837  1.00 62.44  ? 164  PRO   B HG2  1 
ATOM   11436 H  HG3  . PRO   B  2  160 ? -1.334  -32.704 -13.645  1.00 62.44  ? 164  PRO   B HG3  1 
ATOM   11437 H  HD2  . PRO   B  2  160 ? 0.910   -31.416 -13.859  1.00 65.11  ? 164  PRO   B HD2  1 
ATOM   11438 H  HD3  . PRO   B  2  160 ? 0.829   -32.825 -13.128  1.00 65.11  ? 164  PRO   B HD3  1 
ATOM   11439 N  N    . VAL   B  2  161 ? 1.605   -32.360 -17.981  1.00 51.35  ? 165  VAL   B N    1 
ATOM   11440 C  CA   . VAL   B  2  161 ? 1.674   -31.527 -19.175  1.00 53.24  ? 165  VAL   B CA   1 
ATOM   11441 C  C    . VAL   B  2  161 ? 2.608   -32.174 -20.187  1.00 53.65  ? 165  VAL   B C    1 
ATOM   11442 O  O    . VAL   B  2  161 ? 3.442   -33.019 -19.853  1.00 54.59  ? 165  VAL   B O    1 
ATOM   11443 C  CB   . VAL   B  2  161 ? 2.154   -30.090 -18.865  1.00 55.19  ? 165  VAL   B CB   1 
ATOM   11444 C  CG1  . VAL   B  2  161 ? 1.106   -29.342 -18.062  1.00 55.49  ? 165  VAL   B CG1  1 
ATOM   11445 C  CG2  . VAL   B  2  161 ? 3.486   -30.116 -18.126  1.00 56.74  ? 165  VAL   B CG2  1 
ATOM   11446 H  H    . VAL   B  2  161 ? 2.364   -32.685 -17.743  1.00 61.60  ? 165  VAL   B H    1 
ATOM   11447 H  HA   . VAL   B  2  161 ? 0.789   -31.479 -19.568  1.00 63.87  ? 165  VAL   B HA   1 
ATOM   11448 H  HB   . VAL   B  2  161 ? 2.286   -29.617 -19.702  1.00 66.21  ? 165  VAL   B HB   1 
ATOM   11449 H  HG11 . VAL   B  2  161 ? 1.436   -28.451 -17.865  1.00 66.57  ? 165  VAL   B HG11 1 
ATOM   11450 H  HG12 . VAL   B  2  161 ? 0.290   -29.285 -18.583  1.00 66.57  ? 165  VAL   B HG12 1 
ATOM   11451 H  HG13 . VAL   B  2  161 ? 0.938   -29.823 -17.236  1.00 66.57  ? 165  VAL   B HG13 1 
ATOM   11452 H  HG21 . VAL   B  2  161 ? 3.769   -29.204 -17.954  1.00 68.07  ? 165  VAL   B HG21 1 
ATOM   11453 H  HG22 . VAL   B  2  161 ? 3.373   -30.591 -17.288  1.00 68.07  ? 165  VAL   B HG22 1 
ATOM   11454 H  HG23 . VAL   B  2  161 ? 4.144   -30.568 -18.676  1.00 68.07  ? 165  VAL   B HG23 1 
ATOM   11455 N  N    . SER   B  2  162 ? 2.451   -31.763 -21.442  1.00 52.43  ? 166  SER   B N    1 
ATOM   11456 C  CA   . SER   B  2  162 ? 3.369   -32.181 -22.485  1.00 52.22  ? 166  SER   B CA   1 
ATOM   11457 C  C    . SER   B  2  162 ? 4.730   -31.524 -22.260  1.00 54.93  ? 166  SER   B C    1 
ATOM   11458 O  O    . SER   B  2  162 ? 4.807   -30.395 -21.768  1.00 54.51  ? 166  SER   B O    1 
ATOM   11459 C  CB   . SER   B  2  162 ? 2.821   -31.799 -23.858  1.00 51.73  ? 166  SER   B CB   1 
ATOM   11460 O  OG   . SER   B  2  162 ? 3.522   -32.460 -24.894  1.00 57.51  ? 166  SER   B OG   1 
ATOM   11461 H  H    . SER   B  2  162 ? 1.821   -31.244 -21.712  1.00 62.89  ? 166  SER   B H    1 
ATOM   11462 H  HA   . SER   B  2  162 ? 3.482   -33.145 -22.469  1.00 62.64  ? 166  SER   B HA   1 
ATOM   11463 H  HB2  . SER   B  2  162 ? 1.885   -32.049 -23.903  1.00 62.05  ? 166  SER   B HB2  1 
ATOM   11464 H  HB3  . SER   B  2  162 ? 2.915   -30.841 -23.977  1.00 62.05  ? 166  SER   B HB3  1 
ATOM   11465 H  HG   . SER   B  2  162 ? 3.418   -32.049 -25.619  1.00 68.99  ? 166  SER   B HG   1 
ATOM   11466 N  N    . PRO   B  2  163 ? 5.830   -32.206 -22.617  1.00 57.08  ? 167  PRO   B N    1 
ATOM   11467 C  CA   . PRO   B  2  163 ? 5.955   -33.515 -23.263  1.00 58.15  ? 167  PRO   B CA   1 
ATOM   11468 C  C    . PRO   B  2  163 ? 6.114   -34.674 -22.285  1.00 56.40  ? 167  PRO   B C    1 
ATOM   11469 O  O    . PRO   B  2  163 ? 6.554   -35.749 -22.689  1.00 53.81  ? 167  PRO   B O    1 
ATOM   11470 C  CB   . PRO   B  2  163 ? 7.226   -33.350 -24.090  1.00 60.03  ? 167  PRO   B CB   1 
ATOM   11471 C  CG   . PRO   B  2  163 ? 8.087   -32.502 -23.206  1.00 58.75  ? 167  PRO   B CG   1 
ATOM   11472 C  CD   . PRO   B  2  163 ? 7.150   -31.572 -22.452  1.00 56.22  ? 167  PRO   B CD   1 
ATOM   11473 H  HA   . PRO   B  2  163 ? 5.187   -33.687 -23.829  1.00 69.77  ? 167  PRO   B HA   1 
ATOM   11474 H  HB2  . PRO   B  2  163 ? 7.634   -34.214 -24.262  1.00 72.02  ? 167  PRO   B HB2  1 
ATOM   11475 H  HB3  . PRO   B  2  163 ? 7.030   -32.904 -24.929  1.00 72.02  ? 167  PRO   B HB3  1 
ATOM   11476 H  HG2  . PRO   B  2  163 ? 8.575   -33.069 -22.588  1.00 70.48  ? 167  PRO   B HG2  1 
ATOM   11477 H  HG3  . PRO   B  2  163 ? 8.709   -31.993 -23.749  1.00 70.48  ? 167  PRO   B HG3  1 
ATOM   11478 H  HD2  . PRO   B  2  163 ? 7.394   -31.523 -21.514  1.00 67.44  ? 167  PRO   B HD2  1 
ATOM   11479 H  HD3  . PRO   B  2  163 ? 7.158   -30.685 -22.843  1.00 67.44  ? 167  PRO   B HD3  1 
ATOM   11480 N  N    . PHE   B  2  164 ? 5.771   -34.458 -21.017  1.00 56.28  ? 168  PHE   B N    1 
ATOM   11481 C  CA   . PHE   B  2  164 ? 5.951   -35.488 -20.002  1.00 56.78  ? 168  PHE   B CA   1 
ATOM   11482 C  C    . PHE   B  2  164 ? 4.808   -36.492 -19.965  1.00 53.83  ? 168  PHE   B C    1 
ATOM   11483 O  O    . PHE   B  2  164 ? 4.946   -37.535 -19.318  1.00 52.94  ? 168  PHE   B O    1 
ATOM   11484 C  CB   . PHE   B  2  164 ? 6.106   -34.839 -18.627  1.00 60.01  ? 168  PHE   B CB   1 
ATOM   11485 C  CG   . PHE   B  2  164 ? 7.209   -33.824 -18.561  1.00 58.97  ? 168  PHE   B CG   1 
ATOM   11486 C  CD1  . PHE   B  2  164 ? 8.439   -34.080 -19.141  1.00 60.10  ? 168  PHE   B CD1  1 
ATOM   11487 C  CD2  . PHE   B  2  164 ? 7.012   -32.607 -17.931  1.00 58.33  ? 168  PHE   B CD2  1 
ATOM   11488 C  CE1  . PHE   B  2  164 ? 9.456   -33.146 -19.087  1.00 62.51  ? 168  PHE   B CE1  1 
ATOM   11489 C  CE2  . PHE   B  2  164 ? 8.026   -31.668 -17.874  1.00 60.28  ? 168  PHE   B CE2  1 
ATOM   11490 C  CZ   . PHE   B  2  164 ? 9.247   -31.938 -18.453  1.00 62.24  ? 168  PHE   B CZ   1 
ATOM   11491 H  H    . PHE   B  2  164 ? 5.433   -33.725 -20.721  1.00 67.52  ? 168  PHE   B H    1 
ATOM   11492 H  HA   . PHE   B  2  164 ? 6.766   -35.978 -20.198  1.00 68.11  ? 168  PHE   B HA   1 
ATOM   11493 H  HB2  . PHE   B  2  164 ? 5.277   -34.391 -18.397  1.00 71.99  ? 168  PHE   B HB2  1 
ATOM   11494 H  HB3  . PHE   B  2  164 ? 6.301   -35.531 -17.975  1.00 71.99  ? 168  PHE   B HB3  1 
ATOM   11495 H  HD1  . PHE   B  2  164 ? 8.583   -34.890 -19.574  1.00 72.11  ? 168  PHE   B HD1  1 
ATOM   11496 H  HD2  . PHE   B  2  164 ? 6.189   -32.419 -17.542  1.00 69.97  ? 168  PHE   B HD2  1 
ATOM   11497 H  HE1  . PHE   B  2  164 ? 10.279  -33.331 -19.477  1.00 74.99  ? 168  PHE   B HE1  1 
ATOM   11498 H  HE2  . PHE   B  2  164 ? 7.883   -30.855 -17.446  1.00 72.31  ? 168  PHE   B HE2  1 
ATOM   11499 H  HZ   . PHE   B  2  164 ? 9.930   -31.307 -18.416  1.00 74.67  ? 168  PHE   B HZ   1 
ATOM   11500 N  N    . VAL   B  2  165 ? 3.689   -36.203 -20.632  1.00 53.76  ? 169  VAL   B N    1 
ATOM   11501 C  CA   . VAL   B  2  165 ? 2.557   -37.115 -20.709  1.00 55.11  ? 169  VAL   B CA   1 
ATOM   11502 C  C    . VAL   B  2  165 ? 2.021   -37.112 -22.134  1.00 56.24  ? 169  VAL   B C    1 
ATOM   11503 O  O    . VAL   B  2  165 ? 2.201   -36.153 -22.887  1.00 58.24  ? 169  VAL   B O    1 
ATOM   11504 C  CB   . VAL   B  2  165 ? 1.423   -36.740 -19.725  1.00 54.52  ? 169  VAL   B CB   1 
ATOM   11505 C  CG1  . VAL   B  2  165 ? 1.907   -36.837 -18.291  1.00 54.21  ? 169  VAL   B CG1  1 
ATOM   11506 C  CG2  . VAL   B  2  165 ? 0.886   -35.335 -20.015  1.00 55.79  ? 169  VAL   B CG2  1 
ATOM   11507 H  H    . VAL   B  2  165 ? 3.563   -35.466 -21.057  1.00 64.50  ? 169  VAL   B H    1 
ATOM   11508 H  HA   . VAL   B  2  165 ? 2.863   -38.010 -20.494  1.00 66.11  ? 169  VAL   B HA   1 
ATOM   11509 H  HB   . VAL   B  2  165 ? 0.694   -37.369 -19.844  1.00 65.41  ? 169  VAL   B HB   1 
ATOM   11510 H  HG11 . VAL   B  2  165 ? 1.159   -36.681 -17.694  1.00 65.04  ? 169  VAL   B HG11 1 
ATOM   11511 H  HG12 . VAL   B  2  165 ? 2.271   -37.723 -18.140  1.00 65.04  ? 169  VAL   B HG12 1 
ATOM   11512 H  HG13 . VAL   B  2  165 ? 2.594   -36.168 -18.144  1.00 65.04  ? 169  VAL   B HG13 1 
ATOM   11513 H  HG21 . VAL   B  2  165 ? -0.036  -35.282 -19.718  1.00 66.93  ? 169  VAL   B HG21 1 
ATOM   11514 H  HG22 . VAL   B  2  165 ? 1.426   -34.686 -19.539  1.00 66.93  ? 169  VAL   B HG22 1 
ATOM   11515 H  HG23 . VAL   B  2  165 ? 0.935   -35.170 -20.970  1.00 66.93  ? 169  VAL   B HG23 1 
ATOM   11516 N  N    . LYS   B  2  166 ? 1.358   -38.206 -22.498  1.00 55.45  ? 170  LYS   B N    1 
ATOM   11517 C  CA   . LYS   B  2  166 ? 0.545   -38.209 -23.705  1.00 57.00  ? 170  LYS   B CA   1 
ATOM   11518 C  C    . LYS   B  2  166 ? -0.652  -37.288 -23.506  1.00 58.28  ? 170  LYS   B C    1 
ATOM   11519 O  O    . LYS   B  2  166 ? -1.273  -37.275 -22.438  1.00 58.73  ? 170  LYS   B O    1 
ATOM   11520 C  CB   . LYS   B  2  166 ? 0.075   -39.624 -24.040  1.00 60.74  ? 170  LYS   B CB   1 
ATOM   11521 C  CG   . LYS   B  2  166 ? 1.162   -40.545 -24.573  1.00 63.27  ? 170  LYS   B CG   1 
ATOM   11522 C  CD   . LYS   B  2  166 ? 1.726   -40.056 -25.898  1.00 67.54  ? 170  LYS   B CD   1 
ATOM   11523 C  CE   . LYS   B  2  166 ? 2.672   -41.076 -26.511  1.00 75.03  ? 170  LYS   B CE   1 
ATOM   11524 N  NZ   . LYS   B  2  166 ? 1.985   -42.358 -26.831  1.00 82.69  ? 170  LYS   B NZ   1 
ATOM   11525 H  H    . LYS   B  2  166 ? 1.364   -38.951 -22.068  1.00 66.52  ? 170  LYS   B H    1 
ATOM   11526 H  HA   . LYS   B  2  166 ? 1.069   -37.894 -24.458  1.00 68.38  ? 170  LYS   B HA   1 
ATOM   11527 H  HB2  . LYS   B  2  166 ? -0.282  -40.029 -23.234  1.00 72.87  ? 170  LYS   B HB2  1 
ATOM   11528 H  HB3  . LYS   B  2  166 ? -0.618  -39.566 -24.717  1.00 72.87  ? 170  LYS   B HB3  1 
ATOM   11529 H  HG2  . LYS   B  2  166 ? 1.889   -40.585 -23.932  1.00 75.91  ? 170  LYS   B HG2  1 
ATOM   11530 H  HG3  . LYS   B  2  166 ? 0.791   -41.430 -24.710  1.00 75.91  ? 170  LYS   B HG3  1 
ATOM   11531 H  HD2  . LYS   B  2  166 ? 0.998   -39.903 -26.520  1.00 81.03  ? 170  LYS   B HD2  1 
ATOM   11532 H  HD3  . LYS   B  2  166 ? 2.217   -39.232 -25.753  1.00 81.03  ? 170  LYS   B HD3  1 
ATOM   11533 H  HE2  . LYS   B  2  166 ? 3.040   -40.716 -27.333  1.00 90.01  ? 170  LYS   B HE2  1 
ATOM   11534 H  HE3  . LYS   B  2  166 ? 3.387   -41.265 -25.883  1.00 90.01  ? 170  LYS   B HE3  1 
ATOM   11535 H  HZ1  . LYS   B  2  166 ? 2.517   -42.874 -27.324  1.00 99.21  ? 170  LYS   B HZ1  1 
ATOM   11536 H  HZ2  . LYS   B  2  166 ? 1.778   -42.789 -26.080  1.00 99.21  ? 170  LYS   B HZ2  1 
ATOM   11537 H  HZ3  . LYS   B  2  166 ? 1.237   -42.197 -27.287  1.00 99.21  ? 170  LYS   B HZ3  1 
ATOM   11538 N  N    . THR   B  2  167 ? -0.977  -36.512 -24.540  1.00 60.12  ? 171  THR   B N    1 
ATOM   11539 C  CA   . THR   B  2  167 ? -1.997  -35.475 -24.433  1.00 60.94  ? 171  THR   B CA   1 
ATOM   11540 C  C    . THR   B  2  167 ? -3.168  -35.706 -25.382  1.00 65.02  ? 171  THR   B C    1 
ATOM   11541 O  O    . THR   B  2  167 ? -3.908  -34.765 -25.688  1.00 64.42  ? 171  THR   B O    1 
ATOM   11542 C  CB   . THR   B  2  167 ? -1.378  -34.096 -24.673  1.00 57.61  ? 171  THR   B CB   1 
ATOM   11543 O  OG1  . THR   B  2  167 ? -0.495  -34.148 -25.800  1.00 62.01  ? 171  THR   B OG1  1 
ATOM   11544 C  CG2  . THR   B  2  167 ? -0.596  -33.646 -23.447  1.00 54.20  ? 171  THR   B CG2  1 
ATOM   11545 H  H    . THR   B  2  167 ? -0.616  -36.568 -25.319  1.00 72.13  ? 171  THR   B H    1 
ATOM   11546 H  HA   . THR   B  2  167 ? -2.355  -35.493 -23.532  1.00 73.11  ? 171  THR   B HA   1 
ATOM   11547 H  HB   . THR   B  2  167 ? -2.083  -33.452 -24.846  1.00 69.11  ? 171  THR   B HB   1 
ATOM   11548 H  HG1  . THR   B  2  167 ? 0.278   -34.364 -25.550  1.00 74.39  ? 171  THR   B HG1  1 
ATOM   11549 H  HG21 . THR   B  2  167 ? -0.363  -32.708 -23.528  1.00 65.02  ? 171  THR   B HG21 1 
ATOM   11550 H  HG22 . THR   B  2  167 ? -1.133  -33.769 -22.648  1.00 65.02  ? 171  THR   B HG22 1 
ATOM   11551 H  HG23 . THR   B  2  167 ? 0.218   -34.167 -23.363  1.00 65.02  ? 171  THR   B HG23 1 
ATOM   11552 N  N    . THR   B  2  168 ? -3.360  -36.936 -25.850  1.00 66.34  ? 172  THR   B N    1 
ATOM   11553 C  CA   . THR   B  2  168 ? -4.594  -37.249 -26.551  1.00 64.83  ? 172  THR   B CA   1 
ATOM   11554 C  C    . THR   B  2  168 ? -5.720  -37.444 -25.536  1.00 63.84  ? 172  THR   B C    1 
ATOM   11555 O  O    . THR   B  2  168 ? -5.466  -37.818 -24.388  1.00 62.06  ? 172  THR   B O    1 
ATOM   11556 C  CB   . THR   B  2  168 ? -4.438  -38.511 -27.391  1.00 67.78  ? 172  THR   B CB   1 
ATOM   11557 O  OG1  . THR   B  2  168 ? -4.264  -39.643 -26.530  1.00 68.44  ? 172  THR   B OG1  1 
ATOM   11558 C  CG2  . THR   B  2  168 ? -3.239  -38.399 -28.321  1.00 68.48  ? 172  THR   B CG2  1 
ATOM   11559 H  H    . THR   B  2  168 ? -2.805  -37.589 -25.775  1.00 79.59  ? 172  THR   B H    1 
ATOM   11560 H  HA   . THR   B  2  168 ? -4.826  -36.523 -27.153  1.00 77.77  ? 172  THR   B HA   1 
ATOM   11561 H  HB   . THR   B  2  168 ? -5.233  -38.633 -27.934  1.00 81.32  ? 172  THR   B HB   1 
ATOM   11562 H  HG1  . THR   B  2  168 ? -4.189  -40.343 -26.988  1.00 82.11  ? 172  THR   B HG1  1 
ATOM   11563 H  HG21 . THR   B  2  168 ? -3.157  -39.204 -28.855  1.00 82.15  ? 172  THR   B HG21 1 
ATOM   11564 H  HG22 . THR   B  2  168 ? -3.349  -37.638 -28.914  1.00 82.15  ? 172  THR   B HG22 1 
ATOM   11565 H  HG23 . THR   B  2  168 ? -2.428  -38.280 -27.803  1.00 82.15  ? 172  THR   B HG23 1 
ATOM   11566 N  N    . PRO   B  2  169 ? -6.973  -37.191 -25.927  1.00 67.26  ? 173  PRO   B N    1 
ATOM   11567 C  CA   . PRO   B  2  169 ? -8.077  -37.371 -24.967  1.00 64.97  ? 173  PRO   B CA   1 
ATOM   11568 C  C    . PRO   B  2  169 ? -8.071  -38.735 -24.296  1.00 62.35  ? 173  PRO   B C    1 
ATOM   11569 O  O    . PRO   B  2  169 ? -8.261  -38.825 -23.076  1.00 60.43  ? 173  PRO   B O    1 
ATOM   11570 C  CB   . PRO   B  2  169 ? -9.329  -37.162 -25.831  1.00 64.25  ? 173  PRO   B CB   1 
ATOM   11571 C  CG   . PRO   B  2  169 ? -8.871  -36.311 -26.965  1.00 65.52  ? 173  PRO   B CG   1 
ATOM   11572 C  CD   . PRO   B  2  169 ? -7.452  -36.724 -27.241  1.00 67.63  ? 173  PRO   B CD   1 
ATOM   11573 H  HA   . PRO   B  2  169 ? -8.039  -36.679 -24.288  1.00 77.94  ? 173  PRO   B HA   1 
ATOM   11574 H  HB2  . PRO   B  2  169 ? -9.658  -38.018 -26.149  1.00 77.08  ? 173  PRO   B HB2  1 
ATOM   11575 H  HB3  . PRO   B  2  169 ? -10.016 -36.713 -25.315  1.00 77.08  ? 173  PRO   B HB3  1 
ATOM   11576 H  HG2  . PRO   B  2  169 ? -9.432  -36.470 -27.741  1.00 78.61  ? 173  PRO   B HG2  1 
ATOM   11577 H  HG3  . PRO   B  2  169 ? -8.914  -35.376 -26.711  1.00 78.61  ? 173  PRO   B HG3  1 
ATOM   11578 H  HD2  . PRO   B  2  169 ? -7.422  -37.441 -27.894  1.00 81.14  ? 173  PRO   B HD2  1 
ATOM   11579 H  HD3  . PRO   B  2  169 ? -6.928  -35.970 -27.551  1.00 81.14  ? 173  PRO   B HD3  1 
ATOM   11580 N  N    . GLU   B  2  170 ? -7.843  -39.804 -25.062  1.00 64.53  ? 174  GLU   B N    1 
ATOM   11581 C  CA   . GLU   B  2  170 ? -7.846  -41.141 -24.479  1.00 68.80  ? 174  GLU   B CA   1 
ATOM   11582 C  C    . GLU   B  2  170 ? -6.734  -41.296 -23.449  1.00 68.67  ? 174  GLU   B C    1 
ATOM   11583 O  O    . GLU   B  2  170 ? -6.951  -41.856 -22.368  1.00 71.99  ? 174  GLU   B O    1 
ATOM   11584 C  CB   . GLU   B  2  170 ? -7.702  -42.196 -25.577  1.00 74.08  ? 174  GLU   B CB   1 
ATOM   11585 C  CG   . GLU   B  2  170 ? -8.843  -42.232 -26.586  1.00 85.40  ? 174  GLU   B CG   1 
ATOM   11586 C  CD   . GLU   B  2  170 ? -8.709  -41.182 -27.670  1.00 95.89  ? 174  GLU   B CD   1 
ATOM   11587 O  OE1  . GLU   B  2  170 ? -7.801  -40.330 -27.566  1.00 98.91  ? 174  GLU   B OE1  1 
ATOM   11588 O  OE2  . GLU   B  2  170 ? -9.510  -41.211 -28.627  1.00 101.06 ? 174  GLU   B OE2  1 
ATOM   11589 H  H    . GLU   B  2  170 ? -7.686  -39.780 -25.907  1.00 77.42  ? 174  GLU   B H    1 
ATOM   11590 H  HA   . GLU   B  2  170 ? -8.696  -41.282 -24.033  1.00 82.54  ? 174  GLU   B HA   1 
ATOM   11591 H  HB2  . GLU   B  2  170 ? -6.884  -42.018 -26.068  1.00 88.88  ? 174  GLU   B HB2  1 
ATOM   11592 H  HB3  . GLU   B  2  170 ? -7.655  -43.070 -25.160  1.00 88.88  ? 174  GLU   B HB3  1 
ATOM   11593 H  HG2  . GLU   B  2  170 ? -8.858  -43.102 -27.014  1.00 102.46 ? 174  GLU   B HG2  1 
ATOM   11594 H  HG3  . GLU   B  2  170 ? -9.680  -42.076 -26.121  1.00 102.46 ? 174  GLU   B HG3  1 
ATOM   11595 N  N    . GLU   B  2  171 ? -5.533  -40.805 -23.765  1.00 66.33  ? 175  GLU   B N    1 
ATOM   11596 C  CA   . GLU   B  2  171 ? -4.411  -40.955 -22.846  1.00 64.62  ? 175  GLU   B CA   1 
ATOM   11597 C  C    . GLU   B  2  171 ? -4.545  -40.036 -21.637  1.00 59.93  ? 175  GLU   B C    1 
ATOM   11598 O  O    . GLU   B  2  171 ? -4.070  -40.378 -20.547  1.00 58.28  ? 175  GLU   B O    1 
ATOM   11599 C  CB   . GLU   B  2  171 ? -3.099  -40.685 -23.582  1.00 67.66  ? 175  GLU   B CB   1 
ATOM   11600 C  CG   . GLU   B  2  171 ? -2.763  -41.710 -24.661  1.00 70.55  ? 175  GLU   B CG   1 
ATOM   11601 C  CD   . GLU   B  2  171 ? -1.942  -42.872 -24.140  1.00 78.03  ? 175  GLU   B CD   1 
ATOM   11602 O  OE1  . GLU   B  2  171 ? -1.649  -42.904 -22.926  1.00 81.52  ? 175  GLU   B OE1  1 
ATOM   11603 O  OE2  . GLU   B  2  171 ? -1.585  -43.753 -24.949  1.00 82.31  ? 175  GLU   B OE2  1 
ATOM   11604 H  H    . GLU   B  2  171 ? -5.348  -40.388 -24.493  1.00 79.58  ? 175  GLU   B H    1 
ATOM   11605 H  HA   . GLU   B  2  171 ? -4.390  -41.868 -22.520  1.00 77.52  ? 175  GLU   B HA   1 
ATOM   11606 H  HB2  . GLU   B  2  171 ? -3.157  -39.816 -24.011  1.00 81.18  ? 175  GLU   B HB2  1 
ATOM   11607 H  HB3  . GLU   B  2  171 ? -2.375  -40.688 -22.937  1.00 81.18  ? 175  GLU   B HB3  1 
ATOM   11608 H  HG2  . GLU   B  2  171 ? -3.589  -42.067 -25.024  1.00 84.64  ? 175  GLU   B HG2  1 
ATOM   11609 H  HG3  . GLU   B  2  171 ? -2.254  -41.275 -25.362  1.00 84.64  ? 175  GLU   B HG3  1 
ATOM   11610 N  N    . ILE   B  2  172 ? -5.180  -38.874 -21.802  1.00 60.35  ? 176  ILE   B N    1 
ATOM   11611 C  CA   . ILE   B  2  172 ? -5.424  -37.996 -20.661  1.00 61.34  ? 176  ILE   B CA   1 
ATOM   11612 C  C    . ILE   B  2  172 ? -6.373  -38.668 -19.677  1.00 64.45  ? 176  ILE   B C    1 
ATOM   11613 O  O    . ILE   B  2  172 ? -6.120  -38.705 -18.467  1.00 65.61  ? 176  ILE   B O    1 
ATOM   11614 C  CB   . ILE   B  2  172 ? -5.971  -36.635 -21.133  1.00 63.48  ? 176  ILE   B CB   1 
ATOM   11615 C  CG1  . ILE   B  2  172 ? -4.894  -35.872 -21.910  1.00 69.82  ? 176  ILE   B CG1  1 
ATOM   11616 C  CG2  . ILE   B  2  172 ? -6.459  -35.806 -19.943  1.00 58.83  ? 176  ILE   B CG2  1 
ATOM   11617 C  CD1  . ILE   B  2  172 ? -5.380  -34.580 -22.546  1.00 75.00  ? 176  ILE   B CD1  1 
ATOM   11618 H  H    . ILE   B  2  172 ? -5.475  -38.576 -22.553  1.00 72.40  ? 176  ILE   B H    1 
ATOM   11619 H  HA   . ILE   B  2  172 ? -4.581  -37.836 -20.208  1.00 73.59  ? 176  ILE   B HA   1 
ATOM   11620 H  HB   . ILE   B  2  172 ? -6.724  -36.798 -21.722  1.00 76.15  ? 176  ILE   B HB   1 
ATOM   11621 H  HG12 . ILE   B  2  172 ? -4.173  -35.647 -21.302  1.00 83.77  ? 176  ILE   B HG12 1 
ATOM   11622 H  HG13 . ILE   B  2  172 ? -4.563  -36.442 -22.622  1.00 83.77  ? 176  ILE   B HG13 1 
ATOM   11623 H  HG21 . ILE   B  2  172 ? -6.735  -34.931 -20.259  1.00 70.58  ? 176  ILE   B HG21 1 
ATOM   11624 H  HG22 . ILE   B  2  172 ? -7.210  -36.260 -19.528  1.00 70.58  ? 176  ILE   B HG22 1 
ATOM   11625 H  HG23 . ILE   B  2  172 ? -5.735  -35.713 -19.304  1.00 70.58  ? 176  ILE   B HG23 1 
ATOM   11626 H  HD11 . ILE   B  2  172 ? -4.671  -34.211 -23.094  1.00 89.99  ? 176  ILE   B HD11 1 
ATOM   11627 H  HD12 . ILE   B  2  172 ? -6.157  -34.770 -23.094  1.00 89.99  ? 176  ILE   B HD12 1 
ATOM   11628 H  HD13 . ILE   B  2  172 ? -5.616  -33.952 -21.845  1.00 89.99  ? 176  ILE   B HD13 1 
ATOM   11629 N  N    . ALA   B  2  173 ? -7.482  -39.209 -20.184  1.00 66.97  ? 177  ALA   B N    1 
ATOM   11630 C  CA   . ALA   B  2  173 ? -8.454  -39.860 -19.313  1.00 65.93  ? 177  ALA   B CA   1 
ATOM   11631 C  C    . ALA   B  2  173 ? -7.866  -41.106 -18.662  1.00 63.33  ? 177  ALA   B C    1 
ATOM   11632 O  O    . ALA   B  2  173 ? -8.135  -41.386 -17.488  1.00 61.33  ? 177  ALA   B O    1 
ATOM   11633 C  CB   . ALA   B  2  173 ? -9.710  -40.216 -20.107  1.00 64.19  ? 177  ALA   B CB   1 
ATOM   11634 H  H    . ALA   B  2  173 ? -7.692  -39.212 -21.019  1.00 80.34  ? 177  ALA   B H    1 
ATOM   11635 H  HA   . ALA   B  2  173 ? -8.705  -39.243 -18.609  1.00 79.10  ? 177  ALA   B HA   1 
ATOM   11636 H  HB1  . ALA   B  2  173 ? -10.341 -40.659 -19.518  1.00 77.01  ? 177  ALA   B HB1  1 
ATOM   11637 H  HB2  . ALA   B  2  173 ? -10.102 -39.402 -20.460  1.00 77.01  ? 177  ALA   B HB2  1 
ATOM   11638 H  HB3  . ALA   B  2  173 ? -9.466  -40.808 -20.836  1.00 77.01  ? 177  ALA   B HB3  1 
ATOM   11639 N  N    . ASN   B  2  174 ? -7.063  -41.864 -19.406  1.00 63.36  ? 178  ASN   B N    1 
ATOM   11640 C  CA   . ASN   B  2  174 ? -6.474  -43.103 -18.897  1.00 66.67  ? 178  ASN   B CA   1 
ATOM   11641 C  C    . ASN   B  2  174 ? -5.113  -43.286 -19.550  1.00 64.87  ? 178  ASN   B C    1 
ATOM   11642 O  O    . ASN   B  2  174 ? -5.005  -43.831 -20.656  1.00 65.26  ? 178  ASN   B O    1 
ATOM   11643 C  CB   . ASN   B  2  174 ? -7.376  -44.307 -19.170  1.00 70.96  ? 178  ASN   B CB   1 
ATOM   11644 C  CG   . ASN   B  2  174 ? -6.773  -45.611 -18.682  1.00 73.36  ? 178  ASN   B CG   1 
ATOM   11645 O  OD1  . ASN   B  2  174 ? -5.747  -45.621 -18.001  1.00 74.53  ? 178  ASN   B OD1  1 
ATOM   11646 N  ND2  . ASN   B  2  174 ? -7.414  -46.721 -19.025  1.00 76.72  ? 178  ASN   B ND2  1 
ATOM   11647 H  H    . ASN   B  2  174 ? -6.841  -41.682 -20.217  1.00 76.01  ? 178  ASN   B H    1 
ATOM   11648 H  HA   . ASN   B  2  174 ? -6.345  -43.032 -17.938  1.00 79.99  ? 178  ASN   B HA   1 
ATOM   11649 H  HB2  . ASN   B  2  174 ? -8.222  -44.178 -18.714  1.00 85.14  ? 178  ASN   B HB2  1 
ATOM   11650 H  HB3  . ASN   B  2  174 ? -7.522  -44.382 -20.126  1.00 85.14  ? 178  ASN   B HB3  1 
ATOM   11651 H  HD21 . ASN   B  2  174 ? -7.113  -47.487 -18.773  1.00 92.04  ? 178  ASN   B HD21 1 
ATOM   11652 H  HD22 . ASN   B  2  174 ? -8.130  -46.676 -19.498  1.00 92.04  ? 178  ASN   B HD22 1 
ATOM   11653 N  N    . PRO   B  2  175 ? -4.034  -42.841 -18.885  1.00 62.06  ? 179  PRO   B N    1 
ATOM   11654 C  CA   . PRO   B  2  175 ? -2.708  -42.893 -19.521  1.00 61.99  ? 179  PRO   B CA   1 
ATOM   11655 C  C    . PRO   B  2  175 ? -2.210  -44.304 -19.801  1.00 63.54  ? 179  PRO   B C    1 
ATOM   11656 O  O    . PRO   B  2  175 ? -1.149  -44.476 -20.409  1.00 61.42  ? 179  PRO   B O    1 
ATOM   11657 C  CB   . PRO   B  2  175 ? -1.806  -42.172 -18.508  1.00 59.40  ? 179  PRO   B CB   1 
ATOM   11658 C  CG   . PRO   B  2  175 ? -2.530  -42.257 -17.210  1.00 58.67  ? 179  PRO   B CG   1 
ATOM   11659 C  CD   . PRO   B  2  175 ? -3.984  -42.209 -17.555  1.00 59.60  ? 179  PRO   B CD   1 
ATOM   11660 H  HA   . PRO   B  2  175 ? -2.733  -42.402 -20.357  1.00 74.37  ? 179  PRO   B HA   1 
ATOM   11661 H  HB2  . PRO   B  2  175 ? -0.947  -42.619 -18.456  1.00 71.26  ? 179  PRO   B HB2  1 
ATOM   11662 H  HB3  . PRO   B  2  175 ? -1.682  -41.248 -18.776  1.00 71.26  ? 179  PRO   B HB3  1 
ATOM   11663 H  HG2  . PRO   B  2  175 ? -2.309  -43.090 -16.765  1.00 70.38  ? 179  PRO   B HG2  1 
ATOM   11664 H  HG3  . PRO   B  2  175 ? -2.284  -41.505 -16.648  1.00 70.38  ? 179  PRO   B HG3  1 
ATOM   11665 H  HD2  . PRO   B  2  175 ? -4.508  -42.713 -16.913  1.00 71.50  ? 179  PRO   B HD2  1 
ATOM   11666 H  HD3  . PRO   B  2  175 ? -4.300  -41.293 -17.595  1.00 71.50  ? 179  PRO   B HD3  1 
ATOM   11667 N  N    . CYS   B  2  176 ? -2.955  -45.318 -19.363  1.00 66.13  ? 180  CYS   B N    1 
ATOM   11668 C  CA   . CYS   B  2  176 ? -2.632  -46.708 -19.661  1.00 70.03  ? 180  CYS   B CA   1 
ATOM   11669 C  C    . CYS   B  2  176 ? -3.639  -47.348 -20.608  1.00 73.94  ? 180  CYS   B C    1 
ATOM   11670 O  O    . CYS   B  2  176 ? -3.612  -48.570 -20.791  1.00 78.93  ? 180  CYS   B O    1 
ATOM   11671 C  CB   . CYS   B  2  176 ? -2.550  -47.523 -18.370  1.00 68.93  ? 180  CYS   B CB   1 
ATOM   11672 S  SG   . CYS   B  2  176 ? -1.325  -46.933 -17.186  1.00 68.90  ? 180  CYS   B SG   1 
ATOM   11673 H  H    . CYS   B  2  176 ? -3.663  -45.223 -18.885  1.00 79.34  ? 180  CYS   B H    1 
ATOM   11674 H  HA   . CYS   B  2  176 ? -1.761  -46.732 -20.087  1.00 84.02  ? 180  CYS   B HA   1 
ATOM   11675 H  HB2  . CYS   B  2  176 ? -3.415  -47.497 -17.933  1.00 82.70  ? 180  CYS   B HB2  1 
ATOM   11676 H  HB3  . CYS   B  2  176 ? -2.320  -48.438 -18.597  1.00 82.70  ? 180  CYS   B HB3  1 
ATOM   11677 N  N    . SER   B  2  177 ? -4.523  -46.554 -21.217  1.00 72.74  ? 181  SER   B N    1 
ATOM   11678 C  CA   . SER   B  2  177 ? -5.534  -47.106 -22.111  1.00 74.50  ? 181  SER   B CA   1 
ATOM   11679 C  C    . SER   B  2  177 ? -4.925  -47.940 -23.231  1.00 72.75  ? 181  SER   B C    1 
ATOM   11680 O  O    . SER   B  2  177 ? -5.605  -48.815 -23.777  1.00 72.49  ? 181  SER   B O    1 
ATOM   11681 C  CB   . SER   B  2  177 ? -6.378  -45.975 -22.704  1.00 76.43  ? 181  SER   B CB   1 
ATOM   11682 O  OG   . SER   B  2  177 ? -5.567  -45.036 -23.389  1.00 80.02  ? 181  SER   B OG   1 
ATOM   11683 H  H    . SER   B  2  177 ? -4.556  -45.699 -21.129  1.00 87.26  ? 181  SER   B H    1 
ATOM   11684 H  HA   . SER   B  2  177 ? -6.119  -47.685 -21.597  1.00 89.38  ? 181  SER   B HA   1 
ATOM   11685 H  HB2  . SER   B  2  177 ? -7.017  -46.354 -23.328  1.00 91.70  ? 181  SER   B HB2  1 
ATOM   11686 H  HB3  . SER   B  2  177 ? -6.845  -45.522 -21.985  1.00 91.70  ? 181  SER   B HB3  1 
ATOM   11687 H  HG   . SER   B  2  177 ? -5.123  -44.583 -22.838  1.00 96.00  ? 181  SER   B HG   1 
ATOM   11688 N  N    . SER   B  2  178 ? -3.662  -47.693 -23.582  1.00 72.19  ? 182  SER   B N    1 
ATOM   11689 C  CA   . SER   B  2  178 ? -3.013  -48.398 -24.679  1.00 75.63  ? 182  SER   B CA   1 
ATOM   11690 C  C    . SER   B  2  178 ? -2.564  -49.808 -24.311  1.00 78.05  ? 182  SER   B C    1 
ATOM   11691 O  O    . SER   B  2  178 ? -2.189  -50.570 -25.209  1.00 78.94  ? 182  SER   B O    1 
ATOM   11692 C  CB   . SER   B  2  178 ? -1.799  -47.597 -25.162  1.00 74.59  ? 182  SER   B CB   1 
ATOM   11693 O  OG   . SER   B  2  178 ? -0.835  -47.470 -24.129  1.00 74.60  ? 182  SER   B OG   1 
ATOM   11694 H  H    . SER   B  2  178 ? -3.157  -47.115 -23.194  1.00 86.61  ? 182  SER   B H    1 
ATOM   11695 H  HA   . SER   B  2  178 ? -3.646  -48.473 -25.410  1.00 90.73  ? 182  SER   B HA   1 
ATOM   11696 H  HB2  . SER   B  2  178 ? -1.396  -48.057 -25.914  1.00 89.48  ? 182  SER   B HB2  1 
ATOM   11697 H  HB3  . SER   B  2  178 ? -2.091  -46.712 -25.431  1.00 89.48  ? 182  SER   B HB3  1 
ATOM   11698 H  HG   . SER   B  2  178 ? -0.221  -46.950 -24.371  1.00 89.50  ? 182  SER   B HG   1 
ATOM   11699 N  N    . ILE   B  2  179 ? -2.590  -50.174 -23.034  1.00 81.42  ? 183  ILE   B N    1 
ATOM   11700 C  CA   . ILE   B  2  179 ? -2.003  -51.436 -22.584  1.00 85.40  ? 183  ILE   B CA   1 
ATOM   11701 C  C    . ILE   B  2  179 ? -2.904  -52.612 -22.955  1.00 86.13  ? 183  ILE   B C    1 
ATOM   11702 O  O    . ILE   B  2  179 ? -2.445  -53.525 -23.656  1.00 86.73  ? 183  ILE   B O    1 
ATOM   11703 C  CB   . ILE   B  2  179 ? -1.712  -51.396 -21.073  1.00 87.65  ? 183  ILE   B CB   1 
ATOM   11704 C  CG1  . ILE   B  2  179 ? -0.745  -50.249 -20.744  1.00 85.63  ? 183  ILE   B CG1  1 
ATOM   11705 C  CG2  . ILE   B  2  179 ? -1.155  -52.731 -20.594  1.00 91.64  ? 183  ILE   B CG2  1 
ATOM   11706 C  CD1  . ILE   B  2  179 ? 0.571   -50.293 -21.501  1.00 86.92  ? 183  ILE   B CD1  1 
ATOM   11707 H  H    . ILE   B  2  179 ? -2.943  -49.708 -22.403  1.00 97.69  ? 183  ILE   B H    1 
ATOM   11708 H  HA   . ILE   B  2  179 ? -1.168  -51.569 -23.059  1.00 102.46 ? 183  ILE   B HA   1 
ATOM   11709 H  HB   . ILE   B  2  179 ? -2.547  -51.234 -20.606  1.00 105.16 ? 183  ILE   B HB   1 
ATOM   11710 H  HG12 . ILE   B  2  179 ? -1.179  -49.409 -20.961  1.00 102.73 ? 183  ILE   B HG12 1 
ATOM   11711 H  HG13 . ILE   B  2  179 ? -0.539  -50.281 -19.797  1.00 102.73 ? 183  ILE   B HG13 1 
ATOM   11712 H  HG21 . ILE   B  2  179 ? -0.879  -52.645 -19.669  1.00 109.95 ? 183  ILE   B HG21 1 
ATOM   11713 H  HG22 . ILE   B  2  179 ? -1.846  -53.407 -20.671  1.00 109.95 ? 183  ILE   B HG22 1 
ATOM   11714 H  HG23 . ILE   B  2  179 ? -0.394  -52.972 -21.146  1.00 109.95 ? 183  ILE   B HG23 1 
ATOM   11715 H  HD11 . ILE   B  2  179 ? 1.154   -49.597 -21.160  1.00 104.28 ? 183  ILE   B HD11 1 
ATOM   11716 H  HD12 . ILE   B  2  179 ? 0.981   -51.162 -21.370  1.00 104.28 ? 183  ILE   B HD12 1 
ATOM   11717 H  HD13 . ILE   B  2  179 ? 0.398   -50.148 -22.444  1.00 104.28 ? 183  ILE   B HD13 1 
ATOM   11718 N  N    . PRO   B  2  180 ? -4.177  -52.661 -22.518  1.00 87.76  ? 184  PRO   B N    1 
ATOM   11719 C  CA   . PRO   B  2  180 ? -4.914  -51.755 -21.633  1.00 84.57  ? 184  PRO   B CA   1 
ATOM   11720 C  C    . PRO   B  2  180 ? -4.788  -52.108 -20.154  1.00 80.33  ? 184  PRO   B C    1 
ATOM   11721 O  O    . PRO   B  2  180 ? -4.549  -53.261 -19.796  1.00 81.40  ? 184  PRO   B O    1 
ATOM   11722 C  CB   . PRO   B  2  180 ? -6.359  -51.928 -22.099  1.00 87.70  ? 184  PRO   B CB   1 
ATOM   11723 C  CG   . PRO   B  2  180 ? -6.425  -53.356 -22.500  1.00 92.12  ? 184  PRO   B CG   1 
ATOM   11724 C  CD   . PRO   B  2  180 ? -5.065  -53.701 -23.073  1.00 93.35  ? 184  PRO   B CD   1 
ATOM   11725 H  HA   . PRO   B  2  180 ? -4.621  -50.840 -21.766  1.00 101.46 ? 184  PRO   B HA   1 
ATOM   11726 H  HB2  . PRO   B  2  180 ? -6.972  -51.737 -21.372  1.00 105.22 ? 184  PRO   B HB2  1 
ATOM   11727 H  HB3  . PRO   B  2  180 ? -6.543  -51.343 -22.850  1.00 105.22 ? 184  PRO   B HB3  1 
ATOM   11728 H  HG2  . PRO   B  2  180 ? -6.617  -53.903 -21.722  1.00 110.52 ? 184  PRO   B HG2  1 
ATOM   11729 H  HG3  . PRO   B  2  180 ? -7.118  -53.474 -23.168  1.00 110.52 ? 184  PRO   B HG3  1 
ATOM   11730 H  HD2  . PRO   B  2  180 ? -4.784  -54.583 -22.784  1.00 112.00 ? 184  PRO   B HD2  1 
ATOM   11731 H  HD3  . PRO   B  2  180 ? -5.079  -53.658 -24.042  1.00 112.00 ? 184  PRO   B HD3  1 
ATOM   11732 N  N    . TYR   B  2  181 ? -4.943  -51.093 -19.310  1.00 75.75  ? 185  TYR   B N    1 
ATOM   11733 C  CA   . TYR   B  2  181 ? -4.839  -51.238 -17.866  1.00 74.23  ? 185  TYR   B CA   1 
ATOM   11734 C  C    . TYR   B  2  181 ? -5.489  -50.010 -17.252  1.00 69.91  ? 185  TYR   B C    1 
ATOM   11735 O  O    . TYR   B  2  181 ? -5.519  -48.943 -17.871  1.00 69.01  ? 185  TYR   B O    1 
ATOM   11736 C  CB   . TYR   B  2  181 ? -3.378  -51.371 -17.424  1.00 74.15  ? 185  TYR   B CB   1 
ATOM   11737 C  CG   . TYR   B  2  181 ? -3.183  -51.943 -16.037  1.00 74.10  ? 185  TYR   B CG   1 
ATOM   11738 C  CD1  . TYR   B  2  181 ? -3.170  -51.118 -14.921  1.00 73.09  ? 185  TYR   B CD1  1 
ATOM   11739 C  CD2  . TYR   B  2  181 ? -2.994  -53.307 -15.847  1.00 75.23  ? 185  TYR   B CD2  1 
ATOM   11740 C  CE1  . TYR   B  2  181 ? -2.983  -51.635 -13.652  1.00 75.41  ? 185  TYR   B CE1  1 
ATOM   11741 C  CE2  . TYR   B  2  181 ? -2.806  -53.834 -14.582  1.00 76.07  ? 185  TYR   B CE2  1 
ATOM   11742 C  CZ   . TYR   B  2  181 ? -2.802  -52.994 -13.488  1.00 77.56  ? 185  TYR   B CZ   1 
ATOM   11743 O  OH   . TYR   B  2  181 ? -2.615  -53.512 -12.226  1.00 80.88  ? 185  TYR   B OH   1 
ATOM   11744 H  H    . TYR   B  2  181 ? -5.113  -50.288 -19.558  1.00 90.88  ? 185  TYR   B H    1 
ATOM   11745 H  HA   . TYR   B  2  181 ? -5.307  -52.031 -17.560  1.00 89.05  ? 185  TYR   B HA   1 
ATOM   11746 H  HB2  . TYR   B  2  181 ? -2.921  -51.957 -18.048  1.00 88.96  ? 185  TYR   B HB2  1 
ATOM   11747 H  HB3  . TYR   B  2  181 ? -2.972  -50.491 -17.437  1.00 88.96  ? 185  TYR   B HB3  1 
ATOM   11748 H  HD1  . TYR   B  2  181 ? -3.288  -50.202 -15.029  1.00 87.68  ? 185  TYR   B HD1  1 
ATOM   11749 H  HD2  . TYR   B  2  181 ? -2.993  -53.875 -16.583  1.00 90.26  ? 185  TYR   B HD2  1 
ATOM   11750 H  HE1  . TYR   B  2  181 ? -2.980  -51.071 -12.913  1.00 90.47  ? 185  TYR   B HE1  1 
ATOM   11751 H  HE2  . TYR   B  2  181 ? -2.684  -54.749 -14.470  1.00 91.27  ? 185  TYR   B HE2  1 
ATOM   11752 H  HH   . TYR   B  2  181 ? -2.486  -52.890 -11.677  1.00 97.04  ? 185  TYR   B HH   1 
ATOM   11753 N  N    . PHE   B  2  182 ? -6.020  -50.162 -16.043  1.00 70.20  ? 186  PHE   B N    1 
ATOM   11754 C  CA   . PHE   B  2  182 ? -6.714  -49.062 -15.386  1.00 70.85  ? 186  PHE   B CA   1 
ATOM   11755 C  C    . PHE   B  2  182 ? -5.701  -48.219 -14.621  1.00 70.75  ? 186  PHE   B C    1 
ATOM   11756 O  O    . PHE   B  2  182 ? -5.159  -48.656 -13.599  1.00 73.57  ? 186  PHE   B O    1 
ATOM   11757 C  CB   . PHE   B  2  182 ? -7.811  -49.556 -14.451  1.00 70.45  ? 186  PHE   B CB   1 
ATOM   11758 C  CG   . PHE   B  2  182 ? -8.586  -48.440 -13.814  1.00 69.40  ? 186  PHE   B CG   1 
ATOM   11759 C  CD1  . PHE   B  2  182 ? -9.495  -47.705 -14.559  1.00 69.03  ? 186  PHE   B CD1  1 
ATOM   11760 C  CD2  . PHE   B  2  182 ? -8.386  -48.104 -12.486  1.00 67.95  ? 186  PHE   B CD2  1 
ATOM   11761 C  CE1  . PHE   B  2  182 ? -10.203 -46.666 -13.987  1.00 67.12  ? 186  PHE   B CE1  1 
ATOM   11762 C  CE2  . PHE   B  2  182 ? -9.092  -47.065 -11.905  1.00 65.68  ? 186  PHE   B CE2  1 
ATOM   11763 C  CZ   . PHE   B  2  182 ? -10.002 -46.344 -12.657  1.00 66.12  ? 186  PHE   B CZ   1 
ATOM   11764 H  H    . PHE   B  2  182 ? -5.991  -50.890 -15.587  1.00 84.22  ? 186  PHE   B H    1 
ATOM   11765 H  HA   . PHE   B  2  182 ? -7.128  -48.516 -16.073  1.00 85.00  ? 186  PHE   B HA   1 
ATOM   11766 H  HB2  . PHE   B  2  182 ? -8.433  -50.102 -14.956  1.00 84.52  ? 186  PHE   B HB2  1 
ATOM   11767 H  HB3  . PHE   B  2  182 ? -7.408  -50.082 -13.743  1.00 84.52  ? 186  PHE   B HB3  1 
ATOM   11768 H  HD1  . PHE   B  2  182 ? -9.630  -47.914 -15.455  1.00 82.82  ? 186  PHE   B HD1  1 
ATOM   11769 H  HD2  . PHE   B  2  182 ? -7.770  -48.581 -11.978  1.00 81.52  ? 186  PHE   B HD2  1 
ATOM   11770 H  HE1  . PHE   B  2  182 ? -10.814 -46.183 -14.495  1.00 80.53  ? 186  PHE   B HE1  1 
ATOM   11771 H  HE2  . PHE   B  2  182 ? -8.954  -46.851 -11.011  1.00 78.79  ? 186  PHE   B HE2  1 
ATOM   11772 H  HZ   . PHE   B  2  182 ? -10.477 -45.645 -12.270  1.00 79.33  ? 186  PHE   B HZ   1 
ATOM   11773 N  N    . CYS   B  2  183 ? -5.453  -47.012 -15.115  1.00 67.67  ? 187  CYS   B N    1 
ATOM   11774 C  CA   . CYS   B  2  183 ? -4.604  -46.036 -14.453  1.00 66.05  ? 187  CYS   B CA   1 
ATOM   11775 C  C    . CYS   B  2  183 ? -5.380  -44.739 -14.311  1.00 67.22  ? 187  CYS   B C    1 
ATOM   11776 O  O    . CYS   B  2  183 ? -6.175  -44.384 -15.187  1.00 71.85  ? 187  CYS   B O    1 
ATOM   11777 C  CB   . CYS   B  2  183 ? -3.318  -45.782 -15.240  1.00 64.59  ? 187  CYS   B CB   1 
ATOM   11778 S  SG   . CYS   B  2  183 ? -2.233  -47.219 -15.394  1.00 67.16  ? 187  CYS   B SG   1 
ATOM   11779 H  H    . CYS   B  2  183 ? -5.779  -46.727 -15.859  1.00 81.18  ? 187  CYS   B H    1 
ATOM   11780 H  HA   . CYS   B  2  183 ? -4.354  -46.358 -13.573  1.00 79.24  ? 187  CYS   B HA   1 
ATOM   11781 H  HB2  . CYS   B  2  183 ? -3.556  -45.498 -16.137  1.00 77.49  ? 187  CYS   B HB2  1 
ATOM   11782 H  HB3  . CYS   B  2  183 ? -2.815  -45.083 -14.793  1.00 77.49  ? 187  CYS   B HB3  1 
ATOM   11783 N  N    . LEU   B  2  184 ? -5.156  -44.040 -13.211  1.00 63.04  ? 188  LEU   B N    1 
ATOM   11784 C  CA   . LEU   B  2  184 ? -5.788  -42.744 -13.053  1.00 60.58  ? 188  LEU   B CA   1 
ATOM   11785 C  C    . LEU   B  2  184 ? -5.017  -41.689 -13.843  1.00 57.93  ? 188  LEU   B C    1 
ATOM   11786 O  O    . LEU   B  2  184 ? -3.820  -41.847 -14.096  1.00 60.98  ? 188  LEU   B O    1 
ATOM   11787 C  CB   . LEU   B  2  184 ? -5.847  -42.354 -11.582  1.00 60.13  ? 188  LEU   B CB   1 
ATOM   11788 C  CG   . LEU   B  2  184 ? -6.696  -43.276 -10.705  1.00 63.42  ? 188  LEU   B CG   1 
ATOM   11789 C  CD1  . LEU   B  2  184 ? -6.663  -42.806 -9.264   1.00 68.33  ? 188  LEU   B CD1  1 
ATOM   11790 C  CD2  . LEU   B  2  184 ? -8.130  -43.352 -11.210  1.00 62.04  ? 188  LEU   B CD2  1 
ATOM   11791 H  H    . LEU   B  2  184 ? -4.654  -44.288 -12.558  1.00 75.63  ? 188  LEU   B H    1 
ATOM   11792 H  HA   . LEU   B  2  184 ? -6.699  -42.776 -13.386  1.00 72.68  ? 188  LEU   B HA   1 
ATOM   11793 H  HB2  . LEU   B  2  184 ? -4.945  -42.362 -11.226  1.00 72.13  ? 188  LEU   B HB2  1 
ATOM   11794 H  HB3  . LEU   B  2  184 ? -6.222  -41.461 -11.515  1.00 72.13  ? 188  LEU   B HB3  1 
ATOM   11795 H  HG   . LEU   B  2  184 ? -6.326  -44.172 -10.745  1.00 76.08  ? 188  LEU   B HG   1 
ATOM   11796 H  HD11 . LEU   B  2  184 ? -7.228  -43.386 -8.729   1.00 81.97  ? 188  LEU   B HD11 1 
ATOM   11797 H  HD12 . LEU   B  2  184 ? -5.749  -42.844 -8.940   1.00 81.97  ? 188  LEU   B HD12 1 
ATOM   11798 H  HD13 . LEU   B  2  184 ? -6.991  -41.894 -9.222   1.00 81.97  ? 188  LEU   B HD13 1 
ATOM   11799 H  HD21 . LEU   B  2  184 ? -8.663  -43.855 -10.574  1.00 74.43  ? 188  LEU   B HD21 1 
ATOM   11800 H  HD22 . LEU   B  2  184 ? -8.482  -42.453 -11.298  1.00 74.43  ? 188  LEU   B HD22 1 
ATOM   11801 H  HD23 . LEU   B  2  184 ? -8.138  -43.797 -12.072  1.00 74.43  ? 188  LEU   B HD23 1 
ATOM   11802 N  N    . PRO   B  2  185 ? -5.682  -40.613 -14.260  1.00 58.02  ? 189  PRO   B N    1 
ATOM   11803 C  CA   . PRO   B  2  185 ? -4.979  -39.561 -15.002  1.00 58.14  ? 189  PRO   B CA   1 
ATOM   11804 C  C    . PRO   B  2  185 ? -3.763  -39.058 -14.235  1.00 58.73  ? 189  PRO   B C    1 
ATOM   11805 O  O    . PRO   B  2  185 ? -3.761  -38.992 -13.005  1.00 59.68  ? 189  PRO   B O    1 
ATOM   11806 C  CB   . PRO   B  2  185 ? -6.042  -38.465 -15.169  1.00 59.54  ? 189  PRO   B CB   1 
ATOM   11807 C  CG   . PRO   B  2  185 ? -7.177  -38.844 -14.263  1.00 60.69  ? 189  PRO   B CG   1 
ATOM   11808 C  CD   . PRO   B  2  185 ? -7.120  -40.328 -14.127  1.00 62.31  ? 189  PRO   B CD   1 
ATOM   11809 H  HA   . PRO   B  2  185 ? -4.703  -39.881 -15.875  1.00 69.75  ? 189  PRO   B HA   1 
ATOM   11810 H  HB2  . PRO   B  2  185 ? -5.669  -37.607 -14.912  1.00 71.43  ? 189  PRO   B HB2  1 
ATOM   11811 H  HB3  . PRO   B  2  185 ? -6.336  -38.435 -16.093  1.00 71.43  ? 189  PRO   B HB3  1 
ATOM   11812 H  HG2  . PRO   B  2  185 ? -7.062  -38.417 -13.401  1.00 72.81  ? 189  PRO   B HG2  1 
ATOM   11813 H  HG3  . PRO   B  2  185 ? -8.017  -38.569 -14.661  1.00 72.81  ? 189  PRO   B HG3  1 
ATOM   11814 H  HD2  . PRO   B  2  185 ? -7.451  -40.609 -13.260  1.00 74.76  ? 189  PRO   B HD2  1 
ATOM   11815 H  HD3  . PRO   B  2  185 ? -7.627  -40.761 -14.832  1.00 74.76  ? 189  PRO   B HD3  1 
ATOM   11816 N  N    . THR   B  2  186 ? -2.719  -38.712 -14.984  1.00 60.58  ? 190  THR   B N    1 
ATOM   11817 C  CA   . THR   B  2  186 ? -1.469  -38.283 -14.374  1.00 61.13  ? 190  THR   B CA   1 
ATOM   11818 C  C    . THR   B  2  186 ? -1.698  -37.082 -13.463  1.00 61.58  ? 190  THR   B C    1 
ATOM   11819 O  O    . THR   B  2  186 ? -2.527  -36.213 -13.746  1.00 63.50  ? 190  THR   B O    1 
ATOM   11820 C  CB   . THR   B  2  186 ? -0.445  -37.937 -15.457  1.00 57.72  ? 190  THR   B CB   1 
ATOM   11821 O  OG1  . THR   B  2  186 ? -0.401  -38.989 -16.430  1.00 55.97  ? 190  THR   B OG1  1 
ATOM   11822 C  CG2  . THR   B  2  186 ? 0.938   -37.770 -14.849  1.00 57.01  ? 190  THR   B CG2  1 
ATOM   11823 H  H    . THR   B  2  186 ? -2.710  -38.717 -15.844  1.00 72.67  ? 190  THR   B H    1 
ATOM   11824 H  HA   . THR   B  2  186 ? -1.109  -39.005 -13.835  1.00 73.34  ? 190  THR   B HA   1 
ATOM   11825 H  HB   . THR   B  2  186 ? -0.700  -37.106 -15.886  1.00 69.25  ? 190  THR   B HB   1 
ATOM   11826 H  HG1  . THR   B  2  186 ? 0.133   -39.588 -16.182  1.00 67.14  ? 190  THR   B HG1  1 
ATOM   11827 H  HG21 . THR   B  2  186 ? 1.584   -37.568 -15.544  1.00 68.40  ? 190  THR   B HG21 1 
ATOM   11828 H  HG22 . THR   B  2  186 ? 0.931   -37.044 -14.205  1.00 68.40  ? 190  THR   B HG22 1 
ATOM   11829 H  HG23 . THR   B  2  186 ? 1.204   -38.587 -14.399  1.00 68.40  ? 190  THR   B HG23 1 
ATOM   11830 N  N    . PHE   B  2  187 ? -0.956  -37.041 -12.358  1.00 61.21  ? 191  PHE   B N    1 
ATOM   11831 C  CA   . PHE   B  2  187 ? -1.086  -35.977 -11.374  1.00 59.09  ? 191  PHE   B CA   1 
ATOM   11832 C  C    . PHE   B  2  187 ? 0.284   -35.670 -10.790  1.00 58.06  ? 191  PHE   B C    1 
ATOM   11833 O  O    . PHE   B  2  187 ? 1.161   -36.536 -10.737  1.00 56.89  ? 191  PHE   B O    1 
ATOM   11834 C  CB   . PHE   B  2  187 ? -2.066  -36.363 -10.258  1.00 56.32  ? 191  PHE   B CB   1 
ATOM   11835 C  CG   . PHE   B  2  187 ? -1.660  -37.592 -9.494   1.00 56.86  ? 191  PHE   B CG   1 
ATOM   11836 C  CD1  . PHE   B  2  187 ? -2.061  -38.851 -9.912   1.00 55.40  ? 191  PHE   B CD1  1 
ATOM   11837 C  CD2  . PHE   B  2  187 ? -0.877  -37.489 -8.356   1.00 59.48  ? 191  PHE   B CD2  1 
ATOM   11838 C  CE1  . PHE   B  2  187 ? -1.688  -39.982 -9.210   1.00 57.27  ? 191  PHE   B CE1  1 
ATOM   11839 C  CE2  . PHE   B  2  187 ? -0.502  -38.616 -7.651   1.00 60.21  ? 191  PHE   B CE2  1 
ATOM   11840 C  CZ   . PHE   B  2  187 ? -0.909  -39.863 -8.079   1.00 60.60  ? 191  PHE   B CZ   1 
ATOM   11841 H  H    . PHE   B  2  187 ? -0.361  -37.628 -12.156  1.00 73.43  ? 191  PHE   B H    1 
ATOM   11842 H  HA   . PHE   B  2  187 ? -1.419  -35.172 -11.801  1.00 70.89  ? 191  PHE   B HA   1 
ATOM   11843 H  HB2  . PHE   B  2  187 ? -2.125  -35.629 -9.628   1.00 67.57  ? 191  PHE   B HB2  1 
ATOM   11844 H  HB3  . PHE   B  2  187 ? -2.936  -36.534 -10.652  1.00 67.57  ? 191  PHE   B HB3  1 
ATOM   11845 H  HD1  . PHE   B  2  187 ? -2.586  -38.936 -10.675  1.00 66.46  ? 191  PHE   B HD1  1 
ATOM   11846 H  HD2  . PHE   B  2  187 ? -0.600  -36.650 -8.063   1.00 71.36  ? 191  PHE   B HD2  1 
ATOM   11847 H  HE1  . PHE   B  2  187 ? -1.963  -40.821 -9.501   1.00 68.71  ? 191  PHE   B HE1  1 
ATOM   11848 H  HE2  . PHE   B  2  187 ? 0.023   -38.534 -6.888   1.00 72.24  ? 191  PHE   B HE2  1 
ATOM   11849 H  HZ   . PHE   B  2  187 ? -0.657  -40.623 -7.605   1.00 72.71  ? 191  PHE   B HZ   1 
ATOM   11850 N  N    . GLY   B  2  188 ? 0.460   -34.424 -10.353  1.00 57.80  ? 192  GLY   B N    1 
ATOM   11851 C  CA   . GLY   B  2  188 ? 1.729   -33.986 -9.805   1.00 55.51  ? 192  GLY   B CA   1 
ATOM   11852 C  C    . GLY   B  2  188 ? 1.996   -34.496 -8.404   1.00 52.49  ? 192  GLY   B C    1 
ATOM   11853 O  O    . GLY   B  2  188 ? 2.912   -35.297 -8.195   1.00 49.64  ? 192  GLY   B O    1 
ATOM   11854 H  H    . GLY   B  2  188 ? -0.147  -33.814 -10.366  1.00 69.34  ? 192  GLY   B H    1 
ATOM   11855 H  HA2  . GLY   B  2  188 ? 2.445   -34.298 -10.380  1.00 66.59  ? 192  GLY   B HA2  1 
ATOM   11856 H  HA3  . GLY   B  2  188 ? 1.744   -33.017 -9.780   1.00 66.59  ? 192  GLY   B HA3  1 
ATOM   11857 N  N    . PHE   B  2  189 ? 1.203   -34.043 -7.435   1.00 51.38  ? 193  PHE   B N    1 
ATOM   11858 C  CA   . PHE   B  2  189 ? 1.360   -34.480 -6.054   1.00 51.54  ? 193  PHE   B CA   1 
ATOM   11859 C  C    . PHE   B  2  189 ? 0.006   -34.480 -5.362   1.00 57.82  ? 193  PHE   B C    1 
ATOM   11860 O  O    . PHE   B  2  189 ? -0.704  -33.470 -5.380   1.00 56.18  ? 193  PHE   B O    1 
ATOM   11861 C  CB   . PHE   B  2  189 ? 2.337   -33.580 -5.288   1.00 51.62  ? 193  PHE   B CB   1 
ATOM   11862 C  CG   . PHE   B  2  189 ? 2.303   -33.785 -3.800   1.00 52.72  ? 193  PHE   B CG   1 
ATOM   11863 C  CD1  . PHE   B  2  189 ? 2.543   -35.036 -3.258   1.00 52.18  ? 193  PHE   B CD1  1 
ATOM   11864 C  CD2  . PHE   B  2  189 ? 2.029   -32.732 -2.944   1.00 55.49  ? 193  PHE   B CD2  1 
ATOM   11865 C  CE1  . PHE   B  2  189 ? 2.510   -35.233 -1.893   1.00 54.54  ? 193  PHE   B CE1  1 
ATOM   11866 C  CE2  . PHE   B  2  189 ? 1.996   -32.924 -1.577   1.00 55.16  ? 193  PHE   B CE2  1 
ATOM   11867 C  CZ   . PHE   B  2  189 ? 2.237   -34.177 -1.051   1.00 55.82  ? 193  PHE   B CZ   1 
ATOM   11868 H  H    . PHE   B  2  189 ? 0.564   -33.480 -7.554   1.00 61.63  ? 193  PHE   B H    1 
ATOM   11869 H  HA   . PHE   B  2  189 ? 1.705   -35.386 -6.051   1.00 61.83  ? 193  PHE   B HA   1 
ATOM   11870 H  HB2  . PHE   B  2  189 ? 3.238   -33.767 -5.593   1.00 61.92  ? 193  PHE   B HB2  1 
ATOM   11871 H  HB3  . PHE   B  2  189 ? 2.112   -32.653 -5.465   1.00 61.92  ? 193  PHE   B HB3  1 
ATOM   11872 H  HD1  . PHE   B  2  189 ? 2.729   -35.752 -3.822   1.00 62.59  ? 193  PHE   B HD1  1 
ATOM   11873 H  HD2  . PHE   B  2  189 ? 1.866   -31.886 -3.294   1.00 66.57  ? 193  PHE   B HD2  1 
ATOM   11874 H  HE1  . PHE   B  2  189 ? 2.672   -36.079 -1.542   1.00 65.43  ? 193  PHE   B HE1  1 
ATOM   11875 H  HE2  . PHE   B  2  189 ? 1.812   -32.209 -1.011   1.00 66.17  ? 193  PHE   B HE2  1 
ATOM   11876 H  HZ   . PHE   B  2  189 ? 2.214   -34.308 -0.131   1.00 66.97  ? 193  PHE   B HZ   1 
ATOM   11877 N  N    . LYS   B  2  190 ? -0.338  -35.610 -4.750   1.00 62.90  ? 194  LYS   B N    1 
ATOM   11878 C  CA   . LYS   B  2  190 ? -1.579  -35.769 -4.001   1.00 65.11  ? 194  LYS   B CA   1 
ATOM   11879 C  C    . LYS   B  2  190 ? -1.232  -35.987 -2.534   1.00 65.13  ? 194  LYS   B C    1 
ATOM   11880 O  O    . LYS   B  2  190 ? -0.645  -37.014 -2.177   1.00 64.20  ? 194  LYS   B O    1 
ATOM   11881 C  CB   . LYS   B  2  190 ? -2.400  -36.939 -4.540   1.00 66.29  ? 194  LYS   B CB   1 
ATOM   11882 C  CG   . LYS   B  2  190 ? -3.171  -36.646 -5.816   1.00 69.42  ? 194  LYS   B CG   1 
ATOM   11883 C  CD   . LYS   B  2  190 ? -3.888  -37.891 -6.327   1.00 72.12  ? 194  LYS   B CD   1 
ATOM   11884 C  CE   . LYS   B  2  190 ? -4.696  -37.600 -7.582   1.00 79.64  ? 194  LYS   B CE   1 
ATOM   11885 N  NZ   . LYS   B  2  190 ? -5.301  -38.833 -8.163   1.00 83.52  ? 194  LYS   B NZ   1 
ATOM   11886 H  H    . LYS   B  2  190 ? 0.147   -36.321 -4.756   1.00 75.46  ? 194  LYS   B H    1 
ATOM   11887 H  HA   . LYS   B  2  190 ? -2.104  -34.957 -4.082   1.00 78.12  ? 194  LYS   B HA   1 
ATOM   11888 H  HB2  . LYS   B  2  190 ? -1.799  -37.677 -4.725   1.00 79.53  ? 194  LYS   B HB2  1 
ATOM   11889 H  HB3  . LYS   B  2  190 ? -3.045  -37.199 -3.863   1.00 79.53  ? 194  LYS   B HB3  1 
ATOM   11890 H  HG2  . LYS   B  2  190 ? -3.835  -35.960 -5.642   1.00 83.28  ? 194  LYS   B HG2  1 
ATOM   11891 H  HG3  . LYS   B  2  190 ? -2.555  -36.344 -6.502   1.00 83.28  ? 194  LYS   B HG3  1 
ATOM   11892 H  HD2  . LYS   B  2  190 ? -3.232  -38.574 -6.539   1.00 86.52  ? 194  LYS   B HD2  1 
ATOM   11893 H  HD3  . LYS   B  2  190 ? -4.494  -38.215 -5.642   1.00 86.52  ? 194  LYS   B HD3  1 
ATOM   11894 H  HE2  . LYS   B  2  190 ? -5.415  -36.987 -7.362   1.00 95.54  ? 194  LYS   B HE2  1 
ATOM   11895 H  HE3  . LYS   B  2  190 ? -4.115  -37.206 -8.250   1.00 95.54  ? 194  LYS   B HE3  1 
ATOM   11896 H  HZ1  . LYS   B  2  190 ? -5.743  -38.633 -8.909   1.00 100.21 ? 194  LYS   B HZ1  1 
ATOM   11897 H  HZ2  . LYS   B  2  190 ? -4.664  -39.424 -8.354   1.00 100.21 ? 194  LYS   B HZ2  1 
ATOM   11898 H  HZ3  . LYS   B  2  190 ? -5.867  -39.198 -7.581   1.00 100.21 ? 194  LYS   B HZ3  1 
ATOM   11899 N  N    . HIS   B  2  191 ? -1.582  -35.020 -1.689   1.00 65.95  ? 195  HIS   B N    1 
ATOM   11900 C  CA   . HIS   B  2  191 ? -1.532  -35.212 -0.243   1.00 62.06  ? 195  HIS   B CA   1 
ATOM   11901 C  C    . HIS   B  2  191 ? -2.834  -35.881 0.180    1.00 61.25  ? 195  HIS   B C    1 
ATOM   11902 O  O    . HIS   B  2  191 ? -3.911  -35.288 0.064    1.00 63.45  ? 195  HIS   B O    1 
ATOM   11903 C  CB   . HIS   B  2  191 ? -1.331  -33.882 0.476    1.00 59.31  ? 195  HIS   B CB   1 
ATOM   11904 C  CG   . HIS   B  2  191 ? -1.433  -33.983 1.966    1.00 59.90  ? 195  HIS   B CG   1 
ATOM   11905 N  ND1  . HIS   B  2  191 ? -1.024  -35.098 2.665    1.00 59.47  ? 195  HIS   B ND1  1 
ATOM   11906 C  CD2  . HIS   B  2  191 ? -1.896  -33.109 2.890    1.00 62.41  ? 195  HIS   B CD2  1 
ATOM   11907 C  CE1  . HIS   B  2  191 ? -1.232  -34.907 3.956    1.00 62.61  ? 195  HIS   B CE1  1 
ATOM   11908 N  NE2  . HIS   B  2  191 ? -1.759  -33.708 4.119    1.00 63.08  ? 195  HIS   B NE2  1 
ATOM   11909 H  H    . HIS   B  2  191 ? -1.854  -34.241 -1.930   1.00 79.12  ? 195  HIS   B H    1 
ATOM   11910 H  HA   . HIS   B  2  191 ? -0.785  -35.784 -0.009   1.00 74.45  ? 195  HIS   B HA   1 
ATOM   11911 H  HB2  . HIS   B  2  191 ? -0.448  -33.542 0.262    1.00 71.15  ? 195  HIS   B HB2  1 
ATOM   11912 H  HB3  . HIS   B  2  191 ? -2.009  -33.258 0.174    1.00 71.15  ? 195  HIS   B HB3  1 
ATOM   11913 H  HD2  . HIS   B  2  191 ? -2.243  -32.262 2.724    1.00 74.88  ? 195  HIS   B HD2  1 
ATOM   11914 H  HE1  . HIS   B  2  191 ? -1.039  -35.514 4.634    1.00 75.12  ? 195  HIS   B HE1  1 
ATOM   11915 H  HE2  . HIS   B  2  191 ? -1.981  -33.358 4.873    1.00 75.67  ? 195  HIS   B HE2  1 
ATOM   11916 N  N    . ILE   B  2  192 ? -2.742  -37.112 0.666    1.00 61.73  ? 196  ILE   B N    1 
ATOM   11917 C  CA   . ILE   B  2  192 ? -3.902  -37.971 0.864    1.00 64.23  ? 196  ILE   B CA   1 
ATOM   11918 C  C    . ILE   B  2  192 ? -4.249  -38.113 2.342    1.00 60.54  ? 196  ILE   B C    1 
ATOM   11919 O  O    . ILE   B  2  192 ? -5.406  -37.955 2.732    1.00 59.73  ? 196  ILE   B O    1 
ATOM   11920 C  CB   . ILE   B  2  192 ? -3.677  -39.352 0.209    1.00 69.38  ? 196  ILE   B CB   1 
ATOM   11921 C  CG1  . ILE   B  2  192 ? -3.347  -39.177 -1.278   1.00 70.17  ? 196  ILE   B CG1  1 
ATOM   11922 C  CG2  . ILE   B  2  192 ? -4.908  -40.227 0.382    1.00 73.91  ? 196  ILE   B CG2  1 
ATOM   11923 C  CD1  . ILE   B  2  192 ? -2.953  -40.456 -1.989   1.00 73.98  ? 196  ILE   B CD1  1 
ATOM   11924 H  H    . ILE   B  2  192 ? -2.000  -37.482 0.894    1.00 74.06  ? 196  ILE   B H    1 
ATOM   11925 H  HA   . ILE   B  2  192 ? -4.665  -37.557 0.431    1.00 77.06  ? 196  ILE   B HA   1 
ATOM   11926 H  HB   . ILE   B  2  192 ? -2.928  -39.787 0.646    1.00 83.24  ? 196  ILE   B HB   1 
ATOM   11927 H  HG12 . ILE   B  2  192 ? -4.129  -38.821 -1.728   1.00 84.19  ? 196  ILE   B HG12 1 
ATOM   11928 H  HG13 . ILE   B  2  192 ? -2.606  -38.556 -1.359   1.00 84.19  ? 196  ILE   B HG13 1 
ATOM   11929 H  HG21 . ILE   B  2  192 ? -4.760  -41.074 -0.067   1.00 88.68  ? 196  ILE   B HG21 1 
ATOM   11930 H  HG22 . ILE   B  2  192 ? -5.058  -40.377 1.329    1.00 88.68  ? 196  ILE   B HG22 1 
ATOM   11931 H  HG23 . ILE   B  2  192 ? -5.674  -39.775 -0.006   1.00 88.68  ? 196  ILE   B HG23 1 
ATOM   11932 H  HD11 . ILE   B  2  192 ? -2.717  -40.248 -2.907   1.00 88.75  ? 196  ILE   B HD11 1 
ATOM   11933 H  HD12 . ILE   B  2  192 ? -2.192  -40.849 -1.533   1.00 88.75  ? 196  ILE   B HD12 1 
ATOM   11934 H  HD13 . ILE   B  2  192 ? -3.703  -41.071 -1.972   1.00 88.75  ? 196  ILE   B HD13 1 
ATOM   11935 N  N    . LEU   B  2  193 ? -3.260  -38.408 3.178    1.00 62.12  ? 197  LEU   B N    1 
ATOM   11936 C  CA   . LEU   B  2  193 ? -3.488  -38.653 4.602    1.00 60.85  ? 197  LEU   B CA   1 
ATOM   11937 C  C    . LEU   B  2  193 ? -2.570  -37.777 5.441    1.00 57.78  ? 197  LEU   B C    1 
ATOM   11938 O  O    . LEU   B  2  193 ? -1.340  -37.986 5.428    1.00 55.56  ? 197  LEU   B O    1 
ATOM   11939 C  CB   . LEU   B  2  193 ? -3.262  -40.126 4.938    1.00 60.76  ? 197  LEU   B CB   1 
ATOM   11940 C  CG   . LEU   B  2  193 ? -3.318  -40.499 6.424    1.00 60.98  ? 197  LEU   B CG   1 
ATOM   11941 C  CD1  . LEU   B  2  193 ? -4.668  -40.144 7.031    1.00 59.71  ? 197  LEU   B CD1  1 
ATOM   11942 C  CD2  . LEU   B  2  193 ? -3.015  -41.978 6.621    1.00 63.67  ? 197  LEU   B CD2  1 
ATOM   11943 H  H    . LEU   B  2  193 ? -2.436  -38.475 2.943    1.00 74.53  ? 197  LEU   B H    1 
ATOM   11944 H  HA   . LEU   B  2  193 ? -4.404  -38.412 4.812    1.00 73.00  ? 197  LEU   B HA   1 
ATOM   11945 H  HB2  . LEU   B  2  193 ? -3.945  -40.647 4.487    1.00 72.89  ? 197  LEU   B HB2  1 
ATOM   11946 H  HB3  . LEU   B  2  193 ? -2.384  -40.379 4.613    1.00 72.89  ? 197  LEU   B HB3  1 
ATOM   11947 H  HG   . LEU   B  2  193 ? -2.641  -39.986 6.892    1.00 73.16  ? 197  LEU   B HG   1 
ATOM   11948 H  HD11 . LEU   B  2  193 ? -4.669  -40.397 7.968    1.00 71.63  ? 197  LEU   B HD11 1 
ATOM   11949 H  HD12 . LEU   B  2  193 ? -4.812  -39.189 6.946    1.00 71.63  ? 197  LEU   B HD12 1 
ATOM   11950 H  HD13 . LEU   B  2  193 ? -5.364  -40.627 6.558    1.00 71.63  ? 197  LEU   B HD13 1 
ATOM   11951 H  HD21 . LEU   B  2  193 ? -3.008  -42.174 7.571    1.00 76.38  ? 197  LEU   B HD21 1 
ATOM   11952 H  HD22 . LEU   B  2  193 ? -3.702  -42.502 6.180    1.00 76.38  ? 197  LEU   B HD22 1 
ATOM   11953 H  HD23 . LEU   B  2  193 ? -2.148  -42.177 6.235    1.00 76.38  ? 197  LEU   B HD23 1 
ATOM   11954 N  N    . PRO   B  2  194 ? -3.100  -36.804 6.182    1.00 57.84  ? 198  PRO   B N    1 
ATOM   11955 C  CA   . PRO   B  2  194 ? -2.259  -36.086 7.144    1.00 58.31  ? 198  PRO   B CA   1 
ATOM   11956 C  C    . PRO   B  2  194 ? -1.759  -37.028 8.228    1.00 58.03  ? 198  PRO   B C    1 
ATOM   11957 O  O    . PRO   B  2  194 ? -2.287  -38.123 8.433    1.00 59.48  ? 198  PRO   B O    1 
ATOM   11958 C  CB   . PRO   B  2  194 ? -3.195  -35.014 7.717    1.00 59.05  ? 198  PRO   B CB   1 
ATOM   11959 C  CG   . PRO   B  2  194 ? -4.319  -34.908 6.739    1.00 55.31  ? 198  PRO   B CG   1 
ATOM   11960 C  CD   . PRO   B  2  194 ? -4.476  -36.278 6.159    1.00 56.40  ? 198  PRO   B CD   1 
ATOM   11961 H  HA   . PRO   B  2  194 ? -1.510  -35.653 6.704    1.00 69.95  ? 198  PRO   B HA   1 
ATOM   11962 H  HB2  . PRO   B  2  194 ? -3.520  -35.292 8.588    1.00 70.84  ? 198  PRO   B HB2  1 
ATOM   11963 H  HB3  . PRO   B  2  194 ? -2.722  -34.170 7.794    1.00 70.84  ? 198  PRO   B HB3  1 
ATOM   11964 H  HG2  . PRO   B  2  194 ? -5.129  -34.633 7.198    1.00 66.35  ? 198  PRO   B HG2  1 
ATOM   11965 H  HG3  . PRO   B  2  194 ? -4.095  -34.265 6.049    1.00 66.35  ? 198  PRO   B HG3  1 
ATOM   11966 H  HD2  . PRO   B  2  194 ? -5.064  -36.821 6.707    1.00 67.66  ? 198  PRO   B HD2  1 
ATOM   11967 H  HD3  . PRO   B  2  194 ? -4.815  -36.233 5.252    1.00 67.66  ? 198  PRO   B HD3  1 
ATOM   11968 N  N    . LEU   B  2  195 ? -0.720  -36.585 8.930    1.00 56.98  ? 199  LEU   B N    1 
ATOM   11969 C  CA   . LEU   B  2  195 ? -0.120  -37.408 9.971    1.00 56.39  ? 199  LEU   B CA   1 
ATOM   11970 C  C    . LEU   B  2  195 ? -1.159  -37.785 11.019   1.00 57.15  ? 199  LEU   B C    1 
ATOM   11971 O  O    . LEU   B  2  195 ? -1.905  -36.933 11.511   1.00 55.53  ? 199  LEU   B O    1 
ATOM   11972 C  CB   . LEU   B  2  195 ? 1.047   -36.663 10.615   1.00 58.71  ? 199  LEU   B CB   1 
ATOM   11973 C  CG   . LEU   B  2  195 ? 2.236   -36.437 9.678    1.00 63.12  ? 199  LEU   B CG   1 
ATOM   11974 C  CD1  . LEU   B  2  195 ? 3.154   -35.358 10.219   1.00 68.09  ? 199  LEU   B CD1  1 
ATOM   11975 C  CD2  . LEU   B  2  195 ? 3.008   -37.729 9.466    1.00 60.41  ? 199  LEU   B CD2  1 
ATOM   11976 H  H    . LEU   B  2  195 ? -0.347  -35.817 8.823    1.00 68.35  ? 199  LEU   B H    1 
ATOM   11977 H  HA   . LEU   B  2  195 ? 0.221   -38.227 9.580    1.00 67.65  ? 199  LEU   B HA   1 
ATOM   11978 H  HB2  . LEU   B  2  195 ? 0.735   -35.794 10.911   1.00 70.44  ? 199  LEU   B HB2  1 
ATOM   11979 H  HB3  . LEU   B  2  195 ? 1.363   -37.178 11.374   1.00 70.44  ? 199  LEU   B HB3  1 
ATOM   11980 H  HG   . LEU   B  2  195 ? 1.898   -36.140 8.818    1.00 75.72  ? 199  LEU   B HG   1 
ATOM   11981 H  HD11 . LEU   B  2  195 ? 3.936   -35.294 9.649    1.00 81.69  ? 199  LEU   B HD11 1 
ATOM   11982 H  HD12 . LEU   B  2  195 ? 2.678   -34.513 10.225   1.00 81.69  ? 199  LEU   B HD12 1 
ATOM   11983 H  HD13 . LEU   B  2  195 ? 3.420   -35.594 11.122   1.00 81.69  ? 199  LEU   B HD13 1 
ATOM   11984 H  HD21 . LEU   B  2  195 ? 3.760   -37.555 8.878    1.00 72.48  ? 199  LEU   B HD21 1 
ATOM   11985 H  HD22 . LEU   B  2  195 ? 3.327   -38.050 10.324   1.00 72.48  ? 199  LEU   B HD22 1 
ATOM   11986 H  HD23 . LEU   B  2  195 ? 2.419   -38.387 9.065    1.00 72.48  ? 199  LEU   B HD23 1 
ATOM   11987 N  N    . THR   B  2  196 ? -1.210  -39.073 11.352   1.00 58.15  ? 200  THR   B N    1 
ATOM   11988 C  CA   . THR   B  2  196 ? -2.148  -39.576 12.343   1.00 59.74  ? 200  THR   B CA   1 
ATOM   11989 C  C    . THR   B  2  196 ? -1.564  -40.820 12.992   1.00 61.60  ? 200  THR   B C    1 
ATOM   11990 O  O    . THR   B  2  196 ? -0.688  -41.487 12.434   1.00 66.80  ? 200  THR   B O    1 
ATOM   11991 C  CB   . THR   B  2  196 ? -3.515  -39.908 11.728   1.00 65.28  ? 200  THR   B CB   1 
ATOM   11992 O  OG1  . THR   B  2  196 ? -4.379  -40.446 12.739   1.00 71.25  ? 200  THR   B OG1  1 
ATOM   11993 C  CG2  . THR   B  2  196 ? -3.365  -40.922 10.600   1.00 65.50  ? 200  THR   B CG2  1 
ATOM   11994 H  H    . THR   B  2  196 ? -0.705  -39.680 11.012   1.00 69.76  ? 200  THR   B H    1 
ATOM   11995 H  HA   . THR   B  2  196 ? -2.274  -38.895 13.022   1.00 71.67  ? 200  THR   B HA   1 
ATOM   11996 H  HB   . THR   B  2  196 ? -3.909  -39.101 11.362   1.00 78.32  ? 200  THR   B HB   1 
ATOM   11997 H  HG1  . THR   B  2  196 ? -5.119  -40.655 12.403   1.00 85.49  ? 200  THR   B HG1  1 
ATOM   11998 H  HG21 . THR   B  2  196 ? -4.227  -41.093 10.190   1.00 78.58  ? 200  THR   B HG21 1 
ATOM   11999 H  HG22 . THR   B  2  196 ? -2.757  -40.581 9.925    1.00 78.58  ? 200  THR   B HG22 1 
ATOM   12000 H  HG23 . THR   B  2  196 ? -3.012  -41.756 10.948   1.00 78.58  ? 200  THR   B HG23 1 
ATOM   12001 N  N    . ASN   B  2  197 ? -2.066  -41.123 14.188   1.00 63.30  ? 201  ASN   B N    1 
ATOM   12002 C  CA   . ASN   B  2  197 ? -1.725  -42.359 14.877   1.00 63.51  ? 201  ASN   B CA   1 
ATOM   12003 C  C    . ASN   B  2  197 ? -2.568  -43.540 14.417   1.00 66.06  ? 201  ASN   B C    1 
ATOM   12004 O  O    . ASN   B  2  197 ? -2.244  -44.683 14.759   1.00 70.76  ? 201  ASN   B O    1 
ATOM   12005 C  CB   . ASN   B  2  197 ? -1.894  -42.179 16.388   1.00 67.38  ? 201  ASN   B CB   1 
ATOM   12006 C  CG   . ASN   B  2  197 ? -3.268  -41.647 16.762   1.00 79.37  ? 201  ASN   B CG   1 
ATOM   12007 O  OD1  . ASN   B  2  197 ? -3.444  -40.448 16.983   1.00 88.36  ? 201  ASN   B OD1  1 
ATOM   12008 N  ND2  . ASN   B  2  197 ? -4.250  -42.537 16.822   1.00 84.97  ? 201  ASN   B ND2  1 
ATOM   12009 H  H    . ASN   B  2  197 ? -2.612  -40.622 14.624   1.00 75.95  ? 201  ASN   B H    1 
ATOM   12010 H  HA   . ASN   B  2  197 ? -0.794  -42.566 14.701   1.00 76.19  ? 201  ASN   B HA   1 
ATOM   12011 H  HB2  . ASN   B  2  197 ? -1.774  -43.036 16.825   1.00 80.84  ? 201  ASN   B HB2  1 
ATOM   12012 H  HB3  . ASN   B  2  197 ? -1.230  -41.548 16.708   1.00 80.84  ? 201  ASN   B HB3  1 
ATOM   12013 H  HD21 . ASN   B  2  197 ? -5.046  -42.286 17.030   1.00 101.94 ? 201  ASN   B HD21 1 
ATOM   12014 H  HD22 . ASN   B  2  197 ? -4.091  -43.365 16.654   1.00 101.94 ? 201  ASN   B HD22 1 
ATOM   12015 N  N    . ASP   B  2  198 ? -3.633  -43.296 13.657   1.00 67.90  ? 202  ASP   B N    1 
ATOM   12016 C  CA   . ASP   B  2  198 ? -4.539  -44.354 13.215   1.00 70.56  ? 202  ASP   B CA   1 
ATOM   12017 C  C    . ASP   B  2  198 ? -3.858  -45.124 12.091   1.00 71.14  ? 202  ASP   B C    1 
ATOM   12018 O  O    . ASP   B  2  198 ? -3.915  -44.729 10.924   1.00 71.85  ? 202  ASP   B O    1 
ATOM   12019 C  CB   . ASP   B  2  198 ? -5.871  -43.762 12.770   1.00 69.48  ? 202  ASP   B CB   1 
ATOM   12020 C  CG   . ASP   B  2  198 ? -6.942  -44.816 12.579   1.00 73.78  ? 202  ASP   B CG   1 
ATOM   12021 O  OD1  . ASP   B  2  198 ? -6.600  -46.017 12.567   1.00 74.90  ? 202  ASP   B OD1  1 
ATOM   12022 O  OD2  . ASP   B  2  198 ? -8.128  -44.444 12.448   1.00 76.80  ? 202  ASP   B OD2  1 
ATOM   12023 H  H    . ASP   B  2  198 ? -3.856  -42.513 13.380   1.00 81.46  ? 202  ASP   B H    1 
ATOM   12024 H  HA   . ASP   B  2  198 ? -4.711  -44.968 13.946   1.00 84.66  ? 202  ASP   B HA   1 
ATOM   12025 H  HB2  . ASP   B  2  198 ? -6.182  -43.137 13.444   1.00 83.36  ? 202  ASP   B HB2  1 
ATOM   12026 H  HB3  . ASP   B  2  198 ? -5.747  -43.303 11.924   1.00 83.36  ? 202  ASP   B HB3  1 
ATOM   12027 N  N    . ALA   B  2  199 ? -3.207  -46.235 12.446   1.00 70.54  ? 203  ALA   B N    1 
ATOM   12028 C  CA   . ALA   B  2  199 ? -2.458  -47.001 11.456   1.00 66.74  ? 203  ALA   B CA   1 
ATOM   12029 C  C    . ALA   B  2  199 ? -3.380  -47.755 10.507   1.00 63.17  ? 203  ALA   B C    1 
ATOM   12030 O  O    . ALA   B  2  199 ? -3.047  -47.924 9.329    1.00 61.08  ? 203  ALA   B O    1 
ATOM   12031 C  CB   . ALA   B  2  199 ? -1.507  -47.974 12.153   1.00 67.09  ? 203  ALA   B CB   1 
ATOM   12032 H  H    . ALA   B  2  199 ? -3.185  -46.560 13.242   1.00 84.63  ? 203  ALA   B H    1 
ATOM   12033 H  HA   . ALA   B  2  199 ? -1.926  -46.385 10.928   1.00 80.07  ? 203  ALA   B HA   1 
ATOM   12034 H  HB1  . ALA   B  2  199 ? -1.023  -48.478 11.481   1.00 80.49  ? 203  ALA   B HB1  1 
ATOM   12035 H  HB2  . ALA   B  2  199 ? -0.885  -47.469 12.700   1.00 80.49  ? 203  ALA   B HB2  1 
ATOM   12036 H  HB3  . ALA   B  2  199 ? -2.024  -48.576 12.710   1.00 80.49  ? 203  ALA   B HB3  1 
ATOM   12037 N  N    . GLU   B  2  200 ? -4.533  -48.221 10.993   1.00 66.31  ? 204  GLU   B N    1 
ATOM   12038 C  CA   . GLU   B  2  200 ? -5.489  -48.860 10.096   1.00 72.57  ? 204  GLU   B CA   1 
ATOM   12039 C  C    . GLU   B  2  200 ? -5.964  -47.893 9.020    1.00 72.21  ? 204  GLU   B C    1 
ATOM   12040 O  O    . GLU   B  2  200 ? -6.206  -48.303 7.879    1.00 73.74  ? 204  GLU   B O    1 
ATOM   12041 C  CB   . GLU   B  2  200 ? -6.677  -49.406 10.887   1.00 81.21  ? 204  GLU   B CB   1 
ATOM   12042 C  CG   . GLU   B  2  200 ? -6.466  -50.816 11.422   1.00 90.81  ? 204  GLU   B CG   1 
ATOM   12043 C  CD   . GLU   B  2  200 ? -6.338  -51.848 10.315   1.00 94.39  ? 204  GLU   B CD   1 
ATOM   12044 O  OE1  . GLU   B  2  200 ? -6.768  -51.556 9.179    1.00 93.16  ? 204  GLU   B OE1  1 
ATOM   12045 O  OE2  . GLU   B  2  200 ? -5.806  -52.948 10.579   1.00 95.25  ? 204  GLU   B OE2  1 
ATOM   12046 H  H    . GLU   B  2  200 ? -4.777  -48.179 11.816   1.00 79.55  ? 204  GLU   B H    1 
ATOM   12047 H  HA   . GLU   B  2  200 ? -5.057  -49.612 9.660    1.00 87.07  ? 204  GLU   B HA   1 
ATOM   12048 H  HB2  . GLU   B  2  200 ? -6.841  -48.823 11.645   1.00 97.44  ? 204  GLU   B HB2  1 
ATOM   12049 H  HB3  . GLU   B  2  200 ? -7.455  -49.423 10.308   1.00 97.44  ? 204  GLU   B HB3  1 
ATOM   12050 H  HG2  . GLU   B  2  200 ? -5.650  -50.836 11.947   1.00 108.96 ? 204  GLU   B HG2  1 
ATOM   12051 H  HG3  . GLU   B  2  200 ? -7.223  -51.062 11.976   1.00 108.96 ? 204  GLU   B HG3  1 
ATOM   12052 N  N    . ARG   B  2  201 ? -6.099  -46.610 9.361    1.00 68.87  ? 205  ARG   B N    1 
ATOM   12053 C  CA   . ARG   B  2  201 ? -6.450  -45.615 8.355    1.00 68.77  ? 205  ARG   B CA   1 
ATOM   12054 C  C    . ARG   B  2  201 ? -5.381  -45.541 7.272    1.00 67.67  ? 205  ARG   B C    1 
ATOM   12055 O  O    . ARG   B  2  201 ? -5.697  -45.449 6.080    1.00 68.50  ? 205  ARG   B O    1 
ATOM   12056 C  CB   . ARG   B  2  201 ? -6.649  -44.252 9.019    1.00 72.55  ? 205  ARG   B CB   1 
ATOM   12057 C  CG   . ARG   B  2  201 ? -7.018  -43.131 8.062    1.00 80.51  ? 205  ARG   B CG   1 
ATOM   12058 C  CD   . ARG   B  2  201 ? -8.281  -43.454 7.281    1.00 94.42  ? 205  ARG   B CD   1 
ATOM   12059 N  NE   . ARG   B  2  201 ? -8.704  -42.343 6.433    1.00 104.51 ? 205  ARG   B NE   1 
ATOM   12060 C  CZ   . ARG   B  2  201 ? -9.654  -42.428 5.507    1.00 112.74 ? 205  ARG   B CZ   1 
ATOM   12061 N  NH1  . ARG   B  2  201 ? -10.283 -43.577 5.297    1.00 115.87 ? 205  ARG   B NH1  1 
ATOM   12062 N  NH2  . ARG   B  2  201 ? -9.973  -41.363 4.785    1.00 115.44 ? 205  ARG   B NH2  1 
ATOM   12063 H  H    . ARG   B  2  201 ? -5.995  -46.297 10.155   1.00 82.62  ? 205  ARG   B H    1 
ATOM   12064 H  HA   . ARG   B  2  201 ? -7.287  -45.865 7.933    1.00 82.51  ? 205  ARG   B HA   1 
ATOM   12065 H  HB2  . ARG   B  2  201 ? -7.363  -44.328 9.671    1.00 87.04  ? 205  ARG   B HB2  1 
ATOM   12066 H  HB3  . ARG   B  2  201 ? -5.822  -44.000 9.460    1.00 87.04  ? 205  ARG   B HB3  1 
ATOM   12067 H  HG2  . ARG   B  2  201 ? -7.172  -42.316 8.566    1.00 96.59  ? 205  ARG   B HG2  1 
ATOM   12068 H  HG3  . ARG   B  2  201 ? -6.294  -42.998 7.429    1.00 96.59  ? 205  ARG   B HG3  1 
ATOM   12069 H  HD2  . ARG   B  2  201 ? -8.116  -44.222 6.712    1.00 113.28 ? 205  ARG   B HD2  1 
ATOM   12070 H  HD3  . ARG   B  2  201 ? -8.999  -43.650 7.903    1.00 113.28 ? 205  ARG   B HD3  1 
ATOM   12071 H  HE   . ARG   B  2  201 ? -8.313  -41.585 6.540    1.00 125.39 ? 205  ARG   B HE   1 
ATOM   12072 H  HH11 . ARG   B  2  201 ? -10.076 -44.271 5.761    1.00 139.03 ? 205  ARG   B HH11 1 
ATOM   12073 H  HH12 . ARG   B  2  201 ? -10.897 -43.628 4.697    1.00 139.03 ? 205  ARG   B HH12 1 
ATOM   12074 H  HH21 . ARG   B  2  201 ? -9.565  -40.617 4.916    1.00 138.51 ? 205  ARG   B HH21 1 
ATOM   12075 H  HH22 . ARG   B  2  201 ? -10.588 -41.418 4.186    1.00 138.51 ? 205  ARG   B HH22 1 
ATOM   12076 N  N    . PHE   B  2  202 ? -4.107  -45.575 7.670    1.00 65.46  ? 206  PHE   B N    1 
ATOM   12077 C  CA   . PHE   B  2  202 ? -3.025  -45.660 6.693    1.00 61.83  ? 206  PHE   B CA   1 
ATOM   12078 C  C    . PHE   B  2  202 ? -3.175  -46.900 5.819    1.00 61.17  ? 206  PHE   B C    1 
ATOM   12079 O  O    . PHE   B  2  202 ? -2.994  -46.834 4.598    1.00 57.25  ? 206  PHE   B O    1 
ATOM   12080 C  CB   . PHE   B  2  202 ? -1.679  -45.667 7.420    1.00 62.12  ? 206  PHE   B CB   1 
ATOM   12081 C  CG   . PHE   B  2  202 ? -0.485  -45.621 6.507    1.00 58.64  ? 206  PHE   B CG   1 
ATOM   12082 C  CD1  . PHE   B  2  202 ? 0.058   -46.786 5.991    1.00 58.66  ? 206  PHE   B CD1  1 
ATOM   12083 C  CD2  . PHE   B  2  202 ? 0.110   -44.413 6.183    1.00 54.72  ? 206  PHE   B CD2  1 
ATOM   12084 C  CE1  . PHE   B  2  202 ? 1.162   -46.745 5.160    1.00 56.51  ? 206  PHE   B CE1  1 
ATOM   12085 C  CE2  . PHE   B  2  202 ? 1.216   -44.368 5.353    1.00 53.36  ? 206  PHE   B CE2  1 
ATOM   12086 C  CZ   . PHE   B  2  202 ? 1.741   -45.535 4.842    1.00 55.03  ? 206  PHE   B CZ   1 
ATOM   12087 H  H    . PHE   B  2  202 ? -3.847  -45.551 8.489    1.00 78.53  ? 206  PHE   B H    1 
ATOM   12088 H  HA   . PHE   B  2  202 ? -3.052  -44.883 6.114    1.00 74.18  ? 206  PHE   B HA   1 
ATOM   12089 H  HB2  . PHE   B  2  202 ? -1.636  -44.891 8.000    1.00 74.53  ? 206  PHE   B HB2  1 
ATOM   12090 H  HB3  . PHE   B  2  202 ? -1.615  -46.479 7.947    1.00 74.53  ? 206  PHE   B HB3  1 
ATOM   12091 H  HD1  . PHE   B  2  202 ? -0.325  -47.606 6.207    1.00 70.38  ? 206  PHE   B HD1  1 
ATOM   12092 H  HD2  . PHE   B  2  202 ? -0.238  -43.623 6.527    1.00 65.65  ? 206  PHE   B HD2  1 
ATOM   12093 H  HE1  . PHE   B  2  202 ? 1.515   -47.534 4.815    1.00 67.80  ? 206  PHE   B HE1  1 
ATOM   12094 H  HE2  . PHE   B  2  202 ? 1.605   -43.551 5.141    1.00 64.01  ? 206  PHE   B HE2  1 
ATOM   12095 H  HZ   . PHE   B  2  202 ? 2.484   -45.506 4.284    1.00 66.02  ? 206  PHE   B HZ   1 
ATOM   12096 N  N    . ASN   B  2  203 ? -3.512  -48.041 6.428    1.00 64.48  ? 207  ASN   B N    1 
ATOM   12097 C  CA   . ASN   B  2  203 ? -3.716  -49.260 5.652    1.00 65.81  ? 207  ASN   B CA   1 
ATOM   12098 C  C    . ASN   B  2  203 ? -4.856  -49.096 4.654    1.00 71.59  ? 207  ASN   B C    1 
ATOM   12099 O  O    . ASN   B  2  203 ? -4.734  -49.496 3.490    1.00 72.10  ? 207  ASN   B O    1 
ATOM   12100 C  CB   . ASN   B  2  203 ? -4.001  -50.440 6.583    1.00 66.50  ? 207  ASN   B CB   1 
ATOM   12101 C  CG   . ASN   B  2  203 ? -2.763  -50.927 7.309    1.00 65.17  ? 207  ASN   B CG   1 
ATOM   12102 O  OD1  . ASN   B  2  203 ? -1.639  -50.587 6.943    1.00 68.31  ? 207  ASN   B OD1  1 
ATOM   12103 N  ND2  . ASN   B  2  203 ? -2.965  -51.740 8.341    1.00 65.03  ? 207  ASN   B ND2  1 
ATOM   12104 H  H    . ASN   B  2  203 ? -3.625  -48.132 7.275    1.00 77.36  ? 207  ASN   B H    1 
ATOM   12105 H  HA   . ASN   B  2  203 ? -2.902  -49.449 5.159    1.00 78.95  ? 207  ASN   B HA   1 
ATOM   12106 H  HB2  . ASN   B  2  203 ? -4.652  -50.167 7.249    1.00 79.78  ? 207  ASN   B HB2  1 
ATOM   12107 H  HB3  . ASN   B  2  203 ? -4.351  -51.178 6.059    1.00 79.78  ? 207  ASN   B HB3  1 
ATOM   12108 H  HD21 . ASN   B  2  203 ? -2.296  -52.044 8.786    1.00 78.02  ? 207  ASN   B HD21 1 
ATOM   12109 H  HD22 . ASN   B  2  203 ? -3.766  -51.962 8.563    1.00 78.02  ? 207  ASN   B HD22 1 
ATOM   12110 N  N    . GLU   B  2  204 ? -5.976  -48.514 5.090    1.00 76.44  ? 208  GLU   B N    1 
ATOM   12111 C  CA   . GLU   B  2  204 ? -7.142  -48.416 4.218    1.00 79.99  ? 208  GLU   B CA   1 
ATOM   12112 C  C    . GLU   B  2  204 ? -6.846  -47.563 2.992    1.00 72.54  ? 208  GLU   B C    1 
ATOM   12113 O  O    . GLU   B  2  204 ? -7.211  -47.927 1.868    1.00 69.72  ? 208  GLU   B O    1 
ATOM   12114 C  CB   . GLU   B  2  204 ? -8.329  -47.838 4.988    1.00 92.45  ? 208  GLU   B CB   1 
ATOM   12115 C  CG   . GLU   B  2  204 ? -9.655  -47.963 4.252    1.00 106.95 ? 208  GLU   B CG   1 
ATOM   12116 C  CD   . GLU   B  2  204 ? -10.682 -46.949 4.717    1.00 119.61 ? 208  GLU   B CD   1 
ATOM   12117 O  OE1  . GLU   B  2  204 ? -11.645 -46.693 3.963    1.00 125.28 ? 208  GLU   B OE1  1 
ATOM   12118 O  OE2  . GLU   B  2  204 ? -10.526 -46.404 5.831    1.00 123.24 ? 208  GLU   B OE2  1 
ATOM   12119 H  H    . GLU   B  2  204 ? -6.083  -48.174 5.873    1.00 91.71  ? 208  GLU   B H    1 
ATOM   12120 H  HA   . GLU   B  2  204 ? -7.378  -49.308 3.919    1.00 95.97  ? 208  GLU   B HA   1 
ATOM   12121 H  HB2  . GLU   B  2  204 ? -8.413  -48.310 5.832    1.00 110.92 ? 208  GLU   B HB2  1 
ATOM   12122 H  HB3  . GLU   B  2  204 ? -8.167  -46.896 5.150    1.00 110.92 ? 208  GLU   B HB3  1 
ATOM   12123 H  HG2  . GLU   B  2  204 ? -9.504  -47.823 3.304    1.00 128.32 ? 208  GLU   B HG2  1 
ATOM   12124 H  HG3  . GLU   B  2  204 ? -10.018 -48.849 4.404    1.00 128.32 ? 208  GLU   B HG3  1 
ATOM   12125 N  N    . ILE   B  2  205 ? -6.194  -46.417 3.188    1.00 72.84  ? 209  ILE   B N    1 
ATOM   12126 C  CA   . ILE   B  2  205 ? -5.924  -45.521 2.069    1.00 72.18  ? 209  ILE   B CA   1 
ATOM   12127 C  C    . ILE   B  2  205 ? -4.972  -46.176 1.079    1.00 69.92  ? 209  ILE   B C    1 
ATOM   12128 O  O    . ILE   B  2  205 ? -5.176  -46.101 -0.138   1.00 74.05  ? 209  ILE   B O    1 
ATOM   12129 C  CB   . ILE   B  2  205 ? -5.386  -44.177 2.592    1.00 72.02  ? 209  ILE   B CB   1 
ATOM   12130 C  CG1  . ILE   B  2  205 ? -6.511  -43.436 3.317    1.00 74.98  ? 209  ILE   B CG1  1 
ATOM   12131 C  CG2  . ILE   B  2  205 ? -4.825  -43.328 1.457    1.00 71.48  ? 209  ILE   B CG2  1 
ATOM   12132 C  CD1  . ILE   B  2  205 ? -6.084  -42.157 3.967    1.00 76.79  ? 209  ILE   B CD1  1 
ATOM   12133 H  H    . ILE   B  2  205 ? -5.901  -46.140 3.948    1.00 87.39  ? 209  ILE   B H    1 
ATOM   12134 H  HA   . ILE   B  2  205 ? -6.755  -45.346 1.599    1.00 86.59  ? 209  ILE   B HA   1 
ATOM   12135 H  HB   . ILE   B  2  205 ? -4.660  -44.350 3.211    1.00 86.41  ? 209  ILE   B HB   1 
ATOM   12136 H  HG12 . ILE   B  2  205 ? -7.205  -43.222 2.674    1.00 89.96  ? 209  ILE   B HG12 1 
ATOM   12137 H  HG13 . ILE   B  2  205 ? -6.866  -44.014 4.010    1.00 89.96  ? 209  ILE   B HG13 1 
ATOM   12138 H  HG21 . ILE   B  2  205 ? -4.512  -42.484 1.819    1.00 85.76  ? 209  ILE   B HG21 1 
ATOM   12139 H  HG22 . ILE   B  2  205 ? -4.090  -43.803 1.041    1.00 85.76  ? 209  ILE   B HG22 1 
ATOM   12140 H  HG23 . ILE   B  2  205 ? -5.526  -43.168 0.806    1.00 85.76  ? 209  ILE   B HG23 1 
ATOM   12141 H  HD11 . ILE   B  2  205 ? -6.751  -41.898 4.623    1.00 92.13  ? 209  ILE   B HD11 1 
ATOM   12142 H  HD12 . ILE   B  2  205 ? -5.228  -42.293 4.401    1.00 92.13  ? 209  ILE   B HD12 1 
ATOM   12143 H  HD13 . ILE   B  2  205 ? -6.005  -41.468 3.288    1.00 92.13  ? 209  ILE   B HD13 1 
ATOM   12144 N  N    . VAL   B  2  206 ? -3.924  -46.835 1.579    1.00 66.60  ? 210  VAL   B N    1 
ATOM   12145 C  CA   . VAL   B  2  206 ? -3.008  -47.549 0.694    1.00 66.55  ? 210  VAL   B CA   1 
ATOM   12146 C  C    . VAL   B  2  206 ? -3.767  -48.575 -0.139   1.00 68.71  ? 210  VAL   B C    1 
ATOM   12147 O  O    . VAL   B  2  206 ? -3.526  -48.721 -1.344   1.00 67.14  ? 210  VAL   B O    1 
ATOM   12148 C  CB   . VAL   B  2  206 ? -1.878  -48.202 1.512    1.00 67.64  ? 210  VAL   B CB   1 
ATOM   12149 C  CG1  . VAL   B  2  206 ? -1.158  -49.263 0.690    1.00 66.92  ? 210  VAL   B CG1  1 
ATOM   12150 C  CG2  . VAL   B  2  206 ? -0.891  -47.146 1.993    1.00 65.74  ? 210  VAL   B CG2  1 
ATOM   12151 H  H    . VAL   B  2  206 ? -3.725  -46.882 2.414    1.00 79.90  ? 210  VAL   B H    1 
ATOM   12152 H  HA   . VAL   B  2  206 ? -2.605  -46.911 0.084    1.00 79.84  ? 210  VAL   B HA   1 
ATOM   12153 H  HB   . VAL   B  2  206 ? -2.268  -48.636 2.288    1.00 81.15  ? 210  VAL   B HB   1 
ATOM   12154 H  HG11 . VAL   B  2  206 ? -0.329  -49.499 1.136    1.00 80.29  ? 210  VAL   B HG11 1 
ATOM   12155 H  HG12 . VAL   B  2  206 ? -1.727  -50.045 0.615    1.00 80.29  ? 210  VAL   B HG12 1 
ATOM   12156 H  HG13 . VAL   B  2  206 ? -0.969  -48.905 -0.191   1.00 80.29  ? 210  VAL   B HG13 1 
ATOM   12157 H  HG21 . VAL   B  2  206 ? -0.188  -47.578 2.503    1.00 78.87  ? 210  VAL   B HG21 1 
ATOM   12158 H  HG22 . VAL   B  2  206 ? -0.511  -46.695 1.222    1.00 78.87  ? 210  VAL   B HG22 1 
ATOM   12159 H  HG23 . VAL   B  2  206 ? -1.360  -46.506 2.551    1.00 78.87  ? 210  VAL   B HG23 1 
ATOM   12160 N  N    . LYS   B  2  207 ? -4.702  -49.296 0.486    1.00 69.03  ? 211  LYS   B N    1 
ATOM   12161 C  CA   . LYS   B  2  207 ? -5.450  -50.320 -0.234   1.00 71.58  ? 211  LYS   B CA   1 
ATOM   12162 C  C    . LYS   B  2  207 ? -6.317  -49.723 -1.336   1.00 76.16  ? 211  LYS   B C    1 
ATOM   12163 O  O    . LYS   B  2  207 ? -6.601  -50.397 -2.333   1.00 80.28  ? 211  LYS   B O    1 
ATOM   12164 C  CB   . LYS   B  2  207 ? -6.322  -51.116 0.738    1.00 72.51  ? 211  LYS   B CB   1 
ATOM   12165 C  CG   . LYS   B  2  207 ? -5.555  -52.042 1.669    1.00 76.12  ? 211  LYS   B CG   1 
ATOM   12166 C  CD   . LYS   B  2  207 ? -6.491  -52.684 2.682    1.00 82.78  ? 211  LYS   B CD   1 
ATOM   12167 C  CE   . LYS   B  2  207 ? -5.731  -53.373 3.803    1.00 86.30  ? 211  LYS   B CE   1 
ATOM   12168 N  NZ   . LYS   B  2  207 ? -6.620  -53.678 4.960    1.00 91.82  ? 211  LYS   B NZ   1 
ATOM   12169 H  H    . LYS   B  2  207 ? -4.918  -49.211 1.315    1.00 82.82  ? 211  LYS   B H    1 
ATOM   12170 H  HA   . LYS   B  2  207 ? -4.816  -50.928 -0.646   1.00 85.87  ? 211  LYS   B HA   1 
ATOM   12171 H  HB2  . LYS   B  2  207 ? -6.817  -50.491 1.290    1.00 86.99  ? 211  LYS   B HB2  1 
ATOM   12172 H  HB3  . LYS   B  2  207 ? -6.936  -51.663 0.224    1.00 86.99  ? 211  LYS   B HB3  1 
ATOM   12173 H  HG2  . LYS   B  2  207 ? -5.132  -52.744 1.152    1.00 91.33  ? 211  LYS   B HG2  1 
ATOM   12174 H  HG3  . LYS   B  2  207 ? -4.883  -51.533 2.150    1.00 91.33  ? 211  LYS   B HG3  1 
ATOM   12175 H  HD2  . LYS   B  2  207 ? -7.055  -51.999 3.075    1.00 99.32  ? 211  LYS   B HD2  1 
ATOM   12176 H  HD3  . LYS   B  2  207 ? -7.039  -53.348 2.235    1.00 99.32  ? 211  LYS   B HD3  1 
ATOM   12177 H  HE2  . LYS   B  2  207 ? -5.361  -54.207 3.475    1.00 103.54 ? 211  LYS   B HE2  1 
ATOM   12178 H  HE3  . LYS   B  2  207 ? -5.018  -52.792 4.111    1.00 103.54 ? 211  LYS   B HE3  1 
ATOM   12179 H  HZ1  . LYS   B  2  207 ? -6.161  -54.104 5.593    1.00 110.16 ? 211  LYS   B HZ1  1 
ATOM   12180 H  HZ2  . LYS   B  2  207 ? -6.948  -52.923 5.299    1.00 110.16 ? 211  LYS   B HZ2  1 
ATOM   12181 H  HZ3  . LYS   B  2  207 ? -7.296  -54.193 4.697    1.00 110.16 ? 211  LYS   B HZ3  1 
ATOM   12182 N  N    . ASN   B  2  208 ? -6.752  -48.475 -1.178   1.00 74.56  ? 212  ASN   B N    1 
ATOM   12183 C  CA   . ASN   B  2  208 ? -7.624  -47.831 -2.152   1.00 75.90  ? 212  ASN   B CA   1 
ATOM   12184 C  C    . ASN   B  2  208 ? -6.861  -47.069 -3.227   1.00 77.00  ? 212  ASN   B C    1 
ATOM   12185 O  O    . ASN   B  2  208 ? -7.492  -46.462 -4.098   1.00 78.80  ? 212  ASN   B O    1 
ATOM   12186 C  CB   . ASN   B  2  208 ? -8.588  -46.871 -1.445   1.00 78.21  ? 212  ASN   B CB   1 
ATOM   12187 C  CG   . ASN   B  2  208 ? -9.558  -47.588 -0.526   1.00 84.34  ? 212  ASN   B CG   1 
ATOM   12188 O  OD1  . ASN   B  2  208 ? -9.917  -48.742 -0.761   1.00 87.79  ? 212  ASN   B OD1  1 
ATOM   12189 N  ND2  . ASN   B  2  208 ? -9.989  -46.904 0.528    1.00 84.56  ? 212  ASN   B ND2  1 
ATOM   12190 H  H    . ASN   B  2  208 ? -6.552  -47.976 -0.507   1.00 89.45  ? 212  ASN   B H    1 
ATOM   12191 H  HA   . ASN   B  2  208 ? -8.149  -48.519 -2.589   1.00 91.06  ? 212  ASN   B HA   1 
ATOM   12192 H  HB2  . ASN   B  2  208 ? -8.076  -46.244 -0.910   1.00 93.84  ? 212  ASN   B HB2  1 
ATOM   12193 H  HB3  . ASN   B  2  208 ? -9.105  -46.393 -2.112   1.00 93.84  ? 212  ASN   B HB3  1 
ATOM   12194 H  HD21 . ASN   B  2  208 ? -10.540 -47.266 1.080    1.00 101.45 ? 212  ASN   B HD21 1 
ATOM   12195 H  HD22 . ASN   B  2  208 ? -9.717  -46.098 0.659    1.00 101.45 ? 212  ASN   B HD22 1 
ATOM   12196 N  N    . GLN   B  2  209 ? -5.532  -47.086 -3.195   1.00 75.30  ? 213  GLN   B N    1 
ATOM   12197 C  CA   . GLN   B  2  209 ? -4.748  -46.337 -4.166   1.00 72.29  ? 213  GLN   B CA   1 
ATOM   12198 C  C    . GLN   B  2  209 ? -4.686  -47.073 -5.497   1.00 73.11  ? 213  GLN   B C    1 
ATOM   12199 O  O    . GLN   B  2  209 ? -4.626  -48.306 -5.545   1.00 78.23  ? 213  GLN   B O    1 
ATOM   12200 C  CB   . GLN   B  2  209 ? -3.330  -46.096 -3.645   1.00 69.35  ? 213  GLN   B CB   1 
ATOM   12201 C  CG   . GLN   B  2  209 ? -3.238  -45.085 -2.513   1.00 67.52  ? 213  GLN   B CG   1 
ATOM   12202 C  CD   . GLN   B  2  209 ? -3.753  -43.715 -2.905   1.00 63.62  ? 213  GLN   B CD   1 
ATOM   12203 O  OE1  . GLN   B  2  209 ? -3.133  -43.011 -3.704   1.00 66.83  ? 213  GLN   B OE1  1 
ATOM   12204 N  NE2  . GLN   B  2  209 ? -4.895  -43.330 -2.346   1.00 58.84  ? 213  GLN   B NE2  1 
ATOM   12205 H  H    . GLN   B  2  209 ? -5.063  -47.522 -2.622   1.00 90.35  ? 213  GLN   B H    1 
ATOM   12206 H  HA   . GLN   B  2  209 ? -5.170  -45.476 -4.312   1.00 86.73  ? 213  GLN   B HA   1 
ATOM   12207 H  HB2  . GLN   B  2  209 ? -2.975  -46.937 -3.318   1.00 83.20  ? 213  GLN   B HB2  1 
ATOM   12208 H  HB3  . GLN   B  2  209 ? -2.784  -45.767 -4.377   1.00 83.20  ? 213  GLN   B HB3  1 
ATOM   12209 H  HG2  . GLN   B  2  209 ? -3.768  -45.401 -1.764   1.00 81.00  ? 213  GLN   B HG2  1 
ATOM   12210 H  HG3  . GLN   B  2  209 ? -2.310  -44.993 -2.247   1.00 81.00  ? 213  GLN   B HG3  1 
ATOM   12211 H  HE21 . GLN   B  2  209 ? -5.300  -43.850 -1.794   1.00 70.59  ? 213  GLN   B HE21 1 
ATOM   12212 H  HE22 . GLN   B  2  209 ? -5.228  -42.560 -2.536   1.00 70.59  ? 213  GLN   B HE22 1 
ATOM   12213 N  N    . LYS   B  2  210 ? -4.700  -46.302 -6.578   1.00 68.87  ? 214  LYS   B N    1 
ATOM   12214 C  CA   . LYS   B  2  210 ? -4.542  -46.811 -7.929   1.00 65.87  ? 214  LYS   B CA   1 
ATOM   12215 C  C    . LYS   B  2  210 ? -3.387  -46.075 -8.594   1.00 62.37  ? 214  LYS   B C    1 
ATOM   12216 O  O    . LYS   B  2  210 ? -3.156  -44.890 -8.336   1.00 59.73  ? 214  LYS   B O    1 
ATOM   12217 C  CB   . LYS   B  2  210 ? -5.826  -46.630 -8.748   1.00 69.31  ? 214  LYS   B CB   1 
ATOM   12218 C  CG   . LYS   B  2  210 ? -7.066  -47.278 -8.135   1.00 75.07  ? 214  LYS   B CG   1 
ATOM   12219 C  CD   . LYS   B  2  210 ? -7.040  -48.799 -8.258   1.00 81.01  ? 214  LYS   B CD   1 
ATOM   12220 C  CE   . LYS   B  2  210 ? -8.336  -49.423 -7.753   1.00 88.51  ? 214  LYS   B CE   1 
ATOM   12221 N  NZ   . LYS   B  2  210 ? -8.436  -50.875 -8.080   1.00 92.63  ? 214  LYS   B NZ   1 
ATOM   12222 H  H    . LYS   B  2  210 ? -4.803  -45.448 -6.550   1.00 82.63  ? 214  LYS   B H    1 
ATOM   12223 H  HA   . LYS   B  2  210 ? -4.341  -47.760 -7.912   1.00 79.02  ? 214  LYS   B HA   1 
ATOM   12224 H  HB2  . LYS   B  2  210 ? -6.005  -45.680 -8.835   1.00 83.16  ? 214  LYS   B HB2  1 
ATOM   12225 H  HB3  . LYS   B  2  210 ? -5.692  -47.024 -9.624   1.00 83.16  ? 214  LYS   B HB3  1 
ATOM   12226 H  HG2  . LYS   B  2  210 ? -7.112  -47.052 -7.193   1.00 90.07  ? 214  LYS   B HG2  1 
ATOM   12227 H  HG3  . LYS   B  2  210 ? -7.856  -46.952 -8.593   1.00 90.07  ? 214  LYS   B HG3  1 
ATOM   12228 H  HD2  . LYS   B  2  210 ? -6.926  -49.044 -9.190   1.00 97.19  ? 214  LYS   B HD2  1 
ATOM   12229 H  HD3  . LYS   B  2  210 ? -6.306  -49.151 -7.731   1.00 97.19  ? 214  LYS   B HD3  1 
ATOM   12230 H  HE2  . LYS   B  2  210 ? -8.379  -49.328 -6.789   1.00 106.19 ? 214  LYS   B HE2  1 
ATOM   12231 H  HE3  . LYS   B  2  210 ? -9.088  -48.970 -8.165   1.00 106.19 ? 214  LYS   B HE3  1 
ATOM   12232 H  HZ1  . LYS   B  2  210 ? -9.202  -51.205 -7.771   1.00 111.14 ? 214  LYS   B HZ1  1 
ATOM   12233 H  HZ2  . LYS   B  2  210 ? -8.407  -50.992 -8.962   1.00 111.14 ? 214  LYS   B HZ2  1 
ATOM   12234 H  HZ3  . LYS   B  2  210 ? -7.759  -51.318 -7.708   1.00 111.14 ? 214  LYS   B HZ3  1 
ATOM   12235 N  N    . ILE   B  2  211 ? -2.655  -46.789 -9.448   1.00 61.39  ? 215  ILE   B N    1 
ATOM   12236 C  CA   . ILE   B  2  211 ? -1.489  -46.202 -10.092  1.00 59.65  ? 215  ILE   B CA   1 
ATOM   12237 C  C    . ILE   B  2  211 ? -1.926  -45.242 -11.193  1.00 57.16  ? 215  ILE   B C    1 
ATOM   12238 O  O    . ILE   B  2  211 ? -3.049  -45.292 -11.702  1.00 60.88  ? 215  ILE   B O    1 
ATOM   12239 C  CB   . ILE   B  2  211 ? -0.555  -47.290 -10.653  1.00 66.43  ? 215  ILE   B CB   1 
ATOM   12240 C  CG1  . ILE   B  2  211 ? -1.318  -48.190 -11.630  1.00 69.29  ? 215  ILE   B CG1  1 
ATOM   12241 C  CG2  . ILE   B  2  211 ? 0.060   -48.098 -9.522   1.00 70.07  ? 215  ILE   B CG2  1 
ATOM   12242 C  CD1  . ILE   B  2  211 ? -0.430  -49.032 -12.510  1.00 71.61  ? 215  ILE   B CD1  1 
ATOM   12243 H  H    . ILE   B  2  211 ? -2.813  -47.605 -9.667   1.00 73.65  ? 215  ILE   B H    1 
ATOM   12244 H  HA   . ILE   B  2  211 ? -0.998  -45.694 -9.427   1.00 71.56  ? 215  ILE   B HA   1 
ATOM   12245 H  HB   . ILE   B  2  211 ? 0.167   -46.861 -11.140  1.00 79.70  ? 215  ILE   B HB   1 
ATOM   12246 H  HG12 . ILE   B  2  211 ? -1.884  -48.792 -11.120  1.00 83.13  ? 215  ILE   B HG12 1 
ATOM   12247 H  HG13 . ILE   B  2  211 ? -1.862  -47.632 -12.207  1.00 83.13  ? 215  ILE   B HG13 1 
ATOM   12248 H  HG21 . ILE   B  2  211 ? 0.675   -48.747 -9.897   1.00 84.06  ? 215  ILE   B HG21 1 
ATOM   12249 H  HG22 . ILE   B  2  211 ? 0.535   -47.497 -8.927   1.00 84.06  ? 215  ILE   B HG22 1 
ATOM   12250 H  HG23 . ILE   B  2  211 ? -0.647  -48.552 -9.038   1.00 84.06  ? 215  ILE   B HG23 1 
ATOM   12251 H  HD11 . ILE   B  2  211 ? -0.982  -49.639 -13.028  1.00 85.91  ? 215  ILE   B HD11 1 
ATOM   12252 H  HD12 . ILE   B  2  211 ? 0.069   -48.450 -13.104  1.00 85.91  ? 215  ILE   B HD12 1 
ATOM   12253 H  HD13 . ILE   B  2  211 ? 0.182   -49.537 -11.951  1.00 85.91  ? 215  ILE   B HD13 1 
ATOM   12254 N  N    . SER   B  2  212 ? -1.010  -44.356 -11.559  1.00 53.95  ? 216  SER   B N    1 
ATOM   12255 C  CA   . SER   B  2  212 ? -1.099  -43.535 -12.755  1.00 55.28  ? 216  SER   B CA   1 
ATOM   12256 C  C    . SER   B  2  212 ? 0.090   -43.889 -13.647  1.00 55.20  ? 216  SER   B C    1 
ATOM   12257 O  O    . SER   B  2  212 ? 0.802   -44.867 -13.404  1.00 55.50  ? 216  SER   B O    1 
ATOM   12258 C  CB   . SER   B  2  212 ? -1.130  -42.049 -12.400  1.00 56.41  ? 216  SER   B CB   1 
ATOM   12259 O  OG   . SER   B  2  212 ? -1.336  -41.266 -13.561  1.00 58.96  ? 216  SER   B OG   1 
ATOM   12260 H  H    . SER   B  2  212 ? -0.293  -44.207 -11.108  1.00 64.73  ? 216  SER   B H    1 
ATOM   12261 H  HA   . SER   B  2  212 ? -1.925  -43.730 -13.224  1.00 66.31  ? 216  SER   B HA   1 
ATOM   12262 H  HB2  . SER   B  2  212 ? -1.856  -41.887 -11.776  1.00 67.67  ? 216  SER   B HB2  1 
ATOM   12263 H  HB3  . SER   B  2  212 ? -0.284  -41.801 -11.996  1.00 67.67  ? 216  SER   B HB3  1 
ATOM   12264 H  HG   . SER   B  2  212 ? -2.091  -41.433 -13.891  1.00 70.74  ? 216  SER   B HG   1 
ATOM   12265 N  N    . ALA   B  2  213 ? 0.300   -43.098 -14.695  1.00 57.04  ? 217  ALA   B N    1 
ATOM   12266 C  CA   . ALA   B  2  213 ? 1.408   -43.353 -15.601  1.00 54.92  ? 217  ALA   B CA   1 
ATOM   12267 C  C    . ALA   B  2  213 ? 1.831   -42.057 -16.277  1.00 52.00  ? 217  ALA   B C    1 
ATOM   12268 O  O    . ALA   B  2  213 ? 1.158   -41.028 -16.187  1.00 52.31  ? 217  ALA   B O    1 
ATOM   12269 C  CB   . ALA   B  2  213 ? 1.039   -44.407 -16.650  1.00 55.72  ? 217  ALA   B CB   1 
ATOM   12270 H  H    . ALA   B  2  213 ? -0.182  -42.415 -14.898  1.00 68.43  ? 217  ALA   B H    1 
ATOM   12271 H  HA   . ALA   B  2  213 ? 2.160   -43.675 -15.080  1.00 65.88  ? 217  ALA   B HA   1 
ATOM   12272 H  HB1  . ALA   B  2  213 ? 1.791   -44.533 -17.250  1.00 66.85  ? 217  ALA   B HB1  1 
ATOM   12273 H  HB2  . ALA   B  2  213 ? 0.831   -45.241 -16.200  1.00 66.85  ? 217  ALA   B HB2  1 
ATOM   12274 H  HB3  . ALA   B  2  213 ? 0.266   -44.099 -17.149  1.00 66.85  ? 217  ALA   B HB3  1 
ATOM   12275 N  N    . ASN   B  2  214 ? 2.974   -42.129 -16.948  1.00 53.52  ? 218  ASN   B N    1 
ATOM   12276 C  CA   . ASN   B  2  214 ? 3.496   -41.058 -17.788  1.00 53.82  ? 218  ASN   B CA   1 
ATOM   12277 C  C    . ASN   B  2  214 ? 4.526   -41.696 -18.715  1.00 53.79  ? 218  ASN   B C    1 
ATOM   12278 O  O    . ASN   B  2  214 ? 4.692   -42.921 -18.723  1.00 58.65  ? 218  ASN   B O    1 
ATOM   12279 C  CB   . ASN   B  2  214 ? 4.058   -39.914 -16.937  1.00 53.78  ? 218  ASN   B CB   1 
ATOM   12280 C  CG   . ASN   B  2  214 ? 5.360   -40.271 -16.257  1.00 58.19  ? 218  ASN   B CG   1 
ATOM   12281 O  OD1  . ASN   B  2  214 ? 6.361   -39.577 -16.420  1.00 59.94  ? 218  ASN   B OD1  1 
ATOM   12282 N  ND2  . ASN   B  2  214 ? 5.356   -41.352 -15.484  1.00 58.84  ? 218  ASN   B ND2  1 
ATOM   12283 H  H    . ASN   B  2  214 ? 3.488   -42.818 -16.933  1.00 64.21  ? 218  ASN   B H    1 
ATOM   12284 H  HA   . ASN   B  2  214 ? 2.786   -40.678 -18.329  1.00 64.56  ? 218  ASN   B HA   1 
ATOM   12285 H  HB2  . ASN   B  2  214 ? 4.219   -39.146 -17.508  1.00 64.52  ? 218  ASN   B HB2  1 
ATOM   12286 H  HB3  . ASN   B  2  214 ? 3.413   -39.686 -16.249  1.00 64.52  ? 218  ASN   B HB3  1 
ATOM   12287 H  HD21 . ASN   B  2  214 ? 6.074   -41.593 -15.077  1.00 70.59  ? 218  ASN   B HD21 1 
ATOM   12288 H  HD22 . ASN   B  2  214 ? 4.634   -41.811 -15.390  1.00 70.59  ? 218  ASN   B HD22 1 
ATOM   12289 N  N    . ILE   B  2  215 ? 5.226   -40.880 -19.500  1.00 50.48  ? 219  ILE   B N    1 
ATOM   12290 C  CA   . ILE   B  2  215 ? 5.992   -41.391 -20.631  1.00 51.99  ? 219  ILE   B CA   1 
ATOM   12291 C  C    . ILE   B  2  215 ? 7.493   -41.172 -20.514  1.00 54.01  ? 219  ILE   B C    1 
ATOM   12292 O  O    . ILE   B  2  215 ? 8.245   -41.784 -21.288  1.00 58.71  ? 219  ILE   B O    1 
ATOM   12293 C  CB   . ILE   B  2  215 ? 5.480   -40.802 -21.963  1.00 52.06  ? 219  ILE   B CB   1 
ATOM   12294 C  CG1  . ILE   B  2  215 ? 5.655   -39.284 -21.987  1.00 61.05  ? 219  ILE   B CG1  1 
ATOM   12295 C  CG2  . ILE   B  2  215 ? 4.019   -41.163 -22.159  1.00 50.92  ? 219  ILE   B CG2  1 
ATOM   12296 C  CD1  . ILE   B  2  215 ? 5.133   -38.636 -23.250  1.00 68.99  ? 219  ILE   B CD1  1 
ATOM   12297 H  H    . ILE   B  2  215 ? 5.272   -40.027 -19.397  1.00 60.55  ? 219  ILE   B H    1 
ATOM   12298 H  HA   . ILE   B  2  215 ? 5.861   -42.352 -20.657  1.00 62.36  ? 219  ILE   B HA   1 
ATOM   12299 H  HB   . ILE   B  2  215 ? 6.005   -41.180 -22.686  1.00 62.45  ? 219  ILE   B HB   1 
ATOM   12300 H  HG12 . ILE   B  2  215 ? 5.173   -38.902 -21.237  1.00 73.24  ? 219  ILE   B HG12 1 
ATOM   12301 H  HG13 . ILE   B  2  215 ? 6.599   -39.076 -21.915  1.00 73.24  ? 219  ILE   B HG13 1 
ATOM   12302 H  HG21 . ILE   B  2  215 ? 3.766   -40.966 -23.075  1.00 61.08  ? 219  ILE   B HG21 1 
ATOM   12303 H  HG22 . ILE   B  2  215 ? 3.900   -42.108 -21.979  1.00 61.08  ? 219  ILE   B HG22 1 
ATOM   12304 H  HG23 . ILE   B  2  215 ? 3.479   -40.638 -21.547  1.00 61.08  ? 219  ILE   B HG23 1 
ATOM   12305 H  HD11 . ILE   B  2  215 ? 5.400   -37.704 -23.261  1.00 82.77  ? 219  ILE   B HD11 1 
ATOM   12306 H  HD12 . ILE   B  2  215 ? 5.507   -39.096 -24.018  1.00 82.77  ? 219  ILE   B HD12 1 
ATOM   12307 H  HD13 . ILE   B  2  215 ? 4.166   -38.703 -23.263  1.00 82.77  ? 219  ILE   B HD13 1 
ATOM   12308 N  N    . ASP   B  2  216 ? 7.974   -40.340 -19.594  1.00 51.09  ? 220  ASP   B N    1 
ATOM   12309 C  CA   . ASP   B  2  216 ? 9.407   -40.126 -19.433  1.00 50.53  ? 220  ASP   B CA   1 
ATOM   12310 C  C    . ASP   B  2  216 ? 9.848   -40.598 -18.054  1.00 49.21  ? 220  ASP   B C    1 
ATOM   12311 O  O    . ASP   B  2  216 ? 9.137   -40.409 -17.060  1.00 45.27  ? 220  ASP   B O    1 
ATOM   12312 C  CB   . ASP   B  2  216 ? 9.789   -38.654 -19.645  1.00 51.90  ? 220  ASP   B CB   1 
ATOM   12313 C  CG   . ASP   B  2  216 ? 9.397   -37.769 -18.480  1.00 52.95  ? 220  ASP   B CG   1 
ATOM   12314 O  OD1  . ASP   B  2  216 ? 8.375   -38.059 -17.825  1.00 53.85  ? 220  ASP   B OD1  1 
ATOM   12315 O  OD2  . ASP   B  2  216 ? 10.114  -36.778 -18.222  1.00 51.82  ? 220  ASP   B OD2  1 
ATOM   12316 H  H    . ASP   B  2  216 ? 7.486   -39.887 -19.049  1.00 61.29  ? 220  ASP   B H    1 
ATOM   12317 H  HA   . ASP   B  2  216 ? 9.885   -40.650 -20.095  1.00 60.62  ? 220  ASP   B HA   1 
ATOM   12318 H  HB2  . ASP   B  2  216 ? 10.750  -38.590 -19.759  1.00 62.26  ? 220  ASP   B HB2  1 
ATOM   12319 H  HB3  . ASP   B  2  216 ? 9.338   -38.322 -20.437  1.00 62.26  ? 220  ASP   B HB3  1 
ATOM   12320 N  N    . THR   B  2  217 ? 11.036  -41.204 -18.006  1.00 50.07  ? 221  THR   B N    1 
ATOM   12321 C  CA   . THR   B  2  217 ? 11.467  -41.919 -16.805  1.00 52.31  ? 221  THR   B CA   1 
ATOM   12322 C  C    . THR   B  2  217 ? 11.615  -41.010 -15.593  1.00 50.49  ? 221  THR   B C    1 
ATOM   12323 O  O    . THR   B  2  217 ? 11.054  -41.339 -14.533  1.00 50.42  ? 221  THR   B O    1 
ATOM   12324 C  CB   . THR   B  2  217 ? 12.771  -42.670 -17.105  1.00 54.23  ? 221  THR   B CB   1 
ATOM   12325 O  OG1  . THR   B  2  217 ? 12.490  -43.827 -17.905  1.00 55.53  ? 221  THR   B OG1  1 
ATOM   12326 C  CG2  . THR   B  2  217 ? 13.464  -43.097 -15.820  1.00 52.23  ? 221  THR   B CG2  1 
ATOM   12327 H  H    . THR   B  2  217 ? 11.607  -41.215 -18.649  1.00 60.07  ? 221  THR   B H    1 
ATOM   12328 H  HA   . THR   B  2  217 ? 10.779  -42.569 -16.591  1.00 62.76  ? 221  THR   B HA   1 
ATOM   12329 H  HB   . THR   B  2  217 ? 13.372  -42.081 -17.587  1.00 65.05  ? 221  THR   B HB   1 
ATOM   12330 H  HG1  . THR   B  2  217 ? 13.177  -44.054 -18.332  1.00 66.61  ? 221  THR   B HG1  1 
ATOM   12331 H  HG21 . THR   B  2  217 ? 14.121  -43.785 -16.010  1.00 62.65  ? 221  THR   B HG21 1 
ATOM   12332 H  HG22 . THR   B  2  217 ? 13.911  -42.337 -15.415  1.00 62.65  ? 221  THR   B HG22 1 
ATOM   12333 H  HG23 . THR   B  2  217 ? 12.813  -43.450 -15.193  1.00 62.65  ? 221  THR   B HG23 1 
ATOM   12334 N  N    . PRO   B  2  218 ? 12.339  -39.893 -15.653  1.00 50.06  ? 222  PRO   B N    1 
ATOM   12335 C  CA   . PRO   B  2  218 ? 12.444  -39.030 -14.469  1.00 52.89  ? 222  PRO   B CA   1 
ATOM   12336 C  C    . PRO   B  2  218 ? 11.074  -38.519 -14.048  1.00 57.98  ? 222  PRO   B C    1 
ATOM   12337 O  O    . PRO   B  2  218 ? 10.280  -38.067 -14.875  1.00 69.63  ? 222  PRO   B O    1 
ATOM   12338 C  CB   . PRO   B  2  218 ? 13.360  -37.891 -14.934  1.00 48.18  ? 222  PRO   B CB   1 
ATOM   12339 C  CG   . PRO   B  2  218 ? 14.074  -38.425 -16.130  1.00 46.74  ? 222  PRO   B CG   1 
ATOM   12340 C  CD   . PRO   B  2  218 ? 13.109  -39.359 -16.789  1.00 48.27  ? 222  PRO   B CD   1 
ATOM   12341 H  HA   . PRO   B  2  218 ? 12.863  -39.501 -13.732  1.00 63.44  ? 222  PRO   B HA   1 
ATOM   12342 H  HB2  . PRO   B  2  218 ? 12.828  -37.114 -15.167  1.00 57.80  ? 222  PRO   B HB2  1 
ATOM   12343 H  HB3  . PRO   B  2  218 ? 13.987  -37.664 -14.230  1.00 57.80  ? 222  PRO   B HB3  1 
ATOM   12344 H  HG2  . PRO   B  2  218 ? 14.309  -37.696 -16.726  1.00 56.07  ? 222  PRO   B HG2  1 
ATOM   12345 H  HG3  . PRO   B  2  218 ? 14.875  -38.896 -15.852  1.00 56.07  ? 222  PRO   B HG3  1 
ATOM   12346 H  HD2  . PRO   B  2  218 ? 12.532  -38.883 -17.406  1.00 57.91  ? 222  PRO   B HD2  1 
ATOM   12347 H  HD3  . PRO   B  2  218 ? 13.578  -40.070 -17.254  1.00 57.91  ? 222  PRO   B HD3  1 
ATOM   12348 N  N    . GLU   B  2  219 ? 10.804  -38.592 -12.749  1.00 53.39  ? 223  GLU   B N    1 
ATOM   12349 C  CA   . GLU   B  2  219 ? 9.504   -38.249 -12.190  1.00 52.48  ? 223  GLU   B CA   1 
ATOM   12350 C  C    . GLU   B  2  219 ? 9.593   -36.934 -11.424  1.00 52.14  ? 223  GLU   B C    1 
ATOM   12351 O  O    . GLU   B  2  219 ? 10.678  -36.433 -11.117  1.00 51.16  ? 223  GLU   B O    1 
ATOM   12352 C  CB   . GLU   B  2  219 ? 8.995   -39.372 -11.276  1.00 50.88  ? 223  GLU   B CB   1 
ATOM   12353 C  CG   . GLU   B  2  219 ? 9.061   -40.768 -11.893  1.00 51.66  ? 223  GLU   B CG   1 
ATOM   12354 C  CD   . GLU   B  2  219 ? 8.072   -40.969 -13.031  1.00 57.72  ? 223  GLU   B CD   1 
ATOM   12355 O  OE1  . GLU   B  2  219 ? 7.682   -39.975 -13.679  1.00 59.27  ? 223  GLU   B OE1  1 
ATOM   12356 O  OE2  . GLU   B  2  219 ? 7.683   -42.130 -13.276  1.00 64.25  ? 223  GLU   B OE2  1 
ATOM   12357 H  H    . GLU   B  2  219 ? 11.374  -38.844 -12.156  1.00 64.05  ? 223  GLU   B H    1 
ATOM   12358 H  HA   . GLU   B  2  219 ? 8.865   -38.135 -12.910  1.00 62.96  ? 223  GLU   B HA   1 
ATOM   12359 H  HB2  . GLU   B  2  219 ? 9.534   -39.383 -10.469  1.00 61.03  ? 223  GLU   B HB2  1 
ATOM   12360 H  HB3  . GLU   B  2  219 ? 8.068   -39.193 -11.053  1.00 61.03  ? 223  GLU   B HB3  1 
ATOM   12361 H  HG2  . GLU   B  2  219 ? 9.953   -40.915 -12.244  1.00 61.97  ? 223  GLU   B HG2  1 
ATOM   12362 H  HG3  . GLU   B  2  219 ? 8.862   -41.425 -11.207  1.00 61.97  ? 223  GLU   B HG3  1 
ATOM   12363 N  N    . GLY   B  2  220 ? 8.423   -36.378 -11.114  1.00 51.92  ? 224  GLY   B N    1 
ATOM   12364 C  CA   . GLY   B  2  220 ? 8.345   -35.064 -10.507  1.00 54.18  ? 224  GLY   B CA   1 
ATOM   12365 C  C    . GLY   B  2  220 ? 8.194   -35.087 -9.001   1.00 53.69  ? 224  GLY   B C    1 
ATOM   12366 O  O    . GLY   B  2  220 ? 7.463   -34.270 -8.433   1.00 53.49  ? 224  GLY   B O    1 
ATOM   12367 H  H    . GLY   B  2  220 ? 7.659   -36.749 -11.248  1.00 62.28  ? 224  GLY   B H    1 
ATOM   12368 H  HA2  . GLY   B  2  220 ? 9.153   -34.571 -10.719  1.00 64.99  ? 224  GLY   B HA2  1 
ATOM   12369 H  HA3  . GLY   B  2  220 ? 7.582   -34.592 -10.877  1.00 64.99  ? 224  GLY   B HA3  1 
ATOM   12370 N  N    . GLY   B  2  221 ? 8.888   -36.014 -8.338   1.00 51.57  ? 225  GLY   B N    1 
ATOM   12371 C  CA   . GLY   B  2  221 ? 8.777   -36.129 -6.895   1.00 53.03  ? 225  GLY   B CA   1 
ATOM   12372 C  C    . GLY   B  2  221 ? 9.377   -34.967 -6.131   1.00 55.71  ? 225  GLY   B C    1 
ATOM   12373 O  O    . GLY   B  2  221 ? 8.977   -34.721 -4.988   1.00 55.74  ? 225  GLY   B O    1 
ATOM   12374 H  H    . GLY   B  2  221 ? 9.423   -36.580 -8.701   1.00 61.86  ? 225  GLY   B H    1 
ATOM   12375 H  HA2  . GLY   B  2  221 ? 7.838   -36.189 -6.657   1.00 63.62  ? 225  GLY   B HA2  1 
ATOM   12376 H  HA3  . GLY   B  2  221 ? 9.228   -36.938 -6.609   1.00 63.62  ? 225  GLY   B HA3  1 
ATOM   12377 N  N    . PHE   B  2  222 ? 10.327  -34.247 -6.731   1.00 52.88  ? 226  PHE   B N    1 
ATOM   12378 C  CA   . PHE   B  2  222 ? 10.902  -33.094 -6.046   1.00 52.18  ? 226  PHE   B CA   1 
ATOM   12379 C  C    . PHE   B  2  222 ? 9.848   -32.023 -5.787   1.00 49.79  ? 226  PHE   B C    1 
ATOM   12380 O  O    . PHE   B  2  222 ? 9.905   -31.335 -4.761   1.00 48.62  ? 226  PHE   B O    1 
ATOM   12381 C  CB   . PHE   B  2  222 ? 12.071  -32.525 -6.854   1.00 53.84  ? 226  PHE   B CB   1 
ATOM   12382 C  CG   . PHE   B  2  222 ? 13.348  -33.321 -6.725   1.00 57.02  ? 226  PHE   B CG   1 
ATOM   12383 C  CD1  . PHE   B  2  222 ? 13.349  -34.584 -6.151   1.00 58.03  ? 226  PHE   B CD1  1 
ATOM   12384 C  CD2  . PHE   B  2  222 ? 14.551  -32.796 -7.167   1.00 57.56  ? 226  PHE   B CD2  1 
ATOM   12385 C  CE1  . PHE   B  2  222 ? 14.519  -35.308 -6.030   1.00 60.76  ? 226  PHE   B CE1  1 
ATOM   12386 C  CE2  . PHE   B  2  222 ? 15.727  -33.518 -7.048   1.00 59.29  ? 226  PHE   B CE2  1 
ATOM   12387 C  CZ   . PHE   B  2  222 ? 15.709  -34.776 -6.479   1.00 60.28  ? 226  PHE   B CZ   1 
ATOM   12388 H  H    . PHE   B  2  222 ? 10.648  -34.402 -7.514   1.00 63.44  ? 226  PHE   B H    1 
ATOM   12389 H  HA   . PHE   B  2  222 ? 11.255  -33.378 -5.189   1.00 62.59  ? 226  PHE   B HA   1 
ATOM   12390 H  HB2  . PHE   B  2  222 ? 11.824  -32.512 -7.792   1.00 64.59  ? 226  PHE   B HB2  1 
ATOM   12391 H  HB3  . PHE   B  2  222 ? 12.252  -31.623 -6.546   1.00 64.59  ? 226  PHE   B HB3  1 
ATOM   12392 H  HD1  . PHE   B  2  222 ? 12.550  -34.949 -5.844   1.00 69.62  ? 226  PHE   B HD1  1 
ATOM   12393 H  HD2  . PHE   B  2  222 ? 14.569  -31.948 -7.549   1.00 69.05  ? 226  PHE   B HD2  1 
ATOM   12394 H  HE1  . PHE   B  2  222 ? 14.504  -36.155 -5.645   1.00 72.90  ? 226  PHE   B HE1  1 
ATOM   12395 H  HE2  . PHE   B  2  222 ? 16.528  -33.156 -7.351   1.00 71.12  ? 226  PHE   B HE2  1 
ATOM   12396 H  HZ   . PHE   B  2  222 ? 16.497  -35.262 -6.398   1.00 72.32  ? 226  PHE   B HZ   1 
ATOM   12397 N  N    . ASP   B  2  223 ? 8.881   -31.865 -6.696   1.00 51.01  ? 227  ASP   B N    1 
ATOM   12398 C  CA   . ASP   B  2  223 ? 7.728   -31.022 -6.395   1.00 54.50  ? 227  ASP   B CA   1 
ATOM   12399 C  C    . ASP   B  2  223 ? 7.019   -31.509 -5.138   1.00 56.43  ? 227  ASP   B C    1 
ATOM   12400 O  O    . ASP   B  2  223 ? 6.647   -30.707 -4.273   1.00 55.87  ? 227  ASP   B O    1 
ATOM   12401 C  CB   . ASP   B  2  223 ? 6.753   -31.006 -7.573   1.00 55.05  ? 227  ASP   B CB   1 
ATOM   12402 C  CG   . ASP   B  2  223 ? 7.070   -29.923 -8.587   1.00 58.84  ? 227  ASP   B CG   1 
ATOM   12403 O  OD1  . ASP   B  2  223 ? 7.729   -28.928 -8.221   1.00 59.88  ? 227  ASP   B OD1  1 
ATOM   12404 O  OD2  . ASP   B  2  223 ? 6.645   -30.063 -9.754   1.00 59.53  ? 227  ASP   B OD2  1 
ATOM   12405 H  H    . ASP   B  2  223 ? 8.871   -32.228 -7.476   1.00 61.19  ? 227  ASP   B H    1 
ATOM   12406 H  HA   . ASP   B  2  223 ? 8.038   -30.114 -6.250   1.00 65.39  ? 227  ASP   B HA   1 
ATOM   12407 H  HB2  . ASP   B  2  223 ? 6.792   -31.862 -8.028   1.00 66.04  ? 227  ASP   B HB2  1 
ATOM   12408 H  HB3  . ASP   B  2  223 ? 5.856   -30.849 -7.239   1.00 66.04  ? 227  ASP   B HB3  1 
ATOM   12409 N  N    . ALA   B  2  224 ? 6.827   -32.824 -5.020   1.00 58.34  ? 228  ALA   B N    1 
ATOM   12410 C  CA   . ALA   B  2  224 ? 6.121   -33.372 -3.868   1.00 53.20  ? 228  ALA   B CA   1 
ATOM   12411 C  C    . ALA   B  2  224 ? 6.928   -33.197 -2.587   1.00 51.35  ? 228  ALA   B C    1 
ATOM   12412 O  O    . ALA   B  2  224 ? 6.362   -32.904 -1.528   1.00 51.83  ? 228  ALA   B O    1 
ATOM   12413 C  CB   . ALA   B  2  224 ? 5.800   -34.846 -4.108   1.00 50.74  ? 228  ALA   B CB   1 
ATOM   12414 H  H    . ALA   B  2  224 ? 7.094   -33.413 -5.588   1.00 69.99  ? 228  ALA   B H    1 
ATOM   12415 H  HA   . ALA   B  2  224 ? 5.283   -32.895 -3.758   1.00 63.82  ? 228  ALA   B HA   1 
ATOM   12416 H  HB1  . ALA   B  2  224 ? 5.296   -35.187 -3.353   1.00 60.86  ? 228  ALA   B HB1  1 
ATOM   12417 H  HB2  . ALA   B  2  224 ? 5.276   -34.928 -4.920   1.00 60.86  ? 228  ALA   B HB2  1 
ATOM   12418 H  HB3  . ALA   B  2  224 ? 6.631   -35.339 -4.200   1.00 60.86  ? 228  ALA   B HB3  1 
ATOM   12419 N  N    . ILE   B  2  225 ? 8.249   -33.380 -2.659   1.00 50.73  ? 229  ILE   B N    1 
ATOM   12420 C  CA   . ILE   B  2  225 ? 9.093   -33.167 -1.485   1.00 52.46  ? 229  ILE   B CA   1 
ATOM   12421 C  C    . ILE   B  2  225 ? 8.926   -31.743 -0.972   1.00 56.21  ? 229  ILE   B C    1 
ATOM   12422 O  O    . ILE   B  2  225 ? 8.729   -31.513 0.228    1.00 57.52  ? 229  ILE   B O    1 
ATOM   12423 C  CB   . ILE   B  2  225 ? 10.566  -33.475 -1.816   1.00 50.28  ? 229  ILE   B CB   1 
ATOM   12424 C  CG1  . ILE   B  2  225 ? 10.741  -34.965 -2.123   1.00 48.03  ? 229  ILE   B CG1  1 
ATOM   12425 C  CG2  . ILE   B  2  225 ? 11.480  -33.049 -0.663   1.00 44.31  ? 229  ILE   B CG2  1 
ATOM   12426 C  CD1  . ILE   B  2  225 ? 12.144  -35.344 -2.557   1.00 46.29  ? 229  ILE   B CD1  1 
ATOM   12427 H  H    . ILE   B  2  225 ? 8.674   -33.625 -3.366   1.00 60.86  ? 229  ILE   B H    1 
ATOM   12428 H  HA   . ILE   B  2  225 ? 8.809   -33.777 -0.787   1.00 62.93  ? 229  ILE   B HA   1 
ATOM   12429 H  HB   . ILE   B  2  225 ? 10.814  -32.966 -2.604   1.00 60.32  ? 229  ILE   B HB   1 
ATOM   12430 H  HG12 . ILE   B  2  225 ? 10.531  -35.473 -1.324   1.00 57.62  ? 229  ILE   B HG12 1 
ATOM   12431 H  HG13 . ILE   B  2  225 ? 10.134  -35.208 -2.840   1.00 57.62  ? 229  ILE   B HG13 1 
ATOM   12432 H  HG21 . ILE   B  2  225 ? 12.393  -33.294 -0.877   1.00 53.16  ? 229  ILE   B HG21 1 
ATOM   12433 H  HG22 . ILE   B  2  225 ? 11.414  -32.088 -0.547   1.00 53.16  ? 229  ILE   B HG22 1 
ATOM   12434 H  HG23 . ILE   B  2  225 ? 11.197  -33.500 0.147    1.00 53.16  ? 229  ILE   B HG23 1 
ATOM   12435 H  HD11 . ILE   B  2  225 ? 12.149  -36.275 -2.832   1.00 55.52  ? 229  ILE   B HD11 1 
ATOM   12436 H  HD12 . ILE   B  2  225 ? 12.409  -34.779 -3.299   1.00 55.52  ? 229  ILE   B HD12 1 
ATOM   12437 H  HD13 . ILE   B  2  225 ? 12.751  -35.217 -1.811   1.00 55.52  ? 229  ILE   B HD13 1 
ATOM   12438 N  N    . MET   B  2  226 ? 9.013   -30.765 -1.875   1.00 55.67  ? 230  MET   B N    1 
ATOM   12439 C  CA   . MET   B  2  226 ? 8.879   -29.367 -1.480   1.00 54.58  ? 230  MET   B CA   1 
ATOM   12440 C  C    . MET   B  2  226 ? 7.582   -29.134 -0.717   1.00 52.97  ? 230  MET   B C    1 
ATOM   12441 O  O    . MET   B  2  226 ? 7.582   -28.552 0.374    1.00 50.60  ? 230  MET   B O    1 
ATOM   12442 C  CB   . MET   B  2  226 ? 8.940   -28.474 -2.723   1.00 54.09  ? 230  MET   B CB   1 
ATOM   12443 C  CG   . MET   B  2  226 ? 8.676   -27.001 -2.454   1.00 52.15  ? 230  MET   B CG   1 
ATOM   12444 S  SD   . MET   B  2  226 ? 9.918   -26.265 -1.380   1.00 51.84  ? 230  MET   B SD   1 
ATOM   12445 C  CE   . MET   B  2  226 ? 11.326  -26.225 -2.488   1.00 51.68  ? 230  MET   B CE   1 
ATOM   12446 H  H    . MET   B  2  226 ? 9.147   -30.885 -2.716   1.00 66.79  ? 230  MET   B H    1 
ATOM   12447 H  HA   . MET   B  2  226 ? 9.624   -29.132 -0.905   1.00 65.48  ? 230  MET   B HA   1 
ATOM   12448 H  HB2  . MET   B  2  226 ? 9.826   -28.547 -3.112   1.00 64.89  ? 230  MET   B HB2  1 
ATOM   12449 H  HB3  . MET   B  2  226 ? 8.273   -28.781 -3.356   1.00 64.89  ? 230  MET   B HB3  1 
ATOM   12450 H  HG2  . MET   B  2  226 ? 8.681   -26.519 -3.295   1.00 62.56  ? 230  MET   B HG2  1 
ATOM   12451 H  HG3  . MET   B  2  226 ? 7.812   -26.907 -2.023   1.00 62.56  ? 230  MET   B HG3  1 
ATOM   12452 H  HE1  . MET   B  2  226 ? 12.073  -25.804 -2.034   1.00 62.00  ? 230  MET   B HE1  1 
ATOM   12453 H  HE2  . MET   B  2  226 ? 11.558  -27.133 -2.736   1.00 62.00  ? 230  MET   B HE2  1 
ATOM   12454 H  HE3  . MET   B  2  226 ? 11.091  -25.715 -3.279   1.00 62.00  ? 230  MET   B HE3  1 
ATOM   12455 N  N    . GLN   B  2  227 ? 6.461   -29.585 -1.281   1.00 53.74  ? 231  GLN   B N    1 
ATOM   12456 C  CA   . GLN   B  2  227 ? 5.171   -29.366 -0.637   1.00 56.59  ? 231  GLN   B CA   1 
ATOM   12457 C  C    . GLN   B  2  227 ? 5.091   -30.080 0.706    1.00 56.66  ? 231  GLN   B C    1 
ATOM   12458 O  O    . GLN   B  2  227 ? 4.546   -29.537 1.674    1.00 57.21  ? 231  GLN   B O    1 
ATOM   12459 C  CB   . GLN   B  2  227 ? 4.044   -29.834 -1.555   1.00 54.32  ? 231  GLN   B CB   1 
ATOM   12460 C  CG   . GLN   B  2  227 ? 3.907   -29.011 -2.820   1.00 54.13  ? 231  GLN   B CG   1 
ATOM   12461 C  CD   . GLN   B  2  227 ? 3.593   -27.556 -2.530   1.00 55.61  ? 231  GLN   B CD   1 
ATOM   12462 O  OE1  . GLN   B  2  227 ? 2.523   -27.230 -2.015   1.00 57.43  ? 231  GLN   B OE1  1 
ATOM   12463 N  NE2  . GLN   B  2  227 ? 4.532   -26.673 -2.848   1.00 55.71  ? 231  GLN   B NE2  1 
ATOM   12464 H  H    . GLN   B  2  227 ? 6.421   -30.014 -2.026   1.00 64.47  ? 231  GLN   B H    1 
ATOM   12465 H  HA   . GLN   B  2  227 ? 5.060   -28.416 -0.478   1.00 67.88  ? 231  GLN   B HA   1 
ATOM   12466 H  HB2  . GLN   B  2  227 ? 4.216   -30.753 -1.817   1.00 65.17  ? 231  GLN   B HB2  1 
ATOM   12467 H  HB3  . GLN   B  2  227 ? 3.204   -29.779 -1.073   1.00 65.17  ? 231  GLN   B HB3  1 
ATOM   12468 H  HG2  . GLN   B  2  227 ? 4.741   -29.047 -3.314   1.00 64.94  ? 231  GLN   B HG2  1 
ATOM   12469 H  HG3  . GLN   B  2  227 ? 3.186   -29.374 -3.358   1.00 64.94  ? 231  GLN   B HG3  1 
ATOM   12470 H  HE21 . GLN   B  2  227 ? 5.271   -26.939 -3.198   1.00 66.83  ? 231  GLN   B HE21 1 
ATOM   12471 H  HE22 . GLN   B  2  227 ? 4.402   -25.835 -2.703   1.00 66.83  ? 231  GLN   B HE22 1 
ATOM   12472 N  N    . ALA   B  2  228 ? 5.627   -31.299 0.785    1.00 54.91  ? 232  ALA   B N    1 
ATOM   12473 C  CA   . ALA   B  2  228 ? 5.553   -32.049 2.033    1.00 56.35  ? 232  ALA   B CA   1 
ATOM   12474 C  C    . ALA   B  2  228 ? 6.373   -31.390 3.133    1.00 56.09  ? 232  ALA   B C    1 
ATOM   12475 O  O    . ALA   B  2  228 ? 6.037   -31.520 4.316    1.00 61.85  ? 232  ALA   B O    1 
ATOM   12476 C  CB   . ALA   B  2  228 ? 6.022   -33.485 1.810    1.00 55.50  ? 232  ALA   B CB   1 
ATOM   12477 H  H    . ALA   B  2  228 ? 6.031   -31.704 0.143    1.00 65.87  ? 232  ALA   B H    1 
ATOM   12478 H  HA   . ALA   B  2  228 ? 4.628   -32.077 2.325    1.00 67.60  ? 232  ALA   B HA   1 
ATOM   12479 H  HB1  . ALA   B  2  228 ? 5.957   -33.972 2.646    1.00 66.58  ? 232  ALA   B HB1  1 
ATOM   12480 H  HB2  . ALA   B  2  228 ? 5.456   -33.902 1.140    1.00 66.58  ? 232  ALA   B HB2  1 
ATOM   12481 H  HB3  . ALA   B  2  228 ? 6.942   -33.473 1.504    1.00 66.58  ? 232  ALA   B HB3  1 
ATOM   12482 N  N    . ALA   B  2  229 ? 7.442   -30.681 2.769    1.00 54.10  ? 233  ALA   B N    1 
ATOM   12483 C  CA   . ALA   B  2  229 ? 8.279   -30.027 3.767    1.00 58.25  ? 233  ALA   B CA   1 
ATOM   12484 C  C    . ALA   B  2  229 ? 7.713   -28.680 4.199    1.00 59.48  ? 233  ALA   B C    1 
ATOM   12485 O  O    . ALA   B  2  229 ? 7.913   -28.271 5.348    1.00 59.81  ? 233  ALA   B O    1 
ATOM   12486 C  CB   . ALA   B  2  229 ? 9.697   -29.841 3.222    1.00 58.27  ? 233  ALA   B CB   1 
ATOM   12487 H  H    . ALA   B  2  229 ? 7.701   -30.566 1.957    1.00 64.90  ? 233  ALA   B H    1 
ATOM   12488 H  HA   . ALA   B  2  229 ? 8.327   -30.597 4.550    1.00 69.88  ? 233  ALA   B HA   1 
ATOM   12489 H  HB1  . ALA   B  2  229 ? 10.239  -29.400 3.895    1.00 69.91  ? 233  ALA   B HB1  1 
ATOM   12490 H  HB2  . ALA   B  2  229 ? 10.072  -30.711 3.014    1.00 69.91  ? 233  ALA   B HB2  1 
ATOM   12491 H  HB3  . ALA   B  2  229 ? 9.659   -29.297 2.420    1.00 69.91  ? 233  ALA   B HB3  1 
ATOM   12492 N  N    . VAL   B  2  230 ? 7.005   -27.987 3.310    1.00 56.42  ? 234  VAL   B N    1 
ATOM   12493 C  CA   . VAL   B  2  230 ? 6.564   -26.622 3.583    1.00 55.53  ? 234  VAL   B CA   1 
ATOM   12494 C  C    . VAL   B  2  230 ? 5.168   -26.588 4.196    1.00 57.45  ? 234  VAL   B C    1 
ATOM   12495 O  O    . VAL   B  2  230 ? 4.908   -25.803 5.111    1.00 59.99  ? 234  VAL   B O    1 
ATOM   12496 C  CB   . VAL   B  2  230 ? 6.630   -25.793 2.284    1.00 61.76  ? 234  VAL   B CB   1 
ATOM   12497 C  CG1  . VAL   B  2  230 ? 5.942   -24.449 2.464    1.00 75.35  ? 234  VAL   B CG1  1 
ATOM   12498 C  CG2  . VAL   B  2  230 ? 8.079   -25.595 1.859    1.00 56.41  ? 234  VAL   B CG2  1 
ATOM   12499 H  H    . VAL   B  2  230 ? 6.767   -28.286 2.540    1.00 67.68  ? 234  VAL   B H    1 
ATOM   12500 H  HA   . VAL   B  2  230 ? 7.168   -26.226 4.230    1.00 66.62  ? 234  VAL   B HA   1 
ATOM   12501 H  HB   . VAL   B  2  230 ? 6.166   -26.275 1.582    1.00 74.09  ? 234  VAL   B HB   1 
ATOM   12502 H  HG11 . VAL   B  2  230 ? 6.143   -23.886 1.700    1.00 90.41  ? 234  VAL   B HG11 1 
ATOM   12503 H  HG12 . VAL   B  2  230 ? 4.984   -24.590 2.527    1.00 90.41  ? 234  VAL   B HG12 1 
ATOM   12504 H  HG13 . VAL   B  2  230 ? 6.269   -24.032 3.276    1.00 90.41  ? 234  VAL   B HG13 1 
ATOM   12505 H  HG21 . VAL   B  2  230 ? 8.101   -25.045 1.060    1.00 67.67  ? 234  VAL   B HG21 1 
ATOM   12506 H  HG22 . VAL   B  2  230 ? 8.561   -25.155 2.577    1.00 67.67  ? 234  VAL   B HG22 1 
ATOM   12507 H  HG23 . VAL   B  2  230 ? 8.476   -26.461 1.676    1.00 67.67  ? 234  VAL   B HG23 1 
ATOM   12508 N  N    . CYS   B  2  231 ? 4.251   -27.427 3.715    1.00 55.30  ? 235  CYS   B N    1 
ATOM   12509 C  CA   . CYS   B  2  231 ? 2.867   -27.382 4.173    1.00 57.93  ? 235  CYS   B CA   1 
ATOM   12510 C  C    . CYS   B  2  231 ? 2.738   -27.966 5.575    1.00 63.95  ? 235  CYS   B C    1 
ATOM   12511 O  O    . CYS   B  2  231 ? 2.140   -29.032 5.758    1.00 68.56  ? 235  CYS   B O    1 
ATOM   12512 C  CB   . CYS   B  2  231 ? 1.963   -28.139 3.197    1.00 57.14  ? 235  CYS   B CB   1 
ATOM   12513 S  SG   . CYS   B  2  231 ? 2.031   -27.556 1.483    1.00 59.91  ? 235  CYS   B SG   1 
ATOM   12514 H  H    . CYS   B  2  231 ? 4.407   -28.031 3.123    1.00 66.34  ? 235  CYS   B H    1 
ATOM   12515 H  HA   . CYS   B  2  231 ? 2.575   -26.458 4.206    1.00 69.49  ? 235  CYS   B HA   1 
ATOM   12516 H  HB2  . CYS   B  2  231 ? 2.225   -29.073 3.198    1.00 68.55  ? 235  CYS   B HB2  1 
ATOM   12517 H  HB3  . CYS   B  2  231 ? 1.045   -28.052 3.498    1.00 68.55  ? 235  CYS   B HB3  1 
ATOM   12518 N  N    . LYS   B  2  232 ? 3.283   -27.265 6.573    1.00 63.10  ? 236  LYS   B N    1 
ATOM   12519 C  CA   . LYS   B  2  232 ? 3.321   -27.804 7.930    1.00 62.67  ? 236  LYS   B CA   1 
ATOM   12520 C  C    . LYS   B  2  232 ? 1.921   -28.096 8.460    1.00 64.94  ? 236  LYS   B C    1 
ATOM   12521 O  O    . LYS   B  2  232 ? 1.691   -29.145 9.074    1.00 65.24  ? 236  LYS   B O    1 
ATOM   12522 C  CB   . LYS   B  2  232 ? 4.052   -26.830 8.857    1.00 62.26  ? 236  LYS   B CB   1 
ATOM   12523 C  CG   . LYS   B  2  232 ? 3.983   -27.185 10.339   1.00 64.01  ? 236  LYS   B CG   1 
ATOM   12524 C  CD   . LYS   B  2  232 ? 4.791   -26.204 11.177   1.00 64.30  ? 236  LYS   B CD   1 
ATOM   12525 C  CE   . LYS   B  2  232 ? 4.484   -26.335 12.663   1.00 67.77  ? 236  LYS   B CE   1 
ATOM   12526 N  NZ   . LYS   B  2  232 ? 4.922   -27.641 13.231   1.00 69.17  ? 236  LYS   B NZ   1 
ATOM   12527 H  H    . LYS   B  2  232 ? 3.634   -26.484 6.490    1.00 75.70  ? 236  LYS   B H    1 
ATOM   12528 H  HA   . LYS   B  2  232 ? 3.811   -28.641 7.916    1.00 75.18  ? 236  LYS   B HA   1 
ATOM   12529 H  HB2  . LYS   B  2  232 ? 4.988   -26.809 8.605    1.00 74.70  ? 236  LYS   B HB2  1 
ATOM   12530 H  HB3  . LYS   B  2  232 ? 3.660   -25.949 8.749    1.00 74.70  ? 236  LYS   B HB3  1 
ATOM   12531 H  HG2  . LYS   B  2  232 ? 3.060   -27.154 10.636   1.00 76.79  ? 236  LYS   B HG2  1 
ATOM   12532 H  HG3  . LYS   B  2  232 ? 4.345   -28.075 10.475   1.00 76.79  ? 236  LYS   B HG3  1 
ATOM   12533 H  HD2  . LYS   B  2  232 ? 5.736   -26.375 11.046   1.00 77.14  ? 236  LYS   B HD2  1 
ATOM   12534 H  HD3  . LYS   B  2  232 ? 4.577   -25.298 10.902   1.00 77.14  ? 236  LYS   B HD3  1 
ATOM   12535 H  HE2  . LYS   B  2  232 ? 4.945   -25.630 13.144   1.00 81.30  ? 236  LYS   B HE2  1 
ATOM   12536 H  HE3  . LYS   B  2  232 ? 3.527   -26.256 12.796   1.00 81.30  ? 236  LYS   B HE3  1 
ATOM   12537 H  HZ1  . LYS   B  2  232 ? 4.950   -27.594 14.119   1.00 82.98  ? 236  LYS   B HZ1  1 
ATOM   12538 H  HZ2  . LYS   B  2  232 ? 4.352   -28.282 12.994   1.00 82.98  ? 236  LYS   B HZ2  1 
ATOM   12539 H  HZ3  . LYS   B  2  232 ? 5.732   -27.849 12.927   1.00 82.98  ? 236  LYS   B HZ3  1 
ATOM   12540 N  N    . GLU   B  2  233 ? 0.975   -27.182 8.242    1.00 67.32  ? 237  GLU   B N    1 
ATOM   12541 C  CA   . GLU   B  2  233 ? -0.357  -27.357 8.814    1.00 71.44  ? 237  GLU   B CA   1 
ATOM   12542 C  C    . GLU   B  2  233 ? -1.097  -28.509 8.144    1.00 67.11  ? 237  GLU   B C    1 
ATOM   12543 O  O    . GLU   B  2  233 ? -1.647  -29.385 8.821    1.00 64.21  ? 237  GLU   B O    1 
ATOM   12544 C  CB   . GLU   B  2  233 ? -1.159  -26.060 8.691    1.00 82.80  ? 237  GLU   B CB   1 
ATOM   12545 C  CG   . GLU   B  2  233 ? -2.510  -26.102 9.391    1.00 96.55  ? 237  GLU   B CG   1 
ATOM   12546 C  CD   . GLU   B  2  233 ? -3.326  -24.844 9.165    1.00 109.97 ? 237  GLU   B CD   1 
ATOM   12547 O  OE1  . GLU   B  2  233 ? -2.988  -24.070 8.244    1.00 112.81 ? 237  GLU   B OE1  1 
ATOM   12548 O  OE2  . GLU   B  2  233 ? -4.305  -24.629 9.910    1.00 116.40 ? 237  GLU   B OE2  1 
ATOM   12549 H  H    . GLU   B  2  233 ? 1.077   -26.466 7.776    1.00 80.77  ? 237  GLU   B H    1 
ATOM   12550 H  HA   . GLU   B  2  233 ? -0.264  -27.565 9.757    1.00 85.71  ? 237  GLU   B HA   1 
ATOM   12551 H  HB2  . GLU   B  2  233 ? -0.645  -25.337 9.084    1.00 99.34  ? 237  GLU   B HB2  1 
ATOM   12552 H  HB3  . GLU   B  2  233 ? -1.318  -25.880 7.751    1.00 99.34  ? 237  GLU   B HB3  1 
ATOM   12553 H  HG2  . GLU   B  2  233 ? -3.019  -26.855 9.052    1.00 115.85 ? 237  GLU   B HG2  1 
ATOM   12554 H  HG3  . GLU   B  2  233 ? -2.369  -26.200 10.346   1.00 115.85 ? 237  GLU   B HG3  1 
ATOM   12555 N  N    . LYS   B  2  234 ? -1.121  -28.525 6.809    1.00 66.83  ? 238  LYS   B N    1 
ATOM   12556 C  CA   . LYS   B  2  234 ? -1.887  -29.545 6.099    1.00 64.79  ? 238  LYS   B CA   1 
ATOM   12557 C  C    . LYS   B  2  234 ? -1.243  -30.921 6.234    1.00 61.12  ? 238  LYS   B C    1 
ATOM   12558 O  O    . LYS   B  2  234 ? -1.945  -31.923 6.416    1.00 60.39  ? 238  LYS   B O    1 
ATOM   12559 C  CB   . LYS   B  2  234 ? -2.036  -29.153 4.629    1.00 69.06  ? 238  LYS   B CB   1 
ATOM   12560 C  CG   . LYS   B  2  234 ? -3.151  -28.143 4.371    1.00 75.69  ? 238  LYS   B CG   1 
ATOM   12561 C  CD   . LYS   B  2  234 ? -3.005  -27.483 3.006    1.00 80.13  ? 238  LYS   B CD   1 
ATOM   12562 C  CE   . LYS   B  2  234 ? -4.283  -26.775 2.572    1.00 86.67  ? 238  LYS   B CE   1 
ATOM   12563 N  NZ   . LYS   B  2  234 ? -5.321  -27.729 2.089    1.00 90.51  ? 238  LYS   B NZ   1 
ATOM   12564 H  H    . LYS   B  2  234 ? -0.709  -27.967 6.302    1.00 80.18  ? 238  LYS   B H    1 
ATOM   12565 H  HA   . LYS   B  2  234 ? -2.775  -29.598 6.487    1.00 77.73  ? 238  LYS   B HA   1 
ATOM   12566 H  HB2  . LYS   B  2  234 ? -1.204  -28.759 4.326    1.00 82.86  ? 238  LYS   B HB2  1 
ATOM   12567 H  HB3  . LYS   B  2  234 ? -2.234  -29.950 4.113    1.00 82.86  ? 238  LYS   B HB3  1 
ATOM   12568 H  HG2  . LYS   B  2  234 ? -4.008  -28.597 4.399    1.00 90.81  ? 238  LYS   B HG2  1 
ATOM   12569 H  HG3  . LYS   B  2  234 ? -3.119  -27.450 5.049    1.00 90.81  ? 238  LYS   B HG3  1 
ATOM   12570 H  HD2  . LYS   B  2  234 ? -2.293  -26.826 3.045    1.00 96.13  ? 238  LYS   B HD2  1 
ATOM   12571 H  HD3  . LYS   B  2  234 ? -2.796  -28.161 2.345    1.00 96.13  ? 238  LYS   B HD3  1 
ATOM   12572 H  HE2  . LYS   B  2  234 ? -4.649  -26.288 3.327    1.00 103.99 ? 238  LYS   B HE2  1 
ATOM   12573 H  HE3  . LYS   B  2  234 ? -4.077  -26.162 1.850    1.00 103.99 ? 238  LYS   B HE3  1 
ATOM   12574 H  HZ1  . LYS   B  2  234 ? -5.763  -27.375 1.402    1.00 108.59 ? 238  LYS   B HZ1  1 
ATOM   12575 H  HZ2  . LYS   B  2  234 ? -4.938  -28.488 1.825    1.00 108.59 ? 238  LYS   B HZ2  1 
ATOM   12576 H  HZ3  . LYS   B  2  234 ? -5.898  -27.909 2.742    1.00 108.59 ? 238  LYS   B HZ3  1 
ATOM   12577 N  N    . ILE   B  2  235 ? 0.087   -30.996 6.147    1.00 59.87  ? 239  ILE   B N    1 
ATOM   12578 C  CA   . ILE   B  2  235 ? 0.764   -32.273 6.354    1.00 57.08  ? 239  ILE   B CA   1 
ATOM   12579 C  C    . ILE   B  2  235 ? 0.618   -32.718 7.804    1.00 61.54  ? 239  ILE   B C    1 
ATOM   12580 O  O    . ILE   B  2  235 ? 0.392   -33.902 8.084    1.00 61.47  ? 239  ILE   B O    1 
ATOM   12581 C  CB   . ILE   B  2  235 ? 2.245   -32.174 5.942    1.00 56.14  ? 239  ILE   B CB   1 
ATOM   12582 C  CG1  . ILE   B  2  235 ? 2.372   -31.905 4.438    1.00 58.96  ? 239  ILE   B CG1  1 
ATOM   12583 C  CG2  . ILE   B  2  235 ? 2.996   -33.448 6.331    1.00 55.32  ? 239  ILE   B CG2  1 
ATOM   12584 C  CD1  . ILE   B  2  235 ? 1.847   -33.022 3.547    1.00 60.64  ? 239  ILE   B CD1  1 
ATOM   12585 H  H    . ILE   B  2  235 ? 0.609   -30.334 5.974    1.00 71.83  ? 239  ILE   B H    1 
ATOM   12586 H  HA   . ILE   B  2  235 ? 0.342   -32.938 5.788    1.00 68.48  ? 239  ILE   B HA   1 
ATOM   12587 H  HB   . ILE   B  2  235 ? 2.642   -31.428 6.417    1.00 67.35  ? 239  ILE   B HB   1 
ATOM   12588 H  HG12 . ILE   B  2  235 ? 1.873   -31.101 4.225    1.00 70.73  ? 239  ILE   B HG12 1 
ATOM   12589 H  HG13 . ILE   B  2  235 ? 3.310   -31.778 4.226    1.00 70.73  ? 239  ILE   B HG13 1 
ATOM   12590 H  HG21 . ILE   B  2  235 ? 3.875   -33.433 5.922    1.00 66.37  ? 239  ILE   B HG21 1 
ATOM   12591 H  HG22 . ILE   B  2  235 ? 3.080   -33.482 7.297    1.00 66.37  ? 239  ILE   B HG22 1 
ATOM   12592 H  HG23 . ILE   B  2  235 ? 2.497   -34.217 6.015    1.00 66.37  ? 239  ILE   B HG23 1 
ATOM   12593 H  HD11 . ILE   B  2  235 ? 2.013   -32.791 2.620    1.00 72.75  ? 239  ILE   B HD11 1 
ATOM   12594 H  HD12 . ILE   B  2  235 ? 2.306   -33.846 3.770    1.00 72.75  ? 239  ILE   B HD12 1 
ATOM   12595 H  HD13 . ILE   B  2  235 ? 0.894   -33.123 3.697    1.00 72.75  ? 239  ILE   B HD13 1 
ATOM   12596 N  N    . GLY   B  2  236 ? 0.746   -31.787 8.742    1.00 62.80  ? 240  GLY   B N    1 
ATOM   12597 C  CA   . GLY   B  2  236 ? 0.547   -32.077 10.143   1.00 62.50  ? 240  GLY   B CA   1 
ATOM   12598 C  C    . GLY   B  2  236 ? 1.801   -32.203 10.981   1.00 64.22  ? 240  GLY   B C    1 
ATOM   12599 O  O    . GLY   B  2  236 ? 1.725   -32.755 12.084   1.00 65.93  ? 240  GLY   B O    1 
ATOM   12600 H  H    . GLY   B  2  236 ? 0.951   -30.967 8.582    1.00 75.34  ? 240  GLY   B H    1 
ATOM   12601 H  HA2  . GLY   B  2  236 ? 0.011   -31.367 10.529   1.00 74.98  ? 240  GLY   B HA2  1 
ATOM   12602 H  HA3  . GLY   B  2  236 ? 0.063   -32.914 10.216   1.00 74.98  ? 240  GLY   B HA3  1 
ATOM   12603 N  N    . TRP   B  2  237 ? 2.948   -31.725 10.498   1.00 64.52  ? 241  TRP   B N    1 
ATOM   12604 C  CA   . TRP   B  2  237 ? 4.157   -31.754 11.312   1.00 63.52  ? 241  TRP   B CA   1 
ATOM   12605 C  C    . TRP   B  2  237 ? 3.910   -31.021 12.626   1.00 66.47  ? 241  TRP   B C    1 
ATOM   12606 O  O    . TRP   B  2  237 ? 3.407   -29.893 12.636   1.00 71.10  ? 241  TRP   B O    1 
ATOM   12607 C  CB   . TRP   B  2  237 ? 5.333   -31.106 10.576   1.00 60.46  ? 241  TRP   B CB   1 
ATOM   12608 C  CG   . TRP   B  2  237 ? 5.653   -31.675 9.219    1.00 56.44  ? 241  TRP   B CG   1 
ATOM   12609 C  CD1  . TRP   B  2  237 ? 5.499   -31.049 8.016    1.00 55.19  ? 241  TRP   B CD1  1 
ATOM   12610 C  CD2  . TRP   B  2  237 ? 6.198   -32.969 8.929    1.00 55.38  ? 241  TRP   B CD2  1 
ATOM   12611 N  NE1  . TRP   B  2  237 ? 5.908   -31.872 6.996    1.00 51.52  ? 241  TRP   B NE1  1 
ATOM   12612 C  CE2  . TRP   B  2  237 ? 6.340   -33.057 7.529    1.00 53.10  ? 241  TRP   B CE2  1 
ATOM   12613 C  CE3  . TRP   B  2  237 ? 6.576   -34.062 9.715    1.00 60.40  ? 241  TRP   B CE3  1 
ATOM   12614 C  CZ2  . TRP   B  2  237 ? 6.842   -34.195 6.899    1.00 52.79  ? 241  TRP   B CZ2  1 
ATOM   12615 C  CZ3  . TRP   B  2  237 ? 7.073   -35.191 9.087    1.00 57.39  ? 241  TRP   B CZ3  1 
ATOM   12616 C  CH2  . TRP   B  2  237 ? 7.202   -35.248 7.694    1.00 55.00  ? 241  TRP   B CH2  1 
ATOM   12617 H  H    . TRP   B  2  237 ? 3.049   -31.384 9.715    1.00 77.40  ? 241  TRP   B H    1 
ATOM   12618 H  HA   . TRP   B  2  237 ? 4.392   -32.677 11.492   1.00 76.20  ? 241  TRP   B HA   1 
ATOM   12619 H  HB2  . TRP   B  2  237 ? 5.133   -30.165 10.452   1.00 72.53  ? 241  TRP   B HB2  1 
ATOM   12620 H  HB3  . TRP   B  2  237 ? 6.127   -31.207 11.124   1.00 72.53  ? 241  TRP   B HB3  1 
ATOM   12621 H  HD1  . TRP   B  2  237 ? 5.165   -30.188 7.903    1.00 66.20  ? 241  TRP   B HD1  1 
ATOM   12622 H  HE1  . TRP   B  2  237 ? 5.895   -31.675 6.159    1.00 61.81  ? 241  TRP   B HE1  1 
ATOM   12623 H  HE3  . TRP   B  2  237 ? 6.494   -34.031 10.641   1.00 72.47  ? 241  TRP   B HE3  1 
ATOM   12624 H  HZ2  . TRP   B  2  237 ? 6.929   -34.236 5.974    1.00 63.33  ? 241  TRP   B HZ2  1 
ATOM   12625 H  HZ3  . TRP   B  2  237 ? 7.325   -35.925 9.600    1.00 68.85  ? 241  TRP   B HZ3  1 
ATOM   12626 H  HH2  . TRP   B  2  237 ? 7.541   -36.019 7.300    1.00 65.98  ? 241  TRP   B HH2  1 
ATOM   12627 N  N    . ARG   B  2  238 ? 4.266   -31.662 13.735   1.00 63.20  ? 242  ARG   B N    1 
ATOM   12628 C  CA   . ARG   B  2  238 ? 4.134   -31.069 15.058   1.00 67.33  ? 242  ARG   B CA   1 
ATOM   12629 C  C    . ARG   B  2  238 ? 5.494   -30.599 15.560   1.00 66.09  ? 242  ARG   B C    1 
ATOM   12630 O  O    . ARG   B  2  238 ? 6.528   -31.194 15.246   1.00 64.06  ? 242  ARG   B O    1 
ATOM   12631 C  CB   . ARG   B  2  238 ? 3.526   -32.070 16.049   1.00 75.38  ? 242  ARG   B CB   1 
ATOM   12632 C  CG   . ARG   B  2  238 ? 4.264   -33.403 16.142   1.00 84.24  ? 242  ARG   B CG   1 
ATOM   12633 C  CD   . ARG   B  2  238 ? 3.527   -34.412 17.018   1.00 95.84  ? 242  ARG   B CD   1 
ATOM   12634 N  NE   . ARG   B  2  238 ? 4.008   -35.775 16.794   1.00 100.45 ? 242  ARG   B NE   1 
ATOM   12635 C  CZ   . ARG   B  2  238 ? 3.529   -36.855 17.407   1.00 103.61 ? 242  ARG   B CZ   1 
ATOM   12636 N  NH1  . ARG   B  2  238 ? 2.549   -36.748 18.294   1.00 105.31 ? 242  ARG   B NH1  1 
ATOM   12637 N  NH2  . ARG   B  2  238 ? 4.035   -38.049 17.131   1.00 102.20 ? 242  ARG   B NH2  1 
ATOM   12638 H  H    . ARG   B  2  238 ? 4.593   -32.457 13.745   1.00 75.82  ? 242  ARG   B H    1 
ATOM   12639 H  HA   . ARG   B  2  238 ? 3.544   -30.300 15.011   1.00 80.78  ? 242  ARG   B HA   1 
ATOM   12640 H  HB2  . ARG   B  2  238 ? 3.531   -31.670 16.933   1.00 90.44  ? 242  ARG   B HB2  1 
ATOM   12641 H  HB3  . ARG   B  2  238 ? 2.614   -32.259 15.776   1.00 90.44  ? 242  ARG   B HB3  1 
ATOM   12642 H  HG2  . ARG   B  2  238 ? 4.351   -33.782 15.253   1.00 101.06 ? 242  ARG   B HG2  1 
ATOM   12643 H  HG3  . ARG   B  2  238 ? 5.142   -33.254 16.526   1.00 101.06 ? 242  ARG   B HG3  1 
ATOM   12644 H  HD2  . ARG   B  2  238 ? 3.668   -34.189 17.951   1.00 114.99 ? 242  ARG   B HD2  1 
ATOM   12645 H  HD3  . ARG   B  2  238 ? 2.580   -34.386 16.810   1.00 114.99 ? 242  ARG   B HD3  1 
ATOM   12646 H  HE   . ARG   B  2  238 ? 4.645   -35.886 16.227   1.00 120.52 ? 242  ARG   B HE   1 
ATOM   12647 H  HH11 . ARG   B  2  238 ? 2.218   -35.976 18.478   1.00 126.36 ? 242  ARG   B HH11 1 
ATOM   12648 H  HH12 . ARG   B  2  238 ? 2.245   -37.451 18.686   1.00 126.36 ? 242  ARG   B HH12 1 
ATOM   12649 H  HH21 . ARG   B  2  238 ? 4.671   -38.125 16.556   1.00 122.62 ? 242  ARG   B HH21 1 
ATOM   12650 H  HH22 . ARG   B  2  238 ? 3.727   -38.748 17.525   1.00 122.62 ? 242  ARG   B HH22 1 
ATOM   12651 N  N    . ASN   B  2  239 ? 5.486   -29.512 16.338   1.00 70.71  ? 243  ASN   B N    1 
ATOM   12652 C  CA   . ASN   B  2  239 ? 6.709   -29.048 16.983   1.00 77.46  ? 243  ASN   B CA   1 
ATOM   12653 C  C    . ASN   B  2  239 ? 7.342   -30.200 17.756   1.00 74.12  ? 243  ASN   B C    1 
ATOM   12654 O  O    . ASN   B  2  239 ? 6.655   -31.162 18.116   1.00 73.90  ? 243  ASN   B O    1 
ATOM   12655 C  CB   . ASN   B  2  239 ? 6.462   -27.907 17.977   1.00 93.82  ? 243  ASN   B CB   1 
ATOM   12656 C  CG   . ASN   B  2  239 ? 5.905   -26.639 17.346   1.00 106.81 ? 243  ASN   B CG   1 
ATOM   12657 O  OD1  . ASN   B  2  239 ? 5.532   -26.594 16.173   1.00 95.07  ? 243  ASN   B OD1  1 
ATOM   12658 N  ND2  . ASN   B  2  239 ? 5.847   -25.587 18.173   1.00 135.14 ? 243  ASN   B ND2  1 
ATOM   12659 H  H    . ASN   B  2  239 ? 4.791   -29.034 16.504   1.00 84.83  ? 243  ASN   B H    1 
ATOM   12660 H  HA   . ASN   B  2  239 ? 7.295   -28.717 16.285   1.00 92.94  ? 243  ASN   B HA   1 
ATOM   12661 H  HB2  . ASN   B  2  239 ? 5.825   -28.207 18.643   1.00 112.56 ? 243  ASN   B HB2  1 
ATOM   12662 H  HB3  . ASN   B  2  239 ? 7.304   -27.678 18.401   1.00 112.56 ? 243  ASN   B HB3  1 
ATOM   12663 H  HD21 . ASN   B  2  239 ? 6.150   -25.715 18.967   1.00 162.15 ? 243  ASN   B HD21 1 
ATOM   12664 N  N    . ASP   B  2  240 ? 8.640   -30.102 18.029   1.00 72.04  ? 244  ASP   B N    1 
ATOM   12665 C  CA   . ASP   B  2  240 ? 9.305   -30.961 19.008   1.00 73.36  ? 244  ASP   B CA   1 
ATOM   12666 C  C    . ASP   B  2  240 ? 9.053   -32.442 18.726   1.00 64.39  ? 244  ASP   B C    1 
ATOM   12667 O  O    . ASP   B  2  240 ? 8.605   -33.200 19.588   1.00 60.07  ? 244  ASP   B O    1 
ATOM   12668 C  CB   . ASP   B  2  240 ? 8.861   -30.595 20.426   1.00 82.53  ? 244  ASP   B CB   1 
ATOM   12669 C  CG   . ASP   B  2  240 ? 9.278   -29.194 20.822   1.00 95.55  ? 244  ASP   B CG   1 
ATOM   12670 O  OD1  . ASP   B  2  240 ? 10.440  -28.822 20.553   1.00 99.46  ? 244  ASP   B OD1  1 
ATOM   12671 O  OD2  . ASP   B  2  240 ? 8.444   -28.462 21.396   1.00 101.08 ? 244  ASP   B OD2  1 
ATOM   12672 H  H    . ASP   B  2  240 ? 9.168   -29.536 17.655   1.00 86.43  ? 244  ASP   B H    1 
ATOM   12673 H  HA   . ASP   B  2  240 ? 10.262  -30.819 18.933   1.00 88.02  ? 244  ASP   B HA   1 
ATOM   12674 H  HB2  . ASP   B  2  240 ? 7.893   -30.646 20.478   1.00 99.02  ? 244  ASP   B HB2  1 
ATOM   12675 H  HB3  . ASP   B  2  240 ? 9.260   -31.217 21.054   1.00 99.02  ? 244  ASP   B HB3  1 
ATOM   12676 N  N    . SER   B  2  241 ? 9.350   -32.853 17.496   1.00 61.51  ? 245  SER   B N    1 
ATOM   12677 C  CA   . SER   B  2  241 ? 9.294   -34.262 17.134   1.00 65.59  ? 245  SER   B CA   1 
ATOM   12678 C  C    . SER   B  2  241 ? 10.114  -34.466 15.871   1.00 59.35  ? 245  SER   B C    1 
ATOM   12679 O  O    . SER   B  2  241 ? 10.330  -33.533 15.092   1.00 58.59  ? 245  SER   B O    1 
ATOM   12680 C  CB   . SER   B  2  241 ? 7.855   -34.741 16.916   1.00 71.37  ? 245  SER   B CB   1 
ATOM   12681 O  OG   . SER   B  2  241 ? 7.417   -34.454 15.599   1.00 72.33  ? 245  SER   B OG   1 
ATOM   12682 H  H    . SER   B  2  241 ? 9.586   -32.333 16.853   1.00 73.80  ? 245  SER   B H    1 
ATOM   12683 H  HA   . SER   B  2  241 ? 9.683   -34.789 17.850   1.00 78.69  ? 245  SER   B HA   1 
ATOM   12684 H  HB2  . SER   B  2  241 ? 7.817   -35.700 17.058   1.00 85.62  ? 245  SER   B HB2  1 
ATOM   12685 H  HB3  . SER   B  2  241 ? 7.273   -34.289 17.547   1.00 85.62  ? 245  SER   B HB3  1 
ATOM   12686 H  HG   . SER   B  2  241 ? 6.657   -34.786 15.470   1.00 86.77  ? 245  SER   B HG   1 
ATOM   12687 N  N    . LEU   B  2  242 ? 10.573  -35.699 15.679   1.00 57.26  ? 246  LEU   B N    1 
ATOM   12688 C  CA   . LEU   B  2  242 ? 11.265  -36.038 14.444   1.00 56.05  ? 246  LEU   B CA   1 
ATOM   12689 C  C    . LEU   B  2  242 ? 10.311  -35.919 13.261   1.00 56.86  ? 246  LEU   B C    1 
ATOM   12690 O  O    . LEU   B  2  242 ? 9.112   -36.190 13.367   1.00 61.46  ? 246  LEU   B O    1 
ATOM   12691 C  CB   . LEU   B  2  242 ? 11.838  -37.454 14.511   1.00 58.78  ? 246  LEU   B CB   1 
ATOM   12692 C  CG   . LEU   B  2  242 ? 13.333  -37.604 14.808   1.00 64.93  ? 246  LEU   B CG   1 
ATOM   12693 C  CD1  . LEU   B  2  242 ? 13.724  -39.073 14.743   1.00 69.03  ? 246  LEU   B CD1  1 
ATOM   12694 C  CD2  . LEU   B  2  242 ? 14.183  -36.789 13.844   1.00 66.53  ? 246  LEU   B CD2  1 
ATOM   12695 H  H    . LEU   B  2  242 ? 10.496  -36.347 16.239   1.00 68.69  ? 246  LEU   B H    1 
ATOM   12696 H  HA   . LEU   B  2  242 ? 12.006  -35.426 14.313   1.00 67.24  ? 246  LEU   B HA   1 
ATOM   12697 H  HB2  . LEU   B  2  242 ? 11.365  -37.932 15.210   1.00 70.52  ? 246  LEU   B HB2  1 
ATOM   12698 H  HB3  . LEU   B  2  242 ? 11.679  -37.878 13.653   1.00 70.52  ? 246  LEU   B HB3  1 
ATOM   12699 H  HG   . LEU   B  2  242 ? 13.508  -37.265 15.700   1.00 77.89  ? 246  LEU   B HG   1 
ATOM   12700 H  HD11 . LEU   B  2  242 ? 14.680  -39.152 14.889   1.00 82.81  ? 246  LEU   B HD11 1 
ATOM   12701 H  HD12 . LEU   B  2  242 ? 13.243  -39.558 15.431   1.00 82.81  ? 246  LEU   B HD12 1 
ATOM   12702 H  HD13 . LEU   B  2  242 ? 13.494  -39.422 13.868   1.00 82.81  ? 246  LEU   B HD13 1 
ATOM   12703 H  HD21 . LEU   B  2  242 ? 15.113  -37.045 13.948   1.00 79.82  ? 246  LEU   B HD21 1 
ATOM   12704 H  HD22 . LEU   B  2  242 ? 13.891  -36.968 12.936   1.00 79.82  ? 246  LEU   B HD22 1 
ATOM   12705 H  HD23 . LEU   B  2  242 ? 14.075  -35.846 14.046   1.00 79.82  ? 246  LEU   B HD23 1 
ATOM   12706 N  N    . HIS   B  2  243 ? 10.859  -35.505 12.122   1.00 56.44  ? 247  HIS   B N    1 
ATOM   12707 C  CA   . HIS   B  2  243 ? 10.100  -35.308 10.889   1.00 52.65  ? 247  HIS   B CA   1 
ATOM   12708 C  C    . HIS   B  2  243 ? 10.768  -36.142 9.801    1.00 52.41  ? 247  HIS   B C    1 
ATOM   12709 O  O    . HIS   B  2  243 ? 11.712  -35.689 9.149    1.00 53.73  ? 247  HIS   B O    1 
ATOM   12710 C  CB   . HIS   B  2  243 ? 10.046  -33.834 10.512   1.00 53.97  ? 247  HIS   B CB   1 
ATOM   12711 C  CG   . HIS   B  2  243 ? 9.464   -32.959 11.578   1.00 56.79  ? 247  HIS   B CG   1 
ATOM   12712 N  ND1  . HIS   B  2  243 ? 9.905   -31.673 11.806   1.00 59.41  ? 247  HIS   B ND1  1 
ATOM   12713 C  CD2  . HIS   B  2  243 ? 8.474   -33.182 12.474   1.00 60.68  ? 247  HIS   B CD2  1 
ATOM   12714 C  CE1  . HIS   B  2  243 ? 9.214   -31.143 12.800   1.00 61.97  ? 247  HIS   B CE1  1 
ATOM   12715 N  NE2  . HIS   B  2  243 ? 8.339   -32.038 13.222   1.00 61.41  ? 247  HIS   B NE2  1 
ATOM   12716 H  H    . HIS   B  2  243 ? 11.696  -35.326 12.036   1.00 67.70  ? 247  HIS   B H    1 
ATOM   12717 H  HA   . HIS   B  2  243 ? 9.192   -35.627 11.013   1.00 63.16  ? 247  HIS   B HA   1 
ATOM   12718 H  HB2  . HIS   B  2  243 ? 10.949  -33.525 10.336   1.00 64.74  ? 247  HIS   B HB2  1 
ATOM   12719 H  HB3  . HIS   B  2  243 ? 9.500   -33.735 9.717    1.00 64.74  ? 247  HIS   B HB3  1 
ATOM   12720 H  HD1  . HIS   B  2  243 ? 10.533  -31.278 11.371   1.00 71.27  ? 247  HIS   B HD1  1 
ATOM   12721 H  HD2  . HIS   B  2  243 ? 7.979   -33.963 12.566   1.00 72.80  ? 247  HIS   B HD2  1 
ATOM   12722 H  HE1  . HIS   B  2  243 ? 9.325   -30.286 13.143   1.00 74.35  ? 247  HIS   B HE1  1 
ATOM   12723 H  HE2  . HIS   B  2  243 ? 7.776   -31.922 13.862   1.00 73.68  ? 247  HIS   B HE2  1 
ATOM   12724 N  N    . LEU   B  2  244 ? 10.275  -37.361 9.605    1.00 54.09  ? 248  LEU   B N    1 
ATOM   12725 C  CA   . LEU   B  2  244 ? 10.844  -38.292 8.638    1.00 52.37  ? 248  LEU   B CA   1 
ATOM   12726 C  C    . LEU   B  2  244 ? 9.987   -38.273 7.377    1.00 54.48  ? 248  LEU   B C    1 
ATOM   12727 O  O    . LEU   B  2  244 ? 8.824   -38.687 7.399    1.00 57.65  ? 248  LEU   B O    1 
ATOM   12728 C  CB   . LEU   B  2  244 ? 10.928  -39.698 9.227    1.00 52.65  ? 248  LEU   B CB   1 
ATOM   12729 C  CG   . LEU   B  2  244 ? 11.725  -39.820 10.528   1.00 54.06  ? 248  LEU   B CG   1 
ATOM   12730 C  CD1  . LEU   B  2  244 ? 11.728  -41.259 11.020   1.00 54.78  ? 248  LEU   B CD1  1 
ATOM   12731 C  CD2  . LEU   B  2  244 ? 13.151  -39.319 10.345   1.00 53.86  ? 248  LEU   B CD2  1 
ATOM   12732 H  H    . LEU   B  2  244 ? 9.597   -37.677 10.030   1.00 64.89  ? 248  LEU   B H    1 
ATOM   12733 H  HA   . LEU   B  2  244 ? 11.739  -38.003 8.402    1.00 62.83  ? 248  LEU   B HA   1 
ATOM   12734 H  HB2  . LEU   B  2  244 ? 10.027  -40.006 9.410    1.00 63.16  ? 248  LEU   B HB2  1 
ATOM   12735 H  HB3  . LEU   B  2  244 ? 11.350  -40.277 8.573    1.00 63.16  ? 248  LEU   B HB3  1 
ATOM   12736 H  HG   . LEU   B  2  244 ? 11.301  -39.268 11.202   1.00 64.85  ? 248  LEU   B HG   1 
ATOM   12737 H  HD11 . LEU   B  2  244 ? 12.248  -41.312 11.836   1.00 65.72  ? 248  LEU   B HD11 1 
ATOM   12738 H  HD12 . LEU   B  2  244 ? 10.814  -41.535 11.191   1.00 65.72  ? 248  LEU   B HD12 1 
ATOM   12739 H  HD13 . LEU   B  2  244 ? 12.123  -41.825 10.338   1.00 65.72  ? 248  LEU   B HD13 1 
ATOM   12740 H  HD21 . LEU   B  2  244 ? 13.646  -39.468 11.166   1.00 64.62  ? 248  LEU   B HD21 1 
ATOM   12741 H  HD22 . LEU   B  2  244 ? 13.566  -39.806 9.616    1.00 64.62  ? 248  LEU   B HD22 1 
ATOM   12742 H  HD23 . LEU   B  2  244 ? 13.129  -38.372 10.140   1.00 64.62  ? 248  LEU   B HD23 1 
ATOM   12743 N  N    . LEU   B  2  245 ? 10.562  -37.783 6.283    1.00 52.06  ? 249  LEU   B N    1 
ATOM   12744 C  CA   . LEU   B  2  245 ? 9.920   -37.798 4.973    1.00 49.70  ? 249  LEU   B CA   1 
ATOM   12745 C  C    . LEU   B  2  245 ? 10.555  -38.920 4.159    1.00 51.33  ? 249  LEU   B C    1 
ATOM   12746 O  O    . LEU   B  2  245 ? 11.714  -38.813 3.744    1.00 53.60  ? 249  LEU   B O    1 
ATOM   12747 C  CB   . LEU   B  2  245 ? 10.075  -36.449 4.276    1.00 48.76  ? 249  LEU   B CB   1 
ATOM   12748 C  CG   . LEU   B  2  245 ? 9.465   -36.333 2.878    1.00 51.68  ? 249  LEU   B CG   1 
ATOM   12749 C  CD1  . LEU   B  2  245 ? 7.958   -36.529 2.920    1.00 53.14  ? 249  LEU   B CD1  1 
ATOM   12750 C  CD2  . LEU   B  2  245 ? 9.812   -34.986 2.261    1.00 53.33  ? 249  LEU   B CD2  1 
ATOM   12751 H  H    . LEU   B  2  245 ? 11.345  -37.427 6.274    1.00 62.45  ? 249  LEU   B H    1 
ATOM   12752 H  HA   . LEU   B  2  245 ? 8.971   -37.977 5.070    1.00 59.62  ? 249  LEU   B HA   1 
ATOM   12753 H  HB2  . LEU   B  2  245 ? 9.653   -35.774 4.829    1.00 58.49  ? 249  LEU   B HB2  1 
ATOM   12754 H  HB3  . LEU   B  2  245 ? 11.023  -36.262 4.190    1.00 58.49  ? 249  LEU   B HB3  1 
ATOM   12755 H  HG   . LEU   B  2  245 ? 9.836   -37.031 2.317    1.00 62.00  ? 249  LEU   B HG   1 
ATOM   12756 H  HD11 . LEU   B  2  245 ? 7.600   -36.416 2.026    1.00 63.75  ? 249  LEU   B HD11 1 
ATOM   12757 H  HD12 . LEU   B  2  245 ? 7.765   -37.423 3.243    1.00 63.75  ? 249  LEU   B HD12 1 
ATOM   12758 H  HD13 . LEU   B  2  245 ? 7.571   -35.871 3.518    1.00 63.75  ? 249  LEU   B HD13 1 
ATOM   12759 H  HD21 . LEU   B  2  245 ? 9.412   -34.931 1.379    1.00 63.98  ? 249  LEU   B HD21 1 
ATOM   12760 H  HD22 . LEU   B  2  245 ? 9.462   -34.280 2.827    1.00 63.98  ? 249  LEU   B HD22 1 
ATOM   12761 H  HD23 . LEU   B  2  245 ? 10.776  -34.909 2.193    1.00 63.98  ? 249  LEU   B HD23 1 
ATOM   12762 N  N    . VAL   B  2  246 ? 9.802   -39.992 3.936    1.00 52.04  ? 250  VAL   B N    1 
ATOM   12763 C  CA   . VAL   B  2  246 ? 10.309  -41.190 3.276    1.00 51.76  ? 250  VAL   B CA   1 
ATOM   12764 C  C    . VAL   B  2  246 ? 9.909   -41.105 1.807    1.00 51.77  ? 250  VAL   B C    1 
ATOM   12765 O  O    . VAL   B  2  246 ? 8.751   -41.329 1.446    1.00 53.77  ? 250  VAL   B O    1 
ATOM   12766 C  CB   . VAL   B  2  246 ? 9.786   -42.468 3.937    1.00 56.55  ? 250  VAL   B CB   1 
ATOM   12767 C  CG1  . VAL   B  2  246 ? 10.461  -43.690 3.331    1.00 59.06  ? 250  VAL   B CG1  1 
ATOM   12768 C  CG2  . VAL   B  2  246 ? 10.017  -42.422 5.442    1.00 58.52  ? 250  VAL   B CG2  1 
ATOM   12769 H  H    . VAL   B  2  246 ? 8.975   -40.050 4.163    1.00 62.43  ? 250  VAL   B H    1 
ATOM   12770 H  HA   . VAL   B  2  246 ? 11.278  -41.192 3.326    1.00 62.09  ? 250  VAL   B HA   1 
ATOM   12771 H  HB   . VAL   B  2  246 ? 8.832   -42.537 3.780    1.00 67.84  ? 250  VAL   B HB   1 
ATOM   12772 H  HG11 . VAL   B  2  246 ? 10.137  -44.485 3.781    1.00 70.85  ? 250  VAL   B HG11 1 
ATOM   12773 H  HG12 . VAL   B  2  246 ? 10.246  -43.733 2.386    1.00 70.85  ? 250  VAL   B HG12 1 
ATOM   12774 H  HG13 . VAL   B  2  246 ? 11.421  -43.611 3.448    1.00 70.85  ? 250  VAL   B HG13 1 
ATOM   12775 H  HG21 . VAL   B  2  246 ? 9.718   -43.258 5.832    1.00 70.20  ? 250  VAL   B HG21 1 
ATOM   12776 H  HG22 . VAL   B  2  246 ? 10.964  -42.297 5.612    1.00 70.20  ? 250  VAL   B HG22 1 
ATOM   12777 H  HG23 . VAL   B  2  246 ? 9.513   -41.683 5.816    1.00 70.20  ? 250  VAL   B HG23 1 
ATOM   12778 N  N    . PHE   B  2  247 ? 10.881  -40.781 0.959    1.00 51.68  ? 251  PHE   B N    1 
ATOM   12779 C  CA   . PHE   B  2  247 ? 10.687  -40.688 -0.484   1.00 49.26  ? 251  PHE   B CA   1 
ATOM   12780 C  C    . PHE   B  2  247 ? 10.925  -42.064 -1.097   1.00 49.98  ? 251  PHE   B C    1 
ATOM   12781 O  O    . PHE   B  2  247 ? 12.039  -42.595 -1.028   1.00 51.26  ? 251  PHE   B O    1 
ATOM   12782 C  CB   . PHE   B  2  247 ? 11.643  -39.641 -1.058   1.00 50.41  ? 251  PHE   B CB   1 
ATOM   12783 C  CG   . PHE   B  2  247 ? 11.573  -39.485 -2.552   1.00 51.90  ? 251  PHE   B CG   1 
ATOM   12784 C  CD1  . PHE   B  2  247 ? 12.374  -40.255 -3.379   1.00 54.84  ? 251  PHE   B CD1  1 
ATOM   12785 C  CD2  . PHE   B  2  247 ? 10.731  -38.548 -3.128   1.00 53.97  ? 251  PHE   B CD2  1 
ATOM   12786 C  CE1  . PHE   B  2  247 ? 12.323  -40.106 -4.754   1.00 54.55  ? 251  PHE   B CE1  1 
ATOM   12787 C  CE2  . PHE   B  2  247 ? 10.676  -38.393 -4.501   1.00 55.24  ? 251  PHE   B CE2  1 
ATOM   12788 C  CZ   . PHE   B  2  247 ? 11.473  -39.173 -5.315   1.00 54.39  ? 251  PHE   B CZ   1 
ATOM   12789 H  H    . PHE   B  2  247 ? 11.687  -40.605 1.203    1.00 62.00  ? 251  PHE   B H    1 
ATOM   12790 H  HA   . PHE   B  2  247 ? 9.779   -40.422 -0.697   1.00 59.09  ? 251  PHE   B HA   1 
ATOM   12791 H  HB2  . PHE   B  2  247 ? 11.431  -38.780 -0.664   1.00 60.47  ? 251  PHE   B HB2  1 
ATOM   12792 H  HB3  . PHE   B  2  247 ? 12.552  -39.895 -0.832   1.00 60.47  ? 251  PHE   B HB3  1 
ATOM   12793 H  HD1  . PHE   B  2  247 ? 12.953  -40.880 -3.006   1.00 65.79  ? 251  PHE   B HD1  1 
ATOM   12794 H  HD2  . PHE   B  2  247 ? 10.195  -38.017 -2.584   1.00 64.75  ? 251  PHE   B HD2  1 
ATOM   12795 H  HE1  . PHE   B  2  247 ? 12.861  -40.633 -5.299   1.00 65.44  ? 251  PHE   B HE1  1 
ATOM   12796 H  HE2  . PHE   B  2  247 ? 10.103  -37.764 -4.876   1.00 66.27  ? 251  PHE   B HE2  1 
ATOM   12797 H  HZ   . PHE   B  2  247 ? 11.438  -39.071 -6.238   1.00 65.25  ? 251  PHE   B HZ   1 
ATOM   12798 N  N    . VAL   B  2  248 ? 9.880   -42.640 -1.688   1.00 50.44  ? 252  VAL   B N    1 
ATOM   12799 C  CA   . VAL   B  2  248 ? 9.902   -44.011 -2.193   1.00 50.61  ? 252  VAL   B CA   1 
ATOM   12800 C  C    . VAL   B  2  248 ? 9.675   -43.958 -3.698   1.00 51.19  ? 252  VAL   B C    1 
ATOM   12801 O  O    . VAL   B  2  248 ? 8.574   -43.619 -4.155   1.00 53.92  ? 252  VAL   B O    1 
ATOM   12802 C  CB   . VAL   B  2  248 ? 8.847   -44.891 -1.508   1.00 52.29  ? 252  VAL   B CB   1 
ATOM   12803 C  CG1  . VAL   B  2  248 ? 8.915   -46.319 -2.032   1.00 55.05  ? 252  VAL   B CG1  1 
ATOM   12804 C  CG2  . VAL   B  2  248 ? 9.036   -44.865 0.002    1.00 54.11  ? 252  VAL   B CG2  1 
ATOM   12805 H  H    . VAL   B  2  248 ? 9.126   -42.246 -1.811   1.00 60.51  ? 252  VAL   B H    1 
ATOM   12806 H  HA   . VAL   B  2  248 ? 10.779  -44.394 -2.034   1.00 60.71  ? 252  VAL   B HA   1 
ATOM   12807 H  HB   . VAL   B  2  248 ? 7.967   -44.539 -1.712   1.00 62.72  ? 252  VAL   B HB   1 
ATOM   12808 H  HG11 . VAL   B  2  248 ? 8.279   -46.865 -1.543   1.00 66.05  ? 252  VAL   B HG11 1 
ATOM   12809 H  HG12 . VAL   B  2  248 ? 8.695   -46.320 -2.976   1.00 66.05  ? 252  VAL   B HG12 1 
ATOM   12810 H  HG13 . VAL   B  2  248 ? 9.813   -46.661 -1.901   1.00 66.05  ? 252  VAL   B HG13 1 
ATOM   12811 H  HG21 . VAL   B  2  248 ? 8.379   -45.449 0.413    1.00 64.91  ? 252  VAL   B HG21 1 
ATOM   12812 H  HG22 . VAL   B  2  248 ? 9.931   -45.174 0.214    1.00 64.91  ? 252  VAL   B HG22 1 
ATOM   12813 H  HG23 . VAL   B  2  248 ? 8.916   -43.957 0.320    1.00 64.91  ? 252  VAL   B HG23 1 
ATOM   12814 N  N    . SER   B  2  249 ? 10.704  -44.301 -4.468   1.00 49.30  ? 253  SER   B N    1 
ATOM   12815 C  CA   . SER   B  2  249 ? 10.611  -44.265 -5.921   1.00 53.67  ? 253  SER   B CA   1 
ATOM   12816 C  C    . SER   B  2  249 ? 11.649  -45.207 -6.511   1.00 55.28  ? 253  SER   B C    1 
ATOM   12817 O  O    . SER   B  2  249 ? 12.578  -45.645 -5.830   1.00 59.79  ? 253  SER   B O    1 
ATOM   12818 C  CB   . SER   B  2  249 ? 10.814  -42.846 -6.457   1.00 54.43  ? 253  SER   B CB   1 
ATOM   12819 O  OG   . SER   B  2  249 ? 10.783  -42.832 -7.873   1.00 55.16  ? 253  SER   B OG   1 
ATOM   12820 H  H    . SER   B  2  249 ? 11.469  -44.558 -4.170   1.00 59.14  ? 253  SER   B H    1 
ATOM   12821 H  HA   . SER   B  2  249 ? 9.731   -44.579 -6.182   1.00 64.39  ? 253  SER   B HA   1 
ATOM   12822 H  HB2  . SER   B  2  249 ? 10.104  -42.277 -6.120   1.00 65.30  ? 253  SER   B HB2  1 
ATOM   12823 H  HB3  . SER   B  2  249 ? 11.675  -42.515 -6.157   1.00 65.30  ? 253  SER   B HB3  1 
ATOM   12824 H  HG   . SER   B  2  249 ? 10.023  -43.063 -8.146   1.00 66.18  ? 253  SER   B HG   1 
ATOM   12825 N  N    . ASP   B  2  250 ? 11.476  -45.513 -7.800   1.00 50.16  ? 254  ASP   B N    1 
ATOM   12826 C  CA   . ASP   B  2  250 ? 12.411  -46.343 -8.550   1.00 52.39  ? 254  ASP   B CA   1 
ATOM   12827 C  C    . ASP   B  2  250 ? 12.924  -45.620 -9.793   1.00 53.44  ? 254  ASP   B C    1 
ATOM   12828 O  O    . ASP   B  2  250 ? 13.266  -46.255 -10.793  1.00 52.62  ? 254  ASP   B O    1 
ATOM   12829 C  CB   . ASP   B  2  250 ? 11.764  -47.675 -8.934   1.00 53.06  ? 254  ASP   B CB   1 
ATOM   12830 C  CG   . ASP   B  2  250 ? 10.621  -47.512 -9.921   1.00 56.01  ? 254  ASP   B CG   1 
ATOM   12831 O  OD1  . ASP   B  2  250 ? 10.269  -46.361 -10.255  1.00 57.16  ? 254  ASP   B OD1  1 
ATOM   12832 O  OD2  . ASP   B  2  250 ? 10.071  -48.542 -10.364  1.00 58.51  ? 254  ASP   B OD2  1 
ATOM   12833 H  H    . ASP   B  2  250 ? 10.808  -45.243 -8.269   1.00 60.18  ? 254  ASP   B H    1 
ATOM   12834 H  HA   . ASP   B  2  250 ? 13.175  -46.535 -7.983   1.00 62.85  ? 254  ASP   B HA   1 
ATOM   12835 H  HB2  . ASP   B  2  250 ? 12.434  -48.245 -9.343   1.00 63.65  ? 254  ASP   B HB2  1 
ATOM   12836 H  HB3  . ASP   B  2  250 ? 11.412  -48.097 -8.135   1.00 63.65  ? 254  ASP   B HB3  1 
ATOM   12837 N  N    . ALA   B  2  251 ? 12.986  -44.290 -9.745   1.00 54.76  ? 255  ALA   B N    1 
ATOM   12838 C  CA   . ALA   B  2  251 ? 13.401  -43.505 -10.898  1.00 54.97  ? 255  ALA   B CA   1 
ATOM   12839 C  C    . ALA   B  2  251 ? 14.098  -42.240 -10.422  1.00 54.63  ? 255  ALA   B C    1 
ATOM   12840 O  O    . ALA   B  2  251 ? 13.879  -41.771 -9.302   1.00 57.52  ? 255  ALA   B O    1 
ATOM   12841 C  CB   . ALA   B  2  251 ? 12.206  -43.144 -11.790  1.00 55.79  ? 255  ALA   B CB   1 
ATOM   12842 H  H    . ALA   B  2  251 ? 12.790  -43.820 -9.052   1.00 65.69  ? 255  ALA   B H    1 
ATOM   12843 H  HA   . ALA   B  2  251 ? 14.034  -44.021 -11.420  1.00 65.94  ? 255  ALA   B HA   1 
ATOM   12844 H  HB1  . ALA   B  2  251 ? 12.522  -42.624 -12.546  1.00 66.93  ? 255  ALA   B HB1  1 
ATOM   12845 H  HB2  . ALA   B  2  251 ? 11.788  -43.961 -12.103  1.00 66.93  ? 255  ALA   B HB2  1 
ATOM   12846 H  HB3  . ALA   B  2  251 ? 11.571  -42.624 -11.273  1.00 66.93  ? 255  ALA   B HB3  1 
ATOM   12847 N  N    . ASP   B  2  252 ? 14.947  -41.692 -11.288  1.00 56.74  ? 256  ASP   B N    1 
ATOM   12848 C  CA   . ASP   B  2  252 ? 15.549  -40.399 -11.010  1.00 57.24  ? 256  ASP   B CA   1 
ATOM   12849 C  C    . ASP   B  2  252 ? 14.470  -39.316 -11.018  1.00 51.26  ? 256  ASP   B C    1 
ATOM   12850 O  O    . ASP   B  2  252 ? 13.311  -39.557 -11.367  1.00 51.06  ? 256  ASP   B O    1 
ATOM   12851 C  CB   . ASP   B  2  252 ? 16.649  -40.086 -12.024  1.00 65.42  ? 256  ASP   B CB   1 
ATOM   12852 C  CG   . ASP   B  2  252 ? 16.186  -40.231 -13.461  1.00 77.18  ? 256  ASP   B CG   1 
ATOM   12853 O  OD1  . ASP   B  2  252 ? 15.301  -41.073 -13.726  1.00 82.07  ? 256  ASP   B OD1  1 
ATOM   12854 O  OD2  . ASP   B  2  252 ? 16.714  -39.505 -14.329  1.00 81.86  ? 256  ASP   B OD2  1 
ATOM   12855 H  H    . ASP   B  2  252 ? 15.186  -42.047 -12.034  1.00 68.07  ? 256  ASP   B H    1 
ATOM   12856 H  HA   . ASP   B  2  252 ? 15.962  -40.410 -10.132  1.00 68.67  ? 256  ASP   B HA   1 
ATOM   12857 H  HB2  . ASP   B  2  252 ? 16.946  -39.171 -11.896  1.00 78.48  ? 256  ASP   B HB2  1 
ATOM   12858 H  HB3  . ASP   B  2  252 ? 17.390  -40.697 -11.885  1.00 78.48  ? 256  ASP   B HB3  1 
ATOM   12859 N  N    . SER   B  2  253 ? 14.860  -38.108 -10.622  1.00 51.99  ? 257  SER   B N    1 
ATOM   12860 C  CA   . SER   B  2  253 ? 13.920  -37.016 -10.408  1.00 52.26  ? 257  SER   B CA   1 
ATOM   12861 C  C    . SER   B  2  253 ? 14.220  -35.845 -11.332  1.00 54.82  ? 257  SER   B C    1 
ATOM   12862 O  O    . SER   B  2  253 ? 15.384  -35.519 -11.586  1.00 56.97  ? 257  SER   B O    1 
ATOM   12863 C  CB   . SER   B  2  253 ? 13.963  -36.533 -8.952   1.00 50.82  ? 257  SER   B CB   1 
ATOM   12864 O  OG   . SER   B  2  253 ? 13.412  -37.494 -8.069   1.00 51.52  ? 257  SER   B OG   1 
ATOM   12865 H  H    . SER   B  2  253 ? 15.678  -37.894 -10.468  1.00 62.37  ? 257  SER   B H    1 
ATOM   12866 H  HA   . SER   B  2  253 ? 13.028  -37.334 -10.616  1.00 62.69  ? 257  SER   B HA   1 
ATOM   12867 H  HB2  . SER   B  2  253 ? 14.887  -36.373 -8.702   1.00 60.97  ? 257  SER   B HB2  1 
ATOM   12868 H  HB3  . SER   B  2  253 ? 13.453  -35.712 -8.879   1.00 60.97  ? 257  SER   B HB3  1 
ATOM   12869 H  HG   . SER   B  2  253 ? 13.850  -38.210 -8.113   1.00 61.81  ? 257  SER   B HG   1 
ATOM   12870 N  N    . HIS   B  2  254 ? 13.159  -35.218 -11.832  1.00 58.21  ? 258  HIS   B N    1 
ATOM   12871 C  CA   . HIS   B  2  254 ? 13.292  -33.929 -12.494  1.00 56.10  ? 258  HIS   B CA   1 
ATOM   12872 C  C    . HIS   B  2  254 ? 13.699  -32.866 -11.481  1.00 50.42  ? 258  HIS   B C    1 
ATOM   12873 O  O    . HIS   B  2  254 ? 13.385  -32.957 -10.291  1.00 48.03  ? 258  HIS   B O    1 
ATOM   12874 C  CB   . HIS   B  2  254 ? 11.977  -33.525 -13.160  1.00 56.12  ? 258  HIS   B CB   1 
ATOM   12875 C  CG   . HIS   B  2  254 ? 11.756  -34.152 -14.500  1.00 57.09  ? 258  HIS   B CG   1 
ATOM   12876 N  ND1  . HIS   B  2  254 ? 12.656  -34.029 -15.537  1.00 58.52  ? 258  HIS   B ND1  1 
ATOM   12877 C  CD2  . HIS   B  2  254 ? 10.729  -34.892 -14.979  1.00 56.97  ? 258  HIS   B CD2  1 
ATOM   12878 C  CE1  . HIS   B  2  254 ? 12.197  -34.674 -16.594  1.00 59.32  ? 258  HIS   B CE1  1 
ATOM   12879 N  NE2  . HIS   B  2  254 ? 11.029  -35.207 -16.282  1.00 57.67  ? 258  HIS   B NE2  1 
ATOM   12880 H  H    . HIS   B  2  254 ? 12.353  -35.518 -11.801  1.00 69.84  ? 258  HIS   B H    1 
ATOM   12881 H  HA   . HIS   B  2  254 ? 13.971  -33.988 -13.184  1.00 67.30  ? 258  HIS   B HA   1 
ATOM   12882 H  HB2  . HIS   B  2  254 ? 11.243  -33.792 -12.585  1.00 67.33  ? 258  HIS   B HB2  1 
ATOM   12883 H  HB3  . HIS   B  2  254 ? 11.973  -32.563 -13.280  1.00 67.33  ? 258  HIS   B HB3  1 
ATOM   12884 H  HD1  . HIS   B  2  254 ? 13.400  -33.598 -15.501  1.00 70.21  ? 258  HIS   B HD1  1 
ATOM   12885 H  HD2  . HIS   B  2  254 ? 9.964   -35.141 -14.513  1.00 68.34  ? 258  HIS   B HD2  1 
ATOM   12886 H  HE1  . HIS   B  2  254 ? 12.624  -34.742 -17.417  1.00 71.17  ? 258  HIS   B HE1  1 
ATOM   12887 H  HE2  . HIS   B  2  254 ? 10.537  -35.675 -16.810  1.00 69.19  ? 258  HIS   B HE2  1 
ATOM   12888 N  N    . PHE   B  2  255 ? 14.403  -31.845 -11.962  1.00 51.16  ? 259  PHE   B N    1 
ATOM   12889 C  CA   . PHE   B  2  255 ? 14.815  -30.749 -11.100  1.00 51.35  ? 259  PHE   B CA   1 
ATOM   12890 C  C    . PHE   B  2  255 ? 14.865  -29.463 -11.907  1.00 48.06  ? 259  PHE   B C    1 
ATOM   12891 O  O    . PHE   B  2  255 ? 15.036  -29.482 -13.129  1.00 41.65  ? 259  PHE   B O    1 
ATOM   12892 C  CB   . PHE   B  2  255 ? 16.180  -31.020 -10.453  1.00 55.29  ? 259  PHE   B CB   1 
ATOM   12893 C  CG   . PHE   B  2  255 ? 17.297  -31.192 -11.442  1.00 59.73  ? 259  PHE   B CG   1 
ATOM   12894 C  CD1  . PHE   B  2  255 ? 17.514  -32.414 -12.056  1.00 60.98  ? 259  PHE   B CD1  1 
ATOM   12895 C  CD2  . PHE   B  2  255 ? 18.134  -30.134 -11.753  1.00 62.88  ? 259  PHE   B CD2  1 
ATOM   12896 C  CE1  . PHE   B  2  255 ? 18.543  -32.575 -12.965  1.00 62.61  ? 259  PHE   B CE1  1 
ATOM   12897 C  CE2  . PHE   B  2  255 ? 19.165  -30.290 -12.661  1.00 63.87  ? 259  PHE   B CE2  1 
ATOM   12898 C  CZ   . PHE   B  2  255 ? 19.369  -31.510 -13.267  1.00 63.50  ? 259  PHE   B CZ   1 
ATOM   12899 H  H    . PHE   B  2  255 ? 14.652  -31.767 -12.782  1.00 61.37  ? 259  PHE   B H    1 
ATOM   12900 H  HA   . PHE   B  2  255 ? 14.159  -30.637 -10.394  1.00 61.60  ? 259  PHE   B HA   1 
ATOM   12901 H  HB2  . PHE   B  2  255 ? 16.406  -30.272 -9.879   1.00 66.33  ? 259  PHE   B HB2  1 
ATOM   12902 H  HB3  . PHE   B  2  255 ? 16.120  -31.835 -9.930   1.00 66.33  ? 259  PHE   B HB3  1 
ATOM   12903 H  HD1  . PHE   B  2  255 ? 16.961  -33.134 -11.855  1.00 73.16  ? 259  PHE   B HD1  1 
ATOM   12904 H  HD2  . PHE   B  2  255 ? 18.002  -29.309 -11.346  1.00 75.44  ? 259  PHE   B HD2  1 
ATOM   12905 H  HE1  . PHE   B  2  255 ? 18.679  -33.400 -13.373  1.00 75.12  ? 259  PHE   B HE1  1 
ATOM   12906 H  HE2  . PHE   B  2  255 ? 19.721  -29.572 -12.862  1.00 76.62  ? 259  PHE   B HE2  1 
ATOM   12907 H  HZ   . PHE   B  2  255 ? 20.062  -31.617 -13.879  1.00 76.19  ? 259  PHE   B HZ   1 
ATOM   12908 N  N    . GLY   B  2  256 ? 14.699  -28.346 -11.202  1.00 50.19  ? 260  GLY   B N    1 
ATOM   12909 C  CA   . GLY   B  2  256 ? 14.848  -27.027 -11.782  1.00 54.25  ? 260  GLY   B CA   1 
ATOM   12910 C  C    . GLY   B  2  256 ? 14.187  -26.837 -13.130  1.00 51.59  ? 260  GLY   B C    1 
ATOM   12911 O  O    . GLY   B  2  256 ? 12.975  -27.024 -13.276  1.00 48.39  ? 260  GLY   B O    1 
ATOM   12912 H  H    . GLY   B  2  256 ? 14.496  -28.331 -10.367  1.00 60.21  ? 260  GLY   B H    1 
ATOM   12913 H  HA2  . GLY   B  2  256 ? 14.466  -26.376 -11.173  1.00 65.08  ? 260  GLY   B HA2  1 
ATOM   12914 H  HA3  . GLY   B  2  256 ? 15.794  -26.842 -11.890  1.00 65.08  ? 260  GLY   B HA3  1 
ATOM   12915 N  N    . MET   B  2  257 ? 14.989  -26.474 -14.130  1.00 51.70  ? 261  MET   B N    1 
ATOM   12916 C  CA   . MET   B  2  257 ? 14.487  -26.017 -15.416  1.00 52.16  ? 261  MET   B CA   1 
ATOM   12917 C  C    . MET   B  2  257 ? 14.181  -27.157 -16.384  1.00 48.75  ? 261  MET   B C    1 
ATOM   12918 O  O    . MET   B  2  257 ? 14.034  -26.910 -17.587  1.00 48.45  ? 261  MET   B O    1 
ATOM   12919 C  CB   . MET   B  2  257 ? 15.488  -25.045 -16.045  1.00 52.72  ? 261  MET   B CB   1 
ATOM   12920 C  CG   . MET   B  2  257 ? 15.704  -23.781 -15.223  1.00 54.00  ? 261  MET   B CG   1 
ATOM   12921 S  SD   . MET   B  2  257 ? 16.778  -24.026 -13.796  1.00 52.08  ? 261  MET   B SD   1 
ATOM   12922 C  CE   . MET   B  2  257 ? 18.383  -23.833 -14.563  1.00 53.80  ? 261  MET   B CE   1 
ATOM   12923 H  H    . MET   B  2  257 ? 15.847  -26.486 -14.083  1.00 62.03  ? 261  MET   B H    1 
ATOM   12924 H  HA   . MET   B  2  257 ? 13.660  -25.535 -15.259  1.00 62.57  ? 261  MET   B HA   1 
ATOM   12925 H  HB2  . MET   B  2  257 ? 16.345  -25.492 -16.134  1.00 63.24  ? 261  MET   B HB2  1 
ATOM   12926 H  HB3  . MET   B  2  257 ? 15.161  -24.779 -16.919  1.00 63.24  ? 261  MET   B HB3  1 
ATOM   12927 H  HG2  . MET   B  2  257 ? 16.111  -23.105 -15.788  1.00 64.78  ? 261  MET   B HG2  1 
ATOM   12928 H  HG3  . MET   B  2  257 ? 14.845  -23.468 -14.898  1.00 64.78  ? 261  MET   B HG3  1 
ATOM   12929 H  HE1  . MET   B  2  257 ? 19.070  -23.920 -13.884  1.00 64.54  ? 261  MET   B HE1  1 
ATOM   12930 H  HE2  . MET   B  2  257 ? 18.495  -24.522 -15.237  1.00 64.54  ? 261  MET   B HE2  1 
ATOM   12931 H  HE3  . MET   B  2  257 ? 18.433  -22.956 -14.975  1.00 64.54  ? 261  MET   B HE3  1 
ATOM   12932 N  N    . ASP   B  2  258 ? 14.082  -28.396 -15.896  1.00 46.90  ? 262  ASP   B N    1 
ATOM   12933 C  CA   . ASP   B  2  258 ? 13.554  -29.463 -16.740  1.00 52.98  ? 262  ASP   B CA   1 
ATOM   12934 C  C    . ASP   B  2  258 ? 12.180  -29.088 -17.278  1.00 55.45  ? 262  ASP   B C    1 
ATOM   12935 O  O    . ASP   B  2  258 ? 11.846  -29.398 -18.428  1.00 56.41  ? 262  ASP   B O    1 
ATOM   12936 C  CB   . ASP   B  2  258 ? 13.468  -30.772 -15.956  1.00 54.34  ? 262  ASP   B CB   1 
ATOM   12937 C  CG   . ASP   B  2  258 ? 14.818  -31.430 -15.766  1.00 56.21  ? 262  ASP   B CG   1 
ATOM   12938 O  OD1  . ASP   B  2  258 ? 15.808  -30.947 -16.355  1.00 56.41  ? 262  ASP   B OD1  1 
ATOM   12939 O  OD2  . ASP   B  2  258 ? 14.885  -32.433 -15.026  1.00 54.84  ? 262  ASP   B OD2  1 
ATOM   12940 H  H    . ASP   B  2  258 ? 14.309  -28.636 -15.102  1.00 56.26  ? 262  ASP   B H    1 
ATOM   12941 H  HA   . ASP   B  2  258 ? 14.159  -29.599 -17.485  1.00 63.55  ? 262  ASP   B HA   1 
ATOM   12942 H  HB2  . ASP   B  2  258 ? 13.096  -30.592 -15.079  1.00 65.18  ? 262  ASP   B HB2  1 
ATOM   12943 H  HB3  . ASP   B  2  258 ? 12.898  -31.392 -16.437  1.00 65.18  ? 262  ASP   B HB3  1 
ATOM   12944 N  N    . SER   B  2  259 ? 11.372  -28.414 -16.456  1.00 53.65  ? 263  SER   B N    1 
ATOM   12945 C  CA   . SER   B  2  259 ? 10.029  -28.015 -16.853  1.00 52.34  ? 263  SER   B CA   1 
ATOM   12946 C  C    . SER   B  2  259 ? 10.028  -27.063 -18.040  1.00 51.82  ? 263  SER   B C    1 
ATOM   12947 O  O    . SER   B  2  259 ? 8.972   -26.861 -18.649  1.00 53.44  ? 263  SER   B O    1 
ATOM   12948 C  CB   . SER   B  2  259 ? 9.319   -27.360 -15.666  1.00 55.91  ? 263  SER   B CB   1 
ATOM   12949 O  OG   . SER   B  2  259 ? 9.847   -26.071 -15.401  1.00 58.81  ? 263  SER   B OG   1 
ATOM   12950 H  H    . SER   B  2  259 ? 11.584  -28.175 -15.658  1.00 64.36  ? 263  SER   B H    1 
ATOM   12951 H  HA   . SER   B  2  259 ? 9.530   -28.806 -17.108  1.00 62.79  ? 263  SER   B HA   1 
ATOM   12952 H  HB2  . SER   B  2  259 ? 8.374   -27.276 -15.872  1.00 67.07  ? 263  SER   B HB2  1 
ATOM   12953 H  HB3  . SER   B  2  259 ? 9.439   -27.916 -14.881  1.00 67.07  ? 263  SER   B HB3  1 
ATOM   12954 H  HG   . SER   B  2  259 ? 9.681   -25.555 -16.043  1.00 70.56  ? 263  SER   B HG   1 
ATOM   12955 N  N    . LYS   B  2  260 ? 11.178  -26.475 -18.379  1.00 48.87  ? 264  LYS   B N    1 
ATOM   12956 C  CA   . LYS   B  2  260 ? 11.237  -25.561 -19.513  1.00 49.46  ? 264  LYS   B CA   1 
ATOM   12957 C  C    . LYS   B  2  260 ? 10.793  -26.238 -20.803  1.00 49.58  ? 264  LYS   B C    1 
ATOM   12958 O  O    . LYS   B  2  260 ? 10.302  -25.566 -21.717  1.00 46.82  ? 264  LYS   B O    1 
ATOM   12959 C  CB   . LYS   B  2  260 ? 12.656  -25.010 -19.653  1.00 50.66  ? 264  LYS   B CB   1 
ATOM   12960 C  CG   . LYS   B  2  260 ? 12.869  -24.075 -20.831  1.00 51.91  ? 264  LYS   B CG   1 
ATOM   12961 C  CD   . LYS   B  2  260 ? 14.270  -23.484 -20.783  1.00 55.48  ? 264  LYS   B CD   1 
ATOM   12962 C  CE   . LYS   B  2  260 ? 14.753  -23.020 -22.148  1.00 59.77  ? 264  LYS   B CE   1 
ATOM   12963 N  NZ   . LYS   B  2  260 ? 14.263  -21.663 -22.509  1.00 62.93  ? 264  LYS   B NZ   1 
ATOM   12964 H  H    . LYS   B  2  260 ? 11.927  -26.588 -17.972  1.00 58.63  ? 264  LYS   B H    1 
ATOM   12965 H  HA   . LYS   B  2  260 ? 10.639  -24.814 -19.354  1.00 59.33  ? 264  LYS   B HA   1 
ATOM   12966 H  HB2  . LYS   B  2  260 ? 12.875  -24.517 -18.847  1.00 60.77  ? 264  LYS   B HB2  1 
ATOM   12967 H  HB3  . LYS   B  2  260 ? 13.266  -25.757 -19.761  1.00 60.77  ? 264  LYS   B HB3  1 
ATOM   12968 H  HG2  . LYS   B  2  260 ? 12.767  -24.566 -21.661  1.00 62.27  ? 264  LYS   B HG2  1 
ATOM   12969 H  HG3  . LYS   B  2  260 ? 12.225  -23.350 -20.793  1.00 62.27  ? 264  LYS   B HG3  1 
ATOM   12970 H  HD2  . LYS   B  2  260 ? 14.272  -22.719 -20.187  1.00 66.55  ? 264  LYS   B HD2  1 
ATOM   12971 H  HD3  . LYS   B  2  260 ? 14.887  -24.159 -20.459  1.00 66.55  ? 264  LYS   B HD3  1 
ATOM   12972 H  HE2  . LYS   B  2  260 ? 15.723  -22.996 -22.147  1.00 71.70  ? 264  LYS   B HE2  1 
ATOM   12973 H  HE3  . LYS   B  2  260 ? 14.436  -23.641 -22.822  1.00 71.70  ? 264  LYS   B HE3  1 
ATOM   12974 H  HZ1  . LYS   B  2  260 ? 14.918  -21.193 -22.887  1.00 75.49  ? 264  LYS   B HZ1  1 
ATOM   12975 H  HZ2  . LYS   B  2  260 ? 13.585  -21.727 -23.082  1.00 75.49  ? 264  LYS   B HZ2  1 
ATOM   12976 H  HZ3  . LYS   B  2  260 ? 13.985  -21.235 -21.780  1.00 75.49  ? 264  LYS   B HZ3  1 
ATOM   12977 N  N    . LEU   B  2  261 ? 10.952  -27.561 -20.898  1.00 49.89  ? 265  LEU   B N    1 
ATOM   12978 C  CA   . LEU   B  2  261 ? 10.456  -28.275 -22.069  1.00 51.85  ? 265  LEU   B CA   1 
ATOM   12979 C  C    . LEU   B  2  261 ? 8.943   -28.147 -22.195  1.00 51.86  ? 265  LEU   B C    1 
ATOM   12980 O  O    . LEU   B  2  261 ? 8.410   -28.158 -23.310  1.00 51.66  ? 265  LEU   B O    1 
ATOM   12981 C  CB   . LEU   B  2  261 ? 10.855  -29.750 -22.003  1.00 52.91  ? 265  LEU   B CB   1 
ATOM   12982 C  CG   . LEU   B  2  261 ? 12.350  -30.080 -21.952  1.00 57.26  ? 265  LEU   B CG   1 
ATOM   12983 C  CD1  . LEU   B  2  261 ? 12.575  -31.549 -22.288  1.00 59.19  ? 265  LEU   B CD1  1 
ATOM   12984 C  CD2  . LEU   B  2  261 ? 13.153  -29.195 -22.885  1.00 58.94  ? 265  LEU   B CD2  1 
ATOM   12985 H  H    . LEU   B  2  261 ? 11.337  -28.056 -20.309  1.00 59.85  ? 265  LEU   B H    1 
ATOM   12986 H  HA   . LEU   B  2  261 ? 10.863  -27.891 -22.861  1.00 62.20  ? 265  LEU   B HA   1 
ATOM   12987 H  HB2  . LEU   B  2  261 ? 10.457  -30.129 -21.204  1.00 63.47  ? 265  LEU   B HB2  1 
ATOM   12988 H  HB3  . LEU   B  2  261 ? 10.498  -30.188 -22.792  1.00 63.47  ? 265  LEU   B HB3  1 
ATOM   12989 H  HG   . LEU   B  2  261 ? 12.670  -29.912 -21.052  1.00 68.69  ? 265  LEU   B HG   1 
ATOM   12990 H  HD11 . LEU   B  2  261 ? 13.523  -31.745 -22.227  1.00 71.01  ? 265  LEU   B HD11 1 
ATOM   12991 H  HD12 . LEU   B  2  261 ? 12.083  -32.096 -21.656  1.00 71.01  ? 265  LEU   B HD12 1 
ATOM   12992 H  HD13 . LEU   B  2  261 ? 12.259  -31.719 -23.189  1.00 71.01  ? 265  LEU   B HD13 1 
ATOM   12993 H  HD21 . LEU   B  2  261 ? 14.074  -29.501 -22.896  1.00 70.70  ? 265  LEU   B HD21 1 
ATOM   12994 H  HD22 . LEU   B  2  261 ? 12.775  -29.251 -23.777  1.00 70.70  ? 265  LEU   B HD22 1 
ATOM   12995 H  HD23 . LEU   B  2  261 ? 13.112  -28.280 -22.565  1.00 70.70  ? 265  LEU   B HD23 1 
ATOM   12996 N  N    . ALA   B  2  262 ? 8.240   -28.021 -21.071  1.00 49.42  ? 266  ALA   B N    1 
ATOM   12997 C  CA   . ALA   B  2  262 ? 6.791   -27.893 -21.061  1.00 47.57  ? 266  ALA   B CA   1 
ATOM   12998 C  C    . ALA   B  2  262 ? 6.326   -26.441 -21.080  1.00 48.99  ? 266  ALA   B C    1 
ATOM   12999 O  O    . ALA   B  2  262 ? 5.124   -26.188 -20.952  1.00 50.70  ? 266  ALA   B O    1 
ATOM   13000 C  CB   . ALA   B  2  262 ? 6.212   -28.603 -19.835  1.00 43.13  ? 266  ALA   B CB   1 
ATOM   13001 H  H    . ALA   B  2  262 ? 8.591   -28.008 -20.286  1.00 59.29  ? 266  ALA   B H    1 
ATOM   13002 H  HA   . ALA   B  2  262 ? 6.439   -28.326 -21.855  1.00 57.07  ? 266  ALA   B HA   1 
ATOM   13003 H  HB1  . ALA   B  2  262 ? 5.245   -28.525 -19.852  1.00 51.73  ? 266  ALA   B HB1  1 
ATOM   13004 H  HB2  . ALA   B  2  262 ? 6.469   -29.538 -19.861  1.00 51.73  ? 266  ALA   B HB2  1 
ATOM   13005 H  HB3  . ALA   B  2  262 ? 6.564   -28.186 -19.033  1.00 51.73  ? 266  ALA   B HB3  1 
ATOM   13006 N  N    . GLY   B  2  263 ? 7.242   -25.488 -21.239  1.00 48.99  ? 267  GLY   B N    1 
ATOM   13007 C  CA   . GLY   B  2  263 ? 6.871   -24.087 -21.223  1.00 55.05  ? 267  GLY   B CA   1 
ATOM   13008 C  C    . GLY   B  2  263 ? 6.698   -23.498 -19.844  1.00 55.12  ? 267  GLY   B C    1 
ATOM   13009 O  O    . GLY   B  2  263 ? 6.070   -22.444 -19.705  1.00 57.61  ? 267  GLY   B O    1 
ATOM   13010 H  H    . GLY   B  2  263 ? 8.081   -25.631 -21.356  1.00 58.77  ? 267  GLY   B H    1 
ATOM   13011 H  HA2  . GLY   B  2  263 ? 7.559   -23.578 -21.680  1.00 66.04  ? 267  GLY   B HA2  1 
ATOM   13012 H  HA3  . GLY   B  2  263 ? 6.032   -23.981 -21.699  1.00 66.04  ? 267  GLY   B HA3  1 
ATOM   13013 N  N    . ILE   B  2  264 ? 7.237   -24.147 -18.817  1.00 53.72  ? 268  ILE   B N    1 
ATOM   13014 C  CA   . ILE   B  2  264 ? 7.117   -23.700 -17.434  1.00 56.03  ? 268  ILE   B CA   1 
ATOM   13015 C  C    . ILE   B  2  264 ? 8.451   -23.058 -17.067  1.00 59.97  ? 268  ILE   B C    1 
ATOM   13016 O  O    . ILE   B  2  264 ? 9.448   -23.752 -16.848  1.00 58.01  ? 268  ILE   B O    1 
ATOM   13017 C  CB   . ILE   B  2  264 ? 6.758   -24.861 -16.502  1.00 50.85  ? 268  ILE   B CB   1 
ATOM   13018 C  CG1  . ILE   B  2  264 ? 5.429   -25.490 -16.940  1.00 46.51  ? 268  ILE   B CG1  1 
ATOM   13019 C  CG2  . ILE   B  2  264 ? 6.686   -24.392 -15.056  1.00 50.49  ? 268  ILE   B CG2  1 
ATOM   13020 C  CD1  . ILE   B  2  264 ? 5.021   -26.718 -16.141  1.00 46.23  ? 268  ILE   B CD1  1 
ATOM   13021 H  H    . ILE   B  2  264 ? 7.692   -24.872 -18.900  1.00 64.44  ? 268  ILE   B H    1 
ATOM   13022 H  HA   . ILE   B  2  264 ? 6.423   -23.026 -17.363  1.00 67.21  ? 268  ILE   B HA   1 
ATOM   13023 H  HB   . ILE   B  2  264 ? 7.455   -25.532 -16.561  1.00 61.00  ? 268  ILE   B HB   1 
ATOM   13024 H  HG12 . ILE   B  2  264 ? 4.726   -24.829 -16.842  1.00 55.79  ? 268  ILE   B HG12 1 
ATOM   13025 H  HG13 . ILE   B  2  264 ? 5.506   -25.758 -17.869  1.00 55.79  ? 268  ILE   B HG13 1 
ATOM   13026 H  HG21 . ILE   B  2  264 ? 6.477   -25.150 -14.488  1.00 60.57  ? 268  ILE   B HG21 1 
ATOM   13027 H  HG22 . ILE   B  2  264 ? 7.544   -24.016 -14.804  1.00 60.57  ? 268  ILE   B HG22 1 
ATOM   13028 H  HG23 . ILE   B  2  264 ? 5.993   -23.718 -14.977  1.00 60.57  ? 268  ILE   B HG23 1 
ATOM   13029 H  HD11 . ILE   B  2  264 ? 4.220   -27.099 -16.535  1.00 55.46  ? 268  ILE   B HD11 1 
ATOM   13030 H  HD12 . ILE   B  2  264 ? 5.742   -27.366 -16.167  1.00 55.46  ? 268  ILE   B HD12 1 
ATOM   13031 H  HD13 . ILE   B  2  264 ? 4.845   -26.454 -15.224  1.00 55.46  ? 268  ILE   B HD13 1 
ATOM   13032 N  N    . VAL   B  2  265 ? 8.474   -21.725 -17.011  1.00 62.05  ? 269  VAL   B N    1 
ATOM   13033 C  CA   . VAL   B  2  265 ? 9.718   -20.985 -16.827  1.00 58.60  ? 269  VAL   B CA   1 
ATOM   13034 C  C    . VAL   B  2  265 ? 9.607   -19.971 -15.694  1.00 62.12  ? 269  VAL   B C    1 
ATOM   13035 O  O    . VAL   B  2  265 ? 10.277  -18.933 -15.714  1.00 68.87  ? 269  VAL   B O    1 
ATOM   13036 C  CB   . VAL   B  2  265 ? 10.131  -20.286 -18.137  1.00 55.85  ? 269  VAL   B CB   1 
ATOM   13037 C  CG1  . VAL   B  2  265 ? 10.585  -21.313 -19.160  1.00 54.48  ? 269  VAL   B CG1  1 
ATOM   13038 C  CG2  . VAL   B  2  265 ? 8.977   -19.452 -18.683  1.00 57.19  ? 269  VAL   B CG2  1 
ATOM   13039 H  H    . VAL   B  2  265 ? 7.777   -21.226 -17.077  1.00 74.44  ? 269  VAL   B H    1 
ATOM   13040 H  HA   . VAL   B  2  265 ? 10.401  -21.622 -16.565  1.00 70.30  ? 269  VAL   B HA   1 
ATOM   13041 H  HB   . VAL   B  2  265 ? 10.874  -19.689 -17.957  1.00 67.00  ? 269  VAL   B HB   1 
ATOM   13042 H  HG11 . VAL   B  2  265 ? 10.839  -20.855 -19.976  1.00 65.35  ? 269  VAL   B HG11 1 
ATOM   13043 H  HG12 . VAL   B  2  265 ? 11.344  -21.800 -18.804  1.00 65.35  ? 269  VAL   B HG12 1 
ATOM   13044 H  HG13 . VAL   B  2  265 ? 9.854   -21.925 -19.339  1.00 65.35  ? 269  VAL   B HG13 1 
ATOM   13045 H  HG21 . VAL   B  2  265 ? 9.275   -18.983 -19.478  1.00 68.61  ? 269  VAL   B HG21 1 
ATOM   13046 H  HG22 . VAL   B  2  265 ? 8.239   -20.041 -18.903  1.00 68.61  ? 269  VAL   B HG22 1 
ATOM   13047 H  HG23 . VAL   B  2  265 ? 8.701   -18.814 -18.007  1.00 68.61  ? 269  VAL   B HG23 1 
ATOM   13048 N  N    . CYS   B  2  266 ? 8.761   -20.254 -14.704  1.00 60.65  ? 270  CYS   B N    1 
ATOM   13049 C  CA   . CYS   B  2  266 ? 8.681   -19.425 -13.506  1.00 63.45  ? 270  CYS   B CA   1 
ATOM   13050 C  C    . CYS   B  2  266 ? 9.221   -20.220 -12.325  1.00 60.91  ? 270  CYS   B C    1 
ATOM   13051 O  O    . CYS   B  2  266 ? 8.652   -21.269 -11.989  1.00 61.31  ? 270  CYS   B O    1 
ATOM   13052 C  CB   . CYS   B  2  266 ? 7.243   -18.974 -13.246  1.00 66.48  ? 270  CYS   B CB   1 
ATOM   13053 S  SG   . CYS   B  2  266 ? 6.450   -18.225 -14.702  1.00 73.57  ? 270  CYS   B SG   1 
ATOM   13054 H  H    . CYS   B  2  266 ? 8.221   -20.923 -14.705  1.00 72.76  ? 270  CYS   B H    1 
ATOM   13055 H  HA   . CYS   B  2  266 ? 9.221   -18.628 -13.623  1.00 76.12  ? 270  CYS   B HA   1 
ATOM   13056 H  HB2  . CYS   B  2  266 ? 6.715   -19.745 -12.982  1.00 79.76  ? 270  CYS   B HB2  1 
ATOM   13057 H  HB3  . CYS   B  2  266 ? 7.245   -18.315 -12.534  1.00 79.76  ? 270  CYS   B HB3  1 
ATOM   13058 N  N    . PRO   B  2  267 ? 10.303  -19.784 -11.674  1.00 59.10  ? 271  PRO   B N    1 
ATOM   13059 C  CA   . PRO   B  2  267 ? 10.938  -20.632 -10.657  1.00 58.00  ? 271  PRO   B CA   1 
ATOM   13060 C  C    . PRO   B  2  267 ? 9.990   -20.993 -9.523   1.00 56.96  ? 271  PRO   B C    1 
ATOM   13061 O  O    . PRO   B  2  267 ? 9.053   -20.258 -9.204   1.00 60.56  ? 271  PRO   B O    1 
ATOM   13062 C  CB   . PRO   B  2  267 ? 12.104  -19.773 -10.150  1.00 61.72  ? 271  PRO   B CB   1 
ATOM   13063 C  CG   . PRO   B  2  267 ? 12.358  -18.782 -11.229  1.00 62.12  ? 271  PRO   B CG   1 
ATOM   13064 C  CD   . PRO   B  2  267 ? 11.024  -18.510 -11.850  1.00 61.28  ? 271  PRO   B CD   1 
ATOM   13065 H  HA   . PRO   B  2  267 ? 11.270  -21.447 -11.067  1.00 69.58  ? 271  PRO   B HA   1 
ATOM   13066 H  HB2  . PRO   B  2  267 ? 11.852  -19.329 -9.326   1.00 74.05  ? 271  PRO   B HB2  1 
ATOM   13067 H  HB3  . PRO   B  2  267 ? 12.884  -20.330 -10.002  1.00 74.05  ? 271  PRO   B HB3  1 
ATOM   13068 H  HG2  . PRO   B  2  267 ? 12.733  -17.972 -10.849  1.00 74.52  ? 271  PRO   B HG2  1 
ATOM   13069 H  HG3  . PRO   B  2  267 ? 12.971  -19.157 -11.881  1.00 74.52  ? 271  PRO   B HG3  1 
ATOM   13070 H  HD2  . PRO   B  2  267 ? 10.569  -17.788 -11.387  1.00 73.52  ? 271  PRO   B HD2  1 
ATOM   13071 H  HD3  . PRO   B  2  267 ? 11.119  -18.293 -12.790  1.00 73.52  ? 271  PRO   B HD3  1 
ATOM   13072 N  N    . ASN   B  2  268 ? 10.248  -22.150 -8.918   1.00 54.06  ? 272  ASN   B N    1 
ATOM   13073 C  CA   . ASN   B  2  268 ? 9.534   -22.550 -7.715   1.00 55.37  ? 272  ASN   B CA   1 
ATOM   13074 C  C    . ASN   B  2  268 ? 9.679   -21.474 -6.644   1.00 56.49  ? 272  ASN   B C    1 
ATOM   13075 O  O    . ASN   B  2  268 ? 10.707  -20.798 -6.549   1.00 59.46  ? 272  ASN   B O    1 
ATOM   13076 C  CB   . ASN   B  2  268 ? 10.075  -23.887 -7.205   1.00 58.73  ? 272  ASN   B CB   1 
ATOM   13077 C  CG   . ASN   B  2  268 ? 9.164   -24.538 -6.187   1.00 62.24  ? 272  ASN   B CG   1 
ATOM   13078 O  OD1  . ASN   B  2  268 ? 9.216   -24.223 -4.999   1.00 59.51  ? 272  ASN   B OD1  1 
ATOM   13079 N  ND2  . ASN   B  2  268 ? 8.328   -25.461 -6.648   1.00 67.11  ? 272  ASN   B ND2  1 
ATOM   13080 H  H    . ASN   B  2  268 ? 10.833  -22.721 -9.186   1.00 64.86  ? 272  ASN   B H    1 
ATOM   13081 H  HA   . ASN   B  2  268 ? 8.590   -22.663 -7.908   1.00 66.42  ? 272  ASN   B HA   1 
ATOM   13082 H  HB2  . ASN   B  2  268 ? 10.170  -24.496 -7.955   1.00 70.46  ? 272  ASN   B HB2  1 
ATOM   13083 H  HB3  . ASN   B  2  268 ? 10.937  -23.740 -6.786   1.00 70.46  ? 272  ASN   B HB3  1 
ATOM   13084 H  HD21 . ASN   B  2  268 ? 7.789   -25.861 -6.109   1.00 80.52  ? 272  ASN   B HD21 1 
ATOM   13085 H  HD22 . ASN   B  2  268 ? 8.325   -25.660 -7.485   1.00 80.52  ? 272  ASN   B HD22 1 
ATOM   13086 N  N    . ASP   B  2  269 ? 8.634   -21.315 -5.832   1.00 55.43  ? 273  ASP   B N    1 
ATOM   13087 C  CA   . ASP   B  2  269 ? 8.597   -20.269 -4.818   1.00 57.59  ? 273  ASP   B CA   1 
ATOM   13088 C  C    . ASP   B  2  269 ? 8.674   -20.807 -3.396   1.00 54.84  ? 273  ASP   B C    1 
ATOM   13089 O  O    . ASP   B  2  269 ? 8.609   -20.016 -2.449   1.00 58.48  ? 273  ASP   B O    1 
ATOM   13090 C  CB   . ASP   B  2  269 ? 7.327   -19.423 -4.979   1.00 64.13  ? 273  ASP   B CB   1 
ATOM   13091 C  CG   . ASP   B  2  269 ? 6.057   -20.221 -4.746   1.00 70.62  ? 273  ASP   B CG   1 
ATOM   13092 O  OD1  . ASP   B  2  269 ? 6.150   -21.445 -4.517   1.00 72.48  ? 273  ASP   B OD1  1 
ATOM   13093 O  OD2  . ASP   B  2  269 ? 4.961   -19.621 -4.788   1.00 74.04  ? 273  ASP   B OD2  1 
ATOM   13094 H  H    . ASP   B  2  269 ? 7.929   -21.806 -5.852   1.00 66.49  ? 273  ASP   B H    1 
ATOM   13095 H  HA   . ASP   B  2  269 ? 9.363   -19.690 -4.953   1.00 69.08  ? 273  ASP   B HA   1 
ATOM   13096 H  HB2  . ASP   B  2  269 ? 7.347   -18.697 -4.336   1.00 76.93  ? 273  ASP   B HB2  1 
ATOM   13097 H  HB3  . ASP   B  2  269 ? 7.296   -19.067 -5.881   1.00 76.93  ? 273  ASP   B HB3  1 
ATOM   13098 N  N    . GLY   B  2  270 ? 8.810   -22.118 -3.218   1.00 52.79  ? 274  GLY   B N    1 
ATOM   13099 C  CA   . GLY   B  2  270 ? 8.944   -22.674 -1.885   1.00 54.88  ? 274  GLY   B CA   1 
ATOM   13100 C  C    . GLY   B  2  270 ? 7.766   -22.426 -0.973   1.00 54.61  ? 274  GLY   B C    1 
ATOM   13101 O  O    . GLY   B  2  270 ? 7.917   -22.486 0.250    1.00 56.34  ? 274  GLY   B O    1 
ATOM   13102 H  H    . GLY   B  2  270 ? 8.828   -22.700 -3.851   1.00 63.32  ? 274  GLY   B H    1 
ATOM   13103 H  HA2  . GLY   B  2  270 ? 9.064   -23.634 -1.959   1.00 65.83  ? 274  GLY   B HA2  1 
ATOM   13104 H  HA3  . GLY   B  2  270 ? 9.729   -22.289 -1.465   1.00 65.83  ? 274  GLY   B HA3  1 
ATOM   13105 N  N    . LEU   B  2  271 ? 6.592   -22.150 -1.532   1.00 54.90  ? 275  LEU   B N    1 
ATOM   13106 C  CA   . LEU   B  2  271 ? 5.379   -21.917 -0.764   1.00 55.82  ? 275  LEU   B CA   1 
ATOM   13107 C  C    . LEU   B  2  271 ? 4.423   -23.092 -0.918   1.00 57.08  ? 275  LEU   B C    1 
ATOM   13108 O  O    . LEU   B  2  271 ? 4.477   -23.847 -1.893   1.00 56.34  ? 275  LEU   B O    1 
ATOM   13109 C  CB   . LEU   B  2  271 ? 4.689   -20.625 -1.214   1.00 55.90  ? 275  LEU   B CB   1 
ATOM   13110 C  CG   . LEU   B  2  271 ? 5.534   -19.356 -1.111   1.00 55.06  ? 275  LEU   B CG   1 
ATOM   13111 C  CD1  . LEU   B  2  271 ? 4.777   -18.182 -1.701   1.00 55.38  ? 275  LEU   B CD1  1 
ATOM   13112 C  CD2  . LEU   B  2  271 ? 5.914   -19.085 0.335    1.00 53.32  ? 275  LEU   B CD2  1 
ATOM   13113 H  H    . LEU   B  2  271 ? 6.472   -22.091 -2.381   1.00 65.86  ? 275  LEU   B H    1 
ATOM   13114 H  HA   . LEU   B  2  271 ? 5.606   -21.831 0.175    1.00 66.97  ? 275  LEU   B HA   1 
ATOM   13115 H  HB2  . LEU   B  2  271 ? 4.431   -20.726 -2.144   1.00 67.07  ? 275  LEU   B HB2  1 
ATOM   13116 H  HB3  . LEU   B  2  271 ? 3.901   -20.494 -0.664   1.00 67.07  ? 275  LEU   B HB3  1 
ATOM   13117 H  HG   . LEU   B  2  271 ? 6.355   -19.473 -1.613   1.00 66.05  ? 275  LEU   B HG   1 
ATOM   13118 H  HD11 . LEU   B  2  271 ? 5.319   -17.382 -1.615   1.00 66.44  ? 275  LEU   B HD11 1 
ATOM   13119 H  HD12 . LEU   B  2  271 ? 4.597   -18.361 -2.637   1.00 66.44  ? 275  LEU   B HD12 1 
ATOM   13120 H  HD13 . LEU   B  2  271 ? 3.943   -18.070 -1.219   1.00 66.44  ? 275  LEU   B HD13 1 
ATOM   13121 H  HD21 . LEU   B  2  271 ? 6.385   -18.238 0.384    1.00 63.97  ? 275  LEU   B HD21 1 
ATOM   13122 H  HD22 . LEU   B  2  271 ? 5.108   -19.046 0.872    1.00 63.97  ? 275  LEU   B HD22 1 
ATOM   13123 H  HD23 . LEU   B  2  271 ? 6.488   -19.801 0.650    1.00 63.97  ? 275  LEU   B HD23 1 
ATOM   13124 N  N    . CYS   B  2  272 ? 3.536   -23.237 0.062    1.00 59.90  ? 276  CYS   B N    1 
ATOM   13125 C  CA   . CYS   B  2  272 ? 2.545   -24.303 0.016    1.00 62.22  ? 276  CYS   B CA   1 
ATOM   13126 C  C    . CYS   B  2  272 ? 1.457   -23.955 -0.993   1.00 61.46  ? 276  CYS   B C    1 
ATOM   13127 O  O    . CYS   B  2  272 ? 0.915   -22.846 -0.980   1.00 64.70  ? 276  CYS   B O    1 
ATOM   13128 C  CB   . CYS   B  2  272 ? 1.935   -24.527 1.397    1.00 66.81  ? 276  CYS   B CB   1 
ATOM   13129 S  SG   . CYS   B  2  272 ? 0.807   -25.935 1.454    1.00 67.92  ? 276  CYS   B SG   1 
ATOM   13130 H  H    . CYS   B  2  272 ? 3.488   -22.736 0.759    1.00 71.86  ? 276  CYS   B H    1 
ATOM   13131 H  HA   . CYS   B  2  272 ? 2.972   -25.129 -0.260   1.00 74.64  ? 276  CYS   B HA   1 
ATOM   13132 H  HB2  . CYS   B  2  272 ? 2.649   -24.690 2.033    1.00 80.15  ? 276  CYS   B HB2  1 
ATOM   13133 H  HB3  . CYS   B  2  272 ? 1.437   -23.735 1.654    1.00 80.15  ? 276  CYS   B HB3  1 
ATOM   13134 N  N    . HIS   B  2  273 ? 1.147   -24.903 -1.874   1.00 57.51  ? 277  HIS   B N    1 
ATOM   13135 C  CA   . HIS   B  2  273 ? 0.152   -24.711 -2.924   1.00 57.12  ? 277  HIS   B CA   1 
ATOM   13136 C  C    . HIS   B  2  273 ? -0.757  -25.933 -3.024   1.00 56.11  ? 277  HIS   B C    1 
ATOM   13137 O  O    . HIS   B  2  273 ? -0.994  -26.476 -4.104   1.00 57.82  ? 277  HIS   B O    1 
ATOM   13138 C  CB   . HIS   B  2  273 ? 0.823   -24.423 -4.266   1.00 60.06  ? 277  HIS   B CB   1 
ATOM   13139 C  CG   . HIS   B  2  273 ? 1.497   -23.088 -4.329   1.00 62.70  ? 277  HIS   B CG   1 
ATOM   13140 N  ND1  . HIS   B  2  273 ? 0.796   -21.902 -4.357   1.00 64.16  ? 277  HIS   B ND1  1 
ATOM   13141 C  CD2  . HIS   B  2  273 ? 2.808   -22.751 -4.375   1.00 62.47  ? 277  HIS   B CD2  1 
ATOM   13142 C  CE1  . HIS   B  2  273 ? 1.645   -20.892 -4.414   1.00 63.82  ? 277  HIS   B CE1  1 
ATOM   13143 N  NE2  . HIS   B  2  273 ? 2.873   -21.380 -4.426   1.00 63.50  ? 277  HIS   B NE2  1 
ATOM   13144 H  H    . HIS   B  2  273 ? 1.509   -25.684 -1.884   1.00 69.00  ? 277  HIS   B H    1 
ATOM   13145 H  HA   . HIS   B  2  273 ? -0.400  -23.951 -2.682   1.00 68.52  ? 277  HIS   B HA   1 
ATOM   13146 H  HB2  . HIS   B  2  273 ? 1.496   -25.102 -4.431   1.00 72.05  ? 277  HIS   B HB2  1 
ATOM   13147 H  HB3  . HIS   B  2  273 ? 0.150   -24.447 -4.964   1.00 72.05  ? 277  HIS   B HB3  1 
ATOM   13148 H  HD2  . HIS   B  2  273 ? 3.529   -23.338 -4.373   1.00 74.94  ? 277  HIS   B HD2  1 
ATOM   13149 H  HE1  . HIS   B  2  273 ? 1.418   -19.991 -4.441   1.00 76.57  ? 277  HIS   B HE1  1 
ATOM   13150 H  HE2  . HIS   B  2  273 ? 3.595   -20.915 -4.461   1.00 76.18  ? 277  HIS   B HE2  1 
ATOM   13151 N  N    . LEU   B  2  274 ? -1.269  -26.390 -1.884   1.00 56.85  ? 278  LEU   B N    1 
ATOM   13152 C  CA   . LEU   B  2  274 ? -2.227  -27.489 -1.851   1.00 60.97  ? 278  LEU   B CA   1 
ATOM   13153 C  C    . LEU   B  2  274 ? -3.638  -26.917 -1.935   1.00 65.07  ? 278  LEU   B C    1 
ATOM   13154 O  O    . LEU   B  2  274 ? -4.034  -26.101 -1.094   1.00 67.79  ? 278  LEU   B O    1 
ATOM   13155 C  CB   . LEU   B  2  274 ? -2.050  -28.325 -0.585   1.00 61.74  ? 278  LEU   B CB   1 
ATOM   13156 C  CG   . LEU   B  2  274 ? -0.724  -29.082 -0.471   1.00 59.99  ? 278  LEU   B CG   1 
ATOM   13157 C  CD1  . LEU   B  2  274 ? -0.670  -29.864 0.830    1.00 60.03  ? 278  LEU   B CD1  1 
ATOM   13158 C  CD2  . LEU   B  2  274 ? -0.516  -30.011 -1.658   1.00 60.98  ? 278  LEU   B CD2  1 
ATOM   13159 H  H    . LEU   B  2  274 ? -1.074  -26.076 -1.108   1.00 68.20  ? 278  LEU   B H    1 
ATOM   13160 H  HA   . LEU   B  2  274 ? -2.084  -28.070 -2.614   1.00 73.14  ? 278  LEU   B HA   1 
ATOM   13161 H  HB2  . LEU   B  2  274 ? -2.112  -27.733 0.181    1.00 74.06  ? 278  LEU   B HB2  1 
ATOM   13162 H  HB3  . LEU   B  2  274 ? -2.762  -28.983 -0.553   1.00 74.06  ? 278  LEU   B HB3  1 
ATOM   13163 H  HG   . LEU   B  2  274 ? 0.000   -28.437 -0.473   1.00 71.96  ? 278  LEU   B HG   1 
ATOM   13164 H  HD11 . LEU   B  2  274 ? 0.177   -30.334 0.881    1.00 72.01  ? 278  LEU   B HD11 1 
ATOM   13165 H  HD12 . LEU   B  2  274 ? -0.751  -29.246 1.573    1.00 72.01  ? 278  LEU   B HD12 1 
ATOM   13166 H  HD13 . LEU   B  2  274 ? -1.403  -30.499 0.847    1.00 72.01  ? 278  LEU   B HD13 1 
ATOM   13167 H  HD21 . LEU   B  2  274 ? 0.286   -30.536 -1.511   1.00 73.16  ? 278  LEU   B HD21 1 
ATOM   13168 H  HD22 . LEU   B  2  274 ? -1.285  -30.597 -1.738   1.00 73.16  ? 278  LEU   B HD22 1 
ATOM   13169 H  HD23 . LEU   B  2  274 ? -0.421  -29.479 -2.463   1.00 73.16  ? 278  LEU   B HD23 1 
ATOM   13170 N  N    . ASP   B  2  275 ? -4.391  -27.343 -2.946   1.00 68.32  ? 279  ASP   B N    1 
ATOM   13171 C  CA   . ASP   B  2  275 ? -5.713  -26.798 -3.211   1.00 73.64  ? 279  ASP   B CA   1 
ATOM   13172 C  C    . ASP   B  2  275 ? -6.764  -27.557 -2.399   1.00 74.58  ? 279  ASP   B C    1 
ATOM   13173 O  O    . ASP   B  2  275 ? -6.445  -28.331 -1.493   1.00 70.82  ? 279  ASP   B O    1 
ATOM   13174 C  CB   . ASP   B  2  275 ? -6.005  -26.835 -4.711   1.00 75.64  ? 279  ASP   B CB   1 
ATOM   13175 C  CG   . ASP   B  2  275 ? -5.999  -28.246 -5.280   1.00 75.51  ? 279  ASP   B CG   1 
ATOM   13176 O  OD1  . ASP   B  2  275 ? -5.980  -29.216 -4.494   1.00 76.03  ? 279  ASP   B OD1  1 
ATOM   13177 O  OD2  . ASP   B  2  275 ? -6.009  -28.383 -6.521   1.00 74.76  ? 279  ASP   B OD2  1 
ATOM   13178 H  H    . ASP   B  2  275 ? -4.153  -27.957 -3.498   1.00 81.96  ? 279  ASP   B H    1 
ATOM   13179 H  HA   . ASP   B  2  275 ? -5.722  -25.873 -2.920   1.00 88.35  ? 279  ASP   B HA   1 
ATOM   13180 H  HB2  . ASP   B  2  275 ? -6.881  -26.452 -4.872   1.00 90.75  ? 279  ASP   B HB2  1 
ATOM   13181 H  HB3  . ASP   B  2  275 ? -5.327  -26.322 -5.178   1.00 90.75  ? 279  ASP   B HB3  1 
ATOM   13182 N  N    . SER   B  2  276 ? -8.041  -27.337 -2.725   1.00 82.99  ? 280  SER   B N    1 
ATOM   13183 C  CA   . SER   B  2  276 ? -9.123  -27.927 -1.941   1.00 89.28  ? 280  SER   B CA   1 
ATOM   13184 C  C    . SER   B  2  276 ? -9.068  -29.449 -1.969   1.00 95.28  ? 280  SER   B C    1 
ATOM   13185 O  O    . SER   B  2  276 ? -9.385  -30.107 -0.970   1.00 100.98 ? 280  SER   B O    1 
ATOM   13186 C  CB   . SER   B  2  276 ? -10.472 -27.426 -2.458   1.00 89.29  ? 280  SER   B CB   1 
ATOM   13187 O  OG   . SER   B  2  276 ? -10.542 -27.507 -3.871   1.00 88.28  ? 280  SER   B OG   1 
ATOM   13188 H  H    . SER   B  2  276 ? -8.303  -26.854 -3.387   1.00 99.57  ? 280  SER   B H    1 
ATOM   13189 H  HA   . SER   B  2  276 ? -9.028  -27.645 -1.018   1.00 107.11 ? 280  SER   B HA   1 
ATOM   13190 H  HB2  . SER   B  2  276 ? -11.177 -27.973 -2.077   1.00 107.13 ? 280  SER   B HB2  1 
ATOM   13191 H  HB3  . SER   B  2  276 ? -10.587 -26.501 -2.190   1.00 107.13 ? 280  SER   B HB3  1 
ATOM   13192 H  HG   . SER   B  2  276 ? -11.283 -27.214 -4.138   1.00 105.92 ? 280  SER   B HG   1 
ATOM   13193 N  N    . LYS   B  2  277 ? -8.672  -30.029 -3.098   1.00 92.83  ? 281  LYS   B N    1 
ATOM   13194 C  CA   . LYS   B  2  277 ? -8.505  -31.472 -3.204   1.00 89.25  ? 281  LYS   B CA   1 
ATOM   13195 C  C    . LYS   B  2  277 ? -7.189  -31.957 -2.602   1.00 80.96  ? 281  LYS   B C    1 
ATOM   13196 O  O    . LYS   B  2  277 ? -6.843  -33.132 -2.768   1.00 76.35  ? 281  LYS   B O    1 
ATOM   13197 C  CB   . LYS   B  2  277 ? -8.598  -31.898 -4.673   1.00 93.58  ? 281  LYS   B CB   1 
ATOM   13198 C  CG   . LYS   B  2  277 ? -9.982  -31.707 -5.279   1.00 102.05 ? 281  LYS   B CG   1 
ATOM   13199 C  CD   . LYS   B  2  277 ? -9.948  -31.697 -6.802   1.00 107.58 ? 281  LYS   B CD   1 
ATOM   13200 C  CE   . LYS   B  2  277 ? -9.442  -33.012 -7.372   1.00 111.39 ? 281  LYS   B CE   1 
ATOM   13201 N  NZ   . LYS   B  2  277 ? -9.469  -33.015 -8.862   1.00 113.92 ? 281  LYS   B NZ   1 
ATOM   13202 H  H    . LYS   B  2  277 ? -8.492  -29.602 -3.822   1.00 111.38 ? 281  LYS   B H    1 
ATOM   13203 H  HA   . LYS   B  2  277 ? -9.226  -31.908 -2.723   1.00 107.08 ? 281  LYS   B HA   1 
ATOM   13204 H  HB2  . LYS   B  2  277 ? -7.971  -31.369 -5.191   1.00 112.28 ? 281  LYS   B HB2  1 
ATOM   13205 H  HB3  . LYS   B  2  277 ? -8.372  -32.839 -4.740   1.00 112.28 ? 281  LYS   B HB3  1 
ATOM   13206 H  HG2  . LYS   B  2  277 ? -10.557 -32.434 -4.995   1.00 122.44 ? 281  LYS   B HG2  1 
ATOM   13207 H  HG3  . LYS   B  2  277 ? -10.346 -30.859 -4.980   1.00 122.44 ? 281  LYS   B HG3  1 
ATOM   13208 H  HD2  . LYS   B  2  277 ? -10.845 -31.546 -7.141   1.00 129.08 ? 281  LYS   B HD2  1 
ATOM   13209 H  HD3  . LYS   B  2  277 ? -9.357  -30.990 -7.104   1.00 129.08 ? 281  LYS   B HD3  1 
ATOM   13210 H  HE2  . LYS   B  2  277 ? -8.526  -33.155 -7.085   1.00 133.64 ? 281  LYS   B HE2  1 
ATOM   13211 H  HE3  . LYS   B  2  277 ? -10.005 -33.736 -7.057   1.00 133.64 ? 281  LYS   B HE3  1 
ATOM   13212 H  HZ1  . LYS   B  2  277 ? -9.153  -33.788 -9.171   1.00 136.69 ? 281  LYS   B HZ1  1 
ATOM   13213 H  HZ2  . LYS   B  2  277 ? -10.304 -32.908 -9.152   1.00 136.69 ? 281  LYS   B HZ2  1 
ATOM   13214 H  HZ3  . LYS   B  2  277 ? -8.967  -32.351 -9.177   1.00 136.69 ? 281  LYS   B HZ3  1 
ATOM   13215 N  N    . ASN   B  2  278 ? -6.461  -31.085 -1.902   1.00 78.82  ? 282  ASN   B N    1 
ATOM   13216 C  CA   . ASN   B  2  278 ? -5.138  -31.409 -1.367   1.00 74.35  ? 282  ASN   B CA   1 
ATOM   13217 C  C    . ASN   B  2  278 ? -4.197  -31.868 -2.480   1.00 68.04  ? 282  ASN   B C    1 
ATOM   13218 O  O    . ASN   B  2  278 ? -3.413  -32.805 -2.313   1.00 66.33  ? 282  ASN   B O    1 
ATOM   13219 C  CB   . ASN   B  2  278 ? -5.224  -32.459 -0.256   1.00 79.13  ? 282  ASN   B CB   1 
ATOM   13220 C  CG   . ASN   B  2  278 ? -5.362  -31.839 1.126    1.00 85.39  ? 282  ASN   B CG   1 
ATOM   13221 O  OD1  . ASN   B  2  278 ? -5.071  -30.659 1.325    1.00 85.47  ? 282  ASN   B OD1  1 
ATOM   13222 N  ND2  . ASN   B  2  278 ? -5.793  -32.641 2.093    1.00 90.40  ? 282  ASN   B ND2  1 
ATOM   13223 H  H    . ASN   B  2  278 ? -6.717  -30.285 -1.720   1.00 94.57  ? 282  ASN   B H    1 
ATOM   13224 H  HA   . ASN   B  2  278 ? -4.761  -30.604 -0.979   1.00 89.20  ? 282  ASN   B HA   1 
ATOM   13225 H  HB2  . ASN   B  2  278 ? -5.999  -33.021 -0.411   1.00 94.93  ? 282  ASN   B HB2  1 
ATOM   13226 H  HB3  . ASN   B  2  278 ? -4.417  -32.996 -0.265   1.00 94.93  ? 282  ASN   B HB3  1 
ATOM   13227 H  HD21 . ASN   B  2  278 ? -5.888  -32.338 2.892    1.00 108.46 ? 282  ASN   B HD21 1 
ATOM   13228 H  HD22 . ASN   B  2  278 ? -5.978  -33.463 1.919    1.00 108.46 ? 282  ASN   B HD22 1 
ATOM   13229 N  N    . GLU   B  2  279 ? -4.276  -31.200 -3.627   1.00 67.66  ? 283  GLU   B N    1 
ATOM   13230 C  CA   . GLU   B  2  279 ? -3.379  -31.442 -4.746   1.00 68.71  ? 283  GLU   B CA   1 
ATOM   13231 C  C    . GLU   B  2  279 ? -2.528  -30.204 -4.994   1.00 64.43  ? 283  GLU   B C    1 
ATOM   13232 O  O    . GLU   B  2  279 ? -3.002  -29.073 -4.849   1.00 66.69  ? 283  GLU   B O    1 
ATOM   13233 C  CB   . GLU   B  2  279 ? -4.154  -31.799 -6.018   1.00 77.77  ? 283  GLU   B CB   1 
ATOM   13234 C  CG   . GLU   B  2  279 ? -4.893  -33.124 -5.948   1.00 88.45  ? 283  GLU   B CG   1 
ATOM   13235 C  CD   . GLU   B  2  279 ? -5.439  -33.560 -7.293   1.00 95.97  ? 283  GLU   B CD   1 
ATOM   13236 O  OE1  . GLU   B  2  279 ? -5.045  -32.967 -8.320   1.00 96.60  ? 283  GLU   B OE1  1 
ATOM   13237 O  OE2  . GLU   B  2  279 ? -6.264  -34.497 -7.323   1.00 98.89  ? 283  GLU   B OE2  1 
ATOM   13238 H  H    . GLU   B  2  279 ? -4.858  -30.586 -3.782   1.00 81.17  ? 283  GLU   B H    1 
ATOM   13239 H  HA   . GLU   B  2  279 ? -2.794  -32.186 -4.534   1.00 82.43  ? 283  GLU   B HA   1 
ATOM   13240 H  HB2  . GLU   B  2  279 ? -4.811  -31.105 -6.186   1.00 93.30  ? 283  GLU   B HB2  1 
ATOM   13241 H  HB3  . GLU   B  2  279 ? -3.529  -31.850 -6.757   1.00 93.30  ? 283  GLU   B HB3  1 
ATOM   13242 H  HG2  . GLU   B  2  279 ? -4.283  -33.811 -5.635   1.00 106.12 ? 283  GLU   B HG2  1 
ATOM   13243 H  HG3  . GLU   B  2  279 ? -5.639  -33.039 -5.334   1.00 106.12 ? 283  GLU   B HG3  1 
ATOM   13244 N  N    . TYR   B  2  280 ? -1.269  -30.429 -5.367   1.00 58.97  ? 284  TYR   B N    1 
ATOM   13245 C  CA   . TYR   B  2  280 ? -0.350  -29.345 -5.693   1.00 58.68  ? 284  TYR   B CA   1 
ATOM   13246 C  C    . TYR   B  2  280 ? -0.850  -28.597 -6.923   1.00 60.14  ? 284  TYR   B C    1 
ATOM   13247 O  O    . TYR   B  2  280 ? -0.800  -29.120 -8.041   1.00 60.87  ? 284  TYR   B O    1 
ATOM   13248 C  CB   . TYR   B  2  280 ? 1.057   -29.908 -5.911   1.00 56.61  ? 284  TYR   B CB   1 
ATOM   13249 C  CG   . TYR   B  2  280 ? 2.102   -28.886 -6.295   1.00 56.38  ? 284  TYR   B CG   1 
ATOM   13250 C  CD1  . TYR   B  2  280 ? 2.200   -27.671 -5.628   1.00 58.55  ? 284  TYR   B CD1  1 
ATOM   13251 C  CD2  . TYR   B  2  280 ? 3.007   -29.149 -7.313   1.00 54.85  ? 284  TYR   B CD2  1 
ATOM   13252 C  CE1  . TYR   B  2  280 ? 3.162   -26.741 -5.978   1.00 60.30  ? 284  TYR   B CE1  1 
ATOM   13253 C  CE2  . TYR   B  2  280 ? 3.970   -28.230 -7.668   1.00 54.27  ? 284  TYR   B CE2  1 
ATOM   13254 C  CZ   . TYR   B  2  280 ? 4.044   -27.027 -6.998   1.00 59.32  ? 284  TYR   B CZ   1 
ATOM   13255 O  OH   . TYR   B  2  280 ? 5.004   -26.108 -7.352   1.00 60.59  ? 284  TYR   B OH   1 
ATOM   13256 H  H    . TYR   B  2  280 ? -0.920  -31.211 -5.439   1.00 70.74  ? 284  TYR   B H    1 
ATOM   13257 H  HA   . TYR   B  2  280 ? -0.300  -28.710 -4.961   1.00 70.40  ? 284  TYR   B HA   1 
ATOM   13258 H  HB2  . TYR   B  2  280 ? 1.350   -30.329 -5.088   1.00 67.91  ? 284  TYR   B HB2  1 
ATOM   13259 H  HB3  . TYR   B  2  280 ? 1.017   -30.565 -6.624   1.00 67.91  ? 284  TYR   B HB3  1 
ATOM   13260 H  HD1  . TYR   B  2  280 ? 1.610   -27.481 -4.935   1.00 70.25  ? 284  TYR   B HD1  1 
ATOM   13261 H  HD2  . TYR   B  2  280 ? 2.963   -29.961 -7.765   1.00 65.80  ? 284  TYR   B HD2  1 
ATOM   13262 H  HE1  . TYR   B  2  280 ? 3.213   -25.929 -5.528   1.00 72.34  ? 284  TYR   B HE1  1 
ATOM   13263 H  HE2  . TYR   B  2  280 ? 4.567   -28.419 -8.356   1.00 65.10  ? 284  TYR   B HE2  1 
ATOM   13264 H  HH   . TYR   B  2  280 ? 5.467   -26.405 -7.987   1.00 72.69  ? 284  TYR   B HH   1 
ATOM   13265 N  N    . SER   B  2  281 ? -1.338  -27.371 -6.723   1.00 62.13  ? 285  SER   B N    1 
ATOM   13266 C  CA   . SER   B  2  281 ? -2.007  -26.651 -7.801   1.00 63.43  ? 285  SER   B CA   1 
ATOM   13267 C  C    . SER   B  2  281 ? -1.028  -26.025 -8.785   1.00 60.59  ? 285  SER   B C    1 
ATOM   13268 O  O    . SER   B  2  281 ? -1.374  -25.839 -9.957   1.00 64.34  ? 285  SER   B O    1 
ATOM   13269 C  CB   . SER   B  2  281 ? -2.918  -25.568 -7.218   1.00 66.88  ? 285  SER   B CB   1 
ATOM   13270 O  OG   . SER   B  2  281 ? -2.189  -24.675 -6.396   1.00 67.75  ? 285  SER   B OG   1 
ATOM   13271 H  H    . SER   B  2  281 ? -1.293  -26.939 -5.981   1.00 74.54  ? 285  SER   B H    1 
ATOM   13272 H  HA   . SER   B  2  281 ? -2.556  -27.282 -8.292   1.00 76.10  ? 285  SER   B HA   1 
ATOM   13273 H  HB2  . SER   B  2  281 ? -3.319  -25.069 -7.947   1.00 80.23  ? 285  SER   B HB2  1 
ATOM   13274 H  HB3  . SER   B  2  281 ? -3.610  -25.992 -6.687   1.00 80.23  ? 285  SER   B HB3  1 
ATOM   13275 H  HG   . SER   B  2  281 ? -2.699  -24.076 -6.099   1.00 81.27  ? 285  SER   B HG   1 
ATOM   13276 N  N    . MET   B  2  282 ? 0.185   -25.695 -8.343   1.00 59.28  ? 286  MET   B N    1 
ATOM   13277 C  CA   . MET   B  2  282 ? 1.181   -25.071 -9.202   1.00 60.91  ? 286  MET   B CA   1 
ATOM   13278 C  C    . MET   B  2  282 ? 2.013   -26.090 -9.973   1.00 56.70  ? 286  MET   B C    1 
ATOM   13279 O  O    . MET   B  2  282 ? 3.078   -25.739 -10.494  1.00 58.96  ? 286  MET   B O    1 
ATOM   13280 C  CB   . MET   B  2  282 ? 2.101   -24.171 -8.375   1.00 62.44  ? 286  MET   B CB   1 
ATOM   13281 C  CG   . MET   B  2  282 ? 1.369   -23.099 -7.586   1.00 65.09  ? 286  MET   B CG   1 
ATOM   13282 S  SD   . MET   B  2  282 ? 0.460   -21.937 -8.623   1.00 68.79  ? 286  MET   B SD   1 
ATOM   13283 C  CE   . MET   B  2  282 ? 1.751   -20.772 -9.053   1.00 69.99  ? 286  MET   B CE   1 
ATOM   13284 H  H    . MET   B  2  282 ? 0.455   -25.827 -7.537   1.00 71.12  ? 286  MET   B H    1 
ATOM   13285 H  HA   . MET   B  2  282 ? 0.713   -24.511 -9.841   1.00 73.07  ? 286  MET   B HA   1 
ATOM   13286 H  HB2  . MET   B  2  282 ? 2.589   -24.721 -7.742   1.00 74.91  ? 286  MET   B HB2  1 
ATOM   13287 H  HB3  . MET   B  2  282 ? 2.721   -23.725 -8.973   1.00 74.91  ? 286  MET   B HB3  1 
ATOM   13288 H  HG2  . MET   B  2  282 ? 0.733   -23.527 -6.991   1.00 78.08  ? 286  MET   B HG2  1 
ATOM   13289 H  HG3  . MET   B  2  282 ? 2.016   -22.593 -7.070   1.00 78.08  ? 286  MET   B HG3  1 
ATOM   13290 H  HE1  . MET   B  2  282 ? 1.362   -20.043 -9.562   1.00 83.97  ? 286  MET   B HE1  1 
ATOM   13291 H  HE2  . MET   B  2  282 ? 2.151   -20.429 -8.239   1.00 83.97  ? 286  MET   B HE2  1 
ATOM   13292 H  HE3  . MET   B  2  282 ? 2.422   -21.226 -9.586   1.00 83.97  ? 286  MET   B HE3  1 
ATOM   13293 N  N    . SER   B  2  283 ? 1.553   -27.341 -10.059  1.00 53.63  ? 287  SER   B N    1 
ATOM   13294 C  CA   . SER   B  2  283 ? 2.318   -28.362 -10.767  1.00 54.07  ? 287  SER   B CA   1 
ATOM   13295 C  C    . SER   B  2  283 ? 2.595   -27.947 -12.207  1.00 48.49  ? 287  SER   B C    1 
ATOM   13296 O  O    . SER   B  2  283 ? 3.691   -28.183 -12.729  1.00 46.59  ? 287  SER   B O    1 
ATOM   13297 C  CB   . SER   B  2  283 ? 1.570   -29.695 -10.732  1.00 58.62  ? 287  SER   B CB   1 
ATOM   13298 O  OG   . SER   B  2  283 ? 2.298   -30.701 -11.413  1.00 62.82  ? 287  SER   B OG   1 
ATOM   13299 H  H    . SER   B  2  283 ? 0.812   -27.617 -9.721   1.00 64.34  ? 287  SER   B H    1 
ATOM   13300 H  HA   . SER   B  2  283 ? 3.170   -28.479 -10.318  1.00 64.86  ? 287  SER   B HA   1 
ATOM   13301 H  HB2  . SER   B  2  283 ? 1.449   -29.964 -9.808   1.00 70.32  ? 287  SER   B HB2  1 
ATOM   13302 H  HB3  . SER   B  2  283 ? 0.708   -29.584 -11.162  1.00 70.32  ? 287  SER   B HB3  1 
ATOM   13303 H  HG   . SER   B  2  283 ? 1.842   -31.405 -11.457  1.00 75.37  ? 287  SER   B HG   1 
ATOM   13304 N  N    . THR   B  2  284 ? 1.617   -27.325 -12.862  1.00 51.64  ? 288  THR   B N    1 
ATOM   13305 C  CA   . THR   B  2  284 ? 1.735   -26.917 -14.254  1.00 51.40  ? 288  THR   B CA   1 
ATOM   13306 C  C    . THR   B  2  284 ? 2.143   -25.457 -14.409  1.00 49.58  ? 288  THR   B C    1 
ATOM   13307 O  O    . THR   B  2  284 ? 2.134   -24.939 -15.530  1.00 49.35  ? 288  THR   B O    1 
ATOM   13308 C  CB   . THR   B  2  284 ? 0.410   -27.154 -14.985  1.00 53.61  ? 288  THR   B CB   1 
ATOM   13309 O  OG1  . THR   B  2  284 ? -0.601  -26.291 -14.445  1.00 57.68  ? 288  THR   B OG1  1 
ATOM   13310 C  CG2  . THR   B  2  284 ? -0.034  -28.601 -14.833  1.00 53.66  ? 288  THR   B CG2  1 
ATOM   13311 H  H    . THR   B  2  284 ? 0.858   -27.124 -12.510  1.00 61.95  ? 288  THR   B H    1 
ATOM   13312 H  HA   . THR   B  2  284 ? 2.417   -27.465 -14.673  1.00 61.66  ? 288  THR   B HA   1 
ATOM   13313 H  HB   . THR   B  2  284 ? 0.525   -26.966 -15.930  1.00 64.32  ? 288  THR   B HB   1 
ATOM   13314 H  HG1  . THR   B  2  284 ? -1.316  -26.383 -14.875  1.00 69.20  ? 288  THR   B HG1  1 
ATOM   13315 H  HG21 . THR   B  2  284 ? -0.828  -28.763 -15.366  1.00 64.37  ? 288  THR   B HG21 1 
ATOM   13316 H  HG22 . THR   B  2  284 ? 0.671   -29.197 -15.129  1.00 64.37  ? 288  THR   B HG22 1 
ATOM   13317 H  HG23 . THR   B  2  284 ? -0.236  -28.790 -13.903  1.00 64.37  ? 288  THR   B HG23 1 
ATOM   13318 N  N    . VAL   B  2  285 ? 2.507   -24.785 -13.313  1.00 52.07  ? 289  VAL   B N    1 
ATOM   13319 C  CA   . VAL   B  2  285 ? 2.781   -23.355 -13.322  1.00 55.27  ? 289  VAL   B CA   1 
ATOM   13320 C  C    . VAL   B  2  285 ? 4.232   -23.047 -12.978  1.00 55.93  ? 289  VAL   B C    1 
ATOM   13321 O  O    . VAL   B  2  285 ? 4.841   -22.160 -13.586  1.00 59.71  ? 289  VAL   B O    1 
ATOM   13322 C  CB   . VAL   B  2  285 ? 1.832   -22.607 -12.359  1.00 58.00  ? 289  VAL   B CB   1 
ATOM   13323 C  CG1  . VAL   B  2  285 ? 2.042   -21.104 -12.462  1.00 59.40  ? 289  VAL   B CG1  1 
ATOM   13324 C  CG2  . VAL   B  2  285 ? 0.384   -22.969 -12.651  1.00 60.94  ? 289  VAL   B CG2  1 
ATOM   13325 H  H    . VAL   B  2  285 ? 2.603   -25.147 -12.539  1.00 62.46  ? 289  VAL   B H    1 
ATOM   13326 H  HA   . VAL   B  2  285 ? 2.625   -23.021 -14.219  1.00 66.31  ? 289  VAL   B HA   1 
ATOM   13327 H  HB   . VAL   B  2  285 ? 2.032   -22.877 -11.449  1.00 69.58  ? 289  VAL   B HB   1 
ATOM   13328 H  HG11 . VAL   B  2  285 ? 1.383   -20.654 -11.911  1.00 71.26  ? 289  VAL   B HG11 1 
ATOM   13329 H  HG12 . VAL   B  2  285 ? 2.936   -20.888 -12.151  1.00 71.26  ? 289  VAL   B HG12 1 
ATOM   13330 H  HG13 . VAL   B  2  285 ? 1.940   -20.833 -13.387  1.00 71.26  ? 289  VAL   B HG13 1 
ATOM   13331 H  HG21 . VAL   B  2  285 ? -0.195  -22.445 -12.076  1.00 73.11  ? 289  VAL   B HG21 1 
ATOM   13332 H  HG22 . VAL   B  2  285 ? 0.191   -22.773 -13.581  1.00 73.11  ? 289  VAL   B HG22 1 
ATOM   13333 H  HG23 . VAL   B  2  285 ? 0.254   -23.915 -12.478  1.00 73.11  ? 289  VAL   B HG23 1 
ATOM   13334 N  N    . LEU   B  2  286 ? 4.806   -23.758 -12.010  1.00 51.59  ? 290  LEU   B N    1 
ATOM   13335 C  CA   . LEU   B  2  286 ? 6.132   -23.454 -11.495  1.00 51.77  ? 290  LEU   B CA   1 
ATOM   13336 C  C    . LEU   B  2  286 ? 7.122   -24.552 -11.863  1.00 55.69  ? 290  LEU   B C    1 
ATOM   13337 O  O    . LEU   B  2  286 ? 6.762   -25.727 -11.980  1.00 57.00  ? 290  LEU   B O    1 
ATOM   13338 C  CB   . LEU   B  2  286 ? 6.098   -23.281 -9.972   1.00 52.28  ? 290  LEU   B CB   1 
ATOM   13339 C  CG   . LEU   B  2  286 ? 5.203   -22.148 -9.462   1.00 52.65  ? 290  LEU   B CG   1 
ATOM   13340 C  CD1  . LEU   B  2  286 ? 5.175   -22.112 -7.944   1.00 55.15  ? 290  LEU   B CD1  1 
ATOM   13341 C  CD2  . LEU   B  2  286 ? 5.666   -20.808 -10.018  1.00 50.06  ? 290  LEU   B CD2  1 
ATOM   13342 H  H    . LEU   B  2  286 ? 4.436   -24.434 -11.630  1.00 61.88  ? 290  LEU   B H    1 
ATOM   13343 H  HA   . LEU   B  2  286 ? 6.445   -22.628 -11.895  1.00 62.11  ? 290  LEU   B HA   1 
ATOM   13344 H  HB2  . LEU   B  2  286 ? 5.774   -24.106 -9.578   1.00 62.72  ? 290  LEU   B HB2  1 
ATOM   13345 H  HB3  . LEU   B  2  286 ? 7.000   -23.098 -9.665   1.00 62.72  ? 290  LEU   B HB3  1 
ATOM   13346 H  HG   . LEU   B  2  286 ? 4.298   -22.309 -9.771   1.00 63.16  ? 290  LEU   B HG   1 
ATOM   13347 H  HD11 . LEU   B  2  286 ? 4.594   -21.391 -7.655   1.00 66.17  ? 290  LEU   B HD11 1 
ATOM   13348 H  HD12 . LEU   B  2  286 ? 4.839   -22.960 -7.614   1.00 66.17  ? 290  LEU   B HD12 1 
ATOM   13349 H  HD13 . LEU   B  2  286 ? 6.076   -21.963 -7.614   1.00 66.17  ? 290  LEU   B HD13 1 
ATOM   13350 H  HD21 . LEU   B  2  286 ? 5.150   -20.099 -9.603   1.00 60.06  ? 290  LEU   B HD21 1 
ATOM   13351 H  HD22 . LEU   B  2  286 ? 6.608   -20.692 -9.818   1.00 60.06  ? 290  LEU   B HD22 1 
ATOM   13352 H  HD23 . LEU   B  2  286 ? 5.529   -20.800 -10.978  1.00 60.06  ? 290  LEU   B HD23 1 
ATOM   13353 N  N    . GLU   B  2  287 ? 8.376   -24.150 -12.049  1.00 54.86  ? 291  GLU   B N    1 
ATOM   13354 C  CA   . GLU   B  2  287 ? 9.436   -25.102 -12.335  1.00 53.86  ? 291  GLU   B CA   1 
ATOM   13355 C  C    . GLU   B  2  287 ? 9.561   -26.113 -11.200  1.00 52.70  ? 291  GLU   B C    1 
ATOM   13356 O  O    . GLU   B  2  287 ? 9.084   -25.898 -10.082  1.00 52.04  ? 291  GLU   B O    1 
ATOM   13357 C  CB   . GLU   B  2  287 ? 10.772  -24.382 -12.519  1.00 55.42  ? 291  GLU   B CB   1 
ATOM   13358 C  CG   . GLU   B  2  287 ? 10.802  -23.370 -13.649  1.00 60.51  ? 291  GLU   B CG   1 
ATOM   13359 C  CD   . GLU   B  2  287 ? 12.108  -22.602 -13.702  1.00 63.86  ? 291  GLU   B CD   1 
ATOM   13360 O  OE1  . GLU   B  2  287 ? 12.831  -22.582 -12.683  1.00 63.91  ? 291  GLU   B OE1  1 
ATOM   13361 O  OE2  . GLU   B  2  287 ? 12.413  -22.020 -14.763  1.00 65.41  ? 291  GLU   B OE2  1 
ATOM   13362 H  H    . GLU   B  2  287 ? 8.637   -23.331 -12.014  1.00 65.81  ? 291  GLU   B H    1 
ATOM   13363 H  HA   . GLU   B  2  287 ? 9.225   -25.575 -13.155  1.00 64.61  ? 291  GLU   B HA   1 
ATOM   13364 H  HB2  . GLU   B  2  287 ? 10.982  -23.909 -11.699  1.00 66.49  ? 291  GLU   B HB2  1 
ATOM   13365 H  HB3  . GLU   B  2  287 ? 11.455  -25.045 -12.704  1.00 66.49  ? 291  GLU   B HB3  1 
ATOM   13366 H  HG2  . GLU   B  2  287 ? 10.691  -23.834 -14.494  1.00 72.59  ? 291  GLU   B HG2  1 
ATOM   13367 H  HG3  . GLU   B  2  287 ? 10.082  -22.732 -13.524  1.00 72.59  ? 291  GLU   B HG3  1 
ATOM   13368 N  N    . TYR   B  2  288 ? 10.215  -27.233 -11.498  1.00 50.35  ? 292  TYR   B N    1 
ATOM   13369 C  CA   . TYR   B  2  288 ? 10.618  -28.137 -10.436  1.00 50.66  ? 292  TYR   B CA   1 
ATOM   13370 C  C    . TYR   B  2  288 ? 11.554  -27.392 -9.485   1.00 51.29  ? 292  TYR   B C    1 
ATOM   13371 O  O    . TYR   B  2  288 ? 12.310  -26.515 -9.913   1.00 53.93  ? 292  TYR   B O    1 
ATOM   13372 C  CB   . TYR   B  2  288 ? 11.333  -29.365 -10.995  1.00 49.65  ? 292  TYR   B CB   1 
ATOM   13373 C  CG   . TYR   B  2  288 ? 10.529  -30.184 -11.977  1.00 52.33  ? 292  TYR   B CG   1 
ATOM   13374 C  CD1  . TYR   B  2  288 ? 9.653   -31.169 -11.540  1.00 50.63  ? 292  TYR   B CD1  1 
ATOM   13375 C  CD2  . TYR   B  2  288 ? 10.662  -29.986 -13.344  1.00 56.34  ? 292  TYR   B CD2  1 
ATOM   13376 C  CE1  . TYR   B  2  288 ? 8.922   -31.926 -12.437  1.00 52.57  ? 292  TYR   B CE1  1 
ATOM   13377 C  CE2  . TYR   B  2  288 ? 9.936   -30.736 -14.249  1.00 56.79  ? 292  TYR   B CE2  1 
ATOM   13378 C  CZ   . TYR   B  2  288 ? 9.067   -31.704 -13.791  1.00 55.66  ? 292  TYR   B CZ   1 
ATOM   13379 O  OH   . TYR   B  2  288 ? 8.343   -32.454 -14.690  1.00 57.44  ? 292  TYR   B OH   1 
ATOM   13380 H  H    . TYR   B  2  288 ? 10.430  -27.485 -12.292  1.00 60.40  ? 292  TYR   B H    1 
ATOM   13381 H  HA   . TYR   B  2  288 ? 9.834   -28.446 -9.955   1.00 60.78  ? 292  TYR   B HA   1 
ATOM   13382 H  HB2  . TYR   B  2  288 ? 12.136  -29.071 -11.452  1.00 59.56  ? 292  TYR   B HB2  1 
ATOM   13383 H  HB3  . TYR   B  2  288 ? 11.567  -29.947 -10.255  1.00 59.56  ? 292  TYR   B HB3  1 
ATOM   13384 H  HD1  . TYR   B  2  288 ? 9.556   -31.322 -10.627  1.00 60.73  ? 292  TYR   B HD1  1 
ATOM   13385 H  HD2  . TYR   B  2  288 ? 11.251  -29.337 -13.656  1.00 67.58  ? 292  TYR   B HD2  1 
ATOM   13386 H  HE1  . TYR   B  2  288 ? 8.337   -32.580 -12.130  1.00 63.07  ? 292  TYR   B HE1  1 
ATOM   13387 H  HE2  . TYR   B  2  288 ? 10.033  -30.589 -15.162  1.00 68.13  ? 292  TYR   B HE2  1 
ATOM   13388 H  HH   . TYR   B  2  288 ? 7.975   -33.098 -14.296  1.00 68.90  ? 292  TYR   B HH   1 
ATOM   13389 N  N    . PRO   B  2  289 ? 11.528  -27.710 -8.194   1.00 53.56  ? 293  PRO   B N    1 
ATOM   13390 C  CA   . PRO   B  2  289 ? 12.501  -27.099 -7.285   1.00 54.70  ? 293  PRO   B CA   1 
ATOM   13391 C  C    . PRO   B  2  289 ? 13.912  -27.557 -7.606   1.00 53.83  ? 293  PRO   B C    1 
ATOM   13392 O  O    . PRO   B  2  289 ? 14.135  -28.657 -8.119   1.00 52.96  ? 293  PRO   B O    1 
ATOM   13393 C  CB   . PRO   B  2  289 ? 12.058  -27.583 -5.899   1.00 54.39  ? 293  PRO   B CB   1 
ATOM   13394 C  CG   . PRO   B  2  289 ? 11.244  -28.797 -6.152   1.00 56.96  ? 293  PRO   B CG   1 
ATOM   13395 C  CD   . PRO   B  2  289 ? 10.587  -28.592 -7.482   1.00 55.85  ? 293  PRO   B CD   1 
ATOM   13396 H  HA   . PRO   B  2  289 ? 12.450  -26.130 -7.318   1.00 65.62  ? 293  PRO   B HA   1 
ATOM   13397 H  HB2  . PRO   B  2  289 ? 12.836  -27.794 -5.359   1.00 65.25  ? 293  PRO   B HB2  1 
ATOM   13398 H  HB3  . PRO   B  2  289 ? 11.529  -26.896 -5.463   1.00 65.25  ? 293  PRO   B HB3  1 
ATOM   13399 H  HG2  . PRO   B  2  289 ? 11.821  -29.577 -6.172   1.00 68.33  ? 293  PRO   B HG2  1 
ATOM   13400 H  HG3  . PRO   B  2  289 ? 10.579  -28.895 -5.453   1.00 68.33  ? 293  PRO   B HG3  1 
ATOM   13401 H  HD2  . PRO   B  2  289 ? 10.483  -29.435 -7.950   1.00 67.00  ? 293  PRO   B HD2  1 
ATOM   13402 H  HD3  . PRO   B  2  289 ? 9.723   -28.162 -7.377   1.00 67.00  ? 293  PRO   B HD3  1 
ATOM   13403 N  N    . THR   B  2  290 ? 14.870  -26.688 -7.312   1.00 55.31  ? 294  THR   B N    1 
ATOM   13404 C  CA   . THR   B  2  290 ? 16.275  -27.038 -7.419   1.00 55.24  ? 294  THR   B CA   1 
ATOM   13405 C  C    . THR   B  2  290 ? 16.737  -27.674 -6.110   1.00 54.25  ? 294  THR   B C    1 
ATOM   13406 O  O    . THR   B  2  290 ? 16.048  -27.624 -5.089   1.00 52.43  ? 294  THR   B O    1 
ATOM   13407 C  CB   . THR   B  2  290 ? 17.122  -25.806 -7.743   1.00 58.58  ? 294  THR   B CB   1 
ATOM   13408 O  OG1  . THR   B  2  290 ? 17.293  -25.015 -6.560   1.00 58.02  ? 294  THR   B OG1  1 
ATOM   13409 C  CG2  . THR   B  2  290 ? 16.460  -24.959 -8.827   1.00 58.53  ? 294  THR   B CG2  1 
ATOM   13410 H  H    . THR   B  2  290 ? 14.728  -25.882 -7.046   1.00 66.36  ? 294  THR   B H    1 
ATOM   13411 H  HA   . THR   B  2  290 ? 16.397  -27.672 -8.143   1.00 66.27  ? 294  THR   B HA   1 
ATOM   13412 H  HB   . THR   B  2  290 ? 17.990  -26.092 -8.070   1.00 70.27  ? 294  THR   B HB   1 
ATOM   13413 H  HG1  . THR   B  2  290 ? 17.957  -24.508 -6.647   1.00 69.61  ? 294  THR   B HG1  1 
ATOM   13414 H  HG21 . THR   B  2  290 ? 17.029  -24.207 -9.054   1.00 70.21  ? 294  THR   B HG21 1 
ATOM   13415 H  HG22 . THR   B  2  290 ? 16.312  -25.494 -9.622   1.00 70.21  ? 294  THR   B HG22 1 
ATOM   13416 H  HG23 . THR   B  2  290 ? 15.606  -24.624 -8.510   1.00 70.21  ? 294  THR   B HG23 1 
ATOM   13417 N  N    . ILE   B  2  291 ? 17.923  -28.283 -6.145   1.00 55.45  ? 295  ILE   B N    1 
ATOM   13418 C  CA   . ILE   B  2  291 ? 18.476  -28.872 -4.927   1.00 55.52  ? 295  ILE   B CA   1 
ATOM   13419 C  C    . ILE   B  2  291 ? 18.666  -27.794 -3.866   1.00 55.34  ? 295  ILE   B C    1 
ATOM   13420 O  O    . ILE   B  2  291 ? 18.312  -27.980 -2.696   1.00 55.86  ? 295  ILE   B O    1 
ATOM   13421 C  CB   . ILE   B  2  291 ? 19.792  -29.609 -5.233   1.00 59.67  ? 295  ILE   B CB   1 
ATOM   13422 C  CG1  . ILE   B  2  291 ? 19.510  -31.044 -5.685   1.00 68.59  ? 295  ILE   B CG1  1 
ATOM   13423 C  CG2  . ILE   B  2  291 ? 20.695  -29.639 -4.007   1.00 58.52  ? 295  ILE   B CG2  1 
ATOM   13424 C  CD1  . ILE   B  2  291 ? 18.645  -31.152 -6.920   1.00 77.08  ? 295  ILE   B CD1  1 
ATOM   13425 H  H    . ILE   B  2  291 ? 18.416  -28.367 -6.844   1.00 66.53  ? 295  ILE   B H    1 
ATOM   13426 H  HA   . ILE   B  2  291 ? 17.847  -29.525 -4.583   1.00 66.61  ? 295  ILE   B HA   1 
ATOM   13427 H  HB   . ILE   B  2  291 ? 20.239  -29.126 -5.947   1.00 71.58  ? 295  ILE   B HB   1 
ATOM   13428 H  HG12 . ILE   B  2  291 ? 20.355  -31.479 -5.880   1.00 82.29  ? 295  ILE   B HG12 1 
ATOM   13429 H  HG13 . ILE   B  2  291 ? 19.055  -31.511 -4.966   1.00 82.29  ? 295  ILE   B HG13 1 
ATOM   13430 H  HG21 . ILE   B  2  291 ? 21.411  -30.276 -4.158   1.00 70.20  ? 295  ILE   B HG21 1 
ATOM   13431 H  HG22 . ILE   B  2  291 ? 21.065  -28.753 -3.865   1.00 70.20  ? 295  ILE   B HG22 1 
ATOM   13432 H  HG23 . ILE   B  2  291 ? 20.172  -29.907 -3.236   1.00 70.20  ? 295  ILE   B HG23 1 
ATOM   13433 H  HD11 . ILE   B  2  291 ? 18.570  -32.086 -7.172   1.00 92.48  ? 295  ILE   B HD11 1 
ATOM   13434 H  HD12 . ILE   B  2  291 ? 17.766  -30.792 -6.722   1.00 92.48  ? 295  ILE   B HD12 1 
ATOM   13435 H  HD13 . ILE   B  2  291 ? 19.055  -30.647 -7.638   1.00 92.48  ? 295  ILE   B HD13 1 
ATOM   13436 N  N    . GLY   B  2  292 ? 19.220  -26.647 -4.262   1.00 55.27  ? 296  GLY   B N    1 
ATOM   13437 C  CA   . GLY   B  2  292 ? 19.405  -25.561 -3.314   1.00 58.43  ? 296  GLY   B CA   1 
ATOM   13438 C  C    . GLY   B  2  292 ? 18.103  -25.117 -2.674   1.00 57.81  ? 296  GLY   B C    1 
ATOM   13439 O  O    . GLY   B  2  292 ? 18.061  -24.807 -1.481   1.00 58.49  ? 296  GLY   B O    1 
ATOM   13440 H  H    . GLY   B  2  292 ? 19.492  -26.478 -5.061   1.00 66.30  ? 296  GLY   B H    1 
ATOM   13441 H  HA2  . GLY   B  2  292 ? 20.007  -25.849 -2.610   1.00 70.09  ? 296  GLY   B HA2  1 
ATOM   13442 H  HA3  . GLY   B  2  292 ? 19.794  -24.799 -3.771   1.00 70.09  ? 296  GLY   B HA3  1 
ATOM   13443 N  N    . GLN   B  2  293 ? 17.022  -25.082 -3.457   1.00 57.17  ? 297  GLN   B N    1 
ATOM   13444 C  CA   . GLN   B  2  293 ? 15.725  -24.713 -2.900   1.00 55.98  ? 297  GLN   B CA   1 
ATOM   13445 C  C    . GLN   B  2  293 ? 15.225  -25.768 -1.921   1.00 51.99  ? 297  GLN   B C    1 
ATOM   13446 O  O    . GLN   B  2  293 ? 14.718  -25.433 -0.844   1.00 49.78  ? 297  GLN   B O    1 
ATOM   13447 C  CB   . GLN   B  2  293 ? 14.712  -24.504 -4.023   1.00 57.77  ? 297  GLN   B CB   1 
ATOM   13448 C  CG   . GLN   B  2  293 ? 14.981  -23.281 -4.883   1.00 61.70  ? 297  GLN   B CG   1 
ATOM   13449 C  CD   . GLN   B  2  293 ? 14.009  -23.162 -6.040   1.00 64.58  ? 297  GLN   B CD   1 
ATOM   13450 O  OE1  . GLN   B  2  293 ? 13.728  -24.141 -6.732   1.00 66.44  ? 297  GLN   B OE1  1 
ATOM   13451 N  NE2  . GLN   B  2  293 ? 13.485  -21.961 -6.253   1.00 65.34  ? 297  GLN   B NE2  1 
ATOM   13452 H  H    . GLN   B  2  293 ? 17.015  -25.264 -4.297   1.00 68.59  ? 297  GLN   B H    1 
ATOM   13453 H  HA   . GLN   B  2  293 ? 15.819  -23.875 -2.419   1.00 67.15  ? 297  GLN   B HA   1 
ATOM   13454 H  HB2  . GLN   B  2  293 ? 14.727  -25.281 -4.603   1.00 69.31  ? 297  GLN   B HB2  1 
ATOM   13455 H  HB3  . GLN   B  2  293 ? 13.831  -24.400 -3.631   1.00 69.31  ? 297  GLN   B HB3  1 
ATOM   13456 H  HG2  . GLN   B  2  293 ? 14.898  -22.484 -4.336   1.00 74.02  ? 297  GLN   B HG2  1 
ATOM   13457 H  HG3  . GLN   B  2  293 ? 15.878  -23.341 -5.247   1.00 74.02  ? 297  GLN   B HG3  1 
ATOM   13458 H  HE21 . GLN   B  2  293 ? 13.702  -21.301 -5.746   1.00 78.39  ? 297  GLN   B HE21 1 
ATOM   13459 H  HE22 . GLN   B  2  293 ? 12.928  -21.842 -6.898   1.00 78.39  ? 297  GLN   B HE22 1 
ATOM   13460 N  N    . LEU   B  2  294 ? 15.354  -27.050 -2.279   1.00 48.69  ? 298  LEU   B N    1 
ATOM   13461 C  CA   . LEU   B  2  294 ? 14.935  -28.114 -1.371   1.00 51.09  ? 298  LEU   B CA   1 
ATOM   13462 C  C    . LEU   B  2  294 ? 15.731  -28.074 -0.073   1.00 55.42  ? 298  LEU   B C    1 
ATOM   13463 O  O    . LEU   B  2  294 ? 15.165  -28.232 1.015    1.00 57.04  ? 298  LEU   B O    1 
ATOM   13464 C  CB   . LEU   B  2  294 ? 15.086  -29.477 -2.047   1.00 48.88  ? 298  LEU   B CB   1 
ATOM   13465 C  CG   . LEU   B  2  294 ? 14.080  -29.818 -3.148   1.00 46.05  ? 298  LEU   B CG   1 
ATOM   13466 C  CD1  . LEU   B  2  294 ? 14.512  -31.076 -3.884   1.00 48.39  ? 298  LEU   B CD1  1 
ATOM   13467 C  CD2  . LEU   B  2  294 ? 12.681  -29.993 -2.578   1.00 45.12  ? 298  LEU   B CD2  1 
ATOM   13468 H  H    . LEU   B  2  294 ? 15.676  -27.323 -3.028   1.00 58.41  ? 298  LEU   B H    1 
ATOM   13469 H  HA   . LEU   B  2  294 ? 13.997  -27.987 -1.158   1.00 61.29  ? 298  LEU   B HA   1 
ATOM   13470 H  HB2  . LEU   B  2  294 ? 15.969  -29.515 -2.448   1.00 58.64  ? 298  LEU   B HB2  1 
ATOM   13471 H  HB3  . LEU   B  2  294 ? 15.002  -30.160 -1.364   1.00 58.64  ? 298  LEU   B HB3  1 
ATOM   13472 H  HG   . LEU   B  2  294 ? 14.051  -29.082 -3.780   1.00 55.24  ? 298  LEU   B HG   1 
ATOM   13473 H  HD11 . LEU   B  2  294 ? 13.865  -31.272 -4.580   1.00 58.05  ? 298  LEU   B HD11 1 
ATOM   13474 H  HD12 . LEU   B  2  294 ? 15.386  -30.927 -4.277   1.00 58.05  ? 298  LEU   B HD12 1 
ATOM   13475 H  HD13 . LEU   B  2  294 ? 14.554  -31.812 -3.254   1.00 58.05  ? 298  LEU   B HD13 1 
ATOM   13476 H  HD21 . LEU   B  2  294 ? 12.073  -30.220 -3.299   1.00 54.13  ? 298  LEU   B HD21 1 
ATOM   13477 H  HD22 . LEU   B  2  294 ? 12.695  -30.705 -1.920   1.00 54.13  ? 298  LEU   B HD22 1 
ATOM   13478 H  HD23 . LEU   B  2  294 ? 12.404  -29.162 -2.161   1.00 54.13  ? 298  LEU   B HD23 1 
ATOM   13479 N  N    . ILE   B  2  295 ? 17.048  -27.870 -0.165   1.00 54.47  ? 299  ILE   B N    1 
ATOM   13480 C  CA   . ILE   B  2  295 ? 17.868  -27.769 1.040    1.00 55.09  ? 299  ILE   B CA   1 
ATOM   13481 C  C    . ILE   B  2  295 ? 17.337  -26.665 1.944    1.00 55.72  ? 299  ILE   B C    1 
ATOM   13482 O  O    . ILE   B  2  295 ? 17.205  -26.841 3.161    1.00 56.37  ? 299  ILE   B O    1 
ATOM   13483 C  CB   . ILE   B  2  295 ? 19.344  -27.527 0.673    1.00 55.12  ? 299  ILE   B CB   1 
ATOM   13484 C  CG1  . ILE   B  2  295 ? 19.932  -28.764 -0.009   1.00 58.69  ? 299  ILE   B CG1  1 
ATOM   13485 C  CG2  . ILE   B  2  295 ? 20.154  -27.164 1.921    1.00 51.56  ? 299  ILE   B CG2  1 
ATOM   13486 C  CD1  . ILE   B  2  295 ? 21.331  -28.557 -0.564   1.00 62.63  ? 299  ILE   B CD1  1 
ATOM   13487 H  H    . ILE   B  2  295 ? 17.482  -27.787 -0.903   1.00 65.34  ? 299  ILE   B H    1 
ATOM   13488 H  HA   . ILE   B  2  295 ? 17.812  -28.610 1.520    1.00 66.09  ? 299  ILE   B HA   1 
ATOM   13489 H  HB   . ILE   B  2  295 ? 19.386  -26.784 0.051    1.00 66.13  ? 299  ILE   B HB   1 
ATOM   13490 H  HG12 . ILE   B  2  295 ? 19.975  -29.485 0.638    1.00 70.41  ? 299  ILE   B HG12 1 
ATOM   13491 H  HG13 . ILE   B  2  295 ? 19.356  -29.015 -0.748   1.00 70.41  ? 299  ILE   B HG13 1 
ATOM   13492 H  HG21 . ILE   B  2  295 ? 21.092  -27.103 1.681    1.00 61.85  ? 299  ILE   B HG21 1 
ATOM   13493 H  HG22 . ILE   B  2  295 ? 19.844  -26.311 2.262    1.00 61.85  ? 299  ILE   B HG22 1 
ATOM   13494 H  HG23 . ILE   B  2  295 ? 20.028  -27.854 2.591    1.00 61.85  ? 299  ILE   B HG23 1 
ATOM   13495 H  HD11 . ILE   B  2  295 ? 21.595  -29.349 -1.057   1.00 75.13  ? 299  ILE   B HD11 1 
ATOM   13496 H  HD12 . ILE   B  2  295 ? 21.326  -27.787 -1.153   1.00 75.13  ? 299  ILE   B HD12 1 
ATOM   13497 H  HD13 . ILE   B  2  295 ? 21.944  -28.407 0.173    1.00 75.13  ? 299  ILE   B HD13 1 
ATOM   13498 N  N    . ASP   B  2  296 ? 17.027  -25.507 1.359    1.00 54.55  ? 300  ASP   B N    1 
ATOM   13499 C  CA   . ASP   B  2  296 ? 16.596  -24.364 2.155    1.00 56.92  ? 300  ASP   B CA   1 
ATOM   13500 C  C    . ASP   B  2  296 ? 15.344  -24.697 2.958    1.00 54.49  ? 300  ASP   B C    1 
ATOM   13501 O  O    . ASP   B  2  296 ? 15.261  -24.396 4.154    1.00 55.29  ? 300  ASP   B O    1 
ATOM   13502 C  CB   . ASP   B  2  296 ? 16.349  -23.160 1.245    1.00 64.38  ? 300  ASP   B CB   1 
ATOM   13503 C  CG   . ASP   B  2  296 ? 16.267  -21.857 2.013    1.00 72.67  ? 300  ASP   B CG   1 
ATOM   13504 O  OD1  . ASP   B  2  296 ? 17.315  -21.392 2.508    1.00 77.12  ? 300  ASP   B OD1  1 
ATOM   13505 O  OD2  . ASP   B  2  296 ? 15.155  -21.297 2.123    1.00 76.12  ? 300  ASP   B OD2  1 
ATOM   13506 H  H    . ASP   B  2  296 ? 17.059  -25.360 0.512    1.00 65.45  ? 300  ASP   B H    1 
ATOM   13507 H  HA   . ASP   B  2  296 ? 17.300  -24.133 2.781    1.00 68.28  ? 300  ASP   B HA   1 
ATOM   13508 H  HB2  . ASP   B  2  296 ? 17.078  -23.089 0.609    1.00 77.24  ? 300  ASP   B HB2  1 
ATOM   13509 H  HB3  . ASP   B  2  296 ? 15.510  -23.285 0.775    1.00 77.24  ? 300  ASP   B HB3  1 
ATOM   13510 N  N    . LYS   B  2  297 ? 14.360  -25.332 2.317    1.00 53.39  ? 301  LYS   B N    1 
ATOM   13511 C  CA   . LYS   B  2  297 ? 13.083  -25.576 2.977    1.00 57.83  ? 301  LYS   B CA   1 
ATOM   13512 C  C    . LYS   B  2  297 ? 13.108  -26.823 3.854    1.00 59.43  ? 301  LYS   B C    1 
ATOM   13513 O  O    . LYS   B  2  297 ? 12.360  -26.894 4.835    1.00 65.20  ? 301  LYS   B O    1 
ATOM   13514 C  CB   . LYS   B  2  297 ? 11.970  -25.683 1.933    1.00 59.19  ? 301  LYS   B CB   1 
ATOM   13515 C  CG   . LYS   B  2  297 ? 11.747  -24.398 1.143    1.00 67.75  ? 301  LYS   B CG   1 
ATOM   13516 C  CD   . LYS   B  2  297 ? 11.347  -23.239 2.049    1.00 75.61  ? 301  LYS   B CD   1 
ATOM   13517 C  CE   . LYS   B  2  297 ? 11.193  -21.947 1.269    1.00 81.14  ? 301  LYS   B CE   1 
ATOM   13518 N  NZ   . LYS   B  2  297 ? 10.853  -20.805 2.161    1.00 88.79  ? 301  LYS   B NZ   1 
ATOM   13519 H  H    . LYS   B  2  297 ? 14.409  -25.627 1.510    1.00 64.05  ? 301  LYS   B H    1 
ATOM   13520 H  HA   . LYS   B  2  297 ? 12.884  -24.823 3.554    1.00 69.38  ? 301  LYS   B HA   1 
ATOM   13521 H  HB2  . LYS   B  2  297 ? 12.200  -26.383 1.302    1.00 71.01  ? 301  LYS   B HB2  1 
ATOM   13522 H  HB3  . LYS   B  2  297 ? 11.140  -25.903 2.383    1.00 71.01  ? 301  LYS   B HB3  1 
ATOM   13523 H  HG2  . LYS   B  2  297 ? 12.567  -24.157 0.685    1.00 81.28  ? 301  LYS   B HG2  1 
ATOM   13524 H  HG3  . LYS   B  2  297 ? 11.036  -24.538 0.498    1.00 81.28  ? 301  LYS   B HG3  1 
ATOM   13525 H  HD2  . LYS   B  2  297 ? 10.498  -23.441 2.473    1.00 90.71  ? 301  LYS   B HD2  1 
ATOM   13526 H  HD3  . LYS   B  2  297 ? 12.032  -23.108 2.723    1.00 90.71  ? 301  LYS   B HD3  1 
ATOM   13527 H  HE2  . LYS   B  2  297 ? 12.027  -21.744 0.818    1.00 97.35  ? 301  LYS   B HE2  1 
ATOM   13528 H  HE3  . LYS   B  2  297 ? 10.480  -22.048 0.618    1.00 97.35  ? 301  LYS   B HE3  1 
ATOM   13529 H  HZ1  . LYS   B  2  297 ? 10.780  -20.058 1.683    1.00 106.53 ? 301  LYS   B HZ1  1 
ATOM   13530 H  HZ2  . LYS   B  2  297 ? 10.080  -20.961 2.574    1.00 106.53 ? 301  LYS   B HZ2  1 
ATOM   13531 H  HZ3  . LYS   B  2  297 ? 11.491  -20.696 2.772    1.00 106.53 ? 301  LYS   B HZ3  1 
ATOM   13532 N  N    . LEU   B  2  298 ? 13.948  -27.808 3.531    1.00 52.50  ? 302  LEU   B N    1 
ATOM   13533 C  CA   . LEU   B  2  298 ? 14.065  -28.972 4.403    1.00 55.61  ? 302  LEU   B CA   1 
ATOM   13534 C  C    . LEU   B  2  298 ? 14.716  -28.598 5.729    1.00 59.66  ? 302  LEU   B C    1 
ATOM   13535 O  O    . LEU   B  2  298 ? 14.286  -29.061 6.792    1.00 60.48  ? 302  LEU   B O    1 
ATOM   13536 C  CB   . LEU   B  2  298 ? 14.859  -30.076 3.707    1.00 52.00  ? 302  LEU   B CB   1 
ATOM   13537 C  CG   . LEU   B  2  298 ? 14.117  -30.803 2.584    1.00 52.56  ? 302  LEU   B CG   1 
ATOM   13538 C  CD1  . LEU   B  2  298 ? 15.075  -31.680 1.796    1.00 52.99  ? 302  LEU   B CD1  1 
ATOM   13539 C  CD2  . LEU   B  2  298 ? 12.967  -31.633 3.144    1.00 52.99  ? 302  LEU   B CD2  1 
ATOM   13540 H  H    . LEU   B  2  298 ? 14.448  -27.824 2.832    1.00 62.98  ? 302  LEU   B H    1 
ATOM   13541 H  HA   . LEU   B  2  298 ? 13.177  -29.316 4.588    1.00 66.72  ? 302  LEU   B HA   1 
ATOM   13542 H  HB2  . LEU   B  2  298 ? 15.656  -29.681 3.320    1.00 62.38  ? 302  LEU   B HB2  1 
ATOM   13543 H  HB3  . LEU   B  2  298 ? 15.105  -30.739 4.370    1.00 62.38  ? 302  LEU   B HB3  1 
ATOM   13544 H  HG   . LEU   B  2  298 ? 13.741  -30.145 1.979    1.00 63.06  ? 302  LEU   B HG   1 
ATOM   13545 H  HD11 . LEU   B  2  298 ? 14.578  -32.158 1.114    1.00 63.57  ? 302  LEU   B HD11 1 
ATOM   13546 H  HD12 . LEU   B  2  298 ? 15.749  -31.118 1.381    1.00 63.57  ? 302  LEU   B HD12 1 
ATOM   13547 H  HD13 . LEU   B  2  298 ? 15.497  -32.310 2.401    1.00 63.57  ? 302  LEU   B HD13 1 
ATOM   13548 H  HD21 . LEU   B  2  298 ? 12.558  -32.134 2.421    1.00 63.57  ? 302  LEU   B HD21 1 
ATOM   13549 H  HD22 . LEU   B  2  298 ? 13.314  -32.243 3.814    1.00 63.57  ? 302  LEU   B HD22 1 
ATOM   13550 H  HD23 . LEU   B  2  298 ? 12.314  -31.038 3.545    1.00 63.57  ? 302  LEU   B HD23 1 
ATOM   13551 N  N    . VAL   B  2  299 ? 15.749  -27.755 5.688    1.00 58.51  ? 303  VAL   B N    1 
ATOM   13552 C  CA   . VAL   B  2  299 ? 16.385  -27.303 6.921    1.00 58.16  ? 303  VAL   B CA   1 
ATOM   13553 C  C    . VAL   B  2  299 ? 15.448  -26.388 7.697    1.00 63.62  ? 303  VAL   B C    1 
ATOM   13554 O  O    . VAL   B  2  299 ? 15.306  -26.512 8.920    1.00 68.62  ? 303  VAL   B O    1 
ATOM   13555 C  CB   . VAL   B  2  299 ? 17.721  -26.605 6.605    1.00 56.14  ? 303  VAL   B CB   1 
ATOM   13556 C  CG1  . VAL   B  2  299 ? 18.338  -26.031 7.871    1.00 58.17  ? 303  VAL   B CG1  1 
ATOM   13557 C  CG2  . VAL   B  2  299 ? 18.683  -27.573 5.933    1.00 57.33  ? 303  VAL   B CG2  1 
ATOM   13558 H  H    . VAL   B  2  299 ? 16.095  -27.435 4.969    1.00 70.19  ? 303  VAL   B H    1 
ATOM   13559 H  HA   . VAL   B  2  299 ? 16.573  -28.079 7.473    1.00 69.77  ? 303  VAL   B HA   1 
ATOM   13560 H  HB   . VAL   B  2  299 ? 17.552  -25.872 5.992    1.00 67.35  ? 303  VAL   B HB   1 
ATOM   13561 H  HG11 . VAL   B  2  299 ? 19.242  -25.739 7.677    1.00 69.79  ? 303  VAL   B HG11 1 
ATOM   13562 H  HG12 . VAL   B  2  299 ? 17.804  -25.279 8.169    1.00 69.79  ? 303  VAL   B HG12 1 
ATOM   13563 H  HG13 . VAL   B  2  299 ? 18.351  -26.719 8.555    1.00 69.79  ? 303  VAL   B HG13 1 
ATOM   13564 H  HG21 . VAL   B  2  299 ? 19.515  -27.111 5.745    1.00 68.77  ? 303  VAL   B HG21 1 
ATOM   13565 H  HG22 . VAL   B  2  299 ? 18.847  -28.320 6.529    1.00 68.77  ? 303  VAL   B HG22 1 
ATOM   13566 H  HG23 . VAL   B  2  299 ? 18.287  -27.890 5.106    1.00 68.77  ? 303  VAL   B HG23 1 
ATOM   13567 N  N    . GLN   B  2  300 ? 14.794  -25.455 7.002    1.00 63.63  ? 304  GLN   B N    1 
ATOM   13568 C  CA   . GLN   B  2  300 ? 13.921  -24.499 7.673    1.00 68.30  ? 304  GLN   B CA   1 
ATOM   13569 C  C    . GLN   B  2  300 ? 12.778  -25.192 8.403    1.00 64.50  ? 304  GLN   B C    1 
ATOM   13570 O  O    . GLN   B  2  300 ? 12.349  -24.727 9.465    1.00 64.91  ? 304  GLN   B O    1 
ATOM   13571 C  CB   . GLN   B  2  300 ? 13.379  -23.501 6.651    1.00 79.07  ? 304  GLN   B CB   1 
ATOM   13572 C  CG   . GLN   B  2  300 ? 12.523  -22.391 7.236    1.00 91.18  ? 304  GLN   B CG   1 
ATOM   13573 C  CD   . GLN   B  2  300 ? 12.167  -21.336 6.206    1.00 100.99 ? 304  GLN   B CD   1 
ATOM   13574 O  OE1  . GLN   B  2  300 ? 12.863  -21.171 5.205    1.00 100.21 ? 304  GLN   B OE1  1 
ATOM   13575 N  NE2  . GLN   B  2  300 ? 11.076  -20.617 6.446    1.00 109.40 ? 304  GLN   B NE2  1 
ATOM   13576 H  H    . GLN   B  2  300 ? 14.839  -25.357 6.149    1.00 76.34  ? 304  GLN   B H    1 
ATOM   13577 H  HA   . GLN   B  2  300 ? 14.435  -24.010 8.335    1.00 81.94  ? 304  GLN   B HA   1 
ATOM   13578 H  HB2  . GLN   B  2  300 ? 14.129  -23.083 6.200    1.00 94.87  ? 304  GLN   B HB2  1 
ATOM   13579 H  HB3  . GLN   B  2  300 ? 12.833  -23.982 6.010    1.00 94.87  ? 304  GLN   B HB3  1 
ATOM   13580 H  HG2  . GLN   B  2  300 ? 11.698  -22.771 7.577    1.00 109.39 ? 304  GLN   B HG2  1 
ATOM   13581 H  HG3  . GLN   B  2  300 ? 13.011  -21.959 7.955    1.00 109.39 ? 304  GLN   B HG3  1 
ATOM   13582 H  HE21 . GLN   B  2  300 ? 10.613  -20.762 7.156    1.00 131.26 ? 304  GLN   B HE21 1 
ATOM   13583 H  HE22 . GLN   B  2  300 ? 10.833  -20.007 5.891    1.00 131.26 ? 304  GLN   B HE22 1 
ATOM   13584 N  N    . ASN   B  2  301 ? 12.276  -26.299 7.859    1.00 62.83  ? 305  ASN   B N    1 
ATOM   13585 C  CA   . ASN   B  2  301 ? 11.164  -27.030 8.449    1.00 60.52  ? 305  ASN   B CA   1 
ATOM   13586 C  C    . ASN   B  2  301 ? 11.614  -28.237 9.262    1.00 58.37  ? 305  ASN   B C    1 
ATOM   13587 O  O    . ASN   B  2  301 ? 10.768  -29.018 9.711    1.00 55.98  ? 305  ASN   B O    1 
ATOM   13588 C  CB   . ASN   B  2  301 ? 10.191  -27.473 7.355    1.00 61.33  ? 305  ASN   B CB   1 
ATOM   13589 C  CG   . ASN   B  2  301 ? 9.410   -26.313 6.769    1.00 66.00  ? 305  ASN   B CG   1 
ATOM   13590 O  OD1  . ASN   B  2  301 ? 8.306   -26.006 7.217    1.00 71.00  ? 305  ASN   B OD1  1 
ATOM   13591 N  ND2  . ASN   B  2  301 ? 9.984   -25.659 5.767    1.00 66.95  ? 305  ASN   B ND2  1 
ATOM   13592 H  H    . ASN   B  2  301 ? 12.572  -26.652 7.132    1.00 75.38  ? 305  ASN   B H    1 
ATOM   13593 H  HA   . ASN   B  2  301 ? 10.690  -26.434 9.049    1.00 72.61  ? 305  ASN   B HA   1 
ATOM   13594 H  HB2  . ASN   B  2  301 ? 10.691  -27.893 6.637    1.00 73.57  ? 305  ASN   B HB2  1 
ATOM   13595 H  HB3  . ASN   B  2  301 ? 9.557   -28.104 7.730    1.00 73.57  ? 305  ASN   B HB3  1 
ATOM   13596 H  HD21 . ASN   B  2  301 ? 9.581   -24.993 5.401    1.00 80.32  ? 305  ASN   B HD21 1 
ATOM   13597 H  HD22 . ASN   B  2  301 ? 10.759  -25.900 5.483    1.00 80.32  ? 305  ASN   B HD22 1 
ATOM   13598 N  N    . ASN   B  2  302 ? 12.919  -28.407 9.462    1.00 58.04  ? 306  ASN   B N    1 
ATOM   13599 C  CA   . ASN   B  2  302 ? 13.452  -29.485 10.291   1.00 59.25  ? 306  ASN   B CA   1 
ATOM   13600 C  C    . ASN   B  2  302 ? 12.925  -30.841 9.824    1.00 56.21  ? 306  ASN   B C    1 
ATOM   13601 O  O    . ASN   B  2  302 ? 12.416  -31.645 10.608   1.00 57.41  ? 306  ASN   B O    1 
ATOM   13602 C  CB   . ASN   B  2  302 ? 13.117  -29.244 11.764   1.00 65.99  ? 306  ASN   B CB   1 
ATOM   13603 C  CG   . ASN   B  2  302 ? 13.907  -30.139 12.699   1.00 76.28  ? 306  ASN   B CG   1 
ATOM   13604 O  OD1  . ASN   B  2  302 ? 15.132  -30.219 12.614   1.00 79.49  ? 306  ASN   B OD1  1 
ATOM   13605 N  ND2  . ASN   B  2  302 ? 13.206  -30.820 13.597   1.00 84.48  ? 306  ASN   B ND2  1 
ATOM   13606 H  H    . ASN   B  2  302 ? 13.527  -27.901 9.122    1.00 69.63  ? 306  ASN   B H    1 
ATOM   13607 H  HA   . ASN   B  2  302 ? 14.417  -29.499 10.199   1.00 71.08  ? 306  ASN   B HA   1 
ATOM   13608 H  HB2  . ASN   B  2  302 ? 13.320  -28.322 11.988   1.00 79.17  ? 306  ASN   B HB2  1 
ATOM   13609 H  HB3  . ASN   B  2  302 ? 12.173  -29.420 11.907   1.00 79.17  ? 306  ASN   B HB3  1 
ATOM   13610 H  HD21 . ASN   B  2  302 ? 13.607  -31.341 14.151   1.00 101.36 ? 306  ASN   B HD21 1 
ATOM   13611 H  HD22 . ASN   B  2  302 ? 12.350  -30.740 13.625   1.00 101.36 ? 306  ASN   B HD22 1 
ATOM   13612 N  N    . VAL   B  2  303 ? 13.054  -31.092 8.523    1.00 55.00  ? 307  VAL   B N    1 
ATOM   13613 C  CA   . VAL   B  2  303 ? 12.590  -32.326 7.898    1.00 54.16  ? 307  VAL   B CA   1 
ATOM   13614 C  C    . VAL   B  2  303 ? 13.805  -33.156 7.509    1.00 54.00  ? 307  VAL   B C    1 
ATOM   13615 O  O    . VAL   B  2  303 ? 14.720  -32.655 6.844    1.00 56.91  ? 307  VAL   B O    1 
ATOM   13616 C  CB   . VAL   B  2  303 ? 11.710  -32.037 6.668    1.00 53.74  ? 307  VAL   B CB   1 
ATOM   13617 C  CG1  . VAL   B  2  303 ? 11.367  -33.329 5.934    1.00 53.56  ? 307  VAL   B CG1  1 
ATOM   13618 C  CG2  . VAL   B  2  303 ? 10.440  -31.307 7.079    1.00 52.43  ? 307  VAL   B CG2  1 
ATOM   13619 H  H    . VAL   B  2  303 ? 13.417  -30.546 7.968    1.00 65.99  ? 307  VAL   B H    1 
ATOM   13620 H  HA   . VAL   B  2  303 ? 12.067  -32.831 8.540    1.00 64.98  ? 307  VAL   B HA   1 
ATOM   13621 H  HB   . VAL   B  2  303 ? 12.207  -31.467 6.061    1.00 64.47  ? 307  VAL   B HB   1 
ATOM   13622 H  HG11 . VAL   B  2  303 ? 10.712  -33.136 5.245    1.00 64.26  ? 307  VAL   B HG11 1 
ATOM   13623 H  HG12 . VAL   B  2  303 ? 12.174  -33.688 5.532    1.00 64.26  ? 307  VAL   B HG12 1 
ATOM   13624 H  HG13 . VAL   B  2  303 ? 11.002  -33.966 6.569    1.00 64.26  ? 307  VAL   B HG13 1 
ATOM   13625 H  HG21 . VAL   B  2  303 ? 9.892   -31.160 6.292    1.00 62.90  ? 307  VAL   B HG21 1 
ATOM   13626 H  HG22 . VAL   B  2  303 ? 9.958   -31.849 7.722    1.00 62.90  ? 307  VAL   B HG22 1 
ATOM   13627 H  HG23 . VAL   B  2  303 ? 10.680  -30.456 7.478    1.00 62.90  ? 307  VAL   B HG23 1 
ATOM   13628 N  N    . LEU   B  2  304 ? 13.813  -34.423 7.919    1.00 53.36  ? 308  LEU   B N    1 
ATOM   13629 C  CA   . LEU   B  2  304 ? 14.853  -35.368 7.533    1.00 54.19  ? 308  LEU   B CA   1 
ATOM   13630 C  C    . LEU   B  2  304 ? 14.345  -36.203 6.365    1.00 58.16  ? 308  LEU   B C    1 
ATOM   13631 O  O    . LEU   B  2  304 ? 13.284  -36.829 6.460    1.00 62.88  ? 308  LEU   B O    1 
ATOM   13632 C  CB   . LEU   B  2  304 ? 15.246  -36.272 8.699    1.00 54.26  ? 308  LEU   B CB   1 
ATOM   13633 C  CG   . LEU   B  2  304 ? 15.796  -35.592 9.954    1.00 57.07  ? 308  LEU   B CG   1 
ATOM   13634 C  CD1  . LEU   B  2  304 ? 16.178  -36.659 10.964   1.00 56.39  ? 308  LEU   B CD1  1 
ATOM   13635 C  CD2  . LEU   B  2  304 ? 16.985  -34.692 9.653    1.00 55.95  ? 308  LEU   B CD2  1 
ATOM   13636 H  H    . LEU   B  2  304 ? 13.212  -34.764 8.432    1.00 64.01  ? 308  LEU   B H    1 
ATOM   13637 H  HA   . LEU   B  2  304 ? 15.642  -34.878 7.254    1.00 65.01  ? 308  LEU   B HA   1 
ATOM   13638 H  HB2  . LEU   B  2  304 ? 14.458  -36.768 8.970    1.00 65.09  ? 308  LEU   B HB2  1 
ATOM   13639 H  HB3  . LEU   B  2  304 ? 15.931  -36.883 8.386    1.00 65.09  ? 308  LEU   B HB3  1 
ATOM   13640 H  HG   . LEU   B  2  304 ? 15.109  -35.016 10.325   1.00 68.46  ? 308  LEU   B HG   1 
ATOM   13641 H  HD11 . LEU   B  2  304 ? 16.589  -36.234 11.733   1.00 67.65  ? 308  LEU   B HD11 1 
ATOM   13642 H  HD12 . LEU   B  2  304 ? 15.378  -37.135 11.238   1.00 67.65  ? 308  LEU   B HD12 1 
ATOM   13643 H  HD13 . LEU   B  2  304 ? 16.804  -37.275 10.552   1.00 67.65  ? 308  LEU   B HD13 1 
ATOM   13644 H  HD21 . LEU   B  2  304 ? 17.157  -34.128 10.423   1.00 67.12  ? 308  LEU   B HD21 1 
ATOM   13645 H  HD22 . LEU   B  2  304 ? 17.760  -35.244 9.467    1.00 67.12  ? 308  LEU   B HD22 1 
ATOM   13646 H  HD23 . LEU   B  2  304 ? 16.778  -34.143 8.880    1.00 67.12  ? 308  LEU   B HD23 1 
ATOM   13647 N  N    . LEU   B  2  305 ? 15.102  -36.213 5.274    1.00 58.25  ? 309  LEU   B N    1 
ATOM   13648 C  CA   . LEU   B  2  305 ? 14.702  -36.884 4.045    1.00 54.99  ? 309  LEU   B CA   1 
ATOM   13649 C  C    . LEU   B  2  305 ? 15.355  -38.257 3.972    1.00 54.29  ? 309  LEU   B C    1 
ATOM   13650 O  O    . LEU   B  2  305 ? 16.551  -38.399 4.243    1.00 55.01  ? 309  LEU   B O    1 
ATOM   13651 C  CB   . LEU   B  2  305 ? 15.086  -36.037 2.831    1.00 52.32  ? 309  LEU   B CB   1 
ATOM   13652 C  CG   . LEU   B  2  305 ? 14.639  -36.505 1.446    1.00 52.15  ? 309  LEU   B CG   1 
ATOM   13653 C  CD1  . LEU   B  2  305 ? 13.146  -36.783 1.373    1.00 55.89  ? 309  LEU   B CD1  1 
ATOM   13654 C  CD2  . LEU   B  2  305 ? 15.020  -35.439 0.430    1.00 49.97  ? 309  LEU   B CD2  1 
ATOM   13655 H  H    . LEU   B  2  305 ? 15.869  -35.828 5.220    1.00 69.89  ? 309  LEU   B H    1 
ATOM   13656 H  HA   . LEU   B  2  305 ? 13.741  -37.013 4.038    1.00 65.97  ? 309  LEU   B HA   1 
ATOM   13657 H  HB2  . LEU   B  2  305 ? 14.708  -35.153 2.959    1.00 62.77  ? 309  LEU   B HB2  1 
ATOM   13658 H  HB3  . LEU   B  2  305 ? 16.054  -35.984 2.806    1.00 62.77  ? 309  LEU   B HB3  1 
ATOM   13659 H  HG   . LEU   B  2  305 ? 15.082  -37.345 1.244    1.00 62.56  ? 309  LEU   B HG   1 
ATOM   13660 H  HD11 . LEU   B  2  305 ? 12.950  -37.237 0.539    1.00 67.05  ? 309  LEU   B HD11 1 
ATOM   13661 H  HD12 . LEU   B  2  305 ? 12.892  -37.343 2.123    1.00 67.05  ? 309  LEU   B HD12 1 
ATOM   13662 H  HD13 . LEU   B  2  305 ? 12.666  -35.941 1.412    1.00 67.05  ? 309  LEU   B HD13 1 
ATOM   13663 H  HD21 . LEU   B  2  305 ? 14.665  -35.689 -0.438   1.00 59.94  ? 309  LEU   B HD21 1 
ATOM   13664 H  HD22 . LEU   B  2  305 ? 14.644  -34.589 0.709    1.00 59.94  ? 309  LEU   B HD22 1 
ATOM   13665 H  HD23 . LEU   B  2  305 ? 15.987  -35.375 0.387    1.00 59.94  ? 309  LEU   B HD23 1 
ATOM   13666 N  N    . ILE   B  2  306 ? 14.562  -39.264 3.612    1.00 54.07  ? 310  ILE   B N    1 
ATOM   13667 C  CA   . ILE   B  2  306 ? 15.031  -40.635 3.449    1.00 52.74  ? 310  ILE   B CA   1 
ATOM   13668 C  C    . ILE   B  2  306 ? 14.698  -41.056 2.024    1.00 58.14  ? 310  ILE   B C    1 
ATOM   13669 O  O    . ILE   B  2  306 ? 13.519  -41.174 1.665    1.00 68.81  ? 310  ILE   B O    1 
ATOM   13670 C  CB   . ILE   B  2  306 ? 14.394  -41.590 4.469    1.00 50.18  ? 310  ILE   B CB   1 
ATOM   13671 C  CG1  . ILE   B  2  306 ? 14.844  -41.235 5.890    1.00 51.24  ? 310  ILE   B CG1  1 
ATOM   13672 C  CG2  . ILE   B  2  306 ? 14.753  -43.038 4.143    1.00 47.72  ? 310  ILE   B CG2  1 
ATOM   13673 C  CD1  . ILE   B  2  306 ? 14.119  -42.012 6.980    1.00 51.36  ? 310  ILE   B CD1  1 
ATOM   13674 H  H    . ILE   B  2  306 ? 13.722  -39.173 3.452    1.00 64.87  ? 310  ILE   B H    1 
ATOM   13675 H  HA   . ILE   B  2  306 ? 15.994  -40.664 3.565    1.00 63.27  ? 310  ILE   B HA   1 
ATOM   13676 H  HB   . ILE   B  2  306 ? 13.431  -41.490 4.417    1.00 60.20  ? 310  ILE   B HB   1 
ATOM   13677 H  HG12 . ILE   B  2  306 ? 15.791  -41.424 5.973    1.00 61.47  ? 310  ILE   B HG12 1 
ATOM   13678 H  HG13 . ILE   B  2  306 ? 14.679  -40.291 6.041    1.00 61.47  ? 310  ILE   B HG13 1 
ATOM   13679 H  HG21 . ILE   B  2  306 ? 14.400  -43.615 4.838    1.00 57.24  ? 310  ILE   B HG21 1 
ATOM   13680 H  HG22 . ILE   B  2  306 ? 14.363  -43.275 3.287    1.00 57.24  ? 310  ILE   B HG22 1 
ATOM   13681 H  HG23 . ILE   B  2  306 ? 15.719  -43.122 4.101    1.00 57.24  ? 310  ILE   B HG23 1 
ATOM   13682 H  HD11 . ILE   B  2  306 ? 14.384  -41.663 7.845    1.00 61.61  ? 310  ILE   B HD11 1 
ATOM   13683 H  HD12 . ILE   B  2  306 ? 13.163  -41.907 6.859    1.00 61.61  ? 310  ILE   B HD12 1 
ATOM   13684 H  HD13 . ILE   B  2  306 ? 14.361  -42.949 6.913    1.00 61.61  ? 310  ILE   B HD13 1 
ATOM   13685 N  N    . PHE   B  2  307 ? 15.728  -41.277 1.211    1.00 53.87  ? 311  PHE   B N    1 
ATOM   13686 C  CA   . PHE   B  2  307 ? 15.552  -41.763 -0.154   1.00 54.13  ? 311  PHE   B CA   1 
ATOM   13687 C  C    . PHE   B  2  307 ? 15.519  -43.287 -0.131   1.00 53.74  ? 311  PHE   B C    1 
ATOM   13688 O  O    . PHE   B  2  307 ? 16.559  -43.935 0.030    1.00 50.05  ? 311  PHE   B O    1 
ATOM   13689 C  CB   . PHE   B  2  307 ? 16.670  -41.263 -1.066   1.00 57.14  ? 311  PHE   B CB   1 
ATOM   13690 C  CG   . PHE   B  2  307 ? 16.614  -39.789 -1.355   1.00 56.62  ? 311  PHE   B CG   1 
ATOM   13691 C  CD1  . PHE   B  2  307 ? 15.516  -39.233 -1.989   1.00 56.86  ? 311  PHE   B CD1  1 
ATOM   13692 C  CD2  . PHE   B  2  307 ? 17.672  -38.964 -1.012   1.00 57.59  ? 311  PHE   B CD2  1 
ATOM   13693 C  CE1  . PHE   B  2  307 ? 15.467  -37.879 -2.261   1.00 59.54  ? 311  PHE   B CE1  1 
ATOM   13694 C  CE2  . PHE   B  2  307 ? 17.629  -37.608 -1.283   1.00 56.36  ? 311  PHE   B CE2  1 
ATOM   13695 C  CZ   . PHE   B  2  307 ? 16.526  -37.066 -1.911   1.00 59.68  ? 311  PHE   B CZ   1 
ATOM   13696 H  H    . PHE   B  2  307 ? 16.550  -41.152 1.430    1.00 64.62  ? 311  PHE   B H    1 
ATOM   13697 H  HA   . PHE   B  2  307 ? 14.707  -41.433 -0.497   1.00 64.93  ? 311  PHE   B HA   1 
ATOM   13698 H  HB2  . PHE   B  2  307 ? 17.523  -41.448 -0.642   1.00 68.55  ? 311  PHE   B HB2  1 
ATOM   13699 H  HB3  . PHE   B  2  307 ? 16.613  -41.732 -1.913   1.00 68.55  ? 311  PHE   B HB3  1 
ATOM   13700 H  HD1  . PHE   B  2  307 ? 14.803  -39.778 -2.234   1.00 68.21  ? 311  PHE   B HD1  1 
ATOM   13701 H  HD2  . PHE   B  2  307 ? 18.420  -39.325 -0.594   1.00 69.09  ? 311  PHE   B HD2  1 
ATOM   13702 H  HE1  . PHE   B  2  307 ? 14.720  -37.515 -2.680   1.00 71.42  ? 311  PHE   B HE1  1 
ATOM   13703 H  HE2  . PHE   B  2  307 ? 18.343  -37.063 -1.043   1.00 67.61  ? 311  PHE   B HE2  1 
ATOM   13704 H  HZ   . PHE   B  2  307 ? 16.497  -36.156 -2.097   1.00 71.60  ? 311  PHE   B HZ   1 
ATOM   13705 N  N    . ALA   B  2  308 ? 14.328  -43.859 -0.291   1.00 54.34  ? 312  ALA   B N    1 
ATOM   13706 C  CA   . ALA   B  2  308 ? 14.153  -45.308 -0.390   1.00 54.60  ? 312  ALA   B CA   1 
ATOM   13707 C  C    . ALA   B  2  308 ? 13.990  -45.636 -1.871   1.00 54.69  ? 312  ALA   B C    1 
ATOM   13708 O  O    . ALA   B  2  308 ? 12.881  -45.648 -2.405   1.00 53.38  ? 312  ALA   B O    1 
ATOM   13709 C  CB   . ALA   B  2  308 ? 12.957  -45.772 0.432    1.00 55.81  ? 312  ALA   B CB   1 
ATOM   13710 H  H    . ALA   B  2  308 ? 13.590  -43.421 -0.347   1.00 65.19  ? 312  ALA   B H    1 
ATOM   13711 H  HA   . ALA   B  2  308 ? 14.941  -45.759 -0.050   1.00 65.50  ? 312  ALA   B HA   1 
ATOM   13712 H  HB1  . ALA   B  2  308 ? 12.859  -46.732 0.332    1.00 66.95  ? 312  ALA   B HB1  1 
ATOM   13713 H  HB2  . ALA   B  2  308 ? 13.109  -45.551 1.364    1.00 66.95  ? 312  ALA   B HB2  1 
ATOM   13714 H  HB3  . ALA   B  2  308 ? 12.160  -45.323 0.111    1.00 66.95  ? 312  ALA   B HB3  1 
ATOM   13715 N  N    . VAL   B  2  309 ? 15.113  -45.907 -2.538   1.00 59.12  ? 313  VAL   B N    1 
ATOM   13716 C  CA   . VAL   B  2  309 ? 15.143  -46.060 -3.985   1.00 61.21  ? 313  VAL   B CA   1 
ATOM   13717 C  C    . VAL   B  2  309 ? 15.784  -47.392 -4.347   1.00 60.74  ? 313  VAL   B C    1 
ATOM   13718 O  O    . VAL   B  2  309 ? 16.504  -48.003 -3.554   1.00 61.66  ? 313  VAL   B O    1 
ATOM   13719 C  CB   . VAL   B  2  309 ? 15.896  -44.897 -4.669   1.00 60.40  ? 313  VAL   B CB   1 
ATOM   13720 C  CG1  . VAL   B  2  309 ? 15.192  -43.580 -4.384   1.00 59.68  ? 313  VAL   B CG1  1 
ATOM   13721 C  CG2  . VAL   B  2  309 ? 17.343  -44.847 -4.199   1.00 59.23  ? 313  VAL   B CG2  1 
ATOM   13722 H  H    . VAL   B  2  309 ? 15.881  -46.009 -2.164   1.00 70.93  ? 313  VAL   B H    1 
ATOM   13723 H  HA   . VAL   B  2  309 ? 14.232  -46.078 -4.317   1.00 73.43  ? 313  VAL   B HA   1 
ATOM   13724 H  HB   . VAL   B  2  309 ? 15.899  -45.041 -5.628   1.00 72.47  ? 313  VAL   B HB   1 
ATOM   13725 H  HG11 . VAL   B  2  309 ? 15.671  -42.863 -4.828   1.00 71.60  ? 313  VAL   B HG11 1 
ATOM   13726 H  HG12 . VAL   B  2  309 ? 14.283  -43.629 -4.720   1.00 71.60  ? 313  VAL   B HG12 1 
ATOM   13727 H  HG13 . VAL   B  2  309 ? 15.182  -43.428 -3.426   1.00 71.60  ? 313  VAL   B HG13 1 
ATOM   13728 H  HG21 . VAL   B  2  309 ? 17.779  -44.079 -4.600   1.00 71.06  ? 313  VAL   B HG21 1 
ATOM   13729 H  HG22 . VAL   B  2  309 ? 17.359  -44.770 -3.232   1.00 71.06  ? 313  VAL   B HG22 1 
ATOM   13730 H  HG23 . VAL   B  2  309 ? 17.792  -45.663 -4.472   1.00 71.06  ? 313  VAL   B HG23 1 
ATOM   13731 N  N    . THR   B  2  310 ? 15.507  -47.836 -5.570   1.00 56.11  ? 314  THR   B N    1 
ATOM   13732 C  CA   . THR   B  2  310 ? 15.982  -49.123 -6.046   1.00 56.91  ? 314  THR   B CA   1 
ATOM   13733 C  C    . THR   B  2  310 ? 17.470  -49.061 -6.387   1.00 60.38  ? 314  THR   B C    1 
ATOM   13734 O  O    . THR   B  2  310 ? 18.079  -47.991 -6.474   1.00 60.47  ? 314  THR   B O    1 
ATOM   13735 C  CB   . THR   B  2  310 ? 15.174  -49.576 -7.264   1.00 53.54  ? 314  THR   B CB   1 
ATOM   13736 O  OG1  . THR   B  2  310 ? 15.144  -48.530 -8.243   1.00 54.43  ? 314  THR   B OG1  1 
ATOM   13737 C  CG2  . THR   B  2  310 ? 13.751  -49.931 -6.856   1.00 52.54  ? 314  THR   B CG2  1 
ATOM   13738 H  H    . THR   B  2  310 ? 15.040  -47.402 -6.148   1.00 67.32  ? 314  THR   B H    1 
ATOM   13739 H  HA   . THR   B  2  310 ? 15.864  -49.780 -5.342   1.00 68.27  ? 314  THR   B HA   1 
ATOM   13740 H  HB   . THR   B  2  310 ? 15.588  -50.364 -7.650   1.00 64.23  ? 314  THR   B HB   1 
ATOM   13741 H  HG1  . THR   B  2  310 ? 14.736  -48.791 -8.930   1.00 65.30  ? 314  THR   B HG1  1 
ATOM   13742 H  HG21 . THR   B  2  310 ? 13.249  -50.229 -7.631   1.00 63.02  ? 314  THR   B HG21 1 
ATOM   13743 H  HG22 . THR   B  2  310 ? 13.762  -50.642 -6.196   1.00 63.02  ? 314  THR   B HG22 1 
ATOM   13744 H  HG23 . THR   B  2  310 ? 13.311  -49.155 -6.476   1.00 63.02  ? 314  THR   B HG23 1 
ATOM   13745 N  N    . GLN   B  2  311 ? 18.050  -50.248 -6.584   1.00 61.31  ? 315  GLN   B N    1 
ATOM   13746 C  CA   . GLN   B  2  311 ? 19.484  -50.374 -6.830   1.00 61.59  ? 315  GLN   B CA   1 
ATOM   13747 C  C    . GLN   B  2  311 ? 19.957  -49.408 -7.910   1.00 61.57  ? 315  GLN   B C    1 
ATOM   13748 O  O    . GLN   B  2  311 ? 20.965  -48.713 -7.742   1.00 62.30  ? 315  GLN   B O    1 
ATOM   13749 C  CB   . GLN   B  2  311 ? 19.800  -51.829 -7.203   1.00 61.91  ? 315  GLN   B CB   1 
ATOM   13750 C  CG   . GLN   B  2  311 ? 20.832  -52.042 -8.310   1.00 68.66  ? 315  GLN   B CG   1 
ATOM   13751 C  CD   . GLN   B  2  311 ? 22.244  -51.703 -7.875   1.00 76.30  ? 315  GLN   B CD   1 
ATOM   13752 O  OE1  . GLN   B  2  311 ? 22.581  -51.790 -6.694   1.00 78.24  ? 315  GLN   B OE1  1 
ATOM   13753 N  NE2  . GLN   B  2  311 ? 23.079  -51.316 -8.831   1.00 81.27  ? 315  GLN   B NE2  1 
ATOM   13754 H  H    . GLN   B  2  311 ? 17.631  -51.000 -6.580   1.00 73.56  ? 315  GLN   B H    1 
ATOM   13755 H  HA   . GLN   B  2  311 ? 19.972  -50.151 -6.021   1.00 73.89  ? 315  GLN   B HA   1 
ATOM   13756 H  HB2  . GLN   B  2  311 ? 20.136  -52.277 -6.411   1.00 74.27  ? 315  GLN   B HB2  1 
ATOM   13757 H  HB3  . GLN   B  2  311 ? 18.977  -52.250 -7.497   1.00 74.27  ? 315  GLN   B HB3  1 
ATOM   13758 H  HG2  . GLN   B  2  311 ? 20.818  -52.974 -8.579   1.00 82.37  ? 315  GLN   B HG2  1 
ATOM   13759 H  HG3  . GLN   B  2  311 ? 20.607  -51.475 -9.064   1.00 82.37  ? 315  GLN   B HG3  1 
ATOM   13760 H  HE21 . GLN   B  2  311 ? 22.807  -51.268 -9.646   1.00 97.51  ? 315  GLN   B HE21 1 
ATOM   13761 H  HE22 . GLN   B  2  311 ? 23.891  -51.112 -8.636   1.00 97.51  ? 315  GLN   B HE22 1 
ATOM   13762 N  N    . GLU   B  2  312 ? 19.231  -49.345 -9.028   1.00 64.49  ? 316  GLU   B N    1 
ATOM   13763 C  CA   . GLU   B  2  312 ? 19.686  -48.555 -10.166  1.00 66.60  ? 316  GLU   B CA   1 
ATOM   13764 C  C    . GLU   B  2  312 ? 19.813  -47.072 -9.841   1.00 58.72  ? 316  GLU   B C    1 
ATOM   13765 O  O    . GLU   B  2  312 ? 20.558  -46.363 -10.527  1.00 57.65  ? 316  GLU   B O    1 
ATOM   13766 C  CB   . GLU   B  2  312 ? 18.728  -48.737 -11.347  1.00 75.72  ? 316  GLU   B CB   1 
ATOM   13767 C  CG   . GLU   B  2  312 ? 18.678  -50.151 -11.918  1.00 87.16  ? 316  GLU   B CG   1 
ATOM   13768 C  CD   . GLU   B  2  312 ? 17.851  -51.103 -11.075  1.00 96.61  ? 316  GLU   B CD   1 
ATOM   13769 O  OE1  . GLU   B  2  312 ? 17.275  -50.657 -10.060  1.00 97.71  ? 316  GLU   B OE1  1 
ATOM   13770 O  OE2  . GLU   B  2  312 ? 17.778  -52.299 -11.427  1.00 101.49 ? 316  GLU   B OE2  1 
ATOM   13771 H  H    . GLU   B  2  312 ? 18.480  -49.747 -9.149   1.00 77.37  ? 316  GLU   B H    1 
ATOM   13772 H  HA   . GLU   B  2  312 ? 20.562  -48.879 -10.426  1.00 79.90  ? 316  GLU   B HA   1 
ATOM   13773 H  HB2  . GLU   B  2  312 ? 17.832  -48.508 -11.055  1.00 90.84  ? 316  GLU   B HB2  1 
ATOM   13774 H  HB3  . GLU   B  2  312 ? 19.006  -48.144 -12.063  1.00 90.84  ? 316  GLU   B HB3  1 
ATOM   13775 H  HG2  . GLU   B  2  312 ? 18.285  -50.119 -12.804  1.00 104.57 ? 316  GLU   B HG2  1 
ATOM   13776 H  HG3  . GLU   B  2  312 ? 19.580  -50.503 -11.967  1.00 104.57 ? 316  GLU   B HG3  1 
ATOM   13777 N  N    . GLN   B  2  313 ? 19.113  -46.585 -8.817   1.00 53.92  ? 317  GLN   B N    1 
ATOM   13778 C  CA   . GLN   B  2  313 ? 19.060  -45.163 -8.510   1.00 55.28  ? 317  GLN   B CA   1 
ATOM   13779 C  C    . GLN   B  2  313 ? 19.851  -44.778 -7.267   1.00 53.97  ? 317  GLN   B C    1 
ATOM   13780 O  O    . GLN   B  2  313 ? 19.942  -43.586 -6.956   1.00 55.14  ? 317  GLN   B O    1 
ATOM   13781 C  CB   . GLN   B  2  313 ? 17.602  -44.720 -8.330   1.00 60.05  ? 317  GLN   B CB   1 
ATOM   13782 C  CG   . GLN   B  2  313 ? 16.686  -45.062 -9.495   1.00 64.70  ? 317  GLN   B CG   1 
ATOM   13783 C  CD   . GLN   B  2  313 ? 17.001  -44.261 -10.739  1.00 66.47  ? 317  GLN   B CD   1 
ATOM   13784 O  OE1  . GLN   B  2  313 ? 17.657  -43.223 -10.673  1.00 68.10  ? 317  GLN   B OE1  1 
ATOM   13785 N  NE2  . GLN   B  2  313 ? 16.534  -44.741 -11.886  1.00 68.64  ? 317  GLN   B NE2  1 
ATOM   13786 H  H    . GLN   B  2  313 ? 18.653  -47.071 -8.277   1.00 64.69  ? 317  GLN   B H    1 
ATOM   13787 H  HA   . GLN   B  2  313 ? 19.441  -44.681 -9.261   1.00 66.32  ? 317  GLN   B HA   1 
ATOM   13788 H  HB2  . GLN   B  2  313 ? 17.243  -45.153 -7.540   1.00 72.03  ? 317  GLN   B HB2  1 
ATOM   13789 H  HB3  . GLN   B  2  313 ? 17.584  -43.756 -8.217   1.00 72.03  ? 317  GLN   B HB3  1 
ATOM   13790 H  HG2  . GLN   B  2  313 ? 16.786  -46.002 -9.711   1.00 77.62  ? 317  GLN   B HG2  1 
ATOM   13791 H  HG3  . GLN   B  2  313 ? 15.768  -44.875 -9.242   1.00 77.62  ? 317  GLN   B HG3  1 
ATOM   13792 H  HE21 . GLN   B  2  313 ? 16.079  -45.471 -11.893  1.00 82.35  ? 317  GLN   B HE21 1 
ATOM   13793 H  HE22 . GLN   B  2  313 ? 16.686  -44.322 -12.621  1.00 82.35  ? 317  GLN   B HE22 1 
ATOM   13794 N  N    . VAL   B  2  314 ? 20.425  -45.745 -6.548   1.00 53.30  ? 318  VAL   B N    1 
ATOM   13795 C  CA   . VAL   B  2  314 ? 21.035  -45.445 -5.255   1.00 55.81  ? 318  VAL   B CA   1 
ATOM   13796 C  C    . VAL   B  2  314 ? 22.167  -44.436 -5.414   1.00 60.93  ? 318  VAL   B C    1 
ATOM   13797 O  O    . VAL   B  2  314 ? 22.223  -43.425 -4.705   1.00 64.27  ? 318  VAL   B O    1 
ATOM   13798 C  CB   . VAL   B  2  314 ? 21.526  -46.737 -4.578   1.00 52.92  ? 318  VAL   B CB   1 
ATOM   13799 C  CG1  . VAL   B  2  314 ? 22.516  -46.418 -3.470   1.00 51.15  ? 318  VAL   B CG1  1 
ATOM   13800 C  CG2  . VAL   B  2  314 ? 20.349  -47.515 -4.018   1.00 51.57  ? 318  VAL   B CG2  1 
ATOM   13801 H  H    . VAL   B  2  314 ? 20.473  -46.571 -6.784   1.00 63.94  ? 318  VAL   B H    1 
ATOM   13802 H  HA   . VAL   B  2  314 ? 20.360  -45.043 -4.686   1.00 66.96  ? 318  VAL   B HA   1 
ATOM   13803 H  HB   . VAL   B  2  314 ? 21.974  -47.286 -5.241   1.00 63.49  ? 318  VAL   B HB   1 
ATOM   13804 H  HG11 . VAL   B  2  314 ? 22.685  -47.223 -2.956   1.00 61.36  ? 318  VAL   B HG11 1 
ATOM   13805 H  HG12 . VAL   B  2  314 ? 23.342  -46.100 -3.867   1.00 61.36  ? 318  VAL   B HG12 1 
ATOM   13806 H  HG13 . VAL   B  2  314 ? 22.138  -45.733 -2.897   1.00 61.36  ? 318  VAL   B HG13 1 
ATOM   13807 H  HG21 . VAL   B  2  314 ? 20.682  -48.300 -3.555   1.00 61.87  ? 318  VAL   B HG21 1 
ATOM   13808 H  HG22 . VAL   B  2  314 ? 19.862  -46.948 -3.400   1.00 61.87  ? 318  VAL   B HG22 1 
ATOM   13809 H  HG23 . VAL   B  2  314 ? 19.770  -47.782 -4.749   1.00 61.87  ? 318  VAL   B HG23 1 
ATOM   13810 N  N    . HIS   B  2  315 ? 23.092  -44.700 -6.341   1.00 65.84  ? 319  HIS   B N    1 
ATOM   13811 C  CA   . HIS   B  2  315 ? 24.265  -43.840 -6.466   1.00 68.65  ? 319  HIS   B CA   1 
ATOM   13812 C  C    . HIS   B  2  315 ? 23.864  -42.396 -6.744   1.00 61.95  ? 319  HIS   B C    1 
ATOM   13813 O  O    . HIS   B  2  315 ? 24.459  -41.462 -6.194   1.00 62.67  ? 319  HIS   B O    1 
ATOM   13814 C  CB   . HIS   B  2  315 ? 25.189  -44.359 -7.567   1.00 77.35  ? 319  HIS   B CB   1 
ATOM   13815 C  CG   . HIS   B  2  315 ? 26.486  -43.617 -7.661   1.00 87.78  ? 319  HIS   B CG   1 
ATOM   13816 N  ND1  . HIS   B  2  315 ? 26.790  -42.776 -8.710   1.00 90.45  ? 319  HIS   B ND1  1 
ATOM   13817 C  CD2  . HIS   B  2  315 ? 27.555  -43.584 -6.831   1.00 91.87  ? 319  HIS   B CD2  1 
ATOM   13818 C  CE1  . HIS   B  2  315 ? 27.992  -42.261 -8.524   1.00 92.52  ? 319  HIS   B CE1  1 
ATOM   13819 N  NE2  . HIS   B  2  315 ? 28.478  -42.735 -7.391   1.00 92.90  ? 319  HIS   B NE2  1 
ATOM   13820 H  H    . HIS   B  2  315 ? 23.064  -45.356 -6.896   1.00 78.99  ? 319  HIS   B H    1 
ATOM   13821 H  HA   . HIS   B  2  315 ? 24.755  -43.862 -5.629   1.00 82.36  ? 319  HIS   B HA   1 
ATOM   13822 H  HB2  . HIS   B  2  315 ? 25.392  -45.291 -7.390   1.00 92.80  ? 319  HIS   B HB2  1 
ATOM   13823 H  HB3  . HIS   B  2  315 ? 24.736  -44.274 -8.420   1.00 92.80  ? 319  HIS   B HB3  1 
ATOM   13824 H  HD2  . HIS   B  2  315 ? 27.647  -44.049 -6.031   1.00 110.23 ? 319  HIS   B HD2  1 
ATOM   13825 H  HE1  . HIS   B  2  315 ? 28.423  -41.665 -9.094   1.00 111.00 ? 319  HIS   B HE1  1 
ATOM   13826 H  HE2  . HIS   B  2  315 ? 29.247  -42.544 -7.059   1.00 111.46 ? 319  HIS   B HE2  1 
ATOM   13827 N  N    . LEU   B  2  316 ? 22.855  -42.192 -7.592   1.00 59.08  ? 320  LEU   B N    1 
ATOM   13828 C  CA   . LEU   B  2  316 ? 22.380  -40.840 -7.865   1.00 56.76  ? 320  LEU   B CA   1 
ATOM   13829 C  C    . LEU   B  2  316 ? 21.879  -40.172 -6.590   1.00 55.51  ? 320  LEU   B C    1 
ATOM   13830 O  O    . LEU   B  2  316 ? 22.312  -39.068 -6.240   1.00 57.70  ? 320  LEU   B O    1 
ATOM   13831 C  CB   . LEU   B  2  316 ? 21.274  -40.878 -8.921   1.00 57.64  ? 320  LEU   B CB   1 
ATOM   13832 C  CG   . LEU   B  2  316 ? 20.586  -39.552 -9.257   1.00 65.88  ? 320  LEU   B CG   1 
ATOM   13833 C  CD1  . LEU   B  2  316 ? 21.524  -38.614 -9.999   1.00 70.82  ? 320  LEU   B CD1  1 
ATOM   13834 C  CD2  . LEU   B  2  316 ? 19.330  -39.810 -10.074  1.00 70.43  ? 320  LEU   B CD2  1 
ATOM   13835 H  H    . LEU   B  2  316 ? 22.436  -42.812 -8.017   1.00 70.88  ? 320  LEU   B H    1 
ATOM   13836 H  HA   . LEU   B  2  316 ? 23.115  -40.313 -8.215   1.00 68.09  ? 320  LEU   B HA   1 
ATOM   13837 H  HB2  . LEU   B  2  316 ? 21.661  -41.213 -9.746   1.00 69.15  ? 320  LEU   B HB2  1 
ATOM   13838 H  HB3  . LEU   B  2  316 ? 20.584  -41.483 -8.609   1.00 69.15  ? 320  LEU   B HB3  1 
ATOM   13839 H  HG   . LEU   B  2  316 ? 20.334  -39.112 -8.430   1.00 79.04  ? 320  LEU   B HG   1 
ATOM   13840 H  HD11 . LEU   B  2  316 ? 21.055  -37.787 -10.193  1.00 84.97  ? 320  LEU   B HD11 1 
ATOM   13841 H  HD12 . LEU   B  2  316 ? 22.296  -38.433 -9.441   1.00 84.97  ? 320  LEU   B HD12 1 
ATOM   13842 H  HD13 . LEU   B  2  316 ? 21.805  -39.036 -10.826  1.00 84.97  ? 320  LEU   B HD13 1 
ATOM   13843 H  HD21 . LEU   B  2  316 ? 18.897  -38.963 -10.264  1.00 84.50  ? 320  LEU   B HD21 1 
ATOM   13844 H  HD22 . LEU   B  2  316 ? 19.578  -40.249 -10.903  1.00 84.50  ? 320  LEU   B HD22 1 
ATOM   13845 H  HD23 . LEU   B  2  316 ? 18.734  -40.380 -9.564   1.00 84.50  ? 320  LEU   B HD23 1 
ATOM   13846 N  N    . TYR   B  2  317 ? 20.965  -40.834 -5.876   1.00 52.80  ? 321  TYR   B N    1 
ATOM   13847 C  CA   . TYR   B  2  317 ? 20.351  -40.214 -4.708   1.00 53.97  ? 321  TYR   B CA   1 
ATOM   13848 C  C    . TYR   B  2  317 ? 21.324  -40.108 -3.540   1.00 55.73  ? 321  TYR   B C    1 
ATOM   13849 O  O    . TYR   B  2  317 ? 21.173  -39.220 -2.694   1.00 60.98  ? 321  TYR   B O    1 
ATOM   13850 C  CB   . TYR   B  2  317 ? 19.100  -40.994 -4.302   1.00 54.13  ? 321  TYR   B CB   1 
ATOM   13851 C  CG   . TYR   B  2  317 ? 17.919  -40.724 -5.207   1.00 50.46  ? 321  TYR   B CG   1 
ATOM   13852 C  CD1  . TYR   B  2  317 ? 17.059  -39.664 -4.957   1.00 50.98  ? 321  TYR   B CD1  1 
ATOM   13853 C  CD2  . TYR   B  2  317 ? 17.670  -41.520 -6.318   1.00 49.52  ? 321  TYR   B CD2  1 
ATOM   13854 C  CE1  . TYR   B  2  317 ? 15.981  -39.407 -5.781   1.00 48.33  ? 321  TYR   B CE1  1 
ATOM   13855 C  CE2  . TYR   B  2  317 ? 16.593  -41.270 -7.150   1.00 50.72  ? 321  TYR   B CE2  1 
ATOM   13856 C  CZ   . TYR   B  2  317 ? 15.752  -40.212 -6.876   1.00 48.85  ? 321  TYR   B CZ   1 
ATOM   13857 O  OH   . TYR   B  2  317 ? 14.679  -39.957 -7.697   1.00 48.49  ? 321  TYR   B OH   1 
ATOM   13858 H  H    . TYR   B  2  317 ? 20.689  -41.631 -6.047   1.00 63.34  ? 321  TYR   B H    1 
ATOM   13859 H  HA   . TYR   B  2  317 ? 20.078  -39.312 -4.939   1.00 64.75  ? 321  TYR   B HA   1 
ATOM   13860 H  HB2  . TYR   B  2  317 ? 19.296  -41.943 -4.339   1.00 64.94  ? 321  TYR   B HB2  1 
ATOM   13861 H  HB3  . TYR   B  2  317 ? 18.850  -40.741 -3.400   1.00 64.94  ? 321  TYR   B HB3  1 
ATOM   13862 H  HD1  . TYR   B  2  317 ? 17.211  -39.117 -4.220   1.00 61.16  ? 321  TYR   B HD1  1 
ATOM   13863 H  HD2  . TYR   B  2  317 ? 18.237  -42.232 -6.506   1.00 59.40  ? 321  TYR   B HD2  1 
ATOM   13864 H  HE1  . TYR   B  2  317 ? 15.412  -38.694 -5.598   1.00 57.98  ? 321  TYR   B HE1  1 
ATOM   13865 H  HE2  . TYR   B  2  317 ? 16.438  -41.812 -7.890   1.00 60.85  ? 321  TYR   B HE2  1 
ATOM   13866 H  HH   . TYR   B  2  317 ? 14.655  -40.519 -8.321   1.00 58.16  ? 321  TYR   B HH   1 
ATOM   13867 N  N    . GLU   B  2  318 ? 22.321  -40.992 -3.470   1.00 53.19  ? 322  GLU   B N    1 
ATOM   13868 C  CA   . GLU   B  2  318 ? 23.364  -40.825 -2.464   1.00 55.37  ? 322  GLU   B CA   1 
ATOM   13869 C  C    . GLU   B  2  318 ? 24.144  -39.540 -2.701   1.00 57.71  ? 322  GLU   B C    1 
ATOM   13870 O  O    . GLU   B  2  318 ? 24.473  -38.820 -1.751   1.00 61.01  ? 322  GLU   B O    1 
ATOM   13871 C  CB   . GLU   B  2  318 ? 24.302  -42.030 -2.465   1.00 60.49  ? 322  GLU   B CB   1 
ATOM   13872 C  CG   . GLU   B  2  318 ? 23.818  -43.184 -1.604   1.00 68.78  ? 322  GLU   B CG   1 
ATOM   13873 C  CD   . GLU   B  2  318 ? 24.765  -44.363 -1.630   1.00 80.74  ? 322  GLU   B CD   1 
ATOM   13874 O  OE1  . GLU   B  2  318 ? 25.597  -44.438 -2.559   1.00 84.95  ? 322  GLU   B OE1  1 
ATOM   13875 O  OE2  . GLU   B  2  318 ? 24.686  -45.212 -0.716   1.00 85.76  ? 322  GLU   B OE2  1 
ATOM   13876 H  H    . GLU   B  2  318 ? 22.413  -41.678 -3.980   1.00 63.81  ? 322  GLU   B H    1 
ATOM   13877 H  HA   . GLU   B  2  318 ? 22.950  -40.775 -1.588   1.00 66.42  ? 322  GLU   B HA   1 
ATOM   13878 H  HB2  . GLU   B  2  318 ? 24.389  -42.356 -3.375   1.00 72.57  ? 322  GLU   B HB2  1 
ATOM   13879 H  HB3  . GLU   B  2  318 ? 25.168  -41.752 -2.128   1.00 72.57  ? 322  GLU   B HB3  1 
ATOM   13880 H  HG2  . GLU   B  2  318 ? 23.739  -42.882 -0.686   1.00 82.52  ? 322  GLU   B HG2  1 
ATOM   13881 H  HG3  . GLU   B  2  318 ? 22.956  -43.483 -1.931   1.00 82.52  ? 322  GLU   B HG3  1 
ATOM   13882 N  N    . ASN   B  2  319 ? 24.446  -39.231 -3.964   1.00 58.47  ? 323  ASN   B N    1 
ATOM   13883 C  CA   . ASN   B  2  319 ? 25.106  -37.967 -4.272   1.00 59.92  ? 323  ASN   B CA   1 
ATOM   13884 C  C    . ASN   B  2  319 ? 24.229  -36.786 -3.877   1.00 57.48  ? 323  ASN   B C    1 
ATOM   13885 O  O    . ASN   B  2  319 ? 24.722  -35.793 -3.330   1.00 59.99  ? 323  ASN   B O    1 
ATOM   13886 C  CB   . ASN   B  2  319 ? 25.457  -37.908 -5.757   1.00 67.06  ? 323  ASN   B CB   1 
ATOM   13887 C  CG   . ASN   B  2  319 ? 26.672  -38.745 -6.100   1.00 75.89  ? 323  ASN   B CG   1 
ATOM   13888 O  OD1  . ASN   B  2  319 ? 26.580  -39.718 -6.849   1.00 78.26  ? 323  ASN   B OD1  1 
ATOM   13889 N  ND2  . ASN   B  2  319 ? 27.822  -38.368 -5.554   1.00 80.37  ? 323  ASN   B ND2  1 
ATOM   13890 H  H    . ASN   B  2  319 ? 24.283  -39.728 -4.647   1.00 70.14  ? 323  ASN   B H    1 
ATOM   13891 H  HA   . ASN   B  2  319 ? 25.933  -37.910 -3.768   1.00 71.89  ? 323  ASN   B HA   1 
ATOM   13892 H  HB2  . ASN   B  2  319 ? 24.707  -38.241 -6.274   1.00 80.45  ? 323  ASN   B HB2  1 
ATOM   13893 H  HB3  . ASN   B  2  319 ? 25.647  -36.989 -6.002   1.00 80.45  ? 323  ASN   B HB3  1 
ATOM   13894 H  HD21 . ASN   B  2  319 ? 28.541  -38.810 -5.717   1.00 96.43  ? 323  ASN   B HD21 1 
ATOM   13895 H  HD22 . ASN   B  2  319 ? 27.847  -37.681 -5.037   1.00 96.43  ? 323  ASN   B HD22 1 
ATOM   13896 N  N    . TYR   B  2  320 ? 22.923  -36.874 -4.148   1.00 57.64  ? 324  TYR   B N    1 
ATOM   13897 C  CA   . TYR   B  2  320 ? 22.002  -35.852 -3.661   1.00 56.94  ? 324  TYR   B CA   1 
ATOM   13898 C  C    . TYR   B  2  320 ? 22.043  -35.761 -2.140   1.00 56.80  ? 324  TYR   B C    1 
ATOM   13899 O  O    . TYR   B  2  320 ? 22.052  -34.661 -1.575   1.00 56.33  ? 324  TYR   B O    1 
ATOM   13900 C  CB   . TYR   B  2  320 ? 20.574  -36.150 -4.128   1.00 53.52  ? 324  TYR   B CB   1 
ATOM   13901 C  CG   . TYR   B  2  320 ? 20.288  -35.887 -5.597   1.00 57.51  ? 324  TYR   B CG   1 
ATOM   13902 C  CD1  . TYR   B  2  320 ? 21.046  -34.985 -6.334   1.00 61.98  ? 324  TYR   B CD1  1 
ATOM   13903 C  CD2  . TYR   B  2  320 ? 19.245  -36.542 -6.241   1.00 61.50  ? 324  TYR   B CD2  1 
ATOM   13904 C  CE1  . TYR   B  2  320 ? 20.776  -34.749 -7.673   1.00 66.98  ? 324  TYR   B CE1  1 
ATOM   13905 C  CE2  . TYR   B  2  320 ? 18.970  -36.313 -7.574   1.00 63.23  ? 324  TYR   B CE2  1 
ATOM   13906 C  CZ   . TYR   B  2  320 ? 19.736  -35.417 -8.285   1.00 67.29  ? 324  TYR   B CZ   1 
ATOM   13907 O  OH   . TYR   B  2  320 ? 19.458  -35.191 -9.613   1.00 70.10  ? 324  TYR   B OH   1 
ATOM   13908 H  H    . TYR   B  2  320 ? 22.554  -37.504 -4.602   1.00 69.15  ? 324  TYR   B H    1 
ATOM   13909 H  HA   . TYR   B  2  320 ? 22.267  -34.996 -4.034   1.00 68.31  ? 324  TYR   B HA   1 
ATOM   13910 H  HB2  . TYR   B  2  320 ? 20.390  -37.088 -3.963   1.00 64.21  ? 324  TYR   B HB2  1 
ATOM   13911 H  HB3  . TYR   B  2  320 ? 19.964  -35.597 -3.614   1.00 64.21  ? 324  TYR   B HB3  1 
ATOM   13912 H  HD1  . TYR   B  2  320 ? 21.746  -34.531 -5.923   1.00 74.35  ? 324  TYR   B HD1  1 
ATOM   13913 H  HD2  . TYR   B  2  320 ? 18.723  -37.146 -5.764   1.00 73.79  ? 324  TYR   B HD2  1 
ATOM   13914 H  HE1  . TYR   B  2  320 ? 21.293  -34.145 -8.155   1.00 80.35  ? 324  TYR   B HE1  1 
ATOM   13915 H  HE2  . TYR   B  2  320 ? 18.270  -36.762 -7.990   1.00 75.85  ? 324  TYR   B HE2  1 
ATOM   13916 H  HH   . TYR   B  2  320 ? 18.814  -35.671 -9.857   1.00 84.10  ? 324  TYR   B HH   1 
ATOM   13917 N  N    . ALA   B  2  321 ? 22.074  -36.911 -1.458   1.00 56.43  ? 325  ALA   B N    1 
ATOM   13918 C  CA   . ALA   B  2  321 ? 22.038  -36.906 0.001    1.00 57.03  ? 325  ALA   B CA   1 
ATOM   13919 C  C    . ALA   B  2  321 ? 23.299  -36.295 0.597    1.00 57.78  ? 325  ALA   B C    1 
ATOM   13920 O  O    . ALA   B  2  321 ? 23.262  -35.779 1.720    1.00 60.40  ? 325  ALA   B O    1 
ATOM   13921 C  CB   . ALA   B  2  321 ? 21.839  -38.327 0.530    1.00 54.74  ? 325  ALA   B CB   1 
ATOM   13922 H  H    . ALA   B  2  321 ? 22.115  -37.693 -1.813   1.00 67.69  ? 325  ALA   B H    1 
ATOM   13923 H  HA   . ALA   B  2  321 ? 21.281  -36.370 0.287    1.00 68.42  ? 325  ALA   B HA   1 
ATOM   13924 H  HB1  . ALA   B  2  321 ? 21.808  -38.302 1.499    1.00 65.67  ? 325  ALA   B HB1  1 
ATOM   13925 H  HB2  . ALA   B  2  321 ? 21.005  -38.680 0.182    1.00 65.67  ? 325  ALA   B HB2  1 
ATOM   13926 H  HB3  . ALA   B  2  321 ? 22.580  -38.880 0.238    1.00 65.67  ? 325  ALA   B HB3  1 
ATOM   13927 N  N    . LYS   B  2  322 ? 24.421  -36.345 -0.124   1.00 55.20  ? 326  LYS   B N    1 
ATOM   13928 C  CA   . LYS   B  2  322 ? 25.630  -35.689 0.362    1.00 61.46  ? 326  LYS   B CA   1 
ATOM   13929 C  C    . LYS   B  2  322 ? 25.404  -34.192 0.533    1.00 68.06  ? 326  LYS   B C    1 
ATOM   13930 O  O    . LYS   B  2  322 ? 25.939  -33.575 1.462    1.00 72.36  ? 326  LYS   B O    1 
ATOM   13931 C  CB   . LYS   B  2  322 ? 26.794  -35.941 -0.596   1.00 61.59  ? 326  LYS   B CB   1 
ATOM   13932 C  CG   . LYS   B  2  322 ? 27.247  -37.391 -0.686   1.00 62.97  ? 326  LYS   B CG   1 
ATOM   13933 C  CD   . LYS   B  2  322 ? 28.414  -37.544 -1.656   1.00 70.48  ? 326  LYS   B CD   1 
ATOM   13934 C  CE   . LYS   B  2  322 ? 28.803  -39.003 -1.848   1.00 83.02  ? 326  LYS   B CE   1 
ATOM   13935 N  NZ   . LYS   B  2  322 ? 29.950  -39.161 -2.788   1.00 92.28  ? 326  LYS   B NZ   1 
ATOM   13936 H  H    . LYS   B  2  322 ? 24.505  -36.745 -0.882   1.00 66.22  ? 326  LYS   B H    1 
ATOM   13937 H  HA   . LYS   B  2  322 ? 25.863  -36.067 1.225    1.00 73.74  ? 326  LYS   B HA   1 
ATOM   13938 H  HB2  . LYS   B  2  322 ? 26.525  -35.664 -1.486   1.00 73.89  ? 326  LYS   B HB2  1 
ATOM   13939 H  HB3  . LYS   B  2  322 ? 27.554  -35.416 -0.301   1.00 73.89  ? 326  LYS   B HB3  1 
ATOM   13940 H  HG2  . LYS   B  2  322 ? 27.534  -37.694 0.190    1.00 75.54  ? 326  LYS   B HG2  1 
ATOM   13941 H  HG3  . LYS   B  2  322 ? 26.512  -37.940 -1.001   1.00 75.54  ? 326  LYS   B HG3  1 
ATOM   13942 H  HD2  . LYS   B  2  322 ? 28.161  -37.181 -2.519   1.00 84.55  ? 326  LYS   B HD2  1 
ATOM   13943 H  HD3  . LYS   B  2  322 ? 29.183  -37.068 -1.308   1.00 84.55  ? 326  LYS   B HD3  1 
ATOM   13944 H  HE2  . LYS   B  2  322 ? 29.061  -39.380 -0.992   1.00 99.60  ? 326  LYS   B HE2  1 
ATOM   13945 H  HE3  . LYS   B  2  322 ? 28.047  -39.490 -2.211   1.00 99.60  ? 326  LYS   B HE3  1 
ATOM   13946 H  HZ1  . LYS   B  2  322 ? 30.150  -40.023 -2.882   1.00 110.71 ? 326  LYS   B HZ1  1 
ATOM   13947 H  HZ2  . LYS   B  2  322 ? 29.740  -38.824 -3.584   1.00 110.71 ? 326  LYS   B HZ2  1 
ATOM   13948 H  HZ3  . LYS   B  2  322 ? 30.664  -38.732 -2.472   1.00 110.71 ? 326  LYS   B HZ3  1 
ATOM   13949 N  N    . LEU   B  2  323 ? 24.608  -33.591 -0.354   1.00 66.25  ? 327  LEU   B N    1 
ATOM   13950 C  CA   . LEU   B  2  323 ? 24.380  -32.152 -0.311   1.00 60.93  ? 327  LEU   B CA   1 
ATOM   13951 C  C    . LEU   B  2  323 ? 23.312  -31.769 0.705    1.00 60.15  ? 327  LEU   B C    1 
ATOM   13952 O  O    . LEU   B  2  323 ? 23.381  -30.683 1.291    1.00 62.61  ? 327  LEU   B O    1 
ATOM   13953 C  CB   . LEU   B  2  323 ? 23.970  -31.647 -1.696   1.00 55.09  ? 327  LEU   B CB   1 
ATOM   13954 C  CG   . LEU   B  2  323 ? 24.870  -32.054 -2.866   1.00 52.46  ? 327  LEU   B CG   1 
ATOM   13955 C  CD1  . LEU   B  2  323 ? 24.252  -31.648 -4.197   1.00 53.43  ? 327  LEU   B CD1  1 
ATOM   13956 C  CD2  . LEU   B  2  323 ? 26.251  -31.440 -2.715   1.00 55.07  ? 327  LEU   B CD2  1 
ATOM   13957 H  H    . LEU   B  2  323 ? 24.190  -33.996 -0.988   1.00 79.48  ? 327  LEU   B H    1 
ATOM   13958 H  HA   . LEU   B  2  323 ? 25.208  -31.717 -0.056   1.00 73.09  ? 327  LEU   B HA   1 
ATOM   13959 H  HB2  . LEU   B  2  323 ? 23.082  -31.987 -1.889   1.00 66.09  ? 327  LEU   B HB2  1 
ATOM   13960 H  HB3  . LEU   B  2  323 ? 23.957  -30.678 -1.671   1.00 66.09  ? 327  LEU   B HB3  1 
ATOM   13961 H  HG   . LEU   B  2  323 ? 24.963  -33.019 -2.862   1.00 62.93  ? 327  LEU   B HG   1 
ATOM   13962 H  HD11 . LEU   B  2  323 ? 24.825  -31.955 -4.917   1.00 64.09  ? 327  LEU   B HD11 1 
ATOM   13963 H  HD12 . LEU   B  2  323 ? 23.375  -32.055 -4.275   1.00 64.09  ? 327  LEU   B HD12 1 
ATOM   13964 H  HD13 . LEU   B  2  323 ? 24.173  -30.682 -4.227   1.00 64.09  ? 327  LEU   B HD13 1 
ATOM   13965 H  HD21 . LEU   B  2  323 ? 26.795  -31.696 -3.477   1.00 66.07  ? 327  LEU   B HD21 1 
ATOM   13966 H  HD22 . LEU   B  2  323 ? 26.165  -30.475 -2.679   1.00 66.07  ? 327  LEU   B HD22 1 
ATOM   13967 H  HD23 . LEU   B  2  323 ? 26.654  -31.767 -1.896   1.00 66.07  ? 327  LEU   B HD23 1 
ATOM   13968 N  N    . ILE   B  2  324 ? 22.331  -32.637 0.929    1.00 58.73  ? 328  ILE   B N    1 
ATOM   13969 C  CA   . ILE   B  2  324 ? 21.171  -32.319 1.755    1.00 59.51  ? 328  ILE   B CA   1 
ATOM   13970 C  C    . ILE   B  2  324 ? 21.511  -32.662 3.203    1.00 66.63  ? 328  ILE   B C    1 
ATOM   13971 O  O    . ILE   B  2  324 ? 21.829  -33.827 3.489    1.00 74.64  ? 328  ILE   B O    1 
ATOM   13972 C  CB   . ILE   B  2  324 ? 19.928  -33.087 1.288    1.00 55.36  ? 328  ILE   B CB   1 
ATOM   13973 C  CG1  . ILE   B  2  324 ? 19.668  -32.816 -0.197   1.00 51.01  ? 328  ILE   B CG1  1 
ATOM   13974 C  CG2  . ILE   B  2  324 ? 18.712  -32.692 2.118    1.00 56.78  ? 328  ILE   B CG2  1 
ATOM   13975 C  CD1  . ILE   B  2  324 ? 18.605  -33.697 -0.808   1.00 47.45  ? 328  ILE   B CD1  1 
ATOM   13976 H  H    . ILE   B  2  324 ? 22.315  -33.434 0.606    1.00 70.46  ? 328  ILE   B H    1 
ATOM   13977 H  HA   . ILE   B  2  324 ? 20.985  -31.368 1.700    1.00 71.39  ? 328  ILE   B HA   1 
ATOM   13978 H  HB   . ILE   B  2  324 ? 20.091  -34.036 1.409    1.00 66.41  ? 328  ILE   B HB   1 
ATOM   13979 H  HG12 . ILE   B  2  324 ? 19.381  -31.895 -0.298   1.00 61.19  ? 328  ILE   B HG12 1 
ATOM   13980 H  HG13 . ILE   B  2  324 ? 20.491  -32.963 -0.689   1.00 61.19  ? 328  ILE   B HG13 1 
ATOM   13981 H  HG21 . ILE   B  2  324 ? 17.941  -33.189 1.805    1.00 68.12  ? 328  ILE   B HG21 1 
ATOM   13982 H  HG22 . ILE   B  2  324 ? 18.884  -32.902 3.050    1.00 68.12  ? 328  ILE   B HG22 1 
ATOM   13983 H  HG23 . ILE   B  2  324 ? 18.556  -31.740 2.017    1.00 68.12  ? 328  ILE   B HG23 1 
ATOM   13984 H  HD11 . ILE   B  2  324 ? 18.556  -33.518 -1.760   1.00 56.92  ? 328  ILE   B HD11 1 
ATOM   13985 H  HD12 . ILE   B  2  324 ? 18.840  -34.626 -0.658   1.00 56.92  ? 328  ILE   B HD12 1 
ATOM   13986 H  HD13 . ILE   B  2  324 ? 17.753  -33.499 -0.389   1.00 56.92  ? 328  ILE   B HD13 1 
ATOM   13987 N  N    . PRO   B  2  325 ? 21.455  -31.707 4.132    1.00 64.99  ? 329  PRO   B N    1 
ATOM   13988 C  CA   . PRO   B  2  325 ? 21.768  -32.031 5.530    1.00 62.05  ? 329  PRO   B CA   1 
ATOM   13989 C  C    . PRO   B  2  325 ? 20.802  -33.065 6.088    1.00 59.35  ? 329  PRO   B C    1 
ATOM   13990 O  O    . PRO   B  2  325 ? 19.583  -32.943 5.946    1.00 58.38  ? 329  PRO   B O    1 
ATOM   13991 C  CB   . PRO   B  2  325 ? 21.630  -30.683 6.251    1.00 59.49  ? 329  PRO   B CB   1 
ATOM   13992 C  CG   . PRO   B  2  325 ? 21.713  -29.650 5.184    1.00 59.84  ? 329  PRO   B CG   1 
ATOM   13993 C  CD   . PRO   B  2  325 ? 21.131  -30.279 3.959    1.00 60.68  ? 329  PRO   B CD   1 
ATOM   13994 H  HA   . PRO   B  2  325 ? 22.679  -32.355 5.609    1.00 74.44  ? 329  PRO   B HA   1 
ATOM   13995 H  HB2  . PRO   B  2  325 ? 20.775  -30.641 6.706    1.00 71.36  ? 329  PRO   B HB2  1 
ATOM   13996 H  HB3  . PRO   B  2  325 ? 22.352  -30.578 6.890    1.00 71.36  ? 329  PRO   B HB3  1 
ATOM   13997 H  HG2  . PRO   B  2  325 ? 21.202  -28.869 5.445    1.00 71.79  ? 329  PRO   B HG2  1 
ATOM   13998 H  HG3  . PRO   B  2  325 ? 22.640  -29.406 5.036    1.00 71.79  ? 329  PRO   B HG3  1 
ATOM   13999 H  HD2  . PRO   B  2  325 ? 20.171  -30.145 3.924    1.00 72.80  ? 329  PRO   B HD2  1 
ATOM   14000 H  HD3  . PRO   B  2  325 ? 21.545  -29.925 3.157    1.00 72.80  ? 329  PRO   B HD3  1 
ATOM   14001 N  N    . GLY   B  2  326 ? 21.359  -34.091 6.729    1.00 59.49  ? 330  GLY   B N    1 
ATOM   14002 C  CA   . GLY   B  2  326 ? 20.567  -35.107 7.389    1.00 61.24  ? 330  GLY   B CA   1 
ATOM   14003 C  C    . GLY   B  2  326 ? 19.944  -36.142 6.479    1.00 59.13  ? 330  GLY   B C    1 
ATOM   14004 O  O    . GLY   B  2  326 ? 19.328  -37.091 6.982    1.00 61.75  ? 330  GLY   B O    1 
ATOM   14005 H  H    . GLY   B  2  326 ? 22.207  -34.216 6.793    1.00 71.36  ? 330  GLY   B H    1 
ATOM   14006 H  HA2  . GLY   B  2  326 ? 21.133  -35.576 8.021    1.00 73.47  ? 330  GLY   B HA2  1 
ATOM   14007 H  HA3  . GLY   B  2  326 ? 19.847  -34.670 7.871    1.00 73.47  ? 330  GLY   B HA3  1 
ATOM   14008 N  N    . ALA   B  2  327 ? 20.078  -36.000 5.163    1.00 56.88  ? 331  ALA   B N    1 
ATOM   14009 C  CA   . ALA   B  2  327 ? 19.482  -36.958 4.243    1.00 58.38  ? 331  ALA   B CA   1 
ATOM   14010 C  C    . ALA   B  2  327 ? 20.254  -38.273 4.248    1.00 60.60  ? 331  ALA   B C    1 
ATOM   14011 O  O    . ALA   B  2  327 ? 21.475  -38.307 4.424    1.00 63.74  ? 331  ALA   B O    1 
ATOM   14012 C  CB   . ALA   B  2  327 ? 19.444  -36.383 2.827    1.00 59.17  ? 331  ALA   B CB   1 
ATOM   14013 H  H    . ALA   B  2  327 ? 20.507  -35.360 4.781    1.00 68.24  ? 331  ALA   B H    1 
ATOM   14014 H  HA   . ALA   B  2  327 ? 18.572  -37.142 4.522    1.00 70.04  ? 331  ALA   B HA   1 
ATOM   14015 H  HB1  . ALA   B  2  327 ? 19.048  -37.038 2.231    1.00 70.99  ? 331  ALA   B HB1  1 
ATOM   14016 H  HB2  . ALA   B  2  327 ? 18.911  -35.572 2.829    1.00 70.99  ? 331  ALA   B HB2  1 
ATOM   14017 H  HB3  . ALA   B  2  327 ? 20.350  -36.182 2.543    1.00 70.99  ? 331  ALA   B HB3  1 
ATOM   14018 N  N    . THR   B  2  328 ? 19.521  -39.369 4.053    1.00 61.45  ? 332  THR   B N    1 
ATOM   14019 C  CA   . THR   B  2  328 ? 20.107  -40.697 3.952    1.00 62.44  ? 332  THR   B CA   1 
ATOM   14020 C  C    . THR   B  2  328 ? 19.436  -41.442 2.806    1.00 55.97  ? 332  THR   B C    1 
ATOM   14021 O  O    . THR   B  2  328 ? 18.429  -40.995 2.250    1.00 51.24  ? 332  THR   B O    1 
ATOM   14022 C  CB   . THR   B  2  328 ? 19.964  -41.486 5.261    1.00 68.30  ? 332  THR   B CB   1 
ATOM   14023 O  OG1  . THR   B  2  328 ? 18.576  -41.639 5.583    1.00 70.12  ? 332  THR   B OG1  1 
ATOM   14024 C  CG2  . THR   B  2  328 ? 20.671  -40.769 6.401    1.00 72.56  ? 332  THR   B CG2  1 
ATOM   14025 H  H    . THR   B  2  328 ? 18.665  -39.365 3.975    1.00 73.71  ? 332  THR   B H    1 
ATOM   14026 H  HA   . THR   B  2  328 ? 21.053  -40.613 3.756    1.00 74.91  ? 332  THR   B HA   1 
ATOM   14027 H  HB   . THR   B  2  328 ? 20.369  -42.361 5.154    1.00 81.94  ? 332  THR   B HB   1 
ATOM   14028 H  HG1  . THR   B  2  328 ? 18.493  -42.066 6.302    1.00 84.12  ? 332  THR   B HG1  1 
ATOM   14029 H  HG21 . THR   B  2  328 ? 20.578  -41.278 7.222    1.00 87.05  ? 332  THR   B HG21 1 
ATOM   14030 H  HG22 . THR   B  2  328 ? 21.614  -40.671 6.197    1.00 87.05  ? 332  THR   B HG22 1 
ATOM   14031 H  HG23 . THR   B  2  328 ? 20.284  -39.889 6.531    1.00 87.05  ? 332  THR   B HG23 1 
ATOM   14032 N  N    . VAL   B  2  329 ? 20.004  -42.594 2.456    1.00 55.98  ? 333  VAL   B N    1 
ATOM   14033 C  CA   . VAL   B  2  329 ? 19.542  -43.391 1.326    1.00 55.71  ? 333  VAL   B CA   1 
ATOM   14034 C  C    . VAL   B  2  329 ? 19.406  -44.841 1.765    1.00 55.30  ? 333  VAL   B C    1 
ATOM   14035 O  O    . VAL   B  2  329 ? 20.261  -45.365 2.488    1.00 54.17  ? 333  VAL   B O    1 
ATOM   14036 C  CB   . VAL   B  2  329 ? 20.502  -43.280 0.122    1.00 58.28  ? 333  VAL   B CB   1 
ATOM   14037 C  CG1  . VAL   B  2  329 ? 20.039  -44.172 -1.023   1.00 54.42  ? 333  VAL   B CG1  1 
ATOM   14038 C  CG2  . VAL   B  2  329 ? 20.611  -41.837 -0.337   1.00 59.39  ? 333  VAL   B CG2  1 
ATOM   14039 H  H    . VAL   B  2  329 ? 20.674  -42.941 2.868    1.00 67.15  ? 333  VAL   B H    1 
ATOM   14040 H  HA   . VAL   B  2  329 ? 18.666  -43.074 1.054    1.00 66.83  ? 333  VAL   B HA   1 
ATOM   14041 H  HB   . VAL   B  2  329 ? 21.383  -43.580 0.398    1.00 69.92  ? 333  VAL   B HB   1 
ATOM   14042 H  HG11 . VAL   B  2  329 ? 20.599  -44.008 -1.798   1.00 65.29  ? 333  VAL   B HG11 1 
ATOM   14043 H  HG12 . VAL   B  2  329 ? 20.113  -45.100 -0.751   1.00 65.29  ? 333  VAL   B HG12 1 
ATOM   14044 H  HG13 . VAL   B  2  329 ? 19.115  -43.962 -1.233   1.00 65.29  ? 333  VAL   B HG13 1 
ATOM   14045 H  HG21 . VAL   B  2  329 ? 21.119  -41.805 -1.163   1.00 71.25  ? 333  VAL   B HG21 1 
ATOM   14046 H  HG22 . VAL   B  2  329 ? 19.719  -41.484 -0.484   1.00 71.25  ? 333  VAL   B HG22 1 
ATOM   14047 H  HG23 . VAL   B  2  329 ? 21.062  -41.320 0.349    1.00 71.25  ? 333  VAL   B HG23 1 
ATOM   14048 N  N    . GLY   B  2  330 ? 18.337  -45.483 1.325    1.00 56.20  ? 334  GLY   B N    1 
ATOM   14049 C  CA   . GLY   B  2  330 ? 18.132  -46.898 1.589    1.00 55.58  ? 334  GLY   B CA   1 
ATOM   14050 C  C    . GLY   B  2  330 ? 17.842  -47.642 0.306    1.00 57.04  ? 334  GLY   B C    1 
ATOM   14051 O  O    . GLY   B  2  330 ? 17.162  -47.129 -0.582   1.00 52.42  ? 334  GLY   B O    1 
ATOM   14052 H  H    . GLY   B  2  330 ? 17.708  -45.118 0.866    1.00 67.42  ? 334  GLY   B H    1 
ATOM   14053 H  HA2  . GLY   B  2  330 ? 18.928  -47.275 1.996    1.00 66.68  ? 334  GLY   B HA2  1 
ATOM   14054 H  HA3  . GLY   B  2  330 ? 17.383  -47.014 2.195    1.00 66.68  ? 334  GLY   B HA3  1 
ATOM   14055 N  N    . LEU   B  2  331 ? 18.369  -48.861 0.215    1.00 61.98  ? 335  LEU   B N    1 
ATOM   14056 C  CA   . LEU   B  2  331 ? 18.219  -49.671 -0.990   1.00 60.63  ? 335  LEU   B CA   1 
ATOM   14057 C  C    . LEU   B  2  331 ? 16.864  -50.367 -0.955   1.00 56.06  ? 335  LEU   B C    1 
ATOM   14058 O  O    . LEU   B  2  331 ? 16.615  -51.219 -0.097   1.00 54.29  ? 335  LEU   B O    1 
ATOM   14059 C  CB   . LEU   B  2  331 ? 19.356  -50.681 -1.101   1.00 63.99  ? 335  LEU   B CB   1 
ATOM   14060 C  CG   . LEU   B  2  331 ? 19.257  -51.663 -2.270   1.00 63.23  ? 335  LEU   B CG   1 
ATOM   14061 C  CD1  . LEU   B  2  331 ? 19.004  -50.937 -3.580   1.00 60.94  ? 335  LEU   B CD1  1 
ATOM   14062 C  CD2  . LEU   B  2  331 ? 20.526  -52.491 -2.368   1.00 65.32  ? 335  LEU   B CD2  1 
ATOM   14063 H  H    . LEU   B  2  331 ? 18.820  -49.242 0.840    1.00 74.36  ? 335  LEU   B H    1 
ATOM   14064 H  HA   . LEU   B  2  331 ? 18.249  -49.096 -1.770   1.00 72.74  ? 335  LEU   B HA   1 
ATOM   14065 H  HB2  . LEU   B  2  331 ? 20.188  -50.192 -1.204   1.00 76.77  ? 335  LEU   B HB2  1 
ATOM   14066 H  HB3  . LEU   B  2  331 ? 19.378  -51.205 -0.285   1.00 76.77  ? 335  LEU   B HB3  1 
ATOM   14067 H  HG   . LEU   B  2  331 ? 18.506  -52.256 -2.112   1.00 75.85  ? 335  LEU   B HG   1 
ATOM   14068 H  HD11 . LEU   B  2  331 ? 19.035  -51.578 -4.307   1.00 73.11  ? 335  LEU   B HD11 1 
ATOM   14069 H  HD12 . LEU   B  2  331 ? 18.129  -50.518 -3.545   1.00 73.11  ? 335  LEU   B HD12 1 
ATOM   14070 H  HD13 . LEU   B  2  331 ? 19.689  -50.262 -3.704   1.00 73.11  ? 335  LEU   B HD13 1 
ATOM   14071 H  HD21 . LEU   B  2  331 ? 20.427  -53.137 -3.085   1.00 78.36  ? 335  LEU   B HD21 1 
ATOM   14072 H  HD22 . LEU   B  2  331 ? 21.274  -51.903 -2.554   1.00 78.36  ? 335  LEU   B HD22 1 
ATOM   14073 H  HD23 . LEU   B  2  331 ? 20.669  -52.951 -1.525   1.00 78.36  ? 335  LEU   B HD23 1 
ATOM   14074 N  N    . LEU   B  2  332 ? 15.995  -50.009 -1.893   1.00 57.23  ? 336  LEU   B N    1 
ATOM   14075 C  CA   . LEU   B  2  332 ? 14.628  -50.505 -1.936   1.00 57.85  ? 336  LEU   B CA   1 
ATOM   14076 C  C    . LEU   B  2  332 ? 14.511  -51.642 -2.941   1.00 56.58  ? 336  LEU   B C    1 
ATOM   14077 O  O    . LEU   B  2  332 ? 15.067  -51.574 -4.040   1.00 56.65  ? 336  LEU   B O    1 
ATOM   14078 C  CB   . LEU   B  2  332 ? 13.668  -49.377 -2.315   1.00 59.79  ? 336  LEU   B CB   1 
ATOM   14079 C  CG   . LEU   B  2  332 ? 12.174  -49.697 -2.297   1.00 61.63  ? 336  LEU   B CG   1 
ATOM   14080 C  CD1  . LEU   B  2  332 ? 11.662  -49.787 -0.871   1.00 65.12  ? 336  LEU   B CD1  1 
ATOM   14081 C  CD2  . LEU   B  2  332 ? 11.413  -48.645 -3.085   1.00 58.98  ? 336  LEU   B CD2  1 
ATOM   14082 H  H    . LEU   B  2  332 ? 16.180  -49.466 -2.533   1.00 68.66  ? 336  LEU   B H    1 
ATOM   14083 H  HA   . LEU   B  2  332 ? 14.378  -50.848 -1.064   1.00 69.40  ? 336  LEU   B HA   1 
ATOM   14084 H  HB2  . LEU   B  2  332 ? 13.807  -48.646 -1.694   1.00 71.73  ? 336  LEU   B HB2  1 
ATOM   14085 H  HB3  . LEU   B  2  332 ? 13.884  -49.093 -3.217   1.00 71.73  ? 336  LEU   B HB3  1 
ATOM   14086 H  HG   . LEU   B  2  332 ? 12.021  -50.560 -2.714   1.00 73.94  ? 336  LEU   B HG   1 
ATOM   14087 H  HD11 . LEU   B  2  332 ? 10.700  -49.910 -0.888   1.00 78.12  ? 336  LEU   B HD11 1 
ATOM   14088 H  HD12 . LEU   B  2  332 ? 12.084  -50.541 -0.430   1.00 78.12  ? 336  LEU   B HD12 1 
ATOM   14089 H  HD13 . LEU   B  2  332 ? 11.881  -48.965 -0.404   1.00 78.12  ? 336  LEU   B HD13 1 
ATOM   14090 H  HD21 . LEU   B  2  332 ? 10.463  -48.839 -3.035   1.00 70.76  ? 336  LEU   B HD21 1 
ATOM   14091 H  HD22 . LEU   B  2  332 ? 11.593  -47.772 -2.703   1.00 70.76  ? 336  LEU   B HD22 1 
ATOM   14092 H  HD23 . LEU   B  2  332 ? 11.707  -48.669 -4.009   1.00 70.76  ? 336  LEU   B HD23 1 
ATOM   14093 N  N    . GLN   B  2  333 ? 13.784  -52.688 -2.558   1.00 57.17  ? 337  GLN   B N    1 
ATOM   14094 C  CA   . GLN   B  2  333 ? 13.507  -53.770 -3.488   1.00 56.72  ? 337  GLN   B CA   1 
ATOM   14095 C  C    . GLN   B  2  333 ? 12.530  -53.301 -4.563   1.00 54.92  ? 337  GLN   B C    1 
ATOM   14096 O  O    . GLN   B  2  333 ? 11.841  -52.287 -4.421   1.00 57.12  ? 337  GLN   B O    1 
ATOM   14097 C  CB   . GLN   B  2  333 ? 12.943  -54.983 -2.750   1.00 60.49  ? 337  GLN   B CB   1 
ATOM   14098 C  CG   . GLN   B  2  333 ? 13.956  -55.666 -1.844   1.00 65.60  ? 337  GLN   B CG   1 
ATOM   14099 C  CD   . GLN   B  2  333 ? 13.366  -56.826 -1.066   1.00 71.17  ? 337  GLN   B CD   1 
ATOM   14100 O  OE1  . GLN   B  2  333 ? 12.267  -57.295 -1.363   1.00 76.52  ? 337  GLN   B OE1  1 
ATOM   14101 N  NE2  . GLN   B  2  333 ? 14.097  -57.294 -0.061   1.00 72.16  ? 337  GLN   B NE2  1 
ATOM   14102 H  H    . GLN   B  2  333 ? 13.445  -52.791 -1.775   1.00 68.59  ? 337  GLN   B H    1 
ATOM   14103 H  HA   . GLN   B  2  333 ? 14.329  -54.046 -3.923   1.00 68.04  ? 337  GLN   B HA   1 
ATOM   14104 H  HB2  . GLN   B  2  333 ? 12.198  -54.697 -2.200   1.00 72.56  ? 337  GLN   B HB2  1 
ATOM   14105 H  HB3  . GLN   B  2  333 ? 12.642  -55.635 -3.403   1.00 72.56  ? 337  GLN   B HB3  1 
ATOM   14106 H  HG2  . GLN   B  2  333 ? 14.684  -56.008 -2.386   1.00 78.71  ? 337  GLN   B HG2  1 
ATOM   14107 H  HG3  . GLN   B  2  333 ? 14.294  -55.019 -1.205   1.00 78.71  ? 337  GLN   B HG3  1 
ATOM   14108 H  HE21 . GLN   B  2  333 ? 14.860  -56.940 0.118    1.00 86.57  ? 337  GLN   B HE21 1 
ATOM   14109 H  HE22 . GLN   B  2  333 ? 13.807  -57.952 0.412    1.00 86.57  ? 337  GLN   B HE22 1 
ATOM   14110 N  N    . LYS   B  2  334 ? 12.475  -54.063 -5.657   1.00 59.30  ? 338  LYS   B N    1 
ATOM   14111 C  CA   . LYS   B  2  334 ? 11.630  -53.683 -6.782   1.00 63.15  ? 338  LYS   B CA   1 
ATOM   14112 C  C    . LYS   B  2  334 ? 10.151  -53.680 -6.417   1.00 57.37  ? 338  LYS   B C    1 
ATOM   14113 O  O    . LYS   B  2  334 ? 9.349   -53.077 -7.137   1.00 54.51  ? 338  LYS   B O    1 
ATOM   14114 C  CB   . LYS   B  2  334 ? 11.881  -54.627 -7.961   1.00 76.73  ? 338  LYS   B CB   1 
ATOM   14115 C  CG   . LYS   B  2  334 ? 13.354  -54.778 -8.336   1.00 90.03  ? 338  LYS   B CG   1 
ATOM   14116 C  CD   . LYS   B  2  334 ? 13.984  -53.444 -8.712   1.00 98.09  ? 338  LYS   B CD   1 
ATOM   14117 C  CE   . LYS   B  2  334 ? 15.477  -53.581 -8.974   1.00 103.22 ? 338  LYS   B CE   1 
ATOM   14118 N  NZ   . LYS   B  2  334 ? 15.778  -54.573 -10.040  1.00 106.95 ? 338  LYS   B NZ   1 
ATOM   14119 H  H    . LYS   B  2  334 ? 12.913  -54.794 -5.769   1.00 71.14  ? 338  LYS   B H    1 
ATOM   14120 H  HA   . LYS   B  2  334 ? 11.864  -52.784 -7.062   1.00 75.76  ? 338  LYS   B HA   1 
ATOM   14121 H  HB2  . LYS   B  2  334 ? 11.544  -55.507 -7.731   1.00 92.06  ? 338  LYS   B HB2  1 
ATOM   14122 H  HB3  . LYS   B  2  334 ? 11.413  -54.285 -8.738   1.00 92.06  ? 338  LYS   B HB3  1 
ATOM   14123 H  HG2  . LYS   B  2  334 ? 13.841  -55.141 -7.580   1.00 108.01 ? 338  LYS   B HG2  1 
ATOM   14124 H  HG3  . LYS   B  2  334 ? 13.430  -55.375 -9.097   1.00 108.01 ? 338  LYS   B HG3  1 
ATOM   14125 H  HD2  . LYS   B  2  334 ? 13.564  -53.107 -9.519   1.00 117.69 ? 338  LYS   B HD2  1 
ATOM   14126 H  HD3  . LYS   B  2  334 ? 13.860  -52.814 -7.985   1.00 117.69 ? 338  LYS   B HD3  1 
ATOM   14127 H  HE2  . LYS   B  2  334 ? 15.830  -52.722 -9.253   1.00 123.84 ? 338  LYS   B HE2  1 
ATOM   14128 H  HE3  . LYS   B  2  334 ? 15.916  -53.872 -8.159   1.00 123.84 ? 338  LYS   B HE3  1 
ATOM   14129 H  HZ1  . LYS   B  2  334 ? 16.639  -54.532 -10.260  1.00 128.32 ? 338  LYS   B HZ1  1 
ATOM   14130 H  HZ2  . LYS   B  2  334 ? 15.592  -55.395 -9.753   1.00 128.32 ? 338  LYS   B HZ2  1 
ATOM   14131 H  HZ3  . LYS   B  2  334 ? 15.287  -54.402 -10.763  1.00 128.32 ? 338  LYS   B HZ3  1 
ATOM   14132 N  N    . ASP   B  2  335 ? 9.773   -54.333 -5.317   1.00 59.34  ? 339  ASP   B N    1 
ATOM   14133 C  CA   . ASP   B  2  335 ? 8.384   -54.382 -4.875   1.00 62.02  ? 339  ASP   B CA   1 
ATOM   14134 C  C    . ASP   B  2  335 ? 8.182   -53.751 -3.503   1.00 62.09  ? 339  ASP   B C    1 
ATOM   14135 O  O    . ASP   B  2  335 ? 7.121   -53.938 -2.897   1.00 64.68  ? 339  ASP   B O    1 
ATOM   14136 C  CB   . ASP   B  2  335 ? 7.887   -55.831 -4.857   1.00 62.73  ? 339  ASP   B CB   1 
ATOM   14137 C  CG   . ASP   B  2  335 ? 8.702   -56.713 -3.940   1.00 60.85  ? 339  ASP   B CG   1 
ATOM   14138 O  OD1  . ASP   B  2  335 ? 9.622   -56.195 -3.272   1.00 57.19  ? 339  ASP   B OD1  1 
ATOM   14139 O  OD2  . ASP   B  2  335 ? 8.422   -57.928 -3.889   1.00 63.42  ? 339  ASP   B OD2  1 
ATOM   14140 H  H    . ASP   B  2  335 ? 10.313  -54.761 -4.803   1.00 71.18  ? 339  ASP   B H    1 
ATOM   14141 H  HA   . ASP   B  2  335 ? 7.844   -53.885 -5.509   1.00 74.40  ? 339  ASP   B HA   1 
ATOM   14142 H  HB2  . ASP   B  2  335 ? 6.967   -55.846 -4.551   1.00 75.26  ? 339  ASP   B HB2  1 
ATOM   14143 H  HB3  . ASP   B  2  335 ? 7.944   -56.196 -5.754   1.00 75.26  ? 339  ASP   B HB3  1 
ATOM   14144 N  N    . SER   B  2  336 ? 9.168   -53.011 -2.998   1.00 58.32  ? 340  SER   B N    1 
ATOM   14145 C  CA   . SER   B  2  336 ? 9.108   -52.385 -1.680   1.00 58.84  ? 340  SER   B CA   1 
ATOM   14146 C  C    . SER   B  2  336 ? 8.961   -53.409 -0.560   1.00 61.96  ? 340  SER   B C    1 
ATOM   14147 O  O    . SER   B  2  336 ? 8.512   -53.071 0.539    1.00 63.18  ? 340  SER   B O    1 
ATOM   14148 C  CB   . SER   B  2  336 ? 7.965   -51.365 -1.601   1.00 57.35  ? 340  SER   B CB   1 
ATOM   14149 O  OG   . SER   B  2  336 ? 8.130   -50.336 -2.560   1.00 55.88  ? 340  SER   B OG   1 
ATOM   14150 H  H    . SER   B  2  336 ? 9.904   -52.853 -3.414   1.00 69.96  ? 340  SER   B H    1 
ATOM   14151 H  HA   . SER   B  2  336 ? 9.943   -51.914 -1.536   1.00 70.59  ? 340  SER   B HA   1 
ATOM   14152 H  HB2  . SER   B  2  336 ? 7.126   -51.820 -1.770   1.00 68.81  ? 340  SER   B HB2  1 
ATOM   14153 H  HB3  . SER   B  2  336 ? 7.957   -50.970 -0.715   1.00 68.81  ? 340  SER   B HB3  1 
ATOM   14154 H  HG   . SER   B  2  336 ? 8.099   -50.658 -3.335   1.00 67.04  ? 340  SER   B HG   1 
ATOM   14155 N  N    . GLY   B  2  337 ? 9.336   -54.663 -0.817   1.00 61.98  ? 341  GLY   B N    1 
ATOM   14156 C  CA   . GLY   B  2  337 ? 9.191   -55.700 0.188    1.00 61.57  ? 341  GLY   B CA   1 
ATOM   14157 C  C    . GLY   B  2  337 ? 9.951   -55.431 1.469    1.00 59.77  ? 341  GLY   B C    1 
ATOM   14158 O  O    . GLY   B  2  337 ? 9.586   -55.970 2.519    1.00 59.77  ? 341  GLY   B O    1 
ATOM   14159 H  H    . GLY   B  2  337 ? 9.675   -54.932 -1.561   1.00 74.36  ? 341  GLY   B H    1 
ATOM   14160 H  HA2  . GLY   B  2  337 ? 8.251   -55.790 0.411    1.00 73.86  ? 341  GLY   B HA2  1 
ATOM   14161 H  HA3  . GLY   B  2  337 ? 9.510   -56.539 -0.179   1.00 73.86  ? 341  GLY   B HA3  1 
ATOM   14162 N  N    . ASN   B  2  338 ? 10.998  -54.605 1.412    1.00 60.63  ? 342  ASN   B N    1 
ATOM   14163 C  CA   . ASN   B  2  338 ? 11.866  -54.352 2.555    1.00 62.89  ? 342  ASN   B CA   1 
ATOM   14164 C  C    . ASN   B  2  338 ? 11.761  -52.920 3.070    1.00 61.81  ? 342  ASN   B C    1 
ATOM   14165 O  O    . ASN   B  2  338 ? 12.660  -52.455 3.778    1.00 63.61  ? 342  ASN   B O    1 
ATOM   14166 C  CB   . ASN   B  2  338 ? 13.317  -54.660 2.185    1.00 65.51  ? 342  ASN   B CB   1 
ATOM   14167 C  CG   . ASN   B  2  338 ? 13.850  -53.732 1.108    1.00 68.21  ? 342  ASN   B CG   1 
ATOM   14168 O  OD1  . ASN   B  2  338 ? 13.116  -53.316 0.210    1.00 66.20  ? 342  ASN   B OD1  1 
ATOM   14169 N  ND2  . ASN   B  2  338 ? 15.133  -53.401 1.194    1.00 70.20  ? 342  ASN   B ND2  1 
ATOM   14170 H  H    . ASN   B  2  338 ? 11.227  -54.171 0.706    1.00 72.74  ? 342  ASN   B H    1 
ATOM   14171 H  HA   . ASN   B  2  338 ? 11.594  -54.942 3.276    1.00 75.45  ? 342  ASN   B HA   1 
ATOM   14172 H  HB2  . ASN   B  2  338 ? 13.874  -54.559 2.973    1.00 78.60  ? 342  ASN   B HB2  1 
ATOM   14173 H  HB3  . ASN   B  2  338 ? 13.373  -55.570 1.854    1.00 78.60  ? 342  ASN   B HB3  1 
ATOM   14174 H  HD21 . ASN   B  2  338 ? 15.482  -52.878 0.608    1.00 84.22  ? 342  ASN   B HD21 1 
ATOM   14175 H  HD22 . ASN   B  2  338 ? 15.614  -53.709 1.837    1.00 84.22  ? 342  ASN   B HD22 1 
ATOM   14176 N  N    . ILE   B  2  339 ? 10.683  -52.209 2.730    1.00 64.92  ? 343  ILE   B N    1 
ATOM   14177 C  CA   . ILE   B  2  339 ? 10.584  -50.800 3.106    1.00 64.20  ? 343  ILE   B CA   1 
ATOM   14178 C  C    . ILE   B  2  339 ? 10.526  -50.653 4.621    1.00 61.32  ? 343  ILE   B C    1 
ATOM   14179 O  O    . ILE   B  2  339 ? 11.065  -49.692 5.185    1.00 59.50  ? 343  ILE   B O    1 
ATOM   14180 C  CB   . ILE   B  2  339 ? 9.368   -50.143 2.424    1.00 65.17  ? 343  ILE   B CB   1 
ATOM   14181 C  CG1  . ILE   B  2  339 ? 9.298   -48.651 2.769    1.00 61.95  ? 343  ILE   B CG1  1 
ATOM   14182 C  CG2  . ILE   B  2  339 ? 8.071   -50.833 2.837    1.00 67.68  ? 343  ILE   B CG2  1 
ATOM   14183 C  CD1  . ILE   B  2  339 ? 10.551  -47.862 2.408    1.00 55.92  ? 343  ILE   B CD1  1 
ATOM   14184 H  H    . ILE   B  2  339 ? 10.010  -52.513 2.291    1.00 77.89  ? 343  ILE   B H    1 
ATOM   14185 H  HA   . ILE   B  2  339 ? 11.382  -50.345 2.793    1.00 77.02  ? 343  ILE   B HA   1 
ATOM   14186 H  HB   . ILE   B  2  339 ? 9.480   -50.241 1.466    1.00 78.18  ? 343  ILE   B HB   1 
ATOM   14187 H  HG12 . ILE   B  2  339 ? 8.554   -48.256 2.288    1.00 74.32  ? 343  ILE   B HG12 1 
ATOM   14188 H  HG13 . ILE   B  2  339 ? 9.161   -48.560 3.725    1.00 74.32  ? 343  ILE   B HG13 1 
ATOM   14189 H  HG21 . ILE   B  2  339 ? 7.330   -50.420 2.367    1.00 81.20  ? 343  ILE   B HG21 1 
ATOM   14190 H  HG22 . ILE   B  2  339 ? 8.126   -51.774 2.606    1.00 81.20  ? 343  ILE   B HG22 1 
ATOM   14191 H  HG23 . ILE   B  2  339 ? 7.951   -50.735 3.794    1.00 81.20  ? 343  ILE   B HG23 1 
ATOM   14192 H  HD11 . ILE   B  2  339 ? 10.388  -46.920 2.570    1.00 67.09  ? 343  ILE   B HD11 1 
ATOM   14193 H  HD12 . ILE   B  2  339 ? 11.288  -48.170 2.958    1.00 67.09  ? 343  ILE   B HD12 1 
ATOM   14194 H  HD13 . ILE   B  2  339 ? 10.755  -48.006 1.470    1.00 67.09  ? 343  ILE   B HD13 1 
ATOM   14195 N  N    . LEU   B  2  340 ? 9.875   -51.596 5.307    1.00 62.00  ? 344  LEU   B N    1 
ATOM   14196 C  CA   . LEU   B  2  340 ? 9.818   -51.528 6.763    1.00 63.29  ? 344  LEU   B CA   1 
ATOM   14197 C  C    . LEU   B  2  340 ? 11.215  -51.586 7.364    1.00 64.51  ? 344  LEU   B C    1 
ATOM   14198 O  O    . LEU   B  2  340 ? 11.543  -50.813 8.272    1.00 66.37  ? 344  LEU   B O    1 
ATOM   14199 C  CB   . LEU   B  2  340 ? 8.953   -52.661 7.315    1.00 65.94  ? 344  LEU   B CB   1 
ATOM   14200 C  CG   . LEU   B  2  340 ? 8.926   -52.816 8.840    1.00 70.34  ? 344  LEU   B CG   1 
ATOM   14201 C  CD1  . LEU   B  2  340 ? 8.473   -51.532 9.516    1.00 72.84  ? 344  LEU   B CD1  1 
ATOM   14202 C  CD2  . LEU   B  2  340 ? 8.025   -53.974 9.244    1.00 73.38  ? 344  LEU   B CD2  1 
ATOM   14203 H  H    . LEU   B  2  340 ? 9.468   -52.269 4.959    1.00 74.38  ? 344  LEU   B H    1 
ATOM   14204 H  HA   . LEU   B  2  340 ? 9.408   -50.687 7.021    1.00 75.93  ? 344  LEU   B HA   1 
ATOM   14205 H  HB2  . LEU   B  2  340 ? 8.039   -52.509 7.027    1.00 79.10  ? 344  LEU   B HB2  1 
ATOM   14206 H  HB3  . LEU   B  2  340 ? 9.281   -53.497 6.948    1.00 79.10  ? 344  LEU   B HB3  1 
ATOM   14207 H  HG   . LEU   B  2  340 ? 9.827   -53.008 9.143    1.00 84.38  ? 344  LEU   B HG   1 
ATOM   14208 H  HD11 . LEU   B  2  340 ? 8.427   -51.679 10.474   1.00 87.39  ? 344  LEU   B HD11 1 
ATOM   14209 H  HD12 . LEU   B  2  340 ? 9.111   -50.829 9.320    1.00 87.39  ? 344  LEU   B HD12 1 
ATOM   14210 H  HD13 . LEU   B  2  340 ? 7.597   -51.288 9.177    1.00 87.39  ? 344  LEU   B HD13 1 
ATOM   14211 H  HD21 . LEU   B  2  340 ? 8.021   -54.049 10.211   1.00 88.03  ? 344  LEU   B HD21 1 
ATOM   14212 H  HD22 . LEU   B  2  340 ? 7.126   -53.802 8.922    1.00 88.03  ? 344  LEU   B HD22 1 
ATOM   14213 H  HD23 . LEU   B  2  340 ? 8.366   -54.792 8.850    1.00 88.03  ? 344  LEU   B HD23 1 
ATOM   14214 N  N    . GLN   B  2  341 ? 12.054  -52.497 6.868    1.00 64.59  ? 345  GLN   B N    1 
ATOM   14215 C  CA   . GLN   B  2  341 ? 13.406  -52.622 7.401    1.00 67.64  ? 345  GLN   B CA   1 
ATOM   14216 C  C    . GLN   B  2  341 ? 14.228  -51.369 7.123    1.00 66.12  ? 345  GLN   B C    1 
ATOM   14217 O  O    . GLN   B  2  341 ? 14.993  -50.919 7.984    1.00 64.97  ? 345  GLN   B O    1 
ATOM   14218 C  CB   . GLN   B  2  341 ? 14.087  -53.857 6.811    1.00 78.64  ? 345  GLN   B CB   1 
ATOM   14219 C  CG   . GLN   B  2  341 ? 13.395  -55.181 7.135    1.00 90.63  ? 345  GLN   B CG   1 
ATOM   14220 C  CD   . GLN   B  2  341 ? 12.276  -55.521 6.171    1.00 96.48  ? 345  GLN   B CD   1 
ATOM   14221 O  OE1  . GLN   B  2  341 ? 11.302  -54.779 6.045    1.00 94.37  ? 345  GLN   B OE1  1 
ATOM   14222 N  NE2  . GLN   B  2  341 ? 12.410  -56.651 5.482    1.00 101.70 ? 345  GLN   B NE2  1 
ATOM   14223 H  H    . GLN   B  2  341 ? 11.867  -53.046 6.232    1.00 77.49  ? 345  GLN   B H    1 
ATOM   14224 H  HA   . GLN   B  2  341 ? 13.354  -52.738 8.363    1.00 81.15  ? 345  GLN   B HA   1 
ATOM   14225 H  HB2  . GLN   B  2  341 ? 14.108  -53.767 5.846    1.00 94.34  ? 345  GLN   B HB2  1 
ATOM   14226 H  HB3  . GLN   B  2  341 ? 14.991  -53.907 7.160    1.00 94.34  ? 345  GLN   B HB3  1 
ATOM   14227 H  HG2  . GLN   B  2  341 ? 14.049  -55.896 7.097    1.00 108.74 ? 345  GLN   B HG2  1 
ATOM   14228 H  HG3  . GLN   B  2  341 ? 13.015  -55.128 8.026    1.00 108.74 ? 345  GLN   B HG3  1 
ATOM   14229 H  HE21 . GLN   B  2  341 ? 13.105  -57.144 5.598    1.00 122.02 ? 345  GLN   B HE21 1 
ATOM   14230 H  HE22 . GLN   B  2  341 ? 11.802  -56.888 4.922    1.00 122.02 ? 345  GLN   B HE22 1 
ATOM   14231 N  N    . LEU   B  2  342 ? 14.089  -50.792 5.926    1.00 66.00  ? 346  LEU   B N    1 
ATOM   14232 C  CA   . LEU   B  2  342 ? 14.796  -49.553 5.616    1.00 64.35  ? 346  LEU   B CA   1 
ATOM   14233 C  C    . LEU   B  2  342 ? 14.445  -48.458 6.616    1.00 61.46  ? 346  LEU   B C    1 
ATOM   14234 O  O    . LEU   B  2  342 ? 15.330  -47.779 7.149    1.00 60.66  ? 346  LEU   B O    1 
ATOM   14235 C  CB   . LEU   B  2  342 ? 14.458  -49.097 4.197    1.00 65.21  ? 346  LEU   B CB   1 
ATOM   14236 C  CG   . LEU   B  2  342 ? 14.928  -49.987 3.046    1.00 71.64  ? 346  LEU   B CG   1 
ATOM   14237 C  CD1  . LEU   B  2  342 ? 14.382  -49.462 1.728    1.00 70.98  ? 346  LEU   B CD1  1 
ATOM   14238 C  CD2  . LEU   B  2  342 ? 16.446  -50.065 3.002    1.00 75.13  ? 346  LEU   B CD2  1 
ATOM   14239 H  H    . LEU   B  2  342 ? 13.599  -51.095 5.288    1.00 79.18  ? 346  LEU   B H    1 
ATOM   14240 H  HA   . LEU   B  2  342 ? 15.750  -49.721 5.665    1.00 77.20  ? 346  LEU   B HA   1 
ATOM   14241 H  HB2  . LEU   B  2  342 ? 13.493  -49.032 4.127    1.00 78.24  ? 346  LEU   B HB2  1 
ATOM   14242 H  HB3  . LEU   B  2  342 ? 14.860  -48.225 4.061    1.00 78.24  ? 346  LEU   B HB3  1 
ATOM   14243 H  HG   . LEU   B  2  342 ? 14.593  -50.887 3.184    1.00 85.95  ? 346  LEU   B HG   1 
ATOM   14244 H  HD11 . LEU   B  2  342 ? 14.660  -50.055 1.012    1.00 85.16  ? 346  LEU   B HD11 1 
ATOM   14245 H  HD12 . LEU   B  2  342 ? 13.413  -49.433 1.776    1.00 85.16  ? 346  LEU   B HD12 1 
ATOM   14246 H  HD13 . LEU   B  2  342 ? 14.732  -48.570 1.573    1.00 85.16  ? 346  LEU   B HD13 1 
ATOM   14247 H  HD21 . LEU   B  2  342 ? 16.711  -50.645 2.271    1.00 90.14  ? 346  LEU   B HD21 1 
ATOM   14248 H  HD22 . LEU   B  2  342 ? 16.804  -49.174 2.864    1.00 90.14  ? 346  LEU   B HD22 1 
ATOM   14249 H  HD23 . LEU   B  2  342 ? 16.768  -50.425 3.843    1.00 90.14  ? 346  LEU   B HD23 1 
ATOM   14250 N  N    . ILE   B  2  343 ? 13.151  -48.272 6.879    1.00 60.85  ? 347  ILE   B N    1 
ATOM   14251 C  CA   . ILE   B  2  343 ? 12.714  -47.186 7.752    1.00 62.62  ? 347  ILE   B CA   1 
ATOM   14252 C  C    . ILE   B  2  343 ? 13.283  -47.369 9.153    1.00 64.05  ? 347  ILE   B C    1 
ATOM   14253 O  O    . ILE   B  2  343 ? 13.818  -46.429 9.753    1.00 63.67  ? 347  ILE   B O    1 
ATOM   14254 C  CB   . ILE   B  2  343 ? 11.176  -47.102 7.767    1.00 62.32  ? 347  ILE   B CB   1 
ATOM   14255 C  CG1  . ILE   B  2  343 ? 10.673  -46.677 6.383    1.00 61.10  ? 347  ILE   B CG1  1 
ATOM   14256 C  CG2  . ILE   B  2  343 ? 10.698  -46.140 8.849    1.00 63.41  ? 347  ILE   B CG2  1 
ATOM   14257 C  CD1  . ILE   B  2  343 ? 9.165   -46.666 6.233    1.00 61.35  ? 347  ILE   B CD1  1 
ATOM   14258 H  H    . ILE   B  2  343 ? 12.512  -48.756 6.566    1.00 73.00  ? 347  ILE   B H    1 
ATOM   14259 H  HA   . ILE   B  2  343 ? 13.056  -46.348 7.403    1.00 75.12  ? 347  ILE   B HA   1 
ATOM   14260 H  HB   . ILE   B  2  343 ? 10.812  -47.977 7.974    1.00 74.76  ? 347  ILE   B HB   1 
ATOM   14261 H  HG12 . ILE   B  2  343 ? 10.992  -45.779 6.202    1.00 73.30  ? 347  ILE   B HG12 1 
ATOM   14262 H  HG13 . ILE   B  2  343 ? 11.027  -47.294 5.724    1.00 73.30  ? 347  ILE   B HG13 1 
ATOM   14263 H  HG21 . ILE   B  2  343 ? 9.735   -46.047 8.787    1.00 76.07  ? 347  ILE   B HG21 1 
ATOM   14264 H  HG22 . ILE   B  2  343 ? 10.941  -46.496 9.718    1.00 76.07  ? 347  ILE   B HG22 1 
ATOM   14265 H  HG23 . ILE   B  2  343 ? 11.123  -45.278 8.715    1.00 76.07  ? 347  ILE   B HG23 1 
ATOM   14266 H  HD11 . ILE   B  2  343 ? 8.941   -46.463 5.312    1.00 73.60  ? 347  ILE   B HD11 1 
ATOM   14267 H  HD12 . ILE   B  2  343 ? 8.817   -47.538 6.474    1.00 73.60  ? 347  ILE   B HD12 1 
ATOM   14268 H  HD13 . ILE   B  2  343 ? 8.795   -45.988 6.821    1.00 73.60  ? 347  ILE   B HD13 1 
ATOM   14269 N  N    . ILE   B  2  344 ? 13.178  -48.585 9.695    1.00 64.29  ? 348  ILE   B N    1 
ATOM   14270 C  CA   . ILE   B  2  344 ? 13.672  -48.834 11.047   1.00 63.69  ? 348  ILE   B CA   1 
ATOM   14271 C  C    . ILE   B  2  344 ? 15.179  -48.616 11.111   1.00 61.90  ? 348  ILE   B C    1 
ATOM   14272 O  O    . ILE   B  2  344 ? 15.694  -48.024 12.067   1.00 65.06  ? 348  ILE   B O    1 
ATOM   14273 C  CB   . ILE   B  2  344 ? 13.284  -50.251 11.510   1.00 64.67  ? 348  ILE   B CB   1 
ATOM   14274 C  CG1  . ILE   B  2  344 ? 11.758  -50.401 11.563   1.00 68.50  ? 348  ILE   B CG1  1 
ATOM   14275 C  CG2  . ILE   B  2  344 ? 13.898  -50.554 12.874   1.00 60.78  ? 348  ILE   B CG2  1 
ATOM   14276 C  CD1  . ILE   B  2  344 ? 11.070  -49.505 12.583   1.00 72.27  ? 348  ILE   B CD1  1 
ATOM   14277 H  H    . ILE   B  2  344 ? 12.831  -49.269 9.308    1.00 77.12  ? 348  ILE   B H    1 
ATOM   14278 H  HA   . ILE   B  2  344 ? 13.252  -48.199 11.649   1.00 76.41  ? 348  ILE   B HA   1 
ATOM   14279 H  HB   . ILE   B  2  344 ? 13.632  -50.886 10.866   1.00 77.58  ? 348  ILE   B HB   1 
ATOM   14280 H  HG12 . ILE   B  2  344 ? 11.396  -50.183 10.690   1.00 82.18  ? 348  ILE   B HG12 1 
ATOM   14281 H  HG13 . ILE   B  2  344 ? 11.546  -51.320 11.790   1.00 82.18  ? 348  ILE   B HG13 1 
ATOM   14282 H  HG21 . ILE   B  2  344 ? 13.522  -51.382 13.213   1.00 72.91  ? 348  ILE   B HG21 1 
ATOM   14283 H  HG22 . ILE   B  2  344 ? 14.859  -50.644 12.775   1.00 72.91  ? 348  ILE   B HG22 1 
ATOM   14284 H  HG23 . ILE   B  2  344 ? 13.695  -49.826 13.481   1.00 72.91  ? 348  ILE   B HG23 1 
ATOM   14285 H  HD11 . ILE   B  2  344 ? 10.116  -49.677 12.562   1.00 86.70  ? 348  ILE   B HD11 1 
ATOM   14286 H  HD12 . ILE   B  2  344 ? 11.422  -49.703 13.465   1.00 86.70  ? 348  ILE   B HD12 1 
ATOM   14287 H  HD13 . ILE   B  2  344 ? 11.244  -48.578 12.358   1.00 86.70  ? 348  ILE   B HD13 1 
ATOM   14288 N  N    . SER   B  2  345 ? 15.910  -49.085 10.097   1.00 59.39  ? 349  SER   B N    1 
ATOM   14289 C  CA   . SER   B  2  345 ? 17.354  -48.878 10.078   1.00 59.35  ? 349  SER   B CA   1 
ATOM   14290 C  C    . SER   B  2  345 ? 17.689  -47.392 10.072   1.00 57.12  ? 349  SER   B C    1 
ATOM   14291 O  O    . SER   B  2  345 ? 18.544  -46.931 10.837   1.00 55.81  ? 349  SER   B O    1 
ATOM   14292 C  CB   . SER   B  2  345 ? 17.971  -49.569 8.861    1.00 59.14  ? 349  SER   B CB   1 
ATOM   14293 O  OG   . SER   B  2  345 ? 17.818  -50.976 8.935    1.00 66.57  ? 349  SER   B OG   1 
ATOM   14294 H  H    . SER   B  2  345 ? 15.598  -49.519 9.423    1.00 71.25  ? 349  SER   B H    1 
ATOM   14295 H  HA   . SER   B  2  345 ? 17.737  -49.276 10.875   1.00 71.20  ? 349  SER   B HA   1 
ATOM   14296 H  HB2  . SER   B  2  345 ? 17.529  -49.247 8.060    1.00 70.95  ? 349  SER   B HB2  1 
ATOM   14297 H  HB3  . SER   B  2  345 ? 18.917  -49.358 8.826    1.00 70.95  ? 349  SER   B HB3  1 
ATOM   14298 H  HG   . SER   B  2  345 ? 17.007  -51.181 8.863    1.00 79.87  ? 349  SER   B HG   1 
ATOM   14299 N  N    . ALA   B  2  346 ? 17.018  -46.623 9.212    1.00 58.04  ? 350  ALA   B N    1 
ATOM   14300 C  CA   . ALA   B  2  346 ? 17.276  -45.189 9.145    1.00 57.37  ? 350  ALA   B CA   1 
ATOM   14301 C  C    . ALA   B  2  346 ? 16.985  -44.516 10.480   1.00 59.06  ? 350  ALA   B C    1 
ATOM   14302 O  O    . ALA   B  2  346 ? 17.775  -43.695 10.958   1.00 60.46  ? 350  ALA   B O    1 
ATOM   14303 C  CB   . ALA   B  2  346 ? 16.439  -44.558 8.034    1.00 54.66  ? 350  ALA   B CB   1 
ATOM   14304 H  H    . ALA   B  2  346 ? 16.417  -46.904 8.666    1.00 69.63  ? 350  ALA   B H    1 
ATOM   14305 H  HA   . ALA   B  2  346 ? 18.213  -45.051 8.935    1.00 68.82  ? 350  ALA   B HA   1 
ATOM   14306 H  HB1  . ALA   B  2  346 ? 16.617  -43.605 8.007    1.00 65.57  ? 350  ALA   B HB1  1 
ATOM   14307 H  HB2  . ALA   B  2  346 ? 16.681  -44.964 7.187    1.00 65.57  ? 350  ALA   B HB2  1 
ATOM   14308 H  HB3  . ALA   B  2  346 ? 15.500  -44.714 8.219    1.00 65.57  ? 350  ALA   B HB3  1 
ATOM   14309 N  N    . TYR   B  2  347 ? 15.849  -44.853 11.097   1.00 60.09  ? 351  TYR   B N    1 
ATOM   14310 C  CA   . TYR   B  2  347 ? 15.508  -44.273 12.392   1.00 60.37  ? 351  TYR   B CA   1 
ATOM   14311 C  C    . TYR   B  2  347 ? 16.559  -44.622 13.438   1.00 59.94  ? 351  TYR   B C    1 
ATOM   14312 O  O    . TYR   B  2  347 ? 17.018  -43.754 14.189   1.00 61.71  ? 351  TYR   B O    1 
ATOM   14313 C  CB   . TYR   B  2  347 ? 14.127  -44.761 12.829   1.00 61.01  ? 351  TYR   B CB   1 
ATOM   14314 C  CG   . TYR   B  2  347 ? 13.702  -44.266 14.193   1.00 60.48  ? 351  TYR   B CG   1 
ATOM   14315 C  CD1  . TYR   B  2  347 ? 13.326  -42.944 14.384   1.00 61.33  ? 351  TYR   B CD1  1 
ATOM   14316 C  CD2  . TYR   B  2  347 ? 13.671  -45.121 15.287   1.00 61.00  ? 351  TYR   B CD2  1 
ATOM   14317 C  CE1  . TYR   B  2  347 ? 12.937  -42.485 15.626   1.00 63.77  ? 351  TYR   B CE1  1 
ATOM   14318 C  CE2  . TYR   B  2  347 ? 13.281  -44.671 16.534   1.00 62.75  ? 351  TYR   B CE2  1 
ATOM   14319 C  CZ   . TYR   B  2  347 ? 12.914  -43.353 16.697   1.00 64.26  ? 351  TYR   B CZ   1 
ATOM   14320 O  OH   . TYR   B  2  347 ? 12.524  -42.899 17.937   1.00 67.44  ? 351  TYR   B OH   1 
ATOM   14321 H  H    . TYR   B  2  347 ? 15.268  -45.407 10.789   1.00 72.09  ? 351  TYR   B H    1 
ATOM   14322 H  HA   . TYR   B  2  347 ? 15.476  -43.307 12.308   1.00 72.43  ? 351  TYR   B HA   1 
ATOM   14323 H  HB2  . TYR   B  2  347 ? 13.470  -44.452 12.186   1.00 73.20  ? 351  TYR   B HB2  1 
ATOM   14324 H  HB3  . TYR   B  2  347 ? 14.134  -45.731 12.857   1.00 73.20  ? 351  TYR   B HB3  1 
ATOM   14325 H  HD1  . TYR   B  2  347 ? 13.336  -42.358 13.662   1.00 73.57  ? 351  TYR   B HD1  1 
ATOM   14326 H  HD2  . TYR   B  2  347 ? 13.916  -46.011 15.179   1.00 73.18  ? 351  TYR   B HD2  1 
ATOM   14327 H  HE1  . TYR   B  2  347 ? 12.692  -41.595 15.739   1.00 76.50  ? 351  TYR   B HE1  1 
ATOM   14328 H  HE2  . TYR   B  2  347 ? 13.266  -45.254 17.259   1.00 75.28  ? 351  TYR   B HE2  1 
ATOM   14329 H  HH   . TYR   B  2  347 ? 12.369  -43.549 18.445   1.00 80.91  ? 351  TYR   B HH   1 
ATOM   14330 N  N    . GLU   B  2  348 ? 16.956  -45.894 13.498   1.00 61.37  ? 352  GLU   B N    1 
ATOM   14331 C  CA   . GLU   B  2  348 ? 17.953  -46.306 14.481   1.00 65.85  ? 352  GLU   B CA   1 
ATOM   14332 C  C    . GLU   B  2  348 ? 19.279  -45.593 14.250   1.00 66.26  ? 352  GLU   B C    1 
ATOM   14333 O  O    . GLU   B  2  348 ? 19.932  -45.159 15.206   1.00 66.47  ? 352  GLU   B O    1 
ATOM   14334 C  CB   . GLU   B  2  348 ? 18.131  -47.825 14.437   1.00 69.18  ? 352  GLU   B CB   1 
ATOM   14335 C  CG   . GLU   B  2  348 ? 16.920  -48.585 14.964   1.00 74.44  ? 352  GLU   B CG   1 
ATOM   14336 C  CD   . GLU   B  2  348 ? 17.106  -50.089 14.943   1.00 79.69  ? 352  GLU   B CD   1 
ATOM   14337 O  OE1  . GLU   B  2  348 ? 17.853  -50.588 14.075   1.00 81.91  ? 352  GLU   B OE1  1 
ATOM   14338 O  OE2  . GLU   B  2  348 ? 16.503  -50.773 15.797   1.00 81.79  ? 352  GLU   B OE2  1 
ATOM   14339 H  H    . GLU   B  2  348 ? 16.668  -46.526 12.990   1.00 73.63  ? 352  GLU   B H    1 
ATOM   14340 H  HA   . GLU   B  2  348 ? 17.641  -46.071 15.368   1.00 79.00  ? 352  GLU   B HA   1 
ATOM   14341 H  HB2  . GLU   B  2  348 ? 18.277  -48.097 13.517   1.00 82.99  ? 352  GLU   B HB2  1 
ATOM   14342 H  HB3  . GLU   B  2  348 ? 18.896  -48.067 14.980   1.00 82.99  ? 352  GLU   B HB3  1 
ATOM   14343 H  HG2  . GLU   B  2  348 ? 16.757  -48.317 15.883   1.00 89.31  ? 352  GLU   B HG2  1 
ATOM   14344 H  HG3  . GLU   B  2  348 ? 16.150  -48.371 14.415   1.00 89.31  ? 352  GLU   B HG3  1 
ATOM   14345 N  N    . GLU   B  2  349 ? 19.689  -45.450 12.987   1.00 66.88  ? 353  GLU   B N    1 
ATOM   14346 C  CA   . GLU   B  2  349 ? 20.909  -44.704 12.696   1.00 73.04  ? 353  GLU   B CA   1 
ATOM   14347 C  C    . GLU   B  2  349 ? 20.783  -43.254 13.147   1.00 69.43  ? 353  GLU   B C    1 
ATOM   14348 O  O    . GLU   B  2  349 ? 21.751  -42.663 13.640   1.00 71.51  ? 353  GLU   B O    1 
ATOM   14349 C  CB   . GLU   B  2  349 ? 21.230  -44.773 11.203   1.00 81.93  ? 353  GLU   B CB   1 
ATOM   14350 C  CG   . GLU   B  2  349 ? 22.564  -44.139 10.832   1.00 92.63  ? 353  GLU   B CG   1 
ATOM   14351 C  CD   . GLU   B  2  349 ? 22.872  -44.240 9.350    1.00 105.43 ? 353  GLU   B CD   1 
ATOM   14352 O  OE1  . GLU   B  2  349 ? 21.986  -44.675 8.585    1.00 109.15 ? 353  GLU   B OE1  1 
ATOM   14353 O  OE2  . GLU   B  2  349 ? 24.002  -43.886 8.951    1.00 111.14 ? 353  GLU   B OE2  1 
ATOM   14354 H  H    . GLU   B  2  349 ? 19.287  -45.769 12.297   1.00 80.23  ? 353  GLU   B H    1 
ATOM   14355 H  HA   . GLU   B  2  349 ? 21.646  -45.111 13.178   1.00 87.62  ? 353  GLU   B HA   1 
ATOM   14356 H  HB2  . GLU   B  2  349 ? 21.260  -45.705 10.933   1.00 98.30  ? 353  GLU   B HB2  1 
ATOM   14357 H  HB3  . GLU   B  2  349 ? 20.534  -44.308 10.712   1.00 98.30  ? 353  GLU   B HB3  1 
ATOM   14358 H  HG2  . GLU   B  2  349 ? 22.543  -43.199 11.071   1.00 111.14 ? 353  GLU   B HG2  1 
ATOM   14359 H  HG3  . GLU   B  2  349 ? 23.273  -44.588 11.318   1.00 111.14 ? 353  GLU   B HG3  1 
ATOM   14360 N  N    . LEU   B  2  350 ? 19.597  -42.663 12.986   1.00 64.91  ? 354  LEU   B N    1 
ATOM   14361 C  CA   . LEU   B  2  350 ? 19.390  -41.287 13.426   1.00 63.28  ? 354  LEU   B CA   1 
ATOM   14362 C  C    . LEU   B  2  350 ? 19.500  -41.175 14.942   1.00 65.10  ? 354  LEU   B C    1 
ATOM   14363 O  O    . LEU   B  2  350 ? 20.190  -40.289 15.460   1.00 66.19  ? 354  LEU   B O    1 
ATOM   14364 C  CB   . LEU   B  2  350 ? 18.029  -40.782 12.946   1.00 62.19  ? 354  LEU   B CB   1 
ATOM   14365 C  CG   . LEU   B  2  350 ? 17.886  -40.543 11.442   1.00 63.31  ? 354  LEU   B CG   1 
ATOM   14366 C  CD1  . LEU   B  2  350 ? 16.430  -40.287 11.095   1.00 64.63  ? 354  LEU   B CD1  1 
ATOM   14367 C  CD2  . LEU   B  2  350 ? 18.754  -39.381 10.987   1.00 62.43  ? 354  LEU   B CD2  1 
ATOM   14368 H  H    . LEU   B  2  350 ? 18.907  -43.033 12.629   1.00 77.87  ? 354  LEU   B H    1 
ATOM   14369 H  HA   . LEU   B  2  350 ? 20.075  -40.726 13.031   1.00 75.92  ? 354  LEU   B HA   1 
ATOM   14370 H  HB2  . LEU   B  2  350 ? 17.360  -41.438 13.197   1.00 74.61  ? 354  LEU   B HB2  1 
ATOM   14371 H  HB3  . LEU   B  2  350 ? 17.849  -39.938 13.388   1.00 74.61  ? 354  LEU   B HB3  1 
ATOM   14372 H  HG   . LEU   B  2  350 ? 18.185  -41.335 10.968   1.00 75.95  ? 354  LEU   B HG   1 
ATOM   14373 H  HD11 . LEU   B  2  350 ? 16.357  -40.121 10.142   1.00 77.54  ? 354  LEU   B HD11 1 
ATOM   14374 H  HD12 . LEU   B  2  350 ? 15.906  -41.066 11.336   1.00 77.54  ? 354  LEU   B HD12 1 
ATOM   14375 H  HD13 . LEU   B  2  350 ? 16.119  -39.513 11.590   1.00 77.54  ? 354  LEU   B HD13 1 
ATOM   14376 H  HD21 . LEU   B  2  350 ? 18.623  -39.243 10.035   1.00 74.90  ? 354  LEU   B HD21 1 
ATOM   14377 H  HD22 . LEU   B  2  350 ? 18.495  -38.583 11.475   1.00 74.90  ? 354  LEU   B HD22 1 
ATOM   14378 H  HD23 . LEU   B  2  350 ? 19.683  -39.592 11.166   1.00 74.90  ? 354  LEU   B HD23 1 
ATOM   14379 N  N    . ARG   B  2  351 ? 18.825  -42.066 15.673   1.00 67.31  ? 355  ARG   B N    1 
ATOM   14380 C  CA   . ARG   B  2  351 ? 18.943  -42.076 17.126   1.00 70.55  ? 355  ARG   B CA   1 
ATOM   14381 C  C    . ARG   B  2  351 ? 20.348  -42.439 17.589   1.00 71.42  ? 355  ARG   B C    1 
ATOM   14382 O  O    . ARG   B  2  351 ? 20.646  -42.294 18.779   1.00 71.88  ? 355  ARG   B O    1 
ATOM   14383 C  CB   . ARG   B  2  351 ? 17.938  -43.057 17.736   1.00 73.43  ? 355  ARG   B CB   1 
ATOM   14384 C  CG   . ARG   B  2  351 ? 16.489  -42.839 17.319   1.00 74.84  ? 355  ARG   B CG   1 
ATOM   14385 C  CD   . ARG   B  2  351 ? 15.923  -41.514 17.809   1.00 76.07  ? 355  ARG   B CD   1 
ATOM   14386 N  NE   . ARG   B  2  351 ? 16.033  -41.337 19.255   1.00 76.07  ? 355  ARG   B NE   1 
ATOM   14387 C  CZ   . ARG   B  2  351 ? 15.336  -42.025 20.155   1.00 76.87  ? 355  ARG   B CZ   1 
ATOM   14388 N  NH1  . ARG   B  2  351 ? 14.483  -42.965 19.772   1.00 83.70  ? 355  ARG   B NH1  1 
ATOM   14389 N  NH2  . ARG   B  2  351 ? 15.503  -41.780 21.447   1.00 74.85  ? 355  ARG   B NH2  1 
ATOM   14390 H  H    . ARG   B  2  351 ? 18.299  -42.666 15.352   1.00 80.75  ? 355  ARG   B H    1 
ATOM   14391 H  HA   . ARG   B  2  351 ? 18.729  -41.190 17.457   1.00 84.64  ? 355  ARG   B HA   1 
ATOM   14392 H  HB2  . ARG   B  2  351 ? 18.185  -43.956 17.468   1.00 88.10  ? 355  ARG   B HB2  1 
ATOM   14393 H  HB3  . ARG   B  2  351 ? 17.978  -42.976 18.702   1.00 88.10  ? 355  ARG   B HB3  1 
ATOM   14394 H  HG2  . ARG   B  2  351 ? 16.434  -42.848 16.350   1.00 89.79  ? 355  ARG   B HG2  1 
ATOM   14395 H  HG3  . ARG   B  2  351 ? 15.943  -43.551 17.688   1.00 89.79  ? 355  ARG   B HG3  1 
ATOM   14396 H  HD2  . ARG   B  2  351 ? 16.408  -40.789 17.383   1.00 91.27  ? 355  ARG   B HD2  1 
ATOM   14397 H  HD3  . ARG   B  2  351 ? 14.983  -41.468 17.574   1.00 91.27  ? 355  ARG   B HD3  1 
ATOM   14398 H  HE   . ARG   B  2  351 ? 16.588  -40.747 19.545   1.00 91.27  ? 355  ARG   B HE   1 
ATOM   14399 H  HH11 . ARG   B  2  351 ? 14.376  -43.134 18.935   1.00 100.42 ? 355  ARG   B HH11 1 
ATOM   14400 H  HH12 . ARG   B  2  351 ? 14.035  -43.405 20.359   1.00 100.42 ? 355  ARG   B HH12 1 
ATOM   14401 H  HH21 . ARG   B  2  351 ? 16.061  -41.177 21.702   1.00 89.80  ? 355  ARG   B HH21 1 
ATOM   14402 H  HH22 . ARG   B  2  351 ? 15.053  -42.223 22.031   1.00 89.80  ? 355  ARG   B HH22 1 
ATOM   14403 N  N    . SER   B  2  352 ? 21.206  -42.910 16.685   1.00 74.51  ? 356  SER   B N    1 
ATOM   14404 C  CA   . SER   B  2  352 ? 22.580  -43.270 17.004   1.00 78.89  ? 356  SER   B CA   1 
ATOM   14405 C  C    . SER   B  2  352 ? 23.576  -42.168 16.672   1.00 75.91  ? 356  SER   B C    1 
ATOM   14406 O  O    . SER   B  2  352 ? 24.781  -42.371 16.849   1.00 78.04  ? 356  SER   B O    1 
ATOM   14407 C  CB   . SER   B  2  352 ? 22.970  -44.549 16.256   1.00 86.46  ? 356  SER   B CB   1 
ATOM   14408 O  OG   . SER   B  2  352 ? 24.377  -44.652 16.115   1.00 97.33  ? 356  SER   B OG   1 
ATOM   14409 H  H    . SER   B  2  352 ? 21.007  -43.032 15.858   1.00 89.39  ? 356  SER   B H    1 
ATOM   14410 H  HA   . SER   B  2  352 ? 22.639  -43.445 17.956   1.00 94.64  ? 356  SER   B HA   1 
ATOM   14411 H  HB2  . SER   B  2  352 ? 22.648  -45.316 16.755   1.00 103.73 ? 356  SER   B HB2  1 
ATOM   14412 H  HB3  . SER   B  2  352 ? 22.566  -44.533 15.374   1.00 103.73 ? 356  SER   B HB3  1 
ATOM   14413 H  HG   . SER   B  2  352 ? 24.750  -44.518 16.855   1.00 116.78 ? 356  SER   B HG   1 
ATOM   14414 N  N    . GLU   B  2  353 ? 23.110  -41.015 16.197   1.00 73.48  ? 357  GLU   B N    1 
ATOM   14415 C  CA   . GLU   B  2  353 ? 23.989  -39.933 15.786   1.00 77.60  ? 357  GLU   B CA   1 
ATOM   14416 C  C    . GLU   B  2  353 ? 23.510  -38.613 16.374   1.00 75.58  ? 357  GLU   B C    1 
ATOM   14417 O  O    . GLU   B  2  353 ? 22.346  -38.455 16.751   1.00 76.65  ? 357  GLU   B O    1 
ATOM   14418 C  CB   . GLU   B  2  353 ? 24.058  -39.807 14.257   1.00 85.08  ? 357  GLU   B CB   1 
ATOM   14419 C  CG   . GLU   B  2  353 ? 24.742  -40.964 13.554   1.00 97.85  ? 357  GLU   B CG   1 
ATOM   14420 C  CD   . GLU   B  2  353 ? 24.803  -40.769 12.053   1.00 104.15 ? 357  GLU   B CD   1 
ATOM   14421 O  OE1  . GLU   B  2  353 ? 24.078  -39.892 11.537   1.00 104.09 ? 357  GLU   B OE1  1 
ATOM   14422 O  OE2  . GLU   B  2  353 ? 25.578  -41.489 11.389   1.00 108.60 ? 357  GLU   B OE2  1 
ATOM   14423 H  H    . GLU   B  2  353 ? 22.274  -40.837 16.102   1.00 88.16  ? 357  GLU   B H    1 
ATOM   14424 H  HA   . GLU   B  2  353 ? 24.878  -40.113 16.127   1.00 93.10  ? 357  GLU   B HA   1 
ATOM   14425 H  HB2  . GLU   B  2  353 ? 23.154  -39.748 13.911   1.00 102.08 ? 357  GLU   B HB2  1 
ATOM   14426 H  HB3  . GLU   B  2  353 ? 24.550  -39.000 14.036   1.00 102.08 ? 357  GLU   B HB3  1 
ATOM   14427 H  HG2  . GLU   B  2  353 ? 25.649  -41.046 13.885   1.00 117.40 ? 357  GLU   B HG2  1 
ATOM   14428 H  HG3  . GLU   B  2  353 ? 24.248  -41.780 13.732   1.00 117.40 ? 357  GLU   B HG3  1 
ATOM   14429 N  N    . VAL   B  2  354 ? 24.438  -37.661 16.439   1.00 73.31  ? 358  VAL   B N    1 
ATOM   14430 C  CA   . VAL   B  2  354 ? 24.156  -36.287 16.838   1.00 69.11  ? 358  VAL   B CA   1 
ATOM   14431 C  C    . VAL   B  2  354 ? 24.997  -35.396 15.935   1.00 63.60  ? 358  VAL   B C    1 
ATOM   14432 O  O    . VAL   B  2  354 ? 26.228  -35.382 16.050   1.00 64.39  ? 358  VAL   B O    1 
ATOM   14433 C  CB   . VAL   B  2  354 ? 24.480  -36.020 18.315   1.00 73.06  ? 358  VAL   B CB   1 
ATOM   14434 C  CG1  . VAL   B  2  354 ? 24.476  -34.523 18.612   1.00 72.31  ? 358  VAL   B CG1  1 
ATOM   14435 C  CG2  . VAL   B  2  354 ? 23.486  -36.740 19.213   1.00 75.07  ? 358  VAL   B CG2  1 
ATOM   14436 H  H    . VAL   B  2  354 ? 25.267  -37.793 16.251   1.00 87.95  ? 358  VAL   B H    1 
ATOM   14437 H  HA   . VAL   B  2  354 ? 23.217  -36.088 16.697   1.00 82.91  ? 358  VAL   B HA   1 
ATOM   14438 H  HB   . VAL   B  2  354 ? 25.369  -36.360 18.503   1.00 87.65  ? 358  VAL   B HB   1 
ATOM   14439 H  HG11 . VAL   B  2  354 ? 24.631  -34.389 19.561   1.00 86.75  ? 358  VAL   B HG11 1 
ATOM   14440 H  HG12 . VAL   B  2  354 ? 25.180  -34.097 18.099   1.00 86.75  ? 358  VAL   B HG12 1 
ATOM   14441 H  HG13 . VAL   B  2  354 ? 23.614  -34.154 18.362   1.00 86.75  ? 358  VAL   B HG13 1 
ATOM   14442 H  HG21 . VAL   B  2  354 ? 23.650  -36.484 20.134   1.00 90.07  ? 358  VAL   B HG21 1 
ATOM   14443 H  HG22 . VAL   B  2  354 ? 22.586  -36.487 18.954   1.00 90.07  ? 358  VAL   B HG22 1 
ATOM   14444 H  HG23 . VAL   B  2  354 ? 23.604  -37.697 19.110   1.00 90.07  ? 358  VAL   B HG23 1 
ATOM   14445 N  N    . GLU   B  2  355 ? 24.345  -34.662 15.039   1.00 56.85  ? 359  GLU   B N    1 
ATOM   14446 C  CA   . GLU   B  2  355 ? 25.017  -33.737 14.136   1.00 59.34  ? 359  GLU   B CA   1 
ATOM   14447 C  C    . GLU   B  2  355 ? 24.575  -32.320 14.463   1.00 60.79  ? 359  GLU   B C    1 
ATOM   14448 O  O    . GLU   B  2  355 ? 23.374  -32.048 14.558   1.00 61.69  ? 359  GLU   B O    1 
ATOM   14449 C  CB   . GLU   B  2  355 ? 24.708  -34.055 12.670   1.00 63.71  ? 359  GLU   B CB   1 
ATOM   14450 C  CG   . GLU   B  2  355 ? 25.400  -33.116 11.688   1.00 71.92  ? 359  GLU   B CG   1 
ATOM   14451 C  CD   . GLU   B  2  355 ? 25.222  -33.539 10.247   1.00 81.98  ? 359  GLU   B CD   1 
ATOM   14452 O  OE1  . GLU   B  2  355 ? 24.830  -34.701 10.010   1.00 86.92  ? 359  GLU   B OE1  1 
ATOM   14453 O  OE2  . GLU   B  2  355 ? 25.473  -32.708 9.350    1.00 86.18  ? 359  GLU   B OE2  1 
ATOM   14454 H  H    . GLU   B  2  355 ? 23.492  -34.684 14.933   1.00 68.21  ? 359  GLU   B H    1 
ATOM   14455 H  HA   . GLU   B  2  355 ? 25.976  -33.807 14.264   1.00 71.18  ? 359  GLU   B HA   1 
ATOM   14456 H  HB2  . GLU   B  2  355 ? 25.004  -34.958 12.477   1.00 76.43  ? 359  GLU   B HB2  1 
ATOM   14457 H  HB3  . GLU   B  2  355 ? 23.752  -33.981 12.529   1.00 76.43  ? 359  GLU   B HB3  1 
ATOM   14458 H  HG2  . GLU   B  2  355 ? 25.028  -32.226 11.787   1.00 86.28  ? 359  GLU   B HG2  1 
ATOM   14459 H  HG3  . GLU   B  2  355 ? 26.351  -33.102 11.881   1.00 86.28  ? 359  GLU   B HG3  1 
ATOM   14460 N  N    . LEU   B  2  356 ? 25.541  -31.424 14.631   1.00 61.88  ? 360  LEU   B N    1 
ATOM   14461 C  CA   . LEU   B  2  356 ? 25.221  -30.034 14.908   1.00 60.54  ? 360  LEU   B CA   1 
ATOM   14462 C  C    . LEU   B  2  356 ? 24.919  -29.286 13.617   1.00 59.63  ? 360  LEU   B C    1 
ATOM   14463 O  O    . LEU   B  2  356 ? 25.430  -29.613 12.542   1.00 58.14  ? 360  LEU   B O    1 
ATOM   14464 C  CB   . LEU   B  2  356 ? 26.364  -29.339 15.647   1.00 57.90  ? 360  LEU   B CB   1 
ATOM   14465 C  CG   . LEU   B  2  356 ? 26.286  -29.308 17.176   1.00 56.51  ? 360  LEU   B CG   1 
ATOM   14466 C  CD1  . LEU   B  2  356 ? 27.389  -28.422 17.730   1.00 57.20  ? 360  LEU   B CD1  1 
ATOM   14467 C  CD2  . LEU   B  2  356 ? 24.925  -28.829 17.666   1.00 56.14  ? 360  LEU   B CD2  1 
ATOM   14468 H  H    . LEU   B  2  356 ? 26.383  -31.596 14.590   1.00 74.24  ? 360  LEU   B H    1 
ATOM   14469 H  HA   . LEU   B  2  356 ? 24.436  -30.002 15.477   1.00 72.63  ? 360  LEU   B HA   1 
ATOM   14470 H  HB2  . LEU   B  2  356 ? 27.189  -29.792 15.415   1.00 69.47  ? 360  LEU   B HB2  1 
ATOM   14471 H  HB3  . LEU   B  2  356 ? 26.396  -28.417 15.347   1.00 69.47  ? 360  LEU   B HB3  1 
ATOM   14472 H  HG   . LEU   B  2  356 ? 26.405  -30.212 17.508   1.00 67.79  ? 360  LEU   B HG   1 
ATOM   14473 H  HD11 . LEU   B  2  356 ? 27.323  -28.403 18.698   1.00 68.62  ? 360  LEU   B HD11 1 
ATOM   14474 H  HD12 . LEU   B  2  356 ? 28.249  -28.784 17.465   1.00 68.62  ? 360  LEU   B HD12 1 
ATOM   14475 H  HD13 . LEU   B  2  356 ? 27.283  -27.526 17.374   1.00 68.62  ? 360  LEU   B HD13 1 
ATOM   14476 H  HD21 . LEU   B  2  356 ? 24.990  -28.601 18.606   1.00 67.35  ? 360  LEU   B HD21 1 
ATOM   14477 H  HD22 . LEU   B  2  356 ? 24.662  -28.048 17.154   1.00 67.35  ? 360  LEU   B HD22 1 
ATOM   14478 H  HD23 . LEU   B  2  356 ? 24.277  -29.539 17.542   1.00 67.35  ? 360  LEU   B HD23 1 
ATOM   14479 N  N    . GLU   B  2  357 ? 24.077  -28.265 13.744   1.00 58.20  ? 361  GLU   B N    1 
ATOM   14480 C  CA   . GLU   B  2  357 ? 23.623  -27.460 12.621   1.00 60.18  ? 361  GLU   B CA   1 
ATOM   14481 C  C    . GLU   B  2  357 ? 23.589  -26.010 13.075   1.00 60.82  ? 361  GLU   B C    1 
ATOM   14482 O  O    . GLU   B  2  357 ? 23.051  -25.711 14.145   1.00 63.76  ? 361  GLU   B O    1 
ATOM   14483 C  CB   . GLU   B  2  357 ? 22.236  -27.911 12.159   1.00 67.17  ? 361  GLU   B CB   1 
ATOM   14484 C  CG   . GLU   B  2  357 ? 21.971  -27.766 10.673   1.00 75.60  ? 361  GLU   B CG   1 
ATOM   14485 C  CD   . GLU   B  2  357 ? 20.539  -28.116 10.319   1.00 82.18  ? 361  GLU   B CD   1 
ATOM   14486 O  OE1  . GLU   B  2  357 ? 19.741  -28.342 11.253   1.00 81.53  ? 361  GLU   B OE1  1 
ATOM   14487 O  OE2  . GLU   B  2  357 ? 20.209  -28.169 9.115    1.00 86.58  ? 361  GLU   B OE2  1 
ATOM   14488 H  H    . GLU   B  2  357 ? 23.745  -28.013 14.496   1.00 69.83  ? 361  GLU   B H    1 
ATOM   14489 H  HA   . GLU   B  2  357 ? 24.232  -27.539 11.870   1.00 72.19  ? 361  GLU   B HA   1 
ATOM   14490 H  HB2  . GLU   B  2  357 ? 22.129  -28.849 12.382   1.00 80.59  ? 361  GLU   B HB2  1 
ATOM   14491 H  HB3  . GLU   B  2  357 ? 21.570  -27.381 12.625   1.00 80.59  ? 361  GLU   B HB3  1 
ATOM   14492 H  HG2  . GLU   B  2  357 ? 22.134  -26.848 10.408   1.00 90.70  ? 361  GLU   B HG2  1 
ATOM   14493 H  HG3  . GLU   B  2  357 ? 22.559  -28.363 10.184   1.00 90.70  ? 361  GLU   B HG3  1 
ATOM   14494 N  N    . VAL   B  2  358 ? 24.168  -25.119 12.276   1.00 59.78  ? 362  VAL   B N    1 
ATOM   14495 C  CA   . VAL   B  2  358 ? 24.198  -23.693 12.581   1.00 60.92  ? 362  VAL   B CA   1 
ATOM   14496 C  C    . VAL   B  2  358 ? 23.341  -22.977 11.550   1.00 65.83  ? 362  VAL   B C    1 
ATOM   14497 O  O    . VAL   B  2  358 ? 23.636  -23.017 10.349   1.00 70.22  ? 362  VAL   B O    1 
ATOM   14498 C  CB   . VAL   B  2  358 ? 25.631  -23.139 12.591   1.00 59.51  ? 362  VAL   B CB   1 
ATOM   14499 C  CG1  . VAL   B  2  358 ? 25.628  -21.647 12.923   1.00 62.33  ? 362  VAL   B CG1  1 
ATOM   14500 C  CG2  . VAL   B  2  358 ? 26.479  -23.903 13.590   1.00 57.37  ? 362  VAL   B CG2  1 
ATOM   14501 H  H    . VAL   B  2  358 ? 24.557  -25.321 11.537   1.00 71.71  ? 362  VAL   B H    1 
ATOM   14502 H  HA   . VAL   B  2  358 ? 23.813  -23.545 13.459   1.00 73.09  ? 362  VAL   B HA   1 
ATOM   14503 H  HB   . VAL   B  2  358 ? 26.019  -23.250 11.709   1.00 71.39  ? 362  VAL   B HB   1 
ATOM   14504 H  HG11 . VAL   B  2  358 ? 26.530  -21.302 12.832   1.00 74.78  ? 362  VAL   B HG11 1 
ATOM   14505 H  HG12 . VAL   B  2  358 ? 25.035  -21.188 12.308   1.00 74.78  ? 362  VAL   B HG12 1 
ATOM   14506 H  HG13 . VAL   B  2  358 ? 25.318  -21.527 13.834   1.00 74.78  ? 362  VAL   B HG13 1 
ATOM   14507 H  HG21 . VAL   B  2  358 ? 27.225  -23.346 13.863   1.00 68.83  ? 362  VAL   B HG21 1 
ATOM   14508 H  HG22 . VAL   B  2  358 ? 25.934  -24.128 14.360   1.00 68.83  ? 362  VAL   B HG22 1 
ATOM   14509 H  HG23 . VAL   B  2  358 ? 26.808  -24.713 13.170   1.00 68.83  ? 362  VAL   B HG23 1 
ATOM   14510 N  N    . LEU   B  2  359 ? 22.280  -22.329 12.018   1.00 66.85  ? 363  LEU   B N    1 
ATOM   14511 C  CA   . LEU   B  2  359 ? 21.375  -21.572 11.170   1.00 71.27  ? 363  LEU   B CA   1 
ATOM   14512 C  C    . LEU   B  2  359 ? 21.368  -20.113 11.608   1.00 71.18  ? 363  LEU   B C    1 
ATOM   14513 O  O    . LEU   B  2  359 ? 21.769  -19.776 12.725   1.00 71.61  ? 363  LEU   B O    1 
ATOM   14514 C  CB   . LEU   B  2  359 ? 19.951  -22.142 11.228   1.00 75.17  ? 363  LEU   B CB   1 
ATOM   14515 C  CG   . LEU   B  2  359 ? 19.718  -23.516 10.591   1.00 80.89  ? 363  LEU   B CG   1 
ATOM   14516 C  CD1  . LEU   B  2  359 ? 20.468  -24.624 11.329   1.00 75.66  ? 363  LEU   B CD1  1 
ATOM   14517 C  CD2  . LEU   B  2  359 ? 18.223  -23.808 10.532   1.00 88.64  ? 363  LEU   B CD2  1 
ATOM   14518 H  H    . LEU   B  2  359 ? 22.060  -22.313 12.849   1.00 80.20  ? 363  LEU   B H    1 
ATOM   14519 H  HA   . LEU   B  2  359 ? 21.678  -21.615 10.250   1.00 85.51  ? 363  LEU   B HA   1 
ATOM   14520 H  HB2  . LEU   B  2  359 ? 19.698  -22.218 12.162   1.00 90.19  ? 363  LEU   B HB2  1 
ATOM   14521 H  HB3  . LEU   B  2  359 ? 19.362  -21.518 10.775   1.00 90.19  ? 363  LEU   B HB3  1 
ATOM   14522 H  HG   . LEU   B  2  359 ? 20.071  -23.505 9.687    1.00 97.05  ? 363  LEU   B HG   1 
ATOM   14523 H  HD11 . LEU   B  2  359 ? 19.979  -25.456 11.230   1.00 90.77  ? 363  LEU   B HD11 1 
ATOM   14524 H  HD12 . LEU   B  2  359 ? 21.355  -24.714 10.947   1.00 90.77  ? 363  LEU   B HD12 1 
ATOM   14525 H  HD13 . LEU   B  2  359 ? 20.535  -24.389 12.268   1.00 90.77  ? 363  LEU   B HD13 1 
ATOM   14526 H  HD21 . LEU   B  2  359 ? 18.089  -24.768 10.495   1.00 106.35 ? 363  LEU   B HD21 1 
ATOM   14527 H  HD22 . LEU   B  2  359 ? 17.799  -23.446 11.326   1.00 106.35 ? 363  LEU   B HD22 1 
ATOM   14528 H  HD23 . LEU   B  2  359 ? 17.850  -23.391 9.740    1.00 106.35 ? 363  LEU   B HD23 1 
ATOM   14529 N  N    . GLY   B  2  360 ? 20.907  -19.247 10.709   1.00 70.41  ? 364  GLY   B N    1 
ATOM   14530 C  CA   . GLY   B  2  360 ? 20.787  -17.836 11.016   1.00 72.83  ? 364  GLY   B CA   1 
ATOM   14531 C  C    . GLY   B  2  360 ? 21.725  -16.954 10.218   1.00 74.65  ? 364  GLY   B C    1 
ATOM   14532 O  O    . GLY   B  2  360 ? 22.104  -17.289 9.092    1.00 76.71  ? 364  GLY   B O    1 
ATOM   14533 H  H    . GLY   B  2  360 ? 20.658  -19.457 9.913    1.00 84.47  ? 364  GLY   B H    1 
ATOM   14534 H  HA2  . GLY   B  2  360 ? 19.879  -17.550 10.832   1.00 87.38  ? 364  GLY   B HA2  1 
ATOM   14535 H  HA3  . GLY   B  2  360 ? 20.977  -17.701 11.957   1.00 87.38  ? 364  GLY   B HA3  1 
ATOM   14536 N  N    . ASP   B  2  361 ? 22.110  -15.819 10.804   1.00 76.31  ? 365  ASP   B N    1 
ATOM   14537 C  CA   . ASP   B  2  361 ? 22.956  -14.834 10.131   1.00 80.53  ? 365  ASP   B CA   1 
ATOM   14538 C  C    . ASP   B  2  361 ? 24.416  -15.219 10.350   1.00 76.81  ? 365  ASP   B C    1 
ATOM   14539 O  O    . ASP   B  2  361 ? 25.119  -14.680 11.208   1.00 73.69  ? 365  ASP   B O    1 
ATOM   14540 C  CB   . ASP   B  2  361 ? 22.652  -13.434 10.650   1.00 86.75  ? 365  ASP   B CB   1 
ATOM   14541 C  CG   . ASP   B  2  361 ? 23.285  -12.346 9.808    1.00 92.35  ? 365  ASP   B CG   1 
ATOM   14542 O  OD1  . ASP   B  2  361 ? 23.926  -12.673 8.787    1.00 93.61  ? 365  ASP   B OD1  1 
ATOM   14543 O  OD2  . ASP   B  2  361 ? 23.136  -11.160 10.169   1.00 96.04  ? 365  ASP   B OD2  1 
ATOM   14544 H  H    . ASP   B  2  361 ? 21.890  -15.593 11.604   1.00 91.55  ? 365  ASP   B H    1 
ATOM   14545 H  HA   . ASP   B  2  361 ? 22.777  -14.853 9.177    1.00 96.61  ? 365  ASP   B HA   1 
ATOM   14546 H  HB2  . ASP   B  2  361 ? 21.692  -13.297 10.646   1.00 104.08 ? 365  ASP   B HB2  1 
ATOM   14547 H  HB3  . ASP   B  2  361 ? 22.995  -13.351 11.554   1.00 104.08 ? 365  ASP   B HB3  1 
ATOM   14548 N  N    . THR   B  2  362 ? 24.877  -16.177 9.544    1.00 78.55  ? 366  THR   B N    1 
ATOM   14549 C  CA   . THR   B  2  362 ? 26.226  -16.709 9.664    1.00 79.05  ? 366  THR   B CA   1 
ATOM   14550 C  C    . THR   B  2  362 ? 27.142  -16.329 8.508    1.00 82.55  ? 366  THR   B C    1 
ATOM   14551 O  O    . THR   B  2  362 ? 28.349  -16.578 8.596    1.00 82.00  ? 366  THR   B O    1 
ATOM   14552 C  CB   . THR   B  2  362 ? 26.185  -18.241 9.778    1.00 77.14  ? 366  THR   B CB   1 
ATOM   14553 O  OG1  . THR   B  2  362 ? 25.504  -18.791 8.643    1.00 81.30  ? 366  THR   B OG1  1 
ATOM   14554 C  CG2  . THR   B  2  362 ? 25.473  -18.666 11.057   1.00 75.45  ? 366  THR   B CG2  1 
ATOM   14555 H  H    A THR   B  2  362 ? 24.418  -16.537 8.912    0.40 94.23  ? 366  THR   B H    1 
ATOM   14556 H  H    B THR   B  2  362 ? 24.418  -16.537 8.912    0.60 94.23  ? 366  THR   B H    1 
ATOM   14557 H  HA   . THR   B  2  362 ? 26.618  -16.355 10.478   1.00 94.84  ? 366  THR   B HA   1 
ATOM   14558 H  HB   . THR   B  2  362 ? 27.091  -18.587 9.807    1.00 92.54  ? 366  THR   B HB   1 
ATOM   14559 H  HG1  . THR   B  2  362 ? 25.934  -18.624 7.941    1.00 97.54  ? 366  THR   B HG1  1 
ATOM   14560 H  HG21 . THR   B  2  362 ? 24.797  -19.332 10.855   1.00 90.52  ? 366  THR   B HG21 1 
ATOM   14561 H  HG22 . THR   B  2  362 ? 26.111  -19.045 11.682   1.00 90.52  ? 366  THR   B HG22 1 
ATOM   14562 H  HG23 . THR   B  2  362 ? 25.046  -17.899 11.470   1.00 90.52  ? 366  THR   B HG23 1 
ATOM   14563 N  N    . GLU   B  2  363 ? 26.613  -15.745 7.435    1.00 84.61  ? 367  GLU   B N    1 
ATOM   14564 C  CA   . GLU   B  2  363 ? 27.463  -15.335 6.323    1.00 85.42  ? 367  GLU   B CA   1 
ATOM   14565 C  C    . GLU   B  2  363 ? 28.512  -14.340 6.802    1.00 82.92  ? 367  GLU   B C    1 
ATOM   14566 O  O    . GLU   B  2  363 ? 28.197  -13.368 7.495    1.00 81.84  ? 367  GLU   B O    1 
ATOM   14567 C  CB   . GLU   B  2  363 ? 26.621  -14.718 5.206    1.00 94.49  ? 367  GLU   B CB   1 
ATOM   14568 C  CG   . GLU   B  2  363 ? 26.270  -15.684 4.082    1.00 104.75 ? 367  GLU   B CG   1 
ATOM   14569 C  CD   . GLU   B  2  363 ? 27.489  -16.148 3.311    1.00 113.53 ? 367  GLU   B CD   1 
ATOM   14570 O  OE1  . GLU   B  2  363 ? 28.517  -15.439 3.336    1.00 116.89 ? 367  GLU   B OE1  1 
ATOM   14571 O  OE2  . GLU   B  2  363 ? 27.420  -17.225 2.683    1.00 116.46 ? 367  GLU   B OE2  1 
ATOM   14572 H  H    . GLU   B  2  363 ? 25.777  -15.577 7.328    1.00 101.52 ? 367  GLU   B H    1 
ATOM   14573 H  HA   . GLU   B  2  363 ? 27.914  -16.114 5.963    1.00 102.49 ? 367  GLU   B HA   1 
ATOM   14574 H  HB2  . GLU   B  2  363 ? 25.789  -14.395 5.586    1.00 113.37 ? 367  GLU   B HB2  1 
ATOM   14575 H  HB3  . GLU   B  2  363 ? 27.116  -13.981 4.816    1.00 113.37 ? 367  GLU   B HB3  1 
ATOM   14576 H  HG2  . GLU   B  2  363 ? 25.838  -16.466 4.460    1.00 125.68 ? 367  GLU   B HG2  1 
ATOM   14577 H  HG3  . GLU   B  2  363 ? 25.671  -15.242 3.460    1.00 125.68 ? 367  GLU   B HG3  1 
ATOM   14578 N  N    . GLY   B  2  364 ? 29.766  -14.586 6.426    1.00 84.44  ? 368  GLY   B N    1 
ATOM   14579 C  CA   . GLY   B  2  364 ? 30.872  -13.752 6.841    1.00 84.87  ? 368  GLY   B CA   1 
ATOM   14580 C  C    . GLY   B  2  364 ? 31.504  -14.136 8.160    1.00 83.55  ? 368  GLY   B C    1 
ATOM   14581 O  O    . GLY   B  2  364 ? 32.450  -13.465 8.592    1.00 82.54  ? 368  GLY   B O    1 
ATOM   14582 H  H    . GLY   B  2  364 ? 29.998  -15.244 5.923    1.00 101.30 ? 368  GLY   B H    1 
ATOM   14583 H  HA2  . GLY   B  2  364 ? 31.562  -13.791 6.160    1.00 101.82 ? 368  GLY   B HA2  1 
ATOM   14584 H  HA3  . GLY   B  2  364 ? 30.557  -12.838 6.920    1.00 101.82 ? 368  GLY   B HA3  1 
ATOM   14585 N  N    . LEU   B  2  365 ? 31.019  -15.187 8.812    1.00 83.83  ? 369  LEU   B N    1 
ATOM   14586 C  CA   . LEU   B  2  365 ? 31.575  -15.649 10.074   1.00 81.35  ? 369  LEU   B CA   1 
ATOM   14587 C  C    . LEU   B  2  365 ? 32.479  -16.854 9.850    1.00 80.57  ? 369  LEU   B C    1 
ATOM   14588 O  O    . LEU   B  2  365 ? 32.240  -17.681 8.966    1.00 83.70  ? 369  LEU   B O    1 
ATOM   14589 C  CB   . LEU   B  2  365 ? 30.466  -16.022 11.061   1.00 78.64  ? 369  LEU   B CB   1 
ATOM   14590 C  CG   . LEU   B  2  365 ? 29.906  -14.914 11.953   1.00 81.50  ? 369  LEU   B CG   1 
ATOM   14591 C  CD1  . LEU   B  2  365 ? 28.787  -15.477 12.817   1.00 77.89  ? 369  LEU   B CD1  1 
ATOM   14592 C  CD2  . LEU   B  2  365 ? 30.990  -14.297 12.825   1.00 84.10  ? 369  LEU   B CD2  1 
ATOM   14593 H  H    . LEU   B  2  365 ? 30.354  -15.657 8.537    1.00 100.58 ? 369  LEU   B H    1 
ATOM   14594 H  HA   . LEU   B  2  365 ? 32.104  -14.936 10.464   1.00 97.60  ? 369  LEU   B HA   1 
ATOM   14595 H  HB2  . LEU   B  2  365 ? 29.721  -16.373 10.549   1.00 94.35  ? 369  LEU   B HB2  1 
ATOM   14596 H  HB3  . LEU   B  2  365 ? 30.815  -16.708 11.652   1.00 94.35  ? 369  LEU   B HB3  1 
ATOM   14597 H  HG   . LEU   B  2  365 ? 29.553  -14.206 11.393   1.00 97.78  ? 369  LEU   B HG   1 
ATOM   14598 H  HD11 . LEU   B  2  365 ? 28.412  -14.761 13.353   1.00 93.45  ? 369  LEU   B HD11 1 
ATOM   14599 H  HD12 . LEU   B  2  365 ? 28.103  -15.853 12.241   1.00 93.45  ? 369  LEU   B HD12 1 
ATOM   14600 H  HD13 . LEU   B  2  365 ? 29.150  -16.167 13.394   1.00 93.45  ? 369  LEU   B HD13 1 
ATOM   14601 H  HD21 . LEU   B  2  365 ? 30.586  -13.641 13.415   1.00 100.90 ? 369  LEU   B HD21 1 
ATOM   14602 H  HD22 . LEU   B  2  365 ? 31.412  -14.996 13.347   1.00 100.90 ? 369  LEU   B HD22 1 
ATOM   14603 H  HD23 . LEU   B  2  365 ? 31.647  -13.867 12.255   1.00 100.90 ? 369  LEU   B HD23 1 
ATOM   14604 N  N    . ASN   B  2  366 ? 33.525  -16.943 10.665   1.00 76.60  ? 370  ASN   B N    1 
ATOM   14605 C  CA   . ASN   B  2  366 ? 34.419  -18.092 10.676   1.00 73.77  ? 370  ASN   B CA   1 
ATOM   14606 C  C    . ASN   B  2  366 ? 34.021  -19.007 11.824   1.00 65.54  ? 370  ASN   B C    1 
ATOM   14607 O  O    . ASN   B  2  366 ? 33.922  -18.562 12.973   1.00 60.05  ? 370  ASN   B O    1 
ATOM   14608 C  CB   . ASN   B  2  366 ? 35.877  -17.657 10.824   1.00 78.26  ? 370  ASN   B CB   1 
ATOM   14609 C  CG   . ASN   B  2  366 ? 36.284  -16.621 9.797    1.00 83.02  ? 370  ASN   B CG   1 
ATOM   14610 O  OD1  . ASN   B  2  366 ? 36.889  -15.604 10.134   1.00 82.69  ? 370  ASN   B OD1  1 
ATOM   14611 N  ND2  . ASN   B  2  366 ? 35.948  -16.871 8.536    1.00 87.08  ? 370  ASN   B ND2  1 
ATOM   14612 H  H    . ASN   B  2  366 ? 33.740  -16.335 11.235   1.00 91.90  ? 370  ASN   B H    1 
ATOM   14613 H  HA   . ASN   B  2  366 ? 34.340  -18.577 9.840    1.00 88.50  ? 370  ASN   B HA   1 
ATOM   14614 H  HB2  . ASN   B  2  366 ? 36.004  -17.273 11.706   1.00 93.89  ? 370  ASN   B HB2  1 
ATOM   14615 H  HB3  . ASN   B  2  366 ? 36.451  -18.432 10.714   1.00 93.89  ? 370  ASN   B HB3  1 
ATOM   14616 H  HD21 . ASN   B  2  366 ? 36.157  -16.312 7.917    1.00 104.47 ? 370  ASN   B HD21 1 
ATOM   14617 H  HD22 . ASN   B  2  366 ? 35.521  -17.591 8.340    1.00 104.47 ? 370  ASN   B HD22 1 
ATOM   14618 N  N    . LEU   B  2  367 ? 33.786  -20.278 11.511   1.00 64.68  ? 371  LEU   B N    1 
ATOM   14619 C  CA   . LEU   B  2  367 ? 33.354  -21.261 12.492   1.00 62.21  ? 371  LEU   B CA   1 
ATOM   14620 C  C    . LEU   B  2  367 ? 34.280  -22.465 12.450   1.00 63.53  ? 371  LEU   B C    1 
ATOM   14621 O  O    . LEU   B  2  367 ? 34.685  -22.912 11.373   1.00 64.49  ? 371  LEU   B O    1 
ATOM   14622 C  CB   . LEU   B  2  367 ? 31.913  -21.712 12.229   1.00 63.35  ? 371  LEU   B CB   1 
ATOM   14623 C  CG   . LEU   B  2  367 ? 30.857  -20.608 12.169   1.00 64.59  ? 371  LEU   B CG   1 
ATOM   14624 C  CD1  . LEU   B  2  367 ? 29.534  -21.175 11.683   1.00 65.26  ? 371  LEU   B CD1  1 
ATOM   14625 C  CD2  . LEU   B  2  367 ? 30.688  -19.943 13.527   1.00 61.76  ? 371  LEU   B CD2  1 
ATOM   14626 H  H    . LEU   B  2  367 ? 33.873  -20.599 10.718   1.00 77.60  ? 371  LEU   B H    1 
ATOM   14627 H  HA   . LEU   B  2  367 ? 33.398  -20.871 13.379   1.00 74.63  ? 371  LEU   B HA   1 
ATOM   14628 H  HB2  . LEU   B  2  367 ? 31.892  -22.174 11.376   1.00 76.00  ? 371  LEU   B HB2  1 
ATOM   14629 H  HB3  . LEU   B  2  367 ? 31.653  -22.318 12.941   1.00 76.00  ? 371  LEU   B HB3  1 
ATOM   14630 H  HG   . LEU   B  2  367 ? 31.147  -19.926 11.543   1.00 77.49  ? 371  LEU   B HG   1 
ATOM   14631 H  HD11 . LEU   B  2  367 ? 28.862  -20.476 11.709   1.00 78.29  ? 371  LEU   B HD11 1 
ATOM   14632 H  HD12 . LEU   B  2  367 ? 29.643  -21.495 10.773   1.00 78.29  ? 371  LEU   B HD12 1 
ATOM   14633 H  HD13 . LEU   B  2  367 ? 29.272  -21.908 12.262   1.00 78.29  ? 371  LEU   B HD13 1 
ATOM   14634 H  HD21 . LEU   B  2  367 ? 29.993  -19.270 13.466   1.00 74.09  ? 371  LEU   B HD21 1 
ATOM   14635 H  HD22 . LEU   B  2  367 ? 30.440  -20.617 14.180   1.00 74.09  ? 371  LEU   B HD22 1 
ATOM   14636 H  HD23 . LEU   B  2  367 ? 31.528  -19.529 13.783   1.00 74.09  ? 371  LEU   B HD23 1 
ATOM   14637 N  N    . SER   B  2  368 ? 34.617  -22.982 13.628   1.00 67.10  ? 372  SER   B N    1 
ATOM   14638 C  CA   . SER   B  2  368 ? 35.362  -24.224 13.759   1.00 66.14  ? 372  SER   B CA   1 
ATOM   14639 C  C    . SER   B  2  368 ? 34.593  -25.152 14.685   1.00 60.72  ? 372  SER   B C    1 
ATOM   14640 O  O    . SER   B  2  368 ? 34.081  -24.720 15.723   1.00 58.65  ? 372  SER   B O    1 
ATOM   14641 C  CB   . SER   B  2  368 ? 36.772  -23.988 14.309   1.00 68.96  ? 372  SER   B CB   1 
ATOM   14642 O  OG   . SER   B  2  368 ? 37.582  -25.134 14.116   1.00 75.11  ? 372  SER   B OG   1 
ATOM   14643 H  H    . SER   B  2  368 ? 34.418  -22.620 14.383   1.00 80.50  ? 372  SER   B H    1 
ATOM   14644 H  HA   . SER   B  2  368 ? 35.455  -24.645 12.891   1.00 79.35  ? 372  SER   B HA   1 
ATOM   14645 H  HB2  . SER   B  2  368 ? 37.171  -23.236 13.845   1.00 82.73  ? 372  SER   B HB2  1 
ATOM   14646 H  HB3  . SER   B  2  368 ? 36.713  -23.799 15.259   1.00 82.73  ? 372  SER   B HB3  1 
ATOM   14647 H  HG   . SER   B  2  368 ? 38.171  -25.174 14.714   1.00 90.12  ? 372  SER   B HG   1 
ATOM   14648 N  N    . PHE   B  2  369 ? 34.508  -26.423 14.306   1.00 60.68  ? 373  PHE   B N    1 
ATOM   14649 C  CA   . PHE   B  2  369 ? 33.788  -27.423 15.080   1.00 60.30  ? 373  PHE   B CA   1 
ATOM   14650 C  C    . PHE   B  2  369 ? 34.737  -28.542 15.476   1.00 62.29  ? 373  PHE   B C    1 
ATOM   14651 O  O    . PHE   B  2  369 ? 35.439  -29.099 14.626   1.00 67.93  ? 373  PHE   B O    1 
ATOM   14652 C  CB   . PHE   B  2  369 ? 32.609  -27.993 14.289   1.00 58.17  ? 373  PHE   B CB   1 
ATOM   14653 C  CG   . PHE   B  2  369 ? 31.546  -26.984 13.979   1.00 58.25  ? 373  PHE   B CG   1 
ATOM   14654 C  CD1  . PHE   B  2  369 ? 30.570  -26.679 14.912   1.00 59.18  ? 373  PHE   B CD1  1 
ATOM   14655 C  CD2  . PHE   B  2  369 ? 31.522  -26.339 12.755   1.00 59.42  ? 373  PHE   B CD2  1 
ATOM   14656 C  CE1  . PHE   B  2  369 ? 29.590  -25.750 14.629   1.00 60.65  ? 373  PHE   B CE1  1 
ATOM   14657 C  CE2  . PHE   B  2  369 ? 30.546  -25.410 12.466   1.00 63.33  ? 373  PHE   B CE2  1 
ATOM   14658 C  CZ   . PHE   B  2  369 ? 29.578  -25.114 13.404   1.00 62.63  ? 373  PHE   B CZ   1 
ATOM   14659 H  H    . PHE   B  2  369 ? 34.868  -26.734 13.589   1.00 72.80  ? 373  PHE   B H    1 
ATOM   14660 H  HA   . PHE   B  2  369 ? 33.446  -27.011 15.889   1.00 72.34  ? 373  PHE   B HA   1 
ATOM   14661 H  HB2  . PHE   B  2  369 ? 32.939  -28.344 13.447   1.00 69.79  ? 373  PHE   B HB2  1 
ATOM   14662 H  HB3  . PHE   B  2  369 ? 32.201  -28.704 14.808   1.00 69.79  ? 373  PHE   B HB3  1 
ATOM   14663 H  HD1  . PHE   B  2  369 ? 30.575  -27.105 15.739   1.00 71.00  ? 373  PHE   B HD1  1 
ATOM   14664 H  HD2  . PHE   B  2  369 ? 32.172  -26.536 12.119   1.00 71.28  ? 373  PHE   B HD2  1 
ATOM   14665 H  HE1  . PHE   B  2  369 ? 28.939  -25.552 15.263   1.00 72.77  ? 373  PHE   B HE1  1 
ATOM   14666 H  HE2  . PHE   B  2  369 ? 30.540  -24.983 11.640   1.00 75.98  ? 373  PHE   B HE2  1 
ATOM   14667 H  HZ   . PHE   B  2  369 ? 28.919  -24.488 13.211   1.00 75.14  ? 373  PHE   B HZ   1 
ATOM   14668 N  N    . THR   B  2  370 ? 34.756  -28.858 16.767   1.00 60.04  ? 374  THR   B N    1 
ATOM   14669 C  CA   . THR   B  2  370 ? 35.443  -30.031 17.290   1.00 65.10  ? 374  THR   B CA   1 
ATOM   14670 C  C    . THR   B  2  370 ? 34.427  -30.846 18.076   1.00 67.30  ? 374  THR   B C    1 
ATOM   14671 O  O    . THR   B  2  370 ? 33.850  -30.349 19.049   1.00 65.51  ? 374  THR   B O    1 
ATOM   14672 C  CB   . THR   B  2  370 ? 36.626  -29.645 18.180   1.00 65.26  ? 374  THR   B CB   1 
ATOM   14673 O  OG1  . THR   B  2  370 ? 37.575  -28.884 17.422   1.00 69.13  ? 374  THR   B OG1  1 
ATOM   14674 C  CG2  . THR   B  2  370 ? 37.308  -30.890 18.732   1.00 64.76  ? 374  THR   B CG2  1 
ATOM   14675 H  H    . THR   B  2  370 ? 34.366  -28.394 17.376   1.00 72.03  ? 374  THR   B H    1 
ATOM   14676 H  HA   . THR   B  2  370 ? 35.790  -30.565 16.558   1.00 78.10  ? 374  THR   B HA   1 
ATOM   14677 H  HB   . THR   B  2  370 ? 36.307  -29.112 18.925   1.00 78.29  ? 374  THR   B HB   1 
ATOM   14678 H  HG1  . THR   B  2  370 ? 37.952  -29.377 16.856   1.00 82.93  ? 374  THR   B HG1  1 
ATOM   14679 H  HG21 . THR   B  2  370 ? 38.098  -30.640 19.236   1.00 77.69  ? 374  THR   B HG21 1 
ATOM   14680 H  HG22 . THR   B  2  370 ? 36.700  -31.369 19.317   1.00 77.69  ? 374  THR   B HG22 1 
ATOM   14681 H  HG23 . THR   B  2  370 ? 37.570  -31.475 18.004   1.00 77.69  ? 374  THR   B HG23 1 
ATOM   14682 N  N    . ALA   B  2  371 ? 34.201  -32.083 17.649   1.00 68.76  ? 375  ALA   B N    1 
ATOM   14683 C  CA   . ALA   B  2  371 ? 33.235  -32.963 18.289   1.00 67.75  ? 375  ALA   B CA   1 
ATOM   14684 C  C    . ALA   B  2  371 ? 33.956  -33.861 19.284   1.00 71.18  ? 375  ALA   B C    1 
ATOM   14685 O  O    . ALA   B  2  371 ? 34.983  -34.463 18.955   1.00 76.50  ? 375  ALA   B O    1 
ATOM   14686 C  CB   . ALA   B  2  371 ? 32.492  -33.805 17.252   1.00 67.23  ? 375  ALA   B CB   1 
ATOM   14687 H  H    . ALA   B  2  371 ? 34.604  -32.440 16.978   1.00 82.49  ? 375  ALA   B H    1 
ATOM   14688 H  HA   . ALA   B  2  371 ? 32.581  -32.433 18.770   1.00 81.28  ? 375  ALA   B HA   1 
ATOM   14689 H  HB1  . ALA   B  2  371 ? 31.642  -34.087 17.625   1.00 80.66  ? 375  ALA   B HB1  1 
ATOM   14690 H  HB2  . ALA   B  2  371 ? 32.343  -33.269 16.458   1.00 80.66  ? 375  ALA   B HB2  1 
ATOM   14691 H  HB3  . ALA   B  2  371 ? 33.030  -34.581 17.032   1.00 80.66  ? 375  ALA   B HB3  1 
ATOM   14692 N  N    . ILE   B  2  372 ? 33.418  -33.941 20.496   1.00 71.83  ? 376  ILE   B N    1 
ATOM   14693 C  CA   . ILE   B  2  372 ? 33.960  -34.777 21.561   1.00 79.45  ? 376  ILE   B CA   1 
ATOM   14694 C  C    . ILE   B  2  372 ? 32.826  -35.683 22.026   1.00 78.23  ? 376  ILE   B C    1 
ATOM   14695 O  O    . ILE   B  2  372 ? 31.823  -35.207 22.571   1.00 74.44  ? 376  ILE   B O    1 
ATOM   14696 C  CB   . ILE   B  2  372 ? 34.540  -33.942 22.717   1.00 86.20  ? 376  ILE   B CB   1 
ATOM   14697 C  CG1  . ILE   B  2  372 ? 34.202  -34.564 24.081   1.00 96.81  ? 376  ILE   B CG1  1 
ATOM   14698 C  CG2  . ILE   B  2  372 ? 34.063  -32.491 22.620   1.00 79.08  ? 376  ILE   B CG2  1 
ATOM   14699 C  CD1  . ILE   B  2  372 ? 34.927  -33.926 25.260   1.00 104.21 ? 376  ILE   B CD1  1 
ATOM   14700 H  H    . ILE   B  2  372 ? 32.716  -33.505 20.734   1.00 86.18  ? 376  ILE   B H    1 
ATOM   14701 H  HA   . ILE   B  2  372 ? 34.674  -35.335 21.215   1.00 95.32  ? 376  ILE   B HA   1 
ATOM   14702 H  HB   . ILE   B  2  372 ? 35.506  -33.947 22.637   1.00 103.42 ? 376  ILE   B HB   1 
ATOM   14703 H  HG12 . ILE   B  2  372 ? 33.249  -34.469 24.237   1.00 116.15 ? 376  ILE   B HG12 1 
ATOM   14704 H  HG13 . ILE   B  2  372 ? 34.443  -35.503 24.062   1.00 116.15 ? 376  ILE   B HG13 1 
ATOM   14705 H  HG21 . ILE   B  2  372 ? 34.295  -32.026 23.439   1.00 94.88  ? 376  ILE   B HG21 1 
ATOM   14706 H  HG22 . ILE   B  2  372 ? 34.497  -32.065 21.863   1.00 94.88  ? 376  ILE   B HG22 1 
ATOM   14707 H  HG23 . ILE   B  2  372 ? 33.100  -32.482 22.496   1.00 94.88  ? 376  ILE   B HG23 1 
ATOM   14708 H  HD11 . ILE   B  2  372 ? 35.661  -34.502 25.528   1.00 125.03 ? 376  ILE   B HD11 1 
ATOM   14709 H  HD12 . ILE   B  2  372 ? 35.269  -33.059 24.990   1.00 125.03 ? 376  ILE   B HD12 1 
ATOM   14710 H  HD13 . ILE   B  2  372 ? 34.304  -33.821 25.996   1.00 125.03 ? 376  ILE   B HD13 1 
ATOM   14711 N  N    . CYS   B  2  373 ? 32.974  -36.983 21.787   1.00 84.69  ? 377  CYS   B N    1 
ATOM   14712 C  CA   . CYS   B  2  373 ? 32.024  -38.002 22.210   1.00 96.52  ? 377  CYS   B CA   1 
ATOM   14713 C  C    . CYS   B  2  373 ? 32.730  -38.960 23.159   1.00 103.14 ? 377  CYS   B C    1 
ATOM   14714 O  O    . CYS   B  2  373 ? 33.951  -38.901 23.324   1.00 106.04 ? 377  CYS   B O    1 
ATOM   14715 C  CB   . CYS   B  2  373 ? 31.460  -38.770 21.007   1.00 102.82 ? 377  CYS   B CB   1 
ATOM   14716 S  SG   . CYS   B  2  373 ? 31.900  -38.101 19.389   1.00 100.55 ? 377  CYS   B SG   1 
ATOM   14717 H  H    . CYS   B  2  373 ? 33.646  -37.311 21.363   1.00 101.61 ? 377  CYS   B H    1 
ATOM   14718 H  HA   . CYS   B  2  373 ? 31.279  -37.586 22.671   1.00 115.81 ? 377  CYS   B HA   1 
ATOM   14719 H  HB2  . CYS   B  2  373 ? 31.790  -39.681 21.044   1.00 123.36 ? 377  CYS   B HB2  1 
ATOM   14720 H  HB3  . CYS   B  2  373 ? 30.492  -38.766 21.069   1.00 123.36 ? 377  CYS   B HB3  1 
ATOM   14721 H  HG   . CYS   B  2  373 ? 32.961  -38.551 19.055   1.00 120.63 ? 377  CYS   B HG   1 
ATOM   14722 N  N    . ASN   B  2  374 ? 31.965  -39.867 23.776   1.00 105.76 ? 378  ASN   B N    1 
ATOM   14723 C  CA   . ASN   B  2  374 ? 32.607  -40.875 24.617   1.00 114.25 ? 378  ASN   B CA   1 
ATOM   14724 C  C    . ASN   B  2  374 ? 33.493  -40.165 25.634   1.00 120.74 ? 378  ASN   B C    1 
ATOM   14725 O  O    . ASN   B  2  374 ? 34.700  -40.010 25.418   1.00 126.29 ? 378  ASN   B O    1 
ATOM   14726 C  CB   . ASN   B  2  374 ? 33.392  -41.888 23.789   1.00 117.55 ? 378  ASN   B CB   1 
ATOM   14727 C  CG   . ASN   B  2  374 ? 32.581  -42.448 22.638   1.00 116.74 ? 378  ASN   B CG   1 
ATOM   14728 O  OD1  . ASN   B  2  374 ? 31.351  -42.377 22.636   1.00 115.82 ? 378  ASN   B OD1  1 
ATOM   14729 N  ND2  . ASN   B  2  374 ? 33.267  -43.014 21.654   1.00 117.58 ? 378  ASN   B ND2  1 
ATOM   14730 H  H    . ASN   B  2  374 ? 31.108  -39.915 23.724   1.00 126.90 ? 378  ASN   B H    1 
ATOM   14731 H  HA   . ASN   B  2  374 ? 31.936  -41.394 25.087   1.00 137.09 ? 378  ASN   B HA   1 
ATOM   14732 H  HB2  . ASN   B  2  374 ? 34.178  -41.455 23.421   1.00 141.04 ? 378  ASN   B HB2  1 
ATOM   14733 H  HB3  . ASN   B  2  374 ? 33.656  -42.627 24.359   1.00 141.04 ? 378  ASN   B HB3  1 
ATOM   14734 H  HD21 . ASN   B  2  374 ? 32.853  -43.347 20.977   1.00 141.07 ? 378  ASN   B HD21 1 
ATOM   14735 H  HD22 . ASN   B  2  374 ? 34.125  -43.048 21.692   1.00 141.07 ? 378  ASN   B HD22 1 
ATOM   14736 N  N    . ASN   B  2  375 ? 32.906  -39.746 26.753   1.00 121.34 ? 379  ASN   B N    1 
ATOM   14737 C  CA   . ASN   B  2  375 ? 33.090  -38.460 27.410   1.00 122.86 ? 379  ASN   B CA   1 
ATOM   14738 C  C    . ASN   B  2  375 ? 34.348  -37.651 27.112   1.00 120.15 ? 379  ASN   B C    1 
ATOM   14739 O  O    . ASN   B  2  375 ? 34.245  -36.584 26.498   1.00 113.74 ? 379  ASN   B O    1 
ATOM   14740 C  CB   . ASN   B  2  375 ? 33.092  -38.744 28.926   1.00 134.53 ? 379  ASN   B CB   1 
ATOM   14741 C  CG   . ASN   B  2  375 ? 31.842  -39.473 29.398   1.00 142.11 ? 379  ASN   B CG   1 
ATOM   14742 O  OD1  . ASN   B  2  375 ? 30.966  -38.873 30.021   1.00 146.40 ? 379  ASN   B OD1  1 
ATOM   14743 N  ND2  . ASN   B  2  375 ? 31.761  -40.774 29.123   1.00 144.29 ? 379  ASN   B ND2  1 
ATOM   14744 H  H    . ASN   B  2  375 ? 32.348  -40.234 27.189   1.00 145.59 ? 379  ASN   B H    1 
ATOM   14745 H  HA   . ASN   B  2  375 ? 32.373  -37.899 27.073   1.00 147.41 ? 379  ASN   B HA   1 
ATOM   14746 H  HB2  . ASN   B  2  375 ? 33.859  -39.296 29.142   1.00 161.42 ? 379  ASN   B HB2  1 
ATOM   14747 H  HB3  . ASN   B  2  375 ? 33.145  -37.901 29.404   1.00 161.42 ? 379  ASN   B HB3  1 
ATOM   14748 H  HD21 . ASN   B  2  375 ? 31.072  -41.224 29.371   1.00 173.13 ? 379  ASN   B HD21 1 
ATOM   14749 H  HD22 . ASN   B  2  375 ? 32.399  -41.164 28.697   1.00 173.13 ? 379  ASN   B HD22 1 
ATOM   14750 N  N    . GLY   B  2  376 ? 35.526  -38.121 27.495   1.00 126.62 ? 380  GLY   B N    1 
ATOM   14751 C  CA   . GLY   B  2  376 ? 36.728  -37.346 27.244   1.00 126.98 ? 380  GLY   B CA   1 
ATOM   14752 C  C    . GLY   B  2  376 ? 37.696  -38.103 26.365   1.00 129.52 ? 380  GLY   B C    1 
ATOM   14753 O  O    . GLY   B  2  376 ? 38.751  -37.593 25.973   1.00 128.36 ? 380  GLY   B O    1 
ATOM   14754 H  H    . GLY   B  2  376 ? 35.652  -38.872 27.895   1.00 151.92 ? 380  GLY   B H    1 
ATOM   14755 H  HA2  . GLY   B  2  376 ? 36.493  -36.515 26.803   1.00 152.36 ? 380  GLY   B HA2  1 
ATOM   14756 H  HA3  . GLY   B  2  376 ? 37.166  -37.144 28.085   1.00 152.36 ? 380  GLY   B HA3  1 
ATOM   14757 N  N    . THR   B  2  377 ? 37.314  -39.335 26.039   1.00 131.55 ? 381  THR   B N    1 
ATOM   14758 C  CA   . THR   B  2  377 ? 38.229  -40.255 25.380   1.00 133.17 ? 381  THR   B CA   1 
ATOM   14759 C  C    . THR   B  2  377 ? 38.508  -39.843 23.939   1.00 131.23 ? 381  THR   B C    1 
ATOM   14760 O  O    . THR   B  2  377 ? 39.641  -39.980 23.463   1.00 141.25 ? 381  THR   B O    1 
ATOM   14761 C  CB   . THR   B  2  377 ? 37.643  -41.664 25.440   1.00 130.35 ? 381  THR   B CB   1 
ATOM   14762 O  OG1  . THR   B  2  377 ? 36.401  -41.692 24.725   1.00 123.79 ? 381  THR   B OG1  1 
ATOM   14763 C  CG2  . THR   B  2  377 ? 37.392  -42.067 26.893   1.00 131.30 ? 381  THR   B CG2  1 
ATOM   14764 H  H    . THR   B  2  377 ? 36.532  -39.661 26.188   1.00 157.84 ? 381  THR   B H    1 
ATOM   14765 H  HA   . THR   B  2  377 ? 39.079  -40.250 25.846   1.00 159.79 ? 381  THR   B HA   1 
ATOM   14766 H  HB   . THR   B  2  377 ? 38.263  -42.296 25.043   1.00 156.40 ? 381  THR   B HB   1 
ATOM   14767 H  HG1  . THR   B  2  377 ? 35.906  -41.066 24.984   1.00 148.53 ? 381  THR   B HG1  1 
ATOM   14768 H  HG21 . THR   B  2  377 ? 37.061  -42.978 26.932   1.00 157.54 ? 381  THR   B HG21 1 
ATOM   14769 H  HG22 . THR   B  2  377 ? 38.217  -42.010 27.400   1.00 157.54 ? 381  THR   B HG22 1 
ATOM   14770 H  HG23 . THR   B  2  377 ? 36.736  -41.476 27.293   1.00 157.54 ? 381  THR   B HG23 1 
ATOM   14771 N  N    . LEU   B  2  378 ? 37.503  -39.331 23.229   1.00 117.49 ? 382  LEU   B N    1 
ATOM   14772 C  CA   . LEU   B  2  378 ? 37.602  -39.109 21.792   1.00 110.86 ? 382  LEU   B CA   1 
ATOM   14773 C  C    . LEU   B  2  378 ? 37.427  -37.636 21.448   1.00 105.45 ? 382  LEU   B C    1 
ATOM   14774 O  O    . LEU   B  2  378 ? 36.492  -36.984 21.925   1.00 104.59 ? 382  LEU   B O    1 
ATOM   14775 C  CB   . LEU   B  2  378 ? 36.562  -39.949 21.041   1.00 109.21 ? 382  LEU   B CB   1 
ATOM   14776 C  CG   . LEU   B  2  378 ? 36.660  -39.869 19.515   1.00 108.71 ? 382  LEU   B CG   1 
ATOM   14777 C  CD1  . LEU   B  2  378 ? 36.232  -41.184 18.877   1.00 109.10 ? 382  LEU   B CD1  1 
ATOM   14778 C  CD2  . LEU   B  2  378 ? 35.837  -38.712 18.954   1.00 104.50 ? 382  LEU   B CD2  1 
ATOM   14779 H  H    . LEU   B  2  378 ? 36.745  -39.102 23.565   1.00 140.97 ? 382  LEU   B H    1 
ATOM   14780 H  HA   . LEU   B  2  378 ? 38.493  -39.364 21.503   1.00 133.02 ? 382  LEU   B HA   1 
ATOM   14781 H  HB2  . LEU   B  2  378 ? 36.676  -40.879 21.294   1.00 131.03 ? 382  LEU   B HB2  1 
ATOM   14782 H  HB3  . LEU   B  2  378 ? 35.677  -39.643 21.295   1.00 131.03 ? 382  LEU   B HB3  1 
ATOM   14783 H  HG   . LEU   B  2  378 ? 37.587  -39.703 19.284   1.00 130.44 ? 382  LEU   B HG   1 
ATOM   14784 H  HD11 . LEU   B  2  378 ? 36.318  -41.110 17.914   1.00 130.90 ? 382  LEU   B HD11 1 
ATOM   14785 H  HD12 . LEU   B  2  378 ? 36.804  -41.895 19.206   1.00 130.90 ? 382  LEU   B HD12 1 
ATOM   14786 H  HD13 . LEU   B  2  378 ? 35.309  -41.364 19.114   1.00 130.90 ? 382  LEU   B HD13 1 
ATOM   14787 H  HD21 . LEU   B  2  378 ? 35.347  -39.021 18.177   1.00 125.37 ? 382  LEU   B HD21 1 
ATOM   14788 H  HD22 . LEU   B  2  378 ? 35.218  -38.405 19.636   1.00 125.37 ? 382  LEU   B HD22 1 
ATOM   14789 H  HD23 . LEU   B  2  378 ? 36.436  -37.991 18.703   1.00 125.37 ? 382  LEU   B HD23 1 
ATOM   14790 N  N    . PHE   B  2  379 ? 38.328  -37.125 20.607   1.00 100.77 ? 383  PHE   B N    1 
ATOM   14791 C  CA   . PHE   B  2  379 ? 38.253  -35.781 20.048   1.00 90.97  ? 383  PHE   B CA   1 
ATOM   14792 C  C    . PHE   B  2  379 ? 38.383  -35.876 18.534   1.00 86.87  ? 383  PHE   B C    1 
ATOM   14793 O  O    . PHE   B  2  379 ? 39.299  -36.534 18.032   1.00 93.56  ? 383  PHE   B O    1 
ATOM   14794 C  CB   . PHE   B  2  379 ? 39.360  -34.879 20.606   1.00 93.04  ? 383  PHE   B CB   1 
ATOM   14795 C  CG   . PHE   B  2  379 ? 39.015  -34.219 21.910   1.00 94.39  ? 383  PHE   B CG   1 
ATOM   14796 C  CD1  . PHE   B  2  379 ? 39.303  -34.837 23.114   1.00 101.37 ? 383  PHE   B CD1  1 
ATOM   14797 C  CD2  . PHE   B  2  379 ? 38.420  -32.969 21.929   1.00 88.98  ? 383  PHE   B CD2  1 
ATOM   14798 C  CE1  . PHE   B  2  379 ? 38.993  -34.225 24.314   1.00 102.08 ? 383  PHE   B CE1  1 
ATOM   14799 C  CE2  . PHE   B  2  379 ? 38.108  -32.353 23.125   1.00 90.68  ? 383  PHE   B CE2  1 
ATOM   14800 C  CZ   . PHE   B  2  379 ? 38.395  -32.981 24.318   1.00 96.65  ? 383  PHE   B CZ   1 
ATOM   14801 H  H    . PHE   B  2  379 ? 39.019  -37.559 20.335   1.00 120.91 ? 383  PHE   B H    1 
ATOM   14802 H  HA   . PHE   B  2  379 ? 37.395  -35.386 20.271   1.00 109.15 ? 383  PHE   B HA   1 
ATOM   14803 H  HB2  . PHE   B  2  379 ? 40.155  -35.416 20.749   1.00 111.63 ? 383  PHE   B HB2  1 
ATOM   14804 H  HB3  . PHE   B  2  379 ? 39.544  -34.179 19.961   1.00 111.63 ? 383  PHE   B HB3  1 
ATOM   14805 H  HD1  . PHE   B  2  379 ? 39.710  -35.674 23.116   1.00 121.63 ? 383  PHE   B HD1  1 
ATOM   14806 H  HD2  . PHE   B  2  379 ? 38.227  -32.540 21.127   1.00 106.76 ? 383  PHE   B HD2  1 
ATOM   14807 H  HE1  . PHE   B  2  379 ? 39.188  -34.651 25.117   1.00 122.48 ? 383  PHE   B HE1  1 
ATOM   14808 H  HE2  . PHE   B  2  379 ? 37.705  -31.515 23.126   1.00 108.79 ? 383  PHE   B HE2  1 
ATOM   14809 H  HZ   . PHE   B  2  379 ? 38.186  -32.568 25.124   1.00 115.96 ? 383  PHE   B HZ   1 
ATOM   14810 N  N    . GLN   B  2  380 ? 37.475  -35.218 17.812   1.00 81.49  ? 384  GLN   B N    1 
ATOM   14811 C  CA   . GLN   B  2  380 ? 37.503  -35.213 16.355   1.00 81.61  ? 384  GLN   B CA   1 
ATOM   14812 C  C    . GLN   B  2  380 ? 37.023  -33.863 15.839   1.00 75.27  ? 384  GLN   B C    1 
ATOM   14813 O  O    . GLN   B  2  380 ? 36.129  -33.247 16.425   1.00 73.05  ? 384  GLN   B O    1 
ATOM   14814 C  CB   . GLN   B  2  380 ? 36.638  -36.340 15.774   1.00 86.23  ? 384  GLN   B CB   1 
ATOM   14815 C  CG   . GLN   B  2  380 ? 37.332  -37.696 15.739   1.00 97.21  ? 384  GLN   B CG   1 
ATOM   14816 C  CD   . GLN   B  2  380 ? 36.430  -38.806 15.235   1.00 101.97 ? 384  GLN   B CD   1 
ATOM   14817 O  OE1  . GLN   B  2  380 ? 35.288  -38.945 15.678   1.00 100.97 ? 384  GLN   B OE1  1 
ATOM   14818 N  NE2  . GLN   B  2  380 ? 36.937  -39.602 14.300   1.00 102.53 ? 384  GLN   B NE2  1 
ATOM   14819 H  H    . GLN   B  2  380 ? 36.828  -34.764 18.149   1.00 97.76  ? 384  GLN   B H    1 
ATOM   14820 H  HA   . GLN   B  2  380 ? 38.416  -35.339 16.053   1.00 97.92  ? 384  GLN   B HA   1 
ATOM   14821 H  HB2  . GLN   B  2  380 ? 35.839  -36.431 16.317   1.00 103.46 ? 384  GLN   B HB2  1 
ATOM   14822 H  HB3  . GLN   B  2  380 ? 36.395  -36.109 14.863   1.00 103.46 ? 384  GLN   B HB3  1 
ATOM   14823 H  HG2  . GLN   B  2  380 ? 38.100  -37.643 15.149   1.00 116.63 ? 384  GLN   B HG2  1 
ATOM   14824 H  HG3  . GLN   B  2  380 ? 37.619  -37.927 16.637   1.00 116.63 ? 384  GLN   B HG3  1 
ATOM   14825 H  HE21 . GLN   B  2  380 ? 37.737  -39.473 14.013   1.00 123.01 ? 384  GLN   B HE21 1 
ATOM   14826 H  HE22 . GLN   B  2  380 ? 36.465  -40.247 13.981   1.00 123.01 ? 384  GLN   B HE22 1 
ATOM   14827 N  N    . HIS   B  2  381 ? 37.622  -33.415 14.734   1.00 72.74  ? 385  HIS   B N    1 
ATOM   14828 C  CA   . HIS   B  2  381 ? 37.315  -32.104 14.160   1.00 69.71  ? 385  HIS   B CA   1 
ATOM   14829 C  C    . HIS   B  2  381 ? 36.157  -32.235 13.169   1.00 67.86  ? 385  HIS   B C    1 
ATOM   14830 O  O    . HIS   B  2  381 ? 36.290  -32.039 11.960   1.00 69.14  ? 385  HIS   B O    1 
ATOM   14831 C  CB   . HIS   B  2  381 ? 38.553  -31.510 13.499   1.00 69.42  ? 385  HIS   B CB   1 
ATOM   14832 C  CG   . HIS   B  2  381 ? 39.756  -31.478 14.390   1.00 71.77  ? 385  HIS   B CG   1 
ATOM   14833 N  ND1  . HIS   B  2  381 ? 39.718  -30.982 15.675   1.00 69.31  ? 385  HIS   B ND1  1 
ATOM   14834 C  CD2  . HIS   B  2  381 ? 41.034  -31.874 14.177   1.00 76.31  ? 385  HIS   B CD2  1 
ATOM   14835 C  CE1  . HIS   B  2  381 ? 40.918  -31.078 16.218   1.00 72.73  ? 385  HIS   B CE1  1 
ATOM   14836 N  NE2  . HIS   B  2  381 ? 41.735  -31.615 15.330   1.00 77.69  ? 385  HIS   B NE2  1 
ATOM   14837 H  H    . HIS   B  2  381 ? 38.215  -33.856 14.294   1.00 87.27  ? 385  HIS   B H    1 
ATOM   14838 H  HA   . HIS   B  2  381 ? 37.036  -31.509 14.874   1.00 83.63  ? 385  HIS   B HA   1 
ATOM   14839 H  HB2  . HIS   B  2  381 ? 38.776  -32.043 12.720   1.00 83.29  ? 385  HIS   B HB2  1 
ATOM   14840 H  HB3  . HIS   B  2  381 ? 38.357  -30.598 13.233   1.00 83.29  ? 385  HIS   B HB3  1 
ATOM   14841 H  HD2  . HIS   B  2  381 ? 41.373  -32.250 13.397   1.00 91.55  ? 385  HIS   B HD2  1 
ATOM   14842 H  HE1  . HIS   B  2  381 ? 41.149  -30.813 17.079   1.00 87.26  ? 385  HIS   B HE1  1 
ATOM   14843 H  HE2  . HIS   B  2  381 ? 42.571  -31.777 15.453   1.00 93.21  ? 385  HIS   B HE2  1 
ATOM   14844 N  N    . GLN   B  2  382 ? 34.995  -32.576 13.719   1.00 66.29  ? 386  GLN   B N    1 
ATOM   14845 C  CA   . GLN   B  2  382 ? 33.759  -32.686 12.961   1.00 64.56  ? 386  GLN   B CA   1 
ATOM   14846 C  C    . GLN   B  2  382 ? 32.656  -31.967 13.726   1.00 62.88  ? 386  GLN   B C    1 
ATOM   14847 O  O    . GLN   B  2  382 ? 32.869  -31.438 14.821   1.00 65.26  ? 386  GLN   B O    1 
ATOM   14848 C  CB   . GLN   B  2  382 ? 33.359  -34.149 12.725   1.00 65.99  ? 386  GLN   B CB   1 
ATOM   14849 C  CG   . GLN   B  2  382 ? 34.503  -35.111 12.467   1.00 77.18  ? 386  GLN   B CG   1 
ATOM   14850 C  CD   . GLN   B  2  382 ? 34.049  -36.558 12.531   1.00 86.25  ? 386  GLN   B CD   1 
ATOM   14851 O  OE1  . GLN   B  2  382 ? 33.414  -36.977 13.499   1.00 85.62  ? 386  GLN   B OE1  1 
ATOM   14852 N  NE2  . GLN   B  2  382 ? 34.361  -37.324 11.493   1.00 92.81  ? 386  GLN   B NE2  1 
ATOM   14853 H  H    . GLN   B  2  382 ? 34.898  -32.753 14.555   1.00 79.53  ? 386  GLN   B H    1 
ATOM   14854 H  HA   . GLN   B  2  382 ? 33.889  -32.263 12.098   1.00 77.45  ? 386  GLN   B HA   1 
ATOM   14855 H  HB2  . GLN   B  2  382 ? 32.889  -34.467 13.511   1.00 79.17  ? 386  GLN   B HB2  1 
ATOM   14856 H  HB3  . GLN   B  2  382 ? 32.775  -34.184 11.952   1.00 79.17  ? 386  GLN   B HB3  1 
ATOM   14857 H  HG2  . GLN   B  2  382 ? 34.867  -34.945 11.583   1.00 92.60  ? 386  GLN   B HG2  1 
ATOM   14858 H  HG3  . GLN   B  2  382 ? 35.190  -34.978 13.139   1.00 92.60  ? 386  GLN   B HG3  1 
ATOM   14859 H  HE21 . GLN   B  2  382 ? 34.799  -36.994 10.831   1.00 111.35 ? 386  GLN   B HE21 1 
ATOM   14860 H  HE22 . GLN   B  2  382 ? 34.125  -38.151 11.483   1.00 111.35 ? 386  GLN   B HE22 1 
ATOM   14861 N  N    . LYS   B  2  383 ? 31.460  -31.956 13.139   1.00 61.28  ? 387  LYS   B N    1 
ATOM   14862 C  CA   . LYS   B  2  383 ? 30.261  -31.467 13.803   1.00 61.61  ? 387  LYS   B CA   1 
ATOM   14863 C  C    . LYS   B  2  383 ? 29.267  -32.590 14.077   1.00 62.53  ? 387  LYS   B C    1 
ATOM   14864 O  O    . LYS   B  2  383 ? 28.066  -32.333 14.211   1.00 64.08  ? 387  LYS   B O    1 
ATOM   14865 C  CB   . LYS   B  2  383 ? 29.604  -30.367 12.968   1.00 61.62  ? 387  LYS   B CB   1 
ATOM   14866 C  CG   . LYS   B  2  383 ? 29.369  -30.753 11.516   1.00 71.07  ? 387  LYS   B CG   1 
ATOM   14867 C  CD   . LYS   B  2  383 ? 28.559  -29.703 10.770   1.00 80.15  ? 387  LYS   B CD   1 
ATOM   14868 C  CE   . LYS   B  2  383 ? 29.197  -28.326 10.867   1.00 86.94  ? 387  LYS   B CE   1 
ATOM   14869 N  NZ   . LYS   B  2  383 ? 28.577  -27.360 9.923    1.00 92.03  ? 387  LYS   B NZ   1 
ATOM   14870 H  H    . LYS   B  2  383 ? 31.318  -32.235 12.337   1.00 73.52  ? 387  LYS   B H    1 
ATOM   14871 H  HA   . LYS   B  2  383 ? 30.514  -31.079 14.656   1.00 73.91  ? 387  LYS   B HA   1 
ATOM   14872 H  HB2  . LYS   B  2  383 ? 28.743  -30.152 13.360   1.00 73.93  ? 387  LYS   B HB2  1 
ATOM   14873 H  HB3  . LYS   B  2  383 ? 30.177  -29.585 12.977   1.00 73.93  ? 387  LYS   B HB3  1 
ATOM   14874 H  HG2  . LYS   B  2  383 ? 30.224  -30.850 11.069   1.00 85.26  ? 387  LYS   B HG2  1 
ATOM   14875 H  HG3  . LYS   B  2  383 ? 28.881  -31.591 11.483   1.00 85.26  ? 387  LYS   B HG3  1 
ATOM   14876 H  HD2  . LYS   B  2  383 ? 28.504  -29.948 9.833    1.00 96.16  ? 387  LYS   B HD2  1 
ATOM   14877 H  HD3  . LYS   B  2  383 ? 27.669  -29.653 11.153   1.00 96.16  ? 387  LYS   B HD3  1 
ATOM   14878 H  HE2  . LYS   B  2  383 ? 29.085  -27.985 11.767   1.00 104.31 ? 387  LYS   B HE2  1 
ATOM   14879 H  HE3  . LYS   B  2  383 ? 30.141  -28.395 10.653   1.00 104.31 ? 387  LYS   B HE3  1 
ATOM   14880 H  HZ1  . LYS   B  2  383 ? 29.030  -26.594 9.931    1.00 110.42 ? 387  LYS   B HZ1  1 
ATOM   14881 H  HZ2  . LYS   B  2  383 ? 28.586  -27.692 9.097    1.00 110.42 ? 387  LYS   B HZ2  1 
ATOM   14882 H  HZ3  . LYS   B  2  383 ? 27.734  -27.200 10.161   1.00 110.42 ? 387  LYS   B HZ3  1 
ATOM   14883 N  N    . LYS   B  2  384 ? 29.740  -33.833 14.159   1.00 62.36  ? 388  LYS   B N    1 
ATOM   14884 C  CA   . LYS   B  2  384 ? 28.853  -34.961 14.395   1.00 65.28  ? 388  LYS   B CA   1 
ATOM   14885 C  C    . LYS   B  2  384 ? 29.551  -36.014 15.242   1.00 63.41  ? 388  LYS   B C    1 
ATOM   14886 O  O    . LYS   B  2  384 ? 30.749  -36.263 15.081   1.00 65.55  ? 388  LYS   B O    1 
ATOM   14887 C  CB   . LYS   B  2  384 ? 28.381  -35.591 13.079   1.00 76.89  ? 388  LYS   B CB   1 
ATOM   14888 C  CG   . LYS   B  2  384 ? 27.385  -36.721 13.280   1.00 90.24  ? 388  LYS   B CG   1 
ATOM   14889 C  CD   . LYS   B  2  384 ? 26.699  -37.118 11.987   1.00 98.60  ? 388  LYS   B CD   1 
ATOM   14890 C  CE   . LYS   B  2  384 ? 27.640  -37.840 11.042   1.00 104.68 ? 388  LYS   B CE   1 
ATOM   14891 N  NZ   . LYS   B  2  384 ? 26.915  -38.314 9.833    1.00 105.92 ? 388  LYS   B NZ   1 
ATOM   14892 H  H    . LYS   B  2  384 ? 30.570  -34.044 14.081   1.00 74.81  ? 388  LYS   B H    1 
ATOM   14893 H  HA   . LYS   B  2  384 ? 28.081  -34.645 14.890   1.00 78.32  ? 388  LYS   B HA   1 
ATOM   14894 H  HB2  . LYS   B  2  384 ? 27.953  -34.908 12.539   1.00 92.25  ? 388  LYS   B HB2  1 
ATOM   14895 H  HB3  . LYS   B  2  384 ? 29.150  -35.951 12.609   1.00 92.25  ? 388  LYS   B HB3  1 
ATOM   14896 H  HG2  . LYS   B  2  384 ? 27.850  -37.498 13.626   1.00 108.27 ? 388  LYS   B HG2  1 
ATOM   14897 H  HG3  . LYS   B  2  384 ? 26.703  -36.436 13.908   1.00 108.27 ? 388  LYS   B HG3  1 
ATOM   14898 H  HD2  . LYS   B  2  384 ? 25.958  -37.711 12.187   1.00 118.31 ? 388  LYS   B HD2  1 
ATOM   14899 H  HD3  . LYS   B  2  384 ? 26.375  -36.321 11.539   1.00 118.31 ? 388  LYS   B HD3  1 
ATOM   14900 H  HE2  . LYS   B  2  384 ? 28.345  -37.235 10.761   1.00 125.59 ? 388  LYS   B HE2  1 
ATOM   14901 H  HE3  . LYS   B  2  384 ? 28.023  -38.609 11.492   1.00 125.59 ? 388  LYS   B HE3  1 
ATOM   14902 H  HZ1  . LYS   B  2  384 ? 27.270  -39.078 9.545    1.00 127.09 ? 388  LYS   B HZ1  1 
ATOM   14903 H  HZ2  . LYS   B  2  384 ? 26.057  -38.448 10.025   1.00 127.09 ? 388  LYS   B HZ2  1 
ATOM   14904 H  HZ3  . LYS   B  2  384 ? 26.975  -37.706 9.185    1.00 127.09 ? 388  LYS   B HZ3  1 
ATOM   14905 N  N    . CYS   B  2  385 ? 28.786  -36.620 16.146   1.00 64.51  ? 389  CYS   B N    1 
ATOM   14906 C  CA   . CYS   B  2  385 ? 29.203  -37.786 16.911   1.00 70.35  ? 389  CYS   B CA   1 
ATOM   14907 C  C    . CYS   B  2  385 ? 28.313  -38.960 16.529   1.00 72.67  ? 389  CYS   B C    1 
ATOM   14908 O  O    . CYS   B  2  385 ? 27.098  -38.799 16.374   1.00 74.70  ? 389  CYS   B O    1 
ATOM   14909 C  CB   . CYS   B  2  385 ? 29.114  -37.524 18.414   1.00 76.52  ? 389  CYS   B CB   1 
ATOM   14910 S  SG   . CYS   B  2  385 ? 30.527  -36.639 19.091   1.00 90.19  ? 389  CYS   B SG   1 
ATOM   14911 H  H    . CYS   B  2  385 ? 27.989  -36.362 16.341   1.00 77.40  ? 389  CYS   B H    1 
ATOM   14912 H  HA   . CYS   B  2  385 ? 30.124  -38.011 16.705   1.00 84.41  ? 389  CYS   B HA   1 
ATOM   14913 H  HB2  . CYS   B  2  385 ? 28.322  -36.994 18.590   1.00 91.80  ? 389  CYS   B HB2  1 
ATOM   14914 H  HB3  . CYS   B  2  385 ? 29.052  -38.376 18.874   1.00 91.80  ? 389  CYS   B HB3  1 
ATOM   14915 H  HG   . CYS   B  2  385 ? 31.099  -36.075 18.200   1.00 108.21 ? 389  CYS   B HG   1 
ATOM   14916 N  N    . SER   B  2  386 ? 28.914  -40.138 16.377   1.00 75.37  ? 390  SER   B N    1 
ATOM   14917 C  CA   . SER   B  2  386 ? 28.212  -41.307 15.869   1.00 76.34  ? 390  SER   B CA   1 
ATOM   14918 C  C    . SER   B  2  386 ? 28.433  -42.497 16.793   1.00 78.32  ? 390  SER   B C    1 
ATOM   14919 O  O    . SER   B  2  386 ? 29.242  -42.454 17.723   1.00 77.36  ? 390  SER   B O    1 
ATOM   14920 C  CB   . SER   B  2  386 ? 28.676  -41.654 14.447   1.00 79.87  ? 390  SER   B CB   1 
ATOM   14921 O  OG   . SER   B  2  386 ? 28.748  -40.493 13.638   1.00 80.55  ? 390  SER   B OG   1 
ATOM   14922 H  H    . SER   B  2  386 ? 29.740  -40.283 16.566   1.00 90.42  ? 390  SER   B H    1 
ATOM   14923 H  HA   . SER   B  2  386 ? 27.261  -41.117 15.852   1.00 91.59  ? 390  SER   B HA   1 
ATOM   14924 H  HB2  . SER   B  2  386 ? 29.556  -42.061 14.493   1.00 95.83  ? 390  SER   B HB2  1 
ATOM   14925 H  HB3  . SER   B  2  386 ? 28.044  -42.275 14.052   1.00 95.83  ? 390  SER   B HB3  1 
ATOM   14926 H  HG   . SER   B  2  386 ? 29.247  -40.634 12.977   1.00 96.64  ? 390  SER   B HG   1 
ATOM   14927 N  N    . HIS   B  2  387 ? 27.690  -43.570 16.519   1.00 80.99  ? 391  HIS   B N    1 
ATOM   14928 C  CA   . HIS   B  2  387 ? 27.838  -44.835 17.239   1.00 87.76  ? 391  HIS   B CA   1 
ATOM   14929 C  C    . HIS   B  2  387 ? 27.602  -44.656 18.736   1.00 90.36  ? 391  HIS   B C    1 
ATOM   14930 O  O    . HIS   B  2  387 ? 28.313  -45.226 19.566   1.00 98.06  ? 391  HIS   B O    1 
ATOM   14931 C  CB   . HIS   B  2  387 ? 29.215  -45.452 16.987   1.00 96.65  ? 391  HIS   B CB   1 
ATOM   14932 C  CG   . HIS   B  2  387 ? 29.466  -45.812 15.556   1.00 103.50 ? 391  HIS   B CG   1 
ATOM   14933 N  ND1  . HIS   B  2  387 ? 29.978  -44.917 14.642   1.00 104.61 ? 391  HIS   B ND1  1 
ATOM   14934 C  CD2  . HIS   B  2  387 ? 29.278  -46.972 14.884   1.00 107.70 ? 391  HIS   B CD2  1 
ATOM   14935 C  CE1  . HIS   B  2  387 ? 30.094  -45.510 13.467   1.00 106.55 ? 391  HIS   B CE1  1 
ATOM   14936 N  NE2  . HIS   B  2  387 ? 29.675  -46.758 13.587   1.00 108.09 ? 391  HIS   B NE2  1 
ATOM   14937 H  H    . HIS   B  2  387 ? 27.083  -43.591 15.910   1.00 97.17  ? 391  HIS   B H    1 
ATOM   14938 H  HA   . HIS   B  2  387 ? 27.163  -45.449 16.909   1.00 105.29 ? 391  HIS   B HA   1 
ATOM   14939 H  HB2  . HIS   B  2  387 ? 29.896  -44.814 17.254   1.00 115.96 ? 391  HIS   B HB2  1 
ATOM   14940 H  HB3  . HIS   B  2  387 ? 29.295  -46.262 17.514   1.00 115.96 ? 391  HIS   B HB3  1 
ATOM   14941 H  HD2  . HIS   B  2  387 ? 28.942  -47.765 15.234   1.00 129.22 ? 391  HIS   B HD2  1 
ATOM   14942 H  HE1  . HIS   B  2  387 ? 30.415  -45.117 12.688   1.00 127.84 ? 391  HIS   B HE1  1 
ATOM   14943 H  HE2  . HIS   B  2  387 ? 29.655  -47.341 12.955   1.00 129.68 ? 391  HIS   B HE2  1 
ATOM   14944 N  N    . MET   B  2  388 ? 26.594  -43.863 19.087   1.00 86.23  ? 392  MET   B N    1 
ATOM   14945 C  CA   . MET   B  2  388 ? 26.285  -43.557 20.476   1.00 87.63  ? 392  MET   B CA   1 
ATOM   14946 C  C    . MET   B  2  388 ? 24.927  -44.131 20.857   1.00 86.44  ? 392  MET   B C    1 
ATOM   14947 O  O    . MET   B  2  388 ? 23.979  -44.091 20.067   1.00 85.89  ? 392  MET   B O    1 
ATOM   14948 C  CB   . MET   B  2  388 ? 26.300  -42.043 20.722   1.00 86.17  ? 392  MET   B CB   1 
ATOM   14949 C  CG   . MET   B  2  388 ? 25.386  -41.240 19.810   1.00 82.57  ? 392  MET   B CG   1 
ATOM   14950 S  SD   . MET   B  2  388 ? 25.670  -39.461 19.927   1.00 80.24  ? 392  MET   B SD   1 
ATOM   14951 C  CE   . MET   B  2  388 ? 25.372  -39.166 21.668   1.00 81.07  ? 392  MET   B CE   1 
ATOM   14952 H  H    . MET   B  2  388 ? 26.064  -43.485 18.525   1.00 103.46 ? 392  MET   B H    1 
ATOM   14953 H  HA   . MET   B  2  388 ? 26.961  -43.960 21.043   1.00 105.13 ? 392  MET   B HA   1 
ATOM   14954 H  HB2  . MET   B  2  388 ? 26.019  -41.877 21.635   1.00 103.38 ? 392  MET   B HB2  1 
ATOM   14955 H  HB3  . MET   B  2  388 ? 27.204  -41.718 20.588   1.00 103.38 ? 392  MET   B HB3  1 
ATOM   14956 H  HG2  . MET   B  2  388 ? 25.541  -41.509 18.891   1.00 99.07  ? 392  MET   B HG2  1 
ATOM   14957 H  HG3  . MET   B  2  388 ? 24.463  -41.413 20.055   1.00 99.07  ? 392  MET   B HG3  1 
ATOM   14958 H  HE1  . MET   B  2  388 ? 25.480  -38.219 21.851   1.00 97.27  ? 392  MET   B HE1  1 
ATOM   14959 H  HE2  . MET   B  2  388 ? 24.469  -39.444 21.886   1.00 97.27  ? 392  MET   B HE2  1 
ATOM   14960 H  HE3  . MET   B  2  388 ? 26.011  -39.678 22.189   1.00 97.27  ? 392  MET   B HE3  1 
ATOM   14961 N  N    . LYS   B  2  389 ? 24.847  -44.669 22.070   1.00 86.46  ? 393  LYS   B N    1 
ATOM   14962 C  CA   . LYS   B  2  389 ? 23.593  -45.172 22.605   1.00 87.20  ? 393  LYS   B CA   1 
ATOM   14963 C  C    . LYS   B  2  389 ? 22.709  -44.012 23.045   1.00 86.84  ? 393  LYS   B C    1 
ATOM   14964 O  O    . LYS   B  2  389 ? 23.193  -42.978 23.515   1.00 88.80  ? 393  LYS   B O    1 
ATOM   14965 C  CB   . LYS   B  2  389 ? 23.855  -46.109 23.786   1.00 94.45  ? 393  LYS   B CB   1 
ATOM   14966 C  CG   . LYS   B  2  389 ? 22.604  -46.674 24.447   1.00 100.29 ? 393  LYS   B CG   1 
ATOM   14967 C  CD   . LYS   B  2  389 ? 22.961  -47.562 25.633   1.00 108.79 ? 393  LYS   B CD   1 
ATOM   14968 C  CE   . LYS   B  2  389 ? 21.722  -48.130 26.309   1.00 111.97 ? 393  LYS   B CE   1 
ATOM   14969 N  NZ   . LYS   B  2  389 ? 22.070  -49.018 27.454   1.00 119.13 ? 393  LYS   B NZ   1 
ATOM   14970 H  H    . LYS   B  2  389 ? 25.514  -44.753 22.607   1.00 103.73 ? 393  LYS   B H    1 
ATOM   14971 H  HA   . LYS   B  2  389 ? 23.120  -45.676 21.924   1.00 104.62 ? 393  LYS   B HA   1 
ATOM   14972 H  HB2  . LYS   B  2  389 ? 24.383  -46.859 23.472   1.00 113.32 ? 393  LYS   B HB2  1 
ATOM   14973 H  HB3  . LYS   B  2  389 ? 24.346  -45.619 24.464   1.00 113.32 ? 393  LYS   B HB3  1 
ATOM   14974 H  HG2  . LYS   B  2  389 ? 22.050  -45.945 24.766   1.00 120.33 ? 393  LYS   B HG2  1 
ATOM   14975 H  HG3  . LYS   B  2  389 ? 22.112  -47.207 23.803   1.00 120.33 ? 393  LYS   B HG3  1 
ATOM   14976 H  HD2  . LYS   B  2  389 ? 23.505  -48.304 25.325   1.00 130.53 ? 393  LYS   B HD2  1 
ATOM   14977 H  HD3  . LYS   B  2  389 ? 23.452  -47.041 26.287   1.00 130.53 ? 393  LYS   B HD3  1 
ATOM   14978 H  HE2  . LYS   B  2  389 ? 21.180  -47.400 26.646   1.00 134.34 ? 393  LYS   B HE2  1 
ATOM   14979 H  HE3  . LYS   B  2  389 ? 21.216  -48.649 25.665   1.00 134.34 ? 393  LYS   B HE3  1 
ATOM   14980 H  HZ1  . LYS   B  2  389 ? 21.328  -49.337 27.829   1.00 142.94 ? 393  LYS   B HZ1  1 
ATOM   14981 H  HZ2  . LYS   B  2  389 ? 22.566  -49.700 27.170   1.00 142.94 ? 393  LYS   B HZ2  1 
ATOM   14982 H  HZ3  . LYS   B  2  389 ? 22.529  -48.562 28.065   1.00 142.94 ? 393  LYS   B HZ3  1 
ATOM   14983 N  N    . VAL   B  2  390 ? 21.397  -44.189 22.882   1.00 84.92  ? 394  VAL   B N    1 
ATOM   14984 C  CA   . VAL   B  2  390 ? 20.458  -43.161 23.312   1.00 82.59  ? 394  VAL   B CA   1 
ATOM   14985 C  C    . VAL   B  2  390 ? 20.641  -42.925 24.803   1.00 83.76  ? 394  VAL   B C    1 
ATOM   14986 O  O    . VAL   B  2  390 ? 20.708  -43.872 25.598   1.00 85.59  ? 394  VAL   B O    1 
ATOM   14987 C  CB   . VAL   B  2  390 ? 19.019  -43.568 22.969   1.00 81.99  ? 394  VAL   B CB   1 
ATOM   14988 C  CG1  . VAL   B  2  390 ? 18.033  -42.514 23.457   1.00 84.74  ? 394  VAL   B CG1  1 
ATOM   14989 C  CG2  . VAL   B  2  390 ? 18.875  -43.775 21.468   1.00 73.32  ? 394  VAL   B CG2  1 
ATOM   14990 H  H    . VAL   B  2  390 ? 21.033  -44.885 22.531   1.00 101.88 ? 394  VAL   B H    1 
ATOM   14991 H  HA   . VAL   B  2  390 ? 20.648  -42.334 22.843   1.00 99.09  ? 394  VAL   B HA   1 
ATOM   14992 H  HB   . VAL   B  2  390 ? 18.813  -44.404 23.417   1.00 98.37  ? 394  VAL   B HB   1 
ATOM   14993 H  HG11 . VAL   B  2  390 ? 17.138  -42.768 23.183   1.00 101.67 ? 394  VAL   B HG11 1 
ATOM   14994 H  HG12 . VAL   B  2  390 ? 18.080  -42.461 24.424   1.00 101.67 ? 394  VAL   B HG12 1 
ATOM   14995 H  HG13 . VAL   B  2  390 ? 18.269  -41.658 23.067   1.00 101.67 ? 394  VAL   B HG13 1 
ATOM   14996 H  HG21 . VAL   B  2  390 ? 17.951  -43.988 21.266   1.00 87.97  ? 394  VAL   B HG21 1 
ATOM   14997 H  HG22 . VAL   B  2  390 ? 19.134  -42.959 21.011   1.00 87.97  ? 394  VAL   B HG22 1 
ATOM   14998 H  HG23 . VAL   B  2  390 ? 19.451  -44.505 21.193   1.00 87.97  ? 394  VAL   B HG23 1 
ATOM   14999 N  N    . GLY   B  2  391 ? 20.724  -41.655 25.188   1.00 81.11  ? 395  GLY   B N    1 
ATOM   15000 C  CA   . GLY   B  2  391 ? 21.092  -41.265 26.526   1.00 84.60  ? 395  GLY   B CA   1 
ATOM   15001 C  C    . GLY   B  2  391 ? 22.529  -40.810 26.661   1.00 86.96  ? 395  GLY   B C    1 
ATOM   15002 O  O    . GLY   B  2  391 ? 22.852  -40.094 27.615   1.00 92.50  ? 395  GLY   B O    1 
ATOM   15003 H  H    . GLY   B  2  391 ? 20.566  -40.987 24.669   1.00 97.32  ? 395  GLY   B H    1 
ATOM   15004 H  HA2  . GLY   B  2  391 ? 20.518  -40.536 26.810   1.00 101.50 ? 395  GLY   B HA2  1 
ATOM   15005 H  HA3  . GLY   B  2  391 ? 20.960  -42.020 27.121   1.00 101.50 ? 395  GLY   B HA3  1 
ATOM   15006 N  N    . ASP   B  2  392 ? 23.396  -41.207 25.733   1.00 83.49  ? 396  ASP   B N    1 
ATOM   15007 C  CA   . ASP   B  2  392 ? 24.757  -40.695 25.716   1.00 81.70  ? 396  ASP   B CA   1 
ATOM   15008 C  C    . ASP   B  2  392 ? 24.757  -39.221 25.330   1.00 74.19  ? 396  ASP   B C    1 
ATOM   15009 O  O    . ASP   B  2  392 ? 23.884  -38.745 24.599   1.00 70.92  ? 396  ASP   B O    1 
ATOM   15010 C  CB   . ASP   B  2  392 ? 25.622  -41.488 24.738   1.00 83.49  ? 396  ASP   B CB   1 
ATOM   15011 C  CG   . ASP   B  2  392 ? 25.965  -42.868 25.252   1.00 91.42  ? 396  ASP   B CG   1 
ATOM   15012 O  OD1  . ASP   B  2  392 ? 26.047  -43.039 26.486   1.00 96.49  ? 396  ASP   B OD1  1 
ATOM   15013 O  OD2  . ASP   B  2  392 ? 26.157  -43.781 24.422   1.00 92.49  ? 396  ASP   B OD2  1 
ATOM   15014 H  H    . ASP   B  2  392 ? 23.220  -41.769 25.106   1.00 100.17 ? 396  ASP   B H    1 
ATOM   15015 H  HA   . ASP   B  2  392 ? 25.148  -40.786 26.599   1.00 98.02  ? 396  ASP   B HA   1 
ATOM   15016 H  HB2  . ASP   B  2  392 ? 25.142  -41.590 23.901   1.00 100.17 ? 396  ASP   B HB2  1 
ATOM   15017 H  HB3  . ASP   B  2  392 ? 26.451  -41.008 24.588   1.00 100.17 ? 396  ASP   B HB3  1 
ATOM   15018 N  N    . THR   B  2  393 ? 25.755  -38.499 25.828   1.00 73.95  ? 397  THR   B N    1 
ATOM   15019 C  CA   . THR   B  2  393 ? 25.878  -37.066 25.612   1.00 70.10  ? 397  THR   B CA   1 
ATOM   15020 C  C    . THR   B  2  393 ? 27.014  -36.787 24.638   1.00 69.46  ? 397  THR   B C    1 
ATOM   15021 O  O    . THR   B  2  393 ? 28.100  -37.366 24.756   1.00 72.44  ? 397  THR   B O    1 
ATOM   15022 C  CB   . THR   B  2  393 ? 26.127  -36.336 26.934   1.00 71.86  ? 397  THR   B CB   1 
ATOM   15023 O  OG1  . THR   B  2  393 ? 25.094  -36.674 27.869   1.00 73.97  ? 397  THR   B OG1  1 
ATOM   15024 C  CG2  . THR   B  2  393 ? 26.138  -34.830 26.727   1.00 72.00  ? 397  THR   B CG2  1 
ATOM   15025 H  H    . THR   B  2  393 ? 26.388  -38.828 26.308   1.00 88.72  ? 397  THR   B H    1 
ATOM   15026 H  HA   . THR   B  2  393 ? 25.057  -36.728 25.222   1.00 84.10  ? 397  THR   B HA   1 
ATOM   15027 H  HB   . THR   B  2  393 ? 26.990  -36.601 27.289   1.00 86.21  ? 397  THR   B HB   1 
ATOM   15028 H  HG1  . THR   B  2  393 ? 25.228  -36.281 28.599   1.00 88.74  ? 397  THR   B HG1  1 
ATOM   15029 H  HG21 . THR   B  2  393 ? 26.240  -34.378 27.579   1.00 86.38  ? 397  THR   B HG21 1 
ATOM   15030 H  HG22 . THR   B  2  393 ? 26.876  -34.580 26.148   1.00 86.38  ? 397  THR   B HG22 1 
ATOM   15031 H  HG23 . THR   B  2  393 ? 25.306  -34.545 26.317   1.00 86.38  ? 397  THR   B HG23 1 
ATOM   15032 N  N    . ALA   B  2  394 ? 26.758  -35.904 23.679   1.00 69.14  ? 398  ALA   B N    1 
ATOM   15033 C  CA   . ALA   B  2  394 ? 27.752  -35.482 22.702   1.00 69.81  ? 398  ALA   B CA   1 
ATOM   15034 C  C    . ALA   B  2  394 ? 28.051  -34.005 22.920   1.00 70.54  ? 398  ALA   B C    1 
ATOM   15035 O  O    . ALA   B  2  394 ? 27.150  -33.165 22.826   1.00 70.05  ? 398  ALA   B O    1 
ATOM   15036 C  CB   . ALA   B  2  394 ? 27.261  -35.727 21.275   1.00 66.62  ? 398  ALA   B CB   1 
ATOM   15037 H  H    . ALA   B  2  394 ? 25.993  -35.526 23.572   1.00 82.95  ? 398  ALA   B H    1 
ATOM   15038 H  HA   . ALA   B  2  394 ? 28.570  -35.987 22.832   1.00 83.75  ? 398  ALA   B HA   1 
ATOM   15039 H  HB1  . ALA   B  2  394 ? 27.942  -35.428 20.651   1.00 79.92  ? 398  ALA   B HB1  1 
ATOM   15040 H  HB2  . ALA   B  2  394 ? 27.097  -36.675 21.156   1.00 79.92  ? 398  ALA   B HB2  1 
ATOM   15041 H  HB3  . ALA   B  2  394 ? 26.441  -35.229 21.133   1.00 79.92  ? 398  ALA   B HB3  1 
ATOM   15042 N  N    . SER   B  2  395 ? 29.308  -33.696 23.216   1.00 71.77  ? 399  SER   B N    1 
ATOM   15043 C  CA   . SER   B  2  395 ? 29.754  -32.325 23.405   1.00 74.35  ? 399  SER   B CA   1 
ATOM   15044 C  C    . SER   B  2  395 ? 30.392  -31.801 22.125   1.00 73.62  ? 399  SER   B C    1 
ATOM   15045 O  O    . SER   B  2  395 ? 30.881  -32.562 21.287   1.00 76.40  ? 399  SER   B O    1 
ATOM   15046 C  CB   . SER   B  2  395 ? 30.750  -32.232 24.563   1.00 78.93  ? 399  SER   B CB   1 
ATOM   15047 O  OG   . SER   B  2  395 ? 30.163  -32.684 25.770   1.00 84.77  ? 399  SER   B OG   1 
ATOM   15048 H  H    . SER   B  2  395 ? 29.934  -34.277 23.314   1.00 86.11  ? 399  SER   B H    1 
ATOM   15049 H  HA   . SER   B  2  395 ? 28.993  -31.765 23.621   1.00 89.20  ? 399  SER   B HA   1 
ATOM   15050 H  HB2  . SER   B  2  395 ? 31.521  -32.784 24.361   1.00 94.70  ? 399  SER   B HB2  1 
ATOM   15051 H  HB3  . SER   B  2  395 ? 31.023  -31.307 24.671   1.00 94.70  ? 399  SER   B HB3  1 
ATOM   15052 H  HG   . SER   B  2  395 ? 29.352  -32.468 25.793   1.00 101.71 ? 399  SER   B HG   1 
ATOM   15053 N  N    . PHE   B  2  396 ? 30.377  -30.478 21.982   1.00 71.66  ? 400  PHE   B N    1 
ATOM   15054 C  CA   . PHE   B  2  396 ? 30.920  -29.826 20.799   1.00 71.19  ? 400  PHE   B CA   1 
ATOM   15055 C  C    . PHE   B  2  396 ? 31.583  -28.521 21.200   1.00 69.27  ? 400  PHE   B C    1 
ATOM   15056 O  O    . PHE   B  2  396 ? 31.014  -27.741 21.970   1.00 71.28  ? 400  PHE   B O    1 
ATOM   15057 C  CB   . PHE   B  2  396 ? 29.824  -29.556 19.763   1.00 68.69  ? 400  PHE   B CB   1 
ATOM   15058 C  CG   . PHE   B  2  396 ? 29.167  -30.798 19.245   1.00 68.35  ? 400  PHE   B CG   1 
ATOM   15059 C  CD1  . PHE   B  2  396 ? 29.724  -31.500 18.190   1.00 67.34  ? 400  PHE   B CD1  1 
ATOM   15060 C  CD2  . PHE   B  2  396 ? 27.996  -31.266 19.813   1.00 67.70  ? 400  PHE   B CD2  1 
ATOM   15061 C  CE1  . PHE   B  2  396 ? 29.124  -32.646 17.711   1.00 66.62  ? 400  PHE   B CE1  1 
ATOM   15062 C  CE2  . PHE   B  2  396 ? 27.390  -32.411 19.338   1.00 66.27  ? 400  PHE   B CE2  1 
ATOM   15063 C  CZ   . PHE   B  2  396 ? 27.955  -33.102 18.285   1.00 66.14  ? 400  PHE   B CZ   1 
ATOM   15064 H  H    . PHE   B  2  396 ? 30.054  -29.934 22.563   1.00 85.97  ? 400  PHE   B H    1 
ATOM   15065 H  HA   . PHE   B  2  396 ? 31.592  -30.400 20.400   1.00 85.41  ? 400  PHE   B HA   1 
ATOM   15066 H  HB2  . PHE   B  2  396 ? 29.137  -29.006 20.171   1.00 82.41  ? 400  PHE   B HB2  1 
ATOM   15067 H  HB3  . PHE   B  2  396 ? 30.216  -29.091 19.008   1.00 82.41  ? 400  PHE   B HB3  1 
ATOM   15068 H  HD1  . PHE   B  2  396 ? 30.512  -31.196 17.801   1.00 80.79  ? 400  PHE   B HD1  1 
ATOM   15069 H  HD2  . PHE   B  2  396 ? 27.612  -30.804 20.523   1.00 81.22  ? 400  PHE   B HD2  1 
ATOM   15070 H  HE1  . PHE   B  2  396 ? 29.507  -33.110 17.001   1.00 79.92  ? 400  PHE   B HE1  1 
ATOM   15071 H  HE2  . PHE   B  2  396 ? 26.603  -32.716 19.726   1.00 79.50  ? 400  PHE   B HE2  1 
ATOM   15072 H  HZ   . PHE   B  2  396 ? 27.548  -33.874 17.963   1.00 79.35  ? 400  PHE   B HZ   1 
ATOM   15073 N  N    . SER   B  2  397 ? 32.786  -28.295 20.682   1.00 64.99  ? 401  SER   B N    1 
ATOM   15074 C  CA   . SER   B  2  397 ? 33.476  -27.018 20.814   1.00 63.28  ? 401  SER   B CA   1 
ATOM   15075 C  C    . SER   B  2  397 ? 33.232  -26.235 19.530   1.00 59.16  ? 401  SER   B C    1 
ATOM   15076 O  O    . SER   B  2  397 ? 33.704  -26.625 18.457   1.00 61.93  ? 401  SER   B O    1 
ATOM   15077 C  CB   . SER   B  2  397 ? 34.968  -27.219 21.067   1.00 65.80  ? 401  SER   B CB   1 
ATOM   15078 O  OG   . SER   B  2  397 ? 35.192  -27.875 22.303   1.00 70.52  ? 401  SER   B OG   1 
ATOM   15079 H  H    . SER   B  2  397 ? 33.233  -28.881 20.240   1.00 77.97  ? 401  SER   B H    1 
ATOM   15080 H  HA   . SER   B  2  397 ? 33.116  -26.523 21.565   1.00 75.91  ? 401  SER   B HA   1 
ATOM   15081 H  HB2  . SER   B  2  397 ? 35.339  -27.759 20.352   1.00 78.94  ? 401  SER   B HB2  1 
ATOM   15082 H  HB3  . SER   B  2  397 ? 35.403  -26.352 21.088   1.00 78.94  ? 401  SER   B HB3  1 
ATOM   15083 H  HG   . SER   B  2  397 ? 34.889  -27.411 22.934   1.00 84.60  ? 401  SER   B HG   1 
ATOM   15084 N  N    . VAL   B  2  398 ? 32.485  -25.143 19.639   1.00 58.35  ? 402  VAL   B N    1 
ATOM   15085 C  CA   . VAL   B  2  398 ? 32.141  -24.295 18.506   1.00 61.25  ? 402  VAL   B CA   1 
ATOM   15086 C  C    . VAL   B  2  398 ? 32.905  -22.991 18.672   1.00 60.53  ? 402  VAL   B C    1 
ATOM   15087 O  O    . VAL   B  2  398 ? 32.574  -22.172 19.539   1.00 63.03  ? 402  VAL   B O    1 
ATOM   15088 C  CB   . VAL   B  2  398 ? 30.629  -24.046 18.416   1.00 63.07  ? 402  VAL   B CB   1 
ATOM   15089 C  CG1  . VAL   B  2  398 ? 30.295  -23.228 17.177   1.00 62.64  ? 402  VAL   B CG1  1 
ATOM   15090 C  CG2  . VAL   B  2  398 ? 29.873  -25.365 18.408   1.00 64.56  ? 402  VAL   B CG2  1 
ATOM   15091 H  H    . VAL   B  2  398 ? 32.155  -24.865 20.383   1.00 70.00  ? 402  VAL   B H    1 
ATOM   15092 H  HA   . VAL   B  2  398 ? 32.429  -24.722 17.683   1.00 73.48  ? 402  VAL   B HA   1 
ATOM   15093 H  HB   . VAL   B  2  398 ? 30.348  -23.540 19.194   1.00 75.66  ? 402  VAL   B HB   1 
ATOM   15094 H  HG11 . VAL   B  2  398 ? 29.332  -23.132 17.112   1.00 75.15  ? 402  VAL   B HG11 1 
ATOM   15095 H  HG12 . VAL   B  2  398 ? 30.711  -22.355 17.253   1.00 75.15  ? 402  VAL   B HG12 1 
ATOM   15096 H  HG13 . VAL   B  2  398 ? 30.634  -23.689 16.393   1.00 75.15  ? 402  VAL   B HG13 1 
ATOM   15097 H  HG21 . VAL   B  2  398 ? 28.924  -25.184 18.316   1.00 77.46  ? 402  VAL   B HG21 1 
ATOM   15098 H  HG22 . VAL   B  2  398 ? 30.182  -25.901 17.661   1.00 77.46  ? 402  VAL   B HG22 1 
ATOM   15099 H  HG23 . VAL   B  2  398 ? 30.041  -25.830 19.242   1.00 77.46  ? 402  VAL   B HG23 1 
ATOM   15100 N  N    . THR   B  2  399 ? 33.932  -22.797 17.850   1.00 58.57  ? 403  THR   B N    1 
ATOM   15101 C  CA   . THR   B  2  399 ? 34.708  -21.566 17.861   1.00 61.14  ? 403  THR   B CA   1 
ATOM   15102 C  C    . THR   B  2  399 ? 34.116  -20.596 16.848   1.00 64.36  ? 403  THR   B C    1 
ATOM   15103 O  O    . THR   B  2  399 ? 33.881  -20.961 15.691   1.00 65.80  ? 403  THR   B O    1 
ATOM   15104 C  CB   . THR   B  2  399 ? 36.178  -21.845 17.544   1.00 61.08  ? 403  THR   B CB   1 
ATOM   15105 O  OG1  . THR   B  2  399 ? 36.704  -22.777 18.498   1.00 64.37  ? 403  THR   B OG1  1 
ATOM   15106 C  CG2  . THR   B  2  399 ? 36.995  -20.559 17.596   1.00 61.99  ? 403  THR   B CG2  1 
ATOM   15107 H  H    . THR   B  2  399 ? 34.201  -23.372 17.270   1.00 70.26  ? 403  THR   B H    1 
ATOM   15108 H  HA   . THR   B  2  399 ? 34.670  -21.160 18.741   1.00 73.34  ? 403  THR   B HA   1 
ATOM   15109 H  HB   . THR   B  2  399 ? 36.249  -22.215 16.650   1.00 73.27  ? 403  THR   B HB   1 
ATOM   15110 H  HG1  . THR   B  2  399 ? 37.513  -22.933 18.331   1.00 77.22  ? 403  THR   B HG1  1 
ATOM   15111 H  HG21 . THR   B  2  399 ? 37.932  -20.754 17.435   1.00 74.37  ? 403  THR   B HG21 1 
ATOM   15112 H  HG22 . THR   B  2  399 ? 36.682  -19.939 16.919   1.00 74.37  ? 403  THR   B HG22 1 
ATOM   15113 H  HG23 . THR   B  2  399 ? 36.906  -20.144 18.468   1.00 74.37  ? 403  THR   B HG23 1 
ATOM   15114 N  N    . VAL   B  2  400 ? 33.875  -19.365 17.287   1.00 65.66  ? 404  VAL   B N    1 
ATOM   15115 C  CA   . VAL   B  2  400 ? 33.230  -18.340 16.477   1.00 65.63  ? 404  VAL   B CA   1 
ATOM   15116 C  C    . VAL   B  2  400 ? 34.143  -17.125 16.435   1.00 63.44  ? 404  VAL   B C    1 
ATOM   15117 O  O    . VAL   B  2  400 ? 34.634  -16.675 17.477   1.00 60.92  ? 404  VAL   B O    1 
ATOM   15118 C  CB   . VAL   B  2  400 ? 31.847  -17.964 17.037   1.00 68.41  ? 404  VAL   B CB   1 
ATOM   15119 C  CG1  . VAL   B  2  400 ? 31.159  -16.945 16.138   1.00 70.31  ? 404  VAL   B CG1  1 
ATOM   15120 C  CG2  . VAL   B  2  400 ? 30.986  -19.206 17.202   1.00 68.52  ? 404  VAL   B CG2  1 
ATOM   15121 H  H    . VAL   B  2  400 ? 34.083  -19.092 18.076   1.00 78.78  ? 404  VAL   B H    1 
ATOM   15122 H  HA   . VAL   B  2  400 ? 33.115  -18.669 15.571   1.00 78.74  ? 404  VAL   B HA   1 
ATOM   15123 H  HB   . VAL   B  2  400 ? 31.962  -17.558 17.911   1.00 82.08  ? 404  VAL   B HB   1 
ATOM   15124 H  HG11 . VAL   B  2  400 ? 30.276  -16.756 16.492   1.00 84.36  ? 404  VAL   B HG11 1 
ATOM   15125 H  HG12 . VAL   B  2  400 ? 31.689  -16.132 16.120   1.00 84.36  ? 404  VAL   B HG12 1 
ATOM   15126 H  HG13 . VAL   B  2  400 ? 31.086  -17.312 15.244   1.00 84.36  ? 404  VAL   B HG13 1 
ATOM   15127 H  HG21 . VAL   B  2  400 ? 30.114  -18.944 17.536   1.00 82.20  ? 404  VAL   B HG21 1 
ATOM   15128 H  HG22 . VAL   B  2  400 ? 30.894  -19.642 16.340   1.00 82.20  ? 404  VAL   B HG22 1 
ATOM   15129 H  HG23 . VAL   B  2  400 ? 31.415  -19.806 17.832   1.00 82.20  ? 404  VAL   B HG23 1 
ATOM   15130 N  N    . ASN   B  2  401 ? 34.369  -16.599 15.234   1.00 64.69  ? 405  ASN   B N    1 
ATOM   15131 C  CA   . ASN   B  2  401 ? 35.199  -15.420 15.042   1.00 70.07  ? 405  ASN   B CA   1 
ATOM   15132 C  C    . ASN   B  2  401 ? 34.546  -14.504 14.020   1.00 71.81  ? 405  ASN   B C    1 
ATOM   15133 O  O    . ASN   B  2  401 ? 34.014  -14.969 13.007   1.00 71.09  ? 405  ASN   B O    1 
ATOM   15134 C  CB   . ASN   B  2  401 ? 36.613  -15.796 14.575   1.00 72.62  ? 405  ASN   B CB   1 
ATOM   15135 C  CG   . ASN   B  2  401 ? 37.420  -14.590 14.134   1.00 72.02  ? 405  ASN   B CG   1 
ATOM   15136 O  OD1  . ASN   B  2  401 ? 37.802  -13.753 14.951   1.00 74.68  ? 405  ASN   B OD1  1 
ATOM   15137 N  ND2  . ASN   B  2  401 ? 37.686  -14.497 12.835   1.00 69.45  ? 405  ASN   B ND2  1 
ATOM   15138 H  H    . ASN   B  2  401 ? 34.045  -16.915 14.503   1.00 77.61  ? 405  ASN   B H    1 
ATOM   15139 H  HA   . ASN   B  2  401 ? 35.273  -14.939 15.880   1.00 84.06  ? 405  ASN   B HA   1 
ATOM   15140 H  HB2  . ASN   B  2  401 ? 37.085  -16.223 15.307   1.00 87.12  ? 405  ASN   B HB2  1 
ATOM   15141 H  HB3  . ASN   B  2  401 ? 36.547  -16.406 13.823   1.00 87.12  ? 405  ASN   B HB3  1 
ATOM   15142 H  HD21 . ASN   B  2  401 ? 38.141  -13.831 12.536   1.00 83.32  ? 405  ASN   B HD21 1 
ATOM   15143 H  HD22 . ASN   B  2  401 ? 37.404  -15.103 12.294   1.00 83.32  ? 405  ASN   B HD22 1 
ATOM   15144 N  N    . ILE   B  2  402 ? 34.587  -13.208 14.293   1.00 72.66  ? 406  ILE   B N    1 
ATOM   15145 C  CA   . ILE   B  2  402 ? 34.099  -12.175 13.383   1.00 77.34  ? 406  ILE   B CA   1 
ATOM   15146 C  C    . ILE   B  2  402 ? 35.319  -11.479 12.787   1.00 78.29  ? 406  ILE   B C    1 
ATOM   15147 O  O    . ILE   B  2  402 ? 36.139  -10.934 13.538   1.00 74.54  ? 406  ILE   B O    1 
ATOM   15148 C  CB   . ILE   B  2  402 ? 33.170  -11.178 14.101   1.00 81.65  ? 406  ILE   B CB   1 
ATOM   15149 C  CG1  . ILE   B  2  402 ? 32.651  -10.118 13.124   1.00 86.33  ? 406  ILE   B CG1  1 
ATOM   15150 C  CG2  . ILE   B  2  402 ? 33.869  -10.517 15.287   1.00 82.99  ? 406  ILE   B CG2  1 
ATOM   15151 C  CD1  . ILE   B  2  402 ? 31.663  -10.651 12.107   1.00 89.83  ? 406  ILE   B CD1  1 
ATOM   15152 H  H    . ILE   B  2  402 ? 34.904  -12.889 15.026   1.00 87.17  ? 406  ILE   B H    1 
ATOM   15153 H  HA   . ILE   B  2  402 ? 33.596  -12.582 12.661   1.00 92.78  ? 406  ILE   B HA   1 
ATOM   15154 H  HB   . ILE   B  2  402 ? 32.414  -11.681 14.442   1.00 97.96  ? 406  ILE   B HB   1 
ATOM   15155 H  HG12 . ILE   B  2  402 ? 32.206  -9.420  13.630   1.00 103.58 ? 406  ILE   B HG12 1 
ATOM   15156 H  HG13 . ILE   B  2  402 ? 33.404  -9.747  12.638   1.00 103.58 ? 406  ILE   B HG13 1 
ATOM   15157 H  HG21 . ILE   B  2  402 ? 33.231  -9.956  15.756   1.00 99.57  ? 406  ILE   B HG21 1 
ATOM   15158 H  HG22 . ILE   B  2  402 ? 34.203  -11.206 15.881   1.00 99.57  ? 406  ILE   B HG22 1 
ATOM   15159 H  HG23 . ILE   B  2  402 ? 34.605  -9.977  14.958   1.00 99.57  ? 406  ILE   B HG23 1 
ATOM   15160 H  HD11 . ILE   B  2  402 ? 31.407  -9.932  11.508   1.00 107.78 ? 406  ILE   B HD11 1 
ATOM   15161 H  HD12 . ILE   B  2  402 ? 32.083  -11.366 11.604   1.00 107.78 ? 406  ILE   B HD12 1 
ATOM   15162 H  HD13 . ILE   B  2  402 ? 30.882  -10.988 12.572   1.00 107.78 ? 406  ILE   B HD13 1 
ATOM   15163 N  N    . PRO   B  2  403 ? 35.502  -11.489 11.457   1.00 87.03  ? 407  PRO   B N    1 
ATOM   15164 C  CA   . PRO   B  2  403 ? 36.741  -10.936 10.890   1.00 92.24  ? 407  PRO   B CA   1 
ATOM   15165 C  C    . PRO   B  2  403 ? 36.879  -9.435  11.089   1.00 92.43  ? 407  PRO   B C    1 
ATOM   15166 O  O    . PRO   B  2  403 ? 37.904  -8.961  11.588   1.00 91.42  ? 407  PRO   B O    1 
ATOM   15167 C  CB   . PRO   B  2  403 ? 36.637  -11.289 9.398    1.00 98.20  ? 407  PRO   B CB   1 
ATOM   15168 C  CG   . PRO   B  2  403 ? 35.609  -12.367 9.315    1.00 97.16  ? 407  PRO   B CG   1 
ATOM   15169 C  CD   . PRO   B  2  403 ? 34.646  -12.087 10.418   1.00 92.36  ? 407  PRO   B CD   1 
ATOM   15170 H  HA   . PRO   B  2  403 ? 37.507  -11.381 11.285   1.00 110.67 ? 407  PRO   B HA   1 
ATOM   15171 H  HB2  . PRO   B  2  403 ? 36.361  -10.508 8.894    1.00 117.82 ? 407  PRO   B HB2  1 
ATOM   15172 H  HB3  . PRO   B  2  403 ? 37.496  -11.605 9.076    1.00 117.82 ? 407  PRO   B HB3  1 
ATOM   15173 H  HG2  . PRO   B  2  403 ? 35.166  -12.331 8.453    1.00 116.57 ? 407  PRO   B HG2  1 
ATOM   15174 H  HG3  . PRO   B  2  403 ? 36.030  -13.232 9.435    1.00 116.57 ? 407  PRO   B HG3  1 
ATOM   15175 H  HD2  . PRO   B  2  403 ? 33.961  -11.463 10.131   1.00 110.82 ? 407  PRO   B HD2  1 
ATOM   15176 H  HD3  . PRO   B  2  403 ? 34.236  -12.907 10.736   1.00 110.82 ? 407  PRO   B HD3  1 
ATOM   15177 N  N    . HIS   B  2  404 ? 35.854  -8.681  10.704   1.00 95.59  ? 408  HIS   B N    1 
ATOM   15178 C  CA   . HIS   B  2  404 ? 35.856  -7.228  10.776   1.00 100.30 ? 408  HIS   B CA   1 
ATOM   15179 C  C    . HIS   B  2  404 ? 34.758  -6.768  11.726   1.00 96.59  ? 408  HIS   B C    1 
ATOM   15180 O  O    . HIS   B  2  404 ? 33.878  -7.540  12.112   1.00 94.32  ? 408  HIS   B O    1 
ATOM   15181 C  CB   . HIS   B  2  404 ? 35.651  -6.612  9.387    1.00 112.55 ? 408  HIS   B CB   1 
ATOM   15182 C  CG   . HIS   B  2  404 ? 36.589  -7.144  8.349    1.00 124.39 ? 408  HIS   B CG   1 
ATOM   15183 N  ND1  . HIS   B  2  404 ? 36.163  -7.571  7.109    1.00 130.09 ? 408  HIS   B ND1  1 
ATOM   15184 C  CD2  . HIS   B  2  404 ? 37.932  -7.319  8.366    1.00 126.67 ? 408  HIS   B CD2  1 
ATOM   15185 C  CE1  . HIS   B  2  404 ? 37.202  -7.987  6.408    1.00 132.00 ? 408  HIS   B CE1  1 
ATOM   15186 N  NE2  . HIS   B  2  404 ? 38.288  -7.844  7.147    1.00 129.27 ? 408  HIS   B NE2  1 
ATOM   15187 H  H    . HIS   B  2  404 ? 35.122  -9.002  10.387   1.00 114.69 ? 408  HIS   B H    1 
ATOM   15188 H  HA   . HIS   B  2  404 ? 36.708  -6.919  11.121   1.00 120.34 ? 408  HIS   B HA   1 
ATOM   15189 H  HB2  . HIS   B  2  404 ? 34.746  -6.801  9.092    1.00 135.04 ? 408  HIS   B HB2  1 
ATOM   15190 H  HB3  . HIS   B  2  404 ? 35.788  -5.654  9.447    1.00 135.04 ? 408  HIS   B HB3  1 
ATOM   15191 H  HD2  . HIS   B  2  404 ? 38.505  -7.121  9.070    1.00 151.99 ? 408  HIS   B HD2  1 
ATOM   15192 H  HE1  . HIS   B  2  404 ? 37.175  -8.323  5.541    1.00 158.38 ? 408  HIS   B HE1  1 
ATOM   15193 H  HE2  . HIS   B  2  404 ? 39.088  -8.047  6.905    1.00 155.11 ? 408  HIS   B HE2  1 
ATOM   15194 N  N    . CYS   B  2  405 ? 34.810  -5.496  12.109   1.00 97.73  ? 409  CYS   B N    1 
ATOM   15195 C  CA   . CYS   B  2  405 ? 33.776  -4.963  12.982   1.00 97.50  ? 409  CYS   B CA   1 
ATOM   15196 C  C    . CYS   B  2  405 ? 32.502  -4.692  12.193   1.00 97.45  ? 409  CYS   B C    1 
ATOM   15197 O  O    . CYS   B  2  405 ? 32.534  -4.358  11.005   1.00 98.01  ? 409  CYS   B O    1 
ATOM   15198 C  CB   . CYS   B  2  405 ? 34.225  -3.676  13.674   1.00 101.27 ? 409  CYS   B CB   1 
ATOM   15199 S  SG   . CYS   B  2  405 ? 32.998  -3.103  14.879   1.00 108.27 ? 409  CYS   B SG   1 
ATOM   15200 H  H    . CYS   B  2  405 ? 35.421  -4.935  11.881   1.00 117.26 ? 409  CYS   B H    1 
ATOM   15201 H  HA   . CYS   B  2  405 ? 33.591  -5.618  13.673   1.00 116.98 ? 409  CYS   B HA   1 
ATOM   15202 H  HB2  . CYS   B  2  405 ? 35.060  -3.839  14.142   1.00 121.50 ? 409  CYS   B HB2  1 
ATOM   15203 H  HB3  . CYS   B  2  405 ? 34.348  -2.981  13.009   1.00 121.50 ? 409  CYS   B HB3  1 
ATOM   15204 N  N    . GLU   B  2  406 ? 31.371  -4.841  12.875   1.00 97.14  ? 410  GLU   B N    1 
ATOM   15205 C  CA   . GLU   B  2  406 ? 30.058  -4.600  12.302   1.00 99.00  ? 410  GLU   B CA   1 
ATOM   15206 C  C    . GLU   B  2  406 ? 29.240  -3.775  13.285   1.00 99.49  ? 410  GLU   B C    1 
ATOM   15207 O  O    . GLU   B  2  406 ? 29.666  -3.510  14.413   1.00 99.24  ? 410  GLU   B O    1 
ATOM   15208 C  CB   . GLU   B  2  406 ? 29.342  -5.917  11.980   1.00 97.98  ? 410  GLU   B CB   1 
ATOM   15209 C  CG   . GLU   B  2  406 ? 30.137  -6.854  11.087   1.00 98.29  ? 410  GLU   B CG   1 
ATOM   15210 C  CD   . GLU   B  2  406 ? 29.417  -8.165  10.832   1.00 100.80 ? 410  GLU   B CD   1 
ATOM   15211 O  OE1  . GLU   B  2  406 ? 28.431  -8.453  11.543   1.00 101.63 ? 410  GLU   B OE1  1 
ATOM   15212 O  OE2  . GLU   B  2  406 ? 29.834  -8.908  9.918    1.00 102.40 ? 410  GLU   B OE2  1 
ATOM   15213 H  H    . GLU   B  2  406 ? 31.341  -5.089  13.698   1.00 116.55 ? 410  GLU   B H    1 
ATOM   15214 H  HA   . GLU   B  2  406 ? 30.147  -4.098  11.477   1.00 118.78 ? 410  GLU   B HA   1 
ATOM   15215 H  HB2  . GLU   B  2  406 ? 29.162  -6.384  12.811   1.00 117.55 ? 410  GLU   B HB2  1 
ATOM   15216 H  HB3  . GLU   B  2  406 ? 28.509  -5.714  11.526   1.00 117.55 ? 410  GLU   B HB3  1 
ATOM   15217 H  HG2  . GLU   B  2  406 ? 30.290  -6.423  10.232   1.00 117.93 ? 410  GLU   B HG2  1 
ATOM   15218 H  HG3  . GLU   B  2  406 ? 30.985  -7.054  11.514   1.00 117.93 ? 410  GLU   B HG3  1 
ATOM   15219 N  N    . ARG   B  2  407 ? 28.051  -3.364  12.845   1.00 100.70 ? 411  ARG   B N    1 
ATOM   15220 C  CA   . ARG   B  2  407 ? 27.122  -2.626  13.694   1.00 103.57 ? 411  ARG   B CA   1 
ATOM   15221 C  C    . ARG   B  2  407 ? 25.994  -3.516  14.204   1.00 105.88 ? 411  ARG   B C    1 
ATOM   15222 O  O    . ARG   B  2  407 ? 25.784  -3.624  15.416   1.00 105.91 ? 411  ARG   B O    1 
ATOM   15223 C  CB   . ARG   B  2  407 ? 26.542  -1.425  12.935   1.00 108.73 ? 411  ARG   B CB   1 
ATOM   15224 C  CG   . ARG   B  2  407 ? 27.397  -0.174  13.023   1.00 112.12 ? 411  ARG   B CG   1 
ATOM   15225 C  CD   . ARG   B  2  407 ? 26.681  1.055   12.476   1.00 123.53 ? 411  ARG   B CD   1 
ATOM   15226 N  NE   . ARG   B  2  407 ? 25.451  1.359   13.208   1.00 132.35 ? 411  ARG   B NE   1 
ATOM   15227 C  CZ   . ARG   B  2  407 ? 24.217  1.222   12.725   1.00 140.70 ? 411  ARG   B CZ   1 
ATOM   15228 N  NH1  . ARG   B  2  407 ? 23.179  1.530   13.490   1.00 144.01 ? 411  ARG   B NH1  1 
ATOM   15229 N  NH2  . ARG   B  2  407 ? 24.006  0.790   11.487   1.00 144.47 ? 411  ARG   B NH2  1 
ATOM   15230 H  H    . ARG   B  2  407 ? 27.758  -3.502  12.048   1.00 120.82 ? 411  ARG   B H    1 
ATOM   15231 H  HA   . ARG   B  2  407 ? 27.614  -2.288  14.459   1.00 124.26 ? 411  ARG   B HA   1 
ATOM   15232 H  HB2  . ARG   B  2  407 ? 26.456  -1.660  11.998   1.00 130.46 ? 411  ARG   B HB2  1 
ATOM   15233 H  HB3  . ARG   B  2  407 ? 25.670  -1.214  13.305   1.00 130.46 ? 411  ARG   B HB3  1 
ATOM   15234 H  HG2  . ARG   B  2  407 ? 27.620  -0.005  13.951   1.00 134.52 ? 411  ARG   B HG2  1 
ATOM   15235 H  HG3  . ARG   B  2  407 ? 28.207  -0.306  12.506   1.00 134.52 ? 411  ARG   B HG3  1 
ATOM   15236 H  HD2  . ARG   B  2  407 ? 27.270  1.823   12.546   1.00 148.21 ? 411  ARG   B HD2  1 
ATOM   15237 H  HD3  . ARG   B  2  407 ? 26.448  0.900   11.547   1.00 148.21 ? 411  ARG   B HD3  1 
ATOM   15238 H  HE   . ARG   B  2  407 ? 25.531  1.649   14.014   1.00 158.80 ? 411  ARG   B HE   1 
ATOM   15239 H  HH11 . ARG   B  2  407 ? 23.305  1.817   14.291   1.00 172.79 ? 411  ARG   B HH11 1 
ATOM   15240 H  HH12 . ARG   B  2  407 ? 22.379  1.444   13.184   1.00 172.79 ? 411  ARG   B HH12 1 
ATOM   15241 H  HH21 . ARG   B  2  407 ? 24.673  0.594   10.980   1.00 173.34 ? 411  ARG   B HH21 1 
ATOM   15242 H  HH22 . ARG   B  2  407 ? 23.203  0.708   11.191   1.00 173.34 ? 411  ARG   B HH22 1 
ATOM   15243 N  N    . ARG   B  2  408 ? 25.267  -4.164  13.300   1.00 109.06 ? 412  ARG   B N    1 
ATOM   15244 C  CA   . ARG   B  2  408 ? 24.144  -4.989  13.714   1.00 111.04 ? 412  ARG   B CA   1 
ATOM   15245 C  C    . ARG   B  2  408 ? 24.634  -6.258  14.399   1.00 98.77  ? 412  ARG   B C    1 
ATOM   15246 O  O    . ARG   B  2  408 ? 25.710  -6.782  14.098   1.00 92.36  ? 412  ARG   B O    1 
ATOM   15247 C  CB   . ARG   B  2  408 ? 23.269  -5.361  12.516   1.00 122.93 ? 412  ARG   B CB   1 
ATOM   15248 C  CG   . ARG   B  2  408 ? 22.685  -4.175  11.766   1.00 140.03 ? 412  ARG   B CG   1 
ATOM   15249 C  CD   . ARG   B  2  408 ? 21.421  -4.574  11.016   1.00 152.69 ? 412  ARG   B CD   1 
ATOM   15250 N  NE   . ARG   B  2  408 ? 21.243  -3.827  9.773    1.00 164.88 ? 412  ARG   B NE   1 
ATOM   15251 C  CZ   . ARG   B  2  408 ? 20.532  -2.708  9.650    1.00 175.96 ? 412  ARG   B CZ   1 
ATOM   15252 N  NH1  . ARG   B  2  408 ? 20.439  -2.119  8.467    1.00 181.36 ? 412  ARG   B NH1  1 
ATOM   15253 N  NH2  . ARG   B  2  408 ? 19.915  -2.174  10.697   1.00 180.46 ? 412  ARG   B NH2  1 
ATOM   15254 H  H    . ARG   B  2  408 ? 25.403  -4.142  12.451   1.00 130.85 ? 412  ARG   B H    1 
ATOM   15255 H  HA   . ARG   B  2  408 ? 23.599  -4.488  14.341   1.00 133.23 ? 412  ARG   B HA   1 
ATOM   15256 H  HB2  . ARG   B  2  408 ? 23.807  -5.868  11.888   1.00 147.49 ? 412  ARG   B HB2  1 
ATOM   15257 H  HB3  . ARG   B  2  408 ? 22.529  -5.902  12.831   1.00 147.49 ? 412  ARG   B HB3  1 
ATOM   15258 H  HG2  . ARG   B  2  408 ? 22.459  -3.473  12.397   1.00 168.02 ? 412  ARG   B HG2  1 
ATOM   15259 H  HG3  . ARG   B  2  408 ? 23.333  -3.848  11.123   1.00 168.02 ? 412  ARG   B HG3  1 
ATOM   15260 H  HD2  . ARG   B  2  408 ? 21.469  -5.517  10.795   1.00 183.20 ? 412  ARG   B HD2  1 
ATOM   15261 H  HD3  . ARG   B  2  408 ? 20.651  -4.405  11.581   1.00 183.20 ? 412  ARG   B HD3  1 
ATOM   15262 H  HE   . ARG   B  2  408 ? 21.628  -4.133  9.067    1.00 197.84 ? 412  ARG   B HE   1 
ATOM   15263 H  HH11 . ARG   B  2  408 ? 20.837  -2.459  7.785    1.00 217.61 ? 412  ARG   B HH11 1 
ATOM   15264 H  HH12 . ARG   B  2  408 ? 19.981  -1.396  8.381    1.00 217.61 ? 412  ARG   B HH12 1 
ATOM   15265 H  HH21 . ARG   B  2  408 ? 19.971  -2.551  11.468   1.00 216.54 ? 412  ARG   B HH21 1 
ATOM   15266 H  HH22 . ARG   B  2  408 ? 19.459  -1.451  10.604   1.00 216.54 ? 412  ARG   B HH22 1 
ATOM   15267 N  N    . SER   B  2  409 ? 23.829  -6.748  15.335   1.00 97.93  ? 413  SER   B N    1 
ATOM   15268 C  CA   . SER   B  2  409 ? 24.084  -8.042  15.942   1.00 93.66  ? 413  SER   B CA   1 
ATOM   15269 C  C    . SER   B  2  409 ? 23.502  -9.146  15.066   1.00 88.59  ? 413  SER   B C    1 
ATOM   15270 O  O    . SER   B  2  409 ? 22.627  -8.915  14.227   1.00 90.15  ? 413  SER   B O    1 
ATOM   15271 C  CB   . SER   B  2  409 ? 23.484  -8.107  17.346   1.00 99.28  ? 413  SER   B CB   1 
ATOM   15272 O  OG   . SER   B  2  409 ? 24.081  -7.147  18.202   1.00 104.05 ? 413  SER   B OG   1 
ATOM   15273 H  H    . SER   B  2  409 ? 23.129  -6.348  15.635   1.00 117.49 ? 413  SER   B H    1 
ATOM   15274 H  HA   . SER   B  2  409 ? 25.040  -8.184  16.026   1.00 112.38 ? 413  SER   B HA   1 
ATOM   15275 H  HB2  . SER   B  2  409 ? 22.532  -7.930  17.290   1.00 119.11 ? 413  SER   B HB2  1 
ATOM   15276 H  HB3  . SER   B  2  409 ? 23.636  -8.992  17.712   1.00 119.11 ? 413  SER   B HB3  1 
ATOM   15277 H  HG   . SER   B  2  409 ? 24.392  -7.525  18.885   1.00 124.84 ? 413  SER   B HG   1 
ATOM   15278 N  N    . ARG   B  2  410 ? 24.006  -10.359 15.266   1.00 79.61  ? 414  ARG   B N    1 
ATOM   15279 C  CA   . ARG   B  2  410 ? 23.590  -11.523 14.497   1.00 79.07  ? 414  ARG   B CA   1 
ATOM   15280 C  C    . ARG   B  2  410 ? 22.778  -12.456 15.381   1.00 77.23  ? 414  ARG   B C    1 
ATOM   15281 O  O    . ARG   B  2  410 ? 23.196  -12.780 16.498   1.00 76.76  ? 414  ARG   B O    1 
ATOM   15282 C  CB   . ARG   B  2  410 ? 24.801  -12.265 13.931   1.00 80.19  ? 414  ARG   B CB   1 
ATOM   15283 C  CG   . ARG   B  2  410 ? 25.579  -11.489 12.887   1.00 82.68  ? 414  ARG   B CG   1 
ATOM   15284 C  CD   . ARG   B  2  410 ? 26.998  -12.016 12.776   1.00 85.84  ? 414  ARG   B CD   1 
ATOM   15285 N  NE   . ARG   B  2  410 ? 27.669  -11.559 11.563   1.00 90.63  ? 414  ARG   B NE   1 
ATOM   15286 C  CZ   . ARG   B  2  410 ? 27.682  -12.224 10.410   1.00 95.97  ? 414  ARG   B CZ   1 
ATOM   15287 N  NH1  . ARG   B  2  410 ? 27.057  -13.390 10.293   1.00 97.53  ? 414  ARG   B NH1  1 
ATOM   15288 N  NH2  . ARG   B  2  410 ? 28.325  -11.718 9.367    1.00 98.06  ? 414  ARG   B NH2  1 
ATOM   15289 H  H    . ARG   B  2  410 ? 24.605  -10.536 15.858   1.00 95.52  ? 414  ARG   B H    1 
ATOM   15290 H  HA   . ARG   B  2  410 ? 23.031  -11.235 13.759   1.00 94.86  ? 414  ARG   B HA   1 
ATOM   15291 H  HB2  . ARG   B  2  410 ? 25.408  -12.468 14.659   1.00 96.21  ? 414  ARG   B HB2  1 
ATOM   15292 H  HB3  . ARG   B  2  410 ? 24.494  -13.087 13.517   1.00 96.21  ? 414  ARG   B HB3  1 
ATOM   15293 H  HG2  . ARG   B  2  410 ? 25.147  -11.582 12.024   1.00 99.20  ? 414  ARG   B HG2  1 
ATOM   15294 H  HG3  . ARG   B  2  410 ? 25.616  -10.553 13.140   1.00 99.20  ? 414  ARG   B HG3  1 
ATOM   15295 H  HD2  . ARG   B  2  410 ? 27.512  -11.707 13.539   1.00 102.99 ? 414  ARG   B HD2  1 
ATOM   15296 H  HD3  . ARG   B  2  410 ? 26.976  -12.986 12.761   1.00 102.99 ? 414  ARG   B HD3  1 
ATOM   15297 H  HE   . ARG   B  2  410 ? 28.085  -10.807 11.595   1.00 108.74 ? 414  ARG   B HE   1 
ATOM   15298 H  HH11 . ARG   B  2  410 ? 26.638  -13.723 10.966   1.00 117.01 ? 414  ARG   B HH11 1 
ATOM   15299 H  HH12 . ARG   B  2  410 ? 27.072  -13.812 9.543    1.00 117.01 ? 414  ARG   B HH12 1 
ATOM   15300 H  HH21 . ARG   B  2  410 ? 28.731  -10.964 9.437    1.00 117.66 ? 414  ARG   B HH21 1 
ATOM   15301 H  HH22 . ARG   B  2  410 ? 28.336  -12.145 8.620    1.00 117.66 ? 414  ARG   B HH22 1 
ATOM   15302 N  N    . HIS   B  2  411 ? 21.623  -12.882 14.881   1.00 77.37  ? 415  HIS   B N    1 
ATOM   15303 C  CA   . HIS   B  2  411 ? 20.800  -13.888 15.538   1.00 75.33  ? 415  HIS   B CA   1 
ATOM   15304 C  C    . HIS   B  2  411 ? 21.111  -15.240 14.907   1.00 71.85  ? 415  HIS   B C    1 
ATOM   15305 O  O    . HIS   B  2  411 ? 20.950  -15.416 13.694   1.00 72.59  ? 415  HIS   B O    1 
ATOM   15306 C  CB   . HIS   B  2  411 ? 19.316  -13.550 15.408   1.00 79.09  ? 415  HIS   B CB   1 
ATOM   15307 C  CG   . HIS   B  2  411 ? 18.927  -12.276 16.093   1.00 88.04  ? 415  HIS   B CG   1 
ATOM   15308 N  ND1  . HIS   B  2  411 ? 18.293  -12.252 17.317   1.00 91.13  ? 415  HIS   B ND1  1 
ATOM   15309 C  CD2  . HIS   B  2  411 ? 19.089  -10.982 15.729   1.00 92.16  ? 415  HIS   B CD2  1 
ATOM   15310 C  CE1  . HIS   B  2  411 ? 18.077  -10.999 17.675   1.00 93.57  ? 415  HIS   B CE1  1 
ATOM   15311 N  NE2  . HIS   B  2  411 ? 18.551  -10.208 16.729   1.00 93.36  ? 415  HIS   B NE2  1 
ATOM   15312 H  H    . HIS   B  2  411 ? 21.287  -12.594 14.143   1.00 92.83  ? 415  HIS   B H    1 
ATOM   15313 H  HA   . HIS   B  2  411 ? 21.011  -13.929 16.483   1.00 90.38  ? 415  HIS   B HA   1 
ATOM   15314 H  HB2  . HIS   B  2  411 ? 19.097  -13.459 14.467   1.00 94.88  ? 415  HIS   B HB2  1 
ATOM   15315 H  HB3  . HIS   B  2  411 ? 18.796  -14.268 15.801   1.00 94.88  ? 415  HIS   B HB3  1 
ATOM   15316 H  HD2  . HIS   B  2  411 ? 19.489  -10.674 14.948   1.00 110.58 ? 415  HIS   B HD2  1 
ATOM   15317 H  HE1  . HIS   B  2  411 ? 17.663  -10.720 18.459   1.00 112.27 ? 415  HIS   B HE1  1 
ATOM   15318 H  HE2  . HIS   B  2  411 ? 18.527  -9.349  16.737   1.00 112.02 ? 415  HIS   B HE2  1 
ATOM   15319 N  N    . ILE   B  2  412 ? 21.565  -16.186 15.726   1.00 69.95  ? 416  ILE   B N    1 
ATOM   15320 C  CA   . ILE   B  2  412 ? 22.037  -17.477 15.246   1.00 70.13  ? 416  ILE   B CA   1 
ATOM   15321 C  C    . ILE   B  2  412 ? 21.427  -18.578 16.100   1.00 72.56  ? 416  ILE   B C    1 
ATOM   15322 O  O    . ILE   B  2  412 ? 21.155  -18.391 17.290   1.00 75.80  ? 416  ILE   B O    1 
ATOM   15323 C  CB   . ILE   B  2  412 ? 23.582  -17.554 15.268   1.00 68.93  ? 416  ILE   B CB   1 
ATOM   15324 C  CG1  . ILE   B  2  412 ? 24.170  -16.507 14.318   1.00 68.96  ? 416  ILE   B CG1  1 
ATOM   15325 C  CG2  . ILE   B  2  412 ? 24.065  -18.951 14.891   1.00 70.59  ? 416  ILE   B CG2  1 
ATOM   15326 C  CD1  . ILE   B  2  412 ? 25.665  -16.332 14.442   1.00 68.26  ? 416  ILE   B CD1  1 
ATOM   15327 H  H    . ILE   B  2  412 ? 21.610  -16.099 16.580   1.00 83.92  ? 416  ILE   B H    1 
ATOM   15328 H  HA   . ILE   B  2  412 ? 21.735  -17.612 14.334   1.00 84.14  ? 416  ILE   B HA   1 
ATOM   15329 H  HB   . ILE   B  2  412 ? 23.884  -17.367 16.170   1.00 82.70  ? 416  ILE   B HB   1 
ATOM   15330 H  HG12 . ILE   B  2  412 ? 23.979  -16.773 13.405   1.00 82.74  ? 416  ILE   B HG12 1 
ATOM   15331 H  HG13 . ILE   B  2  412 ? 23.757  -15.650 14.507   1.00 82.74  ? 416  ILE   B HG13 1 
ATOM   15332 H  HG21 . ILE   B  2  412 ? 25.034  -18.949 14.847   1.00 84.69  ? 416  ILE   B HG21 1 
ATOM   15333 H  HG22 . ILE   B  2  412 ? 23.765  -19.581 15.564   1.00 84.69  ? 416  ILE   B HG22 1 
ATOM   15334 H  HG23 . ILE   B  2  412 ? 23.695  -19.190 14.026   1.00 84.69  ? 416  ILE   B HG23 1 
ATOM   15335 H  HD11 . ILE   B  2  412 ? 25.944  -15.592 13.880   1.00 81.89  ? 416  ILE   B HD11 1 
ATOM   15336 H  HD12 . ILE   B  2  412 ? 25.886  -16.146 15.368   1.00 81.89  ? 416  ILE   B HD12 1 
ATOM   15337 H  HD13 . ILE   B  2  412 ? 26.103  -17.149 14.156   1.00 81.89  ? 416  ILE   B HD13 1 
ATOM   15338 N  N    . ILE   B  2  413 ? 21.213  -19.734 15.477   1.00 69.72  ? 417  ILE   B N    1 
ATOM   15339 C  CA   . ILE   B  2  413 ? 20.672  -20.911 16.143   1.00 65.36  ? 417  ILE   B CA   1 
ATOM   15340 C  C    . ILE   B  2  413 ? 21.643  -22.065 15.944   1.00 62.72  ? 417  ILE   B C    1 
ATOM   15341 O  O    . ILE   B  2  413 ? 22.089  -22.323 14.820   1.00 64.15  ? 417  ILE   B O    1 
ATOM   15342 C  CB   . ILE   B  2  413 ? 19.274  -21.280 15.611   1.00 67.74  ? 417  ILE   B CB   1 
ATOM   15343 C  CG1  . ILE   B  2  413 ? 18.234  -20.293 16.149   1.00 71.99  ? 417  ILE   B CG1  1 
ATOM   15344 C  CG2  . ILE   B  2  413 ? 18.925  -22.722 15.987   1.00 69.09  ? 417  ILE   B CG2  1 
ATOM   15345 C  CD1  . ILE   B  2  413 ? 16.826  -20.521 15.633   1.00 78.60  ? 417  ILE   B CD1  1 
ATOM   15346 H  H    . ILE   B  2  413 ? 21.379  -19.862 14.643   1.00 83.65  ? 417  ILE   B H    1 
ATOM   15347 H  HA   . ILE   B  2  413 ? 20.600  -20.731 17.094   1.00 78.41  ? 417  ILE   B HA   1 
ATOM   15348 H  HB   . ILE   B  2  413 ? 19.276  -21.218 14.643   1.00 81.26  ? 417  ILE   B HB   1 
ATOM   15349 H  HG12 . ILE   B  2  413 ? 18.207  -20.369 17.116   1.00 86.37  ? 417  ILE   B HG12 1 
ATOM   15350 H  HG13 . ILE   B  2  413 ? 18.498  -19.395 15.894   1.00 86.37  ? 417  ILE   B HG13 1 
ATOM   15351 H  HG21 . ILE   B  2  413 ? 17.988  -22.881 15.792   1.00 82.89  ? 417  ILE   B HG21 1 
ATOM   15352 H  HG22 . ILE   B  2  413 ? 19.478  -23.327 15.468   1.00 82.89  ? 417  ILE   B HG22 1 
ATOM   15353 H  HG23 . ILE   B  2  413 ? 19.092  -22.851 16.934   1.00 82.89  ? 417  ILE   B HG23 1 
ATOM   15354 H  HD11 . ILE   B  2  413 ? 16.262  -19.786 15.920   1.00 94.30  ? 417  ILE   B HD11 1 
ATOM   15355 H  HD12 . ILE   B  2  413 ? 16.848  -20.561 14.664   1.00 94.30  ? 417  ILE   B HD12 1 
ATOM   15356 H  HD13 . ILE   B  2  413 ? 16.489  -21.357 15.991   1.00 94.30  ? 417  ILE   B HD13 1 
ATOM   15357 N  N    . ILE   B  2  414 ? 21.968  -22.751 17.036   1.00 59.07  ? 418  ILE   B N    1 
ATOM   15358 C  CA   . ILE   B  2  414 ? 22.714  -24.002 17.008   1.00 60.16  ? 418  ILE   B CA   1 
ATOM   15359 C  C    . ILE   B  2  414 ? 21.782  -25.081 17.536   1.00 63.26  ? 418  ILE   B C    1 
ATOM   15360 O  O    . ILE   B  2  414 ? 21.300  -24.986 18.672   1.00 64.62  ? 418  ILE   B O    1 
ATOM   15361 C  CB   . ILE   B  2  414 ? 24.000  -23.930 17.846   1.00 61.07  ? 418  ILE   B CB   1 
ATOM   15362 C  CG1  . ILE   B  2  414 ? 24.875  -22.766 17.375   1.00 61.19  ? 418  ILE   B CG1  1 
ATOM   15363 C  CG2  . ILE   B  2  414 ? 24.766  -25.249 17.758   1.00 56.85  ? 418  ILE   B CG2  1 
ATOM   15364 C  CD1  . ILE   B  2  414 ? 26.096  -22.525 18.239   1.00 63.37  ? 418  ILE   B CD1  1 
ATOM   15365 H  H    . ILE   B  2  414 ? 21.758  -22.502 17.832   1.00 70.86  ? 418  ILE   B H    1 
ATOM   15366 H  HA   . ILE   B  2  414 ? 22.968  -24.215 16.096   1.00 72.18  ? 418  ILE   B HA   1 
ATOM   15367 H  HB   . ILE   B  2  414 ? 23.757  -23.776 18.772   1.00 73.27  ? 418  ILE   B HB   1 
ATOM   15368 H  HG12 . ILE   B  2  414 ? 25.183  -22.953 16.475   1.00 73.41  ? 418  ILE   B HG12 1 
ATOM   15369 H  HG13 . ILE   B  2  414 ? 24.344  -21.955 17.382   1.00 73.41  ? 418  ILE   B HG13 1 
ATOM   15370 H  HG21 . ILE   B  2  414 ? 25.563  -25.189 18.307   1.00 68.20  ? 418  ILE   B HG21 1 
ATOM   15371 H  HG22 . ILE   B  2  414 ? 24.197  -25.967 18.079   1.00 68.20  ? 418  ILE   B HG22 1 
ATOM   15372 H  HG23 . ILE   B  2  414 ? 25.012  -25.411 16.834   1.00 68.20  ? 418  ILE   B HG23 1 
ATOM   15373 H  HD11 . ILE   B  2  414 ? 26.553  -21.730 17.924   1.00 76.02  ? 418  ILE   B HD11 1 
ATOM   15374 H  HD12 . ILE   B  2  414 ? 25.813  -22.402 19.158   1.00 76.02  ? 418  ILE   B HD12 1 
ATOM   15375 H  HD13 . ILE   B  2  414 ? 26.685  -23.293 18.174   1.00 76.02  ? 418  ILE   B HD13 1 
ATOM   15376 N  N    . LYS   B  2  415 ? 21.522  -26.094 16.720   1.00 61.96  ? 419  LYS   B N    1 
ATOM   15377 C  CA   . LYS   B  2  415 ? 20.588  -27.147 17.089   1.00 61.31  ? 419  LYS   B CA   1 
ATOM   15378 C  C    . LYS   B  2  415 ? 21.070  -28.456 16.492   1.00 61.59  ? 419  LYS   B C    1 
ATOM   15379 O  O    . LYS   B  2  415 ? 21.793  -28.458 15.489   1.00 60.71  ? 419  LYS   B O    1 
ATOM   15380 C  CB   . LYS   B  2  415 ? 19.170  -26.834 16.595   1.00 63.09  ? 419  LYS   B CB   1 
ATOM   15381 C  CG   . LYS   B  2  415 ? 19.034  -26.823 15.080   1.00 67.96  ? 419  LYS   B CG   1 
ATOM   15382 C  CD   . LYS   B  2  415 ? 17.595  -26.604 14.657   1.00 78.74  ? 419  LYS   B CD   1 
ATOM   15383 C  CE   . LYS   B  2  415 ? 17.479  -26.534 13.147   1.00 91.70  ? 419  LYS   B CE   1 
ATOM   15384 N  NZ   . LYS   B  2  415 ? 16.093  -26.226 12.709   1.00 101.84 ? 419  LYS   B NZ   1 
ATOM   15385 H  H    . LYS   B  2  415 ? 21.877  -26.194 15.943   1.00 74.33  ? 419  LYS   B H    1 
ATOM   15386 H  HA   . LYS   B  2  415 ? 20.571  -27.237 18.054   1.00 73.55  ? 419  LYS   B HA   1 
ATOM   15387 H  HB2  . LYS   B  2  415 ? 18.564  -27.509 16.942   1.00 75.68  ? 419  LYS   B HB2  1 
ATOM   15388 H  HB3  . LYS   B  2  415 ? 18.912  -25.958 16.922   1.00 75.68  ? 419  LYS   B HB3  1 
ATOM   15389 H  HG2  . LYS   B  2  415 ? 19.573  -26.105 14.714   1.00 81.53  ? 419  LYS   B HG2  1 
ATOM   15390 H  HG3  . LYS   B  2  415 ? 19.331  -27.675 14.724   1.00 81.53  ? 419  LYS   B HG3  1 
ATOM   15391 H  HD2  . LYS   B  2  415 ? 17.049  -27.340 14.973   1.00 94.47  ? 419  LYS   B HD2  1 
ATOM   15392 H  HD3  . LYS   B  2  415 ? 17.273  -25.768 15.028   1.00 94.47  ? 419  LYS   B HD3  1 
ATOM   15393 H  HE2  . LYS   B  2  415 ? 18.064  -25.836 12.814   1.00 110.02 ? 419  LYS   B HE2  1 
ATOM   15394 H  HE3  . LYS   B  2  415 ? 17.733  -27.390 12.768   1.00 110.02 ? 419  LYS   B HE3  1 
ATOM   15395 H  HZ1  . LYS   B  2  415 ? 16.060  -26.169 11.822   1.00 122.19 ? 419  LYS   B HZ1  1 
ATOM   15396 H  HZ2  . LYS   B  2  415 ? 15.539  -26.868 12.978   1.00 122.19 ? 419  LYS   B HZ2  1 
ATOM   15397 H  HZ3  . LYS   B  2  415 ? 15.829  -25.451 13.059   1.00 122.19 ? 419  LYS   B HZ3  1 
ATOM   15398 N  N    . PRO   B  2  416 ? 20.683  -29.588 17.076   1.00 63.99  ? 420  PRO   B N    1 
ATOM   15399 C  CA   . PRO   B  2  416 ? 20.942  -30.871 16.418   1.00 66.96  ? 420  PRO   B CA   1 
ATOM   15400 C  C    . PRO   B  2  416 ? 20.072  -31.019 15.183   1.00 71.03  ? 420  PRO   B C    1 
ATOM   15401 O  O    . PRO   B  2  416 ? 18.952  -30.506 15.118   1.00 75.71  ? 420  PRO   B O    1 
ATOM   15402 C  CB   . PRO   B  2  416 ? 20.572  -31.910 17.486   1.00 68.89  ? 420  PRO   B CB   1 
ATOM   15403 C  CG   . PRO   B  2  416 ? 20.371  -31.136 18.762   1.00 67.05  ? 420  PRO   B CG   1 
ATOM   15404 C  CD   . PRO   B  2  416 ? 19.973  -29.761 18.353   1.00 64.02  ? 420  PRO   B CD   1 
ATOM   15405 H  HA   . PRO   B  2  416 ? 21.879  -30.969 16.188   1.00 80.34  ? 420  PRO   B HA   1 
ATOM   15406 H  HB2  . PRO   B  2  416 ? 19.755  -32.366 17.229   1.00 82.65  ? 420  PRO   B HB2  1 
ATOM   15407 H  HB3  . PRO   B  2  416 ? 21.294  -32.550 17.582   1.00 82.65  ? 420  PRO   B HB3  1 
ATOM   15408 H  HG2  . PRO   B  2  416 ? 19.671  -31.552 19.290   1.00 80.44  ? 420  PRO   B HG2  1 
ATOM   15409 H  HG3  . PRO   B  2  416 ? 21.200  -31.117 19.266   1.00 80.44  ? 420  PRO   B HG3  1 
ATOM   15410 H  HD2  . PRO   B  2  416 ? 19.014  -29.699 18.228   1.00 76.81  ? 420  PRO   B HD2  1 
ATOM   15411 H  HD3  . PRO   B  2  416 ? 20.266  -29.105 19.005   1.00 76.81  ? 420  PRO   B HD3  1 
ATOM   15412 N  N    . VAL   B  2  417 ? 20.603  -31.727 14.188   1.00 69.75  ? 421  VAL   B N    1 
ATOM   15413 C  CA   . VAL   B  2  417 ? 19.835  -31.993 12.979   1.00 71.28  ? 421  VAL   B CA   1 
ATOM   15414 C  C    . VAL   B  2  417 ? 18.678  -32.923 13.318   1.00 70.84  ? 421  VAL   B C    1 
ATOM   15415 O  O    . VAL   B  2  417 ? 18.869  -33.981 13.931   1.00 69.88  ? 421  VAL   B O    1 
ATOM   15416 C  CB   . VAL   B  2  417 ? 20.734  -32.589 11.887   1.00 74.33  ? 421  VAL   B CB   1 
ATOM   15417 C  CG1  . VAL   B  2  417 ? 19.915  -32.931 10.653   1.00 75.55  ? 421  VAL   B CG1  1 
ATOM   15418 C  CG2  . VAL   B  2  417 ? 21.850  -31.615 11.532   1.00 75.58  ? 421  VAL   B CG2  1 
ATOM   15419 H  H    . VAL   B  2  417 ? 21.396  -32.060 14.191   1.00 83.68  ? 421  VAL   B H    1 
ATOM   15420 H  HA   . VAL   B  2  417 ? 19.470  -31.159 12.643   1.00 85.51  ? 421  VAL   B HA   1 
ATOM   15421 H  HB   . VAL   B  2  417 ? 21.136  -33.407 12.222   1.00 89.17  ? 421  VAL   B HB   1 
ATOM   15422 H  HG11 . VAL   B  2  417 ? 20.518  -33.160 9.928    1.00 90.64  ? 421  VAL   B HG11 1 
ATOM   15423 H  HG12 . VAL   B  2  417 ? 19.340  -33.686 10.855   1.00 90.64  ? 421  VAL   B HG12 1 
ATOM   15424 H  HG13 . VAL   B  2  417 ? 19.378  -32.162 10.407   1.00 90.64  ? 421  VAL   B HG13 1 
ATOM   15425 H  HG21 . VAL   B  2  417 ? 22.363  -31.979 10.793   1.00 90.68  ? 421  VAL   B HG21 1 
ATOM   15426 H  HG22 . VAL   B  2  417 ? 21.458  -30.766 11.275   1.00 90.68  ? 421  VAL   B HG22 1 
ATOM   15427 H  HG23 . VAL   B  2  417 ? 22.423  -31.495 12.305   1.00 90.68  ? 421  VAL   B HG23 1 
ATOM   15428 N  N    . GLY   B  2  418 ? 17.468  -32.526 12.929   1.00 73.39  ? 422  GLY   B N    1 
ATOM   15429 C  CA   . GLY   B  2  418 ? 16.286  -33.324 13.147   1.00 72.54  ? 422  GLY   B CA   1 
ATOM   15430 C  C    . GLY   B  2  418 ? 15.521  -33.011 14.416   1.00 68.36  ? 422  GLY   B C    1 
ATOM   15431 O  O    . GLY   B  2  418 ? 14.335  -33.350 14.504   1.00 67.00  ? 422  GLY   B O    1 
ATOM   15432 H  H    . GLY   B  2  418 ? 17.312  -31.780 12.530   1.00 88.05  ? 422  GLY   B H    1 
ATOM   15433 H  HA2  . GLY   B  2  418 ? 15.682  -33.193 12.400   1.00 87.03  ? 422  GLY   B HA2  1 
ATOM   15434 H  HA3  . GLY   B  2  418 ? 16.546  -34.258 13.183   1.00 87.03  ? 422  GLY   B HA3  1 
ATOM   15435 N  N    . LEU   B  2  419 ? 16.156  -32.379 15.398   1.00 67.55  ? 423  LEU   B N    1 
ATOM   15436 C  CA   . LEU   B  2  419 ? 15.515  -32.050 16.662   1.00 66.10  ? 423  LEU   B CA   1 
ATOM   15437 C  C    . LEU   B  2  419 ? 15.185  -30.562 16.719   1.00 66.32  ? 423  LEU   B C    1 
ATOM   15438 O  O    . LEU   B  2  419 ? 15.841  -29.734 16.085   1.00 66.16  ? 423  LEU   B O    1 
ATOM   15439 C  CB   . LEU   B  2  419 ? 16.412  -32.423 17.845   1.00 67.35  ? 423  LEU   B CB   1 
ATOM   15440 C  CG   . LEU   B  2  419 ? 16.939  -33.859 17.878   1.00 71.06  ? 423  LEU   B CG   1 
ATOM   15441 C  CD1  . LEU   B  2  419 ? 17.728  -34.100 19.156   1.00 71.39  ? 423  LEU   B CD1  1 
ATOM   15442 C  CD2  . LEU   B  2  419 ? 15.801  -34.860 17.751   1.00 74.53  ? 423  LEU   B CD2  1 
ATOM   15443 H  H    . LEU   B  2  419 ? 16.977  -32.126 15.353   1.00 81.04  ? 423  LEU   B H    1 
ATOM   15444 H  HA   . LEU   B  2  419 ? 14.687  -32.550 16.739   1.00 79.30  ? 423  LEU   B HA   1 
ATOM   15445 H  HB2  . LEU   B  2  419 ? 17.185  -31.836 17.832   1.00 80.80  ? 423  LEU   B HB2  1 
ATOM   15446 H  HB3  . LEU   B  2  419 ? 15.906  -32.286 18.660   1.00 80.80  ? 423  LEU   B HB3  1 
ATOM   15447 H  HG   . LEU   B  2  419 ? 17.532  -33.994 17.123   1.00 85.25  ? 423  LEU   B HG   1 
ATOM   15448 H  HD11 . LEU   B  2  419 ? 18.056  -35.013 19.158   1.00 85.65  ? 423  LEU   B HD11 1 
ATOM   15449 H  HD12 . LEU   B  2  419 ? 18.474  -33.480 19.188   1.00 85.65  ? 423  LEU   B HD12 1 
ATOM   15450 H  HD13 . LEU   B  2  419 ? 17.146  -33.956 19.919   1.00 85.65  ? 423  LEU   B HD13 1 
ATOM   15451 H  HD21 . LEU   B  2  419 ? 16.160  -35.757 17.835   1.00 89.41  ? 423  LEU   B HD21 1 
ATOM   15452 H  HD22 . LEU   B  2  419 ? 15.155  -34.695 18.455   1.00 89.41  ? 423  LEU   B HD22 1 
ATOM   15453 H  HD23 . LEU   B  2  419 ? 15.381  -34.751 16.883   1.00 89.41  ? 423  LEU   B HD23 1 
ATOM   15454 N  N    . GLY   B  2  420 ? 14.150  -30.238 17.500   1.00 69.95  ? 424  GLY   B N    1 
ATOM   15455 C  CA   . GLY   B  2  420 ? 13.727  -28.855 17.640   1.00 74.00  ? 424  GLY   B CA   1 
ATOM   15456 C  C    . GLY   B  2  420 ? 14.499  -28.098 18.696   1.00 75.85  ? 424  GLY   B C    1 
ATOM   15457 O  O    . GLY   B  2  420 ? 14.634  -26.871 18.608   1.00 81.44  ? 424  GLY   B O    1 
ATOM   15458 H  H    . GLY   B  2  420 ? 13.683  -30.799 17.954   1.00 83.93  ? 424  GLY   B H    1 
ATOM   15459 H  HA2  . GLY   B  2  420 ? 13.849  -28.399 16.792   1.00 88.78  ? 424  GLY   B HA2  1 
ATOM   15460 H  HA3  . GLY   B  2  420 ? 12.787  -28.833 17.878   1.00 88.78  ? 424  GLY   B HA3  1 
ATOM   15461 N  N    . ASP   B  2  421 ? 15.011  -28.803 19.701   1.00 71.06  ? 425  ASP   B N    1 
ATOM   15462 C  CA   . ASP   B  2  421 ? 15.800  -28.173 20.752   1.00 68.61  ? 425  ASP   B CA   1 
ATOM   15463 C  C    . ASP   B  2  421 ? 16.915  -27.336 20.144   1.00 66.30  ? 425  ASP   B C    1 
ATOM   15464 O  O    . ASP   B  2  421 ? 17.766  -27.854 19.414   1.00 69.04  ? 425  ASP   B O    1 
ATOM   15465 C  CB   . ASP   B  2  421 ? 16.379  -29.239 21.685   1.00 70.29  ? 425  ASP   B CB   1 
ATOM   15466 C  CG   . ASP   B  2  421 ? 15.305  -30.092 22.336   1.00 75.43  ? 425  ASP   B CG   1 
ATOM   15467 O  OD1  . ASP   B  2  421 ? 14.720  -30.948 21.640   1.00 77.94  ? 425  ASP   B OD1  1 
ATOM   15468 O  OD2  . ASP   B  2  421 ? 15.044  -29.905 23.543   1.00 77.26  ? 425  ASP   B OD2  1 
ATOM   15469 H  H    . ASP   B  2  421 ? 14.916  -29.652 19.798   1.00 85.26  ? 425  ASP   B H    1 
ATOM   15470 H  HA   . ASP   B  2  421 ? 15.228  -27.594 21.280   1.00 82.31  ? 425  ASP   B HA   1 
ATOM   15471 H  HB2  . ASP   B  2  421 ? 16.959  -29.826 21.174   1.00 84.33  ? 425  ASP   B HB2  1 
ATOM   15472 H  HB3  . ASP   B  2  421 ? 16.885  -28.804 22.388   1.00 84.33  ? 425  ASP   B HB3  1 
ATOM   15473 N  N    . ALA   B  2  422 ? 16.910  -26.040 20.446   1.00 64.14  ? 426  ALA   B N    1 
ATOM   15474 C  CA   . ALA   B  2  422 ? 17.806  -25.091 19.804   1.00 64.83  ? 426  ALA   B CA   1 
ATOM   15475 C  C    . ALA   B  2  422 ? 18.503  -24.221 20.838   1.00 65.15  ? 426  ALA   B C    1 
ATOM   15476 O  O    . ALA   B  2  422 ? 17.930  -23.869 21.872   1.00 65.61  ? 426  ALA   B O    1 
ATOM   15477 C  CB   . ALA   B  2  422 ? 17.046  -24.197 18.814   1.00 66.39  ? 426  ALA   B CB   1 
ATOM   15478 H  H    . ALA   B  2  422 ? 16.388  -25.684 21.030   1.00 76.95  ? 426  ALA   B H    1 
ATOM   15479 H  HA   . ALA   B  2  422 ? 18.492  -25.582 19.326   1.00 77.78  ? 426  ALA   B HA   1 
ATOM   15480 H  HB1  . ALA   B  2  422 ? 17.656  -23.534 18.454   1.00 79.65  ? 426  ALA   B HB1  1 
ATOM   15481 H  HB2  . ALA   B  2  422 ? 16.695  -24.748 18.096   1.00 79.65  ? 426  ALA   B HB2  1 
ATOM   15482 H  HB3  . ALA   B  2  422 ? 16.317  -23.758 19.280   1.00 79.65  ? 426  ALA   B HB3  1 
ATOM   15483 N  N    . LEU   B  2  423 ? 19.754  -23.880 20.540   1.00 68.22  ? 427  LEU   B N    1 
ATOM   15484 C  CA   . LEU   B  2  423 ? 20.532  -22.931 21.327   1.00 66.84  ? 427  LEU   B CA   1 
ATOM   15485 C  C    . LEU   B  2  423 ? 20.506  -21.596 20.593   1.00 67.45  ? 427  LEU   B C    1 
ATOM   15486 O  O    . LEU   B  2  423 ? 21.070  -21.470 19.501   1.00 66.50  ? 427  LEU   B O    1 
ATOM   15487 C  CB   . LEU   B  2  423 ? 21.963  -23.427 21.520   1.00 64.88  ? 427  LEU   B CB   1 
ATOM   15488 C  CG   . LEU   B  2  423 ? 22.873  -22.654 22.482   1.00 63.12  ? 427  LEU   B CG   1 
ATOM   15489 C  CD1  . LEU   B  2  423 ? 24.135  -23.460 22.740   1.00 61.98  ? 427  LEU   B CD1  1 
ATOM   15490 C  CD2  . LEU   B  2  423 ? 23.244  -21.271 21.960   1.00 64.80  ? 427  LEU   B CD2  1 
ATOM   15491 H  H    . LEU   B  2  423 ? 20.185  -24.196 19.866   1.00 81.85  ? 427  LEU   B H    1 
ATOM   15492 H  HA   . LEU   B  2  423 ? 20.132  -22.820 22.204   1.00 80.19  ? 427  LEU   B HA   1 
ATOM   15493 H  HB2  . LEU   B  2  423 ? 21.917  -24.337 21.853   1.00 77.84  ? 427  LEU   B HB2  1 
ATOM   15494 H  HB3  . LEU   B  2  423 ? 22.399  -23.412 20.654   1.00 77.84  ? 427  LEU   B HB3  1 
ATOM   15495 H  HG   . LEU   B  2  423 ? 22.386  -22.518 23.310   1.00 75.72  ? 427  LEU   B HG   1 
ATOM   15496 H  HD11 . LEU   B  2  423 ? 24.717  -22.956 23.330   1.00 74.35  ? 427  LEU   B HD11 1 
ATOM   15497 H  HD12 . LEU   B  2  423 ? 23.893  -24.302 23.156   1.00 74.35  ? 427  LEU   B HD12 1 
ATOM   15498 H  HD13 . LEU   B  2  423 ? 24.583  -23.625 21.896   1.00 74.35  ? 427  LEU   B HD13 1 
ATOM   15499 H  HD21 . LEU   B  2  423 ? 23.959  -20.909 22.506   1.00 77.74  ? 427  LEU   B HD21 1 
ATOM   15500 H  HD22 . LEU   B  2  423 ? 23.539  -21.350 21.039   1.00 77.74  ? 427  LEU   B HD22 1 
ATOM   15501 H  HD23 . LEU   B  2  423 ? 22.465  -20.695 22.009   1.00 77.74  ? 427  LEU   B HD23 1 
ATOM   15502 N  N    . GLU   B  2  424 ? 19.856  -20.602 21.189   1.00 72.83  ? 428  GLU   B N    1 
ATOM   15503 C  CA   . GLU   B  2  424 ? 19.803  -19.274 20.594   1.00 75.16  ? 428  GLU   B CA   1 
ATOM   15504 C  C    . GLU   B  2  424 ? 21.074  -18.512 20.944   1.00 70.31  ? 428  GLU   B C    1 
ATOM   15505 O  O    . GLU   B  2  424 ? 21.445  -18.410 22.116   1.00 70.41  ? 428  GLU   B O    1 
ATOM   15506 C  CB   . GLU   B  2  424 ? 18.565  -18.523 21.081   1.00 82.56  ? 428  GLU   B CB   1 
ATOM   15507 C  CG   . GLU   B  2  424 ? 17.287  -19.352 20.995   1.00 91.92  ? 428  GLU   B CG   1 
ATOM   15508 C  CD   . GLU   B  2  424 ? 16.049  -18.513 20.761   1.00 101.21 ? 428  GLU   B CD   1 
ATOM   15509 O  OE1  . GLU   B  2  424 ? 16.101  -17.290 21.005   1.00 105.04 ? 428  GLU   B OE1  1 
ATOM   15510 O  OE2  . GLU   B  2  424 ? 15.023  -19.080 20.329   1.00 104.44 ? 428  GLU   B OE2  1 
ATOM   15511 H  H    . GLU   B  2  424 ? 19.438  -20.672 21.937   1.00 87.38  ? 428  GLU   B H    1 
ATOM   15512 H  HA   . GLU   B  2  424 ? 19.743  -19.344 19.628   1.00 90.17  ? 428  GLU   B HA   1 
ATOM   15513 H  HB2  . GLU   B  2  424 ? 18.695  -18.271 22.008   1.00 99.05  ? 428  GLU   B HB2  1 
ATOM   15514 H  HB3  . GLU   B  2  424 ? 18.444  -17.730 20.535   1.00 99.05  ? 428  GLU   B HB3  1 
ATOM   15515 H  HG2  . GLU   B  2  424 ? 17.367  -19.978 20.257   1.00 110.28 ? 428  GLU   B HG2  1 
ATOM   15516 H  HG3  . GLU   B  2  424 ? 17.168  -19.835 21.828   1.00 110.28 ? 428  GLU   B HG3  1 
ATOM   15517 N  N    . LEU   B  2  425 ? 21.750  -17.989 19.924   1.00 68.89  ? 429  LEU   B N    1 
ATOM   15518 C  CA   . LEU   B  2  425 ? 23.023  -17.302 20.100   1.00 71.18  ? 429  LEU   B CA   1 
ATOM   15519 C  C    . LEU   B  2  425 ? 22.936  -15.928 19.460   1.00 73.59  ? 429  LEU   B C    1 
ATOM   15520 O  O    . LEU   B  2  425 ? 22.617  -15.814 18.272   1.00 73.34  ? 429  LEU   B O    1 
ATOM   15521 C  CB   . LEU   B  2  425 ? 24.177  -18.101 19.486   1.00 71.26  ? 429  LEU   B CB   1 
ATOM   15522 C  CG   . LEU   B  2  425 ? 25.547  -17.418 19.513   1.00 71.63  ? 429  LEU   B CG   1 
ATOM   15523 C  CD1  . LEU   B  2  425 ? 26.076  -17.309 20.935   1.00 73.80  ? 429  LEU   B CD1  1 
ATOM   15524 C  CD2  . LEU   B  2  425 ? 26.528  -18.167 18.626   1.00 69.89  ? 429  LEU   B CD2  1 
ATOM   15525 H  H    . LEU   B  2  425 ? 21.485  -18.022 19.106   1.00 82.65  ? 429  LEU   B H    1 
ATOM   15526 H  HA   . LEU   B  2  425 ? 23.194  -17.190 21.049   1.00 85.39  ? 429  LEU   B HA   1 
ATOM   15527 H  HB2  . LEU   B  2  425 ? 24.261  -18.935 19.974   1.00 85.50  ? 429  LEU   B HB2  1 
ATOM   15528 H  HB3  . LEU   B  2  425 ? 23.962  -18.279 18.558   1.00 85.50  ? 429  LEU   B HB3  1 
ATOM   15529 H  HG   . LEU   B  2  425 ? 25.455  -16.516 19.168   1.00 85.94  ? 429  LEU   B HG   1 
ATOM   15530 H  HD11 . LEU   B  2  425 ? 26.950  -16.889 20.916   1.00 88.54  ? 429  LEU   B HD11 1 
ATOM   15531 H  HD12 . LEU   B  2  425 ? 25.462  -16.772 21.460   1.00 88.54  ? 429  LEU   B HD12 1 
ATOM   15532 H  HD13 . LEU   B  2  425 ? 26.145  -18.199 21.315   1.00 88.54  ? 429  LEU   B HD13 1 
ATOM   15533 H  HD21 . LEU   B  2  425 ? 27.389  -17.722 18.661   1.00 83.85  ? 429  LEU   B HD21 1 
ATOM   15534 H  HD22 . LEU   B  2  425 ? 26.613  -19.078 18.948   1.00 83.85  ? 429  LEU   B HD22 1 
ATOM   15535 H  HD23 . LEU   B  2  425 ? 26.194  -18.168 17.715   1.00 83.85  ? 429  LEU   B HD23 1 
ATOM   15536 N  N    . LEU   B  2  426 ? 23.227  -14.894 20.241   1.00 76.50  ? 430  LEU   B N    1 
ATOM   15537 C  CA   . LEU   B  2  426 ? 23.295  -13.525 19.750   1.00 77.59  ? 430  LEU   B CA   1 
ATOM   15538 C  C    . LEU   B  2  426 ? 24.755  -13.092 19.737   1.00 76.63  ? 430  LEU   B C    1 
ATOM   15539 O  O    . LEU   B  2  426 ? 25.393  -13.021 20.793   1.00 76.57  ? 430  LEU   B O    1 
ATOM   15540 C  CB   . LEU   B  2  426 ? 22.464  -12.584 20.620   1.00 79.98  ? 430  LEU   B CB   1 
ATOM   15541 C  CG   . LEU   B  2  426 ? 22.236  -11.183 20.049   1.00 80.07  ? 430  LEU   B CG   1 
ATOM   15542 C  CD1  . LEU   B  2  426 ? 21.335  -11.238 18.824   1.00 80.66  ? 430  LEU   B CD1  1 
ATOM   15543 C  CD2  . LEU   B  2  426 ? 21.649  -10.270 21.109   1.00 79.29  ? 430  LEU   B CD2  1 
ATOM   15544 H  H    . LEU   B  2  426 ? 23.393  -14.963 21.082   1.00 91.78  ? 430  LEU   B H    1 
ATOM   15545 H  HA   . LEU   B  2  426 ? 22.948  -13.485 18.845   1.00 93.09  ? 430  LEU   B HA   1 
ATOM   15546 H  HB2  . LEU   B  2  426 ? 21.592  -12.986 20.755   1.00 95.95  ? 430  LEU   B HB2  1 
ATOM   15547 H  HB3  . LEU   B  2  426 ? 22.917  -12.478 21.471   1.00 95.95  ? 430  LEU   B HB3  1 
ATOM   15548 H  HG   . LEU   B  2  426 ? 23.089  -10.813 19.770   1.00 96.06  ? 430  LEU   B HG   1 
ATOM   15549 H  HD11 . LEU   B  2  426 ? 21.171  -10.335 18.512   1.00 96.77  ? 430  LEU   B HD11 1 
ATOM   15550 H  HD12 . LEU   B  2  426 ? 21.776  -11.753 18.130   1.00 96.77  ? 430  LEU   B HD12 1 
ATOM   15551 H  HD13 . LEU   B  2  426 ? 20.497  -11.661 19.068   1.00 96.77  ? 430  LEU   B HD13 1 
ATOM   15552 H  HD21 . LEU   B  2  426 ? 21.503  -9.392  20.724   1.00 95.13  ? 430  LEU   B HD21 1 
ATOM   15553 H  HD22 . LEU   B  2  426 ? 20.806  -10.642 21.413   1.00 95.13  ? 430  LEU   B HD22 1 
ATOM   15554 H  HD23 . LEU   B  2  426 ? 22.270  -10.208 21.851   1.00 95.13  ? 430  LEU   B HD23 1 
ATOM   15555 N  N    . VAL   B  2  427 ? 25.278  -12.814 18.548   1.00 77.32  ? 431  VAL   B N    1 
ATOM   15556 C  CA   . VAL   B  2  427 ? 26.649  -12.349 18.375   1.00 79.96  ? 431  VAL   B CA   1 
ATOM   15557 C  C    . VAL   B  2  427 ? 26.612  -10.833 18.257   1.00 86.12  ? 431  VAL   B C    1 
ATOM   15558 O  O    . VAL   B  2  427 ? 26.044  -10.290 17.301   1.00 88.86  ? 431  VAL   B O    1 
ATOM   15559 C  CB   . VAL   B  2  427 ? 27.309  -12.987 17.143   1.00 78.25  ? 431  VAL   B CB   1 
ATOM   15560 C  CG1  . VAL   B  2  427 ? 28.750  -12.515 17.003   1.00 74.02  ? 431  VAL   B CG1  1 
ATOM   15561 C  CG2  . VAL   B  2  427 ? 27.249  -14.505 17.235   1.00 79.63  ? 431  VAL   B CG2  1 
ATOM   15562 H  H    . VAL   B  2  427 ? 24.847  -12.890 17.807   1.00 92.77  ? 431  VAL   B H    1 
ATOM   15563 H  HA   . VAL   B  2  427 ? 27.173  -12.587 19.156   1.00 95.93  ? 431  VAL   B HA   1 
ATOM   15564 H  HB   . VAL   B  2  427 ? 26.825  -12.710 16.349   1.00 93.88  ? 431  VAL   B HB   1 
ATOM   15565 H  HG11 . VAL   B  2  427 ? 29.160  -12.970 16.251   1.00 88.81  ? 431  VAL   B HG11 1 
ATOM   15566 H  HG12 . VAL   B  2  427 ? 28.756  -11.557 16.853   1.00 88.81  ? 431  VAL   B HG12 1 
ATOM   15567 H  HG13 . VAL   B  2  427 ? 29.232  -12.725 17.818   1.00 88.81  ? 431  VAL   B HG13 1 
ATOM   15568 H  HG21 . VAL   B  2  427 ? 27.676  -14.886 16.451   1.00 95.53  ? 431  VAL   B HG21 1 
ATOM   15569 H  HG22 . VAL   B  2  427 ? 27.714  -14.791 18.037   1.00 95.53  ? 431  VAL   B HG22 1 
ATOM   15570 H  HG23 . VAL   B  2  427 ? 26.320  -14.782 17.273   1.00 95.53  ? 431  VAL   B HG23 1 
ATOM   15571 N  N    . SER   B  2  428 ? 27.212  -10.149 19.228   1.00 89.45  ? 432  SER   B N    1 
ATOM   15572 C  CA   . SER   B  2  428 ? 27.242  -8.699  19.260   1.00 94.36  ? 432  SER   B CA   1 
ATOM   15573 C  C    . SER   B  2  428 ? 28.682  -8.215  19.153   1.00 95.11  ? 432  SER   B C    1 
ATOM   15574 O  O    . SER   B  2  428 ? 29.557  -8.733  19.861   1.00 92.74  ? 432  SER   B O    1 
ATOM   15575 C  CB   . SER   B  2  428 ? 26.605  -8.168  20.554   1.00 96.89  ? 432  SER   B CB   1 
ATOM   15576 O  OG   . SER   B  2  428 ? 25.231  -8.510  20.626   1.00 98.51  ? 432  SER   B OG   1 
ATOM   15577 H  H    . SER   B  2  428 ? 27.616  -10.516 19.893   1.00 107.32 ? 432  SER   B H    1 
ATOM   15578 H  HA   . SER   B  2  428 ? 26.741  -8.347  18.508   1.00 113.22 ? 432  SER   B HA   1 
ATOM   15579 H  HB2  . SER   B  2  428 ? 27.066  -8.557  21.314   1.00 116.25 ? 432  SER   B HB2  1 
ATOM   15580 H  HB3  . SER   B  2  428 ? 26.691  -7.202  20.573   1.00 116.25 ? 432  SER   B HB3  1 
ATOM   15581 H  HG   . SER   B  2  428 ? 24.899  -8.217  21.339   1.00 118.19 ? 432  SER   B HG   1 
ATOM   15582 N  N    . PRO   B  2  429 ? 28.975  -7.242  18.295   1.00 99.79  ? 433  PRO   B N    1 
ATOM   15583 C  CA   . PRO   B  2  429 ? 30.355  -6.773  18.160   1.00 98.62  ? 433  PRO   B CA   1 
ATOM   15584 C  C    . PRO   B  2  429 ? 30.766  -5.863  19.306   1.00 92.33  ? 433  PRO   B C    1 
ATOM   15585 O  O    . PRO   B  2  429 ? 29.952  -5.144  19.890   1.00 90.03  ? 433  PRO   B O    1 
ATOM   15586 C  CB   . PRO   B  2  429 ? 30.334  -6.007  16.832   1.00 103.98 ? 433  PRO   B CB   1 
ATOM   15587 C  CG   . PRO   B  2  429 ? 28.942  -5.487  16.738   1.00 106.75 ? 433  PRO   B CG   1 
ATOM   15588 C  CD   . PRO   B  2  429 ? 28.062  -6.530  17.380   1.00 104.89 ? 433  PRO   B CD   1 
ATOM   15589 H  HA   . PRO   B  2  429 ? 30.971  -7.520  18.103   1.00 118.32 ? 433  PRO   B HA   1 
ATOM   15590 H  HB2  . PRO   B  2  429 ? 30.979  -5.283  16.854   1.00 124.76 ? 433  PRO   B HB2  1 
ATOM   15591 H  HB3  . PRO   B  2  429 ? 30.535  -6.607  16.097   1.00 124.76 ? 433  PRO   B HB3  1 
ATOM   15592 H  HG2  . PRO   B  2  429 ? 28.877  -4.643  17.213   1.00 128.08 ? 433  PRO   B HG2  1 
ATOM   15593 H  HG3  . PRO   B  2  429 ? 28.703  -5.362  15.807   1.00 128.08 ? 433  PRO   B HG3  1 
ATOM   15594 H  HD2  . PRO   B  2  429 ? 27.338  -6.112  17.873   1.00 125.85 ? 433  PRO   B HD2  1 
ATOM   15595 H  HD3  . PRO   B  2  429 ? 27.703  -7.135  16.712   1.00 125.85 ? 433  PRO   B HD3  1 
ATOM   15596 N  N    . GLU   B  2  430 ? 32.058  -5.914  19.628   1.00 90.24  ? 434  GLU   B N    1 
ATOM   15597 C  CA   . GLU   B  2  430 ? 32.680  -5.002  20.587   1.00 90.94  ? 434  GLU   B CA   1 
ATOM   15598 C  C    . GLU   B  2  430 ? 33.986  -4.518  19.966   1.00 91.85  ? 434  GLU   B C    1 
ATOM   15599 O  O    . GLU   B  2  430 ? 35.048  -5.103  20.200   1.00 88.16  ? 434  GLU   B O    1 
ATOM   15600 C  CB   . GLU   B  2  430 ? 32.916  -5.675  21.935   1.00 89.42  ? 434  GLU   B CB   1 
ATOM   15601 C  CG   . GLU   B  2  430 ? 31.679  -5.762  22.809   1.00 91.55  ? 434  GLU   B CG   1 
ATOM   15602 C  CD   . GLU   B  2  430 ? 31.988  -5.534  24.275   1.00 93.63  ? 434  GLU   B CD   1 
ATOM   15603 O  OE1  . GLU   B  2  430 ? 33.089  -5.921  24.720   1.00 93.25  ? 434  GLU   B OE1  1 
ATOM   15604 O  OE2  . GLU   B  2  430 ? 31.133  -4.959  24.980   1.00 95.93  ? 434  GLU   B OE2  1 
ATOM   15605 H  H    . GLU   B  2  430 ? 32.609  -6.484  19.294   1.00 108.27 ? 434  GLU   B H    1 
ATOM   15606 H  HA   . GLU   B  2  430 ? 32.093  -4.243  20.730   1.00 109.10 ? 434  GLU   B HA   1 
ATOM   15607 H  HB2  . GLU   B  2  430 ? 33.231  -6.579  21.780   1.00 107.29 ? 434  GLU   B HB2  1 
ATOM   15608 H  HB3  . GLU   B  2  430 ? 33.585  -5.170  22.422   1.00 107.29 ? 434  GLU   B HB3  1 
ATOM   15609 H  HG2  . GLU   B  2  430 ? 31.043  -5.086  22.527   1.00 109.84 ? 434  GLU   B HG2  1 
ATOM   15610 H  HG3  . GLU   B  2  430 ? 31.287  -6.645  22.718   1.00 109.84 ? 434  GLU   B HG3  1 
ATOM   15611 N  N    . CYS   B  2  431 ? 33.904  -3.446  19.176   1.00 98.06  ? 435  CYS   B N    1 
ATOM   15612 C  CA   . CYS   B  2  431 ? 35.080  -2.819  18.583   1.00 103.50 ? 435  CYS   B CA   1 
ATOM   15613 C  C    . CYS   B  2  431 ? 35.171  -1.344  18.953   1.00 102.47 ? 435  CYS   B C    1 
ATOM   15614 O  O    . CYS   B  2  431 ? 35.787  -0.558  18.225   1.00 101.45 ? 435  CYS   B O    1 
ATOM   15615 C  CB   . CYS   B  2  431 ? 35.074  -2.999  17.063   1.00 109.23 ? 435  CYS   B CB   1 
ATOM   15616 S  SG   . CYS   B  2  431 ? 34.012  -1.870  16.132   1.00 112.85 ? 435  CYS   B SG   1 
ATOM   15617 H  H    . CYS   B  2  431 ? 33.165  -3.059  18.968   1.00 117.65 ? 435  CYS   B H    1 
ATOM   15618 H  HA   . CYS   B  2  431 ? 35.876  -3.258  18.922   1.00 124.18 ? 435  CYS   B HA   1 
ATOM   15619 H  HB2  . CYS   B  2  431 ? 35.979  -2.871  16.740   1.00 131.05 ? 435  CYS   B HB2  1 
ATOM   15620 H  HB3  . CYS   B  2  431 ? 34.775  -3.900  16.867   1.00 131.05 ? 435  CYS   B HB3  1 
ATOM   15621 N  N    . ASN   B  2  432 ? 34.565  -0.958  20.073   1.00 102.70 ? 436  ASN   B N    1 
ATOM   15622 C  CA   . ASN   B  2  432 ? 34.630  0.397   20.593   1.00 105.74 ? 436  ASN   B CA   1 
ATOM   15623 C  C    . ASN   B  2  432 ? 35.298  0.385   21.962   1.00 108.06 ? 436  ASN   B C    1 
ATOM   15624 O  O    . ASN   B  2  432 ? 35.341  -0.639  22.650   1.00 105.74 ? 436  ASN   B O    1 
ATOM   15625 C  CB   . ASN   B  2  432 ? 33.233  1.023   20.697   1.00 104.61 ? 436  ASN   B CB   1 
ATOM   15626 C  CG   . ASN   B  2  432 ? 32.611  1.288   19.340   1.00 103.58 ? 436  ASN   B CG   1 
ATOM   15627 O  OD1  . ASN   B  2  432 ? 31.518  0.806   19.039   1.00 103.00 ? 436  ASN   B OD1  1 
ATOM   15628 N  ND2  . ASN   B  2  432 ? 33.306  2.059   18.512   1.00 104.31 ? 436  ASN   B ND2  1 
ATOM   15629 H  H    . ASN   B  2  432 ? 34.093  -1.484  20.563   1.00 123.22 ? 436  ASN   B H    1 
ATOM   15630 H  HA   . ASN   B  2  432 ? 35.162  0.948   19.998   1.00 126.87 ? 436  ASN   B HA   1 
ATOM   15631 H  HB2  . ASN   B  2  432 ? 32.650  0.419   21.183   1.00 125.52 ? 436  ASN   B HB2  1 
ATOM   15632 H  HB3  . ASN   B  2  432 ? 33.300  1.869   21.168   1.00 125.52 ? 436  ASN   B HB3  1 
ATOM   15633 H  HD21 . ASN   B  2  432 ? 32.996  2.239   17.730   1.00 125.16 ? 436  ASN   B HD21 1 
ATOM   15634 H  HD22 . ASN   B  2  432 ? 34.066  2.378   18.757   1.00 125.16 ? 436  ASN   B HD22 1 
ATOM   15635 N  N    . CYS   B  2  433 ? 35.820  1.544   22.350   1.00 112.79 ? 437  CYS   B N    1 
ATOM   15636 C  CA   . CYS   B  2  433 ? 36.514  1.709   23.617   1.00 116.02 ? 437  CYS   B CA   1 
ATOM   15637 C  C    . CYS   B  2  433 ? 35.615  2.419   24.622   1.00 123.56 ? 437  CYS   B C    1 
ATOM   15638 O  O    . CYS   B  2  433 ? 34.765  3.235   24.256   1.00 128.19 ? 437  CYS   B O    1 
ATOM   15639 C  CB   . CYS   B  2  433 ? 37.810  2.501   23.424   1.00 114.51 ? 437  CYS   B CB   1 
ATOM   15640 S  SG   . CYS   B  2  433 ? 38.945  1.793   22.203   1.00 109.01 ? 437  CYS   B SG   1 
ATOM   15641 H  H    . CYS   B  2  433 ? 35.783  2.265   21.883   1.00 135.33 ? 437  CYS   B H    1 
ATOM   15642 H  HA   . CYS   B  2  433 ? 36.742  0.838   23.978   1.00 139.20 ? 437  CYS   B HA   1 
ATOM   15643 H  HB2  . CYS   B  2  433 ? 37.583  3.397   23.130   1.00 137.39 ? 437  CYS   B HB2  1 
ATOM   15644 H  HB3  . CYS   B  2  433 ? 38.278  2.539   24.273   1.00 137.39 ? 437  CYS   B HB3  1 
ATOM   15645 N  N    . ASP   B  2  434 ? 35.808  2.094   25.903   1.00 125.44 ? 438  ASP   B N    1 
ATOM   15646 C  CA   . ASP   B  2  434 ? 35.054  2.773   26.952   1.00 129.74 ? 438  ASP   B CA   1 
ATOM   15647 C  C    . ASP   B  2  434 ? 35.369  4.263   26.978   1.00 128.94 ? 438  ASP   B C    1 
ATOM   15648 O  O    . ASP   B  2  434 ? 34.482  5.089   27.221   1.00 131.30 ? 438  ASP   B O    1 
ATOM   15649 C  CB   . ASP   B  2  434 ? 35.355  2.144   28.312   1.00 134.54 ? 438  ASP   B CB   1 
ATOM   15650 C  CG   . ASP   B  2  434 ? 34.480  0.944   28.606   1.00 136.95 ? 438  ASP   B CG   1 
ATOM   15651 O  OD1  . ASP   B  2  434 ? 33.914  0.369   27.653   1.00 136.91 ? 438  ASP   B OD1  1 
ATOM   15652 O  OD2  . ASP   B  2  434 ? 34.348  0.583   29.795   1.00 138.25 ? 438  ASP   B OD2  1 
ATOM   15653 H  H    . ASP   B  2  434 ? 36.359  1.496   26.184   1.00 150.51 ? 438  ASP   B H    1 
ATOM   15654 H  HA   . ASP   B  2  434 ? 34.107  2.663   26.772   1.00 155.67 ? 438  ASP   B HA   1 
ATOM   15655 H  HB2  . ASP   B  2  434 ? 36.280  1.853   28.328   1.00 161.43 ? 438  ASP   B HB2  1 
ATOM   15656 H  HB3  . ASP   B  2  434 ? 35.202  2.804   29.006   1.00 161.43 ? 438  ASP   B HB3  1 
ATOM   15657 N  N    . CYS   B  2  435 ? 36.630  4.624   26.732   1.00 125.70 ? 439  CYS   B N    1 
ATOM   15658 C  CA   . CYS   B  2  435 ? 37.027  6.026   26.744   1.00 126.07 ? 439  CYS   B CA   1 
ATOM   15659 C  C    . CYS   B  2  435 ? 36.368  6.823   25.627   1.00 131.65 ? 439  CYS   B C    1 
ATOM   15660 O  O    . CYS   B  2  435 ? 36.283  8.052   25.725   1.00 139.52 ? 439  CYS   B O    1 
ATOM   15661 C  CB   . CYS   B  2  435 ? 38.548  6.134   26.627   1.00 118.78 ? 439  CYS   B CB   1 
ATOM   15662 S  SG   . CYS   B  2  435 ? 39.225  5.412   25.117   1.00 108.92 ? 439  CYS   B SG   1 
ATOM   15663 H  H    . CYS   B  2  435 ? 37.270  4.077   26.557   1.00 150.82 ? 439  CYS   B H    1 
ATOM   15664 H  HA   . CYS   B  2  435 ? 36.758  6.420   27.588   1.00 151.27 ? 439  CYS   B HA   1 
ATOM   15665 H  HB2  . CYS   B  2  435 ? 38.795  7.072   26.642   1.00 142.52 ? 439  CYS   B HB2  1 
ATOM   15666 H  HB3  . CYS   B  2  435 ? 38.950  5.673   27.380   1.00 142.52 ? 439  CYS   B HB3  1 
ATOM   15667 N  N    . GLN   B  2  436 ? 35.899  6.152   24.574   1.00 127.12 ? 440  GLN   B N    1 
ATOM   15668 C  CA   . GLN   B  2  436 ? 35.292  6.858   23.452   1.00 126.09 ? 440  GLN   B CA   1 
ATOM   15669 C  C    . GLN   B  2  436 ? 34.039  7.614   23.874   1.00 128.65 ? 440  GLN   B C    1 
ATOM   15670 O  O    . GLN   B  2  436 ? 33.715  8.654   23.288   1.00 130.04 ? 440  GLN   B O    1 
ATOM   15671 C  CB   . GLN   B  2  436 ? 34.962  5.861   22.339   1.00 123.29 ? 440  GLN   B CB   1 
ATOM   15672 C  CG   . GLN   B  2  436 ? 35.249  6.362   20.932   1.00 123.97 ? 440  GLN   B CG   1 
ATOM   15673 C  CD   . GLN   B  2  436 ? 35.572  5.237   19.965   1.00 121.09 ? 440  GLN   B CD   1 
ATOM   15674 O  OE1  . GLN   B  2  436 ? 35.873  4.116   20.376   1.00 113.55 ? 440  GLN   B OE1  1 
ATOM   15675 N  NE2  . GLN   B  2  436 ? 35.513  5.533   18.672   1.00 125.84 ? 440  GLN   B NE2  1 
ATOM   15676 H  H    . GLN   B  2  436 ? 35.922  5.297   24.486   1.00 152.53 ? 440  GLN   B H    1 
ATOM   15677 H  HA   . GLN   B  2  436 ? 35.924  7.507   23.105   1.00 151.29 ? 440  GLN   B HA   1 
ATOM   15678 H  HB2  . GLN   B  2  436 ? 35.490  5.059   22.478   1.00 147.93 ? 440  GLN   B HB2  1 
ATOM   15679 H  HB3  . GLN   B  2  436 ? 34.017  5.648   22.387   1.00 147.93 ? 440  GLN   B HB3  1 
ATOM   15680 H  HG2  . GLN   B  2  436 ? 34.468  6.831   20.598   1.00 148.74 ? 440  GLN   B HG2  1 
ATOM   15681 H  HG3  . GLN   B  2  436 ? 36.010  6.963   20.959   1.00 148.74 ? 440  GLN   B HG3  1 
ATOM   15682 H  HE21 . GLN   B  2  436 ? 35.301  6.328   18.422   1.00 150.99 ? 440  GLN   B HE21 1 
ATOM   15683 H  HE22 . GLN   B  2  436 ? 35.687  4.929   18.084   1.00 150.99 ? 440  GLN   B HE22 1 
ATOM   15684 N  N    . LYS   B  2  437 ? 33.328  7.117   24.888   1.00 129.81 ? 441  LYS   B N    1 
ATOM   15685 C  CA   . LYS   B  2  437 ? 32.059  7.726   25.271   1.00 132.68 ? 441  LYS   B CA   1 
ATOM   15686 C  C    . LYS   B  2  437 ? 32.250  9.101   25.901   1.00 135.79 ? 441  LYS   B C    1 
ATOM   15687 O  O    . LYS   B  2  437 ? 31.380  9.968   25.759   1.00 139.51 ? 441  LYS   B O    1 
ATOM   15688 C  CB   . LYS   B  2  437 ? 31.309  6.800   26.229   1.00 131.16 ? 441  LYS   B CB   1 
ATOM   15689 C  CG   . LYS   B  2  437 ? 30.849  5.501   25.586   1.00 126.14 ? 441  LYS   B CG   1 
ATOM   15690 C  CD   . LYS   B  2  437 ? 30.115  4.609   26.575   1.00 123.35 ? 441  LYS   B CD   1 
ATOM   15691 C  CE   . LYS   B  2  437 ? 29.627  3.330   25.910   1.00 118.94 ? 441  LYS   B CE   1 
ATOM   15692 N  NZ   . LYS   B  2  437 ? 28.924  2.432   26.867   1.00 118.13 ? 441  LYS   B NZ   1 
ATOM   15693 H  H    . LYS   B  2  437 ? 33.557  6.437   25.363   1.00 155.76 ? 441  LYS   B H    1 
ATOM   15694 H  HA   . LYS   B  2  437 ? 31.519  7.843   24.474   1.00 159.20 ? 441  LYS   B HA   1 
ATOM   15695 H  HB2  . LYS   B  2  437 ? 31.894  6.575   26.968   1.00 157.37 ? 441  LYS   B HB2  1 
ATOM   15696 H  HB3  . LYS   B  2  437 ? 30.522  7.263   26.557   1.00 157.37 ? 441  LYS   B HB3  1 
ATOM   15697 H  HG2  . LYS   B  2  437 ? 30.246  5.701   24.853   1.00 151.34 ? 441  LYS   B HG2  1 
ATOM   15698 H  HG3  . LYS   B  2  437 ? 31.622  5.016   25.256   1.00 151.34 ? 441  LYS   B HG3  1 
ATOM   15699 H  HD2  . LYS   B  2  437 ? 30.715  4.368   27.298   1.00 148.01 ? 441  LYS   B HD2  1 
ATOM   15700 H  HD3  . LYS   B  2  437 ? 29.345  5.084   26.926   1.00 148.01 ? 441  LYS   B HD3  1 
ATOM   15701 H  HE2  . LYS   B  2  437 ? 29.008  3.557   25.198   1.00 142.71 ? 441  LYS   B HE2  1 
ATOM   15702 H  HE3  . LYS   B  2  437 ? 30.387  2.850   25.547   1.00 142.71 ? 441  LYS   B HE3  1 
ATOM   15703 H  HZ1  . LYS   B  2  437 ? 28.702  1.671   26.464   1.00 141.73 ? 441  LYS   B HZ1  1 
ATOM   15704 H  HZ2  . LYS   B  2  437 ? 29.455  2.249   27.558   1.00 141.73 ? 441  LYS   B HZ2  1 
ATOM   15705 H  HZ3  . LYS   B  2  437 ? 28.185  2.826   27.168   1.00 141.73 ? 441  LYS   B HZ3  1 
ATOM   15706 N  N    . GLU   B  2  438 ? 33.364  9.323   26.595   1.00 135.83 ? 442  GLU   B N    1 
ATOM   15707 C  CA   . GLU   B  2  438 ? 33.639  10.618  27.221   1.00 141.47 ? 442  GLU   B CA   1 
ATOM   15708 C  C    . GLU   B  2  438 ? 34.218  11.544  26.159   1.00 139.99 ? 442  GLU   B C    1 
ATOM   15709 O  O    . GLU   B  2  438 ? 35.423  11.567  25.904   1.00 133.97 ? 442  GLU   B O    1 
ATOM   15710 C  CB   . GLU   B  2  438 ? 34.577  10.454  28.410   1.00 145.85 ? 442  GLU   B CB   1 
ATOM   15711 C  CG   . GLU   B  2  438 ? 33.947  9.710   29.580   1.00 149.18 ? 442  GLU   B CG   1 
ATOM   15712 C  CD   . GLU   B  2  438 ? 34.890  9.558   30.758   1.00 151.08 ? 442  GLU   B CD   1 
ATOM   15713 O  OE1  . GLU   B  2  438 ? 36.082  9.905   30.616   1.00 151.35 ? 442  GLU   B OE1  1 
ATOM   15714 O  OE2  . GLU   B  2  438 ? 34.440  9.092   31.826   1.00 151.93 ? 442  GLU   B OE2  1 
ATOM   15715 H  H    . GLU   B  2  438 ? 33.981  8.737   26.720   1.00 162.98 ? 442  GLU   B H    1 
ATOM   15716 H  HA   . GLU   B  2  438 ? 32.811  11.006  27.544   1.00 169.75 ? 442  GLU   B HA   1 
ATOM   15717 H  HB2  . GLU   B  2  438 ? 35.359  9.954   28.126   1.00 175.00 ? 442  GLU   B HB2  1 
ATOM   15718 H  HB3  . GLU   B  2  438 ? 34.841  11.333  28.724   1.00 175.00 ? 442  GLU   B HB3  1 
ATOM   15719 H  HG2  . GLU   B  2  438 ? 33.167  10.200  29.882   1.00 178.99 ? 442  GLU   B HG2  1 
ATOM   15720 H  HG3  . GLU   B  2  438 ? 33.689  8.822   29.287   1.00 178.99 ? 442  GLU   B HG3  1 
ATOM   15721 N  N    . VAL   B  2  439 ? 33.336  12.323  25.528   1.00 145.60 ? 443  VAL   B N    1 
ATOM   15722 C  CA   . VAL   B  2  439 ? 33.751  13.175  24.416   1.00 147.25 ? 443  VAL   B CA   1 
ATOM   15723 C  C    . VAL   B  2  439 ? 34.696  14.271  24.898   1.00 147.68 ? 443  VAL   B C    1 
ATOM   15724 O  O    . VAL   B  2  439 ? 35.795  14.442  24.358   1.00 148.94 ? 443  VAL   B O    1 
ATOM   15725 C  CB   . VAL   B  2  439 ? 32.523  13.763  23.693   1.00 150.42 ? 443  VAL   B CB   1 
ATOM   15726 C  CG1  . VAL   B  2  439 ? 31.840  12.686  22.854   1.00 146.85 ? 443  VAL   B CG1  1 
ATOM   15727 C  CG2  . VAL   B  2  439 ? 31.526  14.397  24.674   1.00 154.67 ? 443  VAL   B CG2  1 
ATOM   15728 H  H    . VAL   B  2  439 ? 32.500  12.376  25.724   1.00 174.70 ? 443  VAL   B H    1 
ATOM   15729 H  HA   . VAL   B  2  439 ? 34.235  12.624  23.781   1.00 176.68 ? 443  VAL   B HA   1 
ATOM   15730 H  HB   . VAL   B  2  439 ? 32.831  14.470  23.105   1.00 180.48 ? 443  VAL   B HB   1 
ATOM   15731 H  HG11 . VAL   B  2  439 ? 30.991  13.028  22.532   1.00 176.20 ? 443  VAL   B HG11 1 
ATOM   15732 H  HG12 . VAL   B  2  439 ? 32.412  12.460  22.104   1.00 176.20 ? 443  VAL   B HG12 1 
ATOM   15733 H  HG13 . VAL   B  2  439 ? 31.692  11.902  23.406   1.00 176.20 ? 443  VAL   B HG13 1 
ATOM   15734 H  HG21 . VAL   B  2  439 ? 30.727  14.655  24.189   1.00 185.58 ? 443  VAL   B HG21 1 
ATOM   15735 H  HG22 . VAL   B  2  439 ? 31.302  13.748  25.360   1.00 185.58 ? 443  VAL   B HG22 1 
ATOM   15736 H  HG23 . VAL   B  2  439 ? 31.935  15.178  25.079   1.00 185.58 ? 443  VAL   B HG23 1 
ATOM   15737 N  N    . GLU   B  2  440 ? 34.288  15.028  25.916   1.00 145.66 ? 444  GLU   B N    1 
ATOM   15738 C  CA   . GLU   B  2  440 ? 35.086  16.139  26.434   1.00 143.61 ? 444  GLU   B CA   1 
ATOM   15739 C  C    . GLU   B  2  440 ? 35.360  17.162  25.328   1.00 134.53 ? 444  GLU   B C    1 
ATOM   15740 O  O    . GLU   B  2  440 ? 36.504  17.430  24.954   1.00 129.80 ? 444  GLU   B O    1 
ATOM   15741 C  CB   . GLU   B  2  440 ? 36.393  15.627  27.049   1.00 147.98 ? 444  GLU   B CB   1 
ATOM   15742 C  CG   . GLU   B  2  440 ? 36.204  14.551  28.108   1.00 151.34 ? 444  GLU   B CG   1 
ATOM   15743 C  CD   . GLU   B  2  440 ? 37.504  13.866  28.486   1.00 151.79 ? 444  GLU   B CD   1 
ATOM   15744 O  OE1  . GLU   B  2  440 ? 38.576  14.327  28.039   1.00 152.83 ? 444  GLU   B OE1  1 
ATOM   15745 O  OE2  . GLU   B  2  440 ? 37.453  12.863  29.229   1.00 150.85 ? 444  GLU   B OE2  1 
ATOM   15746 H  H    . GLU   B  2  440 ? 33.542  14.917  26.329   1.00 174.77 ? 444  GLU   B H    1 
ATOM   15747 H  HA   . GLU   B  2  440 ? 34.581  16.585  27.132   1.00 172.31 ? 444  GLU   B HA   1 
ATOM   15748 H  HB2  . GLU   B  2  440 ? 36.942  15.251  26.343   1.00 177.56 ? 444  GLU   B HB2  1 
ATOM   15749 H  HB3  . GLU   B  2  440 ? 36.853  16.372  27.466   1.00 177.56 ? 444  GLU   B HB3  1 
ATOM   15750 H  HG2  . GLU   B  2  440 ? 35.834  14.956  28.908   1.00 181.59 ? 444  GLU   B HG2  1 
ATOM   15751 H  HG3  . GLU   B  2  440 ? 35.597  13.875  27.767   1.00 181.59 ? 444  GLU   B HG3  1 
ATOM   15752 N  N    . VAL   B  2  441 ? 34.273  17.738  24.810   1.00 132.18 ? 445  VAL   B N    1 
ATOM   15753 C  CA   . VAL   B  2  441 ? 34.370  18.614  23.650   1.00 129.84 ? 445  VAL   B CA   1 
ATOM   15754 C  C    . VAL   B  2  441 ? 35.029  19.933  24.036   1.00 129.03 ? 445  VAL   B C    1 
ATOM   15755 O  O    . VAL   B  2  441 ? 34.898  20.417  25.169   1.00 130.11 ? 445  VAL   B O    1 
ATOM   15756 C  CB   . VAL   B  2  441 ? 32.977  18.858  23.039   1.00 132.37 ? 445  VAL   B CB   1 
ATOM   15757 C  CG1  . VAL   B  2  441 ? 33.100  19.615  21.719   1.00 133.85 ? 445  VAL   B CG1  1 
ATOM   15758 C  CG2  . VAL   B  2  441 ? 32.233  17.543  22.855   1.00 129.74 ? 445  VAL   B CG2  1 
ATOM   15759 H  H    . VAL   B  2  441 ? 33.475  17.636  25.112   1.00 158.60 ? 445  VAL   B H    1 
ATOM   15760 H  HA   . VAL   B  2  441 ? 34.927  18.181  22.984   1.00 155.79 ? 445  VAL   B HA   1 
ATOM   15761 H  HB   . VAL   B  2  441 ? 32.456  19.406  23.647   1.00 158.83 ? 445  VAL   B HB   1 
ATOM   15762 H  HG11 . VAL   B  2  441 ? 32.408  19.307  21.113   1.00 160.60 ? 445  VAL   B HG11 1 
ATOM   15763 H  HG12 . VAL   B  2  441 ? 32.993  20.564  21.888   1.00 160.60 ? 445  VAL   B HG12 1 
ATOM   15764 H  HG13 . VAL   B  2  441 ? 33.975  19.443  21.337   1.00 160.60 ? 445  VAL   B HG13 1 
ATOM   15765 H  HG21 . VAL   B  2  441 ? 31.455  17.697  22.296   1.00 155.67 ? 445  VAL   B HG21 1 
ATOM   15766 H  HG22 . VAL   B  2  441 ? 32.824  16.902  22.430   1.00 155.67 ? 445  VAL   B HG22 1 
ATOM   15767 H  HG23 . VAL   B  2  441 ? 31.956  17.213  23.724   1.00 155.67 ? 445  VAL   B HG23 1 
ATOM   15768 N  N    . ASN   B  2  442 ? 35.741  20.525  23.077   1.00 127.77 ? 446  ASN   B N    1 
ATOM   15769 C  CA   . ASN   B  2  442 ? 36.359  21.839  23.242   1.00 130.19 ? 446  ASN   B CA   1 
ATOM   15770 C  C    . ASN   B  2  442 ? 37.172  21.904  24.533   1.00 132.50 ? 446  ASN   B C    1 
ATOM   15771 O  O    . ASN   B  2  442 ? 37.074  22.850  25.318   1.00 135.56 ? 446  ASN   B O    1 
ATOM   15772 C  CB   . ASN   B  2  442 ? 35.300  22.943  23.207   1.00 131.55 ? 446  ASN   B CB   1 
ATOM   15773 C  CG   . ASN   B  2  442 ? 34.496  22.940  21.920   1.00 128.44 ? 446  ASN   B CG   1 
ATOM   15774 O  OD1  . ASN   B  2  442 ? 34.906  22.351  20.920   1.00 124.84 ? 446  ASN   B OD1  1 
ATOM   15775 N  ND2  . ASN   B  2  442 ? 33.346  23.605  21.939   1.00 130.12 ? 446  ASN   B ND2  1 
ATOM   15776 H  H    . ASN   B  2  442 ? 35.884  20.176  22.304   1.00 153.30 ? 446  ASN   B H    1 
ATOM   15777 H  HA   . ASN   B  2  442 ? 36.972  21.985  22.504   1.00 156.21 ? 446  ASN   B HA   1 
ATOM   15778 H  HB2  . ASN   B  2  442 ? 34.685  22.815  23.946   1.00 157.84 ? 446  ASN   B HB2  1 
ATOM   15779 H  HB3  . ASN   B  2  442 ? 35.738  23.805  23.286   1.00 157.84 ? 446  ASN   B HB3  1 
ATOM   15780 H  HD21 . ASN   B  2  442 ? 32.854  23.633  21.234   1.00 156.12 ? 446  ASN   B HD21 1 
ATOM   15781 H  HD22 . ASN   B  2  442 ? 33.094  24.007  22.656   1.00 156.12 ? 446  ASN   B HD22 1 
ATOM   15782 N  N    . SER   B  2  443 ? 37.988  20.877  24.749   1.00 131.12 ? 447  SER   B N    1 
ATOM   15783 C  CA   . SER   B  2  443 ? 38.762  20.774  25.976   1.00 131.62 ? 447  SER   B CA   1 
ATOM   15784 C  C    . SER   B  2  443 ? 39.998  21.663  25.914   1.00 131.87 ? 447  SER   B C    1 
ATOM   15785 O  O    . SER   B  2  443 ? 40.528  21.958  24.839   1.00 127.35 ? 447  SER   B O    1 
ATOM   15786 C  CB   . SER   B  2  443 ? 39.178  19.324  26.224   1.00 128.39 ? 447  SER   B CB   1 
ATOM   15787 O  OG   . SER   B  2  443 ? 39.514  19.122  27.585   1.00 129.31 ? 447  SER   B OG   1 
ATOM   15788 H  H    . SER   B  2  443 ? 38.111  20.228  24.199   1.00 157.33 ? 447  SER   B H    1 
ATOM   15789 H  HA   . SER   B  2  443 ? 38.217  21.067  26.723   1.00 157.92 ? 447  SER   B HA   1 
ATOM   15790 H  HB2  . SER   B  2  443 ? 38.440  18.739  25.991   1.00 154.04 ? 447  SER   B HB2  1 
ATOM   15791 H  HB3  . SER   B  2  443 ? 39.950  19.119  25.674   1.00 154.04 ? 447  SER   B HB3  1 
ATOM   15792 H  HG   . SER   B  2  443 ? 39.194  18.394  27.855   1.00 155.15 ? 447  SER   B HG   1 
ATOM   15793 N  N    . SER   B  2  444 ? 40.455  22.094  27.093   1.00 122.53 ? 448  SER   B N    1 
ATOM   15794 C  CA   . SER   B  2  444 ? 41.668  22.901  27.166   1.00 125.32 ? 448  SER   B CA   1 
ATOM   15795 C  C    . SER   B  2  444 ? 42.874  22.148  26.624   1.00 120.74 ? 448  SER   B C    1 
ATOM   15796 O  O    . SER   B  2  444 ? 43.846  22.768  26.177   1.00 116.90 ? 448  SER   B O    1 
ATOM   15797 C  CB   . SER   B  2  444 ? 41.929  23.324  28.611   1.00 131.89 ? 448  SER   B CB   1 
ATOM   15798 O  OG   . SER   B  2  444 ? 42.192  22.194  29.426   1.00 134.65 ? 448  SER   B OG   1 
ATOM   15799 H  H    . SER   B  2  444 ? 40.085  21.933  27.853   1.00 147.01 ? 448  SER   B H    1 
ATOM   15800 H  HA   . SER   B  2  444 ? 41.540  23.700  26.631   1.00 150.36 ? 448  SER   B HA   1 
ATOM   15801 H  HB2  . SER   B  2  444 ? 42.697  23.915  28.634   1.00 158.25 ? 448  SER   B HB2  1 
ATOM   15802 H  HB3  . SER   B  2  444 ? 41.146  23.784  28.953   1.00 158.25 ? 448  SER   B HB3  1 
ATOM   15803 H  HG   . SER   B  2  444 ? 42.716  22.404  30.048   1.00 161.56 ? 448  SER   B HG   1 
ATOM   15804 N  N    . LYS   B  2  445 ? 42.831  20.817  26.654   1.00 119.60 ? 449  LYS   B N    1 
ATOM   15805 C  CA   . LYS   B  2  445 ? 43.958  19.989  26.244   1.00 115.12 ? 449  LYS   B CA   1 
ATOM   15806 C  C    . LYS   B  2  445 ? 44.163  19.952  24.734   1.00 107.94 ? 449  LYS   B C    1 
ATOM   15807 O  O    . LYS   B  2  445 ? 45.076  19.255  24.278   1.00 103.03 ? 449  LYS   B O    1 
ATOM   15808 C  CB   . LYS   B  2  445 ? 43.761  18.568  26.780   1.00 115.05 ? 449  LYS   B CB   1 
ATOM   15809 C  CG   . LYS   B  2  445 ? 44.018  18.442  28.277   1.00 117.86 ? 449  LYS   B CG   1 
ATOM   15810 C  CD   . LYS   B  2  445 ? 43.273  17.268  28.902   1.00 118.97 ? 449  LYS   B CD   1 
ATOM   15811 C  CE   . LYS   B  2  445 ? 41.788  17.568  29.061   1.00 120.73 ? 449  LYS   B CE   1 
ATOM   15812 N  NZ   . LYS   B  2  445 ? 41.119  16.627  30.004   1.00 123.07 ? 449  LYS   B NZ   1 
ATOM   15813 H  H    . LYS   B  2  445 ? 42.148  20.363  26.914   1.00 143.50 ? 449  LYS   B H    1 
ATOM   15814 H  HA   . LYS   B  2  445 ? 44.769  20.353  26.630   1.00 138.12 ? 449  LYS   B HA   1 
ATOM   15815 H  HB2  . LYS   B  2  445 ? 42.846  18.295  26.612   1.00 138.04 ? 449  LYS   B HB2  1 
ATOM   15816 H  HB3  . LYS   B  2  445 ? 44.375  17.973  26.322   1.00 138.04 ? 449  LYS   B HB3  1 
ATOM   15817 H  HG2  . LYS   B  2  445 ? 44.967  18.307  28.426   1.00 141.42 ? 449  LYS   B HG2  1 
ATOM   15818 H  HG3  . LYS   B  2  445 ? 43.725  19.253  28.720   1.00 141.42 ? 449  LYS   B HG3  1 
ATOM   15819 H  HD2  . LYS   B  2  445 ? 43.367  16.489  28.332   1.00 142.74 ? 449  LYS   B HD2  1 
ATOM   15820 H  HD3  . LYS   B  2  445 ? 43.642  17.084  29.779   1.00 142.74 ? 449  LYS   B HD3  1 
ATOM   15821 H  HE2  . LYS   B  2  445 ? 41.681  18.469  29.405   1.00 144.86 ? 449  LYS   B HE2  1 
ATOM   15822 H  HE3  . LYS   B  2  445 ? 41.354  17.489  28.197   1.00 144.86 ? 449  LYS   B HE3  1 
ATOM   15823 H  HZ1  . LYS   B  2  445 ? 40.298  16.916  30.191   1.00 147.66 ? 449  LYS   B HZ1  1 
ATOM   15824 H  HZ2  . LYS   B  2  445 ? 41.064  15.818  29.640   1.00 147.66 ? 449  LYS   B HZ2  1 
ATOM   15825 H  HZ3  . LYS   B  2  445 ? 41.585  16.573  30.761   1.00 147.66 ? 449  LYS   B HZ3  1 
ATOM   15826 N  N    . CYS   B  2  446 ? 43.361  20.674  23.953   1.00 108.76 ? 450  CYS   B N    1 
ATOM   15827 C  CA   . CYS   B  2  446 ? 43.469  20.686  22.495   1.00 110.60 ? 450  CYS   B CA   1 
ATOM   15828 C  C    . CYS   B  2  446 ? 43.505  22.120  21.973   1.00 111.90 ? 450  CYS   B C    1 
ATOM   15829 O  O    . CYS   B  2  446 ? 42.787  22.495  21.044   1.00 109.51 ? 450  CYS   B O    1 
ATOM   15830 C  CB   . CYS   B  2  446 ? 42.328  19.891  21.862   1.00 113.73 ? 450  CYS   B CB   1 
ATOM   15831 S  SG   . CYS   B  2  446 ? 42.237  18.159  22.413   1.00 115.53 ? 450  CYS   B SG   1 
ATOM   15832 H  H    . CYS   B  2  446 ? 42.731  21.176  24.252   1.00 130.50 ? 450  CYS   B H    1 
ATOM   15833 H  HA   . CYS   B  2  446 ? 44.308  20.268  22.243   1.00 132.69 ? 450  CYS   B HA   1 
ATOM   15834 H  HB2  . CYS   B  2  446 ? 41.488  20.318  22.091   1.00 136.45 ? 450  CYS   B HB2  1 
ATOM   15835 H  HB3  . CYS   B  2  446 ? 42.448  19.888  20.900   1.00 136.45 ? 450  CYS   B HB3  1 
ATOM   15836 N  N    . HIS   B  2  447 ? 44.365  22.943  22.575   1.00 114.80 ? 451  HIS   B N    1 
ATOM   15837 C  CA   . HIS   B  2  447 ? 44.643  24.298  22.099   1.00 114.70 ? 451  HIS   B CA   1 
ATOM   15838 C  C    . HIS   B  2  447 ? 43.386  25.172  22.110   1.00 116.60 ? 451  HIS   B C    1 
ATOM   15839 O  O    . HIS   B  2  447 ? 42.893  25.625  21.075   1.00 118.93 ? 451  HIS   B O    1 
ATOM   15840 C  CB   . HIS   B  2  447 ? 45.268  24.257  20.700   1.00 110.18 ? 451  HIS   B CB   1 
ATOM   15841 C  CG   . HIS   B  2  447 ? 46.023  25.497  20.340   1.00 110.30 ? 451  HIS   B CG   1 
ATOM   15842 N  ND1  . HIS   B  2  447 ? 47.119  25.933  21.053   1.00 111.88 ? 451  HIS   B ND1  1 
ATOM   15843 C  CD2  . HIS   B  2  447 ? 45.844  26.394  19.341   1.00 109.75 ? 451  HIS   B CD2  1 
ATOM   15844 C  CE1  . HIS   B  2  447 ? 47.581  27.045  20.511   1.00 112.82 ? 451  HIS   B CE1  1 
ATOM   15845 N  NE2  . HIS   B  2  447 ? 46.825  27.346  19.470   1.00 111.45 ? 451  HIS   B NE2  1 
ATOM   15846 H  H    . HIS   B  2  447 ? 44.810  22.734  23.280   1.00 137.75 ? 451  HIS   B H    1 
ATOM   15847 H  HA   . HIS   B  2  447 ? 45.276  24.706  22.711   1.00 137.62 ? 451  HIS   B HA   1 
ATOM   15848 H  HB2  . HIS   B  2  447 ? 45.886  23.511  20.657   1.00 132.19 ? 451  HIS   B HB2  1 
ATOM   15849 H  HB3  . HIS   B  2  447 ? 44.561  24.140  20.046   1.00 132.19 ? 451  HIS   B HB3  1 
ATOM   15850 H  HD2  . HIS   B  2  447 ? 45.180  26.369  18.690   1.00 131.68 ? 451  HIS   B HD2  1 
ATOM   15851 H  HE1  . HIS   B  2  447 ? 48.314  27.533  20.810   1.00 135.36 ? 451  HIS   B HE1  1 
ATOM   15852 H  HE2  . HIS   B  2  447 ? 46.931  28.028  18.956   1.00 133.73 ? 451  HIS   B HE2  1 
ATOM   15853 N  N    . HIS   B  2  448 ? 42.873  25.402  23.318   1.00 115.06 ? 452  HIS   B N    1 
ATOM   15854 C  CA   . HIS   B  2  448 ? 41.781  26.345  23.557   1.00 113.77 ? 452  HIS   B CA   1 
ATOM   15855 C  C    . HIS   B  2  448 ? 40.551  25.995  22.717   1.00 116.00 ? 452  HIS   B C    1 
ATOM   15856 O  O    . HIS   B  2  448 ? 40.041  26.803  21.937   1.00 117.85 ? 452  HIS   B O    1 
ATOM   15857 C  CB   . HIS   B  2  448 ? 42.234  27.783  23.282   1.00 108.77 ? 452  HIS   B CB   1 
ATOM   15858 C  CG   . HIS   B  2  448 ? 43.616  28.090  23.769   1.00 107.72 ? 452  HIS   B CG   1 
ATOM   15859 N  ND1  . HIS   B  2  448 ? 43.906  28.317  25.097   1.00 109.68 ? 452  HIS   B ND1  1 
ATOM   15860 C  CD2  . HIS   B  2  448 ? 44.787  28.220  23.101   1.00 106.88 ? 452  HIS   B CD2  1 
ATOM   15861 C  CE1  . HIS   B  2  448 ? 45.197  28.567  25.227   1.00 110.86 ? 452  HIS   B CE1  1 
ATOM   15862 N  NE2  . HIS   B  2  448 ? 45.754  28.516  24.031   1.00 109.06 ? 452  HIS   B NE2  1 
ATOM   15863 H  H    . HIS   B  2  448 ? 43.148  25.013  24.035   1.00 138.05 ? 452  HIS   B H    1 
ATOM   15864 H  HA   . HIS   B  2  448 ? 41.526  26.275  24.491   1.00 136.50 ? 452  HIS   B HA   1 
ATOM   15865 H  HB2  . HIS   B  2  448 ? 42.218  27.936  22.324   1.00 130.50 ? 452  HIS   B HB2  1 
ATOM   15866 H  HB3  . HIS   B  2  448 ? 41.623  28.392  23.726   1.00 130.50 ? 452  HIS   B HB3  1 
ATOM   15867 H  HD2  . HIS   B  2  448 ? 44.913  28.126  22.184   1.00 128.24 ? 452  HIS   B HD2  1 
ATOM   15868 H  HE1  . HIS   B  2  448 ? 45.638  28.749  26.026   1.00 133.01 ? 452  HIS   B HE1  1 
ATOM   15869 H  HE2  . HIS   B  2  448 ? 46.587  28.647  23.861   1.00 130.85 ? 452  HIS   B HE2  1 
ATOM   15870 N  N    . GLY   B  2  449 ? 40.075  24.765  22.893   1.00 115.88 ? 453  GLY   B N    1 
ATOM   15871 C  CA   . GLY   B  2  449 ? 38.840  24.356  22.255   1.00 116.14 ? 453  GLY   B CA   1 
ATOM   15872 C  C    . GLY   B  2  449 ? 38.936  24.085  20.773   1.00 115.43 ? 453  GLY   B C    1 
ATOM   15873 O  O    . GLY   B  2  449 ? 37.907  24.048  20.094   1.00 114.26 ? 453  GLY   B O    1 
ATOM   15874 H  H    . GLY   B  2  449 ? 40.449  24.157  23.373   1.00 139.04 ? 453  GLY   B H    1 
ATOM   15875 H  HA2  . GLY   B  2  449 ? 38.526  23.544  22.682   1.00 139.34 ? 453  GLY   B HA2  1 
ATOM   15876 H  HA3  . GLY   B  2  449 ? 38.181  25.056  22.383   1.00 139.34 ? 453  GLY   B HA3  1 
ATOM   15877 N  N    . ASN   B  2  450 ? 40.142  23.890  20.245   1.00 116.07 ? 454  ASN   B N    1 
ATOM   15878 C  CA   . ASN   B  2  450 ? 40.316  23.579  18.832   1.00 113.26 ? 454  ASN   B CA   1 
ATOM   15879 C  C    . ASN   B  2  450 ? 40.157  22.097  18.526   1.00 111.14 ? 454  ASN   B C    1 
ATOM   15880 O  O    . ASN   B  2  450 ? 40.250  21.708  17.357   1.00 108.11 ? 454  ASN   B O    1 
ATOM   15881 C  CB   . ASN   B  2  450 ? 41.689  24.060  18.360   1.00 110.27 ? 454  ASN   B CB   1 
ATOM   15882 C  CG   . ASN   B  2  450 ? 41.646  25.462  17.796   1.00 105.83 ? 454  ASN   B CG   1 
ATOM   15883 O  OD1  . ASN   B  2  450 ? 40.826  25.768  16.932   1.00 104.63 ? 454  ASN   B OD1  1 
ATOM   15884 N  ND2  . ASN   B  2  450 ? 42.520  26.327  18.290   1.00 104.63 ? 454  ASN   B ND2  1 
ATOM   15885 H  H    . ASN   B  2  450 ? 40.878  23.932  20.688   1.00 139.26 ? 454  ASN   B H    1 
ATOM   15886 H  HA   . ASN   B  2  450 ? 39.642  24.057  18.324   1.00 135.89 ? 454  ASN   B HA   1 
ATOM   15887 H  HB2  . ASN   B  2  450 ? 42.302  24.056  19.112   1.00 132.31 ? 454  ASN   B HB2  1 
ATOM   15888 H  HB3  . ASN   B  2  450 ? 42.012  23.465  17.665   1.00 132.31 ? 454  ASN   B HB3  1 
ATOM   15889 H  HD21 . ASN   B  2  450 ? 42.534  27.136  18.000   1.00 125.53 ? 454  ASN   B HD21 1 
ATOM   15890 H  HD22 . ASN   B  2  450 ? 43.073  26.078  18.899   1.00 125.53 ? 454  ASN   B HD22 1 
ATOM   15891 N  N    . GLY   B  2  451 ? 39.919  21.268  19.538   1.00 112.49 ? 455  GLY   B N    1 
ATOM   15892 C  CA   . GLY   B  2  451 ? 39.682  19.855  19.326   1.00 111.56 ? 455  GLY   B CA   1 
ATOM   15893 C  C    . GLY   B  2  451 ? 39.002  19.266  20.542   1.00 111.48 ? 455  GLY   B C    1 
ATOM   15894 O  O    . GLY   B  2  451 ? 38.677  19.968  21.502   1.00 110.35 ? 455  GLY   B O    1 
ATOM   15895 H  H    . GLY   B  2  451 ? 39.891  21.506  20.364   1.00 134.97 ? 455  GLY   B H    1 
ATOM   15896 H  HA2  . GLY   B  2  451 ? 39.113  19.726  18.551   1.00 133.85 ? 455  GLY   B HA2  1 
ATOM   15897 H  HA3  . GLY   B  2  451 ? 40.523  19.395  19.180   1.00 133.85 ? 455  GLY   B HA3  1 
ATOM   15898 N  N    . SER   B  2  452 ? 38.787  17.955  20.488   1.00 112.71 ? 456  SER   B N    1 
ATOM   15899 C  CA   . SER   B  2  452 ? 38.162  17.212  21.573   1.00 113.87 ? 456  SER   B CA   1 
ATOM   15900 C  C    . SER   B  2  452 ? 39.125  16.152  22.088   1.00 117.49 ? 456  SER   B C    1 
ATOM   15901 O  O    . SER   B  2  452 ? 39.789  15.466  21.304   1.00 118.83 ? 456  SER   B O    1 
ATOM   15902 C  CB   . SER   B  2  452 ? 36.855  16.557  21.111   1.00 110.12 ? 456  SER   B CB   1 
ATOM   15903 O  OG   . SER   B  2  452 ? 37.085  15.662  20.038   1.00 107.58 ? 456  SER   B OG   1 
ATOM   15904 H  H    . SER   B  2  452 ? 39.001  17.463  19.816   1.00 135.23 ? 456  SER   B H    1 
ATOM   15905 H  HA   . SER   B  2  452 ? 37.955  17.814  22.304   1.00 136.62 ? 456  SER   B HA   1 
ATOM   15906 H  HB2  . SER   B  2  452 ? 36.470  16.066  21.854   1.00 132.13 ? 456  SER   B HB2  1 
ATOM   15907 H  HB3  . SER   B  2  452 ? 36.243  17.250  20.818   1.00 132.13 ? 456  SER   B HB3  1 
ATOM   15908 H  HG   . SER   B  2  452 ? 36.382  15.235  19.865   1.00 129.07 ? 456  SER   B HG   1 
ATOM   15909 N  N    . PHE   B  2  453 ? 39.197  16.025  23.412   1.00 118.14 ? 457  PHE   B N    1 
ATOM   15910 C  CA   . PHE   B  2  453 ? 40.076  15.059  24.065   1.00 116.69 ? 457  PHE   B CA   1 
ATOM   15911 C  C    . PHE   B  2  453 ? 39.278  13.787  24.327   1.00 116.53 ? 457  PHE   B C    1 
ATOM   15912 O  O    . PHE   B  2  453 ? 38.392  13.769  25.187   1.00 118.38 ? 457  PHE   B O    1 
ATOM   15913 C  CB   . PHE   B  2  453 ? 40.637  15.641  25.359   1.00 117.32 ? 457  PHE   B CB   1 
ATOM   15914 C  CG   . PHE   B  2  453 ? 42.004  15.131  25.712   1.00 119.36 ? 457  PHE   B CG   1 
ATOM   15915 C  CD1  . PHE   B  2  453 ? 43.088  15.400  24.893   1.00 120.96 ? 457  PHE   B CD1  1 
ATOM   15916 C  CD2  . PHE   B  2  453 ? 42.209  14.398  26.868   1.00 120.53 ? 457  PHE   B CD2  1 
ATOM   15917 C  CE1  . PHE   B  2  453 ? 44.348  14.938  25.214   1.00 121.94 ? 457  PHE   B CE1  1 
ATOM   15918 C  CE2  . PHE   B  2  453 ? 43.469  13.935  27.195   1.00 121.87 ? 457  PHE   B CE2  1 
ATOM   15919 C  CZ   . PHE   B  2  453 ? 44.540  14.206  26.367   1.00 122.38 ? 457  PHE   B CZ   1 
ATOM   15920 H  H    . PHE   B  2  453 ? 38.738  16.498  23.964   1.00 141.75 ? 457  PHE   B H    1 
ATOM   15921 H  HA   . PHE   B  2  453 ? 40.821  14.842  23.481   1.00 140.01 ? 457  PHE   B HA   1 
ATOM   15922 H  HB2  . PHE   B  2  453 ? 40.696  16.605  25.268   1.00 140.76 ? 457  PHE   B HB2  1 
ATOM   15923 H  HB3  . PHE   B  2  453 ? 40.039  15.413  26.088   1.00 140.76 ? 457  PHE   B HB3  1 
ATOM   15924 H  HD1  . PHE   B  2  453 ? 42.965  15.898  24.118   1.00 145.13 ? 457  PHE   B HD1  1 
ATOM   15925 H  HD2  . PHE   B  2  453 ? 41.491  14.215  27.430   1.00 144.62 ? 457  PHE   B HD2  1 
ATOM   15926 H  HE1  . PHE   B  2  453 ? 45.068  15.119  24.653   1.00 146.31 ? 457  PHE   B HE1  1 
ATOM   15927 H  HE2  . PHE   B  2  453 ? 43.595  13.441  27.973   1.00 146.23 ? 457  PHE   B HE2  1 
ATOM   15928 H  HZ   . PHE   B  2  453 ? 45.389  13.896  26.587   1.00 146.84 ? 457  PHE   B HZ   1 
ATOM   15929 N  N    . GLN   B  2  454 ? 39.595  12.722  23.591   1.00 114.76 ? 458  GLN   B N    1 
ATOM   15930 C  CA   . GLN   B  2  454 ? 38.780  11.511  23.587   1.00 112.95 ? 458  GLN   B CA   1 
ATOM   15931 C  C    . GLN   B  2  454 ? 39.359  10.409  24.469   1.00 110.82 ? 458  GLN   B C    1 
ATOM   15932 O  O    . GLN   B  2  454 ? 38.702  9.954   25.410   1.00 113.75 ? 458  GLN   B O    1 
ATOM   15933 C  CB   . GLN   B  2  454 ? 38.622  11.017  22.142   1.00 110.93 ? 458  GLN   B CB   1 
ATOM   15934 C  CG   . GLN   B  2  454 ? 37.263  10.404  21.836   1.00 110.85 ? 458  GLN   B CG   1 
ATOM   15935 C  CD   . GLN   B  2  454 ? 37.078  10.071  20.361   1.00 110.65 ? 458  GLN   B CD   1 
ATOM   15936 O  OE1  . GLN   B  2  454 ? 36.468  9.059   20.018   1.00 111.42 ? 458  GLN   B OE1  1 
ATOM   15937 N  NE2  . GLN   B  2  454 ? 37.592  10.928  19.484   1.00 109.02 ? 458  GLN   B NE2  1 
ATOM   15938 H  H    . GLN   B  2  454 ? 40.285  12.677  23.080   1.00 137.69 ? 458  GLN   B H    1 
ATOM   15939 H  HA   . GLN   B  2  454 ? 37.904  11.726  23.945   1.00 135.52 ? 458  GLN   B HA   1 
ATOM   15940 H  HB2  . GLN   B  2  454 ? 38.747  11.768  21.542   1.00 133.10 ? 458  GLN   B HB2  1 
ATOM   15941 H  HB3  . GLN   B  2  454 ? 39.295  10.339  21.971   1.00 133.10 ? 458  GLN   B HB3  1 
ATOM   15942 H  HG2  . GLN   B  2  454 ? 37.166  9.583   22.342   1.00 133.00 ? 458  GLN   B HG2  1 
ATOM   15943 H  HG3  . GLN   B  2  454 ? 36.570  11.034  22.089   1.00 133.00 ? 458  GLN   B HG3  1 
ATOM   15944 H  HE21 . GLN   B  2  454 ? 38.005  11.630  19.761   1.00 130.80 ? 458  GLN   B HE21 1 
ATOM   15945 H  HE22 . GLN   B  2  454 ? 37.511  10.781  18.641   1.00 130.80 ? 458  GLN   B HE22 1 
ATOM   15946 N  N    . CYS   B  2  455 ? 40.583  9.968   24.180   1.00 106.19 ? 459  CYS   B N    1 
ATOM   15947 C  CA   . CYS   B  2  455 ? 41.202  8.846   24.882   1.00 107.40 ? 459  CYS   B CA   1 
ATOM   15948 C  C    . CYS   B  2  455 ? 42.666  9.141   25.166   1.00 103.34 ? 459  CYS   B C    1 
ATOM   15949 O  O    . CYS   B  2  455 ? 43.538  8.287   24.972   1.00 96.39  ? 459  CYS   B O    1 
ATOM   15950 C  CB   . CYS   B  2  455 ? 41.072  7.554   24.076   1.00 113.74 ? 459  CYS   B CB   1 
ATOM   15951 S  SG   . CYS   B  2  455 ? 39.379  6.982   23.839   1.00 119.77 ? 459  CYS   B SG   1 
ATOM   15952 H  H    . CYS   B  2  455 ? 41.084  10.309  23.570   1.00 127.41 ? 459  CYS   B H    1 
ATOM   15953 H  HA   . CYS   B  2  455 ? 40.747  8.728   25.731   1.00 128.87 ? 459  CYS   B HA   1 
ATOM   15954 H  HB2  . CYS   B  2  455 ? 41.457  7.700   23.198   1.00 136.47 ? 459  CYS   B HB2  1 
ATOM   15955 H  HB3  . CYS   B  2  455 ? 41.556  6.853   24.539   1.00 136.47 ? 459  CYS   B HB3  1 
ATOM   15956 N  N    . GLY   B  2  456 ? 42.959  10.351  25.630   1.00 105.56 ? 460  GLY   B N    1 
ATOM   15957 C  CA   . GLY   B  2  456 ? 44.333  10.789  25.744   1.00 105.73 ? 460  GLY   B CA   1 
ATOM   15958 C  C    . GLY   B  2  456 ? 44.917  11.331  24.461   1.00 104.79 ? 460  GLY   B C    1 
ATOM   15959 O  O    . GLY   B  2  456 ? 46.134  11.537  24.387   1.00 107.89 ? 460  GLY   B O    1 
ATOM   15960 H  H    . GLY   B  2  456 ? 42.378  10.932  25.884   1.00 126.65 ? 460  GLY   B H    1 
ATOM   15961 H  HA2  . GLY   B  2  456 ? 44.385  11.488  26.414   1.00 126.85 ? 460  GLY   B HA2  1 
ATOM   15962 H  HA3  . GLY   B  2  456 ? 44.879  10.039  26.027   1.00 126.85 ? 460  GLY   B HA3  1 
ATOM   15963 N  N    . VAL   B  2  457 ? 44.086  11.559  23.445   1.00 101.24 ? 461  VAL   B N    1 
ATOM   15964 C  CA   . VAL   B  2  457 ? 44.516  12.097  22.161   1.00 99.40  ? 461  VAL   B CA   1 
ATOM   15965 C  C    . VAL   B  2  457 ? 43.496  13.141  21.727   1.00 100.67 ? 461  VAL   B C    1 
ATOM   15966 O  O    . VAL   B  2  457 ? 42.313  13.059  22.070   1.00 102.37 ? 461  VAL   B O    1 
ATOM   15967 C  CB   . VAL   B  2  457 ? 44.656  10.986  21.095   1.00 95.66  ? 461  VAL   B CB   1 
ATOM   15968 C  CG1  . VAL   B  2  457 ? 45.191  11.553  19.788   1.00 94.77  ? 461  VAL   B CG1  1 
ATOM   15969 C  CG2  . VAL   B  2  457 ? 45.558  9.868   21.604   1.00 95.54  ? 461  VAL   B CG2  1 
ATOM   15970 H  H    . VAL   B  2  457 ? 43.240  11.405  23.479   1.00 121.46 ? 461  VAL   B H    1 
ATOM   15971 H  HA   . VAL   B  2  457 ? 45.379  12.529  22.256   1.00 119.26 ? 461  VAL   B HA   1 
ATOM   15972 H  HB   . VAL   B  2  457 ? 43.779  10.612  20.920   1.00 114.77 ? 461  VAL   B HB   1 
ATOM   15973 H  HG11 . VAL   B  2  457 ? 45.347  10.824  19.168   1.00 113.70 ? 461  VAL   B HG11 1 
ATOM   15974 H  HG12 . VAL   B  2  457 ? 44.537  12.167  19.419   1.00 113.70 ? 461  VAL   B HG12 1 
ATOM   15975 H  HG13 . VAL   B  2  457 ? 46.022  12.022  19.964   1.00 113.70 ? 461  VAL   B HG13 1 
ATOM   15976 H  HG21 . VAL   B  2  457 ? 45.664  9.205   20.905   1.00 114.62 ? 461  VAL   B HG21 1 
ATOM   15977 H  HG22 . VAL   B  2  457 ? 46.421  10.241  21.841   1.00 114.62 ? 461  VAL   B HG22 1 
ATOM   15978 H  HG23 . VAL   B  2  457 ? 45.148  9.463   22.385   1.00 114.62 ? 461  VAL   B HG23 1 
ATOM   15979 N  N    . CYS   B  2  458 ? 43.962  14.133  20.971   1.00 100.49 ? 462  CYS   B N    1 
ATOM   15980 C  CA   . CYS   B  2  458 ? 43.097  15.202  20.490   1.00 101.80 ? 462  CYS   B CA   1 
ATOM   15981 C  C    . CYS   B  2  458 ? 42.526  14.845  19.124   1.00 96.28  ? 462  CYS   B C    1 
ATOM   15982 O  O    . CYS   B  2  458 ? 43.274  14.529  18.193   1.00 91.97  ? 462  CYS   B O    1 
ATOM   15983 C  CB   . CYS   B  2  458 ? 43.858  16.526  20.407   1.00 108.34 ? 462  CYS   B CB   1 
ATOM   15984 S  SG   . CYS   B  2  458 ? 44.064  17.362  22.000   1.00 113.58 ? 462  CYS   B SG   1 
ATOM   15985 H  H    . CYS   B  2  458 ? 44.782  14.208  20.723   1.00 120.57 ? 462  CYS   B H    1 
ATOM   15986 H  HA   . CYS   B  2  458 ? 42.360  15.309  21.111   1.00 122.14 ? 462  CYS   B HA   1 
ATOM   15987 H  HB2  . CYS   B  2  458 ? 44.742  16.354  20.048   1.00 129.98 ? 462  CYS   B HB2  1 
ATOM   15988 H  HB3  . CYS   B  2  458 ? 43.372  17.127  19.820   1.00 129.98 ? 462  CYS   B HB3  1 
ATOM   15989 N  N    . ALA   B  2  459 ? 41.201  14.893  19.012   1.00 97.19  ? 463  ALA   B N    1 
ATOM   15990 C  CA   . ALA   B  2  459 ? 40.506  14.791  17.734   1.00 99.49  ? 463  ALA   B CA   1 
ATOM   15991 C  C    . ALA   B  2  459 ? 40.174  16.212  17.293   1.00 104.49 ? 463  ALA   B C    1 
ATOM   15992 O  O    . ALA   B  2  459 ? 39.283  16.853  17.860   1.00 106.37 ? 463  ALA   B O    1 
ATOM   15993 C  CB   . ALA   B  2  459 ? 39.250  13.933  17.858   1.00 97.53  ? 463  ALA   B CB   1 
ATOM   15994 H  H    . ALA   B  2  459 ? 40.670  14.987  19.682   1.00 116.61 ? 463  ALA   B H    1 
ATOM   15995 H  HA   . ALA   B  2  459 ? 41.077  14.373  17.071   1.00 119.37 ? 463  ALA   B HA   1 
ATOM   15996 H  HB1  . ALA   B  2  459 ? 38.813  13.887  16.993   1.00 117.01 ? 463  ALA   B HB1  1 
ATOM   15997 H  HB2  . ALA   B  2  459 ? 39.502  13.043  18.149   1.00 117.01 ? 463  ALA   B HB2  1 
ATOM   15998 H  HB3  . ALA   B  2  459 ? 38.654  14.338  18.508   1.00 117.01 ? 463  ALA   B HB3  1 
ATOM   15999 N  N    . CYS   B  2  460 ? 40.889  16.701  16.285   1.00 106.53 ? 464  CYS   B N    1 
ATOM   16000 C  CA   . CYS   B  2  460 ? 40.883  18.122  15.977   1.00 108.94 ? 464  CYS   B CA   1 
ATOM   16001 C  C    . CYS   B  2  460 ? 39.625  18.532  15.222   1.00 112.12 ? 464  CYS   B C    1 
ATOM   16002 O  O    . CYS   B  2  460 ? 39.007  17.736  14.510   1.00 112.57 ? 464  CYS   B O    1 
ATOM   16003 C  CB   . CYS   B  2  460 ? 42.117  18.491  15.154   1.00 109.70 ? 464  CYS   B CB   1 
ATOM   16004 S  SG   . CYS   B  2  460 ? 43.663  18.285  16.051   1.00 110.22 ? 464  CYS   B SG   1 
ATOM   16005 H  H    . CYS   B  2  460 ? 41.385  16.228  15.766   1.00 127.82 ? 464  CYS   B H    1 
ATOM   16006 H  HA   . CYS   B  2  460 ? 40.899  18.620  16.809   1.00 130.71 ? 464  CYS   B HA   1 
ATOM   16007 H  HB2  . CYS   B  2  460 ? 42.151  17.924  14.368   1.00 131.62 ? 464  CYS   B HB2  1 
ATOM   16008 H  HB3  . CYS   B  2  460 ? 42.049  19.422  14.889   1.00 131.62 ? 464  CYS   B HB3  1 
ATOM   16009 N  N    . HIS   B  2  461 ? 39.256  19.800  15.393   1.00 114.66 ? 465  HIS   B N    1 
ATOM   16010 C  CA   . HIS   B  2  461 ? 38.154  20.393  14.660   1.00 115.88 ? 465  HIS   B CA   1 
ATOM   16011 C  C    . HIS   B  2  461 ? 38.573  20.675  13.219   1.00 115.96 ? 465  HIS   B C    1 
ATOM   16012 O  O    . HIS   B  2  461 ? 39.764  20.758  12.915   1.00 112.41 ? 465  HIS   B O    1 
ATOM   16013 C  CB   . HIS   B  2  461 ? 37.713  21.688  15.336   1.00 116.69 ? 465  HIS   B CB   1 
ATOM   16014 C  CG   . HIS   B  2  461 ? 37.031  21.481  16.653   1.00 117.54 ? 465  HIS   B CG   1 
ATOM   16015 N  ND1  . HIS   B  2  461 ? 36.787  20.231  17.179   1.00 117.75 ? 465  HIS   B ND1  1 
ATOM   16016 C  CD2  . HIS   B  2  461 ? 36.539  22.369  17.549   1.00 118.67 ? 465  HIS   B CD2  1 
ATOM   16017 C  CE1  . HIS   B  2  461 ? 36.175  20.357  18.342   1.00 118.39 ? 465  HIS   B CE1  1 
ATOM   16018 N  NE2  . HIS   B  2  461 ? 36.012  21.644  18.590   1.00 119.06 ? 465  HIS   B NE2  1 
ATOM   16019 H  H    . HIS   B  2  461 ? 39.637  20.344  15.939   1.00 137.58 ? 465  HIS   B H    1 
ATOM   16020 H  HA   . HIS   B  2  461 ? 37.401  19.782  14.646   1.00 139.04 ? 465  HIS   B HA   1 
ATOM   16021 H  HB2  . HIS   B  2  461 ? 38.495  22.240  15.491   1.00 140.01 ? 465  HIS   B HB2  1 
ATOM   16022 H  HB3  . HIS   B  2  461 ? 37.091  22.149  14.751   1.00 140.01 ? 465  HIS   B HB3  1 
ATOM   16023 H  HD2  . HIS   B  2  461 ? 36.554  23.296  17.474   1.00 142.39 ? 465  HIS   B HD2  1 
ATOM   16024 H  HE1  . HIS   B  2  461 ? 35.904  19.658  18.893   1.00 142.05 ? 465  HIS   B HE1  1 
ATOM   16025 H  HE2  . HIS   B  2  461 ? 35.638  21.975  19.290   1.00 142.85 ? 465  HIS   B HE2  1 
ATOM   16026 N  N    . PRO   B  2  462 ? 37.609  20.829  12.312   1.00 120.35 ? 466  PRO   B N    1 
ATOM   16027 C  CA   . PRO   B  2  462 ? 37.964  21.136  10.921   1.00 122.50 ? 466  PRO   B CA   1 
ATOM   16028 C  C    . PRO   B  2  462 ? 38.775  22.420  10.825   1.00 122.35 ? 466  PRO   B C    1 
ATOM   16029 O  O    . PRO   B  2  462 ? 38.475  23.419  11.483   1.00 122.10 ? 466  PRO   B O    1 
ATOM   16030 C  CB   . PRO   B  2  462 ? 36.604  21.270  10.224   1.00 125.51 ? 466  PRO   B CB   1 
ATOM   16031 C  CG   . PRO   B  2  462 ? 35.616  21.489  11.328   1.00 125.65 ? 466  PRO   B CG   1 
ATOM   16032 C  CD   . PRO   B  2  462 ? 36.152  20.728  12.497   1.00 122.64 ? 466  PRO   B CD   1 
ATOM   16033 H  HA   . PRO   B  2  462 ? 38.464  20.405  10.524   1.00 146.98 ? 466  PRO   B HA   1 
ATOM   16034 H  HB2  . PRO   B  2  462 ? 36.618  22.026  9.617    1.00 150.59 ? 466  PRO   B HB2  1 
ATOM   16035 H  HB3  . PRO   B  2  462 ? 36.403  20.456  9.736    1.00 150.59 ? 466  PRO   B HB3  1 
ATOM   16036 H  HG2  . PRO   B  2  462 ? 35.554  22.436  11.531   1.00 150.76 ? 466  PRO   B HG2  1 
ATOM   16037 H  HG3  . PRO   B  2  462 ? 34.746  21.150  11.063   1.00 150.76 ? 466  PRO   B HG3  1 
ATOM   16038 H  HD2  . PRO   B  2  462 ? 35.879  21.137  13.333   1.00 147.15 ? 466  PRO   B HD2  1 
ATOM   16039 H  HD3  . PRO   B  2  462 ? 35.862  19.802  12.471   1.00 147.15 ? 466  PRO   B HD3  1 
ATOM   16040 N  N    . GLY   B  2  463 ? 39.816  22.383  9.999    1.00 122.13 ? 467  GLY   B N    1 
ATOM   16041 C  CA   . GLY   B  2  463 ? 40.675  23.533  9.823    1.00 121.10 ? 467  GLY   B CA   1 
ATOM   16042 C  C    . GLY   B  2  463 ? 41.783  23.660  10.840   1.00 118.03 ? 467  GLY   B C    1 
ATOM   16043 O  O    . GLY   B  2  463 ? 42.388  24.735  10.942   1.00 117.26 ? 467  GLY   B O    1 
ATOM   16044 H  H    . GLY   B  2  463 ? 40.041  21.698  9.530    1.00 146.54 ? 467  GLY   B H    1 
ATOM   16045 H  HA2  . GLY   B  2  463 ? 41.083  23.484  8.944    1.00 145.30 ? 467  GLY   B HA2  1 
ATOM   16046 H  HA3  . GLY   B  2  463 ? 40.133  24.336  9.874    1.00 145.30 ? 467  GLY   B HA3  1 
ATOM   16047 N  N    . HIS   B  2  464 ? 42.075  22.603  11.594   1.00 116.19 ? 468  HIS   B N    1 
ATOM   16048 C  CA   . HIS   B  2  464 ? 43.128  22.636  12.604   1.00 115.21 ? 468  HIS   B CA   1 
ATOM   16049 C  C    . HIS   B  2  464 ? 43.881  21.315  12.566   1.00 114.14 ? 468  HIS   B C    1 
ATOM   16050 O  O    . HIS   B  2  464 ? 43.313  20.261  12.870   1.00 113.91 ? 468  HIS   B O    1 
ATOM   16051 C  CB   . HIS   B  2  464 ? 42.550  22.905  13.993   1.00 114.48 ? 468  HIS   B CB   1 
ATOM   16052 C  CG   . HIS   B  2  464 ? 42.018  24.294  14.158   1.00 112.59 ? 468  HIS   B CG   1 
ATOM   16053 N  ND1  . HIS   B  2  464 ? 40.727  24.641  13.824   1.00 111.78 ? 468  HIS   B ND1  1 
ATOM   16054 C  CD2  . HIS   B  2  464 ? 42.610  25.428  14.600   1.00 112.25 ? 468  HIS   B CD2  1 
ATOM   16055 C  CE1  . HIS   B  2  464 ? 40.543  25.927  14.064   1.00 112.23 ? 468  HIS   B CE1  1 
ATOM   16056 N  NE2  . HIS   B  2  464 ? 41.670  26.428  14.537   1.00 113.19 ? 468  HIS   B NE2  1 
ATOM   16057 H  H    . HIS   B  2  464 ? 41.671  21.846  11.537   1.00 139.41 ? 468  HIS   B H    1 
ATOM   16058 H  HA   . HIS   B  2  464 ? 43.757  23.343  12.390   1.00 138.24 ? 468  HIS   B HA   1 
ATOM   16059 H  HB2  . HIS   B  2  464 ? 41.821  22.286  14.154   1.00 137.36 ? 468  HIS   B HB2  1 
ATOM   16060 H  HB3  . HIS   B  2  464 ? 43.248  22.773  14.654   1.00 137.36 ? 468  HIS   B HB3  1 
ATOM   16061 H  HD2  . HIS   B  2  464 ? 43.489  25.515  14.892   1.00 134.68 ? 468  HIS   B HD2  1 
ATOM   16062 H  HE1  . HIS   B  2  464 ? 39.754  26.400  13.923   1.00 134.66 ? 468  HIS   B HE1  1 
ATOM   16063 H  HE2  . HIS   B  2  464 ? 41.795  27.247  14.768   1.00 135.81 ? 468  HIS   B HE2  1 
ATOM   16064 N  N    . MET   B  2  465 ? 45.157  21.377  12.193   1.00 113.47 ? 469  MET   B N    1 
ATOM   16065 C  CA   . MET   B  2  465 ? 46.012  20.207  12.064   1.00 113.68 ? 469  MET   B CA   1 
ATOM   16066 C  C    . MET   B  2  465 ? 47.100  20.249  13.129   1.00 113.89 ? 469  MET   B C    1 
ATOM   16067 O  O    . MET   B  2  465 ? 47.624  21.320  13.450   1.00 116.93 ? 469  MET   B O    1 
ATOM   16068 C  CB   . MET   B  2  465 ? 46.649  20.150  10.673   1.00 117.00 ? 469  MET   B CB   1 
ATOM   16069 C  CG   . MET   B  2  465 ? 45.645  20.090  9.531    1.00 120.82 ? 469  MET   B CG   1 
ATOM   16070 S  SD   . MET   B  2  465 ? 46.420  20.223  7.907    1.00 124.90 ? 469  MET   B SD   1 
ATOM   16071 C  CE   . MET   B  2  465 ? 44.991  20.071  6.836    1.00 126.35 ? 469  MET   B CE   1 
ATOM   16072 H  H    . MET   B  2  465 ? 45.560  22.112  12.002   1.00 136.14 ? 469  MET   B H    1 
ATOM   16073 H  HA   . MET   B  2  465 ? 45.482  19.404  12.185   1.00 136.39 ? 469  MET   B HA   1 
ATOM   16074 H  HB2  . MET   B  2  465 ? 47.191  20.945  10.547   1.00 140.39 ? 469  MET   B HB2  1 
ATOM   16075 H  HB3  . MET   B  2  465 ? 47.205  19.357  10.618   1.00 140.39 ? 469  MET   B HB3  1 
ATOM   16076 H  HG2  . MET   B  2  465 ? 45.174  19.243  9.569    1.00 144.96 ? 469  MET   B HG2  1 
ATOM   16077 H  HG3  . MET   B  2  465 ? 45.017  20.824  9.624    1.00 144.96 ? 469  MET   B HG3  1 
ATOM   16078 H  HE1  . MET   B  2  465 ? 45.254  20.285  5.927    1.00 151.60 ? 469  MET   B HE1  1 
ATOM   16079 H  HE2  . MET   B  2  465 ? 44.660  19.160  6.879    1.00 151.60 ? 469  MET   B HE2  1 
ATOM   16080 H  HE3  . MET   B  2  465 ? 44.305  20.687  7.136    1.00 151.60 ? 469  MET   B HE3  1 
ATOM   16081 N  N    . GLY   B  2  466 ? 47.431  19.083  13.677   1.00 111.88 ? 470  GLY   B N    1 
ATOM   16082 C  CA   . GLY   B  2  466 ? 48.492  18.976  14.649   1.00 110.15 ? 470  GLY   B CA   1 
ATOM   16083 C  C    . GLY   B  2  466 ? 48.160  18.014  15.771   1.00 107.46 ? 470  GLY   B C    1 
ATOM   16084 O  O    . GLY   B  2  466 ? 47.002  17.634  15.972   1.00 105.86 ? 470  GLY   B O    1 
ATOM   16085 H  H    . GLY   B  2  466 ? 47.047  18.335  13.495   1.00 134.23 ? 470  GLY   B H    1 
ATOM   16086 H  HA2  . GLY   B  2  466 ? 49.299  18.665  14.210   1.00 132.17 ? 470  GLY   B HA2  1 
ATOM   16087 H  HA3  . GLY   B  2  466 ? 48.660  19.849  15.037   1.00 132.17 ? 470  GLY   B HA3  1 
ATOM   16088 N  N    . PRO   B  2  467 ? 49.180  17.595  16.528   1.00 107.00 ? 471  PRO   B N    1 
ATOM   16089 C  CA   . PRO   B  2  467 ? 48.912  16.692  17.660   1.00 108.23 ? 471  PRO   B CA   1 
ATOM   16090 C  C    . PRO   B  2  467 ? 47.917  17.263  18.654   1.00 112.23 ? 471  PRO   B C    1 
ATOM   16091 O  O    . PRO   B  2  467 ? 47.099  16.515  19.205   1.00 114.65 ? 471  PRO   B O    1 
ATOM   16092 C  CB   . PRO   B  2  467 ? 50.301  16.497  18.287   1.00 106.66 ? 471  PRO   B CB   1 
ATOM   16093 C  CG   . PRO   B  2  467 ? 51.265  16.798  17.187   1.00 105.93 ? 471  PRO   B CG   1 
ATOM   16094 C  CD   . PRO   B  2  467 ? 50.618  17.873  16.368   1.00 105.92 ? 471  PRO   B CD   1 
ATOM   16095 H  HA   . PRO   B  2  467 ? 48.587  15.839  17.333   1.00 129.85 ? 471  PRO   B HA   1 
ATOM   16096 H  HB2  . PRO   B  2  467 ? 50.418  17.110  19.029   1.00 127.98 ? 471  PRO   B HB2  1 
ATOM   16097 H  HB3  . PRO   B  2  467 ? 50.399  15.582  18.594   1.00 127.98 ? 471  PRO   B HB3  1 
ATOM   16098 H  HG2  . PRO   B  2  467 ? 52.104  17.109  17.562   1.00 127.10 ? 471  PRO   B HG2  1 
ATOM   16099 H  HG3  . PRO   B  2  467 ? 51.414  16.002  16.654   1.00 127.10 ? 471  PRO   B HG3  1 
ATOM   16100 H  HD2  . PRO   B  2  467 ? 50.841  18.752  16.712   1.00 127.09 ? 471  PRO   B HD2  1 
ATOM   16101 H  HD3  . PRO   B  2  467 ? 50.882  17.805  15.437   1.00 127.09 ? 471  PRO   B HD3  1 
ATOM   16102 N  N    . ARG   B  2  468 ? 47.965  18.573  18.902   1.00 112.00 ? 472  ARG   B N    1 
ATOM   16103 C  CA   . ARG   B  2  468 ? 47.012  19.242  19.780   1.00 108.21 ? 472  ARG   B CA   1 
ATOM   16104 C  C    . ARG   B  2  468 ? 46.224  20.320  19.043   1.00 104.60 ? 472  ARG   B C    1 
ATOM   16105 O  O    . ARG   B  2  468 ? 45.683  21.232  19.676   1.00 101.54 ? 472  ARG   B O    1 
ATOM   16106 C  CB   . ARG   B  2  468 ? 47.730  19.836  20.994   1.00 107.52 ? 472  ARG   B CB   1 
ATOM   16107 C  CG   . ARG   B  2  468 ? 48.301  18.779  21.928   1.00 109.35 ? 472  ARG   B CG   1 
ATOM   16108 C  CD   . ARG   B  2  468 ? 48.974  19.386  23.149   1.00 115.80 ? 472  ARG   B CD   1 
ATOM   16109 N  NE   . ARG   B  2  468 ? 49.565  18.353  23.997   1.00 121.74 ? 472  ARG   B NE   1 
ATOM   16110 C  CZ   . ARG   B  2  468 ? 50.312  18.592  25.071   1.00 125.24 ? 472  ARG   B CZ   1 
ATOM   16111 N  NH1  . ARG   B  2  468 ? 50.574  19.838  25.444   1.00 123.06 ? 472  ARG   B NH1  1 
ATOM   16112 N  NH2  . ARG   B  2  468 ? 50.802  17.580  25.773   1.00 128.50 ? 472  ARG   B NH2  1 
ATOM   16113 H  H    . ARG   B  2  468 ? 48.552  19.103  18.565   1.00 134.38 ? 472  ARG   B H    1 
ATOM   16114 H  HA   . ARG   B  2  468 ? 46.375  18.587  20.105   1.00 129.83 ? 472  ARG   B HA   1 
ATOM   16115 H  HB2  . ARG   B  2  468 ? 48.464  20.389  20.685   1.00 129.00 ? 472  ARG   B HB2  1 
ATOM   16116 H  HB3  . ARG   B  2  468 ? 47.100  20.372  21.500   1.00 129.00 ? 472  ARG   B HB3  1 
ATOM   16117 H  HG2  . ARG   B  2  468 ? 47.582  18.204  22.235   1.00 131.20 ? 472  ARG   B HG2  1 
ATOM   16118 H  HG3  . ARG   B  2  468 ? 48.963  18.255  21.449   1.00 131.20 ? 472  ARG   B HG3  1 
ATOM   16119 H  HD2  . ARG   B  2  468 ? 49.679  19.987  22.863   1.00 138.94 ? 472  ARG   B HD2  1 
ATOM   16120 H  HD3  . ARG   B  2  468 ? 48.316  19.870  23.672   1.00 138.94 ? 472  ARG   B HD3  1 
ATOM   16121 H  HE   . ARG   B  2  468 ? 49.420  17.532  23.786   1.00 146.07 ? 472  ARG   B HE   1 
ATOM   16122 H  HH11 . ARG   B  2  468 ? 50.259  20.497  24.990   1.00 147.65 ? 472  ARG   B HH11 1 
ATOM   16123 H  HH12 . ARG   B  2  468 ? 51.057  19.986  26.139   1.00 147.65 ? 472  ARG   B HH12 1 
ATOM   16124 H  HH21 . ARG   B  2  468 ? 50.637  16.771  25.533   1.00 154.18 ? 472  ARG   B HH21 1 
ATOM   16125 H  HH22 . ARG   B  2  468 ? 51.286  17.732  26.467   1.00 154.18 ? 472  ARG   B HH22 1 
ATOM   16126 N  N    . CYS   B  2  469 ? 46.149  20.234  17.714   1.00 105.59 ? 473  CYS   B N    1 
ATOM   16127 C  CA   . CYS   B  2  469 ? 45.329  21.143  16.915   1.00 108.03 ? 473  CYS   B CA   1 
ATOM   16128 C  C    . CYS   B  2  469 ? 45.832  22.579  17.050   1.00 111.00 ? 473  CYS   B C    1 
ATOM   16129 O  O    . CYS   B  2  469 ? 45.066  23.515  17.294   1.00 111.81 ? 473  CYS   B O    1 
ATOM   16130 C  CB   . CYS   B  2  469 ? 43.858  21.029  17.318   1.00 109.67 ? 473  CYS   B CB   1 
ATOM   16131 S  SG   . CYS   B  2  469 ? 43.365  19.348  17.756   1.00 111.30 ? 473  CYS   B SG   1 
ATOM   16132 H  H    . CYS   B  2  469 ? 46.570  19.648  17.246   1.00 126.69 ? 473  CYS   B H    1 
ATOM   16133 H  HA   . CYS   B  2  469 ? 45.403  20.898  15.980   1.00 129.62 ? 473  CYS   B HA   1 
ATOM   16134 H  HB2  . CYS   B  2  469 ? 43.699  21.597  18.088   1.00 131.59 ? 473  CYS   B HB2  1 
ATOM   16135 H  HB3  . CYS   B  2  469 ? 43.306  21.318  16.574   1.00 131.59 ? 473  CYS   B HB3  1 
ATOM   16136 N  N    . GLU   B  2  470 ? 47.141  22.748  16.873   1.00 112.81 ? 474  GLU   B N    1 
ATOM   16137 C  CA   . GLU   B  2  470 ? 47.815  24.010  17.137   1.00 115.67 ? 474  GLU   B CA   1 
ATOM   16138 C  C    . GLU   B  2  470 ? 48.109  24.814  15.877   1.00 111.94 ? 474  GLU   B C    1 
ATOM   16139 O  O    . GLU   B  2  470 ? 48.477  25.989  15.984   1.00 111.02 ? 474  GLU   B O    1 
ATOM   16140 C  CB   . GLU   B  2  470 ? 49.121  23.743  17.898   1.00 122.36 ? 474  GLU   B CB   1 
ATOM   16141 C  CG   . GLU   B  2  470 ? 48.932  22.862  19.130   1.00 125.91 ? 474  GLU   B CG   1 
ATOM   16142 C  CD   . GLU   B  2  470 ? 50.243  22.439  19.762   1.00 127.61 ? 474  GLU   B CD   1 
ATOM   16143 O  OE1  . GLU   B  2  470 ? 50.911  21.543  19.206   1.00 127.50 ? 474  GLU   B OE1  1 
ATOM   16144 O  OE2  . GLU   B  2  470 ? 50.606  23.007  20.814   1.00 128.31 ? 474  GLU   B OE2  1 
ATOM   16145 H  H    . GLU   B  2  470 ? 47.670  22.129  16.594   1.00 135.36 ? 474  GLU   B H    1 
ATOM   16146 H  HA   . GLU   B  2  470 ? 47.247  24.562  17.698   1.00 138.79 ? 474  GLU   B HA   1 
ATOM   16147 H  HB2  . GLU   B  2  470 ? 49.744  23.295  17.304   1.00 146.81 ? 474  GLU   B HB2  1 
ATOM   16148 H  HB3  . GLU   B  2  470 ? 49.493  24.590  18.190   1.00 146.81 ? 474  GLU   B HB3  1 
ATOM   16149 H  HG2  . GLU   B  2  470 ? 48.425  23.354  19.794   1.00 151.07 ? 474  GLU   B HG2  1 
ATOM   16150 H  HG3  . GLU   B  2  470 ? 48.452  22.060  18.873   1.00 151.07 ? 474  GLU   B HG3  1 
ATOM   16151 N  N    . SER   B  2  471 ? 47.953  24.220  14.696   1.00 109.52 ? 475  SER   B N    1 
ATOM   16152 C  CA   . SER   B  2  471 ? 48.115  24.916  13.428   1.00 110.29 ? 475  SER   B CA   1 
ATOM   16153 C  C    . SER   B  2  471 ? 46.799  24.871  12.664   1.00 107.00 ? 475  SER   B C    1 
ATOM   16154 O  O    . SER   B  2  471 ? 46.030  23.913  12.782   1.00 105.31 ? 475  SER   B O    1 
ATOM   16155 C  CB   . SER   B  2  471 ? 49.232  24.290  12.586   1.00 115.16 ? 475  SER   B CB   1 
ATOM   16156 O  OG   . SER   B  2  471 ? 48.912  22.957  12.228   1.00 119.46 ? 475  SER   B OG   1 
ATOM   16157 H  H    . SER   B  2  471 ? 47.748  23.390  14.604   1.00 131.41 ? 475  SER   B H    1 
ATOM   16158 H  HA   . SER   B  2  471 ? 48.351  25.843  13.586   1.00 132.33 ? 475  SER   B HA   1 
ATOM   16159 H  HB2  . SER   B  2  471 ? 49.349  24.814  11.778   1.00 138.17 ? 475  SER   B HB2  1 
ATOM   16160 H  HB3  . SER   B  2  471 ? 50.053  24.289  13.102   1.00 138.17 ? 475  SER   B HB3  1 
ATOM   16161 H  HG   . SER   B  2  471 ? 48.680  22.525  12.910   1.00 143.33 ? 475  SER   B HG   1 
ATOM   16162 N  N    . GLY   B  2  472 ? 46.546  25.916  11.877   1.00 107.00 ? 476  GLY   B N    1 
ATOM   16163 C  CA   . GLY   B  2  472 ? 45.270  26.050  11.200   1.00 107.59 ? 476  GLY   B CA   1 
ATOM   16164 C  C    . GLY   B  2  472 ? 45.366  26.181  9.694    1.00 110.33 ? 476  GLY   B C    1 
ATOM   16165 O  O    . GLY   B  2  472 ? 46.139  26.994  9.178    1.00 110.97 ? 476  GLY   B O    1 
ATOM   16166 H  H    . GLY   B  2  472 ? 47.099  26.556  11.723   1.00 128.38 ? 476  GLY   B H    1 
ATOM   16167 H  HA2  . GLY   B  2  472 ? 44.729  25.269  11.396   1.00 129.09 ? 476  GLY   B HA2  1 
ATOM   16168 H  HA3  . GLY   B  2  472 ? 44.819  26.839  11.538   1.00 129.09 ? 476  GLY   B HA3  1 
ATOM   16169 N  N    . HIS   B  2  473 ? 44.575  25.385  8.980    1.00 113.07 ? 477  HIS   B N    1 
ATOM   16170 C  CA   . HIS   B  2  473 ? 44.492  25.484  7.528    1.00 119.03 ? 477  HIS   B CA   1 
ATOM   16171 C  C    . HIS   B  2  473 ? 43.834  26.801  7.130    1.00 118.18 ? 477  HIS   B C    1 
ATOM   16172 O  O    . HIS   B  2  473 ? 42.608  26.919  7.136    1.00 117.35 ? 477  HIS   B O    1 
ATOM   16173 C  CB   . HIS   B  2  473 ? 43.706  24.303  6.950    1.00 126.63 ? 477  HIS   B CB   1 
ATOM   16174 C  CG   . HIS   B  2  473 ? 43.533  24.359  5.463    1.00 135.63 ? 477  HIS   B CG   1 
ATOM   16175 N  ND1  . HIS   B  2  473 ? 42.573  23.627  4.798    1.00 138.26 ? 477  HIS   B ND1  1 
ATOM   16176 C  CD2  . HIS   B  2  473 ? 44.198  25.058  4.512    1.00 139.04 ? 477  HIS   B CD2  1 
ATOM   16177 C  CE1  . HIS   B  2  473 ? 42.652  23.873  3.503    1.00 140.71 ? 477  HIS   B CE1  1 
ATOM   16178 N  NE2  . HIS   B  2  473 ? 43.630  24.739  3.303    1.00 140.85 ? 477  HIS   B NE2  1 
ATOM   16179 H  H    . HIS   B  2  473 ? 44.073  24.774  9.317    1.00 135.66 ? 477  HIS   B H    1 
ATOM   16180 H  HA   . HIS   B  2  473 ? 45.384  25.454  7.148    1.00 142.81 ? 477  HIS   B HA   1 
ATOM   16181 H  HB2  . HIS   B  2  473 ? 44.177  23.482  7.162    1.00 151.93 ? 477  HIS   B HB2  1 
ATOM   16182 H  HB3  . HIS   B  2  473 ? 42.823  24.292  7.351    1.00 151.93 ? 477  HIS   B HB3  1 
ATOM   16183 H  HD2  . HIS   B  2  473 ? 44.906  25.643  4.652    1.00 166.83 ? 477  HIS   B HD2  1 
ATOM   16184 H  HE1  . HIS   B  2  473 ? 42.112  23.501  2.844    1.00 168.83 ? 477  HIS   B HE1  1 
ATOM   16185 H  HE2  . HIS   B  2  473 ? 43.871  25.052  2.539    1.00 169.00 ? 477  HIS   B HE2  1 
ATOM   16186 N  N    . ASP   C  3  1   ? -9.255  -56.361 -48.275  1.00 88.86  ? 1    ASP   C N    1 
ATOM   16187 C  CA   . ASP   C  3  1   ? -8.263  -55.463 -48.932  1.00 84.12  ? 1    ASP   C CA   1 
ATOM   16188 C  C    . ASP   C  3  1   ? -8.926  -54.623 -50.016  1.00 83.06  ? 1    ASP   C C    1 
ATOM   16189 O  O    . ASP   C  3  1   ? -9.899  -55.049 -50.636  1.00 88.18  ? 1    ASP   C O    1 
ATOM   16190 C  CB   . ASP   C  3  1   ? -7.116  -56.276 -49.536  1.00 83.31  ? 1    ASP   C CB   1 
ATOM   16191 C  CG   . ASP   C  3  1   ? -6.373  -57.094 -48.502  1.00 86.60  ? 1    ASP   C CG   1 
ATOM   16192 O  OD1  . ASP   C  3  1   ? -6.823  -57.136 -47.338  1.00 88.87  ? 1    ASP   C OD1  1 
ATOM   16193 O  OD2  . ASP   C  3  1   ? -5.336  -57.694 -48.854  1.00 86.10  ? 1    ASP   C OD2  1 
ATOM   16194 H  H1   . ASP   C  3  1   ? -8.852  -56.830 -47.635  1.00 106.61 ? 1    ASP   C H1   1 
ATOM   16195 H  H2   . ASP   C  3  1   ? -9.908  -55.872 -47.919  1.00 106.61 ? 1    ASP   C H2   1 
ATOM   16196 H  H3   . ASP   C  3  1   ? -9.597  -56.918 -48.880  1.00 106.61 ? 1    ASP   C H3   1 
ATOM   16197 H  HA   . ASP   C  3  1   ? -7.891  -54.866 -48.264  1.00 100.93 ? 1    ASP   C HA   1 
ATOM   16198 H  HB2  . ASP   C  3  1   ? -7.475  -56.885 -50.200  1.00 99.95  ? 1    ASP   C HB2  1 
ATOM   16199 H  HB3  . ASP   C  3  1   ? -6.483  -55.669 -49.951  1.00 99.95  ? 1    ASP   C HB3  1 
ATOM   16200 N  N    . ILE   C  3  2   ? -8.390  -53.424 -50.239  1.00 83.44  ? 2    ILE   C N    1 
ATOM   16201 C  CA   . ILE   C  3  2   ? -8.892  -52.567 -51.306  1.00 84.60  ? 2    ILE   C CA   1 
ATOM   16202 C  C    . ILE   C  3  2   ? -8.456  -53.139 -52.647  1.00 83.27  ? 2    ILE   C C    1 
ATOM   16203 O  O    . ILE   C  3  2   ? -7.276  -53.455 -52.852  1.00 83.28  ? 2    ILE   C O    1 
ATOM   16204 C  CB   . ILE   C  3  2   ? -8.385  -51.128 -51.127  1.00 84.55  ? 2    ILE   C CB   1 
ATOM   16205 C  CG1  . ILE   C  3  2   ? -8.721  -50.597 -49.729  1.00 87.27  ? 2    ILE   C CG1  1 
ATOM   16206 C  CG2  . ILE   C  3  2   ? -8.979  -50.219 -52.196  1.00 85.31  ? 2    ILE   C CG2  1 
ATOM   16207 C  CD1  . ILE   C  3  2   ? -10.202 -50.428 -49.461  1.00 90.13  ? 2    ILE   C CD1  1 
ATOM   16208 H  H    . ILE   C  3  2   ? -7.740  -53.087 -49.789  1.00 100.11 ? 2    ILE   C H    1 
ATOM   16209 H  HA   . ILE   C  3  2   ? -9.861  -52.551 -51.273  1.00 101.50 ? 2    ILE   C HA   1 
ATOM   16210 H  HB   . ILE   C  3  2   ? -7.420  -51.137 -51.224  1.00 101.44 ? 2    ILE   C HB   1 
ATOM   16211 H  HG12 . ILE   C  3  2   ? -8.373  -51.219 -49.070  1.00 104.70 ? 2    ILE   C HG12 1 
ATOM   16212 H  HG13 . ILE   C  3  2   ? -8.302  -49.729 -49.619  1.00 104.70 ? 2    ILE   C HG13 1 
ATOM   16213 H  HG21 . ILE   C  3  2   ? -8.729  -49.301 -52.005  1.00 102.35 ? 2    ILE   C HG21 1 
ATOM   16214 H  HG22 . ILE   C  3  2   ? -8.633  -50.482 -53.063  1.00 102.35 ? 2    ILE   C HG22 1 
ATOM   16215 H  HG23 . ILE   C  3  2   ? -9.945  -50.307 -52.185  1.00 102.35 ? 2    ILE   C HG23 1 
ATOM   16216 H  HD11 . ILE   C  3  2   ? -10.326 -50.141 -48.543  1.00 108.14 ? 2    ILE   C HD11 1 
ATOM   16217 H  HD12 . ILE   C  3  2   ? -10.558 -49.759 -50.067  1.00 108.14 ? 2    ILE   C HD12 1 
ATOM   16218 H  HD13 . ILE   C  3  2   ? -10.648 -51.276 -49.606  1.00 108.14 ? 2    ILE   C HD13 1 
ATOM   16219 N  N    . GLN   C  3  3   ? -9.405  -53.276 -53.568  1.00 85.23  ? 3    GLN   C N    1 
ATOM   16220 C  CA   . GLN   C  3  3   ? -9.140  -53.802 -54.900  1.00 88.11  ? 3    GLN   C CA   1 
ATOM   16221 C  C    . GLN   C  3  3   ? -8.999  -52.639 -55.874  1.00 84.02  ? 3    GLN   C C    1 
ATOM   16222 O  O    . GLN   C  3  3   ? -9.949  -51.874 -56.075  1.00 87.11  ? 3    GLN   C O    1 
ATOM   16223 C  CB   . GLN   C  3  3   ? -10.258 -54.745 -55.347  1.00 99.83  ? 3    GLN   C CB   1 
ATOM   16224 C  CG   . GLN   C  3  3   ? -10.055 -55.341 -56.732  1.00 111.36 ? 3    GLN   C CG   1 
ATOM   16225 C  CD   . GLN   C  3  3   ? -8.863  -56.277 -56.796  1.00 119.50 ? 3    GLN   C CD   1 
ATOM   16226 O  OE1  . GLN   C  3  3   ? -8.802  -57.273 -56.076  1.00 123.96 ? 3    GLN   C OE1  1 
ATOM   16227 N  NE2  . GLN   C  3  3   ? -7.905  -55.958 -57.659  1.00 121.13 ? 3    GLN   C NE2  1 
ATOM   16228 H  H    . GLN   C  3  3   ? -10.229 -53.065 -53.440  1.00 102.26 ? 3    GLN   C H    1 
ATOM   16229 H  HA   . GLN   C  3  3   ? -8.308  -54.300 -54.892  1.00 105.71 ? 3    GLN   C HA   1 
ATOM   16230 H  HB2  . GLN   C  3  3   ? -10.316 -55.479 -54.716  1.00 119.78 ? 3    GLN   C HB2  1 
ATOM   16231 H  HB3  . GLN   C  3  3   ? -11.094 -54.252 -55.358  1.00 119.78 ? 3    GLN   C HB3  1 
ATOM   16232 H  HG2  . GLN   C  3  3   ? -10.846 -55.845 -56.979  1.00 133.62 ? 3    GLN   C HG2  1 
ATOM   16233 H  HG3  . GLN   C  3  3   ? -9.907  -54.623 -57.367  1.00 133.62 ? 3    GLN   C HG3  1 
ATOM   16234 H  HE21 . GLN   C  3  3   ? -7.981  -55.252 -58.145  1.00 145.34 ? 3    GLN   C HE21 1 
ATOM   16235 H  HE22 . GLN   C  3  3   ? -7.209  -56.457 -57.733  1.00 145.34 ? 3    GLN   C HE22 1 
ATOM   16236 N  N    . MET   C  3  4   ? -7.820  -52.509 -56.474  1.00 79.48  ? 4    MET   C N    1 
ATOM   16237 C  CA   . MET   C  3  4   ? -7.551  -51.475 -57.463  1.00 79.10  ? 4    MET   C CA   1 
ATOM   16238 C  C    . MET   C  3  4   ? -7.602  -52.091 -58.854  1.00 83.57  ? 4    MET   C C    1 
ATOM   16239 O  O    . MET   C  3  4   ? -6.908  -53.076 -59.128  1.00 87.02  ? 4    MET   C O    1 
ATOM   16240 C  CB   . MET   C  3  4   ? -6.189  -50.825 -57.220  1.00 75.57  ? 4    MET   C CB   1 
ATOM   16241 C  CG   . MET   C  3  4   ? -6.011  -50.268 -55.817  1.00 76.04  ? 4    MET   C CG   1 
ATOM   16242 S  SD   . MET   C  3  4   ? -7.312  -49.113 -55.339  1.00 80.70  ? 4    MET   C SD   1 
ATOM   16243 C  CE   . MET   C  3  4   ? -7.122  -47.844 -56.587  1.00 79.03  ? 4    MET   C CE   1 
ATOM   16244 H  H    . MET   C  3  4   ? -7.145  -53.020 -56.320  1.00 95.35  ? 4    MET   C H    1 
ATOM   16245 H  HA   . MET   C  3  4   ? -8.225  -50.780 -57.394  1.00 94.90  ? 4    MET   C HA   1 
ATOM   16246 H  HB2  . MET   C  3  4   ? -5.497  -51.490 -57.364  1.00 90.67  ? 4    MET   C HB2  1 
ATOM   16247 H  HB3  . MET   C  3  4   ? -6.078  -50.092 -57.845  1.00 90.67  ? 4    MET   C HB3  1 
ATOM   16248 H  HG2  . MET   C  3  4   ? -6.019  -51.003 -55.184  1.00 91.23  ? 4    MET   C HG2  1 
ATOM   16249 H  HG3  . MET   C  3  4   ? -5.164  -49.799 -55.770  1.00 91.23  ? 4    MET   C HG3  1 
ATOM   16250 H  HE1  . MET   C  3  4   ? -7.709  -47.101 -56.374  1.00 94.82  ? 4    MET   C HE1  1 
ATOM   16251 H  HE2  . MET   C  3  4   ? -6.200  -47.544 -56.595  1.00 94.82  ? 4    MET   C HE2  1 
ATOM   16252 H  HE3  . MET   C  3  4   ? -7.357  -48.214 -57.452  1.00 94.82  ? 4    MET   C HE3  1 
ATOM   16253 N  N    . THR   C  3  5   ? -8.419  -51.508 -59.727  1.00 84.61  ? 5    THR   C N    1 
ATOM   16254 C  CA   . THR   C  3  5   ? -8.642  -52.037 -61.064  1.00 84.60  ? 5    THR   C CA   1 
ATOM   16255 C  C    . THR   C  3  5   ? -8.439  -50.935 -62.090  1.00 83.04  ? 5    THR   C C    1 
ATOM   16256 O  O    . THR   C  3  5   ? -9.067  -49.875 -62.003  1.00 83.54  ? 5    THR   C O    1 
ATOM   16257 C  CB   . THR   C  3  5   ? -10.052 -52.623 -61.200  1.00 86.73  ? 5    THR   C CB   1 
ATOM   16258 O  OG1  . THR   C  3  5   ? -11.008 -51.706 -60.652  1.00 86.93  ? 5    THR   C OG1  1 
ATOM   16259 C  CG2  . THR   C  3  5   ? -10.148 -53.955 -60.475  1.00 87.00  ? 5    THR   C CG2  1 
ATOM   16260 H  H    . THR   C  3  5   ? -8.864  -50.790 -59.562  1.00 101.52 ? 5    THR   C H    1 
ATOM   16261 H  HA   . THR   C  3  5   ? -7.995  -52.738 -61.240  1.00 101.51 ? 5    THR   C HA   1 
ATOM   16262 H  HB   . THR   C  3  5   ? -10.253 -52.773 -62.137  1.00 104.05 ? 5    THR   C HB   1 
ATOM   16263 H  HG1  . THR   C  3  5   ? -11.781 -52.029 -60.709  1.00 104.30 ? 5    THR   C HG1  1 
ATOM   16264 H  HG21 . THR   C  3  5   ? -11.042 -54.321 -60.571  1.00 104.38 ? 5    THR   C HG21 1 
ATOM   16265 H  HG22 . THR   C  3  5   ? -9.510  -54.583 -60.848  1.00 104.38 ? 5    THR   C HG22 1 
ATOM   16266 H  HG23 . THR   C  3  5   ? -9.957  -53.834 -59.532  1.00 104.38 ? 5    THR   C HG23 1 
ATOM   16267 N  N    . GLN   C  3  6   ? -7.559  -51.188 -63.052  1.00 81.50  ? 6    GLN   C N    1 
ATOM   16268 C  CA   . GLN   C  3  6   ? -7.352  -50.317 -64.205  1.00 83.24  ? 6    GLN   C CA   1 
ATOM   16269 C  C    . GLN   C  3  6   ? -7.987  -51.025 -65.398  1.00 92.51  ? 6    GLN   C C    1 
ATOM   16270 O  O    . GLN   C  3  6   ? -7.407  -51.960 -65.958  1.00 94.43  ? 6    GLN   C O    1 
ATOM   16271 C  CB   . GLN   C  3  6   ? -5.869  -50.034 -64.418  1.00 79.35  ? 6    GLN   C CB   1 
ATOM   16272 C  CG   . GLN   C  3  6   ? -5.221  -49.325 -63.237  1.00 78.84  ? 6    GLN   C CG   1 
ATOM   16273 C  CD   . GLN   C  3  6   ? -3.725  -49.147 -63.399  1.00 78.43  ? 6    GLN   C CD   1 
ATOM   16274 O  OE1  . GLN   C  3  6   ? -2.947  -49.520 -62.522  1.00 79.12  ? 6    GLN   C OE1  1 
ATOM   16275 N  NE2  . GLN   C  3  6   ? -3.314  -48.565 -64.519  1.00 78.27  ? 6    GLN   C NE2  1 
ATOM   16276 H  H    . GLN   C  3  6   ? -7.052  -51.883 -63.060  1.00 97.78  ? 6    GLN   C H    1 
ATOM   16277 H  HA   . GLN   C  3  6   ? -7.792  -49.462 -64.073  1.00 99.87  ? 6    GLN   C HA   1 
ATOM   16278 H  HB2  . GLN   C  3  6   ? -5.405  -50.875 -64.554  1.00 95.21  ? 6    GLN   C HB2  1 
ATOM   16279 H  HB3  . GLN   C  3  6   ? -5.766  -49.469 -65.200  1.00 95.21  ? 6    GLN   C HB3  1 
ATOM   16280 H  HG2  . GLN   C  3  6   ? -5.618  -48.445 -63.142  1.00 94.58  ? 6    GLN   C HG2  1 
ATOM   16281 H  HG3  . GLN   C  3  6   ? -5.374  -49.846 -62.434  1.00 94.58  ? 6    GLN   C HG3  1 
ATOM   16282 H  HE21 . GLN   C  3  6   ? -3.888  -48.312 -65.108  1.00 93.90  ? 6    GLN   C HE21 1 
ATOM   16283 H  HE22 . GLN   C  3  6   ? -2.474  -48.442 -64.657  1.00 93.90  ? 6    GLN   C HE22 1 
ATOM   16284 N  N    . THR   C  3  7   ? -9.188  -50.577 -65.772  1.00 97.80  ? 7    THR   C N    1 
ATOM   16285 C  CA   . THR   C  3  7   ? -9.983  -51.282 -66.774  1.00 102.07 ? 7    THR   C CA   1 
ATOM   16286 C  C    . THR   C  3  7   ? -9.172  -51.578 -68.029  1.00 98.46  ? 7    THR   C C    1 
ATOM   16287 O  O    . THR   C  3  7   ? -9.110  -52.724 -68.489  1.00 100.89 ? 7    THR   C O    1 
ATOM   16288 C  CB   . THR   C  3  7   ? -11.227 -50.460 -67.119  1.00 110.58 ? 7    THR   C CB   1 
ATOM   16289 O  OG1  . THR   C  3  7   ? -10.844 -49.112 -67.422  1.00 113.03 ? 7    THR   C OG1  1 
ATOM   16290 C  CG2  . THR   C  3  7   ? -12.208 -50.462 -65.953  1.00 111.82 ? 7    THR   C CG2  1 
ATOM   16291 H  H    . THR   C  3  7   ? -9.563  -49.868 -65.461  1.00 117.35 ? 7    THR   C H    1 
ATOM   16292 H  HA   . THR   C  3  7   ? -10.269 -52.131 -66.400  1.00 122.47 ? 7    THR   C HA   1 
ATOM   16293 H  HB   . THR   C  3  7   ? -11.669 -50.848 -67.890  1.00 132.68 ? 7    THR   C HB   1 
ATOM   16294 H  HG1  . THR   C  3  7   ? -11.526 -48.646 -67.574  1.00 135.62 ? 7    THR   C HG1  1 
ATOM   16295 H  HG21 . THR   C  3  7   ? -12.993 -49.937 -66.179  1.00 134.17 ? 7    THR   C HG21 1 
ATOM   16296 H  HG22 . THR   C  3  7   ? -12.484 -51.370 -65.753  1.00 134.17 ? 7    THR   C HG22 1 
ATOM   16297 H  HG23 . THR   C  3  7   ? -11.790 -50.079 -65.166  1.00 134.17 ? 7    THR   C HG23 1 
ATOM   16298 N  N    . THR   C  3  8   ? -8.541  -50.555 -68.598  1.00 94.61  ? 8    THR   C N    1 
ATOM   16299 C  CA   . THR   C  3  8   ? -7.762  -50.704 -69.823  1.00 94.90  ? 8    THR   C CA   1 
ATOM   16300 C  C    . THR   C  3  8   ? -6.345  -51.131 -69.456  1.00 89.86  ? 8    THR   C C    1 
ATOM   16301 O  O    . THR   C  3  8   ? -5.586  -50.353 -68.868  1.00 80.97  ? 8    THR   C O    1 
ATOM   16302 C  CB   . THR   C  3  8   ? -7.755  -49.402 -70.619  1.00 96.86  ? 8    THR   C CB   1 
ATOM   16303 O  OG1  . THR   C  3  8   ? -7.251  -48.338 -69.801  1.00 100.79 ? 8    THR   C OG1  1 
ATOM   16304 C  CG2  . THR   C  3  8   ? -9.161  -49.055 -71.088  1.00 97.24  ? 8    THR   C CG2  1 
ATOM   16305 H  H    . THR   C  3  8   ? -8.549  -49.753 -68.289  1.00 113.51 ? 8    THR   C H    1 
ATOM   16306 H  HA   . THR   C  3  8   ? -8.160  -51.397 -70.373  1.00 113.86 ? 8    THR   C HA   1 
ATOM   16307 H  HB   . THR   C  3  8   ? -7.188  -49.504 -71.400  1.00 116.21 ? 8    THR   C HB   1 
ATOM   16308 H  HG1  . THR   C  3  8   ? -6.516  -48.561 -69.460  1.00 120.93 ? 8    THR   C HG1  1 
ATOM   16309 H  HG21 . THR   C  3  8   ? -9.145  -48.236 -71.608  1.00 116.67 ? 8    THR   C HG21 1 
ATOM   16310 H  HG22 . THR   C  3  8   ? -9.512  -49.771 -71.640  1.00 116.67 ? 8    THR   C HG22 1 
ATOM   16311 H  HG23 . THR   C  3  8   ? -9.744  -48.931 -70.323  1.00 116.67 ? 8    THR   C HG23 1 
ATOM   16312 N  N    . SER   C  3  9   ? -5.990  -52.369 -69.802  1.00 96.30  ? 9    SER   C N    1 
ATOM   16313 C  CA   . SER   C  3  9   ? -4.656  -52.887 -69.530  1.00 98.47  ? 9    SER   C CA   1 
ATOM   16314 C  C    . SER   C  3  9   ? -3.612  -52.393 -70.523  1.00 97.83  ? 9    SER   C C    1 
ATOM   16315 O  O    . SER   C  3  9   ? -2.417  -52.600 -70.290  1.00 96.72  ? 9    SER   C O    1 
ATOM   16316 C  CB   . SER   C  3  9   ? -4.677  -54.418 -69.536  1.00 102.87 ? 9    SER   C CB   1 
ATOM   16317 O  OG   . SER   C  3  9   ? -5.549  -54.926 -68.540  1.00 106.14 ? 9    SER   C OG   1 
ATOM   16318 H  H    . SER   C  3  9   ? -6.508  -52.929 -70.199  1.00 115.54 ? 9    SER   C H    1 
ATOM   16319 H  HA   . SER   C  3  9   ? -4.388  -52.593 -68.645  1.00 118.14 ? 9    SER   C HA   1 
ATOM   16320 H  HB2  . SER   C  3  9   ? -4.982  -54.725 -70.405  1.00 123.42 ? 9    SER   C HB2  1 
ATOM   16321 H  HB3  . SER   C  3  9   ? -3.780  -54.745 -69.364  1.00 123.42 ? 9    SER   C HB3  1 
ATOM   16322 H  HG   . SER   C  3  9   ? -5.536  -55.766 -68.549  1.00 127.35 ? 9    SER   C HG   1 
ATOM   16323 N  N    . SER   C  3  10  ? -4.024  -51.752 -71.613  1.00 96.70  ? 10   SER   C N    1 
ATOM   16324 C  CA   . SER   C  3  10  ? -3.084  -51.271 -72.618  1.00 91.39  ? 10   SER   C CA   1 
ATOM   16325 C  C    . SER   C  3  10  ? -3.816  -50.328 -73.559  1.00 90.48  ? 10   SER   C C    1 
ATOM   16326 O  O    . SER   C  3  10  ? -4.995  -50.530 -73.854  1.00 95.33  ? 10   SER   C O    1 
ATOM   16327 C  CB   . SER   C  3  10  ? -2.469  -52.435 -73.405  1.00 92.89  ? 10   SER   C CB   1 
ATOM   16328 O  OG   . SER   C  3  10  ? -1.622  -51.959 -74.436  1.00 90.94  ? 10   SER   C OG   1 
ATOM   16329 H  H    . SER   C  3  10  ? -4.848  -51.583 -71.794  1.00 116.02 ? 10   SER   C H    1 
ATOM   16330 H  HA   . SER   C  3  10  ? -2.370  -50.778 -72.185  1.00 109.64 ? 10   SER   C HA   1 
ATOM   16331 H  HB2  . SER   C  3  10  ? -1.948  -52.986 -72.798  1.00 111.44 ? 10   SER   C HB2  1 
ATOM   16332 H  HB3  . SER   C  3  10  ? -3.182  -52.961 -73.800  1.00 111.44 ? 10   SER   C HB3  1 
ATOM   16333 H  HG   . SER   C  3  10  ? -1.324  -52.604 -74.884  1.00 109.11 ? 10   SER   C HG   1 
ATOM   16334 N  N    . LEU   C  3  11  ? -3.106  -49.301 -74.027  1.00 86.94  ? 11   LEU   C N    1 
ATOM   16335 C  CA   . LEU   C  3  11  ? -3.675  -48.343 -74.964  1.00 89.37  ? 11   LEU   C CA   1 
ATOM   16336 C  C    . LEU   C  3  11  ? -2.565  -47.822 -75.865  1.00 88.08  ? 11   LEU   C C    1 
ATOM   16337 O  O    . LEU   C  3  11  ? -1.378  -47.913 -75.539  1.00 85.95  ? 11   LEU   C O    1 
ATOM   16338 C  CB   . LEU   C  3  11  ? -4.376  -47.189 -74.233  1.00 90.32  ? 11   LEU   C CB   1 
ATOM   16339 C  CG   . LEU   C  3  11  ? -3.517  -46.262 -73.369  1.00 86.96  ? 11   LEU   C CG   1 
ATOM   16340 C  CD1  . LEU   C  3  11  ? -2.945  -45.108 -74.183  1.00 89.61  ? 11   LEU   C CD1  1 
ATOM   16341 C  CD2  . LEU   C  3  11  ? -4.327  -45.734 -72.193  1.00 84.96  ? 11   LEU   C CD2  1 
ATOM   16342 H  H    . LEU   C  3  11  ? -2.289  -49.140 -73.814  1.00 104.31 ? 11   LEU   C H    1 
ATOM   16343 H  HA   . LEU   C  3  11  ? -4.333  -48.784 -75.523  1.00 107.23 ? 11   LEU   C HA   1 
ATOM   16344 H  HB2  . LEU   C  3  11  ? -4.802  -46.631 -74.903  1.00 108.36 ? 11   LEU   C HB2  1 
ATOM   16345 H  HB3  . LEU   C  3  11  ? -5.047  -47.574 -73.648  1.00 108.36 ? 11   LEU   C HB3  1 
ATOM   16346 H  HG   . LEU   C  3  11  ? -2.767  -46.773 -73.025  1.00 104.33 ? 11   LEU   C HG   1 
ATOM   16347 H  HD11 . LEU   C  3  11  ? -2.493  -44.493 -73.584  1.00 107.51 ? 11   LEU   C HD11 1 
ATOM   16348 H  HD12 . LEU   C  3  11  ? -2.316  -45.460 -74.832  1.00 107.51 ? 11   LEU   C HD12 1 
ATOM   16349 H  HD13 . LEU   C  3  11  ? -3.671  -44.653 -74.638  1.00 107.51 ? 11   LEU   C HD13 1 
ATOM   16350 H  HD21 . LEU   C  3  11  ? -3.771  -45.134 -71.671  1.00 101.93 ? 11   LEU   C HD21 1 
ATOM   16351 H  HD22 . LEU   C  3  11  ? -5.101  -45.258 -72.531  1.00 101.93 ? 11   LEU   C HD22 1 
ATOM   16352 H  HD23 . LEU   C  3  11  ? -4.612  -46.482 -71.645  1.00 101.93 ? 11   LEU   C HD23 1 
ATOM   16353 N  N    . SER   C  3  12  ? -2.968  -47.269 -77.007  1.00 89.71  ? 12   SER   C N    1 
ATOM   16354 C  CA   . SER   C  3  12  ? -2.047  -46.769 -78.016  1.00 89.33  ? 12   SER   C CA   1 
ATOM   16355 C  C    . SER   C  3  12  ? -2.269  -45.278 -78.229  1.00 86.25  ? 12   SER   C C    1 
ATOM   16356 O  O    . SER   C  3  12  ? -3.412  -44.816 -78.313  1.00 87.43  ? 12   SER   C O    1 
ATOM   16357 C  CB   . SER   C  3  12  ? -2.225  -47.520 -79.340  1.00 95.05  ? 12   SER   C CB   1 
ATOM   16358 O  OG   . SER   C  3  12  ? -3.597  -47.664 -79.663  1.00 100.96 ? 12   SER   C OG   1 
ATOM   16359 H  H    . SER   C  3  12  ? -3.795  -47.172 -77.222  1.00 107.63 ? 12   SER   C H    1 
ATOM   16360 H  HA   . SER   C  3  12  ? -1.133  -46.894 -77.714  1.00 107.17 ? 12   SER   C HA   1 
ATOM   16361 H  HB2  . SER   C  3  12  ? -1.786  -47.022 -80.047  1.00 114.04 ? 12   SER   C HB2  1 
ATOM   16362 H  HB3  . SER   C  3  12  ? -1.827  -48.401 -79.258  1.00 114.04 ? 12   SER   C HB3  1 
ATOM   16363 H  HG   . SER   C  3  12  ? -3.685  -48.185 -80.316  1.00 121.14 ? 12   SER   C HG   1 
ATOM   16364 N  N    . ALA   C  3  13  ? -1.170  -44.532 -78.321  1.00 81.81  ? 13   ALA   C N    1 
ATOM   16365 C  CA   . ALA   C  3  13  ? -1.222  -43.088 -78.495  1.00 82.77  ? 13   ALA   C CA   1 
ATOM   16366 C  C    . ALA   C  3  13  ? -0.069  -42.645 -79.384  1.00 81.53  ? 13   ALA   C C    1 
ATOM   16367 O  O    . ALA   C  3  13  ? 0.924   -43.356 -79.551  1.00 78.61  ? 13   ALA   C O    1 
ATOM   16368 C  CB   . ALA   C  3  13  ? -1.160  -42.356 -77.147  1.00 80.04  ? 13   ALA   C CB   1 
ATOM   16369 H  H    . ALA   C  3  13  ? -0.370  -44.847 -78.284  1.00 98.16  ? 13   ALA   C H    1 
ATOM   16370 H  HA   . ALA   C  3  13  ? -2.052  -42.849 -78.936  1.00 99.31  ? 13   ALA   C HA   1 
ATOM   16371 H  HB1  . ALA   C  3  13  ? -1.196  -41.400 -77.305  1.00 96.03  ? 13   ALA   C HB1  1 
ATOM   16372 H  HB2  . ALA   C  3  13  ? -1.914  -42.630 -76.603  1.00 96.03  ? 13   ALA   C HB2  1 
ATOM   16373 H  HB3  . ALA   C  3  13  ? -0.329  -42.586 -76.700  1.00 96.03  ? 13   ALA   C HB3  1 
ATOM   16374 N  N    . SER   C  3  14  ? -0.216  -41.452 -79.954  1.00 84.81  ? 14   SER   C N    1 
ATOM   16375 C  CA   . SER   C  3  14  ? 0.800   -40.846 -80.800  1.00 84.47  ? 14   SER   C CA   1 
ATOM   16376 C  C    . SER   C  3  14  ? 1.454   -39.677 -80.075  1.00 82.41  ? 14   SER   C C    1 
ATOM   16377 O  O    . SER   C  3  14  ? 0.929   -39.156 -79.087  1.00 83.77  ? 14   SER   C O    1 
ATOM   16378 C  CB   . SER   C  3  14  ? 0.198   -40.367 -82.127  1.00 89.98  ? 14   SER   C CB   1 
ATOM   16379 O  OG   . SER   C  3  14  ? -0.374  -41.444 -82.847  1.00 95.40  ? 14   SER   C OG   1 
ATOM   16380 H  H    . SER   C  3  14  ? -0.917  -40.962 -79.861  1.00 101.75 ? 14   SER   C H    1 
ATOM   16381 H  HA   . SER   C  3  14  ? 1.485   -41.503 -81.001  1.00 101.35 ? 14   SER   C HA   1 
ATOM   16382 H  HB2  . SER   C  3  14  ? -0.491  -39.711 -81.940  1.00 107.96 ? 14   SER   C HB2  1 
ATOM   16383 H  HB3  . SER   C  3  14  ? 0.900   -39.967 -82.664  1.00 107.96 ? 14   SER   C HB3  1 
ATOM   16384 H  HG   . SER   C  3  14  ? -0.653  -41.175 -83.593  1.00 114.46 ? 14   SER   C HG   1 
ATOM   16385 N  N    . LEU   C  3  15  ? 2.615   -39.266 -80.583  1.00 81.06  ? 15   LEU   C N    1 
ATOM   16386 C  CA   . LEU   C  3  15  ? 3.359   -38.176 -79.964  1.00 78.29  ? 15   LEU   C CA   1 
ATOM   16387 C  C    . LEU   C  3  15  ? 2.509   -36.913 -79.917  1.00 78.31  ? 15   LEU   C C    1 
ATOM   16388 O  O    . LEU   C  3  15  ? 1.886   -36.531 -80.912  1.00 82.01  ? 15   LEU   C O    1 
ATOM   16389 C  CB   . LEU   C  3  15  ? 4.653   -37.912 -80.733  1.00 81.29  ? 15   LEU   C CB   1 
ATOM   16390 C  CG   . LEU   C  3  15  ? 5.684   -39.042 -80.752  1.00 82.30  ? 15   LEU   C CG   1 
ATOM   16391 C  CD1  . LEU   C  3  15  ? 6.877   -38.645 -81.606  1.00 82.57  ? 15   LEU   C CD1  1 
ATOM   16392 C  CD2  . LEU   C  3  15  ? 6.132   -39.406 -79.344  1.00 80.32  ? 15   LEU   C CD2  1 
ATOM   16393 H  H    . LEU   C  3  15  ? 2.991   -39.601 -81.280  1.00 97.25  ? 15   LEU   C H    1 
ATOM   16394 H  HA   . LEU   C  3  15  ? 3.592   -38.425 -79.055  1.00 93.92  ? 15   LEU   C HA   1 
ATOM   16395 H  HB2  . LEU   C  3  15  ? 4.420   -37.725 -81.656  1.00 97.53  ? 15   LEU   C HB2  1 
ATOM   16396 H  HB3  . LEU   C  3  15  ? 5.085   -37.140 -80.337  1.00 97.53  ? 15   LEU   C HB3  1 
ATOM   16397 H  HG   . LEU   C  3  15  ? 5.274   -39.833 -81.138  1.00 98.74  ? 15   LEU   C HG   1 
ATOM   16398 H  HD11 . LEU   C  3  15  ? 7.517   -39.374 -81.614  1.00 99.07  ? 15   LEU   C HD11 1 
ATOM   16399 H  HD12 . LEU   C  3  15  ? 6.572   -38.463 -82.509  1.00 99.07  ? 15   LEU   C HD12 1 
ATOM   16400 H  HD13 . LEU   C  3  15  ? 7.285   -37.850 -81.228  1.00 99.07  ? 15   LEU   C HD13 1 
ATOM   16401 H  HD21 . LEU   C  3  15  ? 6.814   -40.092 -79.397  1.00 96.36  ? 15   LEU   C HD21 1 
ATOM   16402 H  HD22 . LEU   C  3  15  ? 6.491   -38.614 -78.913  1.00 96.36  ? 15   LEU   C HD22 1 
ATOM   16403 H  HD23 . LEU   C  3  15  ? 5.368   -39.736 -78.845  1.00 96.36  ? 15   LEU   C HD23 1 
ATOM   16404 N  N    . GLY   C  3  16  ? 2.489   -36.264 -78.753  1.00 78.18  ? 16   GLY   C N    1 
ATOM   16405 C  CA   . GLY   C  3  16  ? 1.703   -35.068 -78.549  1.00 80.80  ? 16   GLY   C CA   1 
ATOM   16406 C  C    . GLY   C  3  16  ? 0.283   -35.311 -78.088  1.00 82.43  ? 16   GLY   C C    1 
ATOM   16407 O  O    . GLY   C  3  16  ? -0.378  -34.362 -77.646  1.00 84.63  ? 16   GLY   C O    1 
ATOM   16408 H  H    . GLY   C  3  16  ? 2.934   -36.508 -78.059  1.00 93.80  ? 16   GLY   C H    1 
ATOM   16409 H  HA2  . GLY   C  3  16  ? 2.142   -34.519 -77.880  1.00 96.94  ? 16   GLY   C HA2  1 
ATOM   16410 H  HA3  . GLY   C  3  16  ? 1.663   -34.577 -79.384  1.00 96.94  ? 16   GLY   C HA3  1 
ATOM   16411 N  N    . ASP   C  3  17  ? -0.204  -36.546 -78.169  1.00 84.84  ? 17   ASP   C N    1 
ATOM   16412 C  CA   . ASP   C  3  17  ? -1.578  -36.842 -77.800  1.00 91.01  ? 17   ASP   C CA   1 
ATOM   16413 C  C    . ASP   C  3  17  ? -1.790  -36.681 -76.298  1.00 92.46  ? 17   ASP   C C    1 
ATOM   16414 O  O    . ASP   C  3  17  ? -0.851  -36.701 -75.498  1.00 90.57  ? 17   ASP   C O    1 
ATOM   16415 C  CB   . ASP   C  3  17  ? -1.952  -38.267 -78.212  1.00 89.50  ? 17   ASP   C CB   1 
ATOM   16416 C  CG   . ASP   C  3  17  ? -2.040  -38.439 -79.715  1.00 94.24  ? 17   ASP   C CG   1 
ATOM   16417 O  OD1  . ASP   C  3  17  ? -2.000  -37.420 -80.438  1.00 97.11  ? 17   ASP   C OD1  1 
ATOM   16418 O  OD2  . ASP   C  3  17  ? -2.149  -39.596 -80.175  1.00 94.19  ? 17   ASP   C OD2  1 
ATOM   16419 H  H    . ASP   C  3  17  ? 0.244   -37.230 -78.435  1.00 101.79 ? 17   ASP   C H    1 
ATOM   16420 H  HA   . ASP   C  3  17  ? -2.164  -36.221 -78.261  1.00 109.19 ? 17   ASP   C HA   1 
ATOM   16421 H  HB2  . ASP   C  3  17  ? -1.277  -38.879 -77.879  1.00 107.38 ? 17   ASP   C HB2  1 
ATOM   16422 H  HB3  . ASP   C  3  17  ? -2.817  -38.489 -77.833  1.00 107.38 ? 17   ASP   C HB3  1 
ATOM   16423 N  N    . ARG   C  3  18  ? -3.056  -36.521 -75.923  1.00 95.21  ? 18   ARG   C N    1 
ATOM   16424 C  CA   . ARG   C  3  18  ? -3.465  -36.523 -74.525  1.00 90.86  ? 18   ARG   C CA   1 
ATOM   16425 C  C    . ARG   C  3  18  ? -3.900  -37.933 -74.146  1.00 89.08  ? 18   ARG   C C    1 
ATOM   16426 O  O    . ARG   C  3  18  ? -4.776  -38.514 -74.796  1.00 96.15  ? 18   ARG   C O    1 
ATOM   16427 C  CB   . ARG   C  3  18  ? -4.596  -35.524 -74.289  1.00 91.83  ? 18   ARG   C CB   1 
ATOM   16428 C  CG   . ARG   C  3  18  ? -5.453  -35.840 -73.073  1.00 92.36  ? 18   ARG   C CG   1 
ATOM   16429 C  CD   . ARG   C  3  18  ? -6.267  -34.635 -72.635  1.00 102.16 ? 18   ARG   C CD   1 
ATOM   16430 N  NE   . ARG   C  3  18  ? -5.417  -33.575 -72.101  1.00 107.85 ? 18   ARG   C NE   1 
ATOM   16431 C  CZ   . ARG   C  3  18  ? -5.872  -32.450 -71.557  1.00 114.71 ? 18   ARG   C CZ   1 
ATOM   16432 N  NH1  . ARG   C  3  18  ? -7.176  -32.227 -71.469  1.00 119.34 ? 18   ARG   C NH1  1 
ATOM   16433 N  NH2  . ARG   C  3  18  ? -5.018  -31.546 -71.099  1.00 116.06 ? 18   ARG   C NH2  1 
ATOM   16434 H  H    . ARG   C  3  18  ? -3.708  -36.408 -76.472  1.00 114.23 ? 18   ARG   C H    1 
ATOM   16435 H  HA   . ARG   C  3  18  ? -2.717  -36.265 -73.964  1.00 109.02 ? 18   ARG   C HA   1 
ATOM   16436 H  HB2  . ARG   C  3  18  ? -4.212  -34.644 -74.159  1.00 110.18 ? 18   ARG   C HB2  1 
ATOM   16437 H  HB3  . ARG   C  3  18  ? -5.176  -35.522 -75.067  1.00 110.18 ? 18   ARG   C HB3  1 
ATOM   16438 H  HG2  . ARG   C  3  18  ? -6.067  -36.559 -73.291  1.00 110.82 ? 18   ARG   C HG2  1 
ATOM   16439 H  HG3  . ARG   C  3  18  ? -4.880  -36.104 -72.336  1.00 110.82 ? 18   ARG   C HG3  1 
ATOM   16440 H  HD2  . ARG   C  3  18  ? -6.751  -34.282 -73.397  1.00 122.57 ? 18   ARG   C HD2  1 
ATOM   16441 H  HD3  . ARG   C  3  18  ? -6.890  -34.904 -71.942  1.00 122.57 ? 18   ARG   C HD3  1 
ATOM   16442 H  HE   . ARG   C  3  18  ? -4.565  -33.685 -72.140  1.00 129.39 ? 18   ARG   C HE   1 
ATOM   16443 H  HH11 . ARG   C  3  18  ? -7.733  -32.812 -71.764  1.00 143.19 ? 18   ARG   C HH11 1 
ATOM   16444 H  HH12 . ARG   C  3  18  ? -7.465  -31.498 -71.117  1.00 143.19 ? 18   ARG   C HH12 1 
ATOM   16445 H  HH21 . ARG   C  3  18  ? -4.171  -31.687 -71.153  1.00 139.26 ? 18   ARG   C HH21 1 
ATOM   16446 H  HH22 . ARG   C  3  18  ? -5.311  -30.818 -70.747  1.00 139.26 ? 18   ARG   C HH22 1 
ATOM   16447 N  N    . VAL   C  3  19  ? -3.286  -38.481 -73.101  1.00 78.94  ? 19   VAL   C N    1 
ATOM   16448 C  CA   . VAL   C  3  19  ? -3.560  -39.835 -72.634  1.00 75.11  ? 19   VAL   C CA   1 
ATOM   16449 C  C    . VAL   C  3  19  ? -4.167  -39.745 -71.242  1.00 75.42  ? 19   VAL   C C    1 
ATOM   16450 O  O    . VAL   C  3  19  ? -3.611  -39.083 -70.359  1.00 75.81  ? 19   VAL   C O    1 
ATOM   16451 C  CB   . VAL   C  3  19  ? -2.284  -40.697 -72.620  1.00 70.51  ? 19   VAL   C CB   1 
ATOM   16452 C  CG1  . VAL   C  3  19  ? -2.582  -42.089 -72.079  1.00 70.39  ? 19   VAL   C CG1  1 
ATOM   16453 C  CG2  . VAL   C  3  19  ? -1.690  -40.781 -74.018  1.00 69.70  ? 19   VAL   C CG2  1 
ATOM   16454 H  H    . VAL   C  3  19  ? -2.689  -38.075 -72.633  1.00 94.70  ? 19   VAL   C H    1 
ATOM   16455 H  HA   . VAL   C  3  19  ? -4.206  -40.254 -73.223  1.00 90.11  ? 19   VAL   C HA   1 
ATOM   16456 H  HB   . VAL   C  3  19  ? -1.631  -40.283 -72.035  1.00 84.59  ? 19   VAL   C HB   1 
ATOM   16457 H  HG11 . VAL   C  3  19  ? -1.791  -42.641 -72.175  1.00 84.44  ? 19   VAL   C HG11 1 
ATOM   16458 H  HG12 . VAL   C  3  19  ? -2.824  -42.018 -71.142  1.00 84.44  ? 19   VAL   C HG12 1 
ATOM   16459 H  HG13 . VAL   C  3  19  ? -3.317  -42.473 -72.583  1.00 84.44  ? 19   VAL   C HG13 1 
ATOM   16460 H  HG21 . VAL   C  3  19  ? -0.913  -41.362 -73.996  1.00 83.62  ? 19   VAL   C HG21 1 
ATOM   16461 H  HG22 . VAL   C  3  19  ? -2.356  -41.143 -74.623  1.00 83.62  ? 19   VAL   C HG22 1 
ATOM   16462 H  HG23 . VAL   C  3  19  ? -1.430  -39.892 -74.304  1.00 83.62  ? 19   VAL   C HG23 1 
ATOM   16463 N  N    . ILE   C  3  20  ? -5.304  -40.409 -71.051  1.00 75.44  ? 20   ILE   C N    1 
ATOM   16464 C  CA   . ILE   C  3  20  ? -5.998  -40.444 -69.769  1.00 74.59  ? 20   ILE   C CA   1 
ATOM   16465 C  C    . ILE   C  3  20  ? -6.119  -41.901 -69.345  1.00 80.20  ? 20   ILE   C C    1 
ATOM   16466 O  O    . ILE   C  3  20  ? -6.702  -42.718 -70.069  1.00 85.93  ? 20   ILE   C O    1 
ATOM   16467 C  CB   . ILE   C  3  20  ? -7.380  -39.776 -69.845  1.00 73.24  ? 20   ILE   C CB   1 
ATOM   16468 C  CG1  . ILE   C  3  20  ? -7.234  -38.317 -70.285  1.00 76.38  ? 20   ILE   C CG1  1 
ATOM   16469 C  CG2  . ILE   C  3  20  ? -8.083  -39.858 -68.493  1.00 69.83  ? 20   ILE   C CG2  1 
ATOM   16470 C  CD1  . ILE   C  3  20  ? -8.550  -37.597 -70.491  1.00 87.03  ? 20   ILE   C CD1  1 
ATOM   16471 H  H    . ILE   C  3  20  ? -5.702  -40.858 -71.666  1.00 90.51  ? 20   ILE   C H    1 
ATOM   16472 H  HA   . ILE   C  3  20  ? -5.470  -39.974 -69.105  1.00 89.48  ? 20   ILE   C HA   1 
ATOM   16473 H  HB   . ILE   C  3  20  ? -7.917  -40.247 -70.502  1.00 87.87  ? 20   ILE   C HB   1 
ATOM   16474 H  HG12 . ILE   C  3  20  ? -6.739  -37.835 -69.603  1.00 91.64  ? 20   ILE   C HG12 1 
ATOM   16475 H  HG13 . ILE   C  3  20  ? -6.750  -38.293 -71.125  1.00 91.64  ? 20   ILE   C HG13 1 
ATOM   16476 H  HG21 . ILE   C  3  20  ? -8.954  -39.439 -68.565  1.00 83.77  ? 20   ILE   C HG21 1 
ATOM   16477 H  HG22 . ILE   C  3  20  ? -8.183  -40.791 -68.246  1.00 83.77  ? 20   ILE   C HG22 1 
ATOM   16478 H  HG23 . ILE   C  3  20  ? -7.547  -39.396 -67.830  1.00 83.77  ? 20   ILE   C HG23 1 
ATOM   16479 H  HD11 . ILE   C  3  20  ? -8.374  -36.712 -70.847  1.00 104.42 ? 20   ILE   C HD11 1 
ATOM   16480 H  HD12 . ILE   C  3  20  ? -9.092  -38.103 -71.117  1.00 104.42 ? 20   ILE   C HD12 1 
ATOM   16481 H  HD13 . ILE   C  3  20  ? -9.009  -37.526 -69.640  1.00 104.42 ? 20   ILE   C HD13 1 
ATOM   16482 N  N    . ILE   C  3  21  ? -5.574  -42.220 -68.175  1.00 78.18  ? 21   ILE   C N    1 
ATOM   16483 C  CA   . ILE   C  3  21  ? -5.597  -43.568 -67.619  1.00 77.89  ? 21   ILE   C CA   1 
ATOM   16484 C  C    . ILE   C  3  21  ? -6.546  -43.572 -66.431  1.00 81.39  ? 21   ILE   C C    1 
ATOM   16485 O  O    . ILE   C  3  21  ? -6.480  -42.681 -65.576  1.00 80.91  ? 21   ILE   C O    1 
ATOM   16486 C  CB   . ILE   C  3  21  ? -4.189  -44.026 -67.203  1.00 72.14  ? 21   ILE   C CB   1 
ATOM   16487 C  CG1  . ILE   C  3  21  ? -3.260  -44.042 -68.419  1.00 70.75  ? 21   ILE   C CG1  1 
ATOM   16488 C  CG2  . ILE   C  3  21  ? -4.238  -45.404 -66.560  1.00 71.93  ? 21   ILE   C CG2  1 
ATOM   16489 C  CD1  . ILE   C  3  21  ? -1.798  -43.987 -68.061  1.00 68.01  ? 21   ILE   C CD1  1 
ATOM   16490 H  H    . ILE   C  3  21  ? -5.171  -41.654 -67.669  1.00 93.79  ? 21   ILE   C H    1 
ATOM   16491 H  HA   . ILE   C  3  21  ? -5.934  -44.189 -68.284  1.00 93.45  ? 21   ILE   C HA   1 
ATOM   16492 H  HB   . ILE   C  3  21  ? -3.844  -43.395 -66.552  1.00 86.55  ? 21   ILE   C HB   1 
ATOM   16493 H  HG12 . ILE   C  3  21  ? -3.413  -44.859 -68.918  1.00 84.89  ? 21   ILE   C HG12 1 
ATOM   16494 H  HG13 . ILE   C  3  21  ? -3.459  -43.272 -68.974  1.00 84.89  ? 21   ILE   C HG13 1 
ATOM   16495 H  HG21 . ILE   C  3  21  ? -3.333  -45.702 -66.380  1.00 86.30  ? 21   ILE   C HG21 1 
ATOM   16496 H  HG22 . ILE   C  3  21  ? -4.739  -45.348 -65.731  1.00 86.30  ? 21   ILE   C HG22 1 
ATOM   16497 H  HG23 . ILE   C  3  21  ? -4.674  -46.021 -67.169  1.00 86.30  ? 21   ILE   C HG23 1 
ATOM   16498 H  HD11 . ILE   C  3  21  ? -1.273  -44.004 -68.876  1.00 81.59  ? 21   ILE   C HD11 1 
ATOM   16499 H  HD12 . ILE   C  3  21  ? -1.623  -43.168 -67.571  1.00 81.59  ? 21   ILE   C HD12 1 
ATOM   16500 H  HD13 . ILE   C  3  21  ? -1.579  -44.755 -67.510  1.00 81.59  ? 21   ILE   C HD13 1 
ATOM   16501 N  N    . SER   C  3  22  ? -7.421  -44.569 -66.376  1.00 85.57  ? 22   SER   C N    1 
ATOM   16502 C  CA   . SER   C  3  22  ? -8.429  -44.676 -65.334  1.00 89.54  ? 22   SER   C CA   1 
ATOM   16503 C  C    . SER   C  3  22  ? -7.991  -45.659 -64.253  1.00 90.02  ? 22   SER   C C    1 
ATOM   16504 O  O    . SER   C  3  22  ? -7.160  -46.542 -64.475  1.00 90.63  ? 22   SER   C O    1 
ATOM   16505 C  CB   . SER   C  3  22  ? -9.770  -45.115 -65.928  1.00 96.57  ? 22   SER   C CB   1 
ATOM   16506 O  OG   . SER   C  3  22  ? -10.756 -45.257 -64.920  1.00 100.90 ? 22   SER   C OG   1 
ATOM   16507 H  H    . SER   C  3  22  ? -7.449  -45.211 -66.947  1.00 102.67 ? 22   SER   C H    1 
ATOM   16508 H  HA   . SER   C  3  22  ? -8.547  -43.808 -64.916  1.00 107.43 ? 22   SER   C HA   1 
ATOM   16509 H  HB2  . SER   C  3  22  ? -10.066 -44.445 -66.565  1.00 115.86 ? 22   SER   C HB2  1 
ATOM   16510 H  HB3  . SER   C  3  22  ? -9.652  -45.967 -66.375  1.00 115.86 ? 22   SER   C HB3  1 
ATOM   16511 H  HG   . SER   C  3  22  ? -11.476 -45.527 -65.259  1.00 121.06 ? 22   SER   C HG   1 
ATOM   16512 N  N    . CYS   C  3  23  ? -8.572  -45.488 -63.066  1.00 90.90  ? 23   CYS   C N    1 
ATOM   16513 C  CA   . CYS   C  3  23  ? -8.289  -46.351 -61.926  1.00 89.40  ? 23   CYS   C CA   1 
ATOM   16514 C  C    . CYS   C  3  23  ? -9.474  -46.269 -60.977  1.00 83.43  ? 23   CYS   C C    1 
ATOM   16515 O  O    . CYS   C  3  23  ? -9.936  -45.169 -60.660  1.00 85.33  ? 23   CYS   C O    1 
ATOM   16516 C  CB   . CYS   C  3  23  ? -6.998  -45.924 -61.219  1.00 89.74  ? 23   CYS   C CB   1 
ATOM   16517 S  SG   . CYS   C  3  23  ? -6.559  -46.889 -59.757  1.00 88.72  ? 23   CYS   C SG   1 
ATOM   16518 H  H    . CYS   C  3  23  ? -9.143  -44.868 -62.895  1.00 109.06 ? 23   CYS   C H    1 
ATOM   16519 H  HA   . CYS   C  3  23  ? -8.181  -47.269 -62.218  1.00 107.27 ? 23   CYS   C HA   1 
ATOM   16520 H  HB2  . CYS   C  3  23  ? -6.264  -46.004 -61.849  1.00 107.66 ? 23   CYS   C HB2  1 
ATOM   16521 H  HB3  . CYS   C  3  23  ? -7.094  -45.001 -60.937  1.00 107.66 ? 23   CYS   C HB3  1 
ATOM   16522 N  N    . ARG   C  3  24  ? -9.969  -47.425 -60.536  1.00 75.88  ? 24   ARG   C N    1 
ATOM   16523 C  CA   . ARG   C  3  24  ? -11.120 -47.492 -59.647  1.00 77.09  ? 24   ARG   C CA   1 
ATOM   16524 C  C    . ARG   C  3  24  ? -10.779 -48.328 -58.424  1.00 80.58  ? 24   ARG   C C    1 
ATOM   16525 O  O    . ARG   C  3  24  ? -10.100 -49.354 -58.529  1.00 85.83  ? 24   ARG   C O    1 
ATOM   16526 C  CB   . ARG   C  3  24  ? -12.346 -48.085 -60.362  1.00 81.99  ? 24   ARG   C CB   1 
ATOM   16527 C  CG   . ARG   C  3  24  ? -13.584 -48.194 -59.480  1.00 91.13  ? 24   ARG   C CG   1 
ATOM   16528 C  CD   . ARG   C  3  24  ? -14.770 -48.780 -60.231  1.00 101.20 ? 24   ARG   C CD   1 
ATOM   16529 N  NE   . ARG   C  3  24  ? -15.583 -47.751 -60.877  1.00 111.78 ? 24   ARG   C NE   1 
ATOM   16530 C  CZ   . ARG   C  3  24  ? -16.550 -47.067 -60.271  1.00 120.74 ? 24   ARG   C CZ   1 
ATOM   16531 N  NH1  . ARG   C  3  24  ? -17.235 -46.153 -60.944  1.00 125.04 ? 24   ARG   C NH1  1 
ATOM   16532 N  NH2  . ARG   C  3  24  ? -16.834 -47.289 -58.994  1.00 122.97 ? 24   ARG   C NH2  1 
ATOM   16533 H  H    . ARG   C  3  24  ? -9.647  -48.195 -60.743  1.00 91.04  ? 24   ARG   C H    1 
ATOM   16534 H  HA   . ARG   C  3  24  ? -11.346 -46.598 -59.347  1.00 92.48  ? 24   ARG   C HA   1 
ATOM   16535 H  HB2  . ARG   C  3  24  ? -12.570 -47.519 -61.117  1.00 98.37  ? 24   ARG   C HB2  1 
ATOM   16536 H  HB3  . ARG   C  3  24  ? -12.124 -48.978 -60.671  1.00 98.37  ? 24   ARG   C HB3  1 
ATOM   16537 H  HG2  . ARG   C  3  24  ? -13.388 -48.771 -58.725  1.00 109.34 ? 24   ARG   C HG2  1 
ATOM   16538 H  HG3  . ARG   C  3  24  ? -13.831 -47.310 -59.166  1.00 109.34 ? 24   ARG   C HG3  1 
ATOM   16539 H  HD2  . ARG   C  3  24  ? -14.444 -49.382 -60.919  1.00 121.42 ? 24   ARG   C HD2  1 
ATOM   16540 H  HD3  . ARG   C  3  24  ? -15.334 -49.263 -59.608  1.00 121.42 ? 24   ARG   C HD3  1 
ATOM   16541 H  HE   . ARG   C  3  24  ? -15.425 -47.576 -61.704  1.00 134.11 ? 24   ARG   C HE   1 
ATOM   16542 H  HH11 . ARG   C  3  24  ? -17.054 -46.003 -61.771  1.00 150.02 ? 24   ARG   C HH11 1 
ATOM   16543 H  HH12 . ARG   C  3  24  ? -17.861 -45.711 -60.553  1.00 150.02 ? 24   ARG   C HH12 1 
ATOM   16544 H  HH21 . ARG   C  3  24  ? -16.391 -47.879 -58.551  1.00 147.54 ? 24   ARG   C HH21 1 
ATOM   16545 H  HH22 . ARG   C  3  24  ? -17.460 -46.844 -58.608  1.00 147.54 ? 24   ARG   C HH22 1 
ATOM   16546 N  N    . ALA   C  3  25  ? -11.257 -47.883 -57.265  1.00 80.04  ? 25   ALA   C N    1 
ATOM   16547 C  CA   . ALA   C  3  25  ? -11.055 -48.575 -56.003  1.00 77.65  ? 25   ALA   C CA   1 
ATOM   16548 C  C    . ALA   C  3  25  ? -12.363 -49.196 -55.533  1.00 81.49  ? 25   ALA   C C    1 
ATOM   16549 O  O    . ALA   C  3  25  ? -13.451 -48.697 -55.836  1.00 85.07  ? 25   ALA   C O    1 
ATOM   16550 C  CB   . ALA   C  3  25  ? -10.522 -47.620 -54.931  1.00 73.89  ? 25   ALA   C CB   1 
ATOM   16551 H  H    . ALA   C  3  25  ? -11.716 -47.161 -57.186  1.00 96.02  ? 25   ALA   C H    1 
ATOM   16552 H  HA   . ALA   C  3  25  ? -10.406 -49.286 -56.124  1.00 93.16  ? 25   ALA   C HA   1 
ATOM   16553 H  HB1  . ALA   C  3  25  ? -10.400 -48.111 -54.103  1.00 88.65  ? 25   ALA   C HB1  1 
ATOM   16554 H  HB2  . ALA   C  3  25  ? -9.674  -47.254 -55.226  1.00 88.65  ? 25   ALA   C HB2  1 
ATOM   16555 H  HB3  . ALA   C  3  25  ? -11.163 -46.904 -54.799  1.00 88.65  ? 25   ALA   C HB3  1 
ATOM   16556 N  N    . SER   C  3  26  ? -12.248 -50.294 -54.784  1.00 82.29  ? 26   SER   C N    1 
ATOM   16557 C  CA   . SER   C  3  26  ? -13.426 -50.960 -54.245  1.00 87.47  ? 26   SER   C CA   1 
ATOM   16558 C  C    . SER   C  3  26  ? -14.049 -50.200 -53.081  1.00 91.49  ? 26   SER   C C    1 
ATOM   16559 O  O    . SER   C  3  26  ? -15.158 -50.547 -52.662  1.00 98.42  ? 26   SER   C O    1 
ATOM   16560 C  CB   . SER   C  3  26  ? -13.066 -52.379 -53.798  1.00 87.14  ? 26   SER   C CB   1 
ATOM   16561 O  OG   . SER   C  3  26  ? -12.072 -52.357 -52.788  1.00 85.68  ? 26   SER   C OG   1 
ATOM   16562 H  H    . SER   C  3  26  ? -11.502 -50.668 -54.577  1.00 98.73  ? 26   SER   C H    1 
ATOM   16563 H  HA   . SER   C  3  26  ? -14.092 -51.028 -54.947  1.00 104.94 ? 26   SER   C HA   1 
ATOM   16564 H  HB2  . SER   C  3  26  ? -13.861 -52.810 -53.448  1.00 104.55 ? 26   SER   C HB2  1 
ATOM   16565 H  HB3  . SER   C  3  26  ? -12.728 -52.873 -54.561  1.00 104.55 ? 26   SER   C HB3  1 
ATOM   16566 H  HG   . SER   C  3  26  ? -11.970 -53.127 -52.469  1.00 102.80 ? 26   SER   C HG   1 
ATOM   16567 N  N    . GLN   C  3  27  ? -13.370 -49.184 -52.551  1.00 88.76  ? 27   GLN   C N    1 
ATOM   16568 C  CA   . GLN   C  3  27  ? -13.902 -48.391 -51.453  1.00 93.71  ? 27   GLN   C CA   1 
ATOM   16569 C  C    . GLN   C  3  27  ? -13.385 -46.966 -51.574  1.00 91.89  ? 27   GLN   C C    1 
ATOM   16570 O  O    . GLN   C  3  27  ? -12.412 -46.694 -52.282  1.00 89.04  ? 27   GLN   C O    1 
ATOM   16571 C  CB   . GLN   C  3  27  ? -13.504 -48.959 -50.085  1.00 99.32  ? 27   GLN   C CB   1 
ATOM   16572 C  CG   . GLN   C  3  27  ? -13.871 -50.412 -49.856  1.00 107.20 ? 27   GLN   C CG   1 
ATOM   16573 C  CD   . GLN   C  3  27  ? -13.322 -50.938 -48.544  1.00 109.57 ? 27   GLN   C CD   1 
ATOM   16574 O  OE1  . GLN   C  3  27  ? -12.910 -50.166 -47.678  1.00 106.08 ? 27   GLN   C OE1  1 
ATOM   16575 N  NE2  . GLN   C  3  27  ? -13.306 -52.257 -48.394  1.00 114.91 ? 27   GLN   C NE2  1 
ATOM   16576 H  H    . GLN   C  3  27  ? -12.590 -48.933 -52.815  1.00 106.49 ? 27   GLN   C H    1 
ATOM   16577 H  HA   . GLN   C  3  27  ? -14.869 -48.387 -51.519  1.00 112.43 ? 27   GLN   C HA   1 
ATOM   16578 H  HB2  . GLN   C  3  27  ? -12.541 -48.885 -49.991  1.00 119.16 ? 27   GLN   C HB2  1 
ATOM   16579 H  HB3  . GLN   C  3  27  ? -13.946 -48.437 -49.397  1.00 119.16 ? 27   GLN   C HB3  1 
ATOM   16580 H  HG2  . GLN   C  3  27  ? -14.837 -50.498 -49.837  1.00 128.63 ? 27   GLN   C HG2  1 
ATOM   16581 H  HG3  . GLN   C  3  27  ? -13.505 -50.950 -50.575  1.00 128.63 ? 27   GLN   C HG3  1 
ATOM   16582 H  HE21 . GLN   C  3  27  ? -13.597 -52.765 -49.023  1.00 137.87 ? 27   GLN   C HE21 1 
ATOM   16583 H  HE22 . GLN   C  3  27  ? -13.004 -52.603 -47.667  1.00 137.87 ? 27   GLN   C HE22 1 
ATOM   16584 N  N    . ASP   C  3  28  ? -14.051 -46.056 -50.868  1.00 92.31  ? 28   ASP   C N    1 
ATOM   16585 C  CA   . ASP   C  3  28  ? -13.561 -44.689 -50.759  1.00 87.94  ? 28   ASP   C CA   1 
ATOM   16586 C  C    . ASP   C  3  28  ? -12.171 -44.693 -50.137  1.00 79.24  ? 28   ASP   C C    1 
ATOM   16587 O  O    . ASP   C  3  28  ? -11.994 -45.139 -48.999  1.00 79.56  ? 28   ASP   C O    1 
ATOM   16588 C  CB   . ASP   C  3  28  ? -14.524 -43.856 -49.916  1.00 92.94  ? 28   ASP   C CB   1 
ATOM   16589 C  CG   . ASP   C  3  28  ? -14.140 -42.394 -49.865  1.00 94.34  ? 28   ASP   C CG   1 
ATOM   16590 O  OD1  . ASP   C  3  28  ? -13.152 -42.013 -50.526  1.00 91.55  ? 28   ASP   C OD1  1 
ATOM   16591 O  OD2  . ASP   C  3  28  ? -14.829 -41.626 -49.162  1.00 97.00  ? 28   ASP   C OD2  1 
ATOM   16592 H  H    . ASP   C  3  28  ? -14.784 -46.206 -50.444  1.00 110.75 ? 28   ASP   C H    1 
ATOM   16593 H  HA   . ASP   C  3  28  ? -13.509 -44.287 -51.640  1.00 105.51 ? 28   ASP   C HA   1 
ATOM   16594 H  HB2  . ASP   C  3  28  ? -15.414 -43.919 -50.297  1.00 111.51 ? 28   ASP   C HB2  1 
ATOM   16595 H  HB3  . ASP   C  3  28  ? -14.527 -44.198 -49.008  1.00 111.51 ? 28   ASP   C HB3  1 
ATOM   16596 N  N    . ILE   C  3  29  ? -11.182 -44.205 -50.885  1.00 74.04  ? 29   ILE   C N    1 
ATOM   16597 C  CA   . ILE   C  3  29  ? -9.802  -44.161 -50.420  1.00 72.50  ? 29   ILE   C CA   1 
ATOM   16598 C  C    . ILE   C  3  29  ? -9.366  -42.742 -50.074  1.00 71.42  ? 29   ILE   C C    1 
ATOM   16599 O  O    . ILE   C  3  29  ? -8.174  -42.499 -49.860  1.00 69.92  ? 29   ILE   C O    1 
ATOM   16600 C  CB   . ILE   C  3  29  ? -8.845  -44.798 -51.442  1.00 69.73  ? 29   ILE   C CB   1 
ATOM   16601 C  CG1  . ILE   C  3  29  ? -8.970  -44.117 -52.807  1.00 67.58  ? 29   ILE   C CG1  1 
ATOM   16602 C  CG2  . ILE   C  3  29  ? -9.127  -46.290 -51.559  1.00 72.15  ? 29   ILE   C CG2  1 
ATOM   16603 C  CD1  . ILE   C  3  29  ? -7.995  -44.650 -53.837  1.00 63.90  ? 29   ILE   C CD1  1 
ATOM   16604 H  H    . ILE   C  3  29  ? -11.291 -43.889 -51.678  1.00 88.83  ? 29   ILE   C H    1 
ATOM   16605 H  HA   . ILE   C  3  29  ? -9.747  -44.681 -49.603  1.00 86.98  ? 29   ILE   C HA   1 
ATOM   16606 H  HB   . ILE   C  3  29  ? -7.936  -44.671 -51.128  1.00 83.65  ? 29   ILE   C HB   1 
ATOM   16607 H  HG12 . ILE   C  3  29  ? -9.868  -44.258 -53.146  1.00 81.08  ? 29   ILE   C HG12 1 
ATOM   16608 H  HG13 . ILE   C  3  29  ? -8.800  -43.168 -52.700  1.00 81.08  ? 29   ILE   C HG13 1 
ATOM   16609 H  HG21 . ILE   C  3  29  ? -8.452  -46.696 -52.125  1.00 86.57  ? 29   ILE   C HG21 1 
ATOM   16610 H  HG22 . ILE   C  3  29  ? -9.100  -46.687 -50.675  1.00 86.57  ? 29   ILE   C HG22 1 
ATOM   16611 H  HG23 . ILE   C  3  29  ? -10.006 -46.416 -51.951  1.00 86.57  ? 29   ILE   C HG23 1 
ATOM   16612 H  HD11 . ILE   C  3  29  ? -8.035  -44.089 -54.628  1.00 76.66  ? 29   ILE   C HD11 1 
ATOM   16613 H  HD12 . ILE   C  3  29  ? -7.100  -44.633 -53.464  1.00 76.66  ? 29   ILE   C HD12 1 
ATOM   16614 H  HD13 . ILE   C  3  29  ? -8.242  -45.560 -54.064  1.00 76.66  ? 29   ILE   C HD13 1 
ATOM   16615 N  N    . SER   C  3  30  ? -10.305 -41.799 -50.016  1.00 73.86  ? 30   SER   C N    1 
ATOM   16616 C  CA   . SER   C  3  30  ? -10.046 -40.461 -49.485  1.00 75.88  ? 30   SER   C CA   1 
ATOM   16617 C  C    . SER   C  3  30  ? -8.843  -39.808 -50.162  1.00 73.34  ? 30   SER   C C    1 
ATOM   16618 O  O    . SER   C  3  30  ? -7.978  -39.218 -49.512  1.00 73.46  ? 30   SER   C O    1 
ATOM   16619 C  CB   . SER   C  3  30  ? -9.853  -40.516 -47.968  1.00 77.77  ? 30   SER   C CB   1 
ATOM   16620 O  OG   . SER   C  3  30  ? -10.936 -41.189 -47.347  1.00 80.65  ? 30   SER   C OG   1 
ATOM   16621 H  H    . SER   C  3  30  ? -11.115 -41.910 -50.283  1.00 88.61  ? 30   SER   C H    1 
ATOM   16622 H  HA   . SER   C  3  30  ? -10.815 -39.903 -49.678  1.00 91.04  ? 30   SER   C HA   1 
ATOM   16623 H  HB2  . SER   C  3  30  ? -9.031  -40.992 -47.772  1.00 93.31  ? 30   SER   C HB2  1 
ATOM   16624 H  HB3  . SER   C  3  30  ? -9.804  -39.611 -47.623  1.00 93.31  ? 30   SER   C HB3  1 
ATOM   16625 H  HG   . SER   C  3  30  ? -10.791 -41.266 -46.523  1.00 96.76  ? 30   SER   C HG   1 
ATOM   16626 N  N    . ASN   C  3  31  ? -8.787  -39.920 -51.488  1.00 72.57  ? 31   ASN   C N    1 
ATOM   16627 C  CA   . ASN   C  3  31  ? -7.803  -39.259 -52.341  1.00 69.83  ? 31   ASN   C CA   1 
ATOM   16628 C  C    . ASN   C  3  31  ? -6.378  -39.750 -52.125  1.00 64.47  ? 31   ASN   C C    1 
ATOM   16629 O  O    . ASN   C  3  31  ? -5.447  -39.195 -52.724  1.00 61.17  ? 31   ASN   C O    1 
ATOM   16630 C  CB   . ASN   C  3  31  ? -7.833  -37.736 -52.161  1.00 72.89  ? 31   ASN   C CB   1 
ATOM   16631 C  CG   . ASN   C  3  31  ? -9.004  -37.089 -52.870  1.00 81.03  ? 31   ASN   C CG   1 
ATOM   16632 O  OD1  . ASN   C  3  31  ? -10.085 -36.938 -52.301  1.00 86.38  ? 31   ASN   C OD1  1 
ATOM   16633 N  ND2  . ASN   C  3  31  ? -8.794  -36.704 -54.124  1.00 84.20  ? 31   ASN   C ND2  1 
ATOM   16634 H  H    . ASN   C  3  31  ? -9.341  -40.399 -51.939  1.00 87.07  ? 31   ASN   C H    1 
ATOM   16635 H  HA   . ASN   C  3  31  ? -8.038  -39.471 -53.258  1.00 83.78  ? 31   ASN   C HA   1 
ATOM   16636 H  HB2  . ASN   C  3  31  ? -7.904  -37.530 -51.215  1.00 87.45  ? 31   ASN   C HB2  1 
ATOM   16637 H  HB3  . ASN   C  3  31  ? -7.016  -37.358 -52.522  1.00 87.45  ? 31   ASN   C HB3  1 
ATOM   16638 H  HD21 . ASN   C  3  31  ? -9.427  -36.331 -54.571  1.00 101.02 ? 31   ASN   C HD21 1 
ATOM   16639 H  HD22 . ASN   C  3  31  ? -8.025  -36.828 -54.489  1.00 101.02 ? 31   ASN   C HD22 1 
ATOM   16640 N  N    . TYR   C  3  32  ? -6.168  -40.771 -51.295  1.00 63.74  ? 32   TYR   C N    1 
ATOM   16641 C  CA   . TYR   C  3  32  ? -4.832  -41.339 -51.111  1.00 62.27  ? 32   TYR   C CA   1 
ATOM   16642 C  C    . TYR   C  3  32  ? -4.561  -42.343 -52.233  1.00 60.59  ? 32   TYR   C C    1 
ATOM   16643 O  O    . TYR   C  3  32  ? -4.563  -43.562 -52.049  1.00 58.08  ? 32   TYR   C O    1 
ATOM   16644 C  CB   . TYR   C  3  32  ? -4.702  -41.976 -49.736  1.00 63.70  ? 32   TYR   C CB   1 
ATOM   16645 C  CG   . TYR   C  3  32  ? -4.581  -40.964 -48.621  1.00 69.84  ? 32   TYR   C CG   1 
ATOM   16646 C  CD1  . TYR   C  3  32  ? -3.391  -40.278 -48.409  1.00 71.72  ? 32   TYR   C CD1  1 
ATOM   16647 C  CD2  . TYR   C  3  32  ? -5.653  -40.689 -47.785  1.00 74.42  ? 32   TYR   C CD2  1 
ATOM   16648 C  CE1  . TYR   C  3  32  ? -3.274  -39.348 -47.394  1.00 76.25  ? 32   TYR   C CE1  1 
ATOM   16649 C  CE2  . TYR   C  3  32  ? -5.545  -39.761 -46.766  1.00 79.22  ? 32   TYR   C CE2  1 
ATOM   16650 C  CZ   . TYR   C  3  32  ? -4.353  -39.093 -46.576  1.00 80.73  ? 32   TYR   C CZ   1 
ATOM   16651 O  OH   . TYR   C  3  32  ? -4.237  -38.168 -45.564  1.00 85.38  ? 32   TYR   C OH   1 
ATOM   16652 H  H    . TYR   C  3  32  ? -6.781  -41.151 -50.828  1.00 76.47  ? 32   TYR   C H    1 
ATOM   16653 H  HA   . TYR   C  3  32  ? -4.175  -40.628 -51.171  1.00 74.71  ? 32   TYR   C HA   1 
ATOM   16654 H  HB2  . TYR   C  3  32  ? -5.489  -42.516 -49.564  1.00 76.42  ? 32   TYR   C HB2  1 
ATOM   16655 H  HB3  . TYR   C  3  32  ? -3.908  -42.533 -49.722  1.00 76.42  ? 32   TYR   C HB3  1 
ATOM   16656 H  HD1  . TYR   C  3  32  ? -2.661  -40.448 -48.960  1.00 86.05  ? 32   TYR   C HD1  1 
ATOM   16657 H  HD2  . TYR   C  3  32  ? -6.459  -41.137 -47.912  1.00 89.29  ? 32   TYR   C HD2  1 
ATOM   16658 H  HE1  . TYR   C  3  32  ? -2.471  -38.897 -47.263  1.00 91.48  ? 32   TYR   C HE1  1 
ATOM   16659 H  HE2  . TYR   C  3  32  ? -6.271  -39.587 -46.212  1.00 95.04  ? 32   TYR   C HE2  1 
ATOM   16660 H  HH   . TYR   C  3  32  ? -4.993  -38.006 -45.236  1.00 102.44 ? 32   TYR   C HH   1 
ATOM   16661 N  N    . LEU   C  3  33  ? -4.331  -41.796 -53.426  1.00 61.18  ? 33   LEU   C N    1 
ATOM   16662 C  CA   . LEU   C  3  33  ? -4.009  -42.588 -54.604  1.00 62.24  ? 33   LEU   C CA   1 
ATOM   16663 C  C    . LEU   C  3  33  ? -2.810  -41.974 -55.309  1.00 59.52  ? 33   LEU   C C    1 
ATOM   16664 O  O    . LEU   C  3  33  ? -2.770  -40.760 -55.534  1.00 59.03  ? 33   LEU   C O    1 
ATOM   16665 C  CB   . LEU   C  3  33  ? -5.201  -42.675 -55.565  1.00 66.24  ? 33   LEU   C CB   1 
ATOM   16666 C  CG   . LEU   C  3  33  ? -4.971  -43.642 -56.731  1.00 67.16  ? 33   LEU   C CG   1 
ATOM   16667 C  CD1  . LEU   C  3  33  ? -6.268  -44.324 -57.128  1.00 77.19  ? 33   LEU   C CD1  1 
ATOM   16668 C  CD2  . LEU   C  3  33  ? -4.348  -42.942 -57.936  1.00 61.13  ? 33   LEU   C CD2  1 
ATOM   16669 H  H    . LEU   C  3  33  ? -4.356  -40.950 -53.577  1.00 73.40  ? 33   LEU   C H    1 
ATOM   16670 H  HA   . LEU   C  3  33  ? -3.775  -43.489 -54.330  1.00 74.67  ? 33   LEU   C HA   1 
ATOM   16671 H  HB2  . LEU   C  3  33  ? -5.978  -42.981 -55.072  1.00 79.47  ? 33   LEU   C HB2  1 
ATOM   16672 H  HB3  . LEU   C  3  33  ? -5.369  -41.795 -55.935  1.00 79.47  ? 33   LEU   C HB3  1 
ATOM   16673 H  HG   . LEU   C  3  33  ? -4.345  -44.320 -56.434  1.00 80.57  ? 33   LEU   C HG   1 
ATOM   16674 H  HD11 . LEU   C  3  33  ? -6.069  -45.046 -57.745  1.00 92.61  ? 33   LEU   C HD11 1 
ATOM   16675 H  HD12 . LEU   C  3  33  ? -6.697  -44.677 -56.333  1.00 92.61  ? 33   LEU   C HD12 1 
ATOM   16676 H  HD13 . LEU   C  3  33  ? -6.848  -43.675 -57.556  1.00 92.61  ? 33   LEU   C HD13 1 
ATOM   16677 H  HD21 . LEU   C  3  33  ? -3.448  -43.278 -58.066  1.00 73.34  ? 33   LEU   C HD21 1 
ATOM   16678 H  HD22 . LEU   C  3  33  ? -4.887  -43.127 -58.722  1.00 73.34  ? 33   LEU   C HD22 1 
ATOM   16679 H  HD23 . LEU   C  3  33  ? -4.324  -41.987 -57.769  1.00 73.34  ? 33   LEU   C HD23 1 
ATOM   16680 N  N    . SER   C  3  34  ? -1.844  -42.818 -55.662  1.00 62.47  ? 34   SER   C N    1 
ATOM   16681 C  CA   . SER   C  3  34  ? -0.610  -42.398 -56.305  1.00 62.61  ? 34   SER   C CA   1 
ATOM   16682 C  C    . SER   C  3  34  ? -0.471  -43.092 -57.652  1.00 60.27  ? 34   SER   C C    1 
ATOM   16683 O  O    . SER   C  3  34  ? -1.075  -44.139 -57.898  1.00 62.17  ? 34   SER   C O    1 
ATOM   16684 C  CB   . SER   C  3  34  ? 0.606   -42.720 -55.427  1.00 63.61  ? 34   SER   C CB   1 
ATOM   16685 O  OG   . SER   C  3  34  ? 0.450   -42.181 -54.127  1.00 65.76  ? 34   SER   C OG   1 
ATOM   16686 H  H    . SER   C  3  34  ? -1.885  -43.667 -55.533  1.00 74.95  ? 34   SER   C H    1 
ATOM   16687 H  HA   . SER   C  3  34  ? -0.632  -41.440 -56.456  1.00 75.12  ? 34   SER   C HA   1 
ATOM   16688 H  HB2  . SER   C  3  34  ? 0.699   -43.683 -55.360  1.00 76.31  ? 34   SER   C HB2  1 
ATOM   16689 H  HB3  . SER   C  3  34  ? 1.399   -42.337 -55.834  1.00 76.31  ? 34   SER   C HB3  1 
ATOM   16690 H  HG   . SER   C  3  34  ? 0.314   -42.799 -53.574  1.00 78.89  ? 34   SER   C HG   1 
ATOM   16691 N  N    . TRP   C  3  35  ? 0.340   -42.499 -58.526  1.00 59.51  ? 35   TRP   C N    1 
ATOM   16692 C  CA   . TRP   C  3  35  ? 0.600   -43.038 -59.853  1.00 60.43  ? 35   TRP   C CA   1 
ATOM   16693 C  C    . TRP   C  3  35  ? 2.095   -43.252 -60.046  1.00 57.58  ? 35   TRP   C C    1 
ATOM   16694 O  O    . TRP   C  3  35  ? 2.907   -42.392 -59.692  1.00 55.90  ? 35   TRP   C O    1 
ATOM   16695 C  CB   . TRP   C  3  35  ? 0.063   -42.110 -60.946  1.00 62.47  ? 35   TRP   C CB   1 
ATOM   16696 C  CG   . TRP   C  3  35  ? -1.429  -42.091 -61.021  1.00 67.25  ? 35   TRP   C CG   1 
ATOM   16697 C  CD1  . TRP   C  3  35  ? -2.269  -41.203 -60.417  1.00 70.36  ? 35   TRP   C CD1  1 
ATOM   16698 C  CD2  . TRP   C  3  35  ? -2.262  -43.009 -61.739  1.00 70.97  ? 35   TRP   C CD2  1 
ATOM   16699 N  NE1  . TRP   C  3  35  ? -3.574  -41.508 -60.717  1.00 75.23  ? 35   TRP   C NE1  1 
ATOM   16700 C  CE2  . TRP   C  3  35  ? -3.598  -42.613 -61.527  1.00 73.38  ? 35   TRP   C CE2  1 
ATOM   16701 C  CE3  . TRP   C  3  35  ? -2.009  -44.125 -62.543  1.00 72.25  ? 35   TRP   C CE3  1 
ATOM   16702 C  CZ2  . TRP   C  3  35  ? -4.676  -43.293 -62.089  1.00 73.71  ? 35   TRP   C CZ2  1 
ATOM   16703 C  CZ3  . TRP   C  3  35  ? -3.081  -44.798 -63.101  1.00 75.17  ? 35   TRP   C CZ3  1 
ATOM   16704 C  CH2  . TRP   C  3  35  ? -4.397  -44.380 -62.872  1.00 76.32  ? 35   TRP   C CH2  1 
ATOM   16705 H  H    . TRP   C  3  35  ? 0.759   -41.765 -58.367  1.00 71.39  ? 35   TRP   C H    1 
ATOM   16706 H  HA   . TRP   C  3  35  ? 0.160   -43.898 -59.939  1.00 72.50  ? 35   TRP   C HA   1 
ATOM   16707 H  HB2  . TRP   C  3  35  ? 0.364   -41.206 -60.766  1.00 74.95  ? 35   TRP   C HB2  1 
ATOM   16708 H  HB3  . TRP   C  3  35  ? 0.401   -42.408 -61.805  1.00 74.95  ? 35   TRP   C HB3  1 
ATOM   16709 H  HD1  . TRP   C  3  35  ? -1.997  -40.493 -59.881  1.00 84.41  ? 35   TRP   C HD1  1 
ATOM   16710 H  HE1  . TRP   C  3  35  ? -4.265  -41.076 -60.441  1.00 90.26  ? 35   TRP   C HE1  1 
ATOM   16711 H  HE3  . TRP   C  3  35  ? -1.137  -44.408 -62.700  1.00 86.68  ? 35   TRP   C HE3  1 
ATOM   16712 H  HZ2  . TRP   C  3  35  ? -5.552  -43.018 -61.938  1.00 88.43  ? 35   TRP   C HZ2  1 
ATOM   16713 H  HZ3  . TRP   C  3  35  ? -2.925  -45.542 -63.636  1.00 90.18  ? 35   TRP   C HZ3  1 
ATOM   16714 H  HH2  . TRP   C  3  35  ? -5.098  -44.851 -63.260  1.00 91.56  ? 35   TRP   C HH2  1 
ATOM   16715 N  N    . TYR   C  3  36  ? 2.448   -44.403 -60.616  1.00 58.04  ? 36   TYR   C N    1 
ATOM   16716 C  CA   . TYR   C  3  36  ? 3.832   -44.791 -60.842  1.00 57.14  ? 36   TYR   C CA   1 
ATOM   16717 C  C    . TYR   C  3  36  ? 4.052   -45.119 -62.311  1.00 62.21  ? 36   TYR   C C    1 
ATOM   16718 O  O    . TYR   C  3  36  ? 3.172   -45.682 -62.969  1.00 66.74  ? 36   TYR   C O    1 
ATOM   16719 C  CB   . TYR   C  3  36  ? 4.210   -46.003 -59.987  1.00 56.83  ? 36   TYR   C CB   1 
ATOM   16720 C  CG   . TYR   C  3  36  ? 4.128   -45.741 -58.504  1.00 59.26  ? 36   TYR   C CG   1 
ATOM   16721 C  CD1  . TYR   C  3  36  ? 3.043   -46.181 -57.760  1.00 59.42  ? 36   TYR   C CD1  1 
ATOM   16722 C  CD2  . TYR   C  3  36  ? 5.134   -45.045 -57.850  1.00 63.37  ? 36   TYR   C CD2  1 
ATOM   16723 C  CE1  . TYR   C  3  36  ? 2.965   -45.940 -56.405  1.00 60.34  ? 36   TYR   C CE1  1 
ATOM   16724 C  CE2  . TYR   C  3  36  ? 5.066   -44.800 -56.497  1.00 65.49  ? 36   TYR   C CE2  1 
ATOM   16725 C  CZ   . TYR   C  3  36  ? 3.978   -45.247 -55.778  1.00 62.92  ? 36   TYR   C CZ   1 
ATOM   16726 O  OH   . TYR   C  3  36  ? 3.906   -45.002 -54.427  1.00 63.11  ? 36   TYR   C OH   1 
ATOM   16727 H  H    . TYR   C  3  36  ? 1.883   -44.992 -60.888  1.00 69.63  ? 36   TYR   C H    1 
ATOM   16728 H  HA   . TYR   C  3  36  ? 4.413   -44.050 -60.607  1.00 68.55  ? 36   TYR   C HA   1 
ATOM   16729 H  HB2  . TYR   C  3  36  ? 3.605   -46.732 -60.193  1.00 68.18  ? 36   TYR   C HB2  1 
ATOM   16730 H  HB3  . TYR   C  3  36  ? 5.122   -46.259 -60.193  1.00 68.18  ? 36   TYR   C HB3  1 
ATOM   16731 H  HD1  . TYR   C  3  36  ? 2.357   -46.645 -58.183  1.00 71.28  ? 36   TYR   C HD1  1 
ATOM   16732 H  HD2  . TYR   C  3  36  ? 5.867   -44.739 -58.333  1.00 76.03  ? 36   TYR   C HD2  1 
ATOM   16733 H  HE1  . TYR   C  3  36  ? 2.234   -46.244 -55.917  1.00 72.38  ? 36   TYR   C HE1  1 
ATOM   16734 H  HE2  . TYR   C  3  36  ? 5.749   -44.335 -56.070  1.00 78.57  ? 36   TYR   C HE2  1 
ATOM   16735 H  HH   . TYR   C  3  36  ? 3.239   -45.394 -54.100  1.00 75.72  ? 36   TYR   C HH   1 
ATOM   16736 N  N    . GLN   C  3  37  ? 5.229   -44.767 -62.817  1.00 63.31  ? 37   GLN   C N    1 
ATOM   16737 C  CA   . GLN   C  3  37  ? 5.645   -45.101 -64.172  1.00 65.13  ? 37   GLN   C CA   1 
ATOM   16738 C  C    . GLN   C  3  37  ? 6.739   -46.156 -64.109  1.00 66.16  ? 37   GLN   C C    1 
ATOM   16739 O  O    . GLN   C  3  37  ? 7.743   -45.973 -63.412  1.00 68.02  ? 37   GLN   C O    1 
ATOM   16740 C  CB   . GLN   C  3  37  ? 6.148   -43.862 -64.918  1.00 65.36  ? 37   GLN   C CB   1 
ATOM   16741 C  CG   . GLN   C  3  37  ? 7.327   -44.127 -65.852  1.00 68.44  ? 37   GLN   C CG   1 
ATOM   16742 C  CD   . GLN   C  3  37  ? 7.730   -42.905 -66.655  1.00 71.27  ? 37   GLN   C CD   1 
ATOM   16743 O  OE1  . GLN   C  3  37  ? 8.837   -42.387 -66.504  1.00 74.16  ? 37   GLN   C OE1  1 
ATOM   16744 N  NE2  . GLN   C  3  37  ? 6.834   -42.441 -67.519  1.00 71.61  ? 37   GLN   C NE2  1 
ATOM   16745 H  H    . GLN   C  3  37  ? 5.821   -44.320 -62.381  1.00 75.95  ? 37   GLN   C H    1 
ATOM   16746 H  HA   . GLN   C  3  37  ? 4.891   -45.463 -64.664  1.00 78.14  ? 37   GLN   C HA   1 
ATOM   16747 H  HB2  . GLN   C  3  37  ? 5.422   -43.507 -65.454  1.00 78.41  ? 37   GLN   C HB2  1 
ATOM   16748 H  HB3  . GLN   C  3  37  ? 6.433   -43.202 -64.266  1.00 78.41  ? 37   GLN   C HB3  1 
ATOM   16749 H  HG2  . GLN   C  3  37  ? 8.092   -44.405 -65.324  1.00 82.11  ? 37   GLN   C HG2  1 
ATOM   16750 H  HG3  . GLN   C  3  37  ? 7.083   -44.828 -66.476  1.00 82.11  ? 37   GLN   C HG3  1 
ATOM   16751 H  HE21 . GLN   C  3  37  ? 6.073   -42.832 -67.600  1.00 85.92  ? 37   GLN   C HE21 1 
ATOM   16752 H  HE22 . GLN   C  3  37  ? 7.016   -41.750 -67.997  1.00 85.92  ? 37   GLN   C HE22 1 
ATOM   16753 N  N    . GLN   C  3  38  ? 6.547   -47.253 -64.838  1.00 63.04  ? 38   GLN   C N    1 
ATOM   16754 C  CA   . GLN   C  3  38  ? 7.552   -48.301 -64.955  1.00 62.91  ? 38   GLN   C CA   1 
ATOM   16755 C  C    . GLN   C  3  38  ? 7.980   -48.410 -66.410  1.00 62.40  ? 38   GLN   C C    1 
ATOM   16756 O  O    . GLN   C  3  38  ? 7.154   -48.703 -67.281  1.00 61.55  ? 38   GLN   C O    1 
ATOM   16757 C  CB   . GLN   C  3  38  ? 7.026   -49.647 -64.458  1.00 62.71  ? 38   GLN   C CB   1 
ATOM   16758 C  CG   . GLN   C  3  38  ? 8.034   -50.776 -64.630  1.00 63.85  ? 38   GLN   C CG   1 
ATOM   16759 C  CD   . GLN   C  3  38  ? 7.728   -51.973 -63.758  1.00 64.05  ? 38   GLN   C CD   1 
ATOM   16760 O  OE1  . GLN   C  3  38  ? 6.616   -52.500 -63.773  1.00 66.99  ? 38   GLN   C OE1  1 
ATOM   16761 N  NE2  . GLN   C  3  38  ? 8.715   -52.407 -62.983  1.00 63.75  ? 38   GLN   C NE2  1 
ATOM   16762 H  H    . GLN   C  3  38  ? 5.827   -47.413 -65.281  1.00 75.63  ? 38   GLN   C H    1 
ATOM   16763 H  HA   . GLN   C  3  38  ? 8.322   -48.058 -64.418  1.00 75.47  ? 38   GLN   C HA   1 
ATOM   16764 H  HB2  . GLN   C  3  38  ? 6.816   -49.574 -63.513  1.00 75.24  ? 38   GLN   C HB2  1 
ATOM   16765 H  HB3  . GLN   C  3  38  ? 6.228   -49.878 -64.958  1.00 75.24  ? 38   GLN   C HB3  1 
ATOM   16766 H  HG2  . GLN   C  3  38  ? 8.025   -51.069 -65.555  1.00 76.60  ? 38   GLN   C HG2  1 
ATOM   16767 H  HG3  . GLN   C  3  38  ? 8.916   -50.450 -64.394  1.00 76.60  ? 38   GLN   C HG3  1 
ATOM   16768 H  HE21 . GLN   C  3  38  ? 9.478   -52.009 -62.996  1.00 76.49  ? 38   GLN   C HE21 1 
ATOM   16769 H  HE22 . GLN   C  3  38  ? 8.592   -53.084 -62.468  1.00 76.49  ? 38   GLN   C HE22 1 
ATOM   16770 N  N    . LYS   C  3  39  ? 9.260   -48.184 -66.665  1.00 64.64  ? 39   LYS   C N    1 
ATOM   16771 C  CA   . LYS   C  3  39  ? 9.801   -48.299 -68.009  1.00 71.22  ? 39   LYS   C CA   1 
ATOM   16772 C  C    . LYS   C  3  39  ? 10.215  -49.735 -68.292  1.00 73.16  ? 39   LYS   C C    1 
ATOM   16773 O  O    . LYS   C  3  39  ? 10.412  -50.533 -67.371  1.00 73.21  ? 39   LYS   C O    1 
ATOM   16774 C  CB   . LYS   C  3  39  ? 10.987  -47.352 -68.174  1.00 75.06  ? 39   LYS   C CB   1 
ATOM   16775 C  CG   . LYS   C  3  39  ? 10.571  -45.899 -68.349  1.00 76.87  ? 39   LYS   C CG   1 
ATOM   16776 C  CD   . LYS   C  3  39  ? 11.745  -44.953 -68.176  1.00 80.50  ? 39   LYS   C CD   1 
ATOM   16777 C  CE   . LYS   C  3  39  ? 11.376  -43.533 -68.578  1.00 81.06  ? 39   LYS   C CE   1 
ATOM   16778 N  NZ   . LYS   C  3  39  ? 11.049  -43.435 -70.027  1.00 82.18  ? 39   LYS   C NZ   1 
ATOM   16779 H  H    . LYS   C  3  39  ? 9.840   -47.960 -66.072  1.00 77.55  ? 39   LYS   C H    1 
ATOM   16780 H  HA   . LYS   C  3  39  ? 9.129   -48.048 -68.662  1.00 85.44  ? 39   LYS   C HA   1 
ATOM   16781 H  HB2  . LYS   C  3  39  ? 11.548  -47.410 -67.385  1.00 90.05  ? 39   LYS   C HB2  1 
ATOM   16782 H  HB3  . LYS   C  3  39  ? 11.492  -47.615 -68.960  1.00 90.05  ? 39   LYS   C HB3  1 
ATOM   16783 H  HG2  . LYS   C  3  39  ? 10.209  -45.774 -69.241  1.00 92.22  ? 39   LYS   C HG2  1 
ATOM   16784 H  HG3  . LYS   C  3  39  ? 9.900   -45.675 -67.685  1.00 92.22  ? 39   LYS   C HG3  1 
ATOM   16785 H  HD2  . LYS   C  3  39  ? 12.018  -44.946 -67.246  1.00 96.59  ? 39   LYS   C HD2  1 
ATOM   16786 H  HD3  . LYS   C  3  39  ? 12.481  -45.247 -68.736  1.00 96.59  ? 39   LYS   C HD3  1 
ATOM   16787 H  HE2  . LYS   C  3  39  ? 10.599  -43.249 -68.071  1.00 97.26  ? 39   LYS   C HE2  1 
ATOM   16788 H  HE3  . LYS   C  3  39  ? 12.125  -42.944 -68.395  1.00 97.26  ? 39   LYS   C HE3  1 
ATOM   16789 H  HZ1  . LYS   C  3  39  ? 11.659  -42.938 -70.444  1.00 98.60  ? 39   LYS   C HZ1  1 
ATOM   16790 H  HZ2  . LYS   C  3  39  ? 11.038  -44.246 -70.393  1.00 98.60  ? 39   LYS   C HZ2  1 
ATOM   16791 H  HZ3  . LYS   C  3  39  ? 10.249  -43.059 -70.134  1.00 98.60  ? 39   LYS   C HZ3  1 
ATOM   16792 N  N    . PRO   C  3  40  ? 10.352  -50.100 -69.568  1.00 76.82  ? 40   PRO   C N    1 
ATOM   16793 C  CA   . PRO   C  3  40  ? 10.596  -51.509 -69.907  1.00 82.10  ? 40   PRO   C CA   1 
ATOM   16794 C  C    . PRO   C  3  40  ? 11.789  -52.132 -69.194  1.00 85.05  ? 40   PRO   C C    1 
ATOM   16795 O  O    . PRO   C  3  40  ? 11.828  -53.357 -69.056  1.00 88.54  ? 40   PRO   C O    1 
ATOM   16796 C  CB   . PRO   C  3  40  ? 10.817  -51.473 -71.426  1.00 85.01  ? 40   PRO   C CB   1 
ATOM   16797 C  CG   . PRO   C  3  40  ? 10.100  -50.252 -71.883  1.00 82.89  ? 40   PRO   C CG   1 
ATOM   16798 C  CD   . PRO   C  3  40  ? 10.234  -49.253 -70.771  1.00 78.91  ? 40   PRO   C CD   1 
ATOM   16799 H  HA   . PRO   C  3  40  ? 9.804   -52.026 -69.691  1.00 98.50  ? 40   PRO   C HA   1 
ATOM   16800 H  HB2  . PRO   C  3  40  ? 11.766  -51.413 -71.621  1.00 101.99 ? 40   PRO   C HB2  1 
ATOM   16801 H  HB3  . PRO   C  3  40  ? 10.444  -52.270 -71.834  1.00 101.99 ? 40   PRO   C HB3  1 
ATOM   16802 H  HG2  . PRO   C  3  40  ? 10.509  -49.918 -72.696  1.00 99.45  ? 40   PRO   C HG2  1 
ATOM   16803 H  HG3  . PRO   C  3  40  ? 9.167   -50.463 -72.044  1.00 99.45  ? 40   PRO   C HG3  1 
ATOM   16804 H  HD2  . PRO   C  3  40  ? 11.029  -48.710 -70.889  1.00 94.67  ? 40   PRO   C HD2  1 
ATOM   16805 H  HD3  . PRO   C  3  40  ? 9.449   -48.687 -70.718  1.00 94.67  ? 40   PRO   C HD3  1 
ATOM   16806 N  N    . ASP   C  3  41  ? 12.752  -51.332 -68.733  1.00 84.48  ? 41   ASP   C N    1 
ATOM   16807 C  CA   . ASP   C  3  41  ? 13.933  -51.881 -68.074  1.00 84.56  ? 41   ASP   C CA   1 
ATOM   16808 C  C    . ASP   C  3  41  ? 13.707  -52.188 -66.599  1.00 83.34  ? 41   ASP   C C    1 
ATOM   16809 O  O    . ASP   C  3  41  ? 14.656  -52.589 -65.916  1.00 83.33  ? 41   ASP   C O    1 
ATOM   16810 C  CB   . ASP   C  3  41  ? 15.110  -50.913 -68.222  1.00 83.47  ? 41   ASP   C CB   1 
ATOM   16811 C  CG   . ASP   C  3  41  ? 14.874  -49.595 -67.514  1.00 79.80  ? 41   ASP   C CG   1 
ATOM   16812 O  OD1  . ASP   C  3  41  ? 13.752  -49.379 -67.009  1.00 76.90  ? 41   ASP   C OD1  1 
ATOM   16813 O  OD2  . ASP   C  3  41  ? 15.813  -48.775 -67.459  1.00 80.19  ? 41   ASP   C OD2  1 
ATOM   16814 H  H    . ASP   C  3  41  ? 12.742  -50.474 -68.789  1.00 101.36 ? 41   ASP   C H    1 
ATOM   16815 H  HA   . ASP   C  3  41  ? 14.170  -52.712 -68.514  1.00 101.45 ? 41   ASP   C HA   1 
ATOM   16816 H  HB2  . ASP   C  3  41  ? 15.905  -51.320 -67.842  1.00 100.14 ? 41   ASP   C HB2  1 
ATOM   16817 H  HB3  . ASP   C  3  41  ? 15.251  -50.727 -69.164  1.00 100.14 ? 41   ASP   C HB3  1 
ATOM   16818 N  N    . GLY   C  3  42  ? 12.486  -52.013 -66.092  1.00 80.82  ? 42   GLY   C N    1 
ATOM   16819 C  CA   . GLY   C  3  42  ? 12.173  -52.242 -64.700  1.00 78.88  ? 42   GLY   C CA   1 
ATOM   16820 C  C    . GLY   C  3  42  ? 12.191  -50.995 -63.841  1.00 73.06  ? 42   GLY   C C    1 
ATOM   16821 O  O    . GLY   C  3  42  ? 11.663  -51.022 -62.723  1.00 72.58  ? 42   GLY   C O    1 
ATOM   16822 H  H    . GLY   C  3  42  ? 11.809  -51.755 -66.555  1.00 96.96  ? 42   GLY   C H    1 
ATOM   16823 H  HA2  . GLY   C  3  42  ? 11.288  -52.633 -64.640  1.00 94.63  ? 42   GLY   C HA2  1 
ATOM   16824 H  HA3  . GLY   C  3  42  ? 12.820  -52.865 -64.333  1.00 94.63  ? 42   GLY   C HA3  1 
ATOM   16825 N  N    . THR   C  3  43  ? 12.784  -49.910 -64.332  1.00 70.02  ? 43   THR   C N    1 
ATOM   16826 C  CA   . THR   C  3  43  ? 12.834  -48.666 -63.575  1.00 70.78  ? 43   THR   C CA   1 
ATOM   16827 C  C    . THR   C  3  43  ? 11.431  -48.212 -63.195  1.00 68.64  ? 43   THR   C C    1 
ATOM   16828 O  O    . THR   C  3  43  ? 10.508  -48.244 -64.012  1.00 71.84  ? 43   THR   C O    1 
ATOM   16829 C  CB   . THR   C  3  43  ? 13.535  -47.582 -64.400  1.00 74.34  ? 43   THR   C CB   1 
ATOM   16830 O  OG1  . THR   C  3  43  ? 14.952  -47.797 -64.375  1.00 77.64  ? 43   THR   C OG1  1 
ATOM   16831 C  CG2  . THR   C  3  43  ? 13.223  -46.192 -63.863  1.00 77.35  ? 43   THR   C CG2  1 
ATOM   16832 H  H    . THR   C  3  43  ? 13.165  -49.868 -65.102  1.00 84.00  ? 43   THR   C H    1 
ATOM   16833 H  HA   . THR   C  3  43  ? 13.338  -48.804 -62.758  1.00 84.92  ? 43   THR   C HA   1 
ATOM   16834 H  HB   . THR   C  3  43  ? 13.216  -47.625 -65.314  1.00 89.18  ? 43   THR   C HB   1 
ATOM   16835 H  HG1  . THR   C  3  43  ? 15.342  -47.196 -64.814  1.00 93.14  ? 43   THR   C HG1  1 
ATOM   16836 H  HG21 . THR   C  3  43  ? 13.830  -45.542 -64.251  1.00 92.80  ? 43   THR   C HG21 1 
ATOM   16837 H  HG22 . THR   C  3  43  ? 12.312  -45.946 -64.090  1.00 92.80  ? 43   THR   C HG22 1 
ATOM   16838 H  HG23 . THR   C  3  43  ? 13.321  -46.178 -62.898  1.00 92.80  ? 43   THR   C HG23 1 
ATOM   16839 N  N    . VAL   C  3  44  ? 11.276  -47.781 -61.945  1.00 64.85  ? 44   VAL   C N    1 
ATOM   16840 C  CA   . VAL   C  3  44  ? 10.005  -47.300 -61.418  1.00 64.64  ? 44   VAL   C CA   1 
ATOM   16841 C  C    . VAL   C  3  44  ? 10.209  -45.885 -60.896  1.00 64.54  ? 44   VAL   C C    1 
ATOM   16842 O  O    . VAL   C  3  44  ? 11.189  -45.612 -60.193  1.00 62.43  ? 44   VAL   C O    1 
ATOM   16843 C  CB   . VAL   C  3  44  ? 9.466   -48.218 -60.304  1.00 65.19  ? 44   VAL   C CB   1 
ATOM   16844 C  CG1  . VAL   C  3  44  ? 8.138   -47.694 -59.771  1.00 61.98  ? 44   VAL   C CG1  1 
ATOM   16845 C  CG2  . VAL   C  3  44  ? 9.313   -49.644 -60.814  1.00 66.04  ? 44   VAL   C CG2  1 
ATOM   16846 H  H    . VAL   C  3  44  ? 11.914  -47.757 -61.368  1.00 77.80  ? 44   VAL   C H    1 
ATOM   16847 H  HA   . VAL   C  3  44  ? 9.351   -47.273 -62.134  1.00 77.54  ? 44   VAL   C HA   1 
ATOM   16848 H  HB   . VAL   C  3  44  ? 10.103  -48.225 -59.572  1.00 78.20  ? 44   VAL   C HB   1 
ATOM   16849 H  HG11 . VAL   C  3  44  ? 7.783   -48.329 -59.129  1.00 74.36  ? 44   VAL   C HG11 1 
ATOM   16850 H  HG12 . VAL   C  3  44  ? 8.286   -46.837 -59.342  1.00 74.36  ? 44   VAL   C HG12 1 
ATOM   16851 H  HG13 . VAL   C  3  44  ? 7.520   -47.591 -60.511  1.00 74.36  ? 44   VAL   C HG13 1 
ATOM   16852 H  HG21 . VAL   C  3  44  ? 8.945   -50.194 -60.106  1.00 79.23  ? 44   VAL   C HG21 1 
ATOM   16853 H  HG22 . VAL   C  3  44  ? 8.715   -49.643 -61.578  1.00 79.23  ? 44   VAL   C HG22 1 
ATOM   16854 H  HG23 . VAL   C  3  44  ? 10.184  -49.980 -61.076  1.00 79.23  ? 44   VAL   C HG23 1 
ATOM   16855 N  N    . LYS   C  3  45  ? 9.283   -44.991 -61.239  1.00 64.57  ? 45   LYS   C N    1 
ATOM   16856 C  CA   . LYS   C  3  45  ? 9.306   -43.610 -60.778  1.00 68.75  ? 45   LYS   C CA   1 
ATOM   16857 C  C    . LYS   C  3  45  ? 7.940   -43.235 -60.226  1.00 62.80  ? 45   LYS   C C    1 
ATOM   16858 O  O    . LYS   C  3  45  ? 6.910   -43.672 -60.748  1.00 60.99  ? 45   LYS   C O    1 
ATOM   16859 C  CB   . LYS   C  3  45  ? 9.669   -42.639 -61.908  1.00 79.95  ? 45   LYS   C CB   1 
ATOM   16860 C  CG   . LYS   C  3  45  ? 11.065  -42.804 -62.472  1.00 92.73  ? 45   LYS   C CG   1 
ATOM   16861 C  CD   . LYS   C  3  45  ? 11.306  -41.805 -63.593  1.00 104.93 ? 45   LYS   C CD   1 
ATOM   16862 C  CE   . LYS   C  3  45  ? 12.704  -41.929 -64.170  1.00 113.82 ? 45   LYS   C CE   1 
ATOM   16863 N  NZ   . LYS   C  3  45  ? 12.931  -40.950 -65.268  1.00 119.09 ? 45   LYS   C NZ   1 
ATOM   16864 H  H    . LYS   C  3  45  ? 8.616   -45.168 -61.752  1.00 77.46  ? 45   LYS   C H    1 
ATOM   16865 H  HA   . LYS   C  3  45  ? 9.967   -43.527 -60.074  1.00 82.48  ? 45   LYS   C HA   1 
ATOM   16866 H  HB2  . LYS   C  3  45  ? 9.043   -42.769 -62.638  1.00 95.92  ? 45   LYS   C HB2  1 
ATOM   16867 H  HB3  . LYS   C  3  45  ? 9.598   -41.733 -61.568  1.00 95.92  ? 45   LYS   C HB3  1 
ATOM   16868 H  HG2  . LYS   C  3  45  ? 11.719  -42.649 -61.773  1.00 111.25 ? 45   LYS   C HG2  1 
ATOM   16869 H  HG3  . LYS   C  3  45  ? 11.167  -43.700 -62.829  1.00 111.25 ? 45   LYS   C HG3  1 
ATOM   16870 H  HD2  . LYS   C  3  45  ? 10.668  -41.965 -64.307  1.00 125.90 ? 45   LYS   C HD2  1 
ATOM   16871 H  HD3  . LYS   C  3  45  ? 11.199  -40.905 -63.248  1.00 125.90 ? 45   LYS   C HD3  1 
ATOM   16872 H  HE2  . LYS   C  3  45  ? 13.355  -41.760 -63.471  1.00 136.57 ? 45   LYS   C HE2  1 
ATOM   16873 H  HE3  . LYS   C  3  45  ? 12.826  -42.823 -64.528  1.00 136.57 ? 45   LYS   C HE3  1 
ATOM   16874 H  HZ1  . LYS   C  3  45  ? 13.760  -41.033 -65.583  1.00 142.89 ? 45   LYS   C HZ1  1 
ATOM   16875 H  HZ2  . LYS   C  3  45  ? 12.355  -41.096 -65.930  1.00 142.89 ? 45   LYS   C HZ2  1 
ATOM   16876 H  HZ3  . LYS   C  3  45  ? 12.819  -40.121 -64.965  1.00 142.89 ? 45   LYS   C HZ3  1 
ATOM   16877 N  N    . LEU   C  3  46  ? 7.934   -42.419 -59.174  1.00 59.98  ? 46   LEU   C N    1 
ATOM   16878 C  CA   . LEU   C  3  46  ? 6.694   -41.840 -58.676  1.00 57.27  ? 46   LEU   C CA   1 
ATOM   16879 C  C    . LEU   C  3  46  ? 6.365   -40.585 -59.474  1.00 57.16  ? 46   LEU   C C    1 
ATOM   16880 O  O    . LEU   C  3  46  ? 7.220   -39.712 -59.657  1.00 54.53  ? 46   LEU   C O    1 
ATOM   16881 C  CB   . LEU   C  3  46  ? 6.804   -41.506 -57.189  1.00 57.22  ? 46   LEU   C CB   1 
ATOM   16882 C  CG   . LEU   C  3  46  ? 5.627   -40.703 -56.620  1.00 55.52  ? 46   LEU   C CG   1 
ATOM   16883 C  CD1  . LEU   C  3  46  ? 4.330   -41.495 -56.696  1.00 53.19  ? 46   LEU   C CD1  1 
ATOM   16884 C  CD2  . LEU   C  3  46  ? 5.896   -40.268 -55.189  1.00 55.38  ? 46   LEU   C CD2  1 
ATOM   16885 H  H    . LEU   C  3  46  ? 8.635   -42.188 -58.733  1.00 71.96  ? 46   LEU   C H    1 
ATOM   16886 H  HA   . LEU   C  3  46  ? 5.975   -42.482 -58.783  1.00 68.70  ? 46   LEU   C HA   1 
ATOM   16887 H  HB2  . LEU   C  3  46  ? 6.859   -42.336 -56.690  1.00 68.64  ? 46   LEU   C HB2  1 
ATOM   16888 H  HB3  . LEU   C  3  46  ? 7.609   -40.982 -57.050  1.00 68.64  ? 46   LEU   C HB3  1 
ATOM   16889 H  HG   . LEU   C  3  46  ? 5.524   -39.904 -57.161  1.00 66.60  ? 46   LEU   C HG   1 
ATOM   16890 H  HD11 . LEU   C  3  46  ? 3.592   -40.917 -56.445  1.00 63.80  ? 46   LEU   C HD11 1 
ATOM   16891 H  HD12 . LEU   C  3  46  ? 4.207   -41.813 -57.604  1.00 63.80  ? 46   LEU   C HD12 1 
ATOM   16892 H  HD13 . LEU   C  3  46  ? 4.384   -42.247 -56.087  1.00 63.80  ? 46   LEU   C HD13 1 
ATOM   16893 H  HD21 . LEU   C  3  46  ? 5.163   -39.709 -54.887  1.00 66.44  ? 46   LEU   C HD21 1 
ATOM   16894 H  HD22 . LEU   C  3  46  ? 5.964   -41.056 -54.628  1.00 66.44  ? 46   LEU   C HD22 1 
ATOM   16895 H  HD23 . LEU   C  3  46  ? 6.727   -39.769 -55.162  1.00 66.44  ? 46   LEU   C HD23 1 
ATOM   16896 N  N    . LEU   C  3  47  ? 5.123   -40.497 -59.949  1.00 58.60  ? 47   LEU   C N    1 
ATOM   16897 C  CA   . LEU   C  3  47  ? 4.644   -39.332 -60.680  1.00 58.32  ? 47   LEU   C CA   1 
ATOM   16898 C  C    . LEU   C  3  47  ? 3.701   -38.486 -59.835  1.00 58.49  ? 47   LEU   C C    1 
ATOM   16899 O  O    . LEU   C  3  47  ? 3.944   -37.293 -59.630  1.00 56.08  ? 47   LEU   C O    1 
ATOM   16900 C  CB   . LEU   C  3  47  ? 3.928   -39.771 -61.964  1.00 61.83  ? 47   LEU   C CB   1 
ATOM   16901 C  CG   . LEU   C  3  47  ? 4.628   -40.773 -62.880  1.00 67.73  ? 47   LEU   C CG   1 
ATOM   16902 C  CD1  . LEU   C  3  47  ? 3.633   -41.298 -63.903  1.00 70.33  ? 47   LEU   C CD1  1 
ATOM   16903 C  CD2  . LEU   C  3  47  ? 5.822   -40.140 -63.568  1.00 68.35  ? 47   LEU   C CD2  1 
ATOM   16904 H  H    . LEU   C  3  47  ? 4.530   -41.113 -59.858  1.00 70.30  ? 47   LEU   C H    1 
ATOM   16905 H  HA   . LEU   C  3  47  ? 5.409   -38.788 -60.925  1.00 69.97  ? 47   LEU   C HA   1 
ATOM   16906 H  HB2  . LEU   C  3  47  ? 3.084   -40.174 -61.706  1.00 74.17  ? 47   LEU   C HB2  1 
ATOM   16907 H  HB3  . LEU   C  3  47  ? 3.766   -38.976 -62.496  1.00 74.17  ? 47   LEU   C HB3  1 
ATOM   16908 H  HG   . LEU   C  3  47  ? 4.962   -41.516 -62.353  1.00 81.26  ? 47   LEU   C HG   1 
ATOM   16909 H  HD11 . LEU   C  3  47  ? 4.086   -41.918 -64.496  1.00 84.38  ? 47   LEU   C HD11 1 
ATOM   16910 H  HD12 . LEU   C  3  47  ? 2.912   -41.752 -63.438  1.00 84.38  ? 47   LEU   C HD12 1 
ATOM   16911 H  HD13 . LEU   C  3  47  ? 3.279   -40.552 -64.412  1.00 84.38  ? 47   LEU   C HD13 1 
ATOM   16912 H  HD21 . LEU   C  3  47  ? 6.233   -40.796 -64.153  1.00 82.00  ? 47   LEU   C HD21 1 
ATOM   16913 H  HD22 . LEU   C  3  47  ? 5.521   -39.378 -64.086  1.00 82.00  ? 47   LEU   C HD22 1 
ATOM   16914 H  HD23 . LEU   C  3  47  ? 6.459   -39.852 -62.896  1.00 82.00  ? 47   LEU   C HD23 1 
ATOM   16915 N  N    . ILE   C  3  48  ? 2.628   -39.089 -59.326  1.00 59.47  ? 48   ILE   C N    1 
ATOM   16916 C  CA   . ILE   C  3  48  ? 1.555   -38.374 -58.651  1.00 61.16  ? 48   ILE   C CA   1 
ATOM   16917 C  C    . ILE   C  3  48  ? 1.304   -39.031 -57.303  1.00 61.48  ? 48   ILE   C C    1 
ATOM   16918 O  O    . ILE   C  3  48  ? 1.319   -40.262 -57.189  1.00 55.86  ? 48   ILE   C O    1 
ATOM   16919 C  CB   . ILE   C  3  48  ? 0.259   -38.371 -59.491  1.00 62.40  ? 48   ILE   C CB   1 
ATOM   16920 C  CG1  . ILE   C  3  48  ? 0.509   -37.766 -60.875  1.00 64.41  ? 48   ILE   C CG1  1 
ATOM   16921 C  CG2  . ILE   C  3  48  ? -0.850  -37.619 -58.763  1.00 66.66  ? 48   ILE   C CG2  1 
ATOM   16922 C  CD1  . ILE   C  3  48  ? 0.785   -36.286 -60.858  1.00 61.96  ? 48   ILE   C CD1  1 
ATOM   16923 H  H    . ILE   C  3  48  ? 2.498   -39.938 -59.363  1.00 71.34  ? 48   ILE   C H    1 
ATOM   16924 H  HA   . ILE   C  3  48  ? 1.830   -37.456 -58.500  1.00 73.37  ? 48   ILE   C HA   1 
ATOM   16925 H  HB   . ILE   C  3  48  ? -0.023  -39.291 -59.612  1.00 74.86  ? 48   ILE   C HB   1 
ATOM   16926 H  HG12 . ILE   C  3  48  ? 1.278   -38.204 -61.271  1.00 77.27  ? 48   ILE   C HG12 1 
ATOM   16927 H  HG13 . ILE   C  3  48  ? -0.277  -37.913 -61.424  1.00 77.27  ? 48   ILE   C HG13 1 
ATOM   16928 H  HG21 . ILE   C  3  48  ? -1.610  -37.524 -59.357  1.00 79.97  ? 48   ILE   C HG21 1 
ATOM   16929 H  HG22 . ILE   C  3  48  ? -1.107  -38.122 -57.974  1.00 79.97  ? 48   ILE   C HG22 1 
ATOM   16930 H  HG23 . ILE   C  3  48  ? -0.521  -36.744 -58.505  1.00 79.97  ? 48   ILE   C HG23 1 
ATOM   16931 H  HD11 . ILE   C  3  48  ? 1.062   -36.007 -61.745  1.00 74.33  ? 48   ILE   C HD11 1 
ATOM   16932 H  HD12 . ILE   C  3  48  ? -0.025  -35.817 -60.602  1.00 74.33  ? 48   ILE   C HD12 1 
ATOM   16933 H  HD13 . ILE   C  3  48  ? 1.490   -36.103 -60.218  1.00 74.33  ? 48   ILE   C HD13 1 
ATOM   16934 N  N    . PHE   C  3  49  ? 1.075   -38.207 -56.284  1.00 66.14  ? 49   PHE   C N    1 
ATOM   16935 C  CA   . PHE   C  3  49  ? 0.641   -38.678 -54.978  1.00 65.57  ? 49   PHE   C CA   1 
ATOM   16936 C  C    . PHE   C  3  49  ? -0.486  -37.783 -54.481  1.00 66.39  ? 49   PHE   C C    1 
ATOM   16937 O  O    . PHE   C  3  49  ? -0.629  -36.632 -54.902  1.00 68.57  ? 49   PHE   C O    1 
ATOM   16938 C  CB   . PHE   C  3  49  ? 1.797   -38.709 -53.969  1.00 62.05  ? 49   PHE   C CB   1 
ATOM   16939 C  CG   . PHE   C  3  49  ? 2.363   -37.357 -53.646  1.00 58.27  ? 49   PHE   C CG   1 
ATOM   16940 C  CD1  . PHE   C  3  49  ? 3.288   -36.758 -54.486  1.00 55.99  ? 49   PHE   C CD1  1 
ATOM   16941 C  CD2  . PHE   C  3  49  ? 1.982   -36.691 -52.495  1.00 58.12  ? 49   PHE   C CD2  1 
ATOM   16942 C  CE1  . PHE   C  3  49  ? 3.813   -35.516 -54.189  1.00 59.14  ? 49   PHE   C CE1  1 
ATOM   16943 C  CE2  . PHE   C  3  49  ? 2.505   -35.449 -52.191  1.00 56.73  ? 49   PHE   C CE2  1 
ATOM   16944 C  CZ   . PHE   C  3  49  ? 3.422   -34.861 -53.039  1.00 60.19  ? 49   PHE   C CZ   1 
ATOM   16945 H  H    . PHE   C  3  49  ? 1.166   -37.353 -56.328  1.00 79.35  ? 49   PHE   C H    1 
ATOM   16946 H  HA   . PHE   C  3  49  ? 0.296   -39.582 -55.056  1.00 78.67  ? 49   PHE   C HA   1 
ATOM   16947 H  HB2  . PHE   C  3  49  ? 1.476   -39.099 -53.140  1.00 74.44  ? 49   PHE   C HB2  1 
ATOM   16948 H  HB3  . PHE   C  3  49  ? 2.515   -39.249 -54.334  1.00 74.44  ? 49   PHE   C HB3  1 
ATOM   16949 H  HD1  . PHE   C  3  49  ? 3.557   -37.198 -55.260  1.00 67.17  ? 49   PHE   C HD1  1 
ATOM   16950 H  HD2  . PHE   C  3  49  ? 1.366   -37.084 -51.919  1.00 69.73  ? 49   PHE   C HD2  1 
ATOM   16951 H  HE1  . PHE   C  3  49  ? 4.430   -35.121 -54.762  1.00 70.95  ? 49   PHE   C HE1  1 
ATOM   16952 H  HE2  . PHE   C  3  49  ? 2.239   -35.010 -51.415  1.00 68.05  ? 49   PHE   C HE2  1 
ATOM   16953 H  HZ   . PHE   C  3  49  ? 3.776   -34.025 -52.835  1.00 72.20  ? 49   PHE   C HZ   1 
ATOM   16954 N  N    . TYR   C  3  50  ? -1.293  -38.338 -53.578  1.00 64.93  ? 50   TYR   C N    1 
ATOM   16955 C  CA   . TYR   C  3  50  ? -2.501  -37.676 -53.081  1.00 64.75  ? 50   TYR   C CA   1 
ATOM   16956 C  C    . TYR   C  3  50  ? -3.355  -37.148 -54.234  1.00 65.93  ? 50   TYR   C C    1 
ATOM   16957 O  O    . TYR   C  3  50  ? -3.951  -36.071 -54.158  1.00 67.99  ? 50   TYR   C O    1 
ATOM   16958 C  CB   . TYR   C  3  50  ? -2.154  -36.560 -52.096  1.00 62.72  ? 50   TYR   C CB   1 
ATOM   16959 C  CG   . TYR   C  3  50  ? -3.292  -36.222 -51.159  1.00 63.64  ? 50   TYR   C CG   1 
ATOM   16960 C  CD1  . TYR   C  3  50  ? -3.831  -37.188 -50.322  1.00 63.13  ? 50   TYR   C CD1  1 
ATOM   16961 C  CD2  . TYR   C  3  50  ? -3.824  -34.941 -51.109  1.00 63.92  ? 50   TYR   C CD2  1 
ATOM   16962 C  CE1  . TYR   C  3  50  ? -4.871  -36.894 -49.467  1.00 65.09  ? 50   TYR   C CE1  1 
ATOM   16963 C  CE2  . TYR   C  3  50  ? -4.866  -34.635 -50.252  1.00 65.83  ? 50   TYR   C CE2  1 
ATOM   16964 C  CZ   . TYR   C  3  50  ? -5.385  -35.616 -49.433  1.00 65.52  ? 50   TYR   C CZ   1 
ATOM   16965 O  OH   . TYR   C  3  50  ? -6.421  -35.322 -48.577  1.00 65.35  ? 50   TYR   C OH   1 
ATOM   16966 H  H    . TYR   C  3  50  ? -1.161  -39.113 -53.230  1.00 77.90  ? 50   TYR   C H    1 
ATOM   16967 H  HA   . TYR   C  3  50  ? -3.032  -38.334 -52.605  1.00 77.68  ? 50   TYR   C HA   1 
ATOM   16968 H  HB2  . TYR   C  3  50  ? -1.396  -36.839 -51.558  1.00 75.25  ? 50   TYR   C HB2  1 
ATOM   16969 H  HB3  . TYR   C  3  50  ? -1.929  -35.759 -52.594  1.00 75.25  ? 50   TYR   C HB3  1 
ATOM   16970 H  HD1  . TYR   C  3  50  ? -3.485  -38.051 -50.338  1.00 75.74  ? 50   TYR   C HD1  1 
ATOM   16971 H  HD2  . TYR   C  3  50  ? -3.476  -34.278 -51.660  1.00 76.69  ? 50   TYR   C HD2  1 
ATOM   16972 H  HE1  . TYR   C  3  50  ? -5.224  -37.554 -48.915  1.00 78.09  ? 50   TYR   C HE1  1 
ATOM   16973 H  HE2  . TYR   C  3  50  ? -5.214  -33.773 -50.228  1.00 78.98  ? 50   TYR   C HE2  1 
ATOM   16974 H  HH   . TYR   C  3  50  ? -6.639  -34.515 -48.655  1.00 78.40  ? 50   TYR   C HH   1 
ATOM   16975 N  N    . THR   C  3  51  ? -3.382  -37.913 -55.324  1.00 63.54  ? 51   THR   C N    1 
ATOM   16976 C  CA   . THR   C  3  51  ? -4.329  -37.775 -56.426  1.00 64.47  ? 51   THR   C CA   1 
ATOM   16977 C  C    . THR   C  3  51  ? -4.084  -36.587 -57.350  1.00 62.83  ? 51   THR   C C    1 
ATOM   16978 O  O    . THR   C  3  51  ? -4.578  -36.583 -58.482  1.00 67.28  ? 51   THR   C O    1 
ATOM   16979 C  CB   . THR   C  3  51  ? -5.754  -37.644 -55.859  1.00 69.09  ? 51   THR   C CB   1 
ATOM   16980 O  OG1  . THR   C  3  51  ? -6.091  -38.813 -55.101  1.00 76.32  ? 51   THR   C OG1  1 
ATOM   16981 C  CG2  . THR   C  3  51  ? -6.779  -37.438 -56.970  1.00 68.44  ? 51   THR   C CG2  1 
ATOM   16982 H  H    . THR   C  3  51  ? -2.829  -38.558 -55.457  1.00 76.22  ? 51   THR   C H    1 
ATOM   16983 H  HA   . THR   C  3  51  ? -4.220  -38.570 -56.970  1.00 77.35  ? 51   THR   C HA   1 
ATOM   16984 H  HB   . THR   C  3  51  ? -5.789  -36.868 -55.279  1.00 82.89  ? 51   THR   C HB   1 
ATOM   16985 H  HG1  . THR   C  3  51  ? -5.557  -38.902 -54.458  1.00 91.56  ? 51   THR   C HG1  1 
ATOM   16986 H  HG21 . THR   C  3  51  ? -7.676  -37.558 -56.621  1.00 82.11  ? 51   THR   C HG21 1 
ATOM   16987 H  HG22 . THR   C  3  51  ? -6.700  -36.542 -57.333  1.00 82.11  ? 51   THR   C HG22 1 
ATOM   16988 H  HG23 . THR   C  3  51  ? -6.631  -38.080 -57.682  1.00 82.11  ? 51   THR   C HG23 1 
ATOM   16989 N  N    . SER   C  3  52  ? -3.307  -35.598 -56.921  1.00 61.91  ? 52   SER   C N    1 
ATOM   16990 C  CA   . SER   C  3  52  ? -3.039  -34.468 -57.805  1.00 66.36  ? 52   SER   C CA   1 
ATOM   16991 C  C    . SER   C  3  52  ? -1.674  -33.827 -57.611  1.00 69.39  ? 52   SER   C C    1 
ATOM   16992 O  O    . SER   C  3  52  ? -1.397  -32.824 -58.274  1.00 73.68  ? 52   SER   C O    1 
ATOM   16993 C  CB   . SER   C  3  52  ? -4.141  -33.405 -57.636  1.00 67.24  ? 52   SER   C CB   1 
ATOM   16994 O  OG   . SER   C  3  52  ? -4.189  -32.918 -56.308  1.00 69.28  ? 52   SER   C OG   1 
ATOM   16995 H  H    . SER   C  3  52  ? -2.934  -35.557 -56.148  1.00 74.27  ? 52   SER   C H    1 
ATOM   16996 H  HA   . SER   C  3  52  ? -3.066  -34.791 -58.719  1.00 79.61  ? 52   SER   C HA   1 
ATOM   16997 H  HB2  . SER   C  3  52  ? -3.957  -32.665 -58.235  1.00 80.67  ? 52   SER   C HB2  1 
ATOM   16998 H  HB3  . SER   C  3  52  ? -4.998  -33.804 -57.855  1.00 80.67  ? 52   SER   C HB3  1 
ATOM   16999 H  HG   . SER   C  3  52  ? -4.774  -32.319 -56.242  1.00 83.12  ? 52   SER   C HG   1 
ATOM   17000 N  N    . LYS   C  3  53  ? -0.818  -34.348 -56.741  1.00 69.05  ? 53   LYS   C N    1 
ATOM   17001 C  CA   . LYS   C  3  53  ? 0.403   -33.661 -56.342  1.00 67.76  ? 53   LYS   C CA   1 
ATOM   17002 C  C    . LYS   C  3  53  ? 1.581   -34.215 -57.132  1.00 61.84  ? 53   LYS   C C    1 
ATOM   17003 O  O    . LYS   C  3  53  ? 1.852   -35.420 -57.091  1.00 55.63  ? 53   LYS   C O    1 
ATOM   17004 C  CB   . LYS   C  3  53  ? 0.634   -33.812 -54.839  1.00 68.76  ? 53   LYS   C CB   1 
ATOM   17005 C  CG   . LYS   C  3  53  ? -0.589  -33.476 -53.993  1.00 69.83  ? 53   LYS   C CG   1 
ATOM   17006 C  CD   . LYS   C  3  53  ? -1.089  -32.062 -54.266  1.00 73.10  ? 53   LYS   C CD   1 
ATOM   17007 C  CE   . LYS   C  3  53  ? -2.281  -31.711 -53.389  1.00 77.12  ? 53   LYS   C CE   1 
ATOM   17008 N  NZ   . LYS   C  3  53  ? -2.747  -30.315 -53.615  1.00 83.54  ? 53   LYS   C NZ   1 
ATOM   17009 H  H    . LYS   C  3  53  ? -0.925  -35.113 -56.361  1.00 82.84  ? 53   LYS   C H    1 
ATOM   17010 H  HA   . LYS   C  3  53  ? 0.325   -32.717 -56.550  1.00 81.29  ? 53   LYS   C HA   1 
ATOM   17011 H  HB2  . LYS   C  3  53  ? 0.880   -34.732 -54.652  1.00 82.49  ? 53   LYS   C HB2  1 
ATOM   17012 H  HB3  . LYS   C  3  53  ? 1.352   -33.217 -54.572  1.00 82.49  ? 53   LYS   C HB3  1 
ATOM   17013 H  HG2  . LYS   C  3  53  ? -1.305  -34.097 -54.203  1.00 83.78  ? 53   LYS   C HG2  1 
ATOM   17014 H  HG3  . LYS   C  3  53  ? -0.358  -33.541 -53.054  1.00 83.78  ? 53   LYS   C HG3  1 
ATOM   17015 H  HD2  . LYS   C  3  53  ? -0.378  -31.429 -54.080  1.00 87.70  ? 53   LYS   C HD2  1 
ATOM   17016 H  HD3  . LYS   C  3  53  ? -1.362  -31.992 -55.194  1.00 87.70  ? 53   LYS   C HD3  1 
ATOM   17017 H  HE2  . LYS   C  3  53  ? -3.015  -32.311 -53.592  1.00 92.52  ? 53   LYS   C HE2  1 
ATOM   17018 H  HE3  . LYS   C  3  53  ? -2.029  -31.798 -52.456  1.00 92.52  ? 53   LYS   C HE3  1 
ATOM   17019 H  HZ1  . LYS   C  3  53  ? -3.458  -30.146 -53.108  1.00 100.23 ? 53   LYS   C HZ1  1 
ATOM   17020 H  HZ2  . LYS   C  3  53  ? -2.100  -29.741 -53.406  1.00 100.23 ? 53   LYS   C HZ2  1 
ATOM   17021 H  HZ3  . LYS   C  3  53  ? -2.967  -30.203 -54.470  1.00 100.23 ? 53   LYS   C HZ3  1 
ATOM   17022 N  N    . LEU   C  3  54  ? 2.274   -33.333 -57.849  1.00 64.57  ? 54   LEU   C N    1 
ATOM   17023 C  CA   . LEU   C  3  54  ? 3.447   -33.741 -58.609  1.00 65.81  ? 54   LEU   C CA   1 
ATOM   17024 C  C    . LEU   C  3  54  ? 4.615   -34.010 -57.672  1.00 63.34  ? 54   LEU   C C    1 
ATOM   17025 O  O    . LEU   C  3  54  ? 4.938   -33.187 -56.810  1.00 62.42  ? 54   LEU   C O    1 
ATOM   17026 C  CB   . LEU   C  3  54  ? 3.840   -32.663 -59.617  1.00 72.16  ? 54   LEU   C CB   1 
ATOM   17027 C  CG   . LEU   C  3  54  ? 3.114   -32.601 -60.961  1.00 80.05  ? 54   LEU   C CG   1 
ATOM   17028 C  CD1  . LEU   C  3  54  ? 3.744   -31.515 -61.812  1.00 82.25  ? 54   LEU   C CD1  1 
ATOM   17029 C  CD2  . LEU   C  3  54  ? 3.168   -33.925 -61.694  1.00 82.21  ? 54   LEU   C CD2  1 
ATOM   17030 H  H    . LEU   C  3  54  ? 2.085   -32.496 -57.911  1.00 77.47  ? 54   LEU   C H    1 
ATOM   17031 H  HA   . LEU   C  3  54  ? 3.236   -34.554 -59.094  1.00 78.95  ? 54   LEU   C HA   1 
ATOM   17032 H  HB2  . LEU   C  3  54  ? 3.700   -31.803 -59.191  1.00 86.57  ? 54   LEU   C HB2  1 
ATOM   17033 H  HB3  . LEU   C  3  54  ? 4.780   -32.785 -59.820  1.00 86.57  ? 54   LEU   C HB3  1 
ATOM   17034 H  HG   . LEU   C  3  54  ? 2.178   -32.401 -60.803  1.00 96.04  ? 54   LEU   C HG   1 
ATOM   17035 H  HD11 . LEU   C  3  54  ? 3.130   -31.276 -62.524  1.00 98.68  ? 54   LEU   C HD11 1 
ATOM   17036 H  HD12 . LEU   C  3  54  ? 3.922   -30.741 -61.255  1.00 98.68  ? 54   LEU   C HD12 1 
ATOM   17037 H  HD13 . LEU   C  3  54  ? 4.573   -31.849 -62.189  1.00 98.68  ? 54   LEU   C HD13 1 
ATOM   17038 H  HD21 . LEU   C  3  54  ? 2.693   -33.840 -62.535  1.00 98.63  ? 54   LEU   C HD21 1 
ATOM   17039 H  HD22 . LEU   C  3  54  ? 4.095   -34.157 -61.859  1.00 98.63  ? 54   LEU   C HD22 1 
ATOM   17040 H  HD23 . LEU   C  3  54  ? 2.749   -34.607 -61.146  1.00 98.63  ? 54   LEU   C HD23 1 
ATOM   17041 N  N    . HIS   C  3  55  ? 5.251   -35.164 -57.845  1.00 61.17  ? 55   HIS   C N    1 
ATOM   17042 C  CA   . HIS   C  3  55  ? 6.486   -35.440 -57.130  1.00 62.99  ? 55   HIS   C CA   1 
ATOM   17043 C  C    . HIS   C  3  55  ? 7.615   -34.584 -57.693  1.00 64.24  ? 55   HIS   C C    1 
ATOM   17044 O  O    . HIS   C  3  55  ? 7.610   -34.199 -58.865  1.00 64.15  ? 55   HIS   C O    1 
ATOM   17045 C  CB   . HIS   C  3  55  ? 6.846   -36.921 -57.230  1.00 65.57  ? 55   HIS   C CB   1 
ATOM   17046 C  CG   . HIS   C  3  55  ? 8.083   -37.287 -56.471  1.00 70.00  ? 55   HIS   C CG   1 
ATOM   17047 N  ND1  . HIS   C  3  55  ? 9.136   -37.969 -57.042  1.00 72.40  ? 55   HIS   C ND1  1 
ATOM   17048 C  CD2  . HIS   C  3  55  ? 8.441   -37.047 -55.188  1.00 71.50  ? 55   HIS   C CD2  1 
ATOM   17049 C  CE1  . HIS   C  3  55  ? 10.085  -38.142 -56.139  1.00 74.57  ? 55   HIS   C CE1  1 
ATOM   17050 N  NE2  . HIS   C  3  55  ? 9.688   -37.592 -55.006  1.00 73.67  ? 55   HIS   C NE2  1 
ATOM   17051 H  H    . HIS   C  3  55  ? 4.990   -35.796 -58.367  1.00 73.38  ? 55   HIS   C H    1 
ATOM   17052 H  HA   . HIS   C  3  55  ? 6.375   -35.229 -56.190  1.00 75.56  ? 55   HIS   C HA   1 
ATOM   17053 H  HB2  . HIS   C  3  55  ? 6.113   -37.446 -56.874  1.00 78.66  ? 55   HIS   C HB2  1 
ATOM   17054 H  HB3  . HIS   C  3  55  ? 6.993   -37.145 -58.162  1.00 78.66  ? 55   HIS   C HB3  1 
ATOM   17055 H  HD2  . HIS   C  3  55  ? 7.936   -36.598 -54.548  1.00 85.78  ? 55   HIS   C HD2  1 
ATOM   17056 H  HE1  . HIS   C  3  55  ? 10.895  -38.578 -56.278  1.00 89.46  ? 55   HIS   C HE1  1 
ATOM   17057 H  HE2  . HIS   C  3  55  ? 10.138  -37.577 -54.273  1.00 88.38  ? 55   HIS   C HE2  1 
ATOM   17058 N  N    . SER   C  3  56  ? 8.585   -34.274 -56.840  1.00 64.77  ? 56   SER   C N    1 
ATOM   17059 C  CA   . SER   C  3  56  ? 9.702   -33.437 -57.255  1.00 70.48  ? 56   SER   C CA   1 
ATOM   17060 C  C    . SER   C  3  56  ? 10.421  -34.052 -58.449  1.00 70.33  ? 56   SER   C C    1 
ATOM   17061 O  O    . SER   C  3  56  ? 10.863  -35.204 -58.395  1.00 69.38  ? 56   SER   C O    1 
ATOM   17062 C  CB   . SER   C  3  56  ? 10.675  -33.249 -56.092  1.00 79.77  ? 56   SER   C CB   1 
ATOM   17063 O  OG   . SER   C  3  56  ? 11.852  -32.585 -56.519  1.00 89.19  ? 56   SER   C OG   1 
ATOM   17064 H  H    . SER   C  3  56  ? 8.619   -34.534 -56.021  1.00 77.71  ? 56   SER   C H    1 
ATOM   17065 H  HA   . SER   C  3  56  ? 9.363   -32.567 -57.518  1.00 84.56  ? 56   SER   C HA   1 
ATOM   17066 H  HB2  . SER   C  3  56  ? 10.245  -32.718 -55.404  1.00 95.70  ? 56   SER   C HB2  1 
ATOM   17067 H  HB3  . SER   C  3  56  ? 10.915  -34.120 -55.738  1.00 95.70  ? 56   SER   C HB3  1 
ATOM   17068 H  HG   . SER   C  3  56  ? 12.415  -32.568 -55.896  1.00 107.01 ? 56   SER   C HG   1 
ATOM   17069 N  N    . GLY   C  3  57  ? 10.533  -33.281 -59.530  1.00 71.62  ? 57   GLY   C N    1 
ATOM   17070 C  CA   . GLY   C  3  57  ? 11.335  -33.644 -60.677  1.00 74.82  ? 57   GLY   C CA   1 
ATOM   17071 C  C    . GLY   C  3  57  ? 10.549  -34.093 -61.890  1.00 75.09  ? 57   GLY   C C    1 
ATOM   17072 O  O    . GLY   C  3  57  ? 11.069  -34.006 -63.010  1.00 80.29  ? 57   GLY   C O    1 
ATOM   17073 H  H    . GLY   C  3  57  ? 10.138  -32.522 -59.616  1.00 85.93  ? 57   GLY   C H    1 
ATOM   17074 H  HA2  . GLY   C  3  57  ? 11.868  -32.877 -60.938  1.00 89.77  ? 57   GLY   C HA2  1 
ATOM   17075 H  HA3  . GLY   C  3  57  ? 11.928  -34.369 -60.424  1.00 89.77  ? 57   GLY   C HA3  1 
ATOM   17076 N  N    . VAL   C  3  58  ? 9.321   -34.569 -61.713  1.00 70.60  ? 58   VAL   C N    1 
ATOM   17077 C  CA   . VAL   C  3  58  ? 8.542   -35.085 -62.838  1.00 72.27  ? 58   VAL   C CA   1 
ATOM   17078 C  C    . VAL   C  3  58  ? 7.974   -33.900 -63.613  1.00 72.85  ? 58   VAL   C C    1 
ATOM   17079 O  O    . VAL   C  3  58  ? 7.647   -32.867 -63.011  1.00 73.32  ? 58   VAL   C O    1 
ATOM   17080 C  CB   . VAL   C  3  58  ? 7.441   -36.051 -62.367  1.00 76.35  ? 58   VAL   C CB   1 
ATOM   17081 C  CG1  . VAL   C  3  58  ? 8.057   -37.232 -61.619  1.00 75.12  ? 58   VAL   C CG1  1 
ATOM   17082 C  CG2  . VAL   C  3  58  ? 6.422   -35.353 -61.483  1.00 79.54  ? 58   VAL   C CG2  1 
ATOM   17083 H  H    . VAL   C  3  58  ? 8.917   -34.605 -60.954  1.00 84.70  ? 58   VAL   C H    1 
ATOM   17084 H  HA   . VAL   C  3  58  ? 9.125   -35.582 -63.433  1.00 86.70  ? 58   VAL   C HA   1 
ATOM   17085 H  HB   . VAL   C  3  58  ? 6.975   -36.379 -63.152  1.00 91.60  ? 58   VAL   C HB   1 
ATOM   17086 H  HG11 . VAL   C  3  58  ? 7.367   -37.669 -61.096  1.00 90.13  ? 58   VAL   C HG11 1 
ATOM   17087 H  HG12 . VAL   C  3  58  ? 8.429   -37.855 -62.263  1.00 90.13  ? 58   VAL   C HG12 1 
ATOM   17088 H  HG13 . VAL   C  3  58  ? 8.758   -36.904 -61.034  1.00 90.13  ? 58   VAL   C HG13 1 
ATOM   17089 H  HG21 . VAL   C  3  58  ? 5.581   -35.834 -61.530  1.00 95.43  ? 58   VAL   C HG21 1 
ATOM   17090 H  HG22 . VAL   C  3  58  ? 6.748   -35.346 -60.569  1.00 95.43  ? 58   VAL   C HG22 1 
ATOM   17091 H  HG23 . VAL   C  3  58  ? 6.301   -34.444 -61.798  1.00 95.43  ? 58   VAL   C HG23 1 
ATOM   17092 N  N    . PRO   C  3  59  ? 7.848   -33.992 -64.935  1.00 75.86  ? 59   PRO   C N    1 
ATOM   17093 C  CA   . PRO   C  3  59  ? 7.430   -32.824 -65.718  1.00 81.05  ? 59   PRO   C CA   1 
ATOM   17094 C  C    . PRO   C  3  59  ? 5.966   -32.472 -65.504  1.00 77.98  ? 59   PRO   C C    1 
ATOM   17095 O  O    . PRO   C  3  59  ? 5.160   -33.269 -65.018  1.00 75.37  ? 59   PRO   C O    1 
ATOM   17096 C  CB   . PRO   C  3  59  ? 7.694   -33.253 -67.167  1.00 85.23  ? 59   PRO   C CB   1 
ATOM   17097 C  CG   . PRO   C  3  59  ? 7.674   -34.742 -67.137  1.00 80.46  ? 59   PRO   C CG   1 
ATOM   17098 C  CD   . PRO   C  3  59  ? 8.194   -35.142 -65.789  1.00 75.48  ? 59   PRO   C CD   1 
ATOM   17099 H  HA   . PRO   C  3  59  ? 7.978   -32.056 -65.494  1.00 97.24  ? 59   PRO   C HA   1 
ATOM   17100 H  HB2  . PRO   C  3  59  ? 6.996   -32.908 -67.745  1.00 102.26 ? 59   PRO   C HB2  1 
ATOM   17101 H  HB3  . PRO   C  3  59  ? 8.558   -32.923 -67.457  1.00 102.26 ? 59   PRO   C HB3  1 
ATOM   17102 H  HG2  . PRO   C  3  59  ? 6.765   -35.058 -67.260  1.00 96.53  ? 59   PRO   C HG2  1 
ATOM   17103 H  HG3  . PRO   C  3  59  ? 8.245   -35.090 -67.840  1.00 96.53  ? 59   PRO   C HG3  1 
ATOM   17104 H  HD2  . PRO   C  3  59  ? 7.755   -35.949 -65.476  1.00 90.56  ? 59   PRO   C HD2  1 
ATOM   17105 H  HD3  . PRO   C  3  59  ? 9.154   -35.276 -65.816  1.00 90.56  ? 59   PRO   C HD3  1 
ATOM   17106 N  N    . SER   C  3  60  ? 5.631   -31.236 -65.890  1.00 79.59  ? 60   SER   C N    1 
ATOM   17107 C  CA   . SER   C  3  60  ? 4.284   -30.715 -65.696  1.00 79.18  ? 60   SER   C CA   1 
ATOM   17108 C  C    . SER   C  3  60  ? 3.247   -31.434 -66.546  1.00 78.28  ? 60   SER   C C    1 
ATOM   17109 O  O    . SER   C  3  60  ? 2.049   -31.320 -66.265  1.00 75.65  ? 60   SER   C O    1 
ATOM   17110 C  CB   . SER   C  3  60  ? 4.251   -29.221 -66.023  1.00 84.71  ? 60   SER   C CB   1 
ATOM   17111 O  OG   . SER   C  3  60  ? 4.534   -29.001 -67.395  1.00 90.93  ? 60   SER   C OG   1 
ATOM   17112 H  H    . SER   C  3  60  ? 6.170   -30.682 -66.266  1.00 95.48  ? 60   SER   C H    1 
ATOM   17113 H  HA   . SER   C  3  60  ? 4.044   -30.835 -64.764  1.00 94.99  ? 60   SER   C HA   1 
ATOM   17114 H  HB2  . SER   C  3  60  ? 3.368   -28.873 -65.822  1.00 101.64 ? 60   SER   C HB2  1 
ATOM   17115 H  HB3  . SER   C  3  60  ? 4.917   -28.765 -65.485  1.00 101.64 ? 60   SER   C HB3  1 
ATOM   17116 H  HG   . SER   C  3  60  ? 4.215   -28.263 -67.640  1.00 109.09 ? 60   SER   C HG   1 
ATOM   17117 N  N    . ARG   C  3  61  ? 3.675   -32.160 -67.583  1.00 79.92  ? 61   ARG   C N    1 
ATOM   17118 C  CA   . ARG   C  3  61  ? 2.721   -32.855 -68.441  1.00 79.84  ? 61   ARG   C CA   1 
ATOM   17119 C  C    . ARG   C  3  61  ? 1.803   -33.753 -67.626  1.00 76.38  ? 61   ARG   C C    1 
ATOM   17120 O  O    . ARG   C  3  61  ? 0.598   -33.833 -67.892  1.00 79.63  ? 61   ARG   C O    1 
ATOM   17121 C  CB   . ARG   C  3  61  ? 3.461   -33.685 -69.489  1.00 80.51  ? 61   ARG   C CB   1 
ATOM   17122 C  CG   . ARG   C  3  61  ? 4.563   -32.949 -70.223  1.00 85.03  ? 61   ARG   C CG   1 
ATOM   17123 C  CD   . ARG   C  3  61  ? 5.087   -33.788 -71.375  1.00 83.97  ? 61   ARG   C CD   1 
ATOM   17124 N  NE   . ARG   C  3  61  ? 5.592   -35.085 -70.927  1.00 77.44  ? 61   ARG   C NE   1 
ATOM   17125 C  CZ   . ARG   C  3  61  ? 6.858   -35.334 -70.598  1.00 76.88  ? 61   ARG   C CZ   1 
ATOM   17126 N  NH1  . ARG   C  3  61  ? 7.775   -34.376 -70.660  1.00 76.71  ? 61   ARG   C NH1  1 
ATOM   17127 N  NH2  . ARG   C  3  61  ? 7.210   -36.551 -70.204  1.00 76.07  ? 61   ARG   C NH2  1 
ATOM   17128 H  H    . ARG   C  3  61  ? 4.499   -32.263 -67.805  1.00 95.88  ? 61   ARG   C H    1 
ATOM   17129 H  HA   . ARG   C  3  61  ? 2.182   -32.192 -68.900  1.00 95.78  ? 61   ARG   C HA   1 
ATOM   17130 H  HB2  . ARG   C  3  61  ? 3.864   -34.449 -69.047  1.00 96.59  ? 61   ARG   C HB2  1 
ATOM   17131 H  HB3  . ARG   C  3  61  ? 2.819   -33.986 -70.151  1.00 96.59  ? 61   ARG   C HB3  1 
ATOM   17132 H  HG2  . ARG   C  3  61  ? 4.216   -32.117 -70.580  1.00 102.02 ? 61   ARG   C HG2  1 
ATOM   17133 H  HG3  . ARG   C  3  61  ? 5.296   -32.769 -69.614  1.00 102.02 ? 61   ARG   C HG3  1 
ATOM   17134 H  HD2  . ARG   C  3  61  ? 4.369   -33.946 -72.007  1.00 100.74 ? 61   ARG   C HD2  1 
ATOM   17135 H  HD3  . ARG   C  3  61  ? 5.813   -33.314 -71.809  1.00 100.74 ? 61   ARG   C HD3  1 
ATOM   17136 H  HE   . ARG   C  3  61  ? 5.031   -35.735 -70.873  1.00 92.91  ? 61   ARG   C HE   1 
ATOM   17137 H  HH11 . ARG   C  3  61  ? 7.553   -33.585 -70.915  1.00 92.04  ? 61   ARG   C HH11 1 
ATOM   17138 H  HH12 . ARG   C  3  61  ? 8.590   -34.547 -70.445  1.00 92.04  ? 61   ARG   C HH12 1 
ATOM   17139 H  HH21 . ARG   C  3  61  ? 6.621   -37.176 -70.162  1.00 91.27  ? 61   ARG   C HH21 1 
ATOM   17140 H  HH22 . ARG   C  3  61  ? 8.027   -36.714 -69.990  1.00 91.27  ? 61   ARG   C HH22 1 
ATOM   17141 N  N    . PHE   C  3  62  ? 2.358   -34.440 -66.634  1.00 71.74  ? 62   PHE   C N    1 
ATOM   17142 C  CA   . PHE   C  3  62  ? 1.579   -35.354 -65.815  1.00 70.22  ? 62   PHE   C CA   1 
ATOM   17143 C  C    . PHE   C  3  62  ? 0.707   -34.579 -64.838  1.00 70.96  ? 62   PHE   C C    1 
ATOM   17144 O  O    . PHE   C  3  62  ? 1.127   -33.568 -64.270  1.00 75.79  ? 62   PHE   C O    1 
ATOM   17145 C  CB   . PHE   C  3  62  ? 2.503   -36.307 -65.059  1.00 64.36  ? 62   PHE   C CB   1 
ATOM   17146 C  CG   . PHE   C  3  62  ? 3.308   -37.198 -65.958  1.00 64.97  ? 62   PHE   C CG   1 
ATOM   17147 C  CD1  . PHE   C  3  62  ? 2.779   -38.389 -66.425  1.00 65.83  ? 62   PHE   C CD1  1 
ATOM   17148 C  CD2  . PHE   C  3  62  ? 4.589   -36.841 -66.345  1.00 67.74  ? 62   PHE   C CD2  1 
ATOM   17149 C  CE1  . PHE   C  3  62  ? 3.513   -39.213 -67.258  1.00 64.65  ? 62   PHE   C CE1  1 
ATOM   17150 C  CE2  . PHE   C  3  62  ? 5.330   -37.660 -67.178  1.00 67.48  ? 62   PHE   C CE2  1 
ATOM   17151 C  CZ   . PHE   C  3  62  ? 4.790   -38.848 -67.636  1.00 65.60  ? 62   PHE   C CZ   1 
ATOM   17152 H  H    . PHE   C  3  62  ? 3.188   -34.393 -66.415  1.00 86.07  ? 62   PHE   C H    1 
ATOM   17153 H  HA   . PHE   C  3  62  ? 0.997   -35.885 -66.381  1.00 84.25  ? 62   PHE   C HA   1 
ATOM   17154 H  HB2  . PHE   C  3  62  ? 3.123   -35.785 -64.526  1.00 77.22  ? 62   PHE   C HB2  1 
ATOM   17155 H  HB3  . PHE   C  3  62  ? 1.965   -36.873 -64.484  1.00 77.22  ? 62   PHE   C HB3  1 
ATOM   17156 H  HD1  . PHE   C  3  62  ? 1.918   -38.638 -66.175  1.00 78.97  ? 62   PHE   C HD1  1 
ATOM   17157 H  HD2  . PHE   C  3  62  ? 4.956   -36.042 -66.042  1.00 81.27  ? 62   PHE   C HD2  1 
ATOM   17158 H  HE1  . PHE   C  3  62  ? 3.147   -40.011 -67.563  1.00 77.57  ? 62   PHE   C HE1  1 
ATOM   17159 H  HE2  . PHE   C  3  62  ? 6.190   -37.412 -67.430  1.00 80.96  ? 62   PHE   C HE2  1 
ATOM   17160 H  HZ   . PHE   C  3  62  ? 5.285   -39.400 -68.196  1.00 78.70  ? 62   PHE   C HZ   1 
ATOM   17161 N  N    . SER   C  3  63  ? -0.519  -35.059 -64.656  1.00 68.36  ? 63   SER   C N    1 
ATOM   17162 C  CA   . SER   C  3  63  ? -1.462  -34.441 -63.739  1.00 66.90  ? 63   SER   C CA   1 
ATOM   17163 C  C    . SER   C  3  63  ? -2.439  -35.505 -63.266  1.00 70.82  ? 63   SER   C C    1 
ATOM   17164 O  O    . SER   C  3  63  ? -2.701  -36.484 -63.970  1.00 72.59  ? 63   SER   C O    1 
ATOM   17165 C  CB   . SER   C  3  63  ? -2.210  -33.278 -64.397  1.00 62.89  ? 63   SER   C CB   1 
ATOM   17166 O  OG   . SER   C  3  63  ? -2.880  -33.702 -65.570  1.00 65.86  ? 63   SER   C OG   1 
ATOM   17167 H  H    . SER   C  3  63  ? -0.831  -35.751 -65.060  1.00 82.02  ? 63   SER   C H    1 
ATOM   17168 H  HA   . SER   C  3  63  ? -0.991  -34.092 -62.966  1.00 80.26  ? 63   SER   C HA   1 
ATOM   17169 H  HB2  . SER   C  3  63  ? -2.863  -32.928 -63.770  1.00 75.45  ? 63   SER   C HB2  1 
ATOM   17170 H  HB3  . SER   C  3  63  ? -1.572  -32.586 -64.632  1.00 75.45  ? 63   SER   C HB3  1 
ATOM   17171 H  HG   . SER   C  3  63  ? -3.357  -33.079 -65.870  1.00 79.02  ? 63   SER   C HG   1 
ATOM   17172 N  N    . GLY   C  3  64  ? -2.970  -35.303 -62.068  1.00 71.35  ? 64   GLY   C N    1 
ATOM   17173 C  CA   . GLY   C  3  64  ? -3.876  -36.261 -61.469  1.00 69.07  ? 64   GLY   C CA   1 
ATOM   17174 C  C    . GLY   C  3  64  ? -5.187  -35.615 -61.077  1.00 69.27  ? 64   GLY   C C    1 
ATOM   17175 O  O    . GLY   C  3  64  ? -5.258  -34.419 -60.795  1.00 74.74  ? 64   GLY   C O    1 
ATOM   17176 H  H    . GLY   C  3  64  ? -2.819  -34.611 -61.580  1.00 85.60  ? 64   GLY   C H    1 
ATOM   17177 H  HA2  . GLY   C  3  64  ? -4.059  -36.973 -62.102  1.00 82.86  ? 64   GLY   C HA2  1 
ATOM   17178 H  HA3  . GLY   C  3  64  ? -3.468  -36.641 -60.675  1.00 82.86  ? 64   GLY   C HA3  1 
ATOM   17179 N  N    . SER   C  3  65  ? -6.232  -36.437 -61.056  1.00 67.61  ? 65   SER   C N    1 
ATOM   17180 C  CA   . SER   C  3  65  ? -7.567  -35.982 -60.701  1.00 68.91  ? 65   SER   C CA   1 
ATOM   17181 C  C    . SER   C  3  65  ? -8.340  -37.155 -60.119  1.00 66.43  ? 65   SER   C C    1 
ATOM   17182 O  O    . SER   C  3  65  ? -7.960  -38.316 -60.285  1.00 63.46  ? 65   SER   C O    1 
ATOM   17183 C  CB   . SER   C  3  65  ? -8.308  -35.409 -61.914  1.00 71.88  ? 65   SER   C CB   1 
ATOM   17184 O  OG   . SER   C  3  65  ? -8.431  -36.388 -62.932  1.00 78.74  ? 65   SER   C OG   1 
ATOM   17185 H  H    . SER   C  3  65  ? -6.192  -37.274 -61.248  1.00 81.12  ? 65   SER   C H    1 
ATOM   17186 H  HA   . SER   C  3  65  ? -7.502  -35.287 -60.027  1.00 82.67  ? 65   SER   C HA   1 
ATOM   17187 H  HB2  . SER   C  3  65  ? -9.194  -35.125 -61.639  1.00 86.24  ? 65   SER   C HB2  1 
ATOM   17188 H  HB3  . SER   C  3  65  ? -7.810  -34.652 -62.261  1.00 86.24  ? 65   SER   C HB3  1 
ATOM   17189 H  HG   . SER   C  3  65  ? -8.909  -36.093 -63.557  1.00 94.46  ? 65   SER   C HG   1 
ATOM   17190 N  N    . GLY   C  3  66  ? -9.432  -36.839 -59.432  1.00 68.39  ? 66   GLY   C N    1 
ATOM   17191 C  CA   . GLY   C  3  66  ? -10.343 -37.841 -58.928  1.00 72.64  ? 66   GLY   C CA   1 
ATOM   17192 C  C    . GLY   C  3  66  ? -10.703 -37.607 -57.479  1.00 76.66  ? 66   GLY   C C    1 
ATOM   17193 O  O    . GLY   C  3  66  ? -10.215 -36.690 -56.820  1.00 77.58  ? 66   GLY   C O    1 
ATOM   17194 H  H    . GLY   C  3  66  ? -9.665  -36.032 -59.245  1.00 82.04  ? 66   GLY   C H    1 
ATOM   17195 H  HA2  . GLY   C  3  66  ? -11.159 -37.827 -59.452  1.00 87.15  ? 66   GLY   C HA2  1 
ATOM   17196 H  HA3  . GLY   C  3  66  ? -9.934  -38.716 -59.004  1.00 87.15  ? 66   GLY   C HA3  1 
ATOM   17197 N  N    . SER   C  3  67  ? -11.581 -38.473 -56.982  1.00 79.78  ? 67   SER   C N    1 
ATOM   17198 C  CA   . SER   C  3  67  ? -12.059 -38.427 -55.607  1.00 81.68  ? 67   SER   C CA   1 
ATOM   17199 C  C    . SER   C  3  67  ? -12.892 -39.680 -55.376  1.00 81.51  ? 67   SER   C C    1 
ATOM   17200 O  O    . SER   C  3  67  ? -13.262 -40.384 -56.320  1.00 80.51  ? 67   SER   C O    1 
ATOM   17201 C  CB   . SER   C  3  67  ? -12.879 -37.165 -55.330  1.00 85.76  ? 67   SER   C CB   1 
ATOM   17202 O  OG   . SER   C  3  67  ? -14.073 -37.164 -56.093  1.00 93.12  ? 67   SER   C OG   1 
ATOM   17203 H  H    . SER   C  3  67  ? -11.925 -39.116 -57.438  1.00 95.72  ? 67   SER   C H    1 
ATOM   17204 H  HA   . SER   C  3  67  ? -11.304 -38.432 -54.997  1.00 98.00  ? 67   SER   C HA   1 
ATOM   17205 H  HB2  . SER   C  3  67  ? -13.106 -37.136 -54.388  1.00 102.89 ? 67   SER   C HB2  1 
ATOM   17206 H  HB3  . SER   C  3  67  ? -12.351 -36.387 -55.568  1.00 102.89 ? 67   SER   C HB3  1 
ATOM   17207 H  HG   . SER   C  3  67  ? -14.529 -36.482 -55.912  1.00 111.72 ? 67   SER   C HG   1 
ATOM   17208 N  N    . GLY   C  3  68  ? -13.186 -39.949 -54.108  1.00 83.52  ? 68   GLY   C N    1 
ATOM   17209 C  CA   . GLY   C  3  68  ? -13.973 -41.115 -53.761  1.00 84.82  ? 68   GLY   C CA   1 
ATOM   17210 C  C    . GLY   C  3  68  ? -13.324 -42.408 -54.210  1.00 80.98  ? 68   GLY   C C    1 
ATOM   17211 O  O    . GLY   C  3  68  ? -12.320 -42.838 -53.635  1.00 77.04  ? 68   GLY   C O    1 
ATOM   17212 H  H    . GLY   C  3  68  ? -12.940 -39.471 -53.436  1.00 100.21 ? 68   GLY   C H    1 
ATOM   17213 H  HA2  . GLY   C  3  68  ? -14.087 -41.150 -52.798  1.00 101.77 ? 68   GLY   C HA2  1 
ATOM   17214 H  HA3  . GLY   C  3  68  ? -14.845 -41.049 -54.180  1.00 101.77 ? 68   GLY   C HA3  1 
ATOM   17215 N  N    . THR   C  3  69  ? -13.890 -43.037 -55.243  1.00 83.51  ? 69   THR   C N    1 
ATOM   17216 C  CA   . THR   C  3  69  ? -13.400 -44.315 -55.738  1.00 85.25  ? 69   THR   C CA   1 
ATOM   17217 C  C    . THR   C  3  69  ? -12.835 -44.251 -57.151  1.00 89.48  ? 69   THR   C C    1 
ATOM   17218 O  O    . THR   C  3  69  ? -12.185 -45.211 -57.578  1.00 88.38  ? 69   THR   C O    1 
ATOM   17219 C  CB   . THR   C  3  69  ? -14.523 -45.365 -55.705  1.00 84.71  ? 69   THR   C CB   1 
ATOM   17220 O  OG1  . THR   C  3  69  ? -15.539 -45.014 -56.653  1.00 87.41  ? 69   THR   C OG1  1 
ATOM   17221 C  CG2  . THR   C  3  69  ? -15.139 -45.449 -54.317  1.00 86.33  ? 69   THR   C CG2  1 
ATOM   17222 H  H    . THR   C  3  69  ? -14.569 -42.736 -55.676  1.00 100.20 ? 69   THR   C H    1 
ATOM   17223 H  HA   . THR   C  3  69  ? -12.688 -44.612 -55.149  1.00 102.28 ? 69   THR   C HA   1 
ATOM   17224 H  HB   . THR   C  3  69  ? -14.156 -46.234 -55.931  1.00 101.63 ? 69   THR   C HB   1 
ATOM   17225 H  HG1  . THR   C  3  69  ? -16.171 -45.566 -56.614  1.00 104.87 ? 69   THR   C HG1  1 
ATOM   17226 H  HG21 . THR   C  3  69  ? -15.794 -46.165 -54.288  1.00 103.57 ? 69   THR   C HG21 1 
ATOM   17227 H  HG22 . THR   C  3  69  ? -14.450 -45.626 -53.658  1.00 103.57 ? 69   THR   C HG22 1 
ATOM   17228 H  HG23 . THR   C  3  69  ? -15.578 -44.612 -54.097  1.00 103.57 ? 69   THR   C HG23 1 
ATOM   17229 N  N    . ASP   C  3  70  ? -13.059 -43.162 -57.884  1.00 92.05  ? 70   ASP   C N    1 
ATOM   17230 C  CA   . ASP   C  3  70  ? -12.620 -43.038 -59.268  1.00 88.92  ? 70   ASP   C CA   1 
ATOM   17231 C  C    . ASP   C  3  70  ? -11.497 -42.014 -59.365  1.00 81.69  ? 70   ASP   C C    1 
ATOM   17232 O  O    . ASP   C  3  70  ? -11.604 -40.911 -58.819  1.00 80.83  ? 70   ASP   C O    1 
ATOM   17233 C  CB   . ASP   C  3  70  ? -13.785 -42.635 -60.177  1.00 93.79  ? 70   ASP   C CB   1 
ATOM   17234 C  CG   . ASP   C  3  70  ? -14.854 -43.709 -60.263  1.00 102.14 ? 70   ASP   C CG   1 
ATOM   17235 O  OD1  . ASP   C  3  70  ? -15.685 -43.801 -59.335  1.00 107.14 ? 70   ASP   C OD1  1 
ATOM   17236 O  OD2  . ASP   C  3  70  ? -14.862 -44.465 -61.257  1.00 105.78 ? 70   ASP   C OD2  1 
ATOM   17237 H  H    . ASP   C  3  70  ? -13.474 -42.468 -57.592  1.00 110.43 ? 70   ASP   C H    1 
ATOM   17238 H  HA   . ASP   C  3  70  ? -12.274 -43.891 -59.572  1.00 106.68 ? 70   ASP   C HA   1 
ATOM   17239 H  HB2  . ASP   C  3  70  ? -14.196 -41.829 -59.827  1.00 112.52 ? 70   ASP   C HB2  1 
ATOM   17240 H  HB3  . ASP   C  3  70  ? -13.447 -42.474 -61.072  1.00 112.52 ? 70   ASP   C HB3  1 
ATOM   17241 N  N    . TYR   C  3  71  ? -10.425 -42.385 -60.061  1.00 79.35  ? 71   TYR   C N    1 
ATOM   17242 C  CA   . TYR   C  3  71  ? -9.252  -41.537 -60.212  1.00 78.77  ? 71   TYR   C CA   1 
ATOM   17243 C  C    . TYR   C  3  71  ? -8.672  -41.748 -61.601  1.00 81.82  ? 71   TYR   C C    1 
ATOM   17244 O  O    . TYR   C  3  71  ? -8.922  -42.767 -62.250  1.00 89.05  ? 71   TYR   C O    1 
ATOM   17245 C  CB   . TYR   C  3  71  ? -8.200  -41.842 -59.139  1.00 73.17  ? 71   TYR   C CB   1 
ATOM   17246 C  CG   . TYR   C  3  71  ? -8.708  -41.660 -57.726  1.00 73.89  ? 71   TYR   C CG   1 
ATOM   17247 C  CD1  . TYR   C  3  71  ? -9.404  -42.674 -57.080  1.00 74.38  ? 71   TYR   C CD1  1 
ATOM   17248 C  CD2  . TYR   C  3  71  ? -8.493  -40.474 -57.040  1.00 76.78  ? 71   TYR   C CD2  1 
ATOM   17249 C  CE1  . TYR   C  3  71  ? -9.874  -42.510 -55.793  1.00 76.23  ? 71   TYR   C CE1  1 
ATOM   17250 C  CE2  . TYR   C  3  71  ? -8.956  -40.302 -55.751  1.00 79.02  ? 71   TYR   C CE2  1 
ATOM   17251 C  CZ   . TYR   C  3  71  ? -9.645  -41.323 -55.131  1.00 77.79  ? 71   TYR   C CZ   1 
ATOM   17252 O  OH   . TYR   C  3  71  ? -10.110 -41.156 -53.847  1.00 77.66  ? 71   TYR   C OH   1 
ATOM   17253 H  H    . TYR   C  3  71  ? -10.353 -43.142 -60.464  1.00 95.20  ? 71   TYR   C H    1 
ATOM   17254 H  HA   . TYR   C  3  71  ? -9.506  -40.604 -60.127  1.00 94.51  ? 71   TYR   C HA   1 
ATOM   17255 H  HB2  . TYR   C  3  71  ? -7.914  -42.764 -59.235  1.00 87.78  ? 71   TYR   C HB2  1 
ATOM   17256 H  HB3  . TYR   C  3  71  ? -7.445  -41.245 -59.262  1.00 87.78  ? 71   TYR   C HB3  1 
ATOM   17257 H  HD1  . TYR   C  3  71  ? -9.555  -43.478 -57.523  1.00 89.24  ? 71   TYR   C HD1  1 
ATOM   17258 H  HD2  . TYR   C  3  71  ? -8.030  -39.783 -57.455  1.00 92.12  ? 71   TYR   C HD2  1 
ATOM   17259 H  HE1  . TYR   C  3  71  ? -10.343 -43.196 -55.375  1.00 91.46  ? 71   TYR   C HE1  1 
ATOM   17260 H  HE2  . TYR   C  3  71  ? -8.805  -39.501 -55.303  1.00 94.80  ? 71   TYR   C HE2  1 
ATOM   17261 H  HH   . TYR   C  3  71  ? -10.641 -41.776 -53.651  1.00 93.18  ? 71   TYR   C HH   1 
ATOM   17262 N  N    . SER   C  3  72  ? -7.890  -40.772 -62.057  1.00 76.92  ? 72   SER   C N    1 
ATOM   17263 C  CA   . SER   C  3  72  ? -7.338  -40.832 -63.402  1.00 75.74  ? 72   SER   C CA   1 
ATOM   17264 C  C    . SER   C  3  72  ? -6.035  -40.051 -63.474  1.00 70.64  ? 72   SER   C C    1 
ATOM   17265 O  O    . SER   C  3  72  ? -5.894  -38.997 -62.849  1.00 70.27  ? 72   SER   C O    1 
ATOM   17266 C  CB   . SER   C  3  72  ? -8.329  -40.274 -64.431  1.00 84.03  ? 72   SER   C CB   1 
ATOM   17267 O  OG   . SER   C  3  72  ? -8.505  -38.878 -64.261  1.00 89.91  ? 72   SER   C OG   1 
ATOM   17268 H  H    . SER   C  3  72  ? -7.669  -40.073 -61.609  1.00 92.28  ? 72   SER   C H    1 
ATOM   17269 H  HA   . SER   C  3  72  ? -7.139  -41.757 -63.614  1.00 90.87  ? 72   SER   C HA   1 
ATOM   17270 H  HB2  . SER   C  3  72  ? -7.985  -40.443 -65.322  1.00 100.82 ? 72   SER   C HB2  1 
ATOM   17271 H  HB3  . SER   C  3  72  ? -9.184  -40.716 -64.316  1.00 100.82 ? 72   SER   C HB3  1 
ATOM   17272 H  HG   . SER   C  3  72  ? -8.474  -38.682 -63.445  1.00 107.87 ? 72   SER   C HG   1 
ATOM   17273 N  N    . LEU   C  3  73  ? -5.091  -40.583 -64.245  1.00 70.31  ? 73   LEU   C N    1 
ATOM   17274 C  CA   . LEU   C  3  73  ? -3.864  -39.891 -64.605  1.00 68.41  ? 73   LEU   C CA   1 
ATOM   17275 C  C    . LEU   C  3  73  ? -4.008  -39.316 -66.008  1.00 69.88  ? 73   LEU   C C    1 
ATOM   17276 O  O    . LEU   C  3  73  ? -4.683  -39.892 -66.865  1.00 74.62  ? 73   LEU   C O    1 
ATOM   17277 C  CB   . LEU   C  3  73  ? -2.663  -40.838 -64.551  1.00 65.85  ? 73   LEU   C CB   1 
ATOM   17278 C  CG   . LEU   C  3  73  ? -1.303  -40.267 -64.959  1.00 64.58  ? 73   LEU   C CG   1 
ATOM   17279 C  CD1  . LEU   C  3  73  ? -0.788  -39.292 -63.915  1.00 67.63  ? 73   LEU   C CD1  1 
ATOM   17280 C  CD2  . LEU   C  3  73  ? -0.306  -41.391 -65.183  1.00 61.20  ? 73   LEU   C CD2  1 
ATOM   17281 H  H    . LEU   C  3  73  ? -5.144  -41.372 -64.583  1.00 84.36  ? 73   LEU   C H    1 
ATOM   17282 H  HA   . LEU   C  3  73  ? -3.695  -39.168 -63.981  1.00 82.07  ? 73   LEU   C HA   1 
ATOM   17283 H  HB2  . LEU   C  3  73  ? -2.574  -41.154 -63.639  1.00 79.00  ? 73   LEU   C HB2  1 
ATOM   17284 H  HB3  . LEU   C  3  73  ? -2.845  -41.584 -65.144  1.00 79.00  ? 73   LEU   C HB3  1 
ATOM   17285 H  HG   . LEU   C  3  73  ? -1.404  -39.778 -65.791  1.00 77.48  ? 73   LEU   C HG   1 
ATOM   17286 H  HD11 . LEU   C  3  73  ? 0.080   -38.961 -64.193  1.00 81.13  ? 73   LEU   C HD11 1 
ATOM   17287 H  HD12 . LEU   C  3  73  ? -1.413  -38.555 -63.835  1.00 81.13  ? 73   LEU   C HD12 1 
ATOM   17288 H  HD13 . LEU   C  3  73  ? -0.708  -39.753 -63.065  1.00 81.13  ? 73   LEU   C HD13 1 
ATOM   17289 H  HD21 . LEU   C  3  73  ? 0.548   -41.010 -65.440  1.00 73.42  ? 73   LEU   C HD21 1 
ATOM   17290 H  HD22 . LEU   C  3  73  ? -0.209  -41.896 -64.360  1.00 73.42  ? 73   LEU   C HD22 1 
ATOM   17291 H  HD23 . LEU   C  3  73  ? -0.636  -41.970 -65.889  1.00 73.42  ? 73   LEU   C HD23 1 
ATOM   17292 N  N    . THR   C  3  74  ? -3.367  -38.174 -66.238  1.00 68.19  ? 74   THR   C N    1 
ATOM   17293 C  CA   . THR   C  3  74  ? -3.457  -37.481 -67.516  1.00 68.88  ? 74   THR   C CA   1 
ATOM   17294 C  C    . THR   C  3  74  ? -2.065  -37.085 -67.983  1.00 72.87  ? 74   THR   C C    1 
ATOM   17295 O  O    . THR   C  3  74  ? -1.315  -36.442 -67.241  1.00 72.74  ? 74   THR   C O    1 
ATOM   17296 C  CB   . THR   C  3  74  ? -4.355  -36.242 -67.410  1.00 67.70  ? 74   THR   C CB   1 
ATOM   17297 O  OG1  . THR   C  3  74  ? -5.660  -36.634 -66.965  1.00 69.84  ? 74   THR   C OG1  1 
ATOM   17298 C  CG2  . THR   C  3  74  ? -4.472  -35.546 -68.757  1.00 68.66  ? 74   THR   C CG2  1 
ATOM   17299 H  H    . THR   C  3  74  ? -2.867  -37.777 -65.662  1.00 81.81  ? 74   THR   C H    1 
ATOM   17300 H  HA   . THR   C  3  74  ? -3.834  -38.080 -68.180  1.00 82.64  ? 74   THR   C HA   1 
ATOM   17301 H  HB   . THR   C  3  74  ? -3.968  -35.618 -66.776  1.00 81.22  ? 74   THR   C HB   1 
ATOM   17302 H  HG1  . THR   C  3  74  ? -6.173  -35.968 -66.958  1.00 83.79  ? 74   THR   C HG1  1 
ATOM   17303 H  HG21 . THR   C  3  74  ? -5.108  -34.816 -68.700  1.00 82.37  ? 74   THR   C HG21 1 
ATOM   17304 H  HG22 . THR   C  3  74  ? -3.609  -35.192 -69.024  1.00 82.37  ? 74   THR   C HG22 1 
ATOM   17305 H  HG23 . THR   C  3  74  ? -4.775  -36.176 -69.431  1.00 82.37  ? 74   THR   C HG23 1 
ATOM   17306 N  N    . ILE   C  3  75  ? -1.727  -37.474 -69.208  1.00 76.78  ? 75   ILE   C N    1 
ATOM   17307 C  CA   . ILE   C  3  75  ? -0.471  -37.104 -69.847  1.00 79.44  ? 75   ILE   C CA   1 
ATOM   17308 C  C    . ILE   C  3  75  ? -0.829  -36.215 -71.031  1.00 81.12  ? 75   ILE   C C    1 
ATOM   17309 O  O    . ILE   C  3  75  ? -1.311  -36.700 -72.061  1.00 83.00  ? 75   ILE   C O    1 
ATOM   17310 C  CB   . ILE   C  3  75  ? 0.335   -38.326 -70.302  1.00 81.41  ? 75   ILE   C CB   1 
ATOM   17311 C  CG1  . ILE   C  3  75  ? 0.436   -39.365 -69.183  1.00 78.11  ? 75   ILE   C CG1  1 
ATOM   17312 C  CG2  . ILE   C  3  75  ? 1.726   -37.894 -70.758  1.00 83.36  ? 75   ILE   C CG2  1 
ATOM   17313 C  CD1  . ILE   C  3  75  ? 1.094   -40.664 -69.618  1.00 74.54  ? 75   ILE   C CD1  1 
ATOM   17314 H  H    . ILE   C  3  75  ? -2.226  -37.969 -69.704  1.00 92.12  ? 75   ILE   C H    1 
ATOM   17315 H  HA   . ILE   C  3  75  ? 0.068   -36.597 -69.219  1.00 95.30  ? 75   ILE   C HA   1 
ATOM   17316 H  HB   . ILE   C  3  75  ? -0.131  -38.735 -71.048  1.00 97.67  ? 75   ILE   C HB   1 
ATOM   17317 H  HG12 . ILE   C  3  75  ? 0.963   -38.994 -68.458  1.00 93.71  ? 75   ILE   C HG12 1 
ATOM   17318 H  HG13 . ILE   C  3  75  ? -0.457  -39.575 -68.870  1.00 93.71  ? 75   ILE   C HG13 1 
ATOM   17319 H  HG21 . ILE   C  3  75  ? 2.199   -38.667 -71.104  1.00 100.02 ? 75   ILE   C HG21 1 
ATOM   17320 H  HG22 . ILE   C  3  75  ? 1.637   -37.222 -71.452  1.00 100.02 ? 75   ILE   C HG22 1 
ATOM   17321 H  HG23 . ILE   C  3  75  ? 2.206   -37.525 -70.000  1.00 100.02 ? 75   ILE   C HG23 1 
ATOM   17322 H  HD11 . ILE   C  3  75  ? 1.051   -41.300 -68.887  1.00 89.42  ? 75   ILE   C HD11 1 
ATOM   17323 H  HD12 . ILE   C  3  75  ? 0.622   -41.014 -70.390  1.00 89.42  ? 75   ILE   C HD12 1 
ATOM   17324 H  HD13 . ILE   C  3  75  ? 2.020   -40.488 -69.848  1.00 89.42  ? 75   ILE   C HD13 1 
ATOM   17325 N  N    . SER   C  3  76  ? -0.609  -34.912 -70.889  1.00 83.48  ? 76   SER   C N    1 
ATOM   17326 C  CA   . SER   C  3  76  ? -0.775  -33.983 -71.996  1.00 89.50  ? 76   SER   C CA   1 
ATOM   17327 C  C    . SER   C  3  76  ? 0.540   -33.861 -72.753  1.00 94.15  ? 76   SER   C C    1 
ATOM   17328 O  O    . SER   C  3  76  ? 1.616   -33.835 -72.150  1.00 97.22  ? 76   SER   C O    1 
ATOM   17329 C  CB   . SER   C  3  76  ? -1.222  -32.610 -71.494  1.00 88.45  ? 76   SER   C CB   1 
ATOM   17330 O  OG   . SER   C  3  76  ? -0.235  -32.026 -70.664  1.00 86.80  ? 76   SER   C OG   1 
ATOM   17331 H  H    . SER   C  3  76  ? -0.361  -34.541 -70.154  1.00 100.16 ? 76   SER   C H    1 
ATOM   17332 H  HA   . SER   C  3  76  ? -1.458  -34.311 -72.602  1.00 107.38 ? 76   SER   C HA   1 
ATOM   17333 H  HB2  . SER   C  3  76  ? -1.375  -32.031 -72.257  1.00 106.12 ? 76   SER   C HB2  1 
ATOM   17334 H  HB3  . SER   C  3  76  ? -2.041  -32.713 -70.985  1.00 106.12 ? 76   SER   C HB3  1 
ATOM   17335 H  HG   . SER   C  3  76  ? -0.474  -31.254 -70.434  1.00 104.14 ? 76   SER   C HG   1 
ATOM   17336 N  N    . ASN   C  3  77  ? 0.450   -33.795 -74.080  1.00 94.62  ? 77   ASN   C N    1 
ATOM   17337 C  CA   . ASN   C  3  77  ? 1.627   -33.680 -74.937  1.00 93.60  ? 77   ASN   C CA   1 
ATOM   17338 C  C    . ASN   C  3  77  ? 2.591   -34.841 -74.683  1.00 90.31  ? 77   ASN   C C    1 
ATOM   17339 O  O    . ASN   C  3  77  ? 3.720   -34.666 -74.221  1.00 90.78  ? 77   ASN   C O    1 
ATOM   17340 C  CB   . ASN   C  3  77  ? 2.318   -32.329 -74.724  1.00 96.11  ? 77   ASN   C CB   1 
ATOM   17341 C  CG   . ASN   C  3  77  ? 1.332   -31.182 -74.622  1.00 103.27 ? 77   ASN   C CG   1 
ATOM   17342 O  OD1  . ASN   C  3  77  ? 0.878   -30.833 -73.531  1.00 105.97 ? 77   ASN   C OD1  1 
ATOM   17343 N  ND2  . ASN   C  3  77  ? 0.992   -30.589 -75.760  1.00 107.09 ? 77   ASN   C ND2  1 
ATOM   17344 H  H    . ASN   C  3  77  ? -0.293  -33.816 -74.513  1.00 113.52 ? 77   ASN   C H    1 
ATOM   17345 H  HA   . ASN   C  3  77  ? 1.346   -33.729 -75.864  1.00 112.31 ? 77   ASN   C HA   1 
ATOM   17346 H  HB2  . ASN   C  3  77  ? 2.829   -32.361 -73.900  1.00 115.31 ? 77   ASN   C HB2  1 
ATOM   17347 H  HB3  . ASN   C  3  77  ? 2.908   -32.153 -75.473  1.00 115.31 ? 77   ASN   C HB3  1 
ATOM   17348 H  HD21 . ASN   C  3  77  ? 0.436   -29.933 -75.754  1.00 128.49 ? 77   ASN   C HD21 1 
ATOM   17349 H  HD22 . ASN   C  3  77  ? 1.329   -30.861 -76.503  1.00 128.49 ? 77   ASN   C HD22 1 
ATOM   17350 N  N    . LEU   C  3  78  ? 2.111   -36.044 -74.990  1.00 88.17  ? 78   LEU   C N    1 
ATOM   17351 C  CA   . LEU   C  3  78  ? 2.873   -37.256 -74.719  1.00 82.33  ? 78   LEU   C CA   1 
ATOM   17352 C  C    . LEU   C  3  78  ? 4.238   -37.213 -75.398  1.00 80.74  ? 78   LEU   C C    1 
ATOM   17353 O  O    . LEU   C  3  78  ? 4.345   -36.926 -76.593  1.00 80.17  ? 78   LEU   C O    1 
ATOM   17354 C  CB   . LEU   C  3  78  ? 2.081   -38.475 -75.192  1.00 79.61  ? 78   LEU   C CB   1 
ATOM   17355 C  CG   . LEU   C  3  78  ? 2.744   -39.839 -75.009  1.00 75.19  ? 78   LEU   C CG   1 
ATOM   17356 C  CD1  . LEU   C  3  78  ? 1.731   -40.854 -74.507  1.00 72.26  ? 78   LEU   C CD1  1 
ATOM   17357 C  CD2  . LEU   C  3  78  ? 3.361   -40.308 -76.314  1.00 77.77  ? 78   LEU   C CD2  1 
ATOM   17358 H  H    . LEU   C  3  78  ? 1.346   -36.185 -75.357  1.00 105.78 ? 78   LEU   C H    1 
ATOM   17359 H  HA   . LEU   C  3  78  ? 3.024   -37.332 -73.764  1.00 98.78  ? 78   LEU   C HA   1 
ATOM   17360 H  HB2  . LEU   C  3  78  ? 1.244   -38.497 -74.700  1.00 95.52  ? 78   LEU   C HB2  1 
ATOM   17361 H  HB3  . LEU   C  3  78  ? 1.906   -38.369 -76.140  1.00 95.52  ? 78   LEU   C HB3  1 
ATOM   17362 H  HG   . LEU   C  3  78  ? 3.451   -39.764 -74.350  1.00 90.21  ? 78   LEU   C HG   1 
ATOM   17363 H  HD11 . LEU   C  3  78  ? 2.172   -41.711 -74.394  1.00 86.69  ? 78   LEU   C HD11 1 
ATOM   17364 H  HD12 . LEU   C  3  78  ? 1.375   -40.551 -73.657  1.00 86.69  ? 78   LEU   C HD12 1 
ATOM   17365 H  HD13 . LEU   C  3  78  ? 1.015   -40.934 -75.156  1.00 86.69  ? 78   LEU   C HD13 1 
ATOM   17366 H  HD21 . LEU   C  3  78  ? 3.763   -41.179 -76.178  1.00 93.31  ? 78   LEU   C HD21 1 
ATOM   17367 H  HD22 . LEU   C  3  78  ? 2.666   -40.366 -76.989  1.00 93.31  ? 78   LEU   C HD22 1 
ATOM   17368 H  HD23 . LEU   C  3  78  ? 4.037   -39.670 -76.590  1.00 93.31  ? 78   LEU   C HD23 1 
ATOM   17369 N  N    . ASP   C  3  79  ? 5.281   -37.504 -74.625  1.00 80.33  ? 79   ASP   C N    1 
ATOM   17370 C  CA   . ASP   C  3  79  ? 6.654   -37.532 -75.108  1.00 84.51  ? 79   ASP   C CA   1 
ATOM   17371 C  C    . ASP   C  3  79  ? 7.086   -38.968 -75.390  1.00 87.77  ? 79   ASP   C C    1 
ATOM   17372 O  O    . ASP   C  3  79  ? 6.470   -39.930 -74.928  1.00 87.40  ? 79   ASP   C O    1 
ATOM   17373 C  CB   . ASP   C  3  79  ? 7.594   -36.889 -74.083  1.00 83.96  ? 79   ASP   C CB   1 
ATOM   17374 C  CG   . ASP   C  3  79  ? 8.978   -36.628 -74.642  1.00 88.17  ? 79   ASP   C CG   1 
ATOM   17375 O  OD1  . ASP   C  3  79  ? 9.159   -35.604 -75.335  1.00 91.99  ? 79   ASP   C OD1  1 
ATOM   17376 O  OD2  . ASP   C  3  79  ? 9.885   -37.448 -74.392  1.00 87.29  ? 79   ASP   C OD2  1 
ATOM   17377 H  H    . ASP   C  3  79  ? 5.214   -37.696 -73.789  1.00 96.38  ? 79   ASP   C H    1 
ATOM   17378 H  HA   . ASP   C  3  79  ? 6.719   -37.028 -75.934  1.00 101.39 ? 79   ASP   C HA   1 
ATOM   17379 H  HB2  . ASP   C  3  79  ? 7.220   -36.040 -73.799  1.00 100.73 ? 79   ASP   C HB2  1 
ATOM   17380 H  HB3  . ASP   C  3  79  ? 7.685   -37.482 -73.321  1.00 100.73 ? 79   ASP   C HB3  1 
ATOM   17381 N  N    . GLN   C  3  80  ? 8.166   -39.103 -76.167  1.00 90.29  ? 80   GLN   C N    1 
ATOM   17382 C  CA   . GLN   C  3  80  ? 8.663   -40.434 -76.506  1.00 88.85  ? 80   GLN   C CA   1 
ATOM   17383 C  C    . GLN   C  3  80  ? 9.073   -41.211 -75.262  1.00 78.98  ? 80   GLN   C C    1 
ATOM   17384 O  O    . GLN   C  3  80  ? 8.908   -42.436 -75.214  1.00 72.65  ? 80   GLN   C O    1 
ATOM   17385 C  CB   . GLN   C  3  80  ? 9.841   -40.327 -77.477  1.00 98.07  ? 80   GLN   C CB   1 
ATOM   17386 C  CG   . GLN   C  3  80  ? 10.468  -41.665 -77.871  1.00 102.15 ? 80   GLN   C CG   1 
ATOM   17387 C  CD   . GLN   C  3  80  ? 9.545   -42.530 -78.707  1.00 103.26 ? 80   GLN   C CD   1 
ATOM   17388 O  OE1  . GLN   C  3  80  ? 8.561   -42.047 -79.268  1.00 104.57 ? 80   GLN   C OE1  1 
ATOM   17389 N  NE2  . GLN   C  3  80  ? 9.859   -43.819 -78.794  1.00 101.77 ? 80   GLN   C NE2  1 
ATOM   17390 H  H    . GLN   C  3  80  ? 8.618   -38.453 -76.502  1.00 108.33 ? 80   GLN   C H    1 
ATOM   17391 H  HA   . GLN   C  3  80  ? 7.954   -40.926 -76.949  1.00 106.60 ? 80   GLN   C HA   1 
ATOM   17392 H  HB2  . GLN   C  3  80  ? 9.531   -39.899 -78.291  1.00 117.66 ? 80   GLN   C HB2  1 
ATOM   17393 H  HB3  . GLN   C  3  80  ? 10.534  -39.789 -77.063  1.00 117.66 ? 80   GLN   C HB3  1 
ATOM   17394 H  HG2  . GLN   C  3  80  ? 11.271  -41.496 -78.389  1.00 122.56 ? 80   GLN   C HG2  1 
ATOM   17395 H  HG3  . GLN   C  3  80  ? 10.691  -42.157 -77.065  1.00 122.56 ? 80   GLN   C HG3  1 
ATOM   17396 H  HE21 . GLN   C  3  80  ? 10.554  -44.120 -78.388  1.00 122.11 ? 80   GLN   C HE21 1 
ATOM   17397 H  HE22 . GLN   C  3  80  ? 9.366   -44.351 -79.257  1.00 122.11 ? 80   GLN   C HE22 1 
ATOM   17398 N  N    . GLU   C  3  81  ? 9.611   -40.529 -74.252  1.00 78.91  ? 81   GLU   C N    1 
ATOM   17399 C  CA   . GLU   C  3  81  ? 10.007  -41.194 -73.017  1.00 78.66  ? 81   GLU   C CA   1 
ATOM   17400 C  C    . GLU   C  3  81  ? 8.822   -41.516 -72.117  1.00 72.90  ? 81   GLU   C C    1 
ATOM   17401 O  O    . GLU   C  3  81  ? 9.025   -42.058 -71.025  1.00 71.45  ? 81   GLU   C O    1 
ATOM   17402 C  CB   . GLU   C  3  81  ? 11.021  -40.331 -72.257  1.00 89.61  ? 81   GLU   C CB   1 
ATOM   17403 C  CG   . GLU   C  3  81  ? 10.436  -39.085 -71.613  1.00 103.08 ? 81   GLU   C CG   1 
ATOM   17404 C  CD   . GLU   C  3  81  ? 11.503  -38.161 -71.059  1.00 115.14 ? 81   GLU   C CD   1 
ATOM   17405 O  OE1  . GLU   C  3  81  ? 11.683  -37.058 -71.617  1.00 120.97 ? 81   GLU   C OE1  1 
ATOM   17406 O  OE2  . GLU   C  3  81  ? 12.166  -38.540 -70.070  1.00 117.58 ? 81   GLU   C OE2  1 
ATOM   17407 H  H    . GLU   C  3  81  ? 9.756   -39.682 -74.260  1.00 94.67  ? 81   GLU   C H    1 
ATOM   17408 H  HA   . GLU   C  3  81  ? 10.444  -42.030 -73.241  1.00 94.37  ? 81   GLU   C HA   1 
ATOM   17409 H  HB2  . GLU   C  3  81  ? 11.414  -40.868 -71.551  1.00 107.51 ? 81   GLU   C HB2  1 
ATOM   17410 H  HB3  . GLU   C  3  81  ? 11.709  -40.045 -72.877  1.00 107.51 ? 81   GLU   C HB3  1 
ATOM   17411 H  HG2  . GLU   C  3  81  ? 9.929   -38.593 -72.278  1.00 123.68 ? 81   GLU   C HG2  1 
ATOM   17412 H  HG3  . GLU   C  3  81  ? 9.857   -39.348 -70.881  1.00 123.68 ? 81   GLU   C HG3  1 
ATOM   17413 N  N    . ASP   C  3  82  ? 7.598   -41.199 -72.541  1.00 74.22  ? 82   ASP   C N    1 
ATOM   17414 C  CA   . ASP   C  3  82  ? 6.403   -41.533 -71.779  1.00 72.94  ? 82   ASP   C CA   1 
ATOM   17415 C  C    . ASP   C  3  82  ? 5.889   -42.938 -72.063  1.00 71.55  ? 82   ASP   C C    1 
ATOM   17416 O  O    . ASP   C  3  82  ? 5.033   -43.427 -71.318  1.00 71.06  ? 82   ASP   C O    1 
ATOM   17417 C  CB   . ASP   C  3  82  ? 5.285   -40.526 -72.073  1.00 76.36  ? 82   ASP   C CB   1 
ATOM   17418 C  CG   . ASP   C  3  82  ? 5.608   -39.132 -71.576  1.00 79.81  ? 82   ASP   C CG   1 
ATOM   17419 O  OD1  . ASP   C  3  82  ? 6.526   -38.990 -70.741  1.00 80.81  ? 82   ASP   C OD1  1 
ATOM   17420 O  OD2  . ASP   C  3  82  ? 4.936   -38.176 -72.017  1.00 83.12  ? 82   ASP   C OD2  1 
ATOM   17421 H  H    . ASP   C  3  82  ? 7.435   -40.785 -73.277  1.00 89.04  ? 82   ASP   C H    1 
ATOM   17422 H  HA   . ASP   C  3  82  ? 6.617   -41.475 -70.835  1.00 87.50  ? 82   ASP   C HA   1 
ATOM   17423 H  HB2  . ASP   C  3  82  ? 5.146   -40.479 -73.032  1.00 91.61  ? 82   ASP   C HB2  1 
ATOM   17424 H  HB3  . ASP   C  3  82  ? 4.471   -40.820 -71.635  1.00 91.61  ? 82   ASP   C HB3  1 
ATOM   17425 N  N    . ILE   C  3  83  ? 6.381   -43.595 -73.110  1.00 71.62  ? 83   ILE   C N    1 
ATOM   17426 C  CA   . ILE   C  3  83  ? 5.950   -44.954 -73.426  1.00 71.79  ? 83   ILE   C CA   1 
ATOM   17427 C  C    . ILE   C  3  83  ? 6.424   -45.861 -72.296  1.00 71.84  ? 83   ILE   C C    1 
ATOM   17428 O  O    . ILE   C  3  83  ? 7.626   -46.090 -72.131  1.00 71.40  ? 83   ILE   C O    1 
ATOM   17429 C  CB   . ILE   C  3  83  ? 6.486   -45.420 -74.783  1.00 74.65  ? 83   ILE   C CB   1 
ATOM   17430 C  CG1  . ILE   C  3  83  ? 5.666   -44.805 -75.920  1.00 79.49  ? 83   ILE   C CG1  1 
ATOM   17431 C  CG2  . ILE   C  3  83  ? 6.451   -46.942 -74.893  1.00 72.58  ? 83   ILE   C CG2  1 
ATOM   17432 C  CD1  . ILE   C  3  83  ? 5.901   -43.328 -76.130  1.00 82.47  ? 83   ILE   C CD1  1 
ATOM   17433 H  H    . ILE   C  3  83  ? 6.966   -43.275 -73.654  1.00 85.92  ? 83   ILE   C H    1 
ATOM   17434 H  HA   . ILE   C  3  83  ? 4.981   -44.985 -73.463  1.00 86.13  ? 83   ILE   C HA   1 
ATOM   17435 H  HB   . ILE   C  3  83  ? 7.407   -45.122 -74.853  1.00 89.56  ? 83   ILE   C HB   1 
ATOM   17436 H  HG12 . ILE   C  3  83  ? 5.894   -45.259 -76.747  1.00 95.37  ? 83   ILE   C HG12 1 
ATOM   17437 H  HG13 . ILE   C  3  83  ? 4.724   -44.928 -75.723  1.00 95.37  ? 83   ILE   C HG13 1 
ATOM   17438 H  HG21 . ILE   C  3  83  ? 6.629   -47.197 -75.812  1.00 87.08  ? 83   ILE   C HG21 1 
ATOM   17439 H  HG22 . ILE   C  3  83  ? 7.129   -47.317 -74.309  1.00 87.08  ? 83   ILE   C HG22 1 
ATOM   17440 H  HG23 . ILE   C  3  83  ? 5.573   -47.258 -74.626  1.00 87.08  ? 83   ILE   C HG23 1 
ATOM   17441 H  HD11 . ILE   C  3  83  ? 5.396   -43.034 -76.903  1.00 98.94  ? 83   ILE   C HD11 1 
ATOM   17442 H  HD12 . ILE   C  3  83  ? 5.608   -42.846 -75.340  1.00 98.94  ? 83   ILE   C HD12 1 
ATOM   17443 H  HD13 . ILE   C  3  83  ? 6.848   -43.177 -76.277  1.00 98.94  ? 83   ILE   C HD13 1 
ATOM   17444 N  N    . ALA   C  3  84  ? 5.481   -46.373 -71.516  1.00 72.74  ? 84   ALA   C N    1 
ATOM   17445 C  CA   . ALA   C  3  84  ? 5.786   -47.134 -70.312  1.00 70.07  ? 84   ALA   C CA   1 
ATOM   17446 C  C    . ALA   C  3  84  ? 4.469   -47.663 -69.758  1.00 68.72  ? 84   ALA   C C    1 
ATOM   17447 O  O    . ALA   C  3  84  ? 3.396   -47.420 -70.319  1.00 72.31  ? 84   ALA   C O    1 
ATOM   17448 C  CB   . ALA   C  3  84  ? 6.526   -46.272 -69.288  1.00 69.89  ? 84   ALA   C CB   1 
ATOM   17449 H  H    . ALA   C  3  84  ? 4.639   -46.292 -71.667  1.00 87.27  ? 84   ALA   C H    1 
ATOM   17450 H  HA   . ALA   C  3  84  ? 6.348   -47.892 -70.537  1.00 84.06  ? 84   ALA   C HA   1 
ATOM   17451 H  HB1  . ALA   C  3  84  ? 6.659   -46.787 -68.478  1.00 83.85  ? 84   ALA   C HB1  1 
ATOM   17452 H  HB2  . ALA   C  3  84  ? 7.383   -46.009 -69.658  1.00 83.85  ? 84   ALA   C HB2  1 
ATOM   17453 H  HB3  . ALA   C  3  84  ? 5.993   -45.484 -69.095  1.00 83.85  ? 84   ALA   C HB3  1 
ATOM   17454 N  N    . THR   C  3  85  ? 4.561   -48.398 -68.656  1.00 66.13  ? 85   THR   C N    1 
ATOM   17455 C  CA   . THR   C  3  85  ? 3.392   -48.891 -67.943  1.00 66.11  ? 85   THR   C CA   1 
ATOM   17456 C  C    . THR   C  3  85  ? 3.141   -48.008 -66.727  1.00 65.39  ? 85   THR   C C    1 
ATOM   17457 O  O    . THR   C  3  85  ? 4.083   -47.559 -66.068  1.00 64.56  ? 85   THR   C O    1 
ATOM   17458 C  CB   . THR   C  3  85  ? 3.588   -50.345 -67.512  1.00 66.04  ? 85   THR   C CB   1 
ATOM   17459 O  OG1  . THR   C  3  85  ? 3.971   -51.133 -68.647  1.00 67.20  ? 85   THR   C OG1  1 
ATOM   17460 C  CG2  . THR   C  3  85  ? 2.304   -50.910 -66.921  1.00 67.75  ? 85   THR   C CG2  1 
ATOM   17461 H  H    . THR   C  3  85  ? 5.306   -48.628 -68.295  1.00 79.34  ? 85   THR   C H    1 
ATOM   17462 H  HA   . THR   C  3  85  ? 2.612   -48.858 -68.518  1.00 79.31  ? 85   THR   C HA   1 
ATOM   17463 H  HB   . THR   C  3  85  ? 4.281   -50.390 -66.834  1.00 79.23  ? 85   THR   C HB   1 
ATOM   17464 H  HG1  . THR   C  3  85  ? 4.105   -51.928 -68.413  1.00 80.63  ? 85   THR   C HG1  1 
ATOM   17465 H  HG21 . THR   C  3  85  ? 2.443   -51.827 -66.639  1.00 81.28  ? 85   THR   C HG21 1 
ATOM   17466 H  HG22 . THR   C  3  85  ? 2.031   -50.382 -66.154  1.00 81.28  ? 85   THR   C HG22 1 
ATOM   17467 H  HG23 . THR   C  3  85  ? 1.596   -50.889 -67.585  1.00 81.28  ? 85   THR   C HG23 1 
ATOM   17468 N  N    . TYR   C  3  86  ? 1.867   -47.756 -66.439  1.00 65.68  ? 86   TYR   C N    1 
ATOM   17469 C  CA   . TYR   C  3  86  ? 1.469   -46.847 -65.373  1.00 65.49  ? 86   TYR   C CA   1 
ATOM   17470 C  C    . TYR   C  3  86  ? 0.575   -47.577 -64.382  1.00 69.08  ? 86   TYR   C C    1 
ATOM   17471 O  O    . TYR   C  3  86  ? -0.440  -48.166 -64.768  1.00 69.93  ? 86   TYR   C O    1 
ATOM   17472 C  CB   . TYR   C  3  86  ? 0.760   -45.618 -65.950  1.00 63.21  ? 86   TYR   C CB   1 
ATOM   17473 C  CG   . TYR   C  3  86  ? 1.674   -44.757 -66.794  1.00 66.17  ? 86   TYR   C CG   1 
ATOM   17474 C  CD1  . TYR   C  3  86  ? 1.901   -45.054 -68.132  1.00 68.38  ? 86   TYR   C CD1  1 
ATOM   17475 C  CD2  . TYR   C  3  86  ? 2.322   -43.655 -66.250  1.00 65.96  ? 86   TYR   C CD2  1 
ATOM   17476 C  CE1  . TYR   C  3  86  ? 2.741   -44.275 -68.905  1.00 68.34  ? 86   TYR   C CE1  1 
ATOM   17477 C  CE2  . TYR   C  3  86  ? 3.163   -42.870 -67.017  1.00 64.88  ? 86   TYR   C CE2  1 
ATOM   17478 C  CZ   . TYR   C  3  86  ? 3.368   -43.184 -68.342  1.00 66.40  ? 86   TYR   C CZ   1 
ATOM   17479 O  OH   . TYR   C  3  86  ? 4.205   -42.405 -69.106  1.00 64.50  ? 86   TYR   C OH   1 
ATOM   17480 H  H    . TYR   C  3  86  ? 1.203   -48.109 -66.856  1.00 78.80  ? 86   TYR   C H    1 
ATOM   17481 H  HA   . TYR   C  3  86  ? 2.253   -46.546 -64.887  1.00 78.57  ? 86   TYR   C HA   1 
ATOM   17482 H  HB2  . TYR   C  3  86  ? 0.023   -45.912 -66.508  1.00 75.84  ? 86   TYR   C HB2  1 
ATOM   17483 H  HB3  . TYR   C  3  86  ? 0.425   -45.075 -65.219  1.00 75.84  ? 86   TYR   C HB3  1 
ATOM   17484 H  HD1  . TYR   C  3  86  ? 1.480   -45.790 -68.514  1.00 82.04  ? 86   TYR   C HD1  1 
ATOM   17485 H  HD2  . TYR   C  3  86  ? 2.188   -43.442 -65.355  1.00 79.14  ? 86   TYR   C HD2  1 
ATOM   17486 H  HE1  . TYR   C  3  86  ? 2.882   -44.486 -69.800  1.00 81.99  ? 86   TYR   C HE1  1 
ATOM   17487 H  HE2  . TYR   C  3  86  ? 3.588   -42.134 -66.639  1.00 77.84  ? 86   TYR   C HE2  1 
ATOM   17488 H  HH   . TYR   C  3  86  ? 4.380   -42.795 -69.830  1.00 77.38  ? 86   TYR   C HH   1 
ATOM   17489 N  N    . PHE   C  3  87  ? 0.963   -47.539 -63.109  1.00 67.67  ? 87   PHE   C N    1 
ATOM   17490 C  CA   . PHE   C  3  87  ? 0.244   -48.198 -62.031  1.00 67.26  ? 87   PHE   C CA   1 
ATOM   17491 C  C    . PHE   C  3  87  ? -0.326  -47.162 -61.074  1.00 67.55  ? 87   PHE   C C    1 
ATOM   17492 O  O    . PHE   C  3  87  ? 0.334   -46.165 -60.761  1.00 64.91  ? 87   PHE   C O    1 
ATOM   17493 C  CB   . PHE   C  3  87  ? 1.161   -49.144 -61.249  1.00 64.84  ? 87   PHE   C CB   1 
ATOM   17494 C  CG   . PHE   C  3  87  ? 1.638   -50.327 -62.037  1.00 66.52  ? 87   PHE   C CG   1 
ATOM   17495 C  CD1  . PHE   C  3  87  ? 0.889   -51.490 -62.083  1.00 71.85  ? 87   PHE   C CD1  1 
ATOM   17496 C  CD2  . PHE   C  3  87  ? 2.842   -50.282 -62.719  1.00 64.84  ? 87   PHE   C CD2  1 
ATOM   17497 C  CE1  . PHE   C  3  87  ? 1.326   -52.584 -62.802  1.00 73.86  ? 87   PHE   C CE1  1 
ATOM   17498 C  CE2  . PHE   C  3  87  ? 3.285   -51.375 -63.440  1.00 67.97  ? 87   PHE   C CE2  1 
ATOM   17499 C  CZ   . PHE   C  3  87  ? 2.525   -52.528 -63.481  1.00 71.26  ? 87   PHE   C CZ   1 
ATOM   17500 H  H    . PHE   C  3  87  ? 1.665   -47.121 -62.840  1.00 81.19  ? 87   PHE   C H    1 
ATOM   17501 H  HA   . PHE   C  3  87  ? -0.487  -48.713 -62.410  1.00 80.69  ? 87   PHE   C HA   1 
ATOM   17502 H  HB2  . PHE   C  3  87  ? 1.943   -48.648 -60.959  1.00 77.79  ? 87   PHE   C HB2  1 
ATOM   17503 H  HB3  . PHE   C  3  87  ? 0.676   -49.479 -60.478  1.00 77.79  ? 87   PHE   C HB3  1 
ATOM   17504 H  HD1  . PHE   C  3  87  ? 0.081   -51.534 -61.623  1.00 86.20  ? 87   PHE   C HD1  1 
ATOM   17505 H  HD2  . PHE   C  3  87  ? 3.358   -49.509 -62.691  1.00 77.78  ? 87   PHE   C HD2  1 
ATOM   17506 H  HE1  . PHE   C  3  87  ? 0.812   -53.359 -62.828  1.00 88.62  ? 87   PHE   C HE1  1 
ATOM   17507 H  HE2  . PHE   C  3  87  ? 4.094   -51.333 -63.897  1.00 81.55  ? 87   PHE   C HE2  1 
ATOM   17508 H  HZ   . PHE   C  3  87  ? 2.821   -53.264 -63.966  1.00 85.49  ? 87   PHE   C HZ   1 
ATOM   17509 N  N    . CYS   C  3  88  ? -1.549  -47.401 -60.609  1.00 69.24  ? 88   CYS   C N    1 
ATOM   17510 C  CA   . CYS   C  3  88  ? -2.121  -46.642 -59.508  1.00 69.88  ? 88   CYS   C CA   1 
ATOM   17511 C  C    . CYS   C  3  88  ? -2.008  -47.446 -58.218  1.00 72.23  ? 88   CYS   C C    1 
ATOM   17512 O  O    . CYS   C  3  88  ? -1.929  -48.678 -58.232  1.00 74.37  ? 88   CYS   C O    1 
ATOM   17513 C  CB   . CYS   C  3  88  ? -3.583  -46.269 -59.778  1.00 71.21  ? 88   CYS   C CB   1 
ATOM   17514 S  SG   . CYS   C  3  88  ? -4.710  -47.638 -60.171  1.00 76.45  ? 88   CYS   C SG   1 
ATOM   17515 H  H    . CYS   C  3  88  ? -2.072  -48.007 -60.922  1.00 83.07  ? 88   CYS   C H    1 
ATOM   17516 H  HA   . CYS   C  3  88  ? -1.631  -45.811 -59.401  1.00 83.83  ? 88   CYS   C HA   1 
ATOM   17517 H  HB2  . CYS   C  3  88  ? -3.933  -45.832 -58.986  1.00 85.43  ? 88   CYS   C HB2  1 
ATOM   17518 H  HB3  . CYS   C  3  88  ? -3.604  -45.658 -60.531  1.00 85.43  ? 88   CYS   C HB3  1 
ATOM   17519 N  N    . GLN   C  3  89  ? -1.987  -46.732 -57.097  1.00 73.84  ? 89   GLN   C N    1 
ATOM   17520 C  CA   . GLN   C  3  89  ? -1.784  -47.365 -55.798  1.00 72.36  ? 89   GLN   C CA   1 
ATOM   17521 C  C    . GLN   C  3  89  ? -2.524  -46.570 -54.737  1.00 71.89  ? 89   GLN   C C    1 
ATOM   17522 O  O    . GLN   C  3  89  ? -2.298  -45.364 -54.595  1.00 71.80  ? 89   GLN   C O    1 
ATOM   17523 C  CB   . GLN   C  3  89  ? -0.292  -47.455 -55.465  1.00 68.50  ? 89   GLN   C CB   1 
ATOM   17524 C  CG   . GLN   C  3  89  ? 0.009   -47.907 -54.040  1.00 65.49  ? 89   GLN   C CG   1 
ATOM   17525 C  CD   . GLN   C  3  89  ? 0.571   -46.791 -53.178  1.00 60.86  ? 89   GLN   C CD   1 
ATOM   17526 O  OE1  . GLN   C  3  89  ? 1.273   -45.906 -53.667  1.00 60.77  ? 89   GLN   C OE1  1 
ATOM   17527 N  NE2  . GLN   C  3  89  ? 0.261   -46.827 -51.888  1.00 60.60  ? 89   GLN   C NE2  1 
ATOM   17528 H  H    . GLN   C  3  89  ? -2.088  -45.879 -57.061  1.00 88.59  ? 89   GLN   C H    1 
ATOM   17529 H  HA   . GLN   C  3  89  ? -2.156  -48.261 -55.816  1.00 86.81  ? 89   GLN   C HA   1 
ATOM   17530 H  HB2  . GLN   C  3  89  ? 0.122   -48.091 -56.069  1.00 82.18  ? 89   GLN   C HB2  1 
ATOM   17531 H  HB3  . GLN   C  3  89  ? 0.104   -46.578 -55.584  1.00 82.18  ? 89   GLN   C HB3  1 
ATOM   17532 H  HG2  . GLN   C  3  89  ? -0.810  -48.222 -53.628  1.00 78.57  ? 89   GLN   C HG2  1 
ATOM   17533 H  HG3  . GLN   C  3  89  ? 0.663   -48.623 -54.068  1.00 78.57  ? 89   GLN   C HG3  1 
ATOM   17534 H  HE21 . GLN   C  3  89  ? -0.234  -47.461 -51.582  1.00 72.70  ? 89   GLN   C HE21 1 
ATOM   17535 H  HE22 . GLN   C  3  89  ? 0.554   -46.217 -51.358  1.00 72.70  ? 89   GLN   C HE22 1 
ATOM   17536 N  N    . GLN   C  3  90  ? -3.400  -47.243 -53.998  1.00 72.10  ? 90   GLN   C N    1 
ATOM   17537 C  CA   . GLN   C  3  90  ? -4.077  -46.618 -52.873  1.00 72.24  ? 90   GLN   C CA   1 
ATOM   17538 C  C    . GLN   C  3  90  ? -3.188  -46.685 -51.639  1.00 69.63  ? 90   GLN   C C    1 
ATOM   17539 O  O    . GLN   C  3  90  ? -2.501  -47.683 -51.403  1.00 65.01  ? 90   GLN   C O    1 
ATOM   17540 C  CB   . GLN   C  3  90  ? -5.417  -47.303 -52.601  1.00 73.79  ? 90   GLN   C CB   1 
ATOM   17541 C  CG   . GLN   C  3  90  ? -5.308  -48.720 -52.050  1.00 74.15  ? 90   GLN   C CG   1 
ATOM   17542 C  CD   . GLN   C  3  90  ? -5.246  -48.766 -50.533  1.00 71.97  ? 90   GLN   C CD   1 
ATOM   17543 O  OE1  . GLN   C  3  90  ? -5.455  -47.758 -49.859  1.00 70.69  ? 90   GLN   C OE1  1 
ATOM   17544 N  NE2  . GLN   C  3  90  ? -4.957  -49.943 -49.990  1.00 72.61  ? 90   GLN   C NE2  1 
ATOM   17545 H  H    . GLN   C  3  90  ? -3.619  -48.064 -54.130  1.00 86.50  ? 90   GLN   C H    1 
ATOM   17546 H  HA   . GLN   C  3  90  ? -4.260  -45.687 -53.074  1.00 86.67  ? 90   GLN   C HA   1 
ATOM   17547 H  HB2  . GLN   C  3  90  ? -5.907  -46.774 -51.952  1.00 88.53  ? 90   GLN   C HB2  1 
ATOM   17548 H  HB3  . GLN   C  3  90  ? -5.913  -47.350 -53.433  1.00 88.53  ? 90   GLN   C HB3  1 
ATOM   17549 H  HG2  . GLN   C  3  90  ? -6.085  -49.228 -52.333  1.00 88.96  ? 90   GLN   C HG2  1 
ATOM   17550 H  HG3  . GLN   C  3  90  ? -4.500  -49.131 -52.395  1.00 88.96  ? 90   GLN   C HG3  1 
ATOM   17551 H  HE21 . GLN   C  3  90  ? -4.817  -50.626 -50.493  1.00 87.11  ? 90   GLN   C HE21 1 
ATOM   17552 H  HE22 . GLN   C  3  90  ? -4.910  -50.022 -49.135  1.00 87.11  ? 90   GLN   C HE22 1 
ATOM   17553 N  N    . GLY   C  3  91  ? -3.198  -45.610 -50.857  1.00 69.12  ? 91   GLY   C N    1 
ATOM   17554 C  CA   . GLY   C  3  91  ? -2.400  -45.547 -49.650  1.00 66.25  ? 91   GLY   C CA   1 
ATOM   17555 C  C    . GLY   C  3  91  ? -3.226  -45.197 -48.431  1.00 67.43  ? 91   GLY   C C    1 
ATOM   17556 O  O    . GLY   C  3  91  ? -2.686  -44.803 -47.393  1.00 69.03  ? 91   GLY   C O    1 
ATOM   17557 H  H    . GLY   C  3  91  ? -3.664  -44.902 -51.008  1.00 82.93  ? 91   GLY   C H    1 
ATOM   17558 H  HA2  . GLY   C  3  91  ? -1.979  -46.407 -49.498  1.00 79.48  ? 91   GLY   C HA2  1 
ATOM   17559 H  HA3  . GLY   C  3  91  ? -1.711  -44.872 -49.755  1.00 79.48  ? 91   GLY   C HA3  1 
ATOM   17560 N  N    . ASN   C  3  92  ? -4.547  -45.347 -48.545  1.00 69.27  ? 92   ASN   C N    1 
ATOM   17561 C  CA   . ASN   C  3  92  ? -5.436  -44.970 -47.455  1.00 71.54  ? 92   ASN   C CA   1 
ATOM   17562 C  C    . ASN   C  3  92  ? -5.461  -46.010 -46.343  1.00 70.50  ? 92   ASN   C C    1 
ATOM   17563 O  O    . ASN   C  3  92  ? -5.762  -45.671 -45.194  1.00 73.49  ? 92   ASN   C O    1 
ATOM   17564 C  CB   . ASN   C  3  92  ? -6.854  -44.754 -47.987  1.00 75.18  ? 92   ASN   C CB   1 
ATOM   17565 C  CG   . ASN   C  3  92  ? -7.785  -44.174 -46.942  1.00 82.28  ? 92   ASN   C CG   1 
ATOM   17566 O  OD1  . ASN   C  3  92  ? -7.364  -43.403 -46.080  1.00 84.24  ? 92   ASN   C OD1  1 
ATOM   17567 N  ND2  . ASN   C  3  92  ? -9.057  -44.546 -47.010  1.00 89.62  ? 92   ASN   C ND2  1 
ATOM   17568 H  H    . ASN   C  3  92  ? -4.946  -45.662 -49.239  1.00 83.11  ? 92   ASN   C H    1 
ATOM   17569 H  HA   . ASN   C  3  92  ? -5.120  -44.134 -47.077  1.00 85.83  ? 92   ASN   C HA   1 
ATOM   17570 H  HB2  . ASN   C  3  92  ? -6.821  -44.138 -48.735  1.00 90.20  ? 92   ASN   C HB2  1 
ATOM   17571 H  HB3  . ASN   C  3  92  ? -7.218  -45.606 -48.274  1.00 90.20  ? 92   ASN   C HB3  1 
ATOM   17572 H  HD21 . ASN   C  3  92  ? -9.625  -44.244 -46.439  1.00 107.52 ? 92   ASN   C HD21 1 
ATOM   17573 H  HD22 . ASN   C  3  92  ? -9.314  -45.090 -47.625  1.00 107.52 ? 92   ASN   C HD22 1 
ATOM   17574 N  N    . THR   C  3  93  ? -5.153  -47.267 -46.654  1.00 67.87  ? 93   THR   C N    1 
ATOM   17575 C  CA   . THR   C  3  93  ? -5.239  -48.324 -45.658  1.00 70.92  ? 93   THR   C CA   1 
ATOM   17576 C  C    . THR   C  3  93  ? -4.312  -49.465 -46.048  1.00 67.87  ? 93   THR   C C    1 
ATOM   17577 O  O    . THR   C  3  93  ? -4.112  -49.744 -47.233  1.00 61.75  ? 93   THR   C O    1 
ATOM   17578 C  CB   . THR   C  3  93  ? -6.678  -48.838 -45.514  1.00 76.13  ? 93   THR   C CB   1 
ATOM   17579 O  OG1  . THR   C  3  93  ? -6.695  -49.997 -44.672  1.00 80.75  ? 93   THR   C OG1  1 
ATOM   17580 C  CG2  . THR   C  3  93  ? -7.268  -49.189 -46.880  1.00 76.29  ? 93   THR   C CG2  1 
ATOM   17581 H  H    . THR   C  3  93  ? -4.894  -47.528 -47.431  1.00 81.43  ? 93   THR   C H    1 
ATOM   17582 H  HA   . THR   C  3  93  ? -4.943  -47.978 -44.802  1.00 85.09  ? 93   THR   C HA   1 
ATOM   17583 H  HB   . THR   C  3  93  ? -7.228  -48.145 -45.118  1.00 91.34  ? 93   THR   C HB   1 
ATOM   17584 H  HG1  . THR   C  3  93  ? -7.485  -50.265 -44.568  1.00 96.88  ? 93   THR   C HG1  1 
ATOM   17585 H  HG21 . THR   C  3  93  ? -8.172  -49.524 -46.775  1.00 91.53  ? 93   THR   C HG21 1 
ATOM   17586 H  HG22 . THR   C  3  93  ? -7.288  -48.401 -47.445  1.00 91.53  ? 93   THR   C HG22 1 
ATOM   17587 H  HG23 . THR   C  3  93  ? -6.728  -49.871 -47.310  1.00 91.53  ? 93   THR   C HG23 1 
ATOM   17588 N  N    . PHE   C  3  94  ? -3.751  -50.119 -45.034  1.00 70.60  ? 94   PHE   C N    1 
ATOM   17589 C  CA   . PHE   C  3  94  ? -2.914  -51.282 -45.273  1.00 71.39  ? 94   PHE   C CA   1 
ATOM   17590 C  C    . PHE   C  3  94  ? -3.781  -52.520 -45.499  1.00 72.68  ? 94   PHE   C C    1 
ATOM   17591 O  O    . PHE   C  3  94  ? -4.856  -52.651 -44.907  1.00 74.64  ? 94   PHE   C O    1 
ATOM   17592 C  CB   . PHE   C  3  94  ? -1.981  -51.523 -44.092  1.00 74.74  ? 94   PHE   C CB   1 
ATOM   17593 C  CG   . PHE   C  3  94  ? -0.860  -50.526 -43.981  1.00 78.07  ? 94   PHE   C CG   1 
ATOM   17594 C  CD1  . PHE   C  3  94  ? -0.117  -50.161 -45.094  1.00 77.58  ? 94   PHE   C CD1  1 
ATOM   17595 C  CD2  . PHE   C  3  94  ? -0.545  -49.958 -42.759  1.00 80.03  ? 94   PHE   C CD2  1 
ATOM   17596 C  CE1  . PHE   C  3  94  ? 0.915   -49.247 -44.989  1.00 73.90  ? 94   PHE   C CE1  1 
ATOM   17597 C  CE2  . PHE   C  3  94  ? 0.485   -49.044 -42.648  1.00 77.81  ? 94   PHE   C CE2  1 
ATOM   17598 C  CZ   . PHE   C  3  94  ? 1.216   -48.688 -43.765  1.00 74.98  ? 94   PHE   C CZ   1 
ATOM   17599 H  H    . PHE   C  3  94  ? -3.840  -49.908 -44.205  1.00 84.70  ? 94   PHE   C H    1 
ATOM   17600 H  HA   . PHE   C  3  94  ? -2.371  -51.134 -46.063  1.00 85.65  ? 94   PHE   C HA   1 
ATOM   17601 H  HB2  . PHE   C  3  94  ? -2.498  -51.477 -43.272  1.00 89.67  ? 94   PHE   C HB2  1 
ATOM   17602 H  HB3  . PHE   C  3  94  ? -1.584  -52.403 -44.184  1.00 89.67  ? 94   PHE   C HB3  1 
ATOM   17603 H  HD1  . PHE   C  3  94  ? -0.316  -50.535 -45.922  1.00 93.07  ? 94   PHE   C HD1  1 
ATOM   17604 H  HD2  . PHE   C  3  94  ? -1.033  -50.195 -42.003  1.00 96.02  ? 94   PHE   C HD2  1 
ATOM   17605 H  HE1  . PHE   C  3  94  ? 1.405   -49.010 -45.743  1.00 88.66  ? 94   PHE   C HE1  1 
ATOM   17606 H  HE2  . PHE   C  3  94  ? 0.686   -48.668 -41.821  1.00 93.36  ? 94   PHE   C HE2  1 
ATOM   17607 H  HZ   . PHE   C  3  94  ? 1.909   -48.073 -43.692  1.00 89.96  ? 94   PHE   C HZ   1 
ATOM   17608 N  N    . PRO   C  3  95  ? -3.333  -53.453 -46.355  1.00 72.39  ? 95   PRO   C N    1 
ATOM   17609 C  CA   . PRO   C  3  95  ? -2.086  -53.378 -47.127  1.00 72.04  ? 95   PRO   C CA   1 
ATOM   17610 C  C    . PRO   C  3  95  ? -2.210  -52.482 -48.357  1.00 68.07  ? 95   PRO   C C    1 
ATOM   17611 O  O    . PRO   C  3  95  ? -3.288  -52.406 -48.945  1.00 66.77  ? 95   PRO   C O    1 
ATOM   17612 C  CB   . PRO   C  3  95  ? -1.847  -54.833 -47.534  1.00 74.40  ? 95   PRO   C CB   1 
ATOM   17613 C  CG   . PRO   C  3  95  ? -3.214  -55.412 -47.636  1.00 76.06  ? 95   PRO   C CG   1 
ATOM   17614 C  CD   . PRO   C  3  95  ? -4.041  -54.727 -46.577  1.00 76.05  ? 95   PRO   C CD   1 
ATOM   17615 H  HA   . PRO   C  3  95  ? -1.352  -53.067 -46.576  1.00 86.43  ? 95   PRO   C HA   1 
ATOM   17616 H  HB2  . PRO   C  3  95  ? -1.386  -54.869 -48.387  1.00 89.26  ? 95   PRO   C HB2  1 
ATOM   17617 H  HB3  . PRO   C  3  95  ? -1.323  -55.287 -46.855  1.00 89.26  ? 95   PRO   C HB3  1 
ATOM   17618 H  HG2  . PRO   C  3  95  ? -3.576  -55.239 -48.519  1.00 91.26  ? 95   PRO   C HG2  1 
ATOM   17619 H  HG3  . PRO   C  3  95  ? -3.175  -56.368 -47.475  1.00 91.26  ? 95   PRO   C HG3  1 
ATOM   17620 H  HD2  . PRO   C  3  95  ? -4.943  -54.568 -46.896  1.00 91.24  ? 95   PRO   C HD2  1 
ATOM   17621 H  HD3  . PRO   C  3  95  ? -4.064  -55.254 -45.764  1.00 91.24  ? 95   PRO   C HD3  1 
ATOM   17622 N  N    . TYR   C  3  96  ? -1.125  -51.805 -48.731  1.00 66.27  ? 96   TYR   C N    1 
ATOM   17623 C  CA   . TYR   C  3  96  ? -1.126  -51.021 -49.960  1.00 68.16  ? 96   TYR   C CA   1 
ATOM   17624 C  C    . TYR   C  3  96  ? -1.332  -51.945 -51.155  1.00 70.72  ? 96   TYR   C C    1 
ATOM   17625 O  O    . TYR   C  3  96  ? -0.659  -52.970 -51.284  1.00 74.00  ? 96   TYR   C O    1 
ATOM   17626 C  CB   . TYR   C  3  96  ? 0.189   -50.252 -50.112  1.00 67.08  ? 96   TYR   C CB   1 
ATOM   17627 C  CG   . TYR   C  3  96  ? 0.370   -49.068 -49.177  1.00 67.82  ? 96   TYR   C CG   1 
ATOM   17628 C  CD1  . TYR   C  3  96  ? -0.671  -48.605 -48.383  1.00 71.43  ? 96   TYR   C CD1  1 
ATOM   17629 C  CD2  . TYR   C  3  96  ? 1.591   -48.408 -49.101  1.00 67.08  ? 96   TYR   C CD2  1 
ATOM   17630 C  CE1  . TYR   C  3  96  ? -0.500  -47.524 -47.536  1.00 70.84  ? 96   TYR   C CE1  1 
ATOM   17631 C  CE2  . TYR   C  3  96  ? 1.770   -47.327 -48.258  1.00 66.90  ? 96   TYR   C CE2  1 
ATOM   17632 C  CZ   . TYR   C  3  96  ? 0.722   -46.889 -47.479  1.00 68.33  ? 96   TYR   C CZ   1 
ATOM   17633 O  OH   . TYR   C  3  96  ? 0.899   -45.813 -46.640  1.00 67.84  ? 96   TYR   C OH   1 
ATOM   17634 H  H    . TYR   C  3  96  ? -0.384  -51.784 -48.294  1.00 79.50  ? 96   TYR   C H    1 
ATOM   17635 H  HA   . TYR   C  3  96  ? -1.846  -50.372 -49.928  1.00 81.77  ? 96   TYR   C HA   1 
ATOM   17636 H  HB2  . TYR   C  3  96  ? 0.922   -50.865 -49.944  1.00 80.47  ? 96   TYR   C HB2  1 
ATOM   17637 H  HB3  . TYR   C  3  96  ? 0.241   -49.913 -51.019  1.00 80.47  ? 96   TYR   C HB3  1 
ATOM   17638 H  HD1  . TYR   C  3  96  ? -1.498  -49.029 -48.421  1.00 85.69  ? 96   TYR   C HD1  1 
ATOM   17639 H  HD2  . TYR   C  3  96  ? 2.301   -48.699 -49.627  1.00 80.47  ? 96   TYR   C HD2  1 
ATOM   17640 H  HE1  . TYR   C  3  96  ? -1.205  -47.227 -47.008  1.00 84.99  ? 96   TYR   C HE1  1 
ATOM   17641 H  HE2  . TYR   C  3  96  ? 2.594   -46.897 -48.217  1.00 80.26  ? 96   TYR   C HE2  1 
ATOM   17642 H  HH   . TYR   C  3  96  ? 0.167   -45.602 -46.285  1.00 81.39  ? 96   TYR   C HH   1 
ATOM   17643 N  N    . THR   C  3  97  ? -2.268  -51.582 -52.027  1.00 70.94  ? 97   THR   C N    1 
ATOM   17644 C  CA   . THR   C  3  97  ? -2.597  -52.376 -53.201  1.00 72.79  ? 97   THR   C CA   1 
ATOM   17645 C  C    . THR   C  3  97  ? -2.421  -51.539 -54.460  1.00 72.04  ? 97   THR   C C    1 
ATOM   17646 O  O    . THR   C  3  97  ? -2.639  -50.323 -54.452  1.00 71.48  ? 97   THR   C O    1 
ATOM   17647 C  CB   . THR   C  3  97  ? -4.034  -52.907 -53.129  1.00 73.06  ? 97   THR   C CB   1 
ATOM   17648 O  OG1  . THR   C  3  97  ? -4.945  -51.807 -53.017  1.00 74.27  ? 97   THR   C OG1  1 
ATOM   17649 C  CG2  . THR   C  3  97  ? -4.205  -53.830 -51.931  1.00 71.47  ? 97   THR   C CG2  1 
ATOM   17650 H  H    . THR   C  3  97  ? -2.734  -50.863 -51.957  1.00 85.10  ? 97   THR   C H    1 
ATOM   17651 H  HA   . THR   C  3  97  ? -1.996  -53.136 -53.254  1.00 87.33  ? 97   THR   C HA   1 
ATOM   17652 H  HB   . THR   C  3  97  ? -4.233  -53.412 -53.933  1.00 87.65  ? 97   THR   C HB   1 
ATOM   17653 H  HG1  . THR   C  3  97  ? -5.564  -52.001 -52.483  1.00 89.11  ? 97   THR   C HG1  1 
ATOM   17654 H  HG21 . THR   C  3  97  ? -5.108  -54.184 -51.911  1.00 85.75  ? 97   THR   C HG21 1 
ATOM   17655 H  HG22 . THR   C  3  97  ? -3.578  -54.568 -51.989  1.00 85.75  ? 97   THR   C HG22 1 
ATOM   17656 H  HG23 . THR   C  3  97  ? -4.041  -53.340 -51.110  1.00 85.75  ? 97   THR   C HG23 1 
ATOM   17657 N  N    . PHE   C  3  98  ? -2.026  -52.204 -55.542  1.00 72.00  ? 98   PHE   C N    1 
ATOM   17658 C  CA   . PHE   C  3  98  ? -1.793  -51.569 -56.829  1.00 68.08  ? 98   PHE   C CA   1 
ATOM   17659 C  C    . PHE   C  3  98  ? -2.855  -51.997 -57.833  1.00 66.98  ? 98   PHE   C C    1 
ATOM   17660 O  O    . PHE   C  3  98  ? -3.488  -53.047 -57.694  1.00 68.23  ? 98   PHE   C O    1 
ATOM   17661 C  CB   . PHE   C  3  98  ? -0.409  -51.928 -57.385  1.00 67.33  ? 98   PHE   C CB   1 
ATOM   17662 C  CG   . PHE   C  3  98  ? 0.733   -51.438 -56.546  1.00 64.74  ? 98   PHE   C CG   1 
ATOM   17663 C  CD1  . PHE   C  3  98  ? 1.134   -52.137 -55.421  1.00 66.37  ? 98   PHE   C CD1  1 
ATOM   17664 C  CD2  . PHE   C  3  98  ? 1.416   -50.285 -56.892  1.00 62.45  ? 98   PHE   C CD2  1 
ATOM   17665 C  CE1  . PHE   C  3  98  ? 2.188   -51.689 -54.649  1.00 65.71  ? 98   PHE   C CE1  1 
ATOM   17666 C  CE2  . PHE   C  3  98  ? 2.470   -49.830 -56.125  1.00 62.14  ? 98   PHE   C CE2  1 
ATOM   17667 C  CZ   . PHE   C  3  98  ? 2.858   -50.534 -55.002  1.00 64.67  ? 98   PHE   C CZ   1 
ATOM   17668 H  H    . PHE   C  3  98  ? -1.883  -53.052 -55.552  1.00 86.38  ? 98   PHE   C H    1 
ATOM   17669 H  HA   . PHE   C  3  98  ? -1.842  -50.607 -56.712  1.00 81.67  ? 98   PHE   C HA   1 
ATOM   17670 H  HB2  . PHE   C  3  98  ? -0.339  -52.894 -57.443  1.00 80.78  ? 98   PHE   C HB2  1 
ATOM   17671 H  HB3  . PHE   C  3  98  ? -0.317  -51.536 -58.267  1.00 80.78  ? 98   PHE   C HB3  1 
ATOM   17672 H  HD1  . PHE   C  3  98  ? 0.689   -52.918 -55.182  1.00 79.63  ? 98   PHE   C HD1  1 
ATOM   17673 H  HD2  . PHE   C  3  98  ? 1.162   -49.810 -57.651  1.00 74.92  ? 98   PHE   C HD2  1 
ATOM   17674 H  HE1  . PHE   C  3  98  ? 2.446   -52.164 -53.893  1.00 78.83  ? 98   PHE   C HE1  1 
ATOM   17675 H  HE2  . PHE   C  3  98  ? 2.917   -49.051 -56.364  1.00 74.55  ? 98   PHE   C HE2  1 
ATOM   17676 H  HZ   . PHE   C  3  98  ? 3.569   -50.231 -54.485  1.00 77.59  ? 98   PHE   C HZ   1 
ATOM   17677 N  N    . GLY   C  3  99  ? -3.038  -51.163 -58.858  1.00 65.75  ? 99   GLY   C N    1 
ATOM   17678 C  CA   . GLY   C  3  99  ? -3.846  -51.553 -59.990  1.00 67.80  ? 99   GLY   C CA   1 
ATOM   17679 C  C    . GLY   C  3  99  ? -3.085  -52.450 -60.948  1.00 69.41  ? 99   GLY   C C    1 
ATOM   17680 O  O    . GLY   C  3  99  ? -1.859  -52.547 -60.915  1.00 67.18  ? 99   GLY   C O    1 
ATOM   17681 H  H    . GLY   C  3  99  ? -2.704  -50.372 -58.913  1.00 78.88  ? 99   GLY   C H    1 
ATOM   17682 H  HA2  . GLY   C  3  99  ? -4.630  -52.032 -59.677  1.00 81.34  ? 99   GLY   C HA2  1 
ATOM   17683 H  HA3  . GLY   C  3  99  ? -4.131  -50.761 -60.471  1.00 81.34  ? 99   GLY   C HA3  1 
ATOM   17684 N  N    . GLY   C  3  100 ? -3.838  -53.120 -61.823  1.00 76.47  ? 100  GLY   C N    1 
ATOM   17685 C  CA   . GLY   C  3  100 ? -3.225  -54.066 -62.740  1.00 77.18  ? 100  GLY   C CA   1 
ATOM   17686 C  C    . GLY   C  3  100 ? -2.181  -53.443 -63.645  1.00 75.08  ? 100  GLY   C C    1 
ATOM   17687 O  O    . GLY   C  3  100 ? -1.274  -54.133 -64.118  1.00 73.44  ? 100  GLY   C O    1 
ATOM   17688 H  H    . GLY   C  3  100 ? -4.691  -53.043 -61.901  1.00 91.75  ? 100  GLY   C H    1 
ATOM   17689 H  HA2  . GLY   C  3  100 ? -2.797  -54.771 -62.228  1.00 92.60  ? 100  GLY   C HA2  1 
ATOM   17690 H  HA3  . GLY   C  3  100 ? -3.914  -54.456 -63.300  1.00 92.60  ? 100  GLY   C HA3  1 
ATOM   17691 N  N    . GLY   C  3  101 ? -2.290  -52.140 -63.901  1.00 72.96  ? 101  GLY   C N    1 
ATOM   17692 C  CA   . GLY   C  3  101 ? -1.347  -51.457 -64.764  1.00 70.81  ? 101  GLY   C CA   1 
ATOM   17693 C  C    . GLY   C  3  101 ? -1.888  -51.183 -66.153  1.00 71.78  ? 101  GLY   C C    1 
ATOM   17694 O  O    . GLY   C  3  101 ? -2.562  -52.031 -66.745  1.00 74.04  ? 101  GLY   C O    1 
ATOM   17695 H  H    . GLY   C  3  101 ? -2.906  -51.632 -63.582  1.00 87.53  ? 101  GLY   C H    1 
ATOM   17696 H  HA2  . GLY   C  3  101 ? -1.107  -50.608 -64.362  1.00 84.95  ? 101  GLY   C HA2  1 
ATOM   17697 H  HA3  . GLY   C  3  101 ? -0.548  -52.000 -64.854  1.00 84.95  ? 101  GLY   C HA3  1 
ATOM   17698 N  N    . THR   C  3  102 ? -1.597  -49.996 -66.681  1.00 70.78  ? 102  THR   C N    1 
ATOM   17699 C  CA   . THR   C  3  102 ? -1.983  -49.605 -68.031  1.00 72.65  ? 102  THR   C CA   1 
ATOM   17700 C  C    . THR   C  3  102 ? -0.723  -49.326 -68.837  1.00 72.68  ? 102  THR   C C    1 
ATOM   17701 O  O    . THR   C  3  102 ? 0.140   -48.556 -68.402  1.00 68.99  ? 102  THR   C O    1 
ATOM   17702 C  CB   . THR   C  3  102 ? -2.894  -48.373 -68.016  1.00 73.08  ? 102  THR   C CB   1 
ATOM   17703 O  OG1  . THR   C  3  102 ? -4.115  -48.687 -67.335  1.00 76.23  ? 102  THR   C OG1  1 
ATOM   17704 C  CG2  . THR   C  3  102 ? -3.212  -47.919 -69.438  1.00 74.12  ? 102  THR   C CG2  1 
ATOM   17705 H  H    . THR   C  3  102 ? -1.164  -49.382 -66.262  1.00 84.91  ? 102  THR   C H    1 
ATOM   17706 H  HA   . THR   C  3  102 ? -2.469  -50.330 -68.455  1.00 87.17  ? 102  THR   C HA   1 
ATOM   17707 H  HB   . THR   C  3  102 ? -2.443  -47.647 -67.558  1.00 87.68  ? 102  THR   C HB   1 
ATOM   17708 H  HG1  . THR   C  3  102 ? -4.580  -49.207 -67.804  1.00 91.45  ? 102  THR   C HG1  1 
ATOM   17709 H  HG21 . THR   C  3  102 ? -3.874  -47.210 -69.419  1.00 88.93  ? 102  THR   C HG21 1 
ATOM   17710 H  HG22 . THR   C  3  102 ? -2.408  -47.587 -69.868  1.00 88.93  ? 102  THR   C HG22 1 
ATOM   17711 H  HG23 . THR   C  3  102 ? -3.561  -48.662 -69.954  1.00 88.93  ? 102  THR   C HG23 1 
ATOM   17712 N  N    . LYS   C  3  103 ? -0.628  -49.945 -70.009  1.00 65.78  ? 103  LYS   C N    1 
ATOM   17713 C  CA   . LYS   C  3  103 ? 0.563   -49.882 -70.846  1.00 68.44  ? 103  LYS   C CA   1 
ATOM   17714 C  C    . LYS   C  3  103 ? 0.315   -48.928 -72.008  1.00 70.57  ? 103  LYS   C C    1 
ATOM   17715 O  O    . LYS   C  3  103 ? -0.675  -49.070 -72.733  1.00 74.70  ? 103  LYS   C O    1 
ATOM   17716 C  CB   . LYS   C  3  103 ? 0.921   -51.279 -71.360  1.00 75.66  ? 103  LYS   C CB   1 
ATOM   17717 C  CG   . LYS   C  3  103 ? 0.760   -52.378 -70.305  1.00 83.24  ? 103  LYS   C CG   1 
ATOM   17718 C  CD   . LYS   C  3  103 ? 0.807   -53.778 -70.901  1.00 87.61  ? 103  LYS   C CD   1 
ATOM   17719 C  CE   . LYS   C  3  103 ? -0.066  -54.744 -70.105  1.00 87.92  ? 103  LYS   C CE   1 
ATOM   17720 N  NZ   . LYS   C  3  103 ? 0.056   -54.548 -68.631  1.00 83.26  ? 103  LYS   C NZ   1 
ATOM   17721 H  H    . LYS   C  3  103 ? -1.258  -50.421 -70.349  1.00 78.92  ? 103  LYS   C H    1 
ATOM   17722 H  HA   . LYS   C  3  103 ? 1.314   -49.542 -70.335  1.00 82.11  ? 103  LYS   C HA   1 
ATOM   17723 H  HB2  . LYS   C  3  103 ? 0.340   -51.496 -72.106  1.00 90.77  ? 103  LYS   C HB2  1 
ATOM   17724 H  HB3  . LYS   C  3  103 ? 1.847   -51.278 -71.650  1.00 90.77  ? 103  LYS   C HB3  1 
ATOM   17725 H  HG2  . LYS   C  3  103 ? 1.479   -52.304 -69.658  1.00 99.87  ? 103  LYS   C HG2  1 
ATOM   17726 H  HG3  . LYS   C  3  103 ? -0.096  -52.269 -69.863  1.00 99.87  ? 103  LYS   C HG3  1 
ATOM   17727 H  HD2  . LYS   C  3  103 ? 0.481   -53.751 -71.814  1.00 105.11 ? 103  LYS   C HD2  1 
ATOM   17728 H  HD3  . LYS   C  3  103 ? 1.720   -54.106 -70.884  1.00 105.11 ? 103  LYS   C HD3  1 
ATOM   17729 H  HE2  . LYS   C  3  103 ? -0.994  -54.608 -70.350  1.00 105.49 ? 103  LYS   C HE2  1 
ATOM   17730 H  HE3  . LYS   C  3  103 ? 0.201   -55.654 -70.309  1.00 105.49 ? 103  LYS   C HE3  1 
ATOM   17731 H  HZ1  . LYS   C  3  103 ? -0.223  -55.276 -68.203  1.00 99.89  ? 103  LYS   C HZ1  1 
ATOM   17732 H  HZ2  . LYS   C  3  103 ? 0.904   -54.391 -68.414  1.00 99.89  ? 103  LYS   C HZ2  1 
ATOM   17733 H  HZ3  . LYS   C  3  103 ? -0.441  -53.855 -68.375  1.00 99.89  ? 103  LYS   C HZ3  1 
ATOM   17734 N  N    . VAL   C  3  104 ? 1.210   -47.956 -72.180  1.00 70.13  ? 104  VAL   C N    1 
ATOM   17735 C  CA   . VAL   C  3  104 ? 1.092   -46.942 -73.225  1.00 72.40  ? 104  VAL   C CA   1 
ATOM   17736 C  C    . VAL   C  3  104 ? 2.095   -47.270 -74.324  1.00 71.67  ? 104  VAL   C C    1 
ATOM   17737 O  O    . VAL   C  3  104 ? 3.309   -47.277 -74.089  1.00 67.46  ? 104  VAL   C O    1 
ATOM   17738 C  CB   . VAL   C  3  104 ? 1.315   -45.526 -72.673  1.00 70.79  ? 104  VAL   C CB   1 
ATOM   17739 C  CG1  . VAL   C  3  104 ? 1.381   -44.514 -73.811  1.00 71.24  ? 104  VAL   C CG1  1 
ATOM   17740 C  CG2  . VAL   C  3  104 ? 0.201   -45.156 -71.704  1.00 71.08  ? 104  VAL   C CG2  1 
ATOM   17741 H  H    . VAL   C  3  104 ? 1.911   -47.861 -71.690  1.00 84.14  ? 104  VAL   C H    1 
ATOM   17742 H  HA   . VAL   C  3  104 ? 0.201   -46.985 -73.607  1.00 86.86  ? 104  VAL   C HA   1 
ATOM   17743 H  HB   . VAL   C  3  104 ? 2.159   -45.504 -72.196  1.00 84.93  ? 104  VAL   C HB   1 
ATOM   17744 H  HG11 . VAL   C  3  104 ? 1.349   -43.619 -73.440  1.00 85.47  ? 104  VAL   C HG11 1 
ATOM   17745 H  HG12 . VAL   C  3  104 ? 2.210   -44.641 -74.298  1.00 85.47  ? 104  VAL   C HG12 1 
ATOM   17746 H  HG13 . VAL   C  3  104 ? 0.625   -44.654 -74.403  1.00 85.47  ? 104  VAL   C HG13 1 
ATOM   17747 H  HG21 . VAL   C  3  104 ? 0.318   -44.234 -71.426  1.00 85.28  ? 104  VAL   C HG21 1 
ATOM   17748 H  HG22 . VAL   C  3  104 ? -0.654  -45.262 -72.150  1.00 85.28  ? 104  VAL   C HG22 1 
ATOM   17749 H  HG23 . VAL   C  3  104 ? 0.247   -45.742 -70.932  1.00 85.28  ? 104  VAL   C HG23 1 
ATOM   17750 N  N    . GLU   C  3  105 ? 1.582   -47.528 -75.525  1.00 76.84  ? 105  GLU   C N    1 
ATOM   17751 C  CA   . GLU   C  3  105 ? 2.371   -47.914 -76.687  1.00 77.90  ? 105  GLU   C CA   1 
ATOM   17752 C  C    . GLU   C  3  105 ? 2.230   -46.849 -77.769  1.00 77.92  ? 105  GLU   C C    1 
ATOM   17753 O  O    . GLU   C  3  105 ? 1.173   -46.229 -77.915  1.00 80.09  ? 105  GLU   C O    1 
ATOM   17754 C  CB   . GLU   C  3  105 ? 1.915   -49.311 -77.182  1.00 82.66  ? 105  GLU   C CB   1 
ATOM   17755 C  CG   . GLU   C  3  105 ? 1.864   -49.554 -78.694  1.00 92.56  ? 105  GLU   C CG   1 
ATOM   17756 C  CD   . GLU   C  3  105 ? 0.674   -50.410 -79.104  1.00 101.13 ? 105  GLU   C CD   1 
ATOM   17757 O  OE1  . GLU   C  3  105 ? -0.418  -50.248 -78.516  1.00 104.86 ? 105  GLU   C OE1  1 
ATOM   17758 O  OE2  . GLU   C  3  105 ? 0.834   -51.252 -80.013  1.00 104.78 ? 105  GLU   C OE2  1 
ATOM   17759 H  H    . GLU   C  3  105 ? 0.740   -47.485 -75.697  1.00 92.19  ? 105  GLU   C H    1 
ATOM   17760 H  HA   . GLU   C  3  105 ? 3.317   -47.969 -76.478  1.00 93.46  ? 105  GLU   C HA   1 
ATOM   17761 H  HB2  . GLU   C  3  105 ? 2.525   -49.969 -76.815  1.00 99.17  ? 105  GLU   C HB2  1 
ATOM   17762 H  HB3  . GLU   C  3  105 ? 1.018   -49.465 -76.846  1.00 99.17  ? 105  GLU   C HB3  1 
ATOM   17763 H  HG2  . GLU   C  3  105 ? 1.794   -48.701 -79.150  1.00 111.05 ? 105  GLU   C HG2  1 
ATOM   17764 H  HG3  . GLU   C  3  105 ? 2.674   -50.011 -78.969  1.00 111.05 ? 105  GLU   C HG3  1 
ATOM   17765 N  N    . MET   C  3  106 ? 3.305   -46.637 -78.527  1.00 73.46  ? 106  MET   C N    1 
ATOM   17766 C  CA   . MET   C  3  106 ? 3.258   -45.684 -79.629  1.00 75.84  ? 106  MET   C CA   1 
ATOM   17767 C  C    . MET   C  3  106 ? 2.375   -46.209 -80.755  1.00 76.00  ? 106  MET   C C    1 
ATOM   17768 O  O    . MET   C  3  106 ? 2.291   -47.415 -81.001  1.00 75.56  ? 106  MET   C O    1 
ATOM   17769 C  CB   . MET   C  3  106 ? 4.659   -45.408 -80.181  1.00 81.67  ? 106  MET   C CB   1 
ATOM   17770 C  CG   . MET   C  3  106 ? 5.353   -44.169 -79.623  1.00 89.23  ? 106  MET   C CG   1 
ATOM   17771 S  SD   . MET   C  3  106 ? 4.381   -42.646 -79.706  1.00 97.04  ? 106  MET   C SD   1 
ATOM   17772 C  CE   . MET   C  3  106 ? 4.273   -42.368 -81.474  1.00 107.85 ? 106  MET   C CE   1 
ATOM   17773 H  H    . MET   C  3  106 ? 4.064   -47.029 -78.425  1.00 88.13  ? 106  MET   C H    1 
ATOM   17774 H  HA   . MET   C  3  106 ? 2.899   -44.848 -79.292  1.00 90.99  ? 106  MET   C HA   1 
ATOM   17775 H  HB2  . MET   C  3  106 ? 5.223   -46.171 -79.977  1.00 97.99  ? 106  MET   C HB2  1 
ATOM   17776 H  HB3  . MET   C  3  106 ? 4.591   -45.294 -81.141  1.00 97.99  ? 106  MET   C HB3  1 
ATOM   17777 H  HG2  . MET   C  3  106 ? 5.564   -44.328 -78.690  1.00 107.05 ? 106  MET   C HG2  1 
ATOM   17778 H  HG3  . MET   C  3  106 ? 6.169   -44.021 -80.127  1.00 107.05 ? 106  MET   C HG3  1 
ATOM   17779 H  HE1  . MET   C  3  106 ? 3.706   -41.598 -81.639  1.00 129.40 ? 106  MET   C HE1  1 
ATOM   17780 H  HE2  . MET   C  3  106 ? 5.163   -42.205 -81.824  1.00 129.40 ? 106  MET   C HE2  1 
ATOM   17781 H  HE3  . MET   C  3  106 ? 3.892   -43.155 -81.895  1.00 129.40 ? 106  MET   C HE3  1 
ATOM   17782 N  N    . ARG   C  3  107 ? 1.725   -45.286 -81.457  1.00 78.34  ? 107  ARG   C N    1 
ATOM   17783 C  CA   . ARG   C  3  107 ? 0.885   -45.642 -82.591  1.00 84.16  ? 107  ARG   C CA   1 
ATOM   17784 C  C    . ARG   C  3  107 ? 1.714   -45.716 -83.866  1.00 83.52  ? 107  ARG   C C    1 
ATOM   17785 O  O    . ARG   C  3  107 ? 2.740   -45.045 -84.008  1.00 79.22  ? 107  ARG   C O    1 
ATOM   17786 C  CB   . ARG   C  3  107 ? -0.251  -44.636 -82.773  1.00 92.33  ? 107  ARG   C CB   1 
ATOM   17787 C  CG   . ARG   C  3  107 ? -1.570  -45.094 -82.182  1.00 98.95  ? 107  ARG   C CG   1 
ATOM   17788 C  CD   . ARG   C  3  107 ? -2.746  -44.469 -82.911  1.00 109.87 ? 107  ARG   C CD   1 
ATOM   17789 N  NE   . ARG   C  3  107 ? -3.994  -44.632 -82.171  1.00 116.22 ? 107  ARG   C NE   1 
ATOM   17790 C  CZ   . ARG   C  3  107 ? -4.483  -43.743 -81.310  1.00 121.61 ? 107  ARG   C CZ   1 
ATOM   17791 N  NH1  . ARG   C  3  107 ? -3.838  -42.608 -81.070  1.00 122.20 ? 107  ARG   C NH1  1 
ATOM   17792 N  NH2  . ARG   C  3  107 ? -5.626  -43.991 -80.687  1.00 125.41 ? 107  ARG   C NH2  1 
ATOM   17793 H  H    . ARG   C  3  107 ? 1.756   -44.442 -81.294  1.00 93.99  ? 107  ARG   C H    1 
ATOM   17794 H  HA   . ARG   C  3  107 ? 0.491   -46.512 -82.428  1.00 100.98 ? 107  ARG   C HA   1 
ATOM   17795 H  HB2  . ARG   C  3  107 ? -0.005  -43.805 -82.339  1.00 110.77 ? 107  ARG   C HB2  1 
ATOM   17796 H  HB3  . ARG   C  3  107 ? -0.387  -44.488 -83.722  1.00 110.77 ? 107  ARG   C HB3  1 
ATOM   17797 H  HG2  . ARG   C  3  107 ? -1.640  -46.058 -82.258  1.00 118.72 ? 107  ARG   C HG2  1 
ATOM   17798 H  HG3  . ARG   C  3  107 ? -1.614  -44.831 -81.249  1.00 118.72 ? 107  ARG   C HG3  1 
ATOM   17799 H  HD2  . ARG   C  3  107 ? -2.584  -43.519 -83.026  1.00 131.82 ? 107  ARG   C HD2  1 
ATOM   17800 H  HD3  . ARG   C  3  107 ? -2.849  -44.895 -83.777  1.00 131.82 ? 107  ARG   C HD3  1 
ATOM   17801 H  HE   . ARG   C  3  107 ? -4.444  -45.354 -82.300  1.00 139.45 ? 107  ARG   C HE   1 
ATOM   17802 H  HH11 . ARG   C  3  107 ? -3.097  -42.441 -81.472  1.00 146.63 ? 107  ARG   C HH11 1 
ATOM   17803 H  HH12 . ARG   C  3  107 ? -4.162  -42.040 -80.512  1.00 146.63 ? 107  ARG   C HH12 1 
ATOM   17804 H  HH21 . ARG   C  3  107 ? -6.049  -44.724 -80.840  1.00 150.47 ? 107  ARG   C HH21 1 
ATOM   17805 H  HH22 . ARG   C  3  107 ? -5.945  -43.418 -80.130  1.00 150.47 ? 107  ARG   C HH22 1 
ATOM   17806 N  N    . ARG   C  3  108 ? 1.245   -46.536 -84.802  1.00 86.19  ? 108  ARG   C N    1 
ATOM   17807 C  CA   . ARG   C  3  108 ? 1.993   -46.811 -86.017  1.00 86.45  ? 108  ARG   C CA   1 
ATOM   17808 C  C    . ARG   C  3  108 ? 1.029   -47.293 -87.087  1.00 86.46  ? 108  ARG   C C    1 
ATOM   17809 O  O    . ARG   C  3  108 ? -0.007  -47.891 -86.782  1.00 86.18  ? 108  ARG   C O    1 
ATOM   17810 C  CB   . ARG   C  3  108 ? 3.077   -47.866 -85.773  1.00 86.79  ? 108  ARG   C CB   1 
ATOM   17811 C  CG   . ARG   C  3  108 ? 4.221   -47.815 -86.764  1.00 89.32  ? 108  ARG   C CG   1 
ATOM   17812 C  CD   . ARG   C  3  108 ? 4.990   -49.122 -86.805  1.00 86.09  ? 108  ARG   C CD   1 
ATOM   17813 N  NE   . ARG   C  3  108 ? 5.974   -49.124 -87.882  1.00 89.28  ? 108  ARG   C NE   1 
ATOM   17814 C  CZ   . ARG   C  3  108 ? 5.686   -49.356 -89.159  1.00 97.46  ? 108  ARG   C CZ   1 
ATOM   17815 N  NH1  . ARG   C  3  108 ? 4.438   -49.606 -89.532  1.00 102.15 ? 108  ARG   C NH1  1 
ATOM   17816 N  NH2  . ARG   C  3  108 ? 6.650   -49.335 -90.068  1.00 101.09 ? 108  ARG   C NH2  1 
ATOM   17817 H  H    . ARG   C  3  108 ? 0.492   -46.948 -84.753  1.00 103.41 ? 108  ARG   C H    1 
ATOM   17818 H  HA   . ARG   C  3  108 ? 2.417   -45.996 -86.330  1.00 103.72 ? 108  ARG   C HA   1 
ATOM   17819 H  HB2  . ARG   C  3  108 ? 3.448   -47.731 -84.887  1.00 104.13 ? 108  ARG   C HB2  1 
ATOM   17820 H  HB3  . ARG   C  3  108 ? 2.673   -48.746 -85.833  1.00 104.13 ? 108  ARG   C HB3  1 
ATOM   17821 H  HG2  . ARG   C  3  108 ? 3.869   -47.643 -87.651  1.00 107.16 ? 108  ARG   C HG2  1 
ATOM   17822 H  HG3  . ARG   C  3  108 ? 4.835   -47.109 -86.508  1.00 107.16 ? 108  ARG   C HG3  1 
ATOM   17823 H  HD2  . ARG   C  3  108 ? 5.456   -49.248 -85.964  1.00 103.29 ? 108  ARG   C HD2  1 
ATOM   17824 H  HD3  . ARG   C  3  108 ? 4.372   -49.855 -86.954  1.00 103.29 ? 108  ARG   C HD3  1 
ATOM   17825 H  HE   . ARG   C  3  108 ? 6.794   -48.965 -87.677  1.00 107.12 ? 108  ARG   C HE   1 
ATOM   17826 H  HH11 . ARG   C  3  108 ? 3.808   -49.618 -88.946  1.00 122.56 ? 108  ARG   C HH11 1 
ATOM   17827 H  HH12 . ARG   C  3  108 ? 4.258   -49.755 -90.360  1.00 122.56 ? 108  ARG   C HH12 1 
ATOM   17828 H  HH21 . ARG   C  3  108 ? 7.460   -49.172 -89.832  1.00 121.29 ? 108  ARG   C HH21 1 
ATOM   17829 H  HH22 . ARG   C  3  108 ? 6.465   -49.485 -90.895  1.00 121.29 ? 108  ARG   C HH22 1 
ATOM   17830 N  N    . ALA   C  3  109 ? 1.378   -47.026 -88.341  1.00 88.09  ? 109  ALA   C N    1 
ATOM   17831 C  CA   . ALA   C  3  109 ? 0.643   -47.612 -89.450  1.00 95.17  ? 109  ALA   C CA   1 
ATOM   17832 C  C    . ALA   C  3  109 ? 0.855   -49.121 -89.457  1.00 95.45  ? 109  ALA   C C    1 
ATOM   17833 O  O    . ALA   C  3  109 ? 1.956   -49.609 -89.188  1.00 93.66  ? 109  ALA   C O    1 
ATOM   17834 C  CB   . ALA   C  3  109 ? 1.096   -47.005 -90.776  1.00 101.08 ? 109  ALA   C CB   1 
ATOM   17835 H  H    . ALA   C  3  109 ? 2.029   -46.514 -88.572  1.00 105.69 ? 109  ALA   C H    1 
ATOM   17836 H  HA   . ALA   C  3  109 ? -0.305  -47.428 -89.357  1.00 114.19 ? 109  ALA   C HA   1 
ATOM   17837 H  HB1  . ALA   C  3  109 ? 0.590   -47.408 -91.498  1.00 121.27 ? 109  ALA   C HB1  1 
ATOM   17838 H  HB2  . ALA   C  3  109 ? 0.938   -46.048 -90.755  1.00 121.27 ? 109  ALA   C HB2  1 
ATOM   17839 H  HB3  . ALA   C  3  109 ? 2.043   -47.181 -90.896  1.00 121.27 ? 109  ALA   C HB3  1 
ATOM   17840 N  N    . ASP   C  3  110 ? -0.209  -49.861 -89.755  1.00 98.35  ? 110  ASP   C N    1 
ATOM   17841 C  CA   . ASP   C  3  110 ? -0.134  -51.314 -89.712  1.00 94.48  ? 110  ASP   C CA   1 
ATOM   17842 C  C    . ASP   C  3  110 ? 0.989   -51.822 -90.606  1.00 90.51  ? 110  ASP   C C    1 
ATOM   17843 O  O    . ASP   C  3  110 ? 1.213   -51.309 -91.706  1.00 90.90  ? 110  ASP   C O    1 
ATOM   17844 C  CB   . ASP   C  3  110 ? -1.467  -51.926 -90.141  1.00 103.57 ? 110  ASP   C CB   1 
ATOM   17845 C  CG   . ASP   C  3  110 ? -2.549  -51.749 -89.101  1.00 108.15 ? 110  ASP   C CG   1 
ATOM   17846 O  OD1  . ASP   C  3  110 ? -2.247  -51.219 -88.011  1.00 105.17 ? 110  ASP   C OD1  1 
ATOM   17847 O  OD2  . ASP   C  3  110 ? -3.702  -52.142 -89.373  1.00 113.56 ? 110  ASP   C OD2  1 
ATOM   17848 H  H    . ASP   C  3  110 ? -0.977  -49.548 -89.983  1.00 118.00 ? 110  ASP   C H    1 
ATOM   17849 H  HA   . ASP   C  3  110 ? 0.050   -51.598 -88.802  1.00 113.35 ? 110  ASP   C HA   1 
ATOM   17850 H  HB2  . ASP   C  3  110 ? -1.763  -51.496 -90.959  1.00 124.27 ? 110  ASP   C HB2  1 
ATOM   17851 H  HB3  . ASP   C  3  110 ? -1.346  -52.876 -90.291  1.00 124.27 ? 110  ASP   C HB3  1 
ATOM   17852 N  N    . ALA   C  3  111 ? 1.699   -52.838 -90.124  1.00 89.51  ? 111  ALA   C N    1 
ATOM   17853 C  CA   . ALA   C  3  111 ? 2.798   -53.448 -90.854  1.00 94.02  ? 111  ALA   C CA   1 
ATOM   17854 C  C    . ALA   C  3  111 ? 2.608   -54.956 -90.877  1.00 97.40  ? 111  ALA   C C    1 
ATOM   17855 O  O    . ALA   C  3  111 ? 1.960   -55.530 -89.996  1.00 99.18  ? 111  ALA   C O    1 
ATOM   17856 C  CB   . ALA   C  3  111 ? 4.154   -53.102 -90.228  1.00 88.02  ? 111  ALA   C CB   1 
ATOM   17857 H  H    . ALA   C  3  111 ? 1.557   -53.198 -89.356  1.00 107.39 ? 111  ALA   C H    1 
ATOM   17858 H  HA   . ALA   C  3  111 ? 2.801   -53.125 -91.769  1.00 112.80 ? 111  ALA   C HA   1 
ATOM   17859 H  HB1  . ALA   C  3  111 ? 4.857   -53.537 -90.736  1.00 105.61 ? 111  ALA   C HB1  1 
ATOM   17860 H  HB2  . ALA   C  3  111 ? 4.276   -52.140 -90.251  1.00 105.61 ? 111  ALA   C HB2  1 
ATOM   17861 H  HB3  . ALA   C  3  111 ? 4.167   -53.415 -89.310  1.00 105.61 ? 111  ALA   C HB3  1 
ATOM   17862 N  N    . ALA   C  3  112 ? 3.181   -55.594 -91.894  1.00 97.00  ? 112  ALA   C N    1 
ATOM   17863 C  CA   . ALA   C  3  112 ? 3.065   -57.041 -92.004  1.00 92.54  ? 112  ALA   C CA   1 
ATOM   17864 C  C    . ALA   C  3  112 ? 4.345   -57.715 -91.527  1.00 86.32  ? 112  ALA   C C    1 
ATOM   17865 O  O    . ALA   C  3  112 ? 5.446   -57.237 -91.824  1.00 83.98  ? 112  ALA   C O    1 
ATOM   17866 C  CB   . ALA   C  3  112 ? 2.783   -57.455 -93.448  1.00 94.14  ? 112  ALA   C CB   1 
ATOM   17867 H  H    . ALA   C  3  112 ? 3.633   -55.218 -92.521  1.00 116.38 ? 112  ALA   C H    1 
ATOM   17868 H  HA   . ALA   C  3  112 ? 2.329   -57.350 -91.454  1.00 111.03 ? 112  ALA   C HA   1 
ATOM   17869 H  HB1  . ALA   C  3  112 ? 2.708   -58.421 -93.491  1.00 112.95 ? 112  ALA   C HB1  1 
ATOM   17870 H  HB2  . ALA   C  3  112 ? 1.952   -57.047 -93.737  1.00 112.95 ? 112  ALA   C HB2  1 
ATOM   17871 H  HB3  . ALA   C  3  112 ? 3.513   -57.155 -94.012  1.00 112.95 ? 112  ALA   C HB3  1 
ATOM   17872 N  N    . PRO   C  3  113 ? 4.245   -58.819 -90.787  1.00 86.59  ? 113  PRO   C N    1 
ATOM   17873 C  CA   . PRO   C  3  113 ? 5.460   -59.478 -90.297  1.00 82.76  ? 113  PRO   C CA   1 
ATOM   17874 C  C    . PRO   C  3  113 ? 6.255   -60.111 -91.427  1.00 80.14  ? 113  PRO   C C    1 
ATOM   17875 O  O    . PRO   C  3  113 ? 5.699   -60.754 -92.321  1.00 82.64  ? 113  PRO   C O    1 
ATOM   17876 C  CB   . PRO   C  3  113 ? 4.924   -60.542 -89.332  1.00 81.16  ? 113  PRO   C CB   1 
ATOM   17877 C  CG   . PRO   C  3  113 ? 3.541   -60.821 -89.812  1.00 84.71  ? 113  PRO   C CG   1 
ATOM   17878 C  CD   . PRO   C  3  113 ? 3.023   -59.512 -90.337  1.00 87.94  ? 113  PRO   C CD   1 
ATOM   17879 H  HA   . PRO   C  3  113 ? 6.021   -58.847 -89.820  1.00 99.30  ? 113  PRO   C HA   1 
ATOM   17880 H  HB2  . PRO   C  3  113 ? 5.475   -61.339 -89.376  1.00 97.37  ? 113  PRO   C HB2  1 
ATOM   17881 H  HB3  . PRO   C  3  113 ? 4.915   -60.194 -88.426  1.00 97.37  ? 113  PRO   C HB3  1 
ATOM   17882 H  HG2  . PRO   C  3  113 ? 3.566   -61.488 -90.516  1.00 101.63 ? 113  PRO   C HG2  1 
ATOM   17883 H  HG3  . PRO   C  3  113 ? 2.995   -61.137 -89.075  1.00 101.63 ? 113  PRO   C HG3  1 
ATOM   17884 H  HD2  . PRO   C  3  113 ? 2.414   -59.654 -91.079  1.00 105.50 ? 113  PRO   C HD2  1 
ATOM   17885 H  HD3  . PRO   C  3  113 ? 2.580   -59.009 -89.635  1.00 105.50 ? 113  PRO   C HD3  1 
ATOM   17886 N  N    . THR   C  3  114 ? 7.571   -59.914 -91.382  1.00 82.15  ? 114  THR   C N    1 
ATOM   17887 C  CA   . THR   C  3  114 ? 8.494   -60.668 -92.224  1.00 84.00  ? 114  THR   C CA   1 
ATOM   17888 C  C    . THR   C  3  114 ? 8.799   -61.979 -91.510  1.00 88.25  ? 114  THR   C C    1 
ATOM   17889 O  O    . THR   C  3  114 ? 9.531   -61.995 -90.515  1.00 94.69  ? 114  THR   C O    1 
ATOM   17890 C  CB   . THR   C  3  114 ? 9.770   -59.874 -92.482  1.00 81.93  ? 114  THR   C CB   1 
ATOM   17891 O  OG1  . THR   C  3  114 ? 9.444   -58.631 -93.115  1.00 85.92  ? 114  THR   C OG1  1 
ATOM   17892 C  CG2  . THR   C  3  114 ? 10.720  -60.659 -93.376  1.00 82.34  ? 114  THR   C CG2  1 
ATOM   17893 H  H    . THR   C  3  114 ? 7.956   -59.343 -90.867  1.00 98.56  ? 114  THR   C H    1 
ATOM   17894 H  HA   . THR   C  3  114 ? 8.085   -60.852 -93.084  1.00 100.78 ? 114  THR   C HA   1 
ATOM   17895 H  HB   . THR   C  3  114 ? 10.217  -59.701 -91.638  1.00 98.30  ? 114  THR   C HB   1 
ATOM   17896 H  HG1  . THR   C  3  114 ? 10.139  -58.171 -93.220  1.00 103.09 ? 114  THR   C HG1  1 
ATOM   17897 H  HG21 . THR   C  3  114 ? 11.500  -60.121 -93.584  1.00 98.78  ? 114  THR   C HG21 1 
ATOM   17898 H  HG22 . THR   C  3  114 ? 11.006  -61.468 -92.925  1.00 98.78  ? 114  THR   C HG22 1 
ATOM   17899 H  HG23 . THR   C  3  114 ? 10.274  -60.900 -94.203  1.00 98.78  ? 114  THR   C HG23 1 
ATOM   17900 N  N    . VAL   C  3  115 ? 8.235   -63.075 -92.005  1.00 86.86  ? 115  VAL   C N    1 
ATOM   17901 C  CA   . VAL   C  3  115 ? 8.299   -64.364 -91.326  1.00 84.80  ? 115  VAL   C CA   1 
ATOM   17902 C  C    . VAL   C  3  115 ? 9.369   -65.224 -91.976  1.00 85.51  ? 115  VAL   C C    1 
ATOM   17903 O  O    . VAL   C  3  115 ? 9.465   -65.299 -93.207  1.00 88.47  ? 115  VAL   C O    1 
ATOM   17904 C  CB   . VAL   C  3  115 ? 6.929   -65.068 -91.347  1.00 86.05  ? 115  VAL   C CB   1 
ATOM   17905 C  CG1  . VAL   C  3  115 ? 7.009   -66.401 -90.615  1.00 83.22  ? 115  VAL   C CG1  1 
ATOM   17906 C  CG2  . VAL   C  3  115 ? 5.872   -64.163 -90.731  1.00 85.57  ? 115  VAL   C CG2  1 
ATOM   17907 H  H    . VAL   C  3  115 ? 7.801   -63.098 -92.748  1.00 104.21 ? 115  VAL   C H    1 
ATOM   17908 H  HA   . VAL   C  3  115 ? 8.554   -64.219 -90.401  1.00 101.74 ? 115  VAL   C HA   1 
ATOM   17909 H  HB   . VAL   C  3  115 ? 6.670   -65.251 -92.264  1.00 103.24 ? 115  VAL   C HB   1 
ATOM   17910 H  HG11 . VAL   C  3  115 ? 6.151   -66.588 -90.203  1.00 99.84  ? 115  VAL   C HG11 1 
ATOM   17911 H  HG12 . VAL   C  3  115 ? 7.229   -67.098 -91.253  1.00 99.84  ? 115  VAL   C HG12 1 
ATOM   17912 H  HG13 . VAL   C  3  115 ? 7.698   -66.347 -89.935  1.00 99.84  ? 115  VAL   C HG13 1 
ATOM   17913 H  HG21 . VAL   C  3  115 ? 5.098   -64.697 -90.495  1.00 102.67 ? 115  VAL   C HG21 1 
ATOM   17914 H  HG22 . VAL   C  3  115 ? 6.239   -63.743 -89.937  1.00 102.67 ? 115  VAL   C HG22 1 
ATOM   17915 H  HG23 . VAL   C  3  115 ? 5.622   -63.484 -91.377  1.00 102.67 ? 115  VAL   C HG23 1 
ATOM   17916 N  N    . SER   C  3  116 ? 10.183  -65.872 -91.145  1.00 84.28  ? 116  SER   C N    1 
ATOM   17917 C  CA   . SER   C  3  116 ? 11.245  -66.755 -91.606  1.00 84.49  ? 116  SER   C CA   1 
ATOM   17918 C  C    . SER   C  3  116 ? 11.204  -68.037 -90.790  1.00 83.99  ? 116  SER   C C    1 
ATOM   17919 O  O    . SER   C  3  116 ? 11.120  -67.988 -89.559  1.00 86.84  ? 116  SER   C O    1 
ATOM   17920 C  CB   . SER   C  3  116 ? 12.619  -66.090 -91.472  1.00 84.63  ? 116  SER   C CB   1 
ATOM   17921 O  OG   . SER   C  3  116 ? 12.657  -64.844 -92.148  1.00 89.58  ? 116  SER   C OG   1 
ATOM   17922 H  H    . SER   C  3  116 ? 10.137  -65.812 -90.288  1.00 101.12 ? 116  SER   C H    1 
ATOM   17923 H  HA   . SER   C  3  116 ? 11.104  -66.976 -92.539  1.00 101.37 ? 116  SER   C HA   1 
ATOM   17924 H  HB2  . SER   C  3  116 ? 12.806  -65.942 -90.532  1.00 101.54 ? 116  SER   C HB2  1 
ATOM   17925 H  HB3  . SER   C  3  116 ? 13.290  -66.675 -91.856  1.00 101.54 ? 116  SER   C HB3  1 
ATOM   17926 H  HG   . SER   C  3  116 ? 12.689  -64.969 -92.978  1.00 107.47 ? 116  SER   C HG   1 
ATOM   17927 N  N    . ILE   C  3  117 ? 11.264  -69.176 -91.473  1.00 81.73  ? 117  ILE   C N    1 
ATOM   17928 C  CA   . ILE   C  3  117 ? 11.283  -70.482 -90.826  1.00 80.84  ? 117  ILE   C CA   1 
ATOM   17929 C  C    . ILE   C  3  117 ? 12.666  -71.087 -91.009  1.00 79.06  ? 117  ILE   C C    1 
ATOM   17930 O  O    . ILE   C  3  117 ? 13.327  -70.881 -92.034  1.00 78.36  ? 117  ILE   C O    1 
ATOM   17931 C  CB   . ILE   C  3  117 ? 10.197  -71.426 -91.385  1.00 88.31  ? 117  ILE   C CB   1 
ATOM   17932 C  CG1  . ILE   C  3  117 ? 10.047  -72.649 -90.478  1.00 89.68  ? 117  ILE   C CG1  1 
ATOM   17933 C  CG2  . ILE   C  3  117 ? 10.541  -71.859 -92.806  1.00 92.91  ? 117  ILE   C CG2  1 
ATOM   17934 C  CD1  . ILE   C  3  117 ? 8.863   -73.527 -90.824  1.00 94.08  ? 117  ILE   C CD1  1 
ATOM   17935 H  H    . ILE   C  3  117 ? 11.295  -69.219 -92.332  1.00 98.05  ? 117  ILE   C H    1 
ATOM   17936 H  HA   . ILE   C  3  117 ? 11.116  -70.366 -89.878  1.00 96.99  ? 117  ILE   C HA   1 
ATOM   17937 H  HB   . ILE   C  3  117 ? 9.355   -70.944 -91.406  1.00 105.95 ? 117  ILE   C HB   1 
ATOM   17938 H  HG12 . ILE   C  3  117 ? 10.848  -73.192 -90.551  1.00 107.60 ? 117  ILE   C HG12 1 
ATOM   17939 H  HG13 . ILE   C  3  117 ? 9.932   -72.347 -89.563  1.00 107.60 ? 117  ILE   C HG13 1 
ATOM   17940 H  HG21 . ILE   C  3  117 ? 9.776   -72.314 -93.191  1.00 111.47 ? 117  ILE   C HG21 1 
ATOM   17941 H  HG22 . ILE   C  3  117 ? 10.758  -71.073 -93.332  1.00 111.47 ? 117  ILE   C HG22 1 
ATOM   17942 H  HG23 . ILE   C  3  117 ? 11.303  -72.458 -92.778  1.00 111.47 ? 117  ILE   C HG23 1 
ATOM   17943 H  HD11 . ILE   C  3  117 ? 8.812   -74.255 -90.186  1.00 112.87 ? 117  ILE   C HD11 1 
ATOM   17944 H  HD12 . ILE   C  3  117 ? 8.053   -72.995 -90.785  1.00 112.87 ? 117  ILE   C HD12 1 
ATOM   17945 H  HD13 . ILE   C  3  117 ? 8.984   -73.880 -91.720  1.00 112.87 ? 117  ILE   C HD13 1 
ATOM   17946 N  N    . PHE   C  3  118 ? 13.104  -71.843 -90.004  1.00 80.73  ? 118  PHE   C N    1 
ATOM   17947 C  CA   . PHE   C  3  118 ? 14.420  -72.455 -90.025  1.00 80.79  ? 118  PHE   C CA   1 
ATOM   17948 C  C    . PHE   C  3  118 ? 14.327  -73.927 -89.650  1.00 81.15  ? 118  PHE   C C    1 
ATOM   17949 O  O    . PHE   C  3  118 ? 13.585  -74.290 -88.730  1.00 77.97  ? 118  PHE   C O    1 
ATOM   17950 C  CB   . PHE   C  3  118 ? 15.371  -71.737 -89.058  1.00 77.36  ? 118  PHE   C CB   1 
ATOM   17951 C  CG   . PHE   C  3  118 ? 15.676  -70.326 -89.455  1.00 80.43  ? 118  PHE   C CG   1 
ATOM   17952 C  CD1  . PHE   C  3  118 ? 14.819  -69.296 -89.110  1.00 81.51  ? 118  PHE   C CD1  1 
ATOM   17953 C  CD2  . PHE   C  3  118 ? 16.816  -70.029 -90.181  1.00 82.20  ? 118  PHE   C CD2  1 
ATOM   17954 C  CE1  . PHE   C  3  118 ? 15.095  -67.996 -89.479  1.00 83.10  ? 118  PHE   C CE1  1 
ATOM   17955 C  CE2  . PHE   C  3  118 ? 17.098  -68.731 -90.551  1.00 83.44  ? 118  PHE   C CE2  1 
ATOM   17956 C  CZ   . PHE   C  3  118 ? 16.235  -67.712 -90.200  1.00 83.79  ? 118  PHE   C CZ   1 
ATOM   17957 H  H    . PHE   C  3  118 ? 12.648  -72.015 -89.295  1.00 96.85  ? 118  PHE   C H    1 
ATOM   17958 H  HA   . PHE   C  3  118 ? 14.786  -72.395 -90.921  1.00 96.93  ? 118  PHE   C HA   1 
ATOM   17959 H  HB2  . PHE   C  3  118 ? 14.964  -71.716 -88.177  1.00 92.81  ? 118  PHE   C HB2  1 
ATOM   17960 H  HB3  . PHE   C  3  118 ? 16.209  -72.224 -89.024  1.00 92.81  ? 118  PHE   C HB3  1 
ATOM   17961 H  HD1  . PHE   C  3  118 ? 14.048  -69.482 -88.625  1.00 97.79  ? 118  PHE   C HD1  1 
ATOM   17962 H  HD2  . PHE   C  3  118 ? 17.398  -70.713 -90.422  1.00 98.62  ? 118  PHE   C HD2  1 
ATOM   17963 H  HE1  . PHE   C  3  118 ? 14.512  -67.311 -89.242  1.00 99.70  ? 118  PHE   C HE1  1 
ATOM   17964 H  HE2  . PHE   C  3  118 ? 17.868  -68.542 -91.037  1.00 100.11 ? 118  PHE   C HE2  1 
ATOM   17965 H  HZ   . PHE   C  3  118 ? 16.423  -66.836 -90.448  1.00 100.53 ? 118  PHE   C HZ   1 
ATOM   17966 N  N    . PRO   C  3  119 ? 15.069  -74.793 -90.333  1.00 84.31  ? 119  PRO   C N    1 
ATOM   17967 C  CA   . PRO   C  3  119 ? 15.076  -76.204 -89.969  1.00 85.81  ? 119  PRO   C CA   1 
ATOM   17968 C  C    . PRO   C  3  119 ? 15.974  -76.431 -88.768  1.00 81.89  ? 119  PRO   C C    1 
ATOM   17969 O  O    . PRO   C  3  119 ? 16.752  -75.542 -88.390  1.00 78.85  ? 119  PRO   C O    1 
ATOM   17970 C  CB   . PRO   C  3  119 ? 15.636  -76.882 -91.226  1.00 91.90  ? 119  PRO   C CB   1 
ATOM   17971 C  CG   . PRO   C  3  119 ? 16.595  -75.874 -91.763  1.00 93.76  ? 119  PRO   C CG   1 
ATOM   17972 C  CD   . PRO   C  3  119 ? 16.029  -74.509 -91.417  1.00 90.13  ? 119  PRO   C CD   1 
ATOM   17973 H  HA   . PRO   C  3  119 ? 14.183  -76.535 -89.787  1.00 102.96 ? 119  PRO   C HA   1 
ATOM   17974 H  HB2  . PRO   C  3  119 ? 16.087  -77.708 -90.990  1.00 110.26 ? 119  PRO   C HB2  1 
ATOM   17975 H  HB3  . PRO   C  3  119 ? 14.922  -77.062 -91.857  1.00 110.26 ? 119  PRO   C HB3  1 
ATOM   17976 H  HG2  . PRO   C  3  119 ? 17.463  -75.998 -91.347  1.00 112.50 ? 119  PRO   C HG2  1 
ATOM   17977 H  HG3  . PRO   C  3  119 ? 16.670  -75.978 -92.724  1.00 112.50 ? 119  PRO   C HG3  1 
ATOM   17978 H  HD2  . PRO   C  3  119 ? 16.730  -73.914 -91.108  1.00 108.14 ? 119  PRO   C HD2  1 
ATOM   17979 H  HD3  . PRO   C  3  119 ? 15.578  -74.120 -92.183  1.00 108.14 ? 119  PRO   C HD3  1 
ATOM   17980 N  N    . PRO   C  3  120 ? 15.900  -77.598 -88.137  1.00 83.73  ? 120  PRO   C N    1 
ATOM   17981 C  CA   . PRO   C  3  120 ? 16.810  -77.876 -87.022  1.00 81.35  ? 120  PRO   C CA   1 
ATOM   17982 C  C    . PRO   C  3  120 ? 18.248  -77.950 -87.508  1.00 81.56  ? 120  PRO   C C    1 
ATOM   17983 O  O    . PRO   C  3  120 ? 18.536  -78.509 -88.569  1.00 84.07  ? 120  PRO   C O    1 
ATOM   17984 C  CB   . PRO   C  3  120 ? 16.320  -79.226 -86.489  1.00 84.66  ? 120  PRO   C CB   1 
ATOM   17985 C  CG   . PRO   C  3  120 ? 15.679  -79.874 -87.663  1.00 90.29  ? 120  PRO   C CG   1 
ATOM   17986 C  CD   . PRO   C  3  120 ? 15.058  -78.762 -88.466  1.00 90.18  ? 120  PRO   C CD   1 
ATOM   17987 H  HA   . PRO   C  3  120 ? 16.731  -77.207 -86.324  1.00 97.61  ? 120  PRO   C HA   1 
ATOM   17988 H  HB2  . PRO   C  3  120 ? 17.071  -79.749 -86.167  1.00 101.57 ? 120  PRO   C HB2  1 
ATOM   17989 H  HB3  . PRO   C  3  120 ? 15.680  -79.089 -85.773  1.00 101.57 ? 120  PRO   C HB3  1 
ATOM   17990 H  HG2  . PRO   C  3  120 ? 16.351  -80.340 -88.186  1.00 108.32 ? 120  PRO   C HG2  1 
ATOM   17991 H  HG3  . PRO   C  3  120 ? 15.001  -80.499 -87.361  1.00 108.32 ? 120  PRO   C HG3  1 
ATOM   17992 H  HD2  . PRO   C  3  120 ? 15.095  -78.958 -89.415  1.00 108.20 ? 120  PRO   C HD2  1 
ATOM   17993 H  HD3  . PRO   C  3  120 ? 14.139  -78.611 -88.195  1.00 108.20 ? 120  PRO   C HD3  1 
ATOM   17994 N  N    . SER   C  3  121 ? 19.152  -77.371 -86.725  1.00 79.15  ? 121  SER   C N    1 
ATOM   17995 C  CA   . SER   C  3  121 ? 20.557  -77.363 -87.100  1.00 76.93  ? 121  SER   C CA   1 
ATOM   17996 C  C    . SER   C  3  121 ? 21.121  -78.779 -87.074  1.00 77.71  ? 121  SER   C C    1 
ATOM   17997 O  O    . SER   C  3  121 ? 20.662  -79.643 -86.322  1.00 76.31  ? 121  SER   C O    1 
ATOM   17998 C  CB   . SER   C  3  121 ? 21.361  -76.470 -86.158  1.00 73.62  ? 121  SER   C CB   1 
ATOM   17999 O  OG   . SER   C  3  121 ? 21.644  -77.140 -84.943  1.00 73.15  ? 121  SER   C OG   1 
ATOM   18000 H  H    . SER   C  3  121 ? 18.978  -76.979 -85.979  1.00 94.96  ? 121  SER   C H    1 
ATOM   18001 H  HA   . SER   C  3  121 ? 20.647  -77.010 -87.999  1.00 92.29  ? 121  SER   C HA   1 
ATOM   18002 H  HB2  . SER   C  3  121 ? 22.197  -76.230 -86.588  1.00 88.33  ? 121  SER   C HB2  1 
ATOM   18003 H  HB3  . SER   C  3  121 ? 20.846  -75.671 -85.965  1.00 88.33  ? 121  SER   C HB3  1 
ATOM   18004 H  HG   . SER   C  3  121 ? 22.235  -76.724 -84.516  1.00 87.76  ? 121  SER   C HG   1 
ATOM   18005 N  N    . SER   C  3  122 ? 22.132  -79.013 -87.913  1.00 79.12  ? 122  SER   C N    1 
ATOM   18006 C  CA   . SER   C  3  122 ? 22.799  -80.310 -87.904  1.00 80.76  ? 122  SER   C CA   1 
ATOM   18007 C  C    . SER   C  3  122 ? 23.486  -80.565 -86.570  1.00 77.41  ? 122  SER   C C    1 
ATOM   18008 O  O    . SER   C  3  122 ? 23.567  -81.714 -86.122  1.00 78.80  ? 122  SER   C O    1 
ATOM   18009 C  CB   . SER   C  3  122 ? 23.809  -80.390 -89.047  1.00 85.58  ? 122  SER   C CB   1 
ATOM   18010 O  OG   . SER   C  3  122 ? 23.253  -79.884 -90.247  1.00 90.92  ? 122  SER   C OG   1 
ATOM   18011 H  H    . SER   C  3  122 ? 22.443  -78.450 -88.484  1.00 94.92  ? 122  SER   C H    1 
ATOM   18012 H  HA   . SER   C  3  122 ? 22.138  -81.006 -88.043  1.00 96.90  ? 122  SER   C HA   1 
ATOM   18013 H  HB2  . SER   C  3  122 ? 24.591  -79.865 -88.815  1.00 102.67 ? 122  SER   C HB2  1 
ATOM   18014 H  HB3  . SER   C  3  122 ? 24.061  -81.317 -89.181  1.00 102.67 ? 122  SER   C HB3  1 
ATOM   18015 H  HG   . SER   C  3  122 ? 23.745  -80.084 -90.898  1.00 109.08 ? 122  SER   C HG   1 
ATOM   18016 N  N    . GLU   C  3  123 ? 23.983  -79.509 -85.920  1.00 76.06  ? 123  GLU   C N    1 
ATOM   18017 C  CA   . GLU   C  3  123 ? 24.587  -79.674 -84.603  1.00 74.51  ? 123  GLU   C CA   1 
ATOM   18018 C  C    . GLU   C  3  123 ? 23.582  -80.241 -83.608  1.00 75.18  ? 123  GLU   C C    1 
ATOM   18019 O  O    . GLU   C  3  123 ? 23.913  -81.132 -82.817  1.00 75.70  ? 123  GLU   C O    1 
ATOM   18020 C  CB   . GLU   C  3  123 ? 25.128  -78.335 -84.096  1.00 74.35  ? 123  GLU   C CB   1 
ATOM   18021 C  CG   . GLU   C  3  123 ? 26.360  -77.806 -84.825  1.00 82.10  ? 123  GLU   C CG   1 
ATOM   18022 C  CD   . GLU   C  3  123 ? 26.048  -77.243 -86.197  1.00 94.44  ? 123  GLU   C CD   1 
ATOM   18023 O  OE1  . GLU   C  3  123 ? 24.976  -77.565 -86.749  1.00 100.32 ? 123  GLU   C OE1  1 
ATOM   18024 O  OE2  . GLU   C  3  123 ? 26.877  -76.470 -86.721  1.00 98.22  ? 123  GLU   C OE2  1 
ATOM   18025 H  H    . GLU   C  3  123 ? 23.981  -78.702 -86.216  1.00 91.26  ? 123  GLU   C H    1 
ATOM   18026 H  HA   . GLU   C  3  123 ? 25.331  -80.292 -84.678  1.00 89.39  ? 123  GLU   C HA   1 
ATOM   18027 H  HB2  . GLU   C  3  123 ? 24.429  -77.669 -84.189  1.00 89.21  ? 123  GLU   C HB2  1 
ATOM   18028 H  HB3  . GLU   C  3  123 ? 25.367  -78.437 -83.161  1.00 89.21  ? 123  GLU   C HB3  1 
ATOM   18029 H  HG2  . GLU   C  3  123 ? 26.759  -77.098 -84.295  1.00 98.50  ? 123  GLU   C HG2  1 
ATOM   18030 H  HG3  . GLU   C  3  123 ? 26.994  -78.532 -84.938  1.00 98.50  ? 123  GLU   C HG3  1 
ATOM   18031 N  N    . GLN   C  3  124 ? 22.346  -79.737 -83.637  1.00 76.40  ? 124  GLN   C N    1 
ATOM   18032 C  CA   . GLN   C  3  124 ? 21.343  -80.167 -82.668  1.00 75.66  ? 124  GLN   C CA   1 
ATOM   18033 C  C    . GLN   C  3  124 ? 20.889  -81.597 -82.931  1.00 79.58  ? 124  GLN   C C    1 
ATOM   18034 O  O    . GLN   C  3  124 ? 20.663  -82.365 -81.988  1.00 80.68  ? 124  GLN   C O    1 
ATOM   18035 C  CB   . GLN   C  3  124 ? 20.149  -79.214 -82.702  1.00 71.43  ? 124  GLN   C CB   1 
ATOM   18036 C  CG   . GLN   C  3  124 ? 18.940  -79.708 -81.931  1.00 72.19  ? 124  GLN   C CG   1 
ATOM   18037 C  CD   . GLN   C  3  124 ? 17.842  -78.669 -81.838  1.00 71.74  ? 124  GLN   C CD   1 
ATOM   18038 O  OE1  . GLN   C  3  124 ? 17.601  -77.915 -82.781  1.00 71.36  ? 124  GLN   C OE1  1 
ATOM   18039 N  NE2  . GLN   C  3  124 ? 17.171  -78.621 -80.694  1.00 72.37  ? 124  GLN   C NE2  1 
ATOM   18040 H  H    . GLN   C  3  124 ? 22.067  -79.151 -84.201  1.00 91.66  ? 124  GLN   C H    1 
ATOM   18041 H  HA   . GLN   C  3  124 ? 21.735  -80.138 -81.781  1.00 90.78  ? 124  GLN   C HA   1 
ATOM   18042 H  HB2  . GLN   C  3  124 ? 20.418  -78.365 -82.317  1.00 85.70  ? 124  GLN   C HB2  1 
ATOM   18043 H  HB3  . GLN   C  3  124 ? 19.878  -79.089 -83.625  1.00 85.70  ? 124  GLN   C HB3  1 
ATOM   18044 H  HG2  . GLN   C  3  124 ? 18.577  -80.489 -82.377  1.00 86.61  ? 124  GLN   C HG2  1 
ATOM   18045 H  HG3  . GLN   C  3  124 ? 19.213  -79.938 -81.029  1.00 86.61  ? 124  GLN   C HG3  1 
ATOM   18046 H  HE21 . GLN   C  3  124 ? 17.370  -79.162 -80.056  1.00 86.83  ? 124  GLN   C HE21 1 
ATOM   18047 H  HE22 . GLN   C  3  124 ? 16.537  -78.048 -80.591  1.00 86.83  ? 124  GLN   C HE22 1 
ATOM   18048 N  N    . LEU   C  3  125 ? 20.741  -81.971 -84.203  1.00 82.66  ? 125  LEU   C N    1 
ATOM   18049 C  CA   . LEU   C  3  125 ? 20.229  -83.299 -84.524  1.00 87.48  ? 125  LEU   C CA   1 
ATOM   18050 C  C    . LEU   C  3  125 ? 21.159  -84.391 -84.008  1.00 90.72  ? 125  LEU   C C    1 
ATOM   18051 O  O    . LEU   C  3  125 ? 20.697  -85.445 -83.556  1.00 94.35  ? 125  LEU   C O    1 
ATOM   18052 C  CB   . LEU   C  3  125 ? 20.017  -83.424 -86.033  1.00 86.71  ? 125  LEU   C CB   1 
ATOM   18053 C  CG   . LEU   C  3  125 ? 18.811  -82.647 -86.571  1.00 84.52  ? 125  LEU   C CG   1 
ATOM   18054 C  CD1  . LEU   C  3  125 ? 18.854  -82.534 -88.086  1.00 84.21  ? 125  LEU   C CD1  1 
ATOM   18055 C  CD2  . LEU   C  3  125 ? 17.509  -83.304 -86.128  1.00 86.34  ? 125  LEU   C CD2  1 
ATOM   18056 H  H    . LEU   C  3  125 ? 20.926  -81.482 -84.886  1.00 99.18  ? 125  LEU   C H    1 
ATOM   18057 H  HA   . LEU   C  3  125 ? 19.369  -83.420 -84.092  1.00 104.96 ? 125  LEU   C HA   1 
ATOM   18058 H  HB2  . LEU   C  3  125 ? 20.808  -83.089 -86.484  1.00 104.04 ? 125  LEU   C HB2  1 
ATOM   18059 H  HB3  . LEU   C  3  125 ? 19.883  -84.360 -86.249  1.00 104.04 ? 125  LEU   C HB3  1 
ATOM   18060 H  HG   . LEU   C  3  125 ? 18.843  -81.748 -86.207  1.00 101.40 ? 125  LEU   C HG   1 
ATOM   18061 H  HD11 . LEU   C  3  125 ? 18.074  -82.043 -88.389  1.00 101.04 ? 125  LEU   C HD11 1 
ATOM   18062 H  HD12 . LEU   C  3  125 ? 19.662  -82.063 -88.345  1.00 101.04 ? 125  LEU   C HD12 1 
ATOM   18063 H  HD13 . LEU   C  3  125 ? 18.853  -83.425 -88.469  1.00 101.04 ? 125  LEU   C HD13 1 
ATOM   18064 H  HD21 . LEU   C  3  125 ? 16.764  -82.829 -86.528  1.00 103.59 ? 125  LEU   C HD21 1 
ATOM   18065 H  HD22 . LEU   C  3  125 ? 17.507  -84.229 -86.419  1.00 103.59 ? 125  LEU   C HD22 1 
ATOM   18066 H  HD23 . LEU   C  3  125 ? 17.447  -83.261 -85.161  1.00 103.59 ? 125  LEU   C HD23 1 
ATOM   18067 N  N    . THR   C  3  126 ? 22.474  -84.159 -84.051  1.00 89.78  ? 126  THR   C N    1 
ATOM   18068 C  CA   . THR   C  3  126 ? 23.396  -85.141 -83.490  1.00 90.64  ? 126  THR   C CA   1 
ATOM   18069 C  C    . THR   C  3  126 ? 23.206  -85.279 -81.986  1.00 87.07  ? 126  THR   C C    1 
ATOM   18070 O  O    . THR   C  3  126 ? 23.452  -86.352 -81.424  1.00 87.28  ? 126  THR   C O    1 
ATOM   18071 C  CB   . THR   C  3  126 ? 24.844  -84.757 -83.795  1.00 89.67  ? 126  THR   C CB   1 
ATOM   18072 O  OG1  . THR   C  3  126 ? 25.167  -83.529 -83.132  1.00 88.77  ? 126  THR   C OG1  1 
ATOM   18073 C  CG2  . THR   C  3  126 ? 25.052  -84.604 -85.292  1.00 89.35  ? 126  THR   C CG2  1 
ATOM   18074 H  H    . THR   C  3  126 ? 22.844  -83.461 -84.390  1.00 107.71 ? 126  THR   C H    1 
ATOM   18075 H  HA   . THR   C  3  126 ? 23.221  -85.998 -83.907  1.00 108.75 ? 126  THR   C HA   1 
ATOM   18076 H  HB   . THR   C  3  126 ? 25.438  -85.456 -83.479  1.00 107.59 ? 126  THR   C HB   1 
ATOM   18077 H  HG1  . THR   C  3  126 ? 24.592  -82.944 -83.313  1.00 106.50 ? 126  THR   C HG1  1 
ATOM   18078 H  HG21 . THR   C  3  126 ? 25.984  -84.412 -85.479  1.00 107.20 ? 126  THR   C HG21 1 
ATOM   18079 H  HG22 . THR   C  3  126 ? 24.801  -85.423 -85.747  1.00 107.20 ? 126  THR   C HG22 1 
ATOM   18080 H  HG23 . THR   C  3  126 ? 24.507  -83.876 -85.630  1.00 107.20 ? 126  THR   C HG23 1 
ATOM   18081 N  N    . SER   C  3  127 ? 22.777  -84.207 -81.318  1.00 86.35  ? 127  SER   C N    1 
ATOM   18082 C  CA   . SER   C  3  127 ? 22.490  -84.264 -79.892  1.00 90.79  ? 127  SER   C CA   1 
ATOM   18083 C  C    . SER   C  3  127 ? 21.204  -85.013 -79.585  1.00 92.11  ? 127  SER   C C    1 
ATOM   18084 O  O    . SER   C  3  127 ? 20.918  -85.263 -78.409  1.00 95.29  ? 127  SER   C O    1 
ATOM   18085 C  CB   . SER   C  3  127 ? 22.388  -82.848 -79.323  1.00 96.03  ? 127  SER   C CB   1 
ATOM   18086 O  OG   . SER   C  3  127 ? 23.501  -82.062 -79.705  1.00 101.29 ? 127  SER   C OG   1 
ATOM   18087 H  H    . SER   C  3  127 ? 22.645  -83.434 -81.672  1.00 103.60 ? 127  SER   C H    1 
ATOM   18088 H  HA   . SER   C  3  127 ? 23.223  -84.721 -79.450  1.00 108.93 ? 127  SER   C HA   1 
ATOM   18089 H  HB2  . SER   C  3  127 ? 21.579  -82.432 -79.660  1.00 115.22 ? 127  SER   C HB2  1 
ATOM   18090 H  HB3  . SER   C  3  127 ? 22.356  -82.900 -78.355  1.00 115.22 ? 127  SER   C HB3  1 
ATOM   18091 H  HG   . SER   C  3  127 ? 23.445  -81.859 -80.518  1.00 121.53 ? 127  SER   C HG   1 
ATOM   18092 N  N    . GLY   C  3  128 ? 20.430  -85.376 -80.603  1.00 91.30  ? 128  GLY   C N    1 
ATOM   18093 C  CA   . GLY   C  3  128 ? 19.073  -85.823 -80.381  1.00 92.68  ? 128  GLY   C CA   1 
ATOM   18094 C  C    . GLY   C  3  128 ? 18.183  -84.613 -80.187  1.00 92.29  ? 128  GLY   C C    1 
ATOM   18095 O  O    . GLY   C  3  128 ? 18.627  -83.601 -79.635  1.00 92.81  ? 128  GLY   C O    1 
ATOM   18096 H  H    . GLY   C  3  128 ? 20.673  -85.370 -81.428  1.00 109.55 ? 128  GLY   C H    1 
ATOM   18097 H  HA2  . GLY   C  3  128 ? 18.760  -86.332 -81.145  1.00 111.20 ? 128  GLY   C HA2  1 
ATOM   18098 H  HA3  . GLY   C  3  128 ? 19.030  -86.382 -79.589  1.00 111.20 ? 128  GLY   C HA3  1 
ATOM   18099 N  N    . GLY   C  3  129 ? 16.942  -84.696 -80.641  1.00 92.61  ? 129  GLY   C N    1 
ATOM   18100 C  CA   . GLY   C  3  129 ? 16.039  -83.557 -80.568  1.00 89.04  ? 129  GLY   C CA   1 
ATOM   18101 C  C    . GLY   C  3  129 ? 16.217  -82.629 -81.750  1.00 85.14  ? 129  GLY   C C    1 
ATOM   18102 O  O    . GLY   C  3  129 ? 17.293  -82.501 -82.320  1.00 80.48  ? 129  GLY   C O    1 
ATOM   18103 H  H    . GLY   C  3  129 ? 16.597  -85.399 -80.995  1.00 111.11 ? 129  GLY   C H    1 
ATOM   18104 H  HA2  . GLY   C  3  129 ? 15.121  -83.871 -80.558  1.00 106.83 ? 129  GLY   C HA2  1 
ATOM   18105 H  HA3  . GLY   C  3  129 ? 16.211  -83.058 -79.755  1.00 106.83 ? 129  GLY   C HA3  1 
ATOM   18106 N  N    . ALA   C  3  130 ? 15.119  -81.961 -82.128  1.00 87.41  ? 130  ALA   C N    1 
ATOM   18107 C  CA   . ALA   C  3  130 ? 15.121  -81.059 -83.274  1.00 85.84  ? 130  ALA   C CA   1 
ATOM   18108 C  C    . ALA   C  3  130 ? 14.190  -79.898 -82.972  1.00 84.04  ? 130  ALA   C C    1 
ATOM   18109 O  O    . ALA   C  3  130 ? 13.045  -80.113 -82.562  1.00 86.33  ? 130  ALA   C O    1 
ATOM   18110 C  CB   . ALA   C  3  130 ? 14.676  -81.783 -84.548  1.00 89.45  ? 130  ALA   C CB   1 
ATOM   18111 H  H    . ALA   C  3  130 ? 14.358  -82.017 -81.731  1.00 104.87 ? 130  ALA   C H    1 
ATOM   18112 H  HA   . ALA   C  3  130 ? 16.015  -80.712 -83.420  1.00 102.99 ? 130  ALA   C HA   1 
ATOM   18113 H  HB1  . ALA   C  3  130 ? 14.679  -81.154 -85.287  1.00 107.32 ? 130  ALA   C HB1  1 
ATOM   18114 H  HB2  . ALA   C  3  130 ? 15.292  -82.510 -84.731  1.00 107.32 ? 130  ALA   C HB2  1 
ATOM   18115 H  HB3  . ALA   C  3  130 ? 13.781  -82.134 -84.416  1.00 107.32 ? 130  ALA   C HB3  1 
ATOM   18116 N  N    . SER   C  3  131 ? 14.681  -78.679 -83.168  1.00 80.97  ? 131  SER   C N    1 
ATOM   18117 C  CA   . SER   C  3  131 ? 13.906  -77.469 -82.933  1.00 79.11  ? 131  SER   C CA   1 
ATOM   18118 C  C    . SER   C  3  131 ? 13.691  -76.755 -84.259  1.00 79.74  ? 131  SER   C C    1 
ATOM   18119 O  O    . SER   C  3  131 ? 14.658  -76.439 -84.962  1.00 81.51  ? 131  SER   C O    1 
ATOM   18120 C  CB   . SER   C  3  131 ? 14.616  -76.547 -81.941  1.00 77.62  ? 131  SER   C CB   1 
ATOM   18121 O  OG   . SER   C  3  131 ? 14.772  -77.174 -80.680  1.00 77.04  ? 131  SER   C OG   1 
ATOM   18122 H  H    . SER   C  3  131 ? 15.481  -78.525 -83.444  1.00 97.15  ? 131  SER   C H    1 
ATOM   18123 H  HA   . SER   C  3  131 ? 13.040  -77.707 -82.566  1.00 94.91  ? 131  SER   C HA   1 
ATOM   18124 H  HB2  . SER   C  3  131 ? 15.492  -76.324 -82.291  1.00 93.13  ? 131  SER   C HB2  1 
ATOM   18125 H  HB3  . SER   C  3  131 ? 14.088  -75.741 -81.828  1.00 93.13  ? 131  SER   C HB3  1 
ATOM   18126 H  HG   . SER   C  3  131 ? 15.079  -76.625 -80.122  1.00 92.43  ? 131  SER   C HG   1 
ATOM   18127 N  N    . VAL   C  3  132 ? 12.430  -76.510 -84.600  1.00 79.08  ? 132  VAL   C N    1 
ATOM   18128 C  CA   . VAL   C  3  132 ? 12.066  -75.700 -85.756  1.00 79.97  ? 132  VAL   C CA   1 
ATOM   18129 C  C    . VAL   C  3  132 ? 11.729  -74.307 -85.244  1.00 75.39  ? 132  VAL   C C    1 
ATOM   18130 O  O    . VAL   C  3  132 ? 10.829  -74.145 -84.412  1.00 74.01  ? 132  VAL   C O    1 
ATOM   18131 C  CB   . VAL   C  3  132 ? 10.885  -76.307 -86.529  1.00 87.00  ? 132  VAL   C CB   1 
ATOM   18132 C  CG1  . VAL   C  3  132 ? 10.738  -75.626 -87.884  1.00 90.17  ? 132  VAL   C CG1  1 
ATOM   18133 C  CG2  . VAL   C  3  132 ? 11.066  -77.807 -86.695  1.00 90.22  ? 132  VAL   C CG2  1 
ATOM   18134 H  H    . VAL   C  3  132 ? 11.751  -76.810 -84.165  1.00 94.88  ? 132  VAL   C H    1 
ATOM   18135 H  HA   . VAL   C  3  132 ? 12.820  -75.642 -86.363  1.00 95.94  ? 132  VAL   C HA   1 
ATOM   18136 H  HB   . VAL   C  3  132 ? 10.070  -76.161 -86.024  1.00 104.38 ? 132  VAL   C HB   1 
ATOM   18137 H  HG11 . VAL   C  3  132 ? 10.026  -76.061 -88.380  1.00 108.18 ? 132  VAL   C HG11 1 
ATOM   18138 H  HG12 . VAL   C  3  132 ? 10.521  -74.691 -87.746  1.00 108.18 ? 132  VAL   C HG12 1 
ATOM   18139 H  HG13 . VAL   C  3  132 ? 11.574  -75.703 -88.369  1.00 108.18 ? 132  VAL   C HG13 1 
ATOM   18140 H  HG21 . VAL   C  3  132 ? 10.331  -78.158 -87.222  1.00 108.24 ? 132  VAL   C HG21 1 
ATOM   18141 H  HG22 . VAL   C  3  132 ? 11.908  -77.976 -87.147  1.00 108.24 ? 132  VAL   C HG22 1 
ATOM   18142 H  HG23 . VAL   C  3  132 ? 11.072  -78.224 -85.818  1.00 108.24 ? 132  VAL   C HG23 1 
ATOM   18143 N  N    . VAL   C  3  133 ? 12.453  -73.305 -85.732  1.00 74.46  ? 133  VAL   C N    1 
ATOM   18144 C  CA   . VAL   C  3  133 ? 12.327  -71.931 -85.261  1.00 75.34  ? 133  VAL   C CA   1 
ATOM   18145 C  C    . VAL   C  3  133 ? 11.654  -71.103 -86.345  1.00 79.03  ? 133  VAL   C C    1 
ATOM   18146 O  O    . VAL   C  3  133 ? 11.967  -71.245 -87.533  1.00 83.76  ? 133  VAL   C O    1 
ATOM   18147 C  CB   . VAL   C  3  133 ? 13.701  -71.340 -84.890  1.00 74.51  ? 133  VAL   C CB   1 
ATOM   18148 C  CG1  . VAL   C  3  133 ? 13.580  -69.856 -84.570  1.00 75.33  ? 133  VAL   C CG1  1 
ATOM   18149 C  CG2  . VAL   C  3  133 ? 14.298  -72.094 -83.712  1.00 72.63  ? 133  VAL   C CG2  1 
ATOM   18150 H  H    . VAL   C  3  133 ? 13.039  -73.400 -86.354  1.00 89.33  ? 133  VAL   C H    1 
ATOM   18151 H  HA   . VAL   C  3  133 ? 11.763  -71.913 -84.473  1.00 90.39  ? 133  VAL   C HA   1 
ATOM   18152 H  HB   . VAL   C  3  133 ? 14.299  -71.435 -85.648  1.00 89.39  ? 133  VAL   C HB   1 
ATOM   18153 H  HG11 . VAL   C  3  133 ? 14.423  -69.541 -84.207  1.00 90.38  ? 133  VAL   C HG11 1 
ATOM   18154 H  HG12 . VAL   C  3  133 ? 13.370  -69.374 -85.385  1.00 90.38  ? 133  VAL   C HG12 1 
ATOM   18155 H  HG13 . VAL   C  3  133 ? 12.872  -69.730 -83.919  1.00 90.38  ? 133  VAL   C HG13 1 
ATOM   18156 H  HG21 . VAL   C  3  133 ? 15.251  -71.914 -83.672  1.00 87.14  ? 133  VAL   C HG21 1 
ATOM   18157 H  HG22 . VAL   C  3  133 ? 13.870  -71.793 -82.895  1.00 87.14  ? 133  VAL   C HG22 1 
ATOM   18158 H  HG23 . VAL   C  3  133 ? 14.146  -73.044 -83.835  1.00 87.14  ? 133  VAL   C HG23 1 
ATOM   18159 N  N    . CYS   C  3  134 ? 10.728  -70.239 -85.933  1.00 77.01  ? 134  CYS   C N    1 
ATOM   18160 C  CA   . CYS   C  3  134 ? 10.034  -69.336 -86.842  1.00 80.40  ? 134  CYS   C CA   1 
ATOM   18161 C  C    . CYS   C  3  134 ? 10.114  -67.924 -86.284  1.00 77.03  ? 134  CYS   C C    1 
ATOM   18162 O  O    . CYS   C  3  134 ? 9.607   -67.657 -85.189  1.00 74.41  ? 134  CYS   C O    1 
ATOM   18163 C  CB   . CYS   C  3  134 ? 8.573   -69.752 -87.034  1.00 89.60  ? 134  CYS   C CB   1 
ATOM   18164 S  SG   . CYS   C  3  134 ? 7.762   -68.976 -88.452  1.00 98.21  ? 134  CYS   C SG   1 
ATOM   18165 H  H    . CYS   C  3  134 ? 10.481  -70.158 -85.113  1.00 92.40  ? 134  CYS   C H    1 
ATOM   18166 H  HA   . CYS   C  3  134 ? 10.473  -69.351 -87.707  1.00 96.46  ? 134  CYS   C HA   1 
ATOM   18167 H  HB2  . CYS   C  3  134 ? 8.539   -70.713 -87.165  1.00 107.50 ? 134  CYS   C HB2  1 
ATOM   18168 H  HB3  . CYS   C  3  134 ? 8.074   -69.508 -86.239  1.00 107.50 ? 134  CYS   C HB3  1 
ATOM   18169 N  N    . PHE   C  3  135 ? 10.752  -67.027 -87.032  1.00 76.94  ? 135  PHE   C N    1 
ATOM   18170 C  CA   . PHE   C  3  135 ? 10.856  -65.621 -86.665  1.00 74.06  ? 135  PHE   C CA   1 
ATOM   18171 C  C    . PHE   C  3  135 ? 9.813   -64.824 -87.441  1.00 74.34  ? 135  PHE   C C    1 
ATOM   18172 O  O    . PHE   C  3  135 ? 9.827   -64.825 -88.676  1.00 75.04  ? 135  PHE   C O    1 
ATOM   18173 C  CB   . PHE   C  3  135 ? 12.253  -65.074 -86.962  1.00 74.35  ? 135  PHE   C CB   1 
ATOM   18174 C  CG   . PHE   C  3  135 ? 13.334  -65.631 -86.078  1.00 74.74  ? 135  PHE   C CG   1 
ATOM   18175 C  CD1  . PHE   C  3  135 ? 13.263  -65.501 -84.701  1.00 74.39  ? 135  PHE   C CD1  1 
ATOM   18176 C  CD2  . PHE   C  3  135 ? 14.439  -66.259 -86.629  1.00 74.63  ? 135  PHE   C CD2  1 
ATOM   18177 C  CE1  . PHE   C  3  135 ? 14.263  -66.005 -83.891  1.00 72.59  ? 135  PHE   C CE1  1 
ATOM   18178 C  CE2  . PHE   C  3  135 ? 15.442  -66.762 -85.825  1.00 74.13  ? 135  PHE   C CE2  1 
ATOM   18179 C  CZ   . PHE   C  3  135 ? 15.354  -66.634 -84.454  1.00 73.12  ? 135  PHE   C CZ   1 
ATOM   18180 H  H    . PHE   C  3  135 ? 11.142  -67.215 -87.775  1.00 92.31  ? 135  PHE   C H    1 
ATOM   18181 H  HA   . PHE   C  3  135 ? 10.681  -65.530 -85.715  1.00 88.85  ? 135  PHE   C HA   1 
ATOM   18182 H  HB2  . PHE   C  3  135 ? 12.482  -65.291 -87.879  1.00 89.21  ? 135  PHE   C HB2  1 
ATOM   18183 H  HB3  . PHE   C  3  135 ? 12.242  -64.112 -86.841  1.00 89.21  ? 135  PHE   C HB3  1 
ATOM   18184 H  HD1  . PHE   C  3  135 ? 12.534  -65.070 -84.317  1.00 89.25  ? 135  PHE   C HD1  1 
ATOM   18185 H  HD2  . PHE   C  3  135 ? 14.506  -66.342 -87.553  1.00 89.53  ? 135  PHE   C HD2  1 
ATOM   18186 H  HE1  . PHE   C  3  135 ? 14.201  -65.920 -82.967  1.00 87.09  ? 135  PHE   C HE1  1 
ATOM   18187 H  HE2  . PHE   C  3  135 ? 16.176  -67.186 -86.207  1.00 88.94  ? 135  PHE   C HE2  1 
ATOM   18188 H  HZ   . PHE   C  3  135 ? 16.030  -66.971 -83.910  1.00 87.72  ? 135  PHE   C HZ   1 
ATOM   18189 N  N    . LEU   C  3  136 ? 8.919   -64.146 -86.721  1.00 73.81  ? 136  LEU   C N    1 
ATOM   18190 C  CA   . LEU   C  3  136 ? 7.972   -63.199 -87.308  1.00 77.14  ? 136  LEU   C CA   1 
ATOM   18191 C  C    . LEU   C  3  136 ? 8.291   -61.822 -86.738  1.00 73.81  ? 136  LEU   C C    1 
ATOM   18192 O  O    . LEU   C  3  136 ? 7.994   -61.548 -85.570  1.00 72.79  ? 136  LEU   C O    1 
ATOM   18193 C  CB   . LEU   C  3  136 ? 6.522   -63.589 -87.014  1.00 81.97  ? 136  LEU   C CB   1 
ATOM   18194 C  CG   . LEU   C  3  136 ? 6.217   -64.804 -86.134  1.00 86.77  ? 136  LEU   C CG   1 
ATOM   18195 C  CD1  . LEU   C  3  136 ? 4.826   -64.670 -85.526  1.00 91.06  ? 136  LEU   C CD1  1 
ATOM   18196 C  CD2  . LEU   C  3  136 ? 6.314   -66.102 -86.921  1.00 90.29  ? 136  LEU   C CD2  1 
ATOM   18197 H  H    . LEU   C  3  136 ? 8.841   -64.220 -85.868  1.00 88.56  ? 136  LEU   C H    1 
ATOM   18198 H  HA   . LEU   C  3  136 ? 8.085   -63.186 -88.271  1.00 92.55  ? 136  LEU   C HA   1 
ATOM   18199 H  HB2  . LEU   C  3  136 ? 6.104   -62.829 -86.579  1.00 98.35  ? 136  LEU   C HB2  1 
ATOM   18200 H  HB3  . LEU   C  3  136 ? 6.093   -63.760 -87.867  1.00 98.35  ? 136  LEU   C HB3  1 
ATOM   18201 H  HG   . LEU   C  3  136 ? 6.876   -64.841 -85.423  1.00 104.11 ? 136  LEU   C HG   1 
ATOM   18202 H  HD11 . LEU   C  3  136 ? 4.796   -65.165 -84.693  1.00 109.25 ? 136  LEU   C HD11 1 
ATOM   18203 H  HD12 . LEU   C  3  136 ? 4.642   -63.732 -85.361  1.00 109.25 ? 136  LEU   C HD12 1 
ATOM   18204 H  HD13 . LEU   C  3  136 ? 4.174   -65.030 -86.148  1.00 109.25 ? 136  LEU   C HD13 1 
ATOM   18205 H  HD21 . LEU   C  3  136 ? 5.866   -66.806 -86.425  1.00 108.32 ? 136  LEU   C HD21 1 
ATOM   18206 H  HD22 . LEU   C  3  136 ? 5.886   -65.982 -87.783  1.00 108.32 ? 136  LEU   C HD22 1 
ATOM   18207 H  HD23 . LEU   C  3  136 ? 7.249   -66.328 -87.044  1.00 108.32 ? 136  LEU   C HD23 1 
ATOM   18208 N  N    . ASN   C  3  137 ? 8.882   -60.953 -87.558  1.00 73.02  ? 137  ASN   C N    1 
ATOM   18209 C  CA   . ASN   C  3  137 ? 9.467   -59.711 -87.079  1.00 73.16  ? 137  ASN   C CA   1 
ATOM   18210 C  C    . ASN   C  3  137 ? 8.778   -58.492 -87.680  1.00 74.30  ? 137  ASN   C C    1 
ATOM   18211 O  O    . ASN   C  3  137 ? 8.168   -58.552 -88.751  1.00 74.58  ? 137  ASN   C O    1 
ATOM   18212 C  CB   . ASN   C  3  137 ? 10.966  -59.643 -87.413  1.00 72.94  ? 137  ASN   C CB   1 
ATOM   18213 C  CG   . ASN   C  3  137 ? 11.714  -60.891 -86.999  1.00 72.32  ? 137  ASN   C CG   1 
ATOM   18214 O  OD1  . ASN   C  3  137 ? 11.476  -61.446 -85.926  1.00 70.29  ? 137  ASN   C OD1  1 
ATOM   18215 N  ND2  . ASN   C  3  137 ? 12.626  -61.344 -87.854  1.00 74.08  ? 137  ASN   C ND2  1 
ATOM   18216 H  H    . ASN   C  3  137 ? 8.955   -61.067 -88.407  1.00 87.61  ? 137  ASN   C H    1 
ATOM   18217 H  HA   . ASN   C  3  137 ? 9.342   -59.675 -86.118  1.00 87.77  ? 137  ASN   C HA   1 
ATOM   18218 H  HB2  . ASN   C  3  137 ? 11.072  -59.534 -88.371  1.00 87.51  ? 137  ASN   C HB2  1 
ATOM   18219 H  HB3  . ASN   C  3  137 ? 11.360  -58.889 -86.947  1.00 87.51  ? 137  ASN   C HB3  1 
ATOM   18220 H  HD21 . ASN   C  3  137 ? 13.078  -62.050 -87.666  1.00 88.88  ? 137  ASN   C HD21 1 
ATOM   18221 H  HD22 . ASN   C  3  137 ? 12.762  -60.930 -88.595  1.00 88.88  ? 137  ASN   C HD22 1 
ATOM   18222 N  N    . ASN   C  3  138 ? 8.899   -57.376 -86.962  1.00 76.37  ? 138  ASN   C N    1 
ATOM   18223 C  CA   . ASN   C  3  138 ? 8.555   -56.043 -87.457  1.00 80.68  ? 138  ASN   C CA   1 
ATOM   18224 C  C    . ASN   C  3  138 ? 7.126   -56.000 -88.006  1.00 87.24  ? 138  ASN   C C    1 
ATOM   18225 O  O    . ASN   C  3  138 ? 6.880   -55.806 -89.197  1.00 94.89  ? 138  ASN   C O    1 
ATOM   18226 C  CB   . ASN   C  3  138 ? 9.576   -55.595 -88.508  1.00 78.66  ? 138  ASN   C CB   1 
ATOM   18227 C  CG   . ASN   C  3  138 ? 10.999  -55.606 -87.976  1.00 76.35  ? 138  ASN   C CG   1 
ATOM   18228 O  OD1  . ASN   C  3  138 ? 11.720  -56.594 -88.118  1.00 74.64  ? 138  ASN   C OD1  1 
ATOM   18229 N  ND2  . ASN   C  3  138 ? 11.408  -54.506 -87.354  1.00 78.44  ? 138  ASN   C ND2  1 
ATOM   18230 H  H    . ASN   C  3  138 ? 9.190   -57.364 -86.152  1.00 91.63  ? 138  ASN   C H    1 
ATOM   18231 H  HA   . ASN   C  3  138 ? 8.585   -55.425 -86.711  1.00 96.79  ? 138  ASN   C HA   1 
ATOM   18232 H  HB2  . ASN   C  3  138 ? 9.534   -56.196 -89.268  1.00 94.37  ? 138  ASN   C HB2  1 
ATOM   18233 H  HB3  . ASN   C  3  138 ? 9.366   -54.690 -88.788  1.00 94.37  ? 138  ASN   C HB3  1 
ATOM   18234 H  HD21 . ASN   C  3  138 ? 12.205  -54.464 -87.035  1.00 94.10  ? 138  ASN   C HD21 1 
ATOM   18235 H  HD22 . ASN   C  3  138 ? 10.874  -53.837 -87.270  1.00 94.10  ? 138  ASN   C HD22 1 
ATOM   18236 N  N    . PHE   C  3  139 ? 6.182   -56.187 -87.086  1.00 85.83  ? 139  PHE   C N    1 
ATOM   18237 C  CA   . PHE   C  3  139 ? 4.763   -56.114 -87.398  1.00 85.40  ? 139  PHE   C CA   1 
ATOM   18238 C  C    . PHE   C  3  139 ? 4.058   -55.211 -86.396  1.00 83.30  ? 139  PHE   C C    1 
ATOM   18239 O  O    . PHE   C  3  139 ? 4.473   -55.093 -85.240  1.00 81.85  ? 139  PHE   C O    1 
ATOM   18240 C  CB   . PHE   C  3  139 ? 4.114   -57.504 -87.388  1.00 85.31  ? 139  PHE   C CB   1 
ATOM   18241 C  CG   . PHE   C  3  139 ? 4.245   -58.228 -86.078  1.00 82.61  ? 139  PHE   C CG   1 
ATOM   18242 C  CD1  . PHE   C  3  139 ? 3.263   -58.116 -85.106  1.00 80.80  ? 139  PHE   C CD1  1 
ATOM   18243 C  CD2  . PHE   C  3  139 ? 5.348   -59.026 -85.820  1.00 81.10  ? 139  PHE   C CD2  1 
ATOM   18244 C  CE1  . PHE   C  3  139 ? 3.381   -58.784 -83.903  1.00 78.71  ? 139  PHE   C CE1  1 
ATOM   18245 C  CE2  . PHE   C  3  139 ? 5.472   -59.696 -84.618  1.00 77.30  ? 139  PHE   C CE2  1 
ATOM   18246 C  CZ   . PHE   C  3  139 ? 4.488   -59.575 -83.658  1.00 77.37  ? 139  PHE   C CZ   1 
ATOM   18247 H  H    . PHE   C  3  139 ? 6.345   -56.361 -86.260  1.00 102.97 ? 139  PHE   C H    1 
ATOM   18248 H  HA   . PHE   C  3  139 ? 4.649   -55.729 -88.281  1.00 102.46 ? 139  PHE   C HA   1 
ATOM   18249 H  HB2  . PHE   C  3  139 ? 3.167   -57.407 -87.578  1.00 102.35 ? 139  PHE   C HB2  1 
ATOM   18250 H  HB3  . PHE   C  3  139 ? 4.535   -58.049 -88.071  1.00 102.35 ? 139  PHE   C HB3  1 
ATOM   18251 H  HD1  . PHE   C  3  139 ? 2.516   -57.586 -85.267  1.00 96.94  ? 139  PHE   C HD1  1 
ATOM   18252 H  HD2  . PHE   C  3  139 ? 6.014   -59.111 -86.464  1.00 97.30  ? 139  PHE   C HD2  1 
ATOM   18253 H  HE1  . PHE   C  3  139 ? 2.716   -58.701 -83.257  1.00 94.43  ? 139  PHE   C HE1  1 
ATOM   18254 H  HE2  . PHE   C  3  139 ? 6.217   -60.228 -84.456  1.00 92.74  ? 139  PHE   C HE2  1 
ATOM   18255 H  HZ   . PHE   C  3  139 ? 4.569   -60.025 -82.849  1.00 92.82  ? 139  PHE   C HZ   1 
ATOM   18256 N  N    . TYR   C  3  140 ? 2.985   -54.568 -86.859  1.00 85.44  ? 140  TYR   C N    1 
ATOM   18257 C  CA   . TYR   C  3  140 ? 2.122   -53.746 -86.023  1.00 85.64  ? 140  TYR   C CA   1 
ATOM   18258 C  C    . TYR   C  3  140 ? 0.683   -54.005 -86.449  1.00 89.23  ? 140  TYR   C C    1 
ATOM   18259 O  O    . TYR   C  3  140 ? 0.412   -54.136 -87.652  1.00 96.84  ? 140  TYR   C O    1 
ATOM   18260 C  CB   . TYR   C  3  140 ? 2.441   -52.249 -86.152  1.00 83.21  ? 140  TYR   C CB   1 
ATOM   18261 C  CG   . TYR   C  3  140 ? 1.689   -51.388 -85.162  1.00 82.65  ? 140  TYR   C CG   1 
ATOM   18262 C  CD1  . TYR   C  3  140 ? 0.427   -50.890 -85.461  1.00 85.13  ? 140  TYR   C CD1  1 
ATOM   18263 C  CD2  . TYR   C  3  140 ? 2.236   -51.084 -83.921  1.00 81.18  ? 140  TYR   C CD2  1 
ATOM   18264 C  CE1  . TYR   C  3  140 ? -0.267  -50.108 -84.555  1.00 89.15  ? 140  TYR   C CE1  1 
ATOM   18265 C  CE2  . TYR   C  3  140 ? 1.550   -50.304 -83.009  1.00 85.36  ? 140  TYR   C CE2  1 
ATOM   18266 C  CZ   . TYR   C  3  140 ? 0.300   -49.819 -83.331  1.00 90.99  ? 140  TYR   C CZ   1 
ATOM   18267 O  OH   . TYR   C  3  140 ? -0.384  -49.041 -82.425  1.00 96.68  ? 140  TYR   C OH   1 
ATOM   18268 H  H    . TYR   C  3  140 ? 2.732   -54.597 -87.680  1.00 102.51 ? 140  TYR   C H    1 
ATOM   18269 H  HA   . TYR   C  3  140 ? 2.236   -53.989 -85.091  1.00 102.74 ? 140  TYR   C HA   1 
ATOM   18270 H  HB2  . TYR   C  3  140 ? 3.390   -52.117 -86.001  1.00 99.84  ? 140  TYR   C HB2  1 
ATOM   18271 H  HB3  . TYR   C  3  140 ? 2.203   -51.954 -87.045  1.00 99.84  ? 140  TYR   C HB3  1 
ATOM   18272 H  HD1  . TYR   C  3  140 ? 0.041   -51.086 -86.284  1.00 102.13 ? 140  TYR   C HD1  1 
ATOM   18273 H  HD2  . TYR   C  3  140 ? 3.077   -51.412 -83.700  1.00 97.40  ? 140  TYR   C HD2  1 
ATOM   18274 H  HE1  . TYR   C  3  140 ? -1.110  -49.780 -84.769  1.00 106.96 ? 140  TYR   C HE1  1 
ATOM   18275 H  HE2  . TYR   C  3  140 ? 1.930   -50.106 -82.184  1.00 102.41 ? 140  TYR   C HE2  1 
ATOM   18276 H  HH   . TYR   C  3  140 ? 0.067   -48.956 -81.721  1.00 116.00 ? 140  TYR   C HH   1 
ATOM   18277 N  N    . PRO   C  3  141 ? -0.268  -54.086 -85.499  1.00 83.02  ? 141  PRO   C N    1 
ATOM   18278 C  CA   . PRO   C  3  141 ? -0.147  -53.971 -84.038  1.00 81.20  ? 141  PRO   C CA   1 
ATOM   18279 C  C    . PRO   C  3  141 ? 0.531   -55.177 -83.388  1.00 82.49  ? 141  PRO   C C    1 
ATOM   18280 O  O    . PRO   C  3  141 ? 1.180   -55.969 -84.073  1.00 84.01  ? 141  PRO   C O    1 
ATOM   18281 C  CB   . PRO   C  3  141 ? -1.609  -53.857 -83.568  1.00 81.99  ? 141  PRO   C CB   1 
ATOM   18282 C  CG   . PRO   C  3  141 ? -2.408  -53.557 -84.797  1.00 85.11  ? 141  PRO   C CG   1 
ATOM   18283 C  CD   . PRO   C  3  141 ? -1.673  -54.216 -85.913  1.00 83.16  ? 141  PRO   C CD   1 
ATOM   18284 H  HA   . PRO   C  3  141 ? 0.340   -53.166 -83.805  1.00 97.42  ? 141  PRO   C HA   1 
ATOM   18285 H  HB2  . PRO   C  3  141 ? -1.891  -54.696 -83.170  1.00 98.37  ? 141  PRO   C HB2  1 
ATOM   18286 H  HB3  . PRO   C  3  141 ? -1.689  -53.139 -82.921  1.00 98.37  ? 141  PRO   C HB3  1 
ATOM   18287 H  HG2  . PRO   C  3  141 ? -3.301  -53.924 -84.707  1.00 102.12 ? 141  PRO   C HG2  1 
ATOM   18288 H  HG3  . PRO   C  3  141 ? -2.455  -52.598 -84.933  1.00 102.12 ? 141  PRO   C HG3  1 
ATOM   18289 H  HD2  . PRO   C  3  141 ? -1.927  -55.149 -85.993  1.00 99.77  ? 141  PRO   C HD2  1 
ATOM   18290 H  HD3  . PRO   C  3  141 ? -1.832  -53.756 -86.752  1.00 99.77  ? 141  PRO   C HD3  1 
ATOM   18291 N  N    . LYS   C  3  142 ? 0.374   -55.308 -82.068  1.00 83.03  ? 142  LYS   C N    1 
ATOM   18292 C  CA   . LYS   C  3  142 ? 1.078   -56.352 -81.333  1.00 83.94  ? 142  LYS   C CA   1 
ATOM   18293 C  C    . LYS   C  3  142 ? 0.384   -57.705 -81.431  1.00 89.39  ? 142  LYS   C C    1 
ATOM   18294 O  O    . LYS   C  3  142 ? 1.059   -58.741 -81.433  1.00 91.94  ? 142  LYS   C O    1 
ATOM   18295 C  CB   . LYS   C  3  142 ? 1.217   -55.955 -79.861  1.00 89.78  ? 142  LYS   C CB   1 
ATOM   18296 C  CG   . LYS   C  3  142 ? 1.971   -56.975 -79.022  1.00 99.59  ? 142  LYS   C CG   1 
ATOM   18297 C  CD   . LYS   C  3  142 ? 2.056   -56.566 -77.561  1.00 108.69 ? 142  LYS   C CD   1 
ATOM   18298 C  CE   . LYS   C  3  142 ? 2.788   -57.619 -76.745  1.00 111.76 ? 142  LYS   C CE   1 
ATOM   18299 N  NZ   . LYS   C  3  142 ? 2.921   -57.234 -75.314  1.00 114.64 ? 142  LYS   C NZ   1 
ATOM   18300 H  H    . LYS   C  3  142 ? -0.130  -54.809 -81.582  1.00 99.61  ? 142  LYS   C H    1 
ATOM   18301 H  HA   . LYS   C  3  142 ? 1.965   -56.444 -81.713  1.00 100.71 ? 142  LYS   C HA   1 
ATOM   18302 H  HB2  . LYS   C  3  142 ? 1.698   -55.114 -79.808  1.00 107.72 ? 142  LYS   C HB2  1 
ATOM   18303 H  HB3  . LYS   C  3  142 ? 0.331   -55.855 -79.479  1.00 107.72 ? 142  LYS   C HB3  1 
ATOM   18304 H  HG2  . LYS   C  3  142 ? 1.513   -57.829 -79.070  1.00 119.49 ? 142  LYS   C HG2  1 
ATOM   18305 H  HG3  . LYS   C  3  142 ? 2.875   -57.064 -79.363  1.00 119.49 ? 142  LYS   C HG3  1 
ATOM   18306 H  HD2  . LYS   C  3  142 ? 2.539   -55.728 -77.487  1.00 130.41 ? 142  LYS   C HD2  1 
ATOM   18307 H  HD3  . LYS   C  3  142 ? 1.161   -56.465 -77.201  1.00 130.41 ? 142  LYS   C HD3  1 
ATOM   18308 H  HE2  . LYS   C  3  142 ? 2.296   -58.454 -76.788  1.00 134.09 ? 142  LYS   C HE2  1 
ATOM   18309 H  HE3  . LYS   C  3  142 ? 3.679   -57.740 -77.108  1.00 134.09 ? 142  LYS   C HE3  1 
ATOM   18310 H  HZ1  . LYS   C  3  142 ? 3.350   -57.871 -74.865  1.00 137.55 ? 142  LYS   C HZ1  1 
ATOM   18311 H  HZ2  . LYS   C  3  142 ? 3.378   -56.473 -75.244  1.00 137.55 ? 142  LYS   C HZ2  1 
ATOM   18312 H  HZ3  . LYS   C  3  142 ? 2.115   -57.120 -74.954  1.00 137.55 ? 142  LYS   C HZ3  1 
ATOM   18313 N  N    . ASP   C  3  143 ? -0.944  -57.724 -81.506  1.00 93.48  ? 143  ASP   C N    1 
ATOM   18314 C  CA   . ASP   C  3  143 ? -1.676  -58.983 -81.459  1.00 94.15  ? 143  ASP   C CA   1 
ATOM   18315 C  C    . ASP   C  3  143 ? -1.364  -59.835 -82.684  1.00 93.28  ? 143  ASP   C C    1 
ATOM   18316 O  O    . ASP   C  3  143 ? -1.424  -59.358 -83.821  1.00 92.64  ? 143  ASP   C O    1 
ATOM   18317 C  CB   . ASP   C  3  143 ? -3.175  -58.714 -81.362  1.00 96.83  ? 143  ASP   C CB   1 
ATOM   18318 C  CG   . ASP   C  3  143 ? -3.562  -58.045 -80.058  1.00 98.66  ? 143  ASP   C CG   1 
ATOM   18319 O  OD1  . ASP   C  3  143 ? -2.901  -58.311 -79.032  1.00 97.51  ? 143  ASP   C OD1  1 
ATOM   18320 O  OD2  . ASP   C  3  143 ? -4.526  -57.252 -80.060  1.00 102.52 ? 143  ASP   C OD2  1 
ATOM   18321 H  H    . ASP   C  3  143 ? -1.440  -57.026 -81.585  1.00 112.15 ? 143  ASP   C H    1 
ATOM   18322 H  HA   . ASP   C  3  143 ? -1.403  -59.482 -80.673  1.00 112.97 ? 143  ASP   C HA   1 
ATOM   18323 H  HB2  . ASP   C  3  143 ? -3.441  -58.130 -82.090  1.00 116.17 ? 143  ASP   C HB2  1 
ATOM   18324 H  HB3  . ASP   C  3  143 ? -3.653  -59.556 -81.421  1.00 116.17 ? 143  ASP   C HB3  1 
ATOM   18325 N  N    . ILE   C  3  144 ? -1.032  -61.102 -82.445  1.00 93.26  ? 144  ILE   C N    1 
ATOM   18326 C  CA   . ILE   C  3  144 ? -0.670  -62.028 -83.512  1.00 92.10  ? 144  ILE   C CA   1 
ATOM   18327 C  C    . ILE   C  3  144 ? -0.728  -63.439 -82.945  1.00 93.14  ? 144  ILE   C C    1 
ATOM   18328 O  O    . ILE   C  3  144 ? -0.398  -63.667 -81.778  1.00 92.60  ? 144  ILE   C O    1 
ATOM   18329 C  CB   . ILE   C  3  144 ? 0.730   -61.699 -84.084  1.00 89.22  ? 144  ILE   C CB   1 
ATOM   18330 C  CG1  . ILE   C  3  144 ? 0.999   -62.512 -85.353  1.00 90.63  ? 144  ILE   C CG1  1 
ATOM   18331 C  CG2  . ILE   C  3  144 ? 1.808   -61.974 -83.040  1.00 84.43  ? 144  ILE   C CG2  1 
ATOM   18332 C  CD1  . ILE   C  3  144 ? 2.266   -62.105 -86.082  1.00 87.42  ? 144  ILE   C CD1  1 
ATOM   18333 H  H    . ILE   C  3  144 ? -1.009  -61.453 -81.660  1.00 111.89 ? 144  ILE   C H    1 
ATOM   18334 H  HA   . ILE   C  3  144 ? -1.317  -61.959 -84.230  1.00 110.50 ? 144  ILE   C HA   1 
ATOM   18335 H  HB   . ILE   C  3  144 ? 0.750   -60.757 -84.314  1.00 107.04 ? 144  ILE   C HB   1 
ATOM   18336 H  HG12 . ILE   C  3  144 ? 1.083   -63.448 -85.112  1.00 108.74 ? 144  ILE   C HG12 1 
ATOM   18337 H  HG13 . ILE   C  3  144 ? 0.254   -62.393 -85.963  1.00 108.74 ? 144  ILE   C HG13 1 
ATOM   18338 H  HG21 . ILE   C  3  144 ? 2.655   -61.631 -83.364  1.00 101.30 ? 144  ILE   C HG21 1 
ATOM   18339 H  HG22 . ILE   C  3  144 ? 1.566   -61.531 -82.212  1.00 101.30 ? 144  ILE   C HG22 1 
ATOM   18340 H  HG23 . ILE   C  3  144 ? 1.871   -62.931 -82.897  1.00 101.30 ? 144  ILE   C HG23 1 
ATOM   18341 H  HD11 . ILE   C  3  144 ? 2.370   -62.661 -86.870  1.00 104.89 ? 144  ILE   C HD11 1 
ATOM   18342 H  HD12 . ILE   C  3  144 ? 2.196   -61.173 -86.342  1.00 104.89 ? 144  ILE   C HD12 1 
ATOM   18343 H  HD13 . ILE   C  3  144 ? 3.025   -62.226 -85.489  1.00 104.89 ? 144  ILE   C HD13 1 
ATOM   18344 N  N    . ASN   C  3  145 ? -1.150  -64.387 -83.779  1.00 96.35  ? 145  ASN   C N    1 
ATOM   18345 C  CA   . ASN   C  3  145 ? -1.211  -65.791 -83.404  1.00 98.59  ? 145  ASN   C CA   1 
ATOM   18346 C  C    . ASN   C  3  145 ? -0.371  -66.627 -84.359  1.00 95.69  ? 145  ASN   C C    1 
ATOM   18347 O  O    . ASN   C  3  145 ? -0.203  -66.283 -85.533  1.00 94.45  ? 145  ASN   C O    1 
ATOM   18348 C  CB   . ASN   C  3  145 ? -2.651  -66.318 -83.402  1.00 109.00 ? 145  ASN   C CB   1 
ATOM   18349 C  CG   . ASN   C  3  145 ? -3.361  -66.069 -82.087  1.00 117.13 ? 145  ASN   C CG   1 
ATOM   18350 O  OD1  . ASN   C  3  145 ? -3.119  -66.757 -81.095  1.00 115.09 ? 145  ASN   C OD1  1 
ATOM   18351 N  ND2  . ASN   C  3  145 ? -4.253  -65.087 -82.075  1.00 125.75 ? 145  ASN   C ND2  1 
ATOM   18352 H  H    . ASN   C  3  145 ? -1.412  -64.234 -84.584  1.00 115.60 ? 145  ASN   C H    1 
ATOM   18353 H  HA   . ASN   C  3  145 ? -0.849  -65.890 -82.509  1.00 118.29 ? 145  ASN   C HA   1 
ATOM   18354 H  HB2  . ASN   C  3  145 ? -3.153  -65.873 -84.103  1.00 130.78 ? 145  ASN   C HB2  1 
ATOM   18355 H  HB3  . ASN   C  3  145 ? -2.639  -67.275 -83.559  1.00 130.78 ? 145  ASN   C HB3  1 
ATOM   18356 H  HD21 . ASN   C  3  145 ? -4.683  -64.906 -81.352  1.00 150.88 ? 145  ASN   C HD21 1 
ATOM   18357 H  HD22 . ASN   C  3  145 ? -4.402  -64.632 -82.789  1.00 150.88 ? 145  ASN   C HD22 1 
ATOM   18358 N  N    . VAL   C  3  146 ? 0.148   -67.738 -83.840  1.00 97.17  ? 146  VAL   C N    1 
ATOM   18359 C  CA   . VAL   C  3  146 ? 0.974   -68.662 -84.605  1.00 99.39  ? 146  VAL   C CA   1 
ATOM   18360 C  C    . VAL   C  3  146 ? 0.444   -70.073 -84.401  1.00 108.54 ? 146  VAL   C C    1 
ATOM   18361 O  O    . VAL   C  3  146 ? 0.066   -70.451 -83.286  1.00 112.35 ? 146  VAL   C O    1 
ATOM   18362 C  CB   . VAL   C  3  146 ? 2.459   -68.575 -84.193  1.00 92.79  ? 146  VAL   C CB   1 
ATOM   18363 C  CG1  . VAL   C  3  146 ? 3.033   -67.221 -84.574  1.00 89.48  ? 146  VAL   C CG1  1 
ATOM   18364 C  CG2  . VAL   C  3  146 ? 2.617   -68.821 -82.699  1.00 91.87  ? 146  VAL   C CG2  1 
ATOM   18365 H  H    . VAL   C  3  146 ? 0.031   -67.982 -83.024  1.00 116.58 ? 146  VAL   C H    1 
ATOM   18366 H  HA   . VAL   C  3  146 ? 0.906   -68.444 -85.548  1.00 119.25 ? 146  VAL   C HA   1 
ATOM   18367 H  HB   . VAL   C  3  146 ? 2.956   -69.261 -84.665  1.00 111.33 ? 146  VAL   C HB   1 
ATOM   18368 H  HG11 . VAL   C  3  146 ? 3.964   -67.185 -84.302  1.00 107.36 ? 146  VAL   C HG11 1 
ATOM   18369 H  HG12 . VAL   C  3  146 ? 2.965   -67.108 -85.535  1.00 107.36 ? 146  VAL   C HG12 1 
ATOM   18370 H  HG13 . VAL   C  3  146 ? 2.529   -66.526 -84.123  1.00 107.36 ? 146  VAL   C HG13 1 
ATOM   18371 H  HG21 . VAL   C  3  146 ? 3.553   -68.735 -82.462  1.00 110.22 ? 146  VAL   C HG21 1 
ATOM   18372 H  HG22 . VAL   C  3  146 ? 2.091   -68.166 -82.213  1.00 110.22 ? 146  VAL   C HG22 1 
ATOM   18373 H  HG23 . VAL   C  3  146 ? 2.303   -69.715 -82.491  1.00 110.22 ? 146  VAL   C HG23 1 
ATOM   18374 N  N    . LYS   C  3  147 ? 0.412   -70.849 -85.482  1.00 112.48 ? 147  LYS   C N    1 
ATOM   18375 C  CA   . LYS   C  3  147 ? -0.011  -72.242 -85.444  1.00 113.51 ? 147  LYS   C CA   1 
ATOM   18376 C  C    . LYS   C  3  147 ? 1.026   -73.087 -86.166  1.00 110.94 ? 147  LYS   C C    1 
ATOM   18377 O  O    . LYS   C  3  147 ? 1.439   -72.748 -87.280  1.00 112.92 ? 147  LYS   C O    1 
ATOM   18378 C  CB   . LYS   C  3  147 ? -1.387  -72.426 -86.092  1.00 118.44 ? 147  LYS   C CB   1 
ATOM   18379 C  CG   . LYS   C  3  147 ? -2.522  -71.744 -85.348  1.00 120.86 ? 147  LYS   C CG   1 
ATOM   18380 C  CD   . LYS   C  3  147 ? -3.847  -71.942 -86.065  1.00 126.93 ? 147  LYS   C CD   1 
ATOM   18381 C  CE   . LYS   C  3  147 ? -4.988  -71.286 -85.308  1.00 128.65 ? 147  LYS   C CE   1 
ATOM   18382 N  NZ   . LYS   C  3  147 ? -6.292  -71.453 -86.007  1.00 134.10 ? 147  LYS   C NZ   1 
ATOM   18383 H  H    . LYS   C  3  147 ? 0.637   -70.583 -86.268  1.00 134.96 ? 147  LYS   C H    1 
ATOM   18384 H  HA   . LYS   C  3  147 ? -0.070  -72.541 -84.523  1.00 136.19 ? 147  LYS   C HA   1 
ATOM   18385 H  HB2  . LYS   C  3  147 ? -1.360  -72.056 -86.989  1.00 142.11 ? 147  LYS   C HB2  1 
ATOM   18386 H  HB3  . LYS   C  3  147 ? -1.588  -73.374 -86.130  1.00 142.11 ? 147  LYS   C HB3  1 
ATOM   18387 H  HG2  . LYS   C  3  147 ? -2.596  -72.121 -84.457  1.00 145.01 ? 147  LYS   C HG2  1 
ATOM   18388 H  HG3  . LYS   C  3  147 ? -2.344  -70.792 -85.291  1.00 145.01 ? 147  LYS   C HG3  1 
ATOM   18389 H  HD2  . LYS   C  3  147 ? -3.798  -71.545 -86.948  1.00 152.30 ? 147  LYS   C HD2  1 
ATOM   18390 H  HD3  . LYS   C  3  147 ? -4.035  -72.891 -86.138  1.00 152.30 ? 147  LYS   C HD3  1 
ATOM   18391 H  HE2  . LYS   C  3  147 ? -5.062  -71.690 -84.429  1.00 154.36 ? 147  LYS   C HE2  1 
ATOM   18392 H  HE3  . LYS   C  3  147 ? -4.810  -70.337 -85.222  1.00 154.36 ? 147  LYS   C HE3  1 
ATOM   18393 H  HZ1  . LYS   C  3  147 ? -6.948  -71.109 -85.514  1.00 160.90 ? 147  LYS   C HZ1  1 
ATOM   18394 H  HZ2  . LYS   C  3  147 ? -6.272  -71.036 -86.793  1.00 160.90 ? 147  LYS   C HZ2  1 
ATOM   18395 H  HZ3  . LYS   C  3  147 ? -6.456  -72.318 -86.143  1.00 160.90 ? 147  LYS   C HZ3  1 
ATOM   18396 N  N    . TRP   C  3  148 ? 1.446   -74.178 -85.533  1.00 106.76 ? 148  TRP   C N    1 
ATOM   18397 C  CA   . TRP   C  3  148 ? 2.429   -75.089 -86.104  1.00 104.63 ? 148  TRP   C CA   1 
ATOM   18398 C  C    . TRP   C  3  148 ? 1.705   -76.253 -86.771  1.00 111.43 ? 148  TRP   C C    1 
ATOM   18399 O  O    . TRP   C  3  148 ? 0.955   -76.982 -86.112  1.00 112.68 ? 148  TRP   C O    1 
ATOM   18400 C  CB   . TRP   C  3  148 ? 3.389   -75.601 -85.030  1.00 98.47  ? 148  TRP   C CB   1 
ATOM   18401 C  CG   . TRP   C  3  148 ? 4.472   -74.628 -84.662  1.00 91.80  ? 148  TRP   C CG   1 
ATOM   18402 C  CD1  . TRP   C  3  148 ? 4.519   -73.827 -83.556  1.00 89.08  ? 148  TRP   C CD1  1 
ATOM   18403 C  CD2  . TRP   C  3  148 ? 5.669   -74.357 -85.403  1.00 87.98  ? 148  TRP   C CD2  1 
ATOM   18404 N  NE1  . TRP   C  3  148 ? 5.669   -73.075 -83.564  1.00 84.95  ? 148  TRP   C NE1  1 
ATOM   18405 C  CE2  . TRP   C  3  148 ? 6.392   -73.381 -84.687  1.00 84.54  ? 148  TRP   C CE2  1 
ATOM   18406 C  CE3  . TRP   C  3  148 ? 6.199   -74.844 -86.602  1.00 88.08  ? 148  TRP   C CE3  1 
ATOM   18407 C  CZ2  . TRP   C  3  148 ? 7.615   -72.884 -85.130  1.00 80.32  ? 148  TRP   C CZ2  1 
ATOM   18408 C  CZ3  . TRP   C  3  148 ? 7.414   -74.348 -87.041  1.00 85.55  ? 148  TRP   C CZ3  1 
ATOM   18409 C  CH2  . TRP   C  3  148 ? 8.108   -73.378 -86.306  1.00 80.84  ? 148  TRP   C CH2  1 
ATOM   18410 H  H    . TRP   C  3  148 ? 1.169   -74.416 -84.754  1.00 128.09 ? 148  TRP   C H    1 
ATOM   18411 H  HA   . TRP   C  3  148 ? 2.945   -74.621 -86.778  1.00 125.54 ? 148  TRP   C HA   1 
ATOM   18412 H  HB2  . TRP   C  3  148 ? 2.882   -75.795 -84.226  1.00 118.14 ? 148  TRP   C HB2  1 
ATOM   18413 H  HB3  . TRP   C  3  148 ? 3.817   -76.409 -85.355  1.00 118.14 ? 148  TRP   C HB3  1 
ATOM   18414 H  HD1  . TRP   C  3  148 ? 3.866   -73.795 -82.894  1.00 106.88 ? 148  TRP   C HD1  1 
ATOM   18415 H  HE1  . TRP   C  3  148 ? 5.898   -72.506 -82.961  1.00 101.92 ? 148  TRP   C HE1  1 
ATOM   18416 H  HE3  . TRP   C  3  148 ? 5.744   -75.488 -87.095  1.00 105.67 ? 148  TRP   C HE3  1 
ATOM   18417 H  HZ2  . TRP   C  3  148 ? 8.079   -72.240 -84.645  1.00 96.37  ? 148  TRP   C HZ2  1 
ATOM   18418 H  HZ3  . TRP   C  3  148 ? 7.776   -74.664 -87.837  1.00 102.64 ? 148  TRP   C HZ3  1 
ATOM   18419 H  HH2  . TRP   C  3  148 ? 8.923   -73.064 -86.625  1.00 96.98  ? 148  TRP   C HH2  1 
ATOM   18420 N  N    . LYS   C  3  149 ? 1.931   -76.422 -88.072  1.00 116.51 ? 149  LYS   C N    1 
ATOM   18421 C  CA   . LYS   C  3  149 ? 1.388   -77.539 -88.836  1.00 124.43 ? 149  LYS   C CA   1 
ATOM   18422 C  C    . LYS   C  3  149 ? 2.557   -78.336 -89.399  1.00 123.76 ? 149  LYS   C C    1 
ATOM   18423 O  O    . LYS   C  3  149 ? 3.394   -77.784 -90.121  1.00 122.32 ? 149  LYS   C O    1 
ATOM   18424 C  CB   . LYS   C  3  149 ? 0.479   -77.054 -89.969  1.00 129.51 ? 149  LYS   C CB   1 
ATOM   18425 C  CG   . LYS   C  3  149 ? -0.610  -76.069 -89.558  1.00 129.95 ? 149  LYS   C CG   1 
ATOM   18426 C  CD   . LYS   C  3  149 ? -1.881  -76.763 -89.087  1.00 134.16 ? 149  LYS   C CD   1 
ATOM   18427 C  CE   . LYS   C  3  149 ? -3.034  -75.769 -88.994  1.00 136.02 ? 149  LYS   C CE   1 
ATOM   18428 N  NZ   . LYS   C  3  149 ? -4.270  -76.361 -88.411  1.00 141.34 ? 149  LYS   C NZ   1 
ATOM   18429 H  H    . LYS   C  3  149 ? 2.408   -75.886 -88.546  1.00 139.79 ? 149  LYS   C H    1 
ATOM   18430 H  HA   . LYS   C  3  149 ? 0.863   -78.109 -88.252  1.00 149.29 ? 149  LYS   C HA   1 
ATOM   18431 H  HB2  . LYS   C  3  149 ? 1.030   -76.615 -90.636  1.00 155.39 ? 149  LYS   C HB2  1 
ATOM   18432 H  HB3  . LYS   C  3  149 ? 0.039   -77.826 -90.359  1.00 155.39 ? 149  LYS   C HB3  1 
ATOM   18433 H  HG2  . LYS   C  3  149 ? -0.281  -75.519 -88.830  1.00 155.92 ? 149  LYS   C HG2  1 
ATOM   18434 H  HG3  . LYS   C  3  149 ? -0.836  -75.511 -90.319  1.00 155.92 ? 149  LYS   C HG3  1 
ATOM   18435 H  HD2  . LYS   C  3  149 ? -2.124  -77.458 -89.718  1.00 160.97 ? 149  LYS   C HD2  1 
ATOM   18436 H  HD3  . LYS   C  3  149 ? -1.735  -77.148 -88.209  1.00 160.97 ? 149  LYS   C HD3  1 
ATOM   18437 H  HE2  . LYS   C  3  149 ? -2.765  -75.026 -88.431  1.00 163.20 ? 149  LYS   C HE2  1 
ATOM   18438 H  HE3  . LYS   C  3  149 ? -3.247  -75.451 -89.885  1.00 163.20 ? 149  LYS   C HE3  1 
ATOM   18439 H  HZ1  . LYS   C  3  149 ? -4.982  -76.102 -88.879  1.00 169.59 ? 149  LYS   C HZ1  1 
ATOM   18440 H  HZ2  . LYS   C  3  149 ? -4.220  -77.249 -88.428  1.00 169.59 ? 149  LYS   C HZ2  1 
ATOM   18441 H  HZ3  . LYS   C  3  149 ? -4.367  -76.093 -87.567  1.00 169.59 ? 149  LYS   C HZ3  1 
ATOM   18442 N  N    . ILE   C  3  150 ? 2.614   -79.627 -89.072  1.00 123.37 ? 150  ILE   C N    1 
ATOM   18443 C  CA   . ILE   C  3  150 ? 3.695   -80.486 -89.544  1.00 118.43 ? 150  ILE   C CA   1 
ATOM   18444 C  C    . ILE   C  3  150 ? 3.282   -81.129 -90.860  1.00 120.41 ? 150  ILE   C C    1 
ATOM   18445 O  O    . ILE   C  3  150 ? 3.895   -80.882 -91.904  1.00 122.12 ? 150  ILE   C O    1 
ATOM   18446 C  CB   . ILE   C  3  150 ? 4.055   -81.554 -88.493  1.00 116.22 ? 150  ILE   C CB   1 
ATOM   18447 C  CG1  . ILE   C  3  150 ? 4.637   -80.890 -87.243  1.00 105.70 ? 150  ILE   C CG1  1 
ATOM   18448 C  CG2  . ILE   C  3  150 ? 5.051   -82.558 -89.063  1.00 120.80 ? 150  ILE   C CG2  1 
ATOM   18449 C  CD1  . ILE   C  3  150 ? 4.388   -81.663 -85.966  1.00 103.72 ? 150  ILE   C CD1  1 
ATOM   18450 H  H    . ILE   C  3  150 ? 2.036   -80.028 -88.576  1.00 148.03 ? 150  ILE   C H    1 
ATOM   18451 H  HA   . ILE   C  3  150 ? 4.483   -79.945 -89.704  1.00 142.10 ? 150  ILE   C HA   1 
ATOM   18452 H  HB   . ILE   C  3  150 ? 3.242   -82.026 -88.253  1.00 139.44 ? 150  ILE   C HB   1 
ATOM   18453 H  HG12 . ILE   C  3  150 ? 5.596   -80.805 -87.355  1.00 126.82 ? 150  ILE   C HG12 1 
ATOM   18454 H  HG13 . ILE   C  3  150 ? 4.235   -80.013 -87.141  1.00 126.82 ? 150  ILE   C HG13 1 
ATOM   18455 H  HG21 . ILE   C  3  150 ? 5.335   -83.158 -88.356  1.00 144.94 ? 150  ILE   C HG21 1 
ATOM   18456 H  HG22 . ILE   C  3  150 ? 4.622   -83.062 -89.772  1.00 144.94 ? 150  ILE   C HG22 1 
ATOM   18457 H  HG23 . ILE   C  3  150 ? 5.817   -82.077 -89.416  1.00 144.94 ? 150  ILE   C HG23 1 
ATOM   18458 H  HD11 . ILE   C  3  150 ? 4.699   -81.137 -85.213  1.00 124.45 ? 150  ILE   C HD11 1 
ATOM   18459 H  HD12 . ILE   C  3  150 ? 3.436   -81.832 -85.880  1.00 124.45 ? 150  ILE   C HD12 1 
ATOM   18460 H  HD13 . ILE   C  3  150 ? 4.871   -82.502 -86.006  1.00 124.45 ? 150  ILE   C HD13 1 
ATOM   18461 N  N    . ASP   C  3  151 ? 2.234   -81.948 -90.821  1.00 120.62 ? 151  ASP   C N    1 
ATOM   18462 C  CA   . ASP   C  3  151 ? 1.686   -82.610 -91.998  1.00 124.45 ? 151  ASP   C CA   1 
ATOM   18463 C  C    . ASP   C  3  151 ? 0.212   -82.266 -92.162  1.00 124.64 ? 151  ASP   C C    1 
ATOM   18464 O  O    . ASP   C  3  151 ? -0.625  -83.130 -92.437  1.00 131.49 ? 151  ASP   C O    1 
ATOM   18465 C  CB   . ASP   C  3  151 ? 1.885   -84.122 -91.915  1.00 131.78 ? 151  ASP   C CB   1 
ATOM   18466 C  CG   . ASP   C  3  151 ? 3.319   -84.536 -92.178  1.00 130.66 ? 151  ASP   C CG   1 
ATOM   18467 O  OD1  . ASP   C  3  151 ? 4.065   -83.747 -92.795  1.00 127.41 ? 151  ASP   C OD1  1 
ATOM   18468 O  OD2  . ASP   C  3  151 ? 3.700   -85.654 -91.775  1.00 132.74 ? 151  ASP   C OD2  1 
ATOM   18469 H  H    . ASP   C  3  151 ? 1.810   -82.140 -90.098  1.00 144.73 ? 151  ASP   C H    1 
ATOM   18470 H  HA   . ASP   C  3  151 ? 2.159   -82.294 -92.784  1.00 149.32 ? 151  ASP   C HA   1 
ATOM   18471 H  HB2  . ASP   C  3  151 ? 1.643   -84.424 -91.026  1.00 158.12 ? 151  ASP   C HB2  1 
ATOM   18472 H  HB3  . ASP   C  3  151 ? 1.322   -84.552 -92.577  1.00 158.12 ? 151  ASP   C HB3  1 
ATOM   18473 N  N    . GLY   C  3  152 ? -0.119  -80.989 -91.991  1.00 119.59 ? 152  GLY   C N    1 
ATOM   18474 C  CA   . GLY   C  3  152 ? -1.491  -80.536 -92.021  1.00 125.11 ? 152  GLY   C CA   1 
ATOM   18475 C  C    . GLY   C  3  152 ? -2.213  -80.627 -90.696  1.00 130.58 ? 152  GLY   C C    1 
ATOM   18476 O  O    . GLY   C  3  152 ? -3.395  -80.264 -90.627  1.00 134.05 ? 152  GLY   C O    1 
ATOM   18477 H  H    . GLY   C  3  152 ? 0.449   -80.358 -91.853  1.00 143.49 ? 152  GLY   C H    1 
ATOM   18478 H  HA2  . GLY   C  3  152 ? -1.508  -79.609 -92.305  1.00 150.12 ? 152  GLY   C HA2  1 
ATOM   18479 H  HA3  . GLY   C  3  152 ? -1.982  -81.072 -92.664  1.00 150.12 ? 152  GLY   C HA3  1 
ATOM   18480 N  N    . SER   C  3  153 ? -1.544  -81.095 -89.646  1.00 131.82 ? 153  SER   C N    1 
ATOM   18481 C  CA   . SER   C  3  153 ? -2.128  -81.236 -88.322  1.00 133.93 ? 153  SER   C CA   1 
ATOM   18482 C  C    . SER   C  3  153 ? -1.478  -80.254 -87.357  1.00 124.29 ? 153  SER   C C    1 
ATOM   18483 O  O    . SER   C  3  153 ? -0.306  -79.898 -87.503  1.00 112.59 ? 153  SER   C O    1 
ATOM   18484 C  CB   . SER   C  3  153 ? -1.952  -82.662 -87.794  1.00 140.66 ? 153  SER   C CB   1 
ATOM   18485 O  OG   . SER   C  3  153 ? -0.583  -83.028 -87.780  1.00 138.75 ? 153  SER   C OG   1 
ATOM   18486 H  H    . SER   C  3  153 ? -0.723  -81.346 -89.680  1.00 158.16 ? 153  SER   C H    1 
ATOM   18487 H  HA   . SER   C  3  153 ? -3.077  -81.040 -88.365  1.00 160.70 ? 153  SER   C HA   1 
ATOM   18488 H  HB2  . SER   C  3  153 ? -2.301  -82.710 -86.891  1.00 168.78 ? 153  SER   C HB2  1 
ATOM   18489 H  HB3  . SER   C  3  153 ? -2.437  -83.274 -88.370  1.00 168.78 ? 153  SER   C HB3  1 
ATOM   18490 H  HG   . SER   C  3  153 ? -0.490  -83.779 -87.415  1.00 166.48 ? 153  SER   C HG   1 
ATOM   18491 N  N    . GLU   C  3  154 ? -2.247  -79.830 -86.359  1.00 130.34 ? 154  GLU   C N    1 
ATOM   18492 C  CA   . GLU   C  3  154 ? -1.779  -78.868 -85.370  1.00 129.56 ? 154  GLU   C CA   1 
ATOM   18493 C  C    . GLU   C  3  154 ? -1.132  -79.617 -84.211  1.00 129.96 ? 154  GLU   C C    1 
ATOM   18494 O  O    . GLU   C  3  154 ? -1.788  -80.429 -83.549  1.00 134.58 ? 154  GLU   C O    1 
ATOM   18495 C  CB   . GLU   C  3  154 ? -2.941  -78.007 -84.877  1.00 131.53 ? 154  GLU   C CB   1 
ATOM   18496 C  CG   . GLU   C  3  154 ? -2.522  -76.702 -84.222  1.00 125.81 ? 154  GLU   C CG   1 
ATOM   18497 C  CD   . GLU   C  3  154 ? -3.708  -75.829 -83.860  1.00 127.43 ? 154  GLU   C CD   1 
ATOM   18498 O  OE1  . GLU   C  3  154 ? -4.601  -76.309 -83.130  1.00 130.97 ? 154  GLU   C OE1  1 
ATOM   18499 O  OE2  . GLU   C  3  154 ? -3.752  -74.667 -84.316  1.00 125.38 ? 154  GLU   C OE2  1 
ATOM   18500 H  H    . GLU   C  3  154 ? -3.057  -80.090 -86.233  1.00 156.39 ? 154  GLU   C H    1 
ATOM   18501 H  HA   . GLU   C  3  154 ? -1.113  -78.286 -85.768  1.00 155.46 ? 154  GLU   C HA   1 
ATOM   18502 H  HB2  . GLU   C  3  154 ? -3.506  -77.787 -85.634  1.00 157.81 ? 154  GLU   C HB2  1 
ATOM   18503 H  HB3  . GLU   C  3  154 ? -3.446  -78.515 -84.223  1.00 157.81 ? 154  GLU   C HB3  1 
ATOM   18504 H  HG2  . GLU   C  3  154 ? -2.033  -76.899 -83.408  1.00 150.95 ? 154  GLU   C HG2  1 
ATOM   18505 H  HG3  . GLU   C  3  154 ? -1.959  -76.206 -84.836  1.00 150.95 ? 154  GLU   C HG3  1 
ATOM   18506 N  N    . ARG   C  3  155 ? 0.152   -79.348 -83.967  1.00 124.10 ? 155  ARG   C N    1 
ATOM   18507 C  CA   . ARG   C  3  155 ? 0.847   -80.004 -82.864  1.00 121.10 ? 155  ARG   C CA   1 
ATOM   18508 C  C    . ARG   C  3  155 ? 0.445   -79.394 -81.524  1.00 116.04 ? 155  ARG   C C    1 
ATOM   18509 O  O    . ARG   C  3  155 ? -0.118  -80.079 -80.663  1.00 119.61 ? 155  ARG   C O    1 
ATOM   18510 C  CB   . ARG   C  3  155 ? 2.363   -79.917 -83.066  1.00 116.57 ? 155  ARG   C CB   1 
ATOM   18511 C  CG   . ARG   C  3  155 ? 3.160   -80.465 -81.892  1.00 115.18 ? 155  ARG   C CG   1 
ATOM   18512 C  CD   . ARG   C  3  155 ? 4.222   -81.462 -82.330  1.00 117.56 ? 155  ARG   C CD   1 
ATOM   18513 N  NE   . ARG   C  3  155 ? 4.807   -82.147 -81.177  1.00 120.53 ? 155  ARG   C NE   1 
ATOM   18514 C  CZ   . ARG   C  3  155 ? 4.613   -83.428 -80.865  1.00 127.98 ? 155  ARG   C CZ   1 
ATOM   18515 N  NH1  . ARG   C  3  155 ? 5.194   -83.930 -79.784  1.00 130.17 ? 155  ARG   C NH1  1 
ATOM   18516 N  NH2  . ARG   C  3  155 ? 3.859   -84.215 -81.624  1.00 132.52 ? 155  ARG   C NH2  1 
ATOM   18517 H  H    . ARG   C  3  155 ? 0.634   -78.797 -84.419  1.00 148.90 ? 155  ARG   C H    1 
ATOM   18518 H  HA   . ARG   C  3  155 ? 0.604   -80.943 -82.855  1.00 145.31 ? 155  ARG   C HA   1 
ATOM   18519 H  HB2  . ARG   C  3  155 ? 2.604   -80.429 -83.854  1.00 139.86 ? 155  ARG   C HB2  1 
ATOM   18520 H  HB3  . ARG   C  3  155 ? 2.610   -78.987 -83.186  1.00 139.86 ? 155  ARG   C HB3  1 
ATOM   18521 H  HG2  . ARG   C  3  155 ? 3.604   -79.731 -81.439  1.00 138.20 ? 155  ARG   C HG2  1 
ATOM   18522 H  HG3  . ARG   C  3  155 ? 2.557   -80.915 -81.281  1.00 138.20 ? 155  ARG   C HG3  1 
ATOM   18523 H  HD2  . ARG   C  3  155 ? 3.820   -82.127 -82.911  1.00 141.06 ? 155  ARG   C HD2  1 
ATOM   18524 H  HD3  . ARG   C  3  155 ? 4.929   -80.995 -82.801  1.00 141.06 ? 155  ARG   C HD3  1 
ATOM   18525 H  HE   . ARG   C  3  155 ? 5.317   -81.687 -80.661  1.00 144.62 ? 155  ARG   C HE   1 
ATOM   18526 H  HH11 . ARG   C  3  155 ? 5.692   -83.430 -79.292  1.00 156.19 ? 155  ARG   C HH11 1 
ATOM   18527 H  HH12 . ARG   C  3  155 ? 5.074   -84.755 -79.575  1.00 156.19 ? 155  ARG   C HH12 1 
ATOM   18528 H  HH21 . ARG   C  3  155 ? 3.486   -83.901 -82.332  1.00 159.00 ? 155  ARG   C HH21 1 
ATOM   18529 H  HH22 . ARG   C  3  155 ? 3.744   -85.040 -81.407  1.00 159.00 ? 155  ARG   C HH22 1 
ATOM   18530 N  N    . GLN   C  3  156 ? 0.731   -78.106 -81.331  1.00 108.35 ? 156  GLN   C N    1 
ATOM   18531 C  CA   . GLN   C  3  156 ? 0.250   -77.363 -80.166  1.00 110.54 ? 156  GLN   C CA   1 
ATOM   18532 C  C    . GLN   C  3  156 ? 0.726   -77.983 -78.852  1.00 110.94 ? 156  GLN   C C    1 
ATOM   18533 O  O    . GLN   C  3  156 ? 0.076   -77.839 -77.815  1.00 113.47 ? 156  GLN   C O    1 
ATOM   18534 C  CB   . GLN   C  3  156 ? -1.282  -77.269 -80.193  1.00 119.66 ? 156  GLN   C CB   1 
ATOM   18535 C  CG   . GLN   C  3  156 ? -1.912  -76.357 -79.142  1.00 122.32 ? 156  GLN   C CG   1 
ATOM   18536 C  CD   . GLN   C  3  156 ? -3.425  -76.313 -79.242  1.00 128.98 ? 156  GLN   C CD   1 
ATOM   18537 O  OE1  . GLN   C  3  156 ? -4.011  -76.811 -80.205  1.00 132.15 ? 156  GLN   C OE1  1 
ATOM   18538 N  NE2  . GLN   C  3  156 ? -4.067  -75.719 -78.242  1.00 130.84 ? 156  GLN   C NE2  1 
ATOM   18539 H  H    . GLN   C  3  156 ? 1.208   -77.634 -81.868  1.00 130.00 ? 156  GLN   C H    1 
ATOM   18540 H  HA   . GLN   C  3  156 ? 0.617   -76.466 -80.198  1.00 132.63 ? 156  GLN   C HA   1 
ATOM   18541 H  HB2  . GLN   C  3  156 ? -1.551  -76.933 -81.062  1.00 143.57 ? 156  GLN   C HB2  1 
ATOM   18542 H  HB3  . GLN   C  3  156 ? -1.644  -78.158 -80.055  1.00 143.57 ? 156  GLN   C HB3  1 
ATOM   18543 H  HG2  . GLN   C  3  156 ? -1.678  -76.683 -78.259  1.00 146.77 ? 156  GLN   C HG2  1 
ATOM   18544 H  HG3  . GLN   C  3  156 ? -1.575  -75.456 -79.262  1.00 146.77 ? 156  GLN   C HG3  1 
ATOM   18545 H  HE21 . GLN   C  3  156 ? -3.624  -75.386 -77.585  1.00 156.99 ? 156  GLN   C HE21 1 
ATOM   18546 H  HE22 . GLN   C  3  156 ? -4.926  -75.668 -78.253  1.00 156.99 ? 156  GLN   C HE22 1 
ATOM   18547 N  N    . ASN   C  3  157 ? 1.863   -78.679 -78.862  1.00 109.55 ? 157  ASN   C N    1 
ATOM   18548 C  CA   . ASN   C  3  157 ? 2.329   -79.352 -77.654  1.00 109.97 ? 157  ASN   C CA   1 
ATOM   18549 C  C    . ASN   C  3  157 ? 3.690   -78.870 -77.178  1.00 107.23 ? 157  ASN   C C    1 
ATOM   18550 O  O    . ASN   C  3  157 ? 3.840   -78.535 -75.996  1.00 108.20 ? 157  ASN   C O    1 
ATOM   18551 C  CB   . ASN   C  3  157 ? 2.368   -80.872 -77.880  1.00 112.29 ? 157  ASN   C CB   1 
ATOM   18552 C  CG   . ASN   C  3  157 ? 2.021   -81.652 -76.626  1.00 114.29 ? 157  ASN   C CG   1 
ATOM   18553 O  OD1  . ASN   C  3  157 ? 2.318   -81.220 -75.512  1.00 109.43 ? 157  ASN   C OD1  1 
ATOM   18554 N  ND2  . ASN   C  3  157 ? 1.378   -82.801 -76.800  1.00 121.35 ? 157  ASN   C ND2  1 
ATOM   18555 H  H    . ASN   C  3  157 ? 2.373   -78.773 -79.547  1.00 131.44 ? 157  ASN   C H    1 
ATOM   18556 H  HA   . ASN   C  3  157 ? 1.694   -79.162 -76.946  1.00 131.94 ? 157  ASN   C HA   1 
ATOM   18557 H  HB2  . ASN   C  3  157 ? 1.727   -81.108 -78.569  1.00 134.73 ? 157  ASN   C HB2  1 
ATOM   18558 H  HB3  . ASN   C  3  157 ? 3.262   -81.129 -78.157  1.00 134.73 ? 157  ASN   C HB3  1 
ATOM   18559 H  HD21 . ASN   C  3  157 ? 1.159   -83.278 -76.119  1.00 145.60 ? 157  ASN   C HD21 1 
ATOM   18560 H  HD22 . ASN   C  3  157 ? 1.180   -83.067 -77.593  1.00 145.60 ? 157  ASN   C HD22 1 
ATOM   18561 N  N    . GLY   C  3  158 ? 4.690   -78.821 -78.055  1.00 104.29 ? 158  GLY   C N    1 
ATOM   18562 C  CA   . GLY   C  3  158 ? 6.040   -78.497 -77.630  1.00 101.42 ? 158  GLY   C CA   1 
ATOM   18563 C  C    . GLY   C  3  158 ? 6.507   -77.129 -78.083  1.00 99.62  ? 158  GLY   C C    1 
ATOM   18564 O  O    . GLY   C  3  158 ? 7.709   -76.896 -78.237  1.00 95.97  ? 158  GLY   C O    1 
ATOM   18565 H  H    . GLY   C  3  158 ? 4.609   -78.971 -78.898  1.00 125.13 ? 158  GLY   C H    1 
ATOM   18566 H  HA2  . GLY   C  3  158 ? 6.081   -78.523 -76.661  1.00 121.68 ? 158  GLY   C HA2  1 
ATOM   18567 H  HA3  . GLY   C  3  158 ? 6.652   -79.158 -77.990  1.00 121.68 ? 158  GLY   C HA3  1 
ATOM   18568 N  N    . VAL   C  3  159 ? 5.567   -76.216 -78.290  1.00 100.76 ? 159  VAL   C N    1 
ATOM   18569 C  CA   . VAL   C  3  159 ? 5.869   -74.889 -78.812  1.00 96.09  ? 159  VAL   C CA   1 
ATOM   18570 C  C    . VAL   C  3  159 ? 6.147   -73.935 -77.658  1.00 88.90  ? 159  VAL   C C    1 
ATOM   18571 O  O    . VAL   C  3  159 ? 5.429   -73.921 -76.651  1.00 84.91  ? 159  VAL   C O    1 
ATOM   18572 C  CB   . VAL   C  3  159 ? 4.715   -74.374 -79.695  1.00 98.09  ? 159  VAL   C CB   1 
ATOM   18573 C  CG1  . VAL   C  3  159 ? 3.403   -74.331 -78.915  1.00 104.04 ? 159  VAL   C CG1  1 
ATOM   18574 C  CG2  . VAL   C  3  159 ? 5.051   -73.001 -80.259  1.00 94.46  ? 159  VAL   C CG2  1 
ATOM   18575 H  H    . VAL   C  3  159 ? 4.731   -76.343 -78.133  1.00 120.89 ? 159  VAL   C H    1 
ATOM   18576 H  HA   . VAL   C  3  159 ? 6.672   -74.943 -79.353  1.00 115.29 ? 159  VAL   C HA   1 
ATOM   18577 H  HB   . VAL   C  3  159 ? 4.596   -74.988 -80.436  1.00 117.68 ? 159  VAL   C HB   1 
ATOM   18578 H  HG11 . VAL   C  3  159 ? 2.702   -73.994 -79.494  1.00 124.83 ? 159  VAL   C HG11 1 
ATOM   18579 H  HG12 . VAL   C  3  159 ? 3.183   -75.228 -78.617  1.00 124.83 ? 159  VAL   C HG12 1 
ATOM   18580 H  HG13 . VAL   C  3  159 ? 3.510   -73.746 -78.149  1.00 124.83 ? 159  VAL   C HG13 1 
ATOM   18581 H  HG21 . VAL   C  3  159 ? 4.365   -72.745 -80.896  1.00 113.33 ? 159  VAL   C HG21 1 
ATOM   18582 H  HG22 . VAL   C  3  159 ? 5.083   -72.360 -79.532  1.00 113.33 ? 159  VAL   C HG22 1 
ATOM   18583 H  HG23 . VAL   C  3  159 ? 5.913   -73.044 -80.702  1.00 113.33 ? 159  VAL   C HG23 1 
ATOM   18584 N  N    . LEU   C  3  160 ? 7.203   -73.136 -77.806  1.00 86.98  ? 160  LEU   C N    1 
ATOM   18585 C  CA   . LEU   C  3  160 ? 7.529   -72.062 -76.878  1.00 84.11  ? 160  LEU   C CA   1 
ATOM   18586 C  C    . LEU   C  3  160 ? 7.708   -70.771 -77.664  1.00 80.59  ? 160  LEU   C C    1 
ATOM   18587 O  O    . LEU   C  3  160 ? 8.363   -70.758 -78.710  1.00 78.60  ? 160  LEU   C O    1 
ATOM   18588 C  CB   . LEU   C  3  160 ? 8.801   -72.369 -76.077  1.00 83.79  ? 160  LEU   C CB   1 
ATOM   18589 C  CG   . LEU   C  3  160 ? 8.686   -73.427 -74.976  1.00 89.81  ? 160  LEU   C CG   1 
ATOM   18590 C  CD1  . LEU   C  3  160 ? 10.033  -73.621 -74.296  1.00 87.79  ? 160  LEU   C CD1  1 
ATOM   18591 C  CD2  . LEU   C  3  160 ? 7.624   -73.048 -73.954  1.00 91.26  ? 160  LEU   C CD2  1 
ATOM   18592 H  H    . LEU   C  3  160 ? 7.760   -73.200 -78.458  1.00 104.36 ? 160  LEU   C H    1 
ATOM   18593 H  HA   . LEU   C  3  160 ? 6.804   -71.945 -76.245  1.00 100.92 ? 160  LEU   C HA   1 
ATOM   18594 H  HB2  . LEU   C  3  160 ? 9.478   -72.680 -76.698  1.00 100.52 ? 160  LEU   C HB2  1 
ATOM   18595 H  HB3  . LEU   C  3  160 ? 9.092   -71.548 -75.651  1.00 100.52 ? 160  LEU   C HB3  1 
ATOM   18596 H  HG   . LEU   C  3  160 ? 8.415   -74.267 -75.379  1.00 107.75 ? 160  LEU   C HG   1 
ATOM   18597 H  HD11 . LEU   C  3  160 ? 9.939   -74.283 -73.593  1.00 105.32 ? 160  LEU   C HD11 1 
ATOM   18598 H  HD12 . LEU   C  3  160 ? 10.677  -73.927 -74.953  1.00 105.32 ? 160  LEU   C HD12 1 
ATOM   18599 H  HD13 . LEU   C  3  160 ? 10.321  -72.776 -73.918  1.00 105.32 ? 160  LEU   C HD13 1 
ATOM   18600 H  HD21 . LEU   C  3  160 ? 7.658   -73.677 -73.216  1.00 109.50 ? 160  LEU   C HD21 1 
ATOM   18601 H  HD22 . LEU   C  3  160 ? 7.802   -72.150 -73.632  1.00 109.50 ? 160  LEU   C HD22 1 
ATOM   18602 H  HD23 . LEU   C  3  160 ? 6.752   -73.081 -74.377  1.00 109.50 ? 160  LEU   C HD23 1 
ATOM   18603 N  N    . ASN   C  3  161 ? 7.127   -69.688 -77.155  1.00 79.53  ? 161  ASN   C N    1 
ATOM   18604 C  CA   . ASN   C  3  161 ? 7.104   -68.411 -77.849  1.00 76.71  ? 161  ASN   C CA   1 
ATOM   18605 C  C    . ASN   C  3  161 ? 7.747   -67.329 -76.992  1.00 71.32  ? 161  ASN   C C    1 
ATOM   18606 O  O    . ASN   C  3  161 ? 7.845   -67.449 -75.768  1.00 69.29  ? 161  ASN   C O    1 
ATOM   18607 C  CB   . ASN   C  3  161 ? 5.669   -68.005 -78.207  1.00 78.16  ? 161  ASN   C CB   1 
ATOM   18608 C  CG   . ASN   C  3  161 ? 5.012   -68.978 -79.164  1.00 81.38  ? 161  ASN   C CG   1 
ATOM   18609 O  OD1  . ASN   C  3  161 ? 5.690   -69.703 -79.892  1.00 85.20  ? 161  ASN   C OD1  1 
ATOM   18610 N  ND2  . ASN   C  3  161 ? 3.685   -68.997 -79.170  1.00 82.71  ? 161  ASN   C ND2  1 
ATOM   18611 H  H    . ASN   C  3  161 ? 6.731   -69.671 -76.391  1.00 95.42  ? 161  ASN   C H    1 
ATOM   18612 H  HA   . ASN   C  3  161 ? 7.619   -68.485 -78.668  1.00 92.03  ? 161  ASN   C HA   1 
ATOM   18613 H  HB2  . ASN   C  3  161 ? 5.137   -67.974 -77.397  1.00 93.77  ? 161  ASN   C HB2  1 
ATOM   18614 H  HB3  . ASN   C  3  161 ? 5.683   -67.132 -78.629  1.00 93.77  ? 161  ASN   C HB3  1 
ATOM   18615 H  HD21 . ASN   C  3  161 ? 3.265   -69.532 -79.695  1.00 99.23  ? 161  ASN   C HD21 1 
ATOM   18616 H  HD22 . ASN   C  3  161 ? 3.245   -68.473 -78.648  1.00 99.23  ? 161  ASN   C HD22 1 
ATOM   18617 N  N    . SER   C  3  162 ? 8.184   -66.262 -77.659  1.00 71.30  ? 162  SER   C N    1 
ATOM   18618 C  CA   . SER   C  3  162 ? 8.811   -65.130 -76.988  1.00 72.51  ? 162  SER   C CA   1 
ATOM   18619 C  C    . SER   C  3  162 ? 8.587   -63.874 -77.816  1.00 75.17  ? 162  SER   C C    1 
ATOM   18620 O  O    . SER   C  3  162 ? 8.783   -63.890 -79.035  1.00 74.47  ? 162  SER   C O    1 
ATOM   18621 C  CB   . SER   C  3  162 ? 10.311  -65.371 -76.781  1.00 68.41  ? 162  SER   C CB   1 
ATOM   18622 O  OG   . SER   C  3  162 ? 10.908  -64.293 -76.079  1.00 68.49  ? 162  SER   C OG   1 
ATOM   18623 H  H    . SER   C  3  162 ? 8.127   -66.170 -78.512  1.00 85.55  ? 162  SER   C H    1 
ATOM   18624 H  HA   . SER   C  3  162 ? 8.398   -65.001 -76.120  1.00 86.99  ? 162  SER   C HA   1 
ATOM   18625 H  HB2  . SER   C  3  162 ? 10.432  -66.185 -76.268  1.00 82.07  ? 162  SER   C HB2  1 
ATOM   18626 H  HB3  . SER   C  3  162 ? 10.738  -65.457 -77.647  1.00 82.07  ? 162  SER   C HB3  1 
ATOM   18627 H  HG   . SER   C  3  162 ? 11.678  -64.510 -75.822  1.00 82.17  ? 162  SER   C HG   1 
ATOM   18628 N  N    . TRP   C  3  163 ? 8.179   -62.797 -77.152  1.00 77.45  ? 163  TRP   C N    1 
ATOM   18629 C  CA   . TRP   C  3  163 ? 7.914   -61.516 -77.787  1.00 76.82  ? 163  TRP   C CA   1 
ATOM   18630 C  C    . TRP   C  3  163 ? 8.955   -60.489 -77.357  1.00 72.02  ? 163  TRP   C C    1 
ATOM   18631 O  O    . TRP   C  3  163 ? 9.568   -60.601 -76.292  1.00 71.17  ? 163  TRP   C O    1 
ATOM   18632 C  CB   . TRP   C  3  163 ? 6.514   -61.005 -77.429  1.00 77.87  ? 163  TRP   C CB   1 
ATOM   18633 C  CG   . TRP   C  3  163 ? 5.401   -61.919 -77.838  1.00 82.23  ? 163  TRP   C CG   1 
ATOM   18634 C  CD1  . TRP   C  3  163 ? 4.542   -61.746 -78.883  1.00 89.67  ? 163  TRP   C CD1  1 
ATOM   18635 C  CD2  . TRP   C  3  163 ? 5.022   -63.148 -77.207  1.00 78.70  ? 163  TRP   C CD2  1 
ATOM   18636 N  NE1  . TRP   C  3  163 ? 3.651   -62.789 -78.941  1.00 92.24  ? 163  TRP   C NE1  1 
ATOM   18637 C  CE2  . TRP   C  3  163 ? 3.926   -63.665 -77.925  1.00 84.37  ? 163  TRP   C CE2  1 
ATOM   18638 C  CE3  . TRP   C  3  163 ? 5.503   -63.862 -76.105  1.00 72.66  ? 163  TRP   C CE3  1 
ATOM   18639 C  CZ2  . TRP   C  3  163 ? 3.304   -64.862 -77.578  1.00 81.03  ? 163  TRP   C CZ2  1 
ATOM   18640 C  CZ3  . TRP   C  3  163 ? 4.884   -65.049 -75.763  1.00 71.94  ? 163  TRP   C CZ3  1 
ATOM   18641 C  CH2  . TRP   C  3  163 ? 3.796   -65.537 -76.497  1.00 74.27  ? 163  TRP   C CH2  1 
ATOM   18642 H  H    . TRP   C  3  163 ? 8.045   -62.786 -76.302  1.00 92.92  ? 163  TRP   C H    1 
ATOM   18643 H  HA   . TRP   C  3  163 ? 7.966   -61.622 -78.750  1.00 92.17  ? 163  TRP   C HA   1 
ATOM   18644 H  HB2  . TRP   C  3  163 ? 6.462   -60.891 -76.468  1.00 93.42  ? 163  TRP   C HB2  1 
ATOM   18645 H  HB3  . TRP   C  3  163 ? 6.372   -60.154 -77.872  1.00 93.42  ? 163  TRP   C HB3  1 
ATOM   18646 H  HD1  . TRP   C  3  163 ? 4.558   -61.026 -79.471  1.00 107.58 ? 163  TRP   C HD1  1 
ATOM   18647 H  HE1  . TRP   C  3  163 ? 3.022   -62.877 -79.521  1.00 110.66 ? 163  TRP   C HE1  1 
ATOM   18648 H  HE3  . TRP   C  3  163 ? 6.225   -63.544 -75.612  1.00 87.17  ? 163  TRP   C HE3  1 
ATOM   18649 H  HZ2  . TRP   C  3  163 ? 2.581   -65.188 -78.064  1.00 97.22  ? 163  TRP   C HZ2  1 
ATOM   18650 H  HZ3  . TRP   C  3  163 ? 5.196   -65.533 -75.032  1.00 86.30  ? 163  TRP   C HZ3  1 
ATOM   18651 H  HH2  . TRP   C  3  163 ? 3.400   -66.339 -76.243  1.00 89.10  ? 163  TRP   C HH2  1 
ATOM   18652 N  N    . THR   C  3  164 ? 9.145   -59.480 -78.200  1.00 69.56  ? 164  THR   C N    1 
ATOM   18653 C  CA   . THR   C  3  164 ? 10.038  -58.371 -77.904  1.00 67.68  ? 164  THR   C CA   1 
ATOM   18654 C  C    . THR   C  3  164 ? 9.238   -57.159 -77.443  1.00 73.57  ? 164  THR   C C    1 
ATOM   18655 O  O    . THR   C  3  164 ? 8.087   -56.963 -77.841  1.00 76.61  ? 164  THR   C O    1 
ATOM   18656 C  CB   . THR   C  3  164 ? 10.869  -57.982 -79.130  1.00 65.57  ? 164  THR   C CB   1 
ATOM   18657 O  OG1  . THR   C  3  164 ? 10.001  -57.507 -80.168  1.00 69.03  ? 164  THR   C OG1  1 
ATOM   18658 C  CG2  . THR   C  3  164 ? 11.663  -59.167 -79.647  1.00 64.28  ? 164  THR   C CG2  1 
ATOM   18659 H  H    . THR   C  3  164 ? 8.758   -59.416 -78.966  1.00 83.45  ? 164  THR   C H    1 
ATOM   18660 H  HA   . THR   C  3  164 ? 10.644  -58.639 -77.196  1.00 81.19  ? 164  THR   C HA   1 
ATOM   18661 H  HB   . THR   C  3  164 ? 11.494  -57.284 -78.882  1.00 78.67  ? 164  THR   C HB   1 
ATOM   18662 H  HG1  . THR   C  3  164 ? 10.455  -57.173 -80.791  1.00 82.82  ? 164  THR   C HG1  1 
ATOM   18663 H  HG21 . THR   C  3  164 ? 12.185  -58.904 -80.421  1.00 77.11  ? 164  THR   C HG21 1 
ATOM   18664 H  HG22 . THR   C  3  164 ? 12.264  -59.490 -78.957  1.00 77.11  ? 164  THR   C HG22 1 
ATOM   18665 H  HG23 . THR   C  3  164 ? 11.062  -59.884 -79.901  1.00 77.11  ? 164  THR   C HG23 1 
ATOM   18666 N  N    . ASP   C  3  165 ? 9.860   -56.345 -76.594  1.00 75.38  ? 165  ASP   C N    1 
ATOM   18667 C  CA   . ASP   C  3  165 ? 9.308   -55.029 -76.308  1.00 78.21  ? 165  ASP   C CA   1 
ATOM   18668 C  C    . ASP   C  3  165 ? 9.171   -54.245 -77.607  1.00 72.36  ? 165  ASP   C C    1 
ATOM   18669 O  O    . ASP   C  3  165 ? 9.880   -54.496 -78.585  1.00 68.10  ? 165  ASP   C O    1 
ATOM   18670 C  CB   . ASP   C  3  165 ? 10.201  -54.269 -75.329  1.00 88.24  ? 165  ASP   C CB   1 
ATOM   18671 C  CG   . ASP   C  3  165 ? 10.182  -54.867 -73.943  1.00 94.50  ? 165  ASP   C CG   1 
ATOM   18672 O  OD1  . ASP   C  3  165 ? 9.137   -55.428 -73.552  1.00 97.12  ? 165  ASP   C OD1  1 
ATOM   18673 O  OD2  . ASP   C  3  165 ? 11.213  -54.775 -73.245  1.00 95.93  ? 165  ASP   C OD2  1 
ATOM   18674 H  H    . ASP   C  3  165 ? 10.590  -56.528 -76.178  1.00 90.44  ? 165  ASP   C H    1 
ATOM   18675 H  HA   . ASP   C  3  165 ? 8.434   -55.120 -75.896  1.00 93.83  ? 165  ASP   C HA   1 
ATOM   18676 H  HB2  . ASP   C  3  165 ? 11.115  -54.289 -75.653  1.00 105.87 ? 165  ASP   C HB2  1 
ATOM   18677 H  HB3  . ASP   C  3  165 ? 9.891   -53.352 -75.265  1.00 105.87 ? 165  ASP   C HB3  1 
ATOM   18678 N  N    . GLN   C  3  166 ? 8.245   -53.291 -77.618  1.00 73.93  ? 166  GLN   C N    1 
ATOM   18679 C  CA   . GLN   C  3  166 ? 8.048   -52.480 -78.811  1.00 75.94  ? 166  GLN   C CA   1 
ATOM   18680 C  C    . GLN   C  3  166 ? 9.348   -51.785 -79.192  1.00 75.97  ? 166  GLN   C C    1 
ATOM   18681 O  O    . GLN   C  3  166 ? 9.980   -51.123 -78.363  1.00 78.08  ? 166  GLN   C O    1 
ATOM   18682 C  CB   . GLN   C  3  166 ? 6.947   -51.446 -78.585  1.00 77.22  ? 166  GLN   C CB   1 
ATOM   18683 C  CG   . GLN   C  3  166 ? 6.702   -50.548 -79.792  1.00 78.68  ? 166  GLN   C CG   1 
ATOM   18684 C  CD   . GLN   C  3  166 ? 5.607   -49.529 -79.555  1.00 80.89  ? 166  GLN   C CD   1 
ATOM   18685 O  OE1  . GLN   C  3  166 ? 5.631   -48.791 -78.570  1.00 82.20  ? 166  GLN   C OE1  1 
ATOM   18686 N  NE2  . GLN   C  3  166 ? 4.635   -49.485 -80.459  1.00 81.30  ? 166  GLN   C NE2  1 
ATOM   18687 H  H    . GLN   C  3  166 ? 7.728   -53.097 -76.959  1.00 88.70  ? 166  GLN   C H    1 
ATOM   18688 H  HA   . GLN   C  3  166 ? 7.772   -53.054 -79.542  1.00 91.10  ? 166  GLN   C HA   1 
ATOM   18689 H  HB2  . GLN   C  3  166 ? 6.119   -51.909 -78.385  1.00 92.64  ? 166  GLN   C HB2  1 
ATOM   18690 H  HB3  . GLN   C  3  166 ? 7.199   -50.879 -77.839  1.00 92.64  ? 166  GLN   C HB3  1 
ATOM   18691 H  HG2  . GLN   C  3  166 ? 7.519   -50.067 -79.999  1.00 94.39  ? 166  GLN   C HG2  1 
ATOM   18692 H  HG3  . GLN   C  3  166 ? 6.440   -51.098 -80.547  1.00 94.39  ? 166  GLN   C HG3  1 
ATOM   18693 H  HE21 . GLN   C  3  166 ? 4.651   -50.018 -81.134  1.00 97.55  ? 166  GLN   C HE21 1 
ATOM   18694 H  HE22 . GLN   C  3  166 ? 3.989   -48.924 -80.370  1.00 97.55  ? 166  GLN   C HE22 1 
ATOM   18695 N  N    . ASP   C  3  167 ? 9.745   -51.938 -80.452  1.00 77.73  ? 167  ASP   C N    1 
ATOM   18696 C  CA   . ASP   C  3  167 ? 10.947  -51.278 -80.939  1.00 82.60  ? 167  ASP   C CA   1 
ATOM   18697 C  C    . ASP   C  3  167 ? 10.814  -49.769 -80.763  1.00 86.78  ? 167  ASP   C C    1 
ATOM   18698 O  O    . ASP   C  3  167 ? 9.711   -49.216 -80.766  1.00 88.90  ? 167  ASP   C O    1 
ATOM   18699 C  CB   . ASP   C  3  167 ? 11.186  -51.635 -82.408  1.00 88.51  ? 167  ASP   C CB   1 
ATOM   18700 C  CG   . ASP   C  3  167 ? 12.615  -51.377 -82.847  1.00 93.21  ? 167  ASP   C CG   1 
ATOM   18701 O  OD1  . ASP   C  3  167 ? 13.076  -50.222 -82.737  1.00 96.27  ? 167  ASP   C OD1  1 
ATOM   18702 O  OD2  . ASP   C  3  167 ? 13.281  -52.336 -83.291  1.00 94.02  ? 167  ASP   C OD2  1 
ATOM   18703 H  H    . ASP   C  3  167 ? 9.338   -52.416 -81.040  1.00 93.26  ? 167  ASP   C H    1 
ATOM   18704 H  HA   . ASP   C  3  167 ? 11.721  -51.575 -80.436  1.00 99.10  ? 167  ASP   C HA   1 
ATOM   18705 H  HB2  . ASP   C  3  167 ? 10.997  -52.577 -82.540  1.00 106.19 ? 167  ASP   C HB2  1 
ATOM   18706 H  HB3  . ASP   C  3  167 ? 10.600  -51.098 -82.964  1.00 106.19 ? 167  ASP   C HB3  1 
ATOM   18707 N  N    . SER   C  3  168 ? 11.954  -49.101 -80.590  1.00 89.00  ? 168  SER   C N    1 
ATOM   18708 C  CA   . SER   C  3  168 ? 11.961  -47.662 -80.357  1.00 93.31  ? 168  SER   C CA   1 
ATOM   18709 C  C    . SER   C  3  168 ? 12.023  -46.869 -81.659  1.00 95.37  ? 168  SER   C C    1 
ATOM   18710 O  O    . SER   C  3  168 ? 11.254  -45.921 -81.846  1.00 97.16  ? 168  SER   C O    1 
ATOM   18711 C  CB   . SER   C  3  168 ? 13.139  -47.282 -79.453  1.00 96.40  ? 168  SER   C CB   1 
ATOM   18712 O  OG   . SER   C  3  168 ? 12.942  -47.750 -78.129  1.00 95.43  ? 168  SER   C OG   1 
ATOM   18713 H  H    . SER   C  3  168 ? 12.735  -49.461 -80.604  1.00 106.78 ? 168  SER   C H    1 
ATOM   18714 H  HA   . SER   C  3  168 ? 11.141  -47.420 -79.900  1.00 111.96 ? 168  SER   C HA   1 
ATOM   18715 H  HB2  . SER   C  3  168 ? 13.949  -47.680 -79.809  1.00 115.67 ? 168  SER   C HB2  1 
ATOM   18716 H  HB3  . SER   C  3  168 ? 13.224  -46.316 -79.436  1.00 115.67 ? 168  SER   C HB3  1 
ATOM   18717 H  HG   . SER   C  3  168 ? 13.545  -47.452 -77.626  1.00 114.49 ? 168  SER   C HG   1 
ATOM   18718 N  N    . LYS   C  3  169 ? 12.926  -47.243 -82.567  1.00 96.82  ? 169  LYS   C N    1 
ATOM   18719 C  CA   . LYS   C  3  169 ? 13.067  -46.535 -83.834  1.00 103.95 ? 169  LYS   C CA   1 
ATOM   18720 C  C    . LYS   C  3  169 ? 11.761  -46.608 -84.612  1.00 101.72 ? 169  LYS   C C    1 
ATOM   18721 O  O    . LYS   C  3  169 ? 11.101  -45.587 -84.834  1.00 105.80 ? 169  LYS   C O    1 
ATOM   18722 C  CB   . LYS   C  3  169 ? 14.211  -47.130 -84.654  1.00 112.28 ? 169  LYS   C CB   1 
ATOM   18723 C  CG   . LYS   C  3  169 ? 15.532  -47.217 -83.909  1.00 117.86 ? 169  LYS   C CG   1 
ATOM   18724 C  CD   . LYS   C  3  169 ? 16.592  -47.901 -84.754  1.00 122.47 ? 169  LYS   C CD   1 
ATOM   18725 C  CE   . LYS   C  3  169 ? 17.927  -47.966 -84.033  1.00 123.55 ? 169  LYS   C CE   1 
ATOM   18726 N  NZ   . LYS   C  3  169 ? 18.987  -48.573 -84.885  1.00 125.55 ? 169  LYS   C NZ   1 
ATOM   18727 H  H    . LYS   C  3  169 ? 13.468  -47.903 -82.470  1.00 116.17 ? 169  LYS   C H    1 
ATOM   18728 H  HA   . LYS   C  3  169 ? 13.279  -45.603 -83.666  1.00 124.72 ? 169  LYS   C HA   1 
ATOM   18729 H  HB2  . LYS   C  3  169 ? 13.965  -48.029 -84.922  1.00 134.71 ? 169  LYS   C HB2  1 
ATOM   18730 H  HB3  . LYS   C  3  169 ? 14.351  -46.577 -85.438  1.00 134.71 ? 169  LYS   C HB3  1 
ATOM   18731 H  HG2  . LYS   C  3  169 ? 15.841  -46.323 -83.694  1.00 141.42 ? 169  LYS   C HG2  1 
ATOM   18732 H  HG3  . LYS   C  3  169 ? 15.411  -47.731 -83.095  1.00 141.42 ? 169  LYS   C HG3  1 
ATOM   18733 H  HD2  . LYS   C  3  169 ? 16.309  -48.807 -84.953  1.00 146.94 ? 169  LYS   C HD2  1 
ATOM   18734 H  HD3  . LYS   C  3  169 ? 16.715  -47.404 -85.578  1.00 146.94 ? 169  LYS   C HD3  1 
ATOM   18735 H  HE2  . LYS   C  3  169 ? 18.206  -47.068 -83.794  1.00 148.24 ? 169  LYS   C HE2  1 
ATOM   18736 H  HE3  . LYS   C  3  169 ? 17.833  -48.508 -83.233  1.00 148.24 ? 169  LYS   C HE3  1 
ATOM   18737 H  HZ1  . LYS   C  3  169 ? 19.762  -48.580 -84.448  1.00 150.64 ? 169  LYS   C HZ1  1 
ATOM   18738 H  HZ2  . LYS   C  3  169 ? 18.766  -49.409 -85.096  1.00 150.64 ? 169  LYS   C HZ2  1 
ATOM   18739 H  HZ3  . LYS   C  3  169 ? 19.082  -48.101 -85.634  1.00 150.64 ? 169  LYS   C HZ3  1 
ATOM   18740 N  N    . ASP   C  3  170 ? 11.384  -47.811 -85.027  1.00 97.41  ? 170  ASP   C N    1 
ATOM   18741 C  CA   . ASP   C  3  170 ? 10.028  -48.084 -85.471  1.00 94.24  ? 170  ASP   C CA   1 
ATOM   18742 C  C    . ASP   C  3  170 ? 9.213   -48.561 -84.276  1.00 93.06  ? 170  ASP   C C    1 
ATOM   18743 O  O    . ASP   C  3  170 ? 9.759   -48.946 -83.242  1.00 97.75  ? 170  ASP   C O    1 
ATOM   18744 C  CB   . ASP   C  3  170 ? 10.012  -49.131 -86.584  1.00 90.83  ? 170  ASP   C CB   1 
ATOM   18745 C  CG   . ASP   C  3  170 ? 10.619  -50.449 -86.153  1.00 86.65  ? 170  ASP   C CG   1 
ATOM   18746 O  OD1  . ASP   C  3  170 ? 9.976   -51.169 -85.361  1.00 84.16  ? 170  ASP   C OD1  1 
ATOM   18747 O  OD2  . ASP   C  3  170 ? 11.739  -50.764 -86.604  1.00 88.35  ? 170  ASP   C OD2  1 
ATOM   18748 H  H    . ASP   C  3  170 ? 11.904  -48.495 -85.061  1.00 116.87 ? 170  ASP   C H    1 
ATOM   18749 H  HA   . ASP   C  3  170 ? 9.624   -47.282 -85.838  1.00 113.07 ? 170  ASP   C HA   1 
ATOM   18750 H  HB2  . ASP   C  3  170 ? 9.094   -49.296 -86.851  1.00 108.98 ? 170  ASP   C HB2  1 
ATOM   18751 H  HB3  . ASP   C  3  170 ? 10.522  -48.799 -87.339  1.00 108.98 ? 170  ASP   C HB3  1 
ATOM   18752 N  N    . SER   C  3  171 ? 7.893   -48.523 -84.421  1.00 87.73  ? 171  SER   C N    1 
ATOM   18753 C  CA   . SER   C  3  171 ? 6.983   -48.899 -83.340  1.00 85.23  ? 171  SER   C CA   1 
ATOM   18754 C  C    . SER   C  3  171 ? 6.431   -50.305 -83.533  1.00 89.12  ? 171  SER   C C    1 
ATOM   18755 O  O    . SER   C  3  171 ? 5.280   -50.588 -83.185  1.00 93.17  ? 171  SER   C O    1 
ATOM   18756 C  CB   . SER   C  3  171 ? 5.854   -47.879 -83.232  1.00 85.19  ? 171  SER   C CB   1 
ATOM   18757 O  OG   . SER   C  3  171 ? 6.366   -46.594 -82.917  1.00 85.21  ? 171  SER   C OG   1 
ATOM   18758 H  H    . SER   C  3  171 ? 7.495   -48.281 -85.144  1.00 105.25 ? 171  SER   C H    1 
ATOM   18759 H  HA   . SER   C  3  171 ? 7.470   -48.890 -82.501  1.00 102.26 ? 171  SER   C HA   1 
ATOM   18760 H  HB2  . SER   C  3  171 ? 5.387   -47.834 -84.080  1.00 102.21 ? 171  SER   C HB2  1 
ATOM   18761 H  HB3  . SER   C  3  171 ? 5.244   -48.156 -82.531  1.00 102.21 ? 171  SER   C HB3  1 
ATOM   18762 H  HG   . SER   C  3  171 ? 5.747   -46.027 -82.931  1.00 102.24 ? 171  SER   C HG   1 
ATOM   18763 N  N    . THR   C  3  172 ? 7.240   -51.208 -84.076  1.00 89.20  ? 172  THR   C N    1 
ATOM   18764 C  CA   . THR   C  3  172 ? 6.810   -52.559 -84.399  1.00 87.01  ? 172  THR   C CA   1 
ATOM   18765 C  C    . THR   C  3  172 ? 7.190   -53.532 -83.287  1.00 80.23  ? 172  THR   C C    1 
ATOM   18766 O  O    . THR   C  3  172 ? 7.914   -53.200 -82.346  1.00 76.46  ? 172  THR   C O    1 
ATOM   18767 C  CB   . THR   C  3  172 ? 7.426   -53.017 -85.725  1.00 87.42  ? 172  THR   C CB   1 
ATOM   18768 O  OG1  . THR   C  3  172 ? 8.838   -53.200 -85.562  1.00 84.85  ? 172  THR   C OG1  1 
ATOM   18769 C  CG2  . THR   C  3  172 ? 7.169   -51.991 -86.822  1.00 90.12  ? 172  THR   C CG2  1 
ATOM   18770 H  H    . THR   C  3  172 ? 8.064   -51.056 -84.270  1.00 107.02 ? 172  THR   C H    1 
ATOM   18771 H  HA   . THR   C  3  172 ? 5.844   -52.561 -84.488  1.00 104.39 ? 172  THR   C HA   1 
ATOM   18772 H  HB   . THR   C  3  172 ? 7.021   -53.856 -85.996  1.00 104.89 ? 172  THR   C HB   1 
ATOM   18773 H  HG1  . THR   C  3  172 ? 9.167   -52.547 -85.149  1.00 101.80 ? 172  THR   C HG1  1 
ATOM   18774 H  HG21 . THR   C  3  172 ? 7.513   -52.317 -87.669  1.00 108.13 ? 172  THR   C HG21 1 
ATOM   18775 H  HG22 . THR   C  3  172 ? 6.217   -51.831 -86.910  1.00 108.13 ? 172  THR   C HG22 1 
ATOM   18776 H  HG23 . THR   C  3  172 ? 7.610   -51.155 -86.604  1.00 108.13 ? 172  THR   C HG23 1 
ATOM   18777 N  N    . TYR   C  3  173 ? 6.686   -54.755 -83.417  1.00 80.08  ? 173  TYR   C N    1 
ATOM   18778 C  CA   . TYR   C  3  173 ? 6.970   -55.848 -82.502  1.00 78.50  ? 173  TYR   C CA   1 
ATOM   18779 C  C    . TYR   C  3  173 ? 7.592   -57.003 -83.278  1.00 75.99  ? 173  TYR   C C    1 
ATOM   18780 O  O    . TYR   C  3  173 ? 7.608   -57.015 -84.511  1.00 77.05  ? 173  TYR   C O    1 
ATOM   18781 C  CB   . TYR   C  3  173 ? 5.696   -56.316 -81.789  1.00 77.95  ? 173  TYR   C CB   1 
ATOM   18782 C  CG   . TYR   C  3  173 ? 5.035   -55.254 -80.943  1.00 77.54  ? 173  TYR   C CG   1 
ATOM   18783 C  CD1  . TYR   C  3  173 ? 4.197   -54.306 -81.514  1.00 82.00  ? 173  TYR   C CD1  1 
ATOM   18784 C  CD2  . TYR   C  3  173 ? 5.240   -55.207 -79.571  1.00 76.62  ? 173  TYR   C CD2  1 
ATOM   18785 C  CE1  . TYR   C  3  173 ? 3.587   -53.337 -80.743  1.00 83.02  ? 173  TYR   C CE1  1 
ATOM   18786 C  CE2  . TYR   C  3  173 ? 4.634   -54.244 -78.792  1.00 79.76  ? 173  TYR   C CE2  1 
ATOM   18787 C  CZ   . TYR   C  3  173 ? 3.811   -53.310 -79.382  1.00 82.85  ? 173  TYR   C CZ   1 
ATOM   18788 O  OH   . TYR   C  3  173 ? 3.207   -52.354 -78.603  1.00 84.70  ? 173  TYR   C OH   1 
ATOM   18789 H  H    . TYR   C  3  173 ? 6.154   -54.982 -84.054  1.00 96.08  ? 173  TYR   C H    1 
ATOM   18790 H  HA   . TYR   C  3  173 ? 7.601   -55.551 -81.828  1.00 94.18  ? 173  TYR   C HA   1 
ATOM   18791 H  HB2  . TYR   C  3  173 ? 5.054   -56.602 -82.457  1.00 93.52  ? 173  TYR   C HB2  1 
ATOM   18792 H  HB3  . TYR   C  3  173 ? 5.922   -57.058 -81.206  1.00 93.52  ? 173  TYR   C HB3  1 
ATOM   18793 H  HD1  . TYR   C  3  173 ? 4.044   -54.324 -82.432  1.00 98.38  ? 173  TYR   C HD1  1 
ATOM   18794 H  HD2  . TYR   C  3  173 ? 5.795   -55.836 -79.170  1.00 91.92  ? 173  TYR   C HD2  1 
ATOM   18795 H  HE1  . TYR   C  3  173 ? 3.028   -52.707 -81.138  1.00 99.61  ? 173  TYR   C HE1  1 
ATOM   18796 H  HE2  . TYR   C  3  173 ? 4.781   -54.224 -77.874  1.00 95.69  ? 173  TYR   C HE2  1 
ATOM   18797 H  HH   . TYR   C  3  173 ? 2.471   -52.130 -78.941  1.00 101.62 ? 173  TYR   C HH   1 
ATOM   18798 N  N    . SER   C  3  174 ? 8.104   -57.985 -82.540  1.00 73.24  ? 174  SER   C N    1 
ATOM   18799 C  CA   . SER   C  3  174 ? 8.699   -59.169 -83.143  1.00 74.06  ? 174  SER   C CA   1 
ATOM   18800 C  C    . SER   C  3  174 ? 8.361   -60.390 -82.300  1.00 72.01  ? 174  SER   C C    1 
ATOM   18801 O  O    . SER   C  3  174 ? 8.024   -60.285 -81.118  1.00 72.87  ? 174  SER   C O    1 
ATOM   18802 C  CB   . SER   C  3  174 ? 10.217  -59.018 -83.303  1.00 72.64  ? 174  SER   C CB   1 
ATOM   18803 O  OG   . SER   C  3  174 ? 10.516  -58.006 -84.250  1.00 74.12  ? 174  SER   C OG   1 
ATOM   18804 H  H    . SER   C  3  174 ? 8.119   -57.987 -81.680  1.00 87.87  ? 174  SER   C H    1 
ATOM   18805 H  HA   . SER   C  3  174 ? 8.319   -59.309 -84.025  1.00 88.86  ? 174  SER   C HA   1 
ATOM   18806 H  HB2  . SER   C  3  174 ? 10.603  -58.776 -82.447  1.00 87.15  ? 174  SER   C HB2  1 
ATOM   18807 H  HB3  . SER   C  3  174 ? 10.589  -59.859 -83.609  1.00 87.15  ? 174  SER   C HB3  1 
ATOM   18808 H  HG   . SER   C  3  174 ? 11.293  -58.114 -84.551  1.00 88.92  ? 174  SER   C HG   1 
ATOM   18809 N  N    . PHE   C  3  175 ? 8.467   -61.559 -82.929  1.00 72.53  ? 175  PHE   C N    1 
ATOM   18810 C  CA   . PHE   C  3  175 ? 7.933   -62.802 -82.388  1.00 74.79  ? 175  PHE   C CA   1 
ATOM   18811 C  C    . PHE   C  3  175 ? 8.867   -63.941 -82.764  1.00 74.83  ? 175  PHE   C C    1 
ATOM   18812 O  O    . PHE   C  3  175 ? 9.252   -64.070 -83.930  1.00 78.17  ? 175  PHE   C O    1 
ATOM   18813 C  CB   . PHE   C  3  175 ? 6.519   -63.045 -82.943  1.00 79.24  ? 175  PHE   C CB   1 
ATOM   18814 C  CG   . PHE   C  3  175 ? 5.726   -64.107 -82.218  1.00 83.37  ? 175  PHE   C CG   1 
ATOM   18815 C  CD1  . PHE   C  3  175 ? 6.252   -65.366 -81.971  1.00 91.32  ? 175  PHE   C CD1  1 
ATOM   18816 C  CD2  . PHE   C  3  175 ? 4.433   -63.841 -81.802  1.00 85.34  ? 175  PHE   C CD2  1 
ATOM   18817 C  CE1  . PHE   C  3  175 ? 5.506   -66.330 -81.314  1.00 96.94  ? 175  PHE   C CE1  1 
ATOM   18818 C  CE2  . PHE   C  3  175 ? 3.685   -64.800 -81.148  1.00 90.84  ? 175  PHE   C CE2  1 
ATOM   18819 C  CZ   . PHE   C  3  175 ? 4.222   -66.044 -80.902  1.00 95.87  ? 175  PHE   C CZ   1 
ATOM   18820 H  H    . PHE   C  3  175 ? 8.855   -61.658 -83.690  1.00 87.01  ? 175  PHE   C H    1 
ATOM   18821 H  HA   . PHE   C  3  175 ? 7.887   -62.769 -81.420  1.00 89.72  ? 175  PHE   C HA   1 
ATOM   18822 H  HB2  . PHE   C  3  175 ? 6.018   -62.216 -82.883  1.00 95.07  ? 175  PHE   C HB2  1 
ATOM   18823 H  HB3  . PHE   C  3  175 ? 6.595   -63.320 -83.870  1.00 95.07  ? 175  PHE   C HB3  1 
ATOM   18824 H  HD1  . PHE   C  3  175 ? 7.116   -65.566 -82.251  1.00 109.57 ? 175  PHE   C HD1  1 
ATOM   18825 H  HD2  . PHE   C  3  175 ? 4.062   -63.004 -81.966  1.00 102.39 ? 175  PHE   C HD2  1 
ATOM   18826 H  HE1  . PHE   C  3  175 ? 5.872   -67.169 -81.151  1.00 116.31 ? 175  PHE   C HE1  1 
ATOM   18827 H  HE2  . PHE   C  3  175 ? 2.818   -64.606 -80.874  1.00 108.98 ? 175  PHE   C HE2  1 
ATOM   18828 H  HZ   . PHE   C  3  175 ? 3.720   -66.690 -80.459  1.00 115.02 ? 175  PHE   C HZ   1 
ATOM   18829 N  N    . SER   C  3  176 ? 9.233   -64.760 -81.778  1.00 72.27  ? 176  SER   C N    1 
ATOM   18830 C  CA   . SER   C  3  176 ? 10.001  -65.979 -81.999  1.00 72.54  ? 176  SER   C CA   1 
ATOM   18831 C  C    . SER   C  3  176 ? 9.201   -67.172 -81.496  1.00 74.43  ? 176  SER   C C    1 
ATOM   18832 O  O    . SER   C  3  176 ? 8.757   -67.184 -80.344  1.00 75.48  ? 176  SER   C O    1 
ATOM   18833 C  CB   . SER   C  3  176 ? 11.359  -65.928 -81.290  1.00 68.47  ? 176  SER   C CB   1 
ATOM   18834 O  OG   . SER   C  3  176 ? 11.978  -67.205 -81.302  1.00 67.29  ? 176  SER   C OG   1 
ATOM   18835 H  H    . SER   C  3  176 ? 9.041   -64.624 -80.951  1.00 86.70  ? 176  SER   C H    1 
ATOM   18836 H  HA   . SER   C  3  176 ? 10.160  -66.084 -82.950  1.00 87.03  ? 176  SER   C HA   1 
ATOM   18837 H  HB2  . SER   C  3  176 ? 11.932  -65.294 -81.748  1.00 82.15  ? 176  SER   C HB2  1 
ATOM   18838 H  HB3  . SER   C  3  176 ? 11.225  -65.650 -80.370  1.00 82.15  ? 176  SER   C HB3  1 
ATOM   18839 H  HG   . SER   C  3  176 ? 12.742  -67.158 -80.955  1.00 80.72  ? 176  SER   C HG   1 
ATOM   18840 N  N    . SER   C  3  177 ? 9.024   -68.172 -82.358  1.00 74.37  ? 177  SER   C N    1 
ATOM   18841 C  CA   . SER   C  3  177 ? 8.308   -69.394 -82.013  1.00 76.25  ? 177  SER   C CA   1 
ATOM   18842 C  C    . SER   C  3  177 ? 9.181   -70.590 -82.355  1.00 74.50  ? 177  SER   C C    1 
ATOM   18843 O  O    . SER   C  3  177 ? 9.725   -70.668 -83.462  1.00 74.04  ? 177  SER   C O    1 
ATOM   18844 C  CB   . SER   C  3  177 ? 6.970   -69.483 -82.754  1.00 80.79  ? 177  SER   C CB   1 
ATOM   18845 O  OG   . SER   C  3  177 ? 6.249   -70.642 -82.370  1.00 83.42  ? 177  SER   C OG   1 
ATOM   18846 H  H    . SER   C  3  177 ? 9.318   -68.165 -83.166  1.00 89.22  ? 177  SER   C H    1 
ATOM   18847 H  HA   . SER   C  3  177 ? 8.127   -69.407 -81.060  1.00 91.48  ? 177  SER   C HA   1 
ATOM   18848 H  HB2  . SER   C  3  177 ? 6.440   -68.699 -82.542  1.00 96.93  ? 177  SER   C HB2  1 
ATOM   18849 H  HB3  . SER   C  3  177 ? 7.141   -69.521 -83.708  1.00 96.93  ? 177  SER   C HB3  1 
ATOM   18850 H  HG   . SER   C  3  177 ? 6.067   -70.609 -81.551  1.00 100.08 ? 177  SER   C HG   1 
ATOM   18851 N  N    . THR   C  3  178 ? 9.307   -71.521 -81.411  1.00 74.99  ? 178  THR   C N    1 
ATOM   18852 C  CA   . THR   C  3  178 ? 10.199  -72.668 -81.549  1.00 78.36  ? 178  THR   C CA   1 
ATOM   18853 C  C    . THR   C  3  178 ? 9.429   -73.938 -81.212  1.00 80.01  ? 178  THR   C C    1 
ATOM   18854 O  O    . THR   C  3  178 ? 9.015   -74.131 -80.064  1.00 80.02  ? 178  THR   C O    1 
ATOM   18855 C  CB   . THR   C  3  178 ? 11.422  -72.524 -80.641  1.00 76.26  ? 178  THR   C CB   1 
ATOM   18856 O  OG1  . THR   C  3  178 ? 12.047  -71.255 -80.870  1.00 74.61  ? 178  THR   C OG1  1 
ATOM   18857 C  CG2  . THR   C  3  178 ? 12.426  -73.629 -80.918  1.00 75.96  ? 178  THR   C CG2  1 
ATOM   18858 H  H    . THR   C  3  178 ? 8.876   -71.509 -80.667  1.00 89.96  ? 178  THR   C H    1 
ATOM   18859 H  HA   . THR   C  3  178 ? 10.494  -72.729 -82.471  1.00 94.01  ? 178  THR   C HA   1 
ATOM   18860 H  HB   . THR   C  3  178 ? 11.142  -72.586 -79.714  1.00 91.49  ? 178  THR   C HB   1 
ATOM   18861 H  HG1  . THR   C  3  178 ? 12.696  -71.155 -80.346  1.00 89.52  ? 178  THR   C HG1  1 
ATOM   18862 H  HG21 . THR   C  3  178 ? 13.222  -73.497 -80.380  1.00 91.13  ? 178  THR   C HG21 1 
ATOM   18863 H  HG22 . THR   C  3  178 ? 12.038  -74.492 -80.701  1.00 91.13  ? 178  THR   C HG22 1 
ATOM   18864 H  HG23 . THR   C  3  178 ? 12.675  -73.623 -81.856  1.00 91.13  ? 178  THR   C HG23 1 
ATOM   18865 N  N    . LEU   C  3  179 ? 9.243   -74.801 -82.208  1.00 80.98  ? 179  LEU   C N    1 
ATOM   18866 C  CA   . LEU   C  3  179 ? 8.669   -76.126 -81.995  1.00 83.62  ? 179  LEU   C CA   1 
ATOM   18867 C  C    . LEU   C  3  179 ? 9.814   -77.105 -81.761  1.00 82.61  ? 179  LEU   C C    1 
ATOM   18868 O  O    . LEU   C  3  179 ? 10.616  -77.362 -82.665  1.00 81.08  ? 179  LEU   C O    1 
ATOM   18869 C  CB   . LEU   C  3  179 ? 7.819   -76.558 -83.186  1.00 87.19  ? 179  LEU   C CB   1 
ATOM   18870 C  CG   . LEU   C  3  179 ? 7.222   -77.963 -83.066  1.00 89.24  ? 179  LEU   C CG   1 
ATOM   18871 C  CD1  . LEU   C  3  179 ? 6.156   -78.016 -81.980  1.00 91.55  ? 179  LEU   C CD1  1 
ATOM   18872 C  CD2  . LEU   C  3  179 ? 6.659   -78.422 -84.399  1.00 94.08  ? 179  LEU   C CD2  1 
ATOM   18873 H  H    . LEU   C  3  179 ? 9.445   -74.640 -83.028  1.00 97.16  ? 179  LEU   C H    1 
ATOM   18874 H  HA   . LEU   C  3  179 ? 8.098   -76.106 -81.212  1.00 100.32 ? 179  LEU   C HA   1 
ATOM   18875 H  HB2  . LEU   C  3  179 ? 7.083   -75.934 -83.282  1.00 104.61 ? 179  LEU   C HB2  1 
ATOM   18876 H  HB3  . LEU   C  3  179 ? 8.374   -76.542 -83.982  1.00 104.61 ? 179  LEU   C HB3  1 
ATOM   18877 H  HG   . LEU   C  3  179 ? 7.928   -78.579 -82.812  1.00 107.07 ? 179  LEU   C HG   1 
ATOM   18878 H  HD11 . LEU   C  3  179 ? 5.810   -78.920 -81.920  1.00 109.84 ? 179  LEU   C HD11 1 
ATOM   18879 H  HD12 . LEU   C  3  179 ? 6.555   -77.757 -81.134  1.00 109.84 ? 179  LEU   C HD12 1 
ATOM   18880 H  HD13 . LEU   C  3  179 ? 5.441   -77.402 -82.209  1.00 109.84 ? 179  LEU   C HD13 1 
ATOM   18881 H  HD21 . LEU   C  3  179 ? 6.283   -79.310 -84.294  1.00 112.88 ? 179  LEU   C HD21 1 
ATOM   18882 H  HD22 . LEU   C  3  179 ? 5.968   -77.802 -84.680  1.00 112.88 ? 179  LEU   C HD22 1 
ATOM   18883 H  HD23 . LEU   C  3  179 ? 7.373   -78.440 -85.054  1.00 112.88 ? 179  LEU   C HD23 1 
ATOM   18884 N  N    . THR   C  3  180 ? 9.888   -77.647 -80.550  1.00 85.89  ? 180  THR   C N    1 
ATOM   18885 C  CA   . THR   C  3  180 ? 10.929  -78.591 -80.172  1.00 92.09  ? 180  THR   C CA   1 
ATOM   18886 C  C    . THR   C  3  180 ? 10.358  -80.002 -80.152  1.00 92.49  ? 180  THR   C C    1 
ATOM   18887 O  O    . THR   C  3  180 ? 9.326   -80.252 -79.520  1.00 94.05  ? 180  THR   C O    1 
ATOM   18888 C  CB   . THR   C  3  180 ? 11.512  -78.234 -78.804  1.00 99.50  ? 180  THR   C CB   1 
ATOM   18889 O  OG1  . THR   C  3  180 ? 10.470  -78.228 -77.820  1.00 109.20 ? 180  THR   C OG1  1 
ATOM   18890 C  CG2  . THR   C  3  180 ? 12.164  -76.860 -78.852  1.00 94.48  ? 180  THR   C CG2  1 
ATOM   18891 H  H    . THR   C  3  180 ? 9.332   -77.479 -79.916  1.00 103.05 ? 180  THR   C H    1 
ATOM   18892 H  HA   . THR   C  3  180 ? 11.646  -78.563 -80.825  1.00 110.49 ? 180  THR   C HA   1 
ATOM   18893 H  HB   . THR   C  3  180 ? 12.184  -78.889 -78.557  1.00 119.38 ? 180  THR   C HB   1 
ATOM   18894 H  HG1  . THR   C  3  180 ? 10.005  -78.924 -77.889  1.00 131.02 ? 180  THR   C HG1  1 
ATOM   18895 H  HG21 . THR   C  3  180 ? 12.701  -76.719 -78.056  1.00 113.36 ? 180  THR   C HG21 1 
ATOM   18896 H  HG22 . THR   C  3  180 ? 12.735  -76.790 -79.633  1.00 113.36 ? 180  THR   C HG22 1 
ATOM   18897 H  HG23 . THR   C  3  180 ? 11.482  -76.171 -78.898  1.00 113.36 ? 180  THR   C HG23 1 
ATOM   18898 N  N    . LEU   C  3  181 ? 11.028  -80.916 -80.848  1.00 92.28  ? 181  LEU   C N    1 
ATOM   18899 C  CA   . LEU   C  3  181 ? 10.632  -82.313 -80.923  1.00 94.82  ? 181  LEU   C CA   1 
ATOM   18900 C  C    . LEU   C  3  181 ? 11.834  -83.182 -80.578  1.00 93.63  ? 181  LEU   C C    1 
ATOM   18901 O  O    . LEU   C  3  181 ? 12.936  -82.687 -80.321  1.00 88.72  ? 181  LEU   C O    1 
ATOM   18902 C  CB   . LEU   C  3  181 ? 10.109  -82.673 -82.320  1.00 98.89  ? 181  LEU   C CB   1 
ATOM   18903 C  CG   . LEU   C  3  181 ? 9.178   -81.679 -83.013  1.00 101.59 ? 181  LEU   C CG   1 
ATOM   18904 C  CD1  . LEU   C  3  181 ? 9.108   -81.991 -84.502  1.00 103.73 ? 181  LEU   C CD1  1 
ATOM   18905 C  CD2  . LEU   C  3  181 ? 7.794   -81.710 -82.391  1.00 105.70 ? 181  LEU   C CD2  1 
ATOM   18906 H  H    . LEU   C  3  181 ? 11.739  -80.741 -81.300  1.00 110.72 ? 181  LEU   C H    1 
ATOM   18907 H  HA   . LEU   C  3  181 ? 9.926   -82.472 -80.277  1.00 113.77 ? 181  LEU   C HA   1 
ATOM   18908 H  HB2  . LEU   C  3  181 ? 10.877  -82.788 -82.901  1.00 118.65 ? 181  LEU   C HB2  1 
ATOM   18909 H  HB3  . LEU   C  3  181 ? 9.621   -83.508 -82.246  1.00 118.65 ? 181  LEU   C HB3  1 
ATOM   18910 H  HG   . LEU   C  3  181 ? 9.527   -80.781 -82.902  1.00 121.89 ? 181  LEU   C HG   1 
ATOM   18911 H  HD11 . LEU   C  3  181 ? 8.524   -81.347 -84.932  1.00 124.46 ? 181  LEU   C HD11 1 
ATOM   18912 H  HD12 . LEU   C  3  181 ? 10.000  -81.933 -84.879  1.00 124.46 ? 181  LEU   C HD12 1 
ATOM   18913 H  HD13 . LEU   C  3  181 ? 8.756   -82.887 -84.621  1.00 124.46 ? 181  LEU   C HD13 1 
ATOM   18914 H  HD21 . LEU   C  3  181 ? 7.228   -81.069 -82.850  1.00 126.83 ? 181  LEU   C HD21 1 
ATOM   18915 H  HD22 . LEU   C  3  181 ? 7.426   -82.602 -82.484  1.00 126.83 ? 181  LEU   C HD22 1 
ATOM   18916 H  HD23 . LEU   C  3  181 ? 7.864   -81.477 -81.452  1.00 126.83 ? 181  LEU   C HD23 1 
ATOM   18917 N  N    . THR   C  3  182 ? 11.615  -84.492 -80.575  1.00 98.89  ? 182  THR   C N    1 
ATOM   18918 C  CA   . THR   C  3  182 ? 12.722  -85.430 -80.563  1.00 100.08 ? 182  THR   C CA   1 
ATOM   18919 C  C    . THR   C  3  182 ? 13.257  -85.598 -81.981  1.00 98.94  ? 182  THR   C C    1 
ATOM   18920 O  O    . THR   C  3  182 ? 12.563  -85.339 -82.967  1.00 101.25 ? 182  THR   C O    1 
ATOM   18921 C  CB   . THR   C  3  182 ? 12.288  -86.787 -80.005  1.00 110.80 ? 182  THR   C CB   1 
ATOM   18922 O  OG1  . THR   C  3  182 ? 11.280  -87.357 -80.849  1.00 121.53 ? 182  THR   C OG1  1 
ATOM   18923 C  CG2  . THR   C  3  182 ? 11.742  -86.637 -78.594  1.00 109.51 ? 182  THR   C CG2  1 
ATOM   18924 H  H    . THR   C  3  182 ? 10.837  -84.858 -80.580  1.00 118.65 ? 182  THR   C H    1 
ATOM   18925 H  HA   . THR   C  3  182 ? 13.429  -85.095 -79.990  1.00 120.07 ? 182  THR   C HA   1 
ATOM   18926 H  HB   . THR   C  3  182 ? 13.054  -87.381 -79.974  1.00 132.94 ? 182  THR   C HB   1 
ATOM   18927 H  HG1  . THR   C  3  182 ? 11.072  -88.122 -80.572  1.00 145.81 ? 182  THR   C HG1  1 
ATOM   18928 H  HG21 . THR   C  3  182 ? 11.495  -87.505 -78.240  1.00 131.39 ? 182  THR   C HG21 1 
ATOM   18929 H  HG22 . THR   C  3  182 ? 12.415  -86.241 -78.018  1.00 131.39 ? 182  THR   C HG22 1 
ATOM   18930 H  HG23 . THR   C  3  182 ? 10.958  -86.065 -78.601  1.00 131.39 ? 182  THR   C HG23 1 
ATOM   18931 N  N    . LYS   C  3  183 ? 14.515  -86.030 -82.079  1.00 96.95  ? 183  LYS   C N    1 
ATOM   18932 C  CA   . LYS   C  3  183 ? 15.079  -86.291 -83.398  1.00 97.97  ? 183  LYS   C CA   1 
ATOM   18933 C  C    . LYS   C  3  183 ? 14.285  -87.372 -84.116  1.00 104.99 ? 183  LYS   C C    1 
ATOM   18934 O  O    . LYS   C  3  183 ? 14.079  -87.301 -85.333  1.00 110.72 ? 183  LYS   C O    1 
ATOM   18935 C  CB   . LYS   C  3  183 ? 16.548  -86.695 -83.284  1.00 94.50  ? 183  LYS   C CB   1 
ATOM   18936 C  CG   . LYS   C  3  183 ? 17.155  -87.123 -84.612  1.00 95.78  ? 183  LYS   C CG   1 
ATOM   18937 C  CD   . LYS   C  3  183 ? 18.565  -87.651 -84.454  1.00 97.48  ? 183  LYS   C CD   1 
ATOM   18938 C  CE   . LYS   C  3  183 ? 18.855  -88.708 -85.501  1.00 109.58 ? 183  LYS   C CE   1 
ATOM   18939 N  NZ   . LYS   C  3  183 ? 20.262  -88.669 -85.960  1.00 113.13 ? 183  LYS   C NZ   1 
ATOM   18940 H  H    . LYS   C  3  183 ? 15.045  -86.176 -81.418  1.00 116.33 ? 183  LYS   C H    1 
ATOM   18941 H  HA   . LYS   C  3  183 ? 15.040  -85.475 -83.922  1.00 117.54 ? 183  LYS   C HA   1 
ATOM   18942 H  HB2  . LYS   C  3  183 ? 17.057  -85.939 -82.953  1.00 113.38 ? 183  LYS   C HB2  1 
ATOM   18943 H  HB3  . LYS   C  3  183 ? 16.622  -87.440 -82.668  1.00 113.38 ? 183  LYS   C HB3  1 
ATOM   18944 H  HG2  . LYS   C  3  183 ? 16.611  -87.827 -84.998  1.00 114.91 ? 183  LYS   C HG2  1 
ATOM   18945 H  HG3  . LYS   C  3  183 ? 17.183  -86.360 -85.209  1.00 114.91 ? 183  LYS   C HG3  1 
ATOM   18946 H  HD2  . LYS   C  3  183 ? 19.198  -86.925 -84.565  1.00 116.95 ? 183  LYS   C HD2  1 
ATOM   18947 H  HD3  . LYS   C  3  183 ? 18.667  -88.050 -83.576  1.00 116.95 ? 183  LYS   C HD3  1 
ATOM   18948 H  HE2  . LYS   C  3  183 ? 18.685  -89.586 -85.123  1.00 131.48 ? 183  LYS   C HE2  1 
ATOM   18949 H  HE3  . LYS   C  3  183 ? 18.282  -88.561 -86.270  1.00 131.48 ? 183  LYS   C HE3  1 
ATOM   18950 H  HZ1  . LYS   C  3  183 ? 20.390  -89.275 -86.600  1.00 135.74 ? 183  LYS   C HZ1  1 
ATOM   18951 H  HZ2  . LYS   C  3  183 ? 20.454  -87.863 -86.283  1.00 135.74 ? 183  LYS   C HZ2  1 
ATOM   18952 H  HZ3  . LYS   C  3  183 ? 20.809  -88.846 -85.281  1.00 135.74 ? 183  LYS   C HZ3  1 
ATOM   18953 N  N    . ASP   C  3  184 ? 13.836  -88.387 -83.376  1.00 105.62 ? 184  ASP   C N    1 
ATOM   18954 C  CA   . ASP   C  3  184 ? 13.017  -89.435 -83.970  1.00 113.13 ? 184  ASP   C CA   1 
ATOM   18955 C  C    . ASP   C  3  184 ? 11.742  -88.852 -84.565  1.00 114.99 ? 184  ASP   C C    1 
ATOM   18956 O  O    . ASP   C  3  184 ? 11.482  -88.983 -85.766  1.00 116.76 ? 184  ASP   C O    1 
ATOM   18957 C  CB   . ASP   C  3  184 ? 12.689  -90.497 -82.919  1.00 116.55 ? 184  ASP   C CB   1 
ATOM   18958 C  CG   . ASP   C  3  184 ? 13.920  -91.231 -82.429  1.00 115.24 ? 184  ASP   C CG   1 
ATOM   18959 O  OD1  . ASP   C  3  184 ? 15.019  -90.978 -82.966  1.00 112.54 ? 184  ASP   C OD1  1 
ATOM   18960 O  OD2  . ASP   C  3  184 ? 13.788  -92.060 -81.505  1.00 116.85 ? 184  ASP   C OD2  1 
ATOM   18961 H  H    . ASP   C  3  184 ? 13.992  -88.488 -82.536  1.00 126.73 ? 184  ASP   C H    1 
ATOM   18962 H  HA   . ASP   C  3  184 ? 13.517  -89.863 -84.683  1.00 135.74 ? 184  ASP   C HA   1 
ATOM   18963 H  HB2  . ASP   C  3  184 ? 12.270  -90.069 -82.156  1.00 139.84 ? 184  ASP   C HB2  1 
ATOM   18964 H  HB3  . ASP   C  3  184 ? 12.084  -91.150 -83.306  1.00 139.84 ? 184  ASP   C HB3  1 
ATOM   18965 N  N    . GLU   C  3  185 ? 10.938  -88.184 -83.733  1.00 114.24 ? 185  GLU   C N    1 
ATOM   18966 C  CA   . GLU   C  3  185 ? 9.665   -87.652 -84.206  1.00 118.33 ? 185  GLU   C CA   1 
ATOM   18967 C  C    . GLU   C  3  185 ? 9.866   -86.672 -85.355  1.00 117.66 ? 185  GLU   C C    1 
ATOM   18968 O  O    . GLU   C  3  185 ? 9.058   -86.629 -86.291  1.00 123.09 ? 185  GLU   C O    1 
ATOM   18969 C  CB   . GLU   C  3  185 ? 8.917   -86.980 -83.055  1.00 116.18 ? 185  GLU   C CB   1 
ATOM   18970 C  CG   . GLU   C  3  185 ? 7.460   -86.680 -83.362  1.00 122.52 ? 185  GLU   C CG   1 
ATOM   18971 C  CD   . GLU   C  3  185 ? 6.726   -86.077 -82.180  1.00 123.45 ? 185  GLU   C CD   1 
ATOM   18972 O  OE1  . GLU   C  3  185 ? 7.379   -85.409 -81.350  1.00 119.35 ? 185  GLU   C OE1  1 
ATOM   18973 O  OE2  . GLU   C  3  185 ? 5.498   -86.277 -82.077  1.00 127.77 ? 185  GLU   C OE2  1 
ATOM   18974 H  H    . GLU   C  3  185 ? 11.106  -88.028 -82.904  1.00 137.07 ? 185  GLU   C H    1 
ATOM   18975 H  HA   . GLU   C  3  185 ? 9.122   -88.388 -84.530  1.00 141.97 ? 185  GLU   C HA   1 
ATOM   18976 H  HB2  . GLU   C  3  185 ? 8.942   -87.566 -82.283  1.00 139.39 ? 185  GLU   C HB2  1 
ATOM   18977 H  HB3  . GLU   C  3  185 ? 9.355   -86.139 -82.848  1.00 139.39 ? 185  GLU   C HB3  1 
ATOM   18978 H  HG2  . GLU   C  3  185 ? 7.414   -86.048 -84.097  1.00 147.01 ? 185  GLU   C HG2  1 
ATOM   18979 H  HG3  . GLU   C  3  185 ? 7.011   -87.504 -83.605  1.00 147.01 ? 185  GLU   C HG3  1 
ATOM   18980 N  N    . TYR   C  3  186 ? 10.934  -85.873 -85.305  1.00 111.56 ? 186  TYR   C N    1 
ATOM   18981 C  CA   . TYR   C  3  186 ? 11.200  -84.943 -86.397  1.00 111.03 ? 186  TYR   C CA   1 
ATOM   18982 C  C    . TYR   C  3  186 ? 11.471  -85.692 -87.696  1.00 116.49 ? 186  TYR   C C    1 
ATOM   18983 O  O    . TYR   C  3  186 ? 10.933  -85.343 -88.753  1.00 121.14 ? 186  TYR   C O    1 
ATOM   18984 C  CB   . TYR   C  3  186 ? 12.381  -84.034 -86.054  1.00 104.15 ? 186  TYR   C CB   1 
ATOM   18985 C  CG   . TYR   C  3  186 ? 12.831  -83.187 -87.225  1.00 102.62 ? 186  TYR   C CG   1 
ATOM   18986 C  CD1  . TYR   C  3  186 ? 12.123  -82.053 -87.599  1.00 101.34 ? 186  TYR   C CD1  1 
ATOM   18987 C  CD2  . TYR   C  3  186 ? 13.957  -83.528 -87.962  1.00 103.18 ? 186  TYR   C CD2  1 
ATOM   18988 C  CE1  . TYR   C  3  186 ? 12.525  -81.281 -88.671  1.00 101.15 ? 186  TYR   C CE1  1 
ATOM   18989 C  CE2  . TYR   C  3  186 ? 14.368  -82.760 -89.034  1.00 103.28 ? 186  TYR   C CE2  1 
ATOM   18990 C  CZ   . TYR   C  3  186 ? 13.645  -81.640 -89.387  1.00 101.77 ? 186  TYR   C CZ   1 
ATOM   18991 O  OH   . TYR   C  3  186 ? 14.050  -80.871 -90.453  1.00 100.58 ? 186  TYR   C OH   1 
ATOM   18992 H  H    . TYR   C  3  186 ? 11.506  -85.851 -84.663  1.00 133.86 ? 186  TYR   C H    1 
ATOM   18993 H  HA   . TYR   C  3  186 ? 10.417  -84.382 -86.520  1.00 133.21 ? 186  TYR   C HA   1 
ATOM   18994 H  HB2  . TYR   C  3  186 ? 12.121  -83.438 -85.334  1.00 124.96 ? 186  TYR   C HB2  1 
ATOM   18995 H  HB3  . TYR   C  3  186 ? 13.130  -84.583 -85.775  1.00 124.96 ? 186  TYR   C HB3  1 
ATOM   18996 H  HD1  . TYR   C  3  186 ? 11.364  -81.809 -87.119  1.00 121.59 ? 186  TYR   C HD1  1 
ATOM   18997 H  HD2  . TYR   C  3  186 ? 14.443  -84.286 -87.731  1.00 123.80 ? 186  TYR   C HD2  1 
ATOM   18998 H  HE1  . TYR   C  3  186 ? 12.041  -80.522 -88.908  1.00 121.36 ? 186  TYR   C HE1  1 
ATOM   18999 H  HE2  . TYR   C  3  186 ? 15.128  -82.996 -89.515  1.00 123.92 ? 186  TYR   C HE2  1 
ATOM   19000 H  HH   . TYR   C  3  186 ? 14.777  -81.160 -90.757  1.00 120.68 ? 186  TYR   C HH   1 
ATOM   19001 N  N    . GLU   C  3  187 ? 12.305  -86.731 -87.635  1.00 115.64 ? 187  GLU   C N    1 
ATOM   19002 C  CA   . GLU   C  3  187 ? 12.679  -87.469 -88.834  1.00 119.85 ? 187  GLU   C CA   1 
ATOM   19003 C  C    . GLU   C  3  187 ? 11.555  -88.344 -89.371  1.00 128.37 ? 187  GLU   C C    1 
ATOM   19004 O  O    . GLU   C  3  187 ? 11.708  -88.917 -90.455  1.00 137.81 ? 187  GLU   C O    1 
ATOM   19005 C  CB   . GLU   C  3  187 ? 13.912  -88.332 -88.550  1.00 119.20 ? 187  GLU   C CB   1 
ATOM   19006 C  CG   . GLU   C  3  187 ? 15.186  -87.530 -88.336  1.00 114.35 ? 187  GLU   C CG   1 
ATOM   19007 C  CD   . GLU   C  3  187 ? 16.405  -88.407 -88.163  1.00 114.28 ? 187  GLU   C CD   1 
ATOM   19008 O  OE1  . GLU   C  3  187 ? 16.246  -89.585 -87.781  1.00 117.41 ? 187  GLU   C OE1  1 
ATOM   19009 O  OE2  . GLU   C  3  187 ? 17.525  -87.916 -88.416  1.00 110.53 ? 187  GLU   C OE2  1 
ATOM   19010 H  H    . GLU   C  3  187 ? 12.666  -87.025 -86.911  1.00 138.75 ? 187  GLU   C H    1 
ATOM   19011 H  HA   . GLU   C  3  187 ? 12.910  -86.831 -89.527  1.00 143.80 ? 187  GLU   C HA   1 
ATOM   19012 H  HB2  . GLU   C  3  187 ? 13.750  -88.852 -87.747  1.00 143.02 ? 187  GLU   C HB2  1 
ATOM   19013 H  HB3  . GLU   C  3  187 ? 14.058  -88.924 -89.305  1.00 143.02 ? 187  GLU   C HB3  1 
ATOM   19014 H  HG2  . GLU   C  3  187 ? 15.334  -86.959 -89.106  1.00 137.20 ? 187  GLU   C HG2  1 
ATOM   19015 H  HG3  . GLU   C  3  187 ? 15.089  -86.990 -87.536  1.00 137.20 ? 187  GLU   C HG3  1 
ATOM   19016 N  N    . ARG   C  3  188 ? 10.435  -88.462 -88.654  1.00 125.32 ? 188  ARG   C N    1 
ATOM   19017 C  CA   . ARG   C  3  188 ? 9.338   -89.295 -89.132  1.00 129.01 ? 188  ARG   C CA   1 
ATOM   19018 C  C    . ARG   C  3  188 ? 8.476   -88.577 -90.163  1.00 131.21 ? 188  ARG   C C    1 
ATOM   19019 O  O    . ARG   C  3  188 ? 7.949   -89.222 -91.077  1.00 135.83 ? 188  ARG   C O    1 
ATOM   19020 C  CB   . ARG   C  3  188 ? 8.468   -89.753 -87.960  1.00 128.77 ? 188  ARG   C CB   1 
ATOM   19021 C  CG   . ARG   C  3  188 ? 9.151   -90.771 -87.068  1.00 127.92 ? 188  ARG   C CG   1 
ATOM   19022 C  CD   . ARG   C  3  188 ? 8.155   -91.614 -86.293  1.00 133.14 ? 188  ARG   C CD   1 
ATOM   19023 N  NE   . ARG   C  3  188 ? 8.744   -92.894 -85.909  1.00 137.05 ? 188  ARG   C NE   1 
ATOM   19024 C  CZ   . ARG   C  3  188 ? 8.757   -93.978 -86.681  1.00 145.98 ? 188  ARG   C CZ   1 
ATOM   19025 N  NH1  . ARG   C  3  188 ? 8.210   -93.950 -87.889  1.00 149.87 ? 188  ARG   C NH1  1 
ATOM   19026 N  NH2  . ARG   C  3  188 ? 9.321   -95.096 -86.243  1.00 149.60 ? 188  ARG   C NH2  1 
ATOM   19027 H  H    . ARG   C  3  188 ? 10.290  -88.074 -87.899  1.00 150.37 ? 188  ARG   C H    1 
ATOM   19028 H  HA   . ARG   C  3  188 ? 9.715   -90.083 -89.553  1.00 154.79 ? 188  ARG   C HA   1 
ATOM   19029 H  HB2  . ARG   C  3  188 ? 8.245   -88.982 -87.416  1.00 154.51 ? 188  ARG   C HB2  1 
ATOM   19030 H  HB3  . ARG   C  3  188 ? 7.659   -90.158 -88.309  1.00 154.51 ? 188  ARG   C HB3  1 
ATOM   19031 H  HG2  . ARG   C  3  188 ? 9.688   -91.364 -87.615  1.00 153.48 ? 188  ARG   C HG2  1 
ATOM   19032 H  HG3  . ARG   C  3  188 ? 9.715   -90.307 -86.429  1.00 153.48 ? 188  ARG   C HG3  1 
ATOM   19033 H  HD2  . ARG   C  3  188 ? 7.891   -91.143 -85.487  1.00 159.75 ? 188  ARG   C HD2  1 
ATOM   19034 H  HD3  . ARG   C  3  188 ? 7.378   -91.787 -86.847  1.00 159.75 ? 188  ARG   C HD3  1 
ATOM   19035 H  HE   . ARG   C  3  188 ? 9.106   -92.951 -85.131  1.00 164.44 ? 188  ARG   C HE   1 
ATOM   19036 H  HH11 . ARG   C  3  188 ? 7.843   -93.228 -88.179  1.00 179.83 ? 188  ARG   C HH11 1 
ATOM   19037 H  HH12 . ARG   C  3  188 ? 8.223   -94.654 -88.383  1.00 179.83 ? 188  ARG   C HH12 1 
ATOM   19038 H  HH21 . ARG   C  3  188 ? 9.677   -95.120 -85.461  1.00 179.50 ? 188  ARG   C HH21 1 
ATOM   19039 H  HH22 . ARG   C  3  188 ? 9.330   -95.796 -86.742  1.00 179.50 ? 188  ARG   C HH22 1 
ATOM   19040 N  N    . HIS   C  3  189 ? 8.320   -87.265 -90.039  1.00 129.11 ? 189  HIS   C N    1 
ATOM   19041 C  CA   . HIS   C  3  189 ? 7.516   -86.479 -90.962  1.00 133.74 ? 189  HIS   C CA   1 
ATOM   19042 C  C    . HIS   C  3  189 ? 8.421   -85.726 -91.934  1.00 135.30 ? 189  HIS   C C    1 
ATOM   19043 O  O    . HIS   C  3  189 ? 9.644   -85.686 -91.781  1.00 133.83 ? 189  HIS   C O    1 
ATOM   19044 C  CB   . HIS   C  3  189 ? 6.613   -85.516 -90.189  1.00 126.96 ? 189  HIS   C CB   1 
ATOM   19045 C  CG   . HIS   C  3  189 ? 5.816   -86.180 -89.109  1.00 125.46 ? 189  HIS   C CG   1 
ATOM   19046 N  ND1  . HIS   C  3  189 ? 6.341   -86.462 -87.866  1.00 120.77 ? 189  HIS   C ND1  1 
ATOM   19047 C  CD2  . HIS   C  3  189 ? 4.540   -86.632 -89.089  1.00 130.61 ? 189  HIS   C CD2  1 
ATOM   19048 C  CE1  . HIS   C  3  189 ? 5.420   -87.051 -87.124  1.00 124.30 ? 189  HIS   C CE1  1 
ATOM   19049 N  NE2  . HIS   C  3  189 ? 4.318   -87.166 -87.843  1.00 130.63 ? 189  HIS   C NE2  1 
ATOM   19050 H  H    . HIS   C  3  189 ? 8.678   -86.797 -89.412  1.00 154.91 ? 189  HIS   C H    1 
ATOM   19051 H  HA   . HIS   C  3  189 ? 6.945   -87.067 -91.482  1.00 160.47 ? 189  HIS   C HA   1 
ATOM   19052 H  HB2  . HIS   C  3  189 ? 7.165   -84.834 -89.775  1.00 152.33 ? 189  HIS   C HB2  1 
ATOM   19053 H  HB3  . HIS   C  3  189 ? 5.989   -85.107 -90.809  1.00 152.33 ? 189  HIS   C HB3  1 
ATOM   19054 H  HD1  . HIS   C  3  189 ? 7.143   -86.283 -87.612  1.00 144.91 ? 189  HIS   C HD1  1 
ATOM   19055 H  HD2  . HIS   C  3  189 ? 3.928   -86.588 -89.788  1.00 156.72 ? 189  HIS   C HD2  1 
ATOM   19056 H  HE1  . HIS   C  3  189 ? 5.529   -87.336 -86.245  1.00 149.14 ? 189  HIS   C HE1  1 
ATOM   19057 N  N    . ASN   C  3  190 ? 7.800   -85.126 -92.948  1.00 136.56 ? 190  ASN   C N    1 
ATOM   19058 C  CA   . ASN   C  3  190 ? 8.528   -84.505 -94.048  1.00 132.92 ? 190  ASN   C CA   1 
ATOM   19059 C  C    . ASN   C  3  190 ? 8.354   -82.995 -94.106  1.00 129.27 ? 190  ASN   C C    1 
ATOM   19060 O  O    . ASN   C  3  190 ? 9.347   -82.264 -94.170  1.00 125.59 ? 190  ASN   C O    1 
ATOM   19061 C  CB   . ASN   C  3  190 ? 8.085   -85.130 -95.380  1.00 135.83 ? 190  ASN   C CB   1 
ATOM   19062 C  CG   . ASN   C  3  190 ? 9.208   -85.196 -96.395  1.00 131.92 ? 190  ASN   C CG   1 
ATOM   19063 O  OD1  . ASN   C  3  190 ? 10.070  -86.073 -96.325  1.00 127.41 ? 190  ASN   C OD1  1 
ATOM   19064 N  ND2  . ASN   C  3  190 ? 9.203   -84.273 -97.349  1.00 133.68 ? 190  ASN   C ND2  1 
ATOM   19065 H  H    . ASN   C  3  190 ? 6.945   -85.066 -93.021  1.00 163.85 ? 190  ASN   C H    1 
ATOM   19066 H  HA   . ASN   C  3  190 ? 9.474   -84.682 -93.929  1.00 159.48 ? 190  ASN   C HA   1 
ATOM   19067 H  HB2  . ASN   C  3  190 ? 7.772   -86.034 -95.218  1.00 162.97 ? 190  ASN   C HB2  1 
ATOM   19068 H  HB3  . ASN   C  3  190 ? 7.369   -84.595 -95.758  1.00 162.97 ? 190  ASN   C HB3  1 
ATOM   19069 H  HD21 . ASN   C  3  190 ? 9.820   -84.269 -97.948  1.00 160.40 ? 190  ASN   C HD21 1 
ATOM   19070 H  HD22 . ASN   C  3  190 ? 8.582   -83.678 -97.368  1.00 160.40 ? 190  ASN   C HD22 1 
ATOM   19071 N  N    . SER   C  3  191 ? 7.120   -82.503 -94.085  1.00 129.91 ? 191  SER   C N    1 
ATOM   19072 C  CA   . SER   C  3  191 ? 6.868   -81.074 -94.195  1.00 124.72 ? 191  SER   C CA   1 
ATOM   19073 C  C    . SER   C  3  191 ? 6.788   -80.436 -92.813  1.00 120.51 ? 191  SER   C C    1 
ATOM   19074 O  O    . SER   C  3  191 ? 6.460   -81.091 -91.820  1.00 123.29 ? 191  SER   C O    1 
ATOM   19075 C  CB   . SER   C  3  191 ? 5.572   -80.808 -94.963  1.00 126.77 ? 191  SER   C CB   1 
ATOM   19076 O  OG   . SER   C  3  191 ? 4.436   -81.177 -94.200  1.00 127.46 ? 191  SER   C OG   1 
ATOM   19077 H  H    . SER   C  3  191 ? 6.409   -82.980 -94.008  1.00 155.87 ? 191  SER   C H    1 
ATOM   19078 H  HA   . SER   C  3  191 ? 7.598   -80.659 -94.680  1.00 149.65 ? 191  SER   C HA   1 
ATOM   19079 H  HB2  . SER   C  3  191 ? 5.517   -79.861 -95.169  1.00 152.10 ? 191  SER   C HB2  1 
ATOM   19080 H  HB3  . SER   C  3  191 ? 5.581   -81.325 -95.784  1.00 152.10 ? 191  SER   C HB3  1 
ATOM   19081 H  HG   . SER   C  3  191 ? 4.341   -80.650 -93.553  1.00 152.93 ? 191  SER   C HG   1 
ATOM   19082 N  N    . TYR   C  3  192 ? 7.096   -79.143 -92.762  1.00 113.62 ? 192  TYR   C N    1 
ATOM   19083 C  CA   . TYR   C  3  192 ? 7.023   -78.373 -91.527  1.00 108.60 ? 192  TYR   C CA   1 
ATOM   19084 C  C    . TYR   C  3  192 ? 6.618   -76.951 -91.875  1.00 106.28 ? 192  TYR   C C    1 
ATOM   19085 O  O    . TYR   C  3  192 ? 7.204   -76.340 -92.774  1.00 106.60 ? 192  TYR   C O    1 
ATOM   19086 C  CB   . TYR   C  3  192 ? 8.359   -78.394 -90.782  1.00 103.94 ? 192  TYR   C CB   1 
ATOM   19087 C  CG   . TYR   C  3  192 ? 8.645   -79.727 -90.137  1.00 106.00 ? 192  TYR   C CG   1 
ATOM   19088 C  CD1  . TYR   C  3  192 ? 8.170   -80.019 -88.866  1.00 104.40 ? 192  TYR   C CD1  1 
ATOM   19089 C  CD2  . TYR   C  3  192 ? 9.375   -80.701 -90.804  1.00 110.16 ? 192  TYR   C CD2  1 
ATOM   19090 C  CE1  . TYR   C  3  192 ? 8.421   -81.239 -88.274  1.00 106.11 ? 192  TYR   C CE1  1 
ATOM   19091 C  CE2  . TYR   C  3  192 ? 9.631   -81.924 -90.221  1.00 112.16 ? 192  TYR   C CE2  1 
ATOM   19092 C  CZ   . TYR   C  3  192 ? 9.151   -82.188 -88.956  1.00 110.09 ? 192  TYR   C CZ   1 
ATOM   19093 O  OH   . TYR   C  3  192 ? 9.404   -83.405 -88.371  1.00 110.97 ? 192  TYR   C OH   1 
ATOM   19094 H  H    . TYR   C  3  192 ? 7.353   -78.682 -93.441  1.00 136.32 ? 192  TYR   C H    1 
ATOM   19095 H  HA   . TYR   C  3  192 ? 6.350   -78.749 -90.939  1.00 130.30 ? 192  TYR   C HA   1 
ATOM   19096 H  HB2  . TYR   C  3  192 ? 9.074   -78.204 -91.409  1.00 124.71 ? 192  TYR   C HB2  1 
ATOM   19097 H  HB3  . TYR   C  3  192 ? 8.342   -77.720 -90.084  1.00 124.71 ? 192  TYR   C HB3  1 
ATOM   19098 H  HD1  . TYR   C  3  192 ? 7.673   -79.381 -88.406  1.00 125.27 ? 192  TYR   C HD1  1 
ATOM   19099 H  HD2  . TYR   C  3  192 ? 9.697   -80.525 -91.659  1.00 132.17 ? 192  TYR   C HD2  1 
ATOM   19100 H  HE1  . TYR   C  3  192 ? 8.099   -81.420 -87.420  1.00 127.31 ? 192  TYR   C HE1  1 
ATOM   19101 H  HE2  . TYR   C  3  192 ? 10.124  -82.566 -90.678  1.00 134.58 ? 192  TYR   C HE2  1 
ATOM   19102 H  HH   . TYR   C  3  192 ? 9.905   -83.863 -88.867  1.00 133.14 ? 192  TYR   C HH   1 
ATOM   19103 N  N    . THR   C  3  193 ? 5.622   -76.430 -91.163  1.00 104.78 ? 193  THR   C N    1 
ATOM   19104 C  CA   . THR   C  3  193 ? 4.993   -75.173 -91.533  1.00 105.39 ? 193  THR   C CA   1 
ATOM   19105 C  C    . THR   C  3  193 ? 4.742   -74.322 -90.299  1.00 104.44 ? 193  THR   C C    1 
ATOM   19106 O  O    . THR   C  3  193 ? 4.391   -74.836 -89.233  1.00 103.05 ? 193  THR   C O    1 
ATOM   19107 C  CB   . THR   C  3  193 ? 3.669   -75.415 -92.270  1.00 108.01 ? 193  THR   C CB   1 
ATOM   19108 O  OG1  . THR   C  3  193 ? 3.909   -76.194 -93.449  1.00 108.12 ? 193  THR   C OG1  1 
ATOM   19109 C  CG2  . THR   C  3  193 ? 3.024   -74.096 -92.656  1.00 112.11 ? 193  THR   C CG2  1 
ATOM   19110 H  H    . THR   C  3  193 ? 5.293   -76.792 -90.455  1.00 125.71 ? 193  THR   C H    1 
ATOM   19111 H  HA   . THR   C  3  193 ? 5.594   -74.679 -92.113  1.00 126.44 ? 193  THR   C HA   1 
ATOM   19112 H  HB   . THR   C  3  193 ? 3.058   -75.894 -91.689  1.00 129.59 ? 193  THR   C HB   1 
ATOM   19113 H  HG1  . THR   C  3  193 ? 3.179   -76.432 -93.790  1.00 129.72 ? 193  THR   C HG1  1 
ATOM   19114 H  HG21 . THR   C  3  193 ? 2.315   -74.248 -93.300  1.00 134.51 ? 193  THR   C HG21 1 
ATOM   19115 H  HG22 . THR   C  3  193 ? 2.648   -73.668 -91.871  1.00 134.51 ? 193  THR   C HG22 1 
ATOM   19116 H  HG23 . THR   C  3  193 ? 3.686   -73.505 -93.050  1.00 134.51 ? 193  THR   C HG23 1 
ATOM   19117 N  N    . CYS   C  3  194 ? 4.921   -73.014 -90.465  1.00 104.76 ? 194  CYS   C N    1 
ATOM   19118 C  CA   . CYS   C  3  194 ? 4.691   -72.020 -89.422  1.00 102.81 ? 194  CYS   C CA   1 
ATOM   19119 C  C    . CYS   C  3  194 ? 3.683   -71.010 -89.955  1.00 102.43 ? 194  CYS   C C    1 
ATOM   19120 O  O    . CYS   C  3  194 ? 3.979   -70.268 -90.898  1.00 103.26 ? 194  CYS   C O    1 
ATOM   19121 C  CB   . CYS   C  3  194 ? 6.004   -71.348 -89.026  1.00 100.69 ? 194  CYS   C CB   1 
ATOM   19122 S  SG   . CYS   C  3  194 ? 5.856   -69.674 -88.370  1.00 104.66 ? 194  CYS   C SG   1 
ATOM   19123 H  H    . CYS   C  3  194 ? 5.186   -72.664 -91.205  1.00 125.69 ? 194  CYS   C H    1 
ATOM   19124 H  HA   . CYS   C  3  194 ? 4.315   -72.439 -88.633  1.00 123.35 ? 194  CYS   C HA   1 
ATOM   19125 H  HB2  . CYS   C  3  194 ? 6.429   -71.889 -88.343  1.00 120.80 ? 194  CYS   C HB2  1 
ATOM   19126 H  HB3  . CYS   C  3  194 ? 6.571   -71.301 -89.812  1.00 120.80 ? 194  CYS   C HB3  1 
ATOM   19127 N  N    . GLU   C  3  195 ? 2.496   -70.985 -89.355  1.00 100.30 ? 195  GLU   C N    1 
ATOM   19128 C  CA   . GLU   C  3  195 ? 1.383   -70.176 -89.833  1.00 103.29 ? 195  GLU   C CA   1 
ATOM   19129 C  C    . GLU   C  3  195 ? 1.146   -69.005 -88.892  1.00 103.77 ? 195  GLU   C C    1 
ATOM   19130 O  O    . GLU   C  3  195 ? 0.955   -69.201 -87.688  1.00 104.14 ? 195  GLU   C O    1 
ATOM   19131 C  CB   . GLU   C  3  195 ? 0.107   -71.013 -89.944  1.00 104.09 ? 195  GLU   C CB   1 
ATOM   19132 C  CG   . GLU   C  3  195 ? 0.052   -71.918 -91.156  1.00 110.76 ? 195  GLU   C CG   1 
ATOM   19133 C  CD   . GLU   C  3  195 ? -1.270  -72.651 -91.268  1.00 119.74 ? 195  GLU   C CD   1 
ATOM   19134 O  OE1  . GLU   C  3  195 ? -1.355  -73.606 -92.068  1.00 125.44 ? 195  GLU   C OE1  1 
ATOM   19135 O  OE2  . GLU   C  3  195 ? -2.224  -72.274 -90.555  1.00 122.03 ? 195  GLU   C OE2  1 
ATOM   19136 H  H    . GLU   C  3  195 ? 2.309   -71.440 -88.650  1.00 120.34 ? 195  GLU   C H    1 
ATOM   19137 H  HA   . GLU   C  3  195 ? 1.605   -69.823 -90.709  1.00 123.92 ? 195  GLU   C HA   1 
ATOM   19138 H  HB2  . GLU   C  3  195 ? 0.038   -71.575 -89.156  1.00 124.89 ? 195  GLU   C HB2  1 
ATOM   19139 H  HB3  . GLU   C  3  195 ? -0.653  -70.413 -89.991  1.00 124.89 ? 195  GLU   C HB3  1 
ATOM   19140 H  HG2  . GLU   C  3  195 ? 0.169   -71.383 -91.957  1.00 132.89 ? 195  GLU   C HG2  1 
ATOM   19141 H  HG3  . GLU   C  3  195 ? 0.760   -72.579 -91.092  1.00 132.89 ? 195  GLU   C HG3  1 
ATOM   19142 N  N    . ALA   C  3  196 ? 1.138   -67.796 -89.447  1.00 101.72 ? 196  ALA   C N    1 
ATOM   19143 C  CA   . ALA   C  3  196 ? 0.911   -66.575 -88.687  1.00 97.99  ? 196  ALA   C CA   1 
ATOM   19144 C  C    . ALA   C  3  196 ? -0.410  -65.949 -89.113  1.00 104.04 ? 196  ALA   C C    1 
ATOM   19145 O  O    . ALA   C  3  196 ? -0.689  -65.833 -90.311  1.00 104.96 ? 196  ALA   C O    1 
ATOM   19146 C  CB   . ALA   C  3  196 ? 2.055   -65.580 -88.893  1.00 92.03  ? 196  ALA   C CB   1 
ATOM   19147 H  H    . ALA   C  3  196 ? 1.267   -67.656 -90.286  1.00 122.05 ? 196  ALA   C H    1 
ATOM   19148 H  HA   . ALA   C  3  196 ? 0.857   -66.790 -87.743  1.00 117.57 ? 196  ALA   C HA   1 
ATOM   19149 H  HB1  . ALA   C  3  196 ? 1.886   -64.790 -88.356  1.00 110.42 ? 196  ALA   C HB1  1 
ATOM   19150 H  HB2  . ALA   C  3  196 ? 2.887   -65.995 -88.618  1.00 110.42 ? 196  ALA   C HB2  1 
ATOM   19151 H  HB3  . ALA   C  3  196 ? 2.099   -65.339 -89.831  1.00 110.42 ? 196  ALA   C HB3  1 
ATOM   19152 N  N    . THR   C  3  197 ? -1.215  -65.548 -88.131  1.00 107.64 ? 197  THR   C N    1 
ATOM   19153 C  CA   . THR   C  3  197 ? -2.493  -64.883 -88.368  1.00 114.96 ? 197  THR   C CA   1 
ATOM   19154 C  C    . THR   C  3  197 ? -2.389  -63.471 -87.804  1.00 112.54 ? 197  THR   C C    1 
ATOM   19155 O  O    . THR   C  3  197 ? -2.348  -63.288 -86.582  1.00 110.84 ? 197  THR   C O    1 
ATOM   19156 C  CB   . THR   C  3  197 ? -3.651  -65.644 -87.720  1.00 119.49 ? 197  THR   C CB   1 
ATOM   19157 O  OG1  . THR   C  3  197 ? -3.714  -65.329 -86.324  1.00 120.56 ? 197  THR   C OG1  1 
ATOM   19158 C  CG2  . THR   C  3  197 ? -3.483  -67.156 -87.891  1.00 118.00 ? 197  THR   C CG2  1 
ATOM   19159 H  H    . THR   C  3  197 ? -1.037  -65.654 -87.296  1.00 129.15 ? 197  THR   C H    1 
ATOM   19160 H  HA   . THR   C  3  197 ? -2.661  -64.836 -89.322  1.00 137.93 ? 197  THR   C HA   1 
ATOM   19161 H  HB   . THR   C  3  197 ? -4.481  -65.384 -88.151  1.00 143.37 ? 197  THR   C HB   1 
ATOM   19162 H  HG1  . THR   C  3  197 ? -4.048  -64.565 -86.216  1.00 144.65 ? 197  THR   C HG1  1 
ATOM   19163 H  HG21 . THR   C  3  197 ? -4.178  -67.625 -87.404  1.00 141.58 ? 197  THR   C HG21 1 
ATOM   19164 H  HG22 . THR   C  3  197 ? -3.542  -67.393 -88.830  1.00 141.58 ? 197  THR   C HG22 1 
ATOM   19165 H  HG23 . THR   C  3  197 ? -2.618  -67.434 -87.550  1.00 141.58 ? 197  THR   C HG23 1 
ATOM   19166 N  N    . HIS   C  3  198 ? -2.340  -62.479 -88.688  1.00 104.34 ? 198  HIS   C N    1 
ATOM   19167 C  CA   . HIS   C  3  198 ? -2.233  -61.079 -88.303  1.00 101.40 ? 198  HIS   C CA   1 
ATOM   19168 C  C    . HIS   C  3  198 ? -3.414  -60.304 -88.873  1.00 106.84 ? 198  HIS   C C    1 
ATOM   19169 O  O    . HIS   C  3  198 ? -3.995  -60.687 -89.893  1.00 114.54 ? 198  HIS   C O    1 
ATOM   19170 C  CB   . HIS   C  3  198 ? -0.914  -60.468 -88.798  1.00 96.88  ? 198  HIS   C CB   1 
ATOM   19171 C  CG   . HIS   C  3  198 ? -0.555  -59.178 -88.127  1.00 97.67  ? 198  HIS   C CG   1 
ATOM   19172 N  ND1  . HIS   C  3  198 ? -0.675  -58.988 -86.767  1.00 96.61  ? 198  HIS   C ND1  1 
ATOM   19173 C  CD2  . HIS   C  3  198 ? -0.071  -58.017 -88.627  1.00 98.14  ? 198  HIS   C CD2  1 
ATOM   19174 C  CE1  . HIS   C  3  198 ? -0.285  -57.763 -86.459  1.00 95.10  ? 198  HIS   C CE1  1 
ATOM   19175 N  NE2  . HIS   C  3  198 ? 0.086   -57.153 -87.570  1.00 95.57  ? 198  HIS   C NE2  1 
ATOM   19176 H  H    . HIS   C  3  198 ? -2.367  -62.597 -89.540  1.00 125.19 ? 198  HIS   C H    1 
ATOM   19177 H  HA   . HIS   C  3  198 ? -2.256  -61.001 -87.337  1.00 121.66 ? 198  HIS   C HA   1 
ATOM   19178 H  HB2  . HIS   C  3  198 ? -0.197  -61.098 -88.630  1.00 116.24 ? 198  HIS   C HB2  1 
ATOM   19179 H  HB3  . HIS   C  3  198 ? -0.988  -60.295 -89.749  1.00 116.24 ? 198  HIS   C HB3  1 
ATOM   19180 H  HD1  . HIS   C  3  198 ? -0.958  -59.575 -86.206  1.00 115.91 ? 198  HIS   C HD1  1 
ATOM   19181 H  HD2  . HIS   C  3  198 ? 0.119   -57.837 -89.520  1.00 117.75 ? 198  HIS   C HD2  1 
ATOM   19182 H  HE1  . HIS   C  3  198 ? -0.274  -57.394 -85.606  1.00 114.11 ? 198  HIS   C HE1  1 
ATOM   19183 N  N    . LYS   C  3  199 ? -3.769  -59.206 -88.201  1.00 104.48 ? 199  LYS   C N    1 
ATOM   19184 C  CA   . LYS   C  3  199 ? -4.881  -58.385 -88.665  1.00 109.95 ? 199  LYS   C CA   1 
ATOM   19185 C  C    . LYS   C  3  199 ? -4.561  -57.664 -89.968  1.00 110.66 ? 199  LYS   C C    1 
ATOM   19186 O  O    . LYS   C  3  199 ? -5.483  -57.201 -90.648  1.00 114.69 ? 199  LYS   C O    1 
ATOM   19187 C  CB   . LYS   C  3  199 ? -5.271  -57.361 -87.595  1.00 112.82 ? 199  LYS   C CB   1 
ATOM   19188 C  CG   . LYS   C  3  199 ? -6.507  -56.540 -87.951  1.00 126.93 ? 199  LYS   C CG   1 
ATOM   19189 C  CD   . LYS   C  3  199 ? -6.924  -55.606 -86.822  1.00 134.08 ? 199  LYS   C CD   1 
ATOM   19190 C  CE   . LYS   C  3  199 ? -5.943  -54.457 -86.637  1.00 132.10 ? 199  LYS   C CE   1 
ATOM   19191 N  NZ   . LYS   C  3  199 ? -5.855  -53.588 -87.844  1.00 135.80 ? 199  LYS   C NZ   1 
ATOM   19192 H  H    . LYS   C  3  199 ? -3.386  -58.921 -87.485  1.00 125.36 ? 199  LYS   C H    1 
ATOM   19193 H  HA   . LYS   C  3  199 ? -5.645  -58.963 -88.818  1.00 131.93 ? 199  LYS   C HA   1 
ATOM   19194 H  HB2  . LYS   C  3  199 ? -5.456  -57.831 -86.767  1.00 135.36 ? 199  LYS   C HB2  1 
ATOM   19195 H  HB3  . LYS   C  3  199 ? -4.532  -56.745 -87.470  1.00 135.36 ? 199  LYS   C HB3  1 
ATOM   19196 H  HG2  . LYS   C  3  199 ? -6.316  -56.000 -88.733  1.00 152.29 ? 199  LYS   C HG2  1 
ATOM   19197 H  HG3  . LYS   C  3  199 ? -7.247  -57.140 -88.134  1.00 152.29 ? 199  LYS   C HG3  1 
ATOM   19198 H  HD2  . LYS   C  3  199 ? -7.795  -55.230 -87.024  1.00 160.88 ? 199  LYS   C HD2  1 
ATOM   19199 H  HD3  . LYS   C  3  199 ? -6.963  -56.106 -85.992  1.00 160.88 ? 199  LYS   C HD3  1 
ATOM   19200 H  HE2  . LYS   C  3  199 ? -6.232  -53.908 -85.891  1.00 158.50 ? 199  LYS   C HE2  1 
ATOM   19201 H  HE3  . LYS   C  3  199 ? -5.060  -54.818 -86.460  1.00 158.50 ? 199  LYS   C HE3  1 
ATOM   19202 H  HZ1  . LYS   C  3  199 ? -5.423  -52.835 -87.647  1.00 162.94 ? 199  LYS   C HZ1  1 
ATOM   19203 H  HZ2  . LYS   C  3  199 ? -5.416  -54.011 -88.493  1.00 162.94 ? 199  LYS   C HZ2  1 
ATOM   19204 H  HZ3  . LYS   C  3  199 ? -6.672  -53.385 -88.133  1.00 162.94 ? 199  LYS   C HZ3  1 
ATOM   19205 N  N    . THR   C  3  200 ? -3.282  -57.562 -90.334  1.00 110.02 ? 200  THR   C N    1 
ATOM   19206 C  CA   . THR   C  3  200 ? -2.908  -56.839 -91.542  1.00 117.61 ? 200  THR   C CA   1 
ATOM   19207 C  C    . THR   C  3  200 ? -3.393  -57.535 -92.808  1.00 126.69 ? 200  THR   C C    1 
ATOM   19208 O  O    . THR   C  3  200 ? -3.434  -56.902 -93.869  1.00 135.48 ? 200  THR   C O    1 
ATOM   19209 C  CB   . THR   C  3  200 ? -1.388  -56.657 -91.593  1.00 112.32 ? 200  THR   C CB   1 
ATOM   19210 O  OG1  . THR   C  3  200 ? -1.048  -55.697 -92.601  1.00 119.56 ? 200  THR   C OG1  1 
ATOM   19211 C  CG2  . THR   C  3  200 ? -0.692  -57.979 -91.895  1.00 104.86 ? 200  THR   C CG2  1 
ATOM   19212 H  H    . THR   C  3  200 ? -2.619  -57.901 -89.901  1.00 132.00 ? 200  THR   C H    1 
ATOM   19213 H  HA   . THR   C  3  200 ? -3.314  -55.958 -91.517  1.00 141.11 ? 200  THR   C HA   1 
ATOM   19214 H  HB   . THR   C  3  200 ? -1.076  -56.343 -90.730  1.00 134.76 ? 200  THR   C HB   1 
ATOM   19215 H  HG1  . THR   C  3  200 ? -1.577  -55.762 -93.251  1.00 143.45 ? 200  THR   C HG1  1 
ATOM   19216 H  HG21 . THR   C  3  200 ? 0.267   -57.882 -91.784  1.00 125.81 ? 200  THR   C HG21 1 
ATOM   19217 H  HG22 . THR   C  3  200 ? -1.011  -58.668 -91.290  1.00 125.81 ? 200  THR   C HG22 1 
ATOM   19218 H  HG23 . THR   C  3  200 ? -0.877  -58.251 -92.807  1.00 125.81 ? 200  THR   C HG23 1 
ATOM   19219 N  N    . SER   C  3  201 ? -3.757  -58.813 -92.725  1.00 123.39 ? 201  SER   C N    1 
ATOM   19220 C  CA   . SER   C  3  201 ? -4.273  -59.544 -93.874  1.00 122.62 ? 201  SER   C CA   1 
ATOM   19221 C  C    . SER   C  3  201 ? -5.192  -60.654 -93.387  1.00 120.07 ? 201  SER   C C    1 
ATOM   19222 O  O    . SER   C  3  201 ? -4.938  -61.268 -92.348  1.00 115.26 ? 201  SER   C O    1 
ATOM   19223 C  CB   . SER   C  3  201 ? -3.142  -60.137 -94.722  1.00 118.88 ? 201  SER   C CB   1 
ATOM   19224 O  OG   . SER   C  3  201 ? -2.431  -59.124 -95.413  1.00 117.94 ? 201  SER   C OG   1 
ATOM   19225 H  H    . SER   C  3  201 ? -3.714  -59.282 -92.005  1.00 148.05 ? 201  SER   C H    1 
ATOM   19226 H  HA   . SER   C  3  201 ? -4.788  -58.940 -94.431  1.00 147.13 ? 201  SER   C HA   1 
ATOM   19227 H  HB2  . SER   C  3  201 ? -2.527  -60.610 -94.140  1.00 142.63 ? 201  SER   C HB2  1 
ATOM   19228 H  HB3  . SER   C  3  201 ? -3.523  -60.750 -95.370  1.00 142.63 ? 201  SER   C HB3  1 
ATOM   19229 H  HG   . SER   C  3  201 ? -2.686  -58.367 -95.154  1.00 141.50 ? 201  SER   C HG   1 
ATOM   19230 N  N    . THR   C  3  202 ? -6.260  -60.905 -94.148  1.00 123.72 ? 202  THR   C N    1 
ATOM   19231 C  CA   . THR   C  3  202 ? -7.194  -61.972 -93.813  1.00 123.62 ? 202  THR   C CA   1 
ATOM   19232 C  C    . THR   C  3  202 ? -6.647  -63.352 -94.150  1.00 124.08 ? 202  THR   C C    1 
ATOM   19233 O  O    . THR   C  3  202 ? -7.115  -64.346 -93.583  1.00 119.97 ? 202  THR   C O    1 
ATOM   19234 C  CB   . THR   C  3  202 ? -8.527  -61.768 -94.543  1.00 127.72 ? 202  THR   C CB   1 
ATOM   19235 O  OG1  . THR   C  3  202 ? -9.445  -62.803 -94.166  1.00 131.31 ? 202  THR   C OG1  1 
ATOM   19236 C  CG2  . THR   C  3  202 ? -8.329  -61.793 -96.059  1.00 128.76 ? 202  THR   C CG2  1 
ATOM   19237 H  H    . THR   C  3  202 ? -6.463  -60.470 -94.862  1.00 148.44 ? 202  THR   C H    1 
ATOM   19238 H  HA   . THR   C  3  202 ? -7.368  -61.937 -92.859  1.00 148.33 ? 202  THR   C HA   1 
ATOM   19239 H  HB   . THR   C  3  202 ? -8.894  -60.904 -94.301  1.00 153.24 ? 202  THR   C HB   1 
ATOM   19240 H  HG1  . THR   C  3  202 ? -10.190 -62.674 -94.531  1.00 157.55 ? 202  THR   C HG1  1 
ATOM   19241 H  HG21 . THR   C  3  202 ? -9.176  -61.639 -96.506  1.00 154.49 ? 202  THR   C HG21 1 
ATOM   19242 H  HG22 . THR   C  3  202 ? -7.703  -61.101 -96.323  1.00 154.49 ? 202  THR   C HG22 1 
ATOM   19243 H  HG23 . THR   C  3  202 ? -7.980  -62.655 -96.333  1.00 154.49 ? 202  THR   C HG23 1 
ATOM   19244 N  N    . SER   C  3  203 ? -5.676  -63.434 -95.059  1.00 129.96 ? 203  SER   C N    1 
ATOM   19245 C  CA   . SER   C  3  203 ? -5.065  -64.706 -95.420  1.00 134.27 ? 203  SER   C CA   1 
ATOM   19246 C  C    . SER   C  3  203 ? -3.833  -64.931 -94.557  1.00 127.92 ? 203  SER   C C    1 
ATOM   19247 O  O    . SER   C  3  203 ? -2.867  -64.161 -94.667  1.00 122.81 ? 203  SER   C O    1 
ATOM   19248 C  CB   . SER   C  3  203 ? -4.685  -64.716 -96.892  1.00 139.09 ? 203  SER   C CB   1 
ATOM   19249 O  OG   . SER   C  3  203 ? -3.973  -63.541 -97.241  1.00 137.51 ? 203  SER   C OG   1 
ATOM   19250 H  H    . SER   C  3  203 ? -5.353  -62.760 -95.483  1.00 155.93 ? 203  SER   C H    1 
ATOM   19251 H  HA   . SER   C  3  203 ? -5.694  -65.425 -95.252  1.00 161.11 ? 203  SER   C HA   1 
ATOM   19252 H  HB2  . SER   C  3  203 ? -4.125  -65.488 -97.067  1.00 166.89 ? 203  SER   C HB2  1 
ATOM   19253 H  HB3  . SER   C  3  203 ? -5.494  -64.764 -97.425  1.00 166.89 ? 203  SER   C HB3  1 
ATOM   19254 H  HG   . SER   C  3  203 ? -3.346  -63.414 -96.697  1.00 164.99 ? 203  SER   C HG   1 
ATOM   19255 N  N    . PRO   C  3  204 ? -3.811  -65.945 -93.692  1.00 126.35 ? 204  PRO   C N    1 
ATOM   19256 C  CA   . PRO   C  3  204 ? -2.633  -66.152 -92.840  1.00 116.63 ? 204  PRO   C CA   1 
ATOM   19257 C  C    . PRO   C  3  204 ? -1.372  -66.332 -93.672  1.00 112.36 ? 204  PRO   C C    1 
ATOM   19258 O  O    . PRO   C  3  204 ? -1.348  -67.099 -94.637  1.00 112.61 ? 204  PRO   C O    1 
ATOM   19259 C  CB   . PRO   C  3  204 ? -2.979  -67.423 -92.055  1.00 117.68 ? 204  PRO   C CB   1 
ATOM   19260 C  CG   . PRO   C  3  204 ? -4.462  -67.516 -92.099  1.00 125.68 ? 204  PRO   C CG   1 
ATOM   19261 C  CD   . PRO   C  3  204 ? -4.868  -66.936 -93.419  1.00 131.50 ? 204  PRO   C CD   1 
ATOM   19262 H  HA   . PRO   C  3  204 ? -2.518  -65.408 -92.228  1.00 139.93 ? 204  PRO   C HA   1 
ATOM   19263 H  HB2  . PRO   C  3  204 ? -2.571  -68.194 -92.479  1.00 141.19 ? 204  PRO   C HB2  1 
ATOM   19264 H  HB3  . PRO   C  3  204 ? -2.664  -67.343 -91.141  1.00 141.19 ? 204  PRO   C HB3  1 
ATOM   19265 H  HG2  . PRO   C  3  204 ? -4.735  -68.444 -92.033  1.00 150.80 ? 204  PRO   C HG2  1 
ATOM   19266 H  HG3  . PRO   C  3  204 ? -4.844  -67.005 -91.368  1.00 150.80 ? 204  PRO   C HG3  1 
ATOM   19267 H  HD2  . PRO   C  3  204 ? -4.885  -67.620 -94.106  1.00 157.78 ? 204  PRO   C HD2  1 
ATOM   19268 H  HD3  . PRO   C  3  204 ? -5.736  -66.507 -93.356  1.00 157.78 ? 204  PRO   C HD3  1 
ATOM   19269 N  N    . ILE   C  3  205 ? -0.316  -65.612 -93.292  1.00 110.50 ? 205  ILE   C N    1 
ATOM   19270 C  CA   . ILE   C  3  205 ? 0.973   -65.783 -93.950  1.00 113.05 ? 205  ILE   C CA   1 
ATOM   19271 C  C    . ILE   C  3  205 ? 1.558   -67.126 -93.538  1.00 114.88 ? 205  ILE   C C    1 
ATOM   19272 O  O    . ILE   C  3  205 ? 1.547   -67.492 -92.355  1.00 109.93 ? 205  ILE   C O    1 
ATOM   19273 C  CB   . ILE   C  3  205 ? 1.919   -64.623 -93.607  1.00 107.86 ? 205  ILE   C CB   1 
ATOM   19274 C  CG1  . ILE   C  3  205 ? 1.316   -63.302 -94.097  1.00 112.65 ? 205  ILE   C CG1  1 
ATOM   19275 C  CG2  . ILE   C  3  205 ? 3.296   -64.852 -94.227  1.00 104.05 ? 205  ILE   C CG2  1 
ATOM   19276 C  CD1  . ILE   C  3  205 ? 2.226   -62.095 -93.943  1.00 110.26 ? 205  ILE   C CD1  1 
ATOM   19277 H  H    . ILE   C  3  205 ? -0.322  -65.024 -92.664  1.00 132.58 ? 205  ILE   C H    1 
ATOM   19278 H  HA   . ILE   C  3  205 ? 0.847   -65.783 -94.912  1.00 135.64 ? 205  ILE   C HA   1 
ATOM   19279 H  HB   . ILE   C  3  205 ? 2.025   -64.580 -92.643  1.00 129.41 ? 205  ILE   C HB   1 
ATOM   19280 H  HG12 . ILE   C  3  205 ? 1.106   -63.391 -95.040  1.00 135.16 ? 205  ILE   C HG12 1 
ATOM   19281 H  HG13 . ILE   C  3  205 ? 0.508   -63.126 -93.592  1.00 135.16 ? 205  ILE   C HG13 1 
ATOM   19282 H  HG21 . ILE   C  3  205 ? 3.888   -64.133 -93.956  1.00 124.84 ? 205  ILE   C HG21 1 
ATOM   19283 H  HG22 . ILE   C  3  205 ? 3.645   -65.702 -93.916  1.00 124.84 ? 205  ILE   C HG22 1 
ATOM   19284 H  HG23 . ILE   C  3  205 ? 3.210   -64.863 -95.193  1.00 124.84 ? 205  ILE   C HG23 1 
ATOM   19285 H  HD11 . ILE   C  3  205 ? 1.721   -61.292 -94.147  1.00 132.29 ? 205  ILE   C HD11 1 
ATOM   19286 H  HD12 . ILE   C  3  205 ? 2.550   -62.059 -93.030  1.00 132.29 ? 205  ILE   C HD12 1 
ATOM   19287 H  HD13 . ILE   C  3  205 ? 2.972   -62.181 -94.556  1.00 132.29 ? 205  ILE   C HD13 1 
ATOM   19288 N  N    . VAL   C  3  206 ? 2.073   -67.868 -94.515  1.00 120.15 ? 206  VAL   C N    1 
ATOM   19289 C  CA   . VAL   C  3  206 ? 2.554   -69.226 -94.309  1.00 118.36 ? 206  VAL   C CA   1 
ATOM   19290 C  C    . VAL   C  3  206 ? 3.991   -69.317 -94.800  1.00 116.36 ? 206  VAL   C C    1 
ATOM   19291 O  O    . VAL   C  3  206 ? 4.328   -68.791 -95.866  1.00 118.95 ? 206  VAL   C O    1 
ATOM   19292 C  CB   . VAL   C  3  206 ? 1.667   -70.257 -95.041  1.00 120.81 ? 206  VAL   C CB   1 
ATOM   19293 C  CG1  . VAL   C  3  206 ? 2.073   -71.676 -94.674  1.00 118.88 ? 206  VAL   C CG1  1 
ATOM   19294 C  CG2  . VAL   C  3  206 ? 0.197   -70.018 -94.724  1.00 122.82 ? 206  VAL   C CG2  1 
ATOM   19295 H  H    . VAL   C  3  206 ? 2.155   -67.596 -95.327  1.00 144.16 ? 206  VAL   C H    1 
ATOM   19296 H  HA   . VAL   C  3  206 ? 2.544   -69.428 -93.360  1.00 142.01 ? 206  VAL   C HA   1 
ATOM   19297 H  HB   . VAL   C  3  206 ? 1.791   -70.149 -95.997  1.00 144.96 ? 206  VAL   C HB   1 
ATOM   19298 H  HG11 . VAL   C  3  206 ? 1.484   -72.300 -95.126  1.00 142.64 ? 206  VAL   C HG11 1 
ATOM   19299 H  HG12 . VAL   C  3  206 ? 2.989   -71.824 -94.954  1.00 142.64 ? 206  VAL   C HG12 1 
ATOM   19300 H  HG13 . VAL   C  3  206 ? 1.998   -71.787 -93.713  1.00 142.64 ? 206  VAL   C HG13 1 
ATOM   19301 H  HG21 . VAL   C  3  206 ? -0.334  -70.711 -95.147  1.00 147.36 ? 206  VAL   C HG21 1 
ATOM   19302 H  HG22 . VAL   C  3  206 ? 0.072   -70.045 -93.763  1.00 147.36 ? 206  VAL   C HG22 1 
ATOM   19303 H  HG23 . VAL   C  3  206 ? -0.063  -69.148 -95.067  1.00 147.36 ? 206  VAL   C HG23 1 
ATOM   19304 N  N    . LYS   C  3  207 ? 4.838   -69.980 -94.016  1.00 111.79 ? 207  LYS   C N    1 
ATOM   19305 C  CA   . LYS   C  3  207 ? 6.205   -70.286 -94.415  1.00 109.20 ? 207  LYS   C CA   1 
ATOM   19306 C  C    . LYS   C  3  207 ? 6.498   -71.716 -93.992  1.00 106.88 ? 207  LYS   C C    1 
ATOM   19307 O  O    . LYS   C  3  207 ? 6.237   -72.088 -92.845  1.00 103.35 ? 207  LYS   C O    1 
ATOM   19308 C  CB   . LYS   C  3  207 ? 7.210   -69.315 -93.781  1.00 103.76 ? 207  LYS   C CB   1 
ATOM   19309 C  CG   . LYS   C  3  207 ? 6.945   -67.841 -94.090  1.00 101.53 ? 207  LYS   C CG   1 
ATOM   19310 C  CD   . LYS   C  3  207 ? 7.223   -67.477 -95.548  1.00 101.36 ? 207  LYS   C CD   1 
ATOM   19311 C  CE   . LYS   C  3  207 ? 8.692   -67.143 -95.790  1.00 95.36  ? 207  LYS   C CE   1 
ATOM   19312 N  NZ   . LYS   C  3  207 ? 8.885   -66.289 -97.001  1.00 96.70  ? 207  LYS   C NZ   1 
ATOM   19313 H  H    . LYS   C  3  207 ? 4.637   -70.268 -93.231  1.00 134.12 ? 207  LYS   C H    1 
ATOM   19314 H  HA   . LYS   C  3  207 ? 6.302   -70.212 -95.377  1.00 131.02 ? 207  LYS   C HA   1 
ATOM   19315 H  HB2  . LYS   C  3  207 ? 7.179   -69.423 -92.818  1.00 124.49 ? 207  LYS   C HB2  1 
ATOM   19316 H  HB3  . LYS   C  3  207 ? 8.097   -69.529 -94.111  1.00 124.49 ? 207  LYS   C HB3  1 
ATOM   19317 H  HG2  . LYS   C  3  207 ? 6.014   -67.643 -93.905  1.00 121.81 ? 207  LYS   C HG2  1 
ATOM   19318 H  HG3  . LYS   C  3  207 ? 7.518   -67.294 -93.531  1.00 121.81 ? 207  LYS   C HG3  1 
ATOM   19319 H  HD2  . LYS   C  3  207 ? 6.987   -68.228 -96.115  1.00 121.62 ? 207  LYS   C HD2  1 
ATOM   19320 H  HD3  . LYS   C  3  207 ? 6.694   -66.700 -95.789  1.00 121.62 ? 207  LYS   C HD3  1 
ATOM   19321 H  HE2  . LYS   C  3  207 ? 9.040   -66.662 -95.023  1.00 114.41 ? 207  LYS   C HE2  1 
ATOM   19322 H  HE3  . LYS   C  3  207 ? 9.189   -67.966 -95.919  1.00 114.41 ? 207  LYS   C HE3  1 
ATOM   19323 H  HZ1  . LYS   C  3  207 ? 9.739   -66.045 -97.069  1.00 116.02 ? 207  LYS   C HZ1  1 
ATOM   19324 H  HZ2  . LYS   C  3  207 ? 8.656   -66.742 -97.732  1.00 116.02 ? 207  LYS   C HZ2  1 
ATOM   19325 H  HZ3  . LYS   C  3  207 ? 8.380   -65.559 -96.943  1.00 116.02 ? 207  LYS   C HZ3  1 
ATOM   19326 N  N    . SER   C  3  208 ? 7.029   -72.516 -94.915  1.00 108.98 ? 208  SER   C N    1 
ATOM   19327 C  CA   . SER   C  3  208 ? 7.201   -73.940 -94.670  1.00 107.75 ? 208  SER   C CA   1 
ATOM   19328 C  C    . SER   C  3  208 ? 8.402   -74.453 -95.450  1.00 107.26 ? 208  SER   C C    1 
ATOM   19329 O  O    . SER   C  3  208 ? 8.961   -73.761 -96.305  1.00 107.15 ? 208  SER   C O    1 
ATOM   19330 C  CB   . SER   C  3  208 ? 5.940   -74.724 -95.057  1.00 112.24 ? 208  SER   C CB   1 
ATOM   19331 O  OG   . SER   C  3  208 ? 5.615   -74.516 -96.420  1.00 117.80 ? 208  SER   C OG   1 
ATOM   19332 H  H    . SER   C  3  208 ? 7.296   -72.255 -95.690  1.00 130.76 ? 208  SER   C H    1 
ATOM   19333 H  HA   . SER   C  3  208 ? 7.379   -74.071 -93.726  1.00 129.29 ? 208  SER   C HA   1 
ATOM   19334 H  HB2  . SER   C  3  208 ? 6.100   -75.670 -94.910  1.00 134.67 ? 208  SER   C HB2  1 
ATOM   19335 H  HB3  . SER   C  3  208 ? 5.200   -74.423 -94.506  1.00 134.67 ? 208  SER   C HB3  1 
ATOM   19336 H  HG   . SER   C  3  208 ? 4.932   -74.961 -96.624  1.00 141.34 ? 208  SER   C HG   1 
ATOM   19337 N  N    . PHE   C  3  209 ? 8.791   -75.688 -95.139  1.00 108.81 ? 209  PHE   C N    1 
ATOM   19338 C  CA   . PHE   C  3  209 ? 9.871   -76.368 -95.836  1.00 113.99 ? 209  PHE   C CA   1 
ATOM   19339 C  C    . PHE   C  3  209 ? 9.601   -77.865 -95.788  1.00 118.89 ? 209  PHE   C C    1 
ATOM   19340 O  O    . PHE   C  3  209 ? 8.723   -78.335 -95.060  1.00 119.22 ? 209  PHE   C O    1 
ATOM   19341 C  CB   . PHE   C  3  209 ? 11.236  -76.039 -95.219  1.00 112.25 ? 209  PHE   C CB   1 
ATOM   19342 C  CG   . PHE   C  3  209 ? 11.405  -76.545 -93.813  1.00 111.72 ? 209  PHE   C CG   1 
ATOM   19343 C  CD1  . PHE   C  3  209 ? 11.038  -75.761 -92.732  1.00 108.50 ? 209  PHE   C CD1  1 
ATOM   19344 C  CD2  . PHE   C  3  209 ? 11.934  -77.804 -93.574  1.00 113.89 ? 209  PHE   C CD2  1 
ATOM   19345 C  CE1  . PHE   C  3  209 ? 11.194  -76.224 -91.437  1.00 106.50 ? 209  PHE   C CE1  1 
ATOM   19346 C  CE2  . PHE   C  3  209 ? 12.091  -78.272 -92.283  1.00 111.82 ? 209  PHE   C CE2  1 
ATOM   19347 C  CZ   . PHE   C  3  209 ? 11.722  -77.480 -91.213  1.00 108.60 ? 209  PHE   C CZ   1 
ATOM   19348 H  H    . PHE   C  3  209 ? 8.435   -76.160 -94.514  1.00 130.55 ? 209  PHE   C H    1 
ATOM   19349 H  HA   . PHE   C  3  209 ? 9.886   -76.084 -96.764  1.00 136.77 ? 209  PHE   C HA   1 
ATOM   19350 H  HB2  . PHE   C  3  209 ? 11.929  -76.443 -95.764  1.00 134.68 ? 209  PHE   C HB2  1 
ATOM   19351 H  HB3  . PHE   C  3  209 ? 11.346  -75.076 -95.202  1.00 134.68 ? 209  PHE   C HB3  1 
ATOM   19352 H  HD1  . PHE   C  3  209 ? 10.684  -74.914 -92.877  1.00 130.18 ? 209  PHE   C HD1  1 
ATOM   19353 H  HD2  . PHE   C  3  209 ? 12.186  -78.341 -94.291  1.00 136.64 ? 209  PHE   C HD2  1 
ATOM   19354 H  HE1  . PHE   C  3  209 ? 10.944  -75.689 -90.719  1.00 127.78 ? 209  PHE   C HE1  1 
ATOM   19355 H  HE2  . PHE   C  3  209 ? 12.445  -79.119 -92.134  1.00 134.17 ? 209  PHE   C HE2  1 
ATOM   19356 H  HZ   . PHE   C  3  209 ? 11.828  -77.792 -90.343  1.00 130.30 ? 209  PHE   C HZ   1 
ATOM   19357 N  N    . ASN   C  3  210 ? 10.369  -78.615 -96.575  1.00 122.95 ? 210  ASN   C N    1 
ATOM   19358 C  CA   . ASN   C  3  210 ? 10.284  -80.071 -96.609  1.00 127.49 ? 210  ASN   C CA   1 
ATOM   19359 C  C    . ASN   C  3  210 ? 11.629  -80.645 -96.188  1.00 128.18 ? 210  ASN   C C    1 
ATOM   19360 O  O    . ASN   C  3  210 ? 12.662  -80.315 -96.781  1.00 127.53 ? 210  ASN   C O    1 
ATOM   19361 C  CB   . ASN   C  3  210 ? 9.883   -80.567 -98.000  1.00 134.44 ? 210  ASN   C CB   1 
ATOM   19362 C  CG   . ASN   C  3  210 ? 8.439   -80.241 -98.337  1.00 134.29 ? 210  ASN   C CG   1 
ATOM   19363 O  OD1  . ASN   C  3  210 ? 7.581   -80.199 -97.455  1.00 130.16 ? 210  ASN   C OD1  1 
ATOM   19364 N  ND2  . ASN   C  3  210 ? 8.165   -80.006 -99.615  1.00 138.83 ? 210  ASN   C ND2  1 
ATOM   19365 H  H    . ASN   C  3  210 ? 10.960  -78.294 -97.111  1.00 147.52 ? 210  ASN   C H    1 
ATOM   19366 H  HA   . ASN   C  3  210 ? 9.614   -80.375 -95.978  1.00 152.97 ? 210  ASN   C HA   1 
ATOM   19367 H  HB2  . ASN   C  3  210 ? 10.450  -80.144 -98.664  1.00 161.31 ? 210  ASN   C HB2  1 
ATOM   19368 H  HB3  . ASN   C  3  210 ? 9.991   -81.530 -98.037  1.00 161.31 ? 210  ASN   C HB3  1 
ATOM   19369 H  HD21 . ASN   C  3  210 ? 7.361   -79.817 -99.855  1.00 166.57 ? 210  ASN   C HD21 1 
ATOM   19370 H  HD22 . ASN   C  3  210 ? 8.791   -80.043 -100.203 1.00 166.57 ? 210  ASN   C HD22 1 
ATOM   19371 N  N    . ARG   C  3  211 ? 11.609  -81.501 -95.165  1.00 129.43 ? 211  ARG   C N    1 
ATOM   19372 C  CA   . ARG   C  3  211 ? 12.845  -82.032 -94.598  1.00 127.23 ? 211  ARG   C CA   1 
ATOM   19373 C  C    . ARG   C  3  211 ? 13.690  -82.721 -95.663  1.00 130.89 ? 211  ARG   C C    1 
ATOM   19374 O  O    . ARG   C  3  211 ? 14.867  -82.392 -95.853  1.00 130.12 ? 211  ARG   C O    1 
ATOM   19375 C  CB   . ARG   C  3  211 ? 12.508  -82.997 -93.460  1.00 125.63 ? 211  ARG   C CB   1 
ATOM   19376 C  CG   . ARG   C  3  211 ? 13.710  -83.645 -92.795  1.00 123.65 ? 211  ARG   C CG   1 
ATOM   19377 C  CD   . ARG   C  3  211 ? 13.277  -84.489 -91.604  1.00 120.59 ? 211  ARG   C CD   1 
ATOM   19378 N  NE   . ARG   C  3  211 ? 12.295  -85.505 -91.977  1.00 123.59 ? 211  ARG   C NE   1 
ATOM   19379 C  CZ   . ARG   C  3  211 ? 12.596  -86.732 -92.395  1.00 129.50 ? 211  ARG   C CZ   1 
ATOM   19380 N  NH1  . ARG   C  3  211 ? 13.861  -87.119 -92.502  1.00 131.54 ? 211  ARG   C NH1  1 
ATOM   19381 N  NH2  . ARG   C  3  211 ? 11.624  -87.577 -92.709  1.00 134.14 ? 211  ARG   C NH2  1 
ATOM   19382 H  H    . ARG   C  3  211 ? 10.895  -81.789 -94.783  1.00 155.29 ? 211  ARG   C H    1 
ATOM   19383 H  HA   . ARG   C  3  211 ? 13.368  -81.300 -94.236  1.00 152.66 ? 211  ARG   C HA   1 
ATOM   19384 H  HB2  . ARG   C  3  211 ? 12.024  -82.509 -92.776  1.00 150.74 ? 211  ARG   C HB2  1 
ATOM   19385 H  HB3  . ARG   C  3  211 ? 11.953  -83.709 -93.816  1.00 150.74 ? 211  ARG   C HB3  1 
ATOM   19386 H  HG2  . ARG   C  3  211 ? 14.162  -84.220 -93.431  1.00 148.36 ? 211  ARG   C HG2  1 
ATOM   19387 H  HG3  . ARG   C  3  211 ? 14.316  -82.957 -92.480  1.00 148.36 ? 211  ARG   C HG3  1 
ATOM   19388 H  HD2  . ARG   C  3  211 ? 14.052  -84.939 -91.234  1.00 144.68 ? 211  ARG   C HD2  1 
ATOM   19389 H  HD3  . ARG   C  3  211 ? 12.877  -83.913 -90.934  1.00 144.68 ? 211  ARG   C HD3  1 
ATOM   19390 H  HE   . ARG   C  3  211 ? 11.463  -85.295 -91.922  1.00 148.29 ? 211  ARG   C HE   1 
ATOM   19391 H  HH11 . ARG   C  3  211 ? 14.496  -86.575 -92.300  1.00 157.82 ? 211  ARG   C HH11 1 
ATOM   19392 H  HH12 . ARG   C  3  211 ? 14.047  -87.914 -92.773  1.00 157.82 ? 211  ARG   C HH12 1 
ATOM   19393 H  HH21 . ARG   C  3  211 ? 10.802  -87.332 -92.642  1.00 160.95 ? 211  ARG   C HH21 1 
ATOM   19394 H  HH22 . ARG   C  3  211 ? 11.815  -88.371 -92.979  1.00 160.95 ? 211  ARG   C HH22 1 
ATOM   19395 N  N    . ASN   C  3  212 ? 13.105  -83.694 -96.363  1.00 135.01 ? 212  ASN   C N    1 
ATOM   19396 C  CA   . ASN   C  3  212 ? 13.829  -84.380 -97.428  1.00 140.72 ? 212  ASN   C CA   1 
ATOM   19397 C  C    . ASN   C  3  212 ? 14.359  -83.391 -98.458  1.00 142.20 ? 212  ASN   C C    1 
ATOM   19398 O  O    . ASN   C  3  212 ? 15.540  -83.426 -98.823  1.00 143.82 ? 212  ASN   C O    1 
ATOM   19399 C  CB   . ASN   C  3  212 ? 12.917  -85.409 -98.098  1.00 144.67 ? 212  ASN   C CB   1 
ATOM   19400 C  CG   . ASN   C  3  212 ? 13.435  -85.857 -99.452  1.00 151.08 ? 212  ASN   C CG   1 
ATOM   19401 O  OD1  . ASN   C  3  212 ? 13.241  -85.176 -100.460 1.00 150.03 ? 212  ASN   C OD1  1 
ATOM   19402 N  ND2  . ASN   C  3  212 ? 14.092  -87.011 -99.483  1.00 157.91 ? 212  ASN   C ND2  1 
ATOM   19403 H  H    . ASN   C  3  212 ? 12.300  -83.972 -96.243  1.00 161.99 ? 212  ASN   C H    1 
ATOM   19404 H  HA   . ASN   C  3  212 ? 14.586  -84.848 -97.041  1.00 168.84 ? 212  ASN   C HA   1 
ATOM   19405 H  HB2  . ASN   C  3  212 ? 12.850  -86.191 -97.528  1.00 173.59 ? 212  ASN   C HB2  1 
ATOM   19406 H  HB3  . ASN   C  3  212 ? 12.039  -85.017 -98.227  1.00 173.59 ? 212  ASN   C HB3  1 
ATOM   19407 H  HD21 . ASN   C  3  212 ? 14.405  -87.308 -100.227 1.00 189.47 ? 212  ASN   C HD21 1 
ATOM   19408 H  HD22 . ASN   C  3  212 ? 14.204  -87.462 -98.759  1.00 189.47 ? 212  ASN   C HD22 1 
ATOM   19409 N  N    . GLU   C  3  213 ? 13.500  -82.493 -98.931  1.00 142.73 ? 213  GLU   C N    1 
ATOM   19410 C  CA   . GLU   C  3  213 ? 13.854  -81.624 -100.039 1.00 146.34 ? 213  GLU   C CA   1 
ATOM   19411 C  C    . GLU   C  3  213 ? 14.911  -80.604 -99.619  1.00 143.99 ? 213  GLU   C C    1 
ATOM   19412 O  O    . GLU   C  3  213 ? 15.178  -80.383 -98.434  1.00 136.54 ? 213  GLU   C O    1 
ATOM   19413 C  CB   . GLU   C  3  213 ? 12.616  -80.905 -100.571 1.00 144.00 ? 213  GLU   C CB   1 
ATOM   19414 C  CG   . GLU   C  3  213 ? 11.510  -81.843 -101.013 1.00 147.42 ? 213  GLU   C CG   1 
ATOM   19415 C  CD   . GLU   C  3  213 ? 10.385  -81.120 -101.723 1.00 145.90 ? 213  GLU   C CD   1 
ATOM   19416 O  OE1  . GLU   C  3  213 ? 10.355  -79.872 -101.674 1.00 140.22 ? 213  GLU   C OE1  1 
ATOM   19417 O  OE2  . GLU   C  3  213 ? 9.529   -81.798 -102.329 1.00 151.44 ? 213  GLU   C OE2  1 
ATOM   19418 H  H    . GLU   C  3  213 ? 12.705  -82.369 -98.625  1.00 171.26 ? 213  GLU   C H    1 
ATOM   19419 H  HA   . GLU   C  3  213 ? 14.227  -82.165 -100.753 1.00 175.59 ? 213  GLU   C HA   1 
ATOM   19420 H  HB2  . GLU   C  3  213 ? 12.260  -80.337 -99.870  1.00 172.78 ? 213  GLU   C HB2  1 
ATOM   19421 H  HB3  . GLU   C  3  213 ? 12.872  -80.367 -101.336 1.00 172.78 ? 213  GLU   C HB3  1 
ATOM   19422 H  HG2  . GLU   C  3  213 ? 11.877  -82.501 -101.625 1.00 176.88 ? 213  GLU   C HG2  1 
ATOM   19423 H  HG3  . GLU   C  3  213 ? 11.139  -82.286 -100.234 1.00 176.88 ? 213  GLU   C HG3  1 
ATOM   19424 N  N    . CYS   C  3  214 ? 15.508  -79.974 -100.625 1.00 150.38 ? 214  CYS   C N    1 
ATOM   19425 C  CA   . CYS   C  3  214 ? 16.550  -78.977 -100.417 1.00 148.86 ? 214  CYS   C CA   1 
ATOM   19426 C  C    . CYS   C  3  214 ? 16.805  -78.220 -101.714 1.00 148.20 ? 214  CYS   C C    1 
ATOM   19427 O  O    . CYS   C  3  214 ? 15.882  -77.667 -102.312 1.00 145.57 ? 214  CYS   C O    1 
ATOM   19428 C  CB   . CYS   C  3  214 ? 17.836  -79.637 -99.922  1.00 155.21 ? 214  CYS   C CB   1 
ATOM   19429 S  SG   . CYS   C  3  214 ? 19.306  -78.569 -99.936  1.00 155.43 ? 214  CYS   C SG   1 
ATOM   19430 H  H    . CYS   C  3  214 ? 15.324  -80.110 -101.454 1.00 180.44 ? 214  CYS   C H    1 
ATOM   19431 H  HA   . CYS   C  3  214 ? 16.269  -78.345 -99.737  1.00 178.62 ? 214  CYS   C HA   1 
ATOM   19432 H  HB2  . CYS   C  3  214 ? 17.698  -79.929 -99.007  1.00 186.23 ? 214  CYS   C HB2  1 
ATOM   19433 H  HB3  . CYS   C  3  214 ? 18.026  -80.401 -100.488 1.00 186.23 ? 214  CYS   C HB3  1 
ATOM   19434 N  N    . GLN   D  4  1   ? 18.713  -36.087 -55.223  1.00 94.46  ? 1    GLN   D N    1 
ATOM   19435 C  CA   . GLN   D  4  1   ? 19.865  -37.023 -55.375  1.00 88.42  ? 1    GLN   D CA   1 
ATOM   19436 C  C    . GLN   D  4  1   ? 19.716  -38.216 -54.436  1.00 79.86  ? 1    GLN   D C    1 
ATOM   19437 O  O    . GLN   D  4  1   ? 20.692  -38.684 -53.847  1.00 80.21  ? 1    GLN   D O    1 
ATOM   19438 C  CB   . GLN   D  4  1   ? 21.183  -36.293 -55.112  1.00 95.37  ? 1    GLN   D CB   1 
ATOM   19439 C  CG   . GLN   D  4  1   ? 21.483  -35.203 -56.130  1.00 111.30 ? 1    GLN   D CG   1 
ATOM   19440 C  CD   . GLN   D  4  1   ? 22.716  -34.395 -55.785  1.00 126.55 ? 1    GLN   D CD   1 
ATOM   19441 O  OE1  . GLN   D  4  1   ? 23.189  -34.415 -54.649  1.00 129.50 ? 1    GLN   D OE1  1 
ATOM   19442 N  NE2  . GLN   D  4  1   ? 23.243  -33.675 -56.768  1.00 135.50 ? 1    GLN   D NE2  1 
ATOM   19443 H  H1   . GLN   D  4  1   ? 18.216  -36.107 -55.961  1.00 113.34 ? 1    GLN   D H1   1 
ATOM   19444 H  H2   . GLN   D  4  1   ? 18.220  -36.335 -54.525  1.00 113.34 ? 1    GLN   D H2   1 
ATOM   19445 H  H3   . GLN   D  4  1   ? 19.018  -35.261 -55.093  1.00 113.34 ? 1    GLN   D H3   1 
ATOM   19446 H  HA   . GLN   D  4  1   ? 19.890  -37.359 -56.285  1.00 106.08 ? 1    GLN   D HA   1 
ATOM   19447 H  HB2  . GLN   D  4  1   ? 21.143  -35.880 -54.236  1.00 114.42 ? 1    GLN   D HB2  1 
ATOM   19448 H  HB3  . GLN   D  4  1   ? 21.908  -36.936 -55.143  1.00 114.42 ? 1    GLN   D HB3  1 
ATOM   19449 H  HG2  . GLN   D  4  1   ? 21.627  -35.612 -56.998  1.00 133.54 ? 1    GLN   D HG2  1 
ATOM   19450 H  HG3  . GLN   D  4  1   ? 20.728  -34.594 -56.171  1.00 133.54 ? 1    GLN   D HG3  1 
ATOM   19451 H  HE21 . GLN   D  4  1   ? 22.884  -33.686 -57.549  1.00 162.58 ? 1    GLN   D HE21 1 
ATOM   19452 H  HE22 . GLN   D  4  1   ? 23.944  -33.199 -56.623  1.00 162.58 ? 1    GLN   D HE22 1 
ATOM   19453 N  N    . VAL   D  4  2   ? 18.485  -38.699 -54.301  1.00 72.29  ? 2    VAL   D N    1 
ATOM   19454 C  CA   . VAL   D  4  2   ? 18.193  -39.890 -53.514  1.00 67.17  ? 2    VAL   D CA   1 
ATOM   19455 C  C    . VAL   D  4  2   ? 18.408  -41.113 -54.393  1.00 68.18  ? 2    VAL   D C    1 
ATOM   19456 O  O    . VAL   D  4  2   ? 17.945  -41.155 -55.540  1.00 71.17  ? 2    VAL   D O    1 
ATOM   19457 C  CB   . VAL   D  4  2   ? 16.757  -39.851 -52.965  1.00 64.10  ? 2    VAL   D CB   1 
ATOM   19458 C  CG1  . VAL   D  4  2   ? 16.432  -41.144 -52.229  1.00 60.19  ? 2    VAL   D CG1  1 
ATOM   19459 C  CG2  . VAL   D  4  2   ? 16.573  -38.651 -52.048  1.00 65.02  ? 2    VAL   D CG2  1 
ATOM   19460 H  H    . VAL   D  4  2   ? 17.789  -38.347 -54.663  1.00 86.73  ? 2    VAL   D H    1 
ATOM   19461 H  HA   . VAL   D  4  2   ? 18.804  -39.938 -52.761  1.00 80.59  ? 2    VAL   D HA   1 
ATOM   19462 H  HB   . VAL   D  4  2   ? 16.139  -39.763 -53.707  1.00 76.90  ? 2    VAL   D HB   1 
ATOM   19463 H  HG11 . VAL   D  4  2   ? 15.585  -41.041 -51.768  1.00 72.21  ? 2    VAL   D HG11 1 
ATOM   19464 H  HG12 . VAL   D  4  2   ? 16.373  -41.867 -52.872  1.00 72.21  ? 2    VAL   D HG12 1 
ATOM   19465 H  HG13 . VAL   D  4  2   ? 17.136  -41.328 -51.587  1.00 72.21  ? 2    VAL   D HG13 1 
ATOM   19466 H  HG21 . VAL   D  4  2   ? 15.666  -38.652 -51.705  1.00 78.01  ? 2    VAL   D HG21 1 
ATOM   19467 H  HG22 . VAL   D  4  2   ? 17.204  -38.715 -51.314  1.00 78.01  ? 2    VAL   D HG22 1 
ATOM   19468 H  HG23 . VAL   D  4  2   ? 16.735  -37.839 -52.553  1.00 78.01  ? 2    VAL   D HG23 1 
ATOM   19469 N  N    . GLN   D  4  3   ? 19.111  -42.109 -53.860  1.00 67.49  ? 3    GLN   D N    1 
ATOM   19470 C  CA   . GLN   D  4  3   ? 19.402  -43.330 -54.595  1.00 69.50  ? 3    GLN   D CA   1 
ATOM   19471 C  C    . GLN   D  4  3   ? 19.263  -44.526 -53.668  1.00 65.68  ? 3    GLN   D C    1 
ATOM   19472 O  O    . GLN   D  4  3   ? 19.739  -44.499 -52.530  1.00 65.12  ? 3    GLN   D O    1 
ATOM   19473 C  CB   . GLN   D  4  3   ? 20.813  -43.303 -55.194  1.00 76.52  ? 3    GLN   D CB   1 
ATOM   19474 C  CG   . GLN   D  4  3   ? 21.056  -42.167 -56.174  1.00 85.10  ? 3    GLN   D CG   1 
ATOM   19475 C  CD   . GLN   D  4  3   ? 22.448  -42.211 -56.772  1.00 95.58  ? 3    GLN   D CD   1 
ATOM   19476 O  OE1  . GLN   D  4  3   ? 23.138  -43.227 -56.691  1.00 100.97 ? 3    GLN   D OE1  1 
ATOM   19477 N  NE2  . GLN   D  4  3   ? 22.870  -41.105 -57.373  1.00 99.39  ? 3    GLN   D NE2  1 
ATOM   19478 H  H    . GLN   D  4  3   ? 19.433  -42.098 -53.063  1.00 80.97  ? 3    GLN   D H    1 
ATOM   19479 H  HA   . GLN   D  4  3   ? 18.762  -43.428 -55.318  1.00 83.38  ? 3    GLN   D HA   1 
ATOM   19480 H  HB2  . GLN   D  4  3   ? 21.454  -43.209 -54.472  1.00 91.81  ? 3    GLN   D HB2  1 
ATOM   19481 H  HB3  . GLN   D  4  3   ? 20.965  -44.136 -55.667  1.00 91.81  ? 3    GLN   D HB3  1 
ATOM   19482 H  HG2  . GLN   D  4  3   ? 20.414  -42.230 -56.898  1.00 102.10 ? 3    GLN   D HG2  1 
ATOM   19483 H  HG3  . GLN   D  4  3   ? 20.952  -41.321 -55.711  1.00 102.10 ? 3    GLN   D HG3  1 
ATOM   19484 H  HE21 . GLN   D  4  3   ? 22.360  -40.413 -57.408  1.00 119.25 ? 3    GLN   D HE21 1 
ATOM   19485 H  HE22 . GLN   D  4  3   ? 23.653  -41.080 -57.728  1.00 119.25 ? 3    GLN   D HE22 1 
ATOM   19486 N  N    . LEU   D  4  4   ? 18.605  -45.572 -54.164  1.00 64.13  ? 4    LEU   D N    1 
ATOM   19487 C  CA   . LEU   D  4  4   ? 18.480  -46.844 -53.461  1.00 62.93  ? 4    LEU   D CA   1 
ATOM   19488 C  C    . LEU   D  4  4   ? 19.128  -47.916 -54.328  1.00 61.66  ? 4    LEU   D C    1 
ATOM   19489 O  O    . LEU   D  4  4   ? 18.617  -48.243 -55.405  1.00 60.48  ? 4    LEU   D O    1 
ATOM   19490 C  CB   . LEU   D  4  4   ? 17.018  -47.180 -53.174  1.00 61.61  ? 4    LEU   D CB   1 
ATOM   19491 C  CG   . LEU   D  4  4   ? 16.195  -46.127 -52.426  1.00 59.82  ? 4    LEU   D CG   1 
ATOM   19492 C  CD1  . LEU   D  4  4   ? 14.811  -46.677 -52.107  1.00 59.11  ? 4    LEU   D CD1  1 
ATOM   19493 C  CD2  . LEU   D  4  4   ? 16.892  -45.666 -51.155  1.00 58.80  ? 4    LEU   D CD2  1 
ATOM   19494 H  H    . LEU   D  4  4   ? 18.212  -45.567 -54.929  1.00 76.94  ? 4    LEU   D H    1 
ATOM   19495 H  HA   . LEU   D  4  4   ? 18.948  -46.796 -52.613  1.00 75.50  ? 4    LEU   D HA   1 
ATOM   19496 H  HB2  . LEU   D  4  4   ? 16.574  -47.335 -54.022  1.00 73.91  ? 4    LEU   D HB2  1 
ATOM   19497 H  HB3  . LEU   D  4  4   ? 16.997  -47.988 -52.637  1.00 73.91  ? 4    LEU   D HB3  1 
ATOM   19498 H  HG   . LEU   D  4  4   ? 16.100  -45.349 -52.997  1.00 71.77  ? 4    LEU   D HG   1 
ATOM   19499 H  HD11 . LEU   D  4  4   ? 14.299  -45.994 -51.645  1.00 70.92  ? 4    LEU   D HD11 1 
ATOM   19500 H  HD12 . LEU   D  4  4   ? 14.368  -46.918 -52.935  1.00 70.92  ? 4    LEU   D HD12 1 
ATOM   19501 H  HD13 . LEU   D  4  4   ? 14.904  -47.459 -51.541  1.00 70.92  ? 4    LEU   D HD13 1 
ATOM   19502 H  HD21 . LEU   D  4  4   ? 16.324  -45.027 -50.697  1.00 70.55  ? 4    LEU   D HD21 1 
ATOM   19503 H  HD22 . LEU   D  4  4   ? 17.050  -46.435 -50.585  1.00 70.55  ? 4    LEU   D HD22 1 
ATOM   19504 H  HD23 . LEU   D  4  4   ? 17.736  -45.250 -51.390  1.00 70.55  ? 4    LEU   D HD23 1 
ATOM   19505 N  N    . GLN   D  4  5   ? 20.251  -48.455 -53.864  1.00 63.38  ? 5    GLN   D N    1 
ATOM   19506 C  CA   . GLN   D  4  5   ? 21.002  -49.469 -54.594  1.00 66.05  ? 5    GLN   D CA   1 
ATOM   19507 C  C    . GLN   D  4  5   ? 20.728  -50.832 -53.969  1.00 60.83  ? 5    GLN   D C    1 
ATOM   19508 O  O    . GLN   D  4  5   ? 21.050  -51.057 -52.798  1.00 58.61  ? 5    GLN   D O    1 
ATOM   19509 C  CB   . GLN   D  4  5   ? 22.498  -49.155 -54.569  1.00 75.69  ? 5    GLN   D CB   1 
ATOM   19510 C  CG   . GLN   D  4  5   ? 23.349  -50.097 -55.407  1.00 90.07  ? 5    GLN   D CG   1 
ATOM   19511 C  CD   . GLN   D  4  5   ? 23.042  -49.998 -56.889  1.00 103.01 ? 5    GLN   D CD   1 
ATOM   19512 O  OE1  . GLN   D  4  5   ? 22.320  -50.828 -57.443  1.00 108.67 ? 5    GLN   D OE1  1 
ATOM   19513 N  NE2  . GLN   D  4  5   ? 23.593  -48.980 -57.540  1.00 107.86 ? 5    GLN   D NE2  1 
ATOM   19514 H  H    . GLN   D  4  5   ? 20.606  -48.244 -53.110  1.00 76.04  ? 5    GLN   D H    1 
ATOM   19515 H  HA   . GLN   D  4  5   ? 20.710  -49.490 -55.518  1.00 79.24  ? 5    GLN   D HA   1 
ATOM   19516 H  HB2  . GLN   D  4  5   ? 22.632  -48.257 -54.909  1.00 90.81  ? 5    GLN   D HB2  1 
ATOM   19517 H  HB3  . GLN   D  4  5   ? 22.811  -49.213 -53.652  1.00 90.81  ? 5    GLN   D HB3  1 
ATOM   19518 H  HG2  . GLN   D  4  5   ? 24.285  -49.877 -55.278  1.00 108.07 ? 5    GLN   D HG2  1 
ATOM   19519 H  HG3  . GLN   D  4  5   ? 23.181  -51.010 -55.125  1.00 108.07 ? 5    GLN   D HG3  1 
ATOM   19520 H  HE21 . GLN   D  4  5   ? 24.093  -48.421 -57.119  1.00 129.42 ? 5    GLN   D HE21 1 
ATOM   19521 H  HE22 . GLN   D  4  5   ? 23.449  -48.880 -58.382  1.00 129.42 ? 5    GLN   D HE22 1 
ATOM   19522 N  N    . GLN   D  4  6   ? 20.134  -51.731 -54.747  1.00 62.59  ? 6    GLN   D N    1 
ATOM   19523 C  CA   . GLN   D  4  6   ? 19.809  -53.074 -54.291  1.00 63.21  ? 6    GLN   D CA   1 
ATOM   19524 C  C    . GLN   D  4  6   ? 20.872  -54.066 -54.749  1.00 65.61  ? 6    GLN   D C    1 
ATOM   19525 O  O    . GLN   D  4  6   ? 21.595  -53.838 -55.722  1.00 64.28  ? 6    GLN   D O    1 
ATOM   19526 C  CB   . GLN   D  4  6   ? 18.434  -53.507 -54.807  1.00 66.89  ? 6    GLN   D CB   1 
ATOM   19527 C  CG   . GLN   D  4  6   ? 17.277  -52.709 -54.228  1.00 68.21  ? 6    GLN   D CG   1 
ATOM   19528 C  CD   . GLN   D  4  6   ? 15.925  -53.276 -54.616  1.00 70.64  ? 6    GLN   D CD   1 
ATOM   19529 O  OE1  . GLN   D  4  6   ? 15.097  -52.585 -55.209  1.00 72.88  ? 6    GLN   D OE1  1 
ATOM   19530 N  NE2  . GLN   D  4  6   ? 15.693  -54.539 -54.277  1.00 70.94  ? 6    GLN   D NE2  1 
ATOM   19531 H  H    . GLN   D  4  6   ? 19.904  -51.581 -55.563  1.00 75.09  ? 6    GLN   D H    1 
ATOM   19532 H  HA   . GLN   D  4  6   ? 19.784  -53.081 -53.321  1.00 75.84  ? 6    GLN   D HA   1 
ATOM   19533 H  HB2  . GLN   D  4  6   ? 18.415  -53.397 -55.770  1.00 80.25  ? 6    GLN   D HB2  1 
ATOM   19534 H  HB3  . GLN   D  4  6   ? 18.295  -54.439 -54.576  1.00 80.25  ? 6    GLN   D HB3  1 
ATOM   19535 H  HG2  . GLN   D  4  6   ? 17.340  -52.718 -53.260  1.00 81.83  ? 6    GLN   D HG2  1 
ATOM   19536 H  HG3  . GLN   D  4  6   ? 17.326  -51.797 -54.555  1.00 81.83  ? 6    GLN   D HG3  1 
ATOM   19537 H  HE21 . GLN   D  4  6   ? 16.294  -54.989 -53.859  1.00 85.11  ? 6    GLN   D HE21 1 
ATOM   19538 H  HE22 . GLN   D  4  6   ? 14.941  -54.906 -54.475  1.00 85.11  ? 6    GLN   D HE22 1 
ATOM   19539 N  N    . SER   D  4  7   ? 20.955  -55.182 -54.028  1.00 71.61  ? 7    SER   D N    1 
ATOM   19540 C  CA   . SER   D  4  7   ? 21.954  -56.197 -54.321  1.00 72.24  ? 7    SER   D CA   1 
ATOM   19541 C  C    . SER   D  4  7   ? 21.638  -56.883 -55.651  1.00 67.84  ? 7    SER   D C    1 
ATOM   19542 O  O    . SER   D  4  7   ? 20.618  -56.622 -56.296  1.00 61.65  ? 7    SER   D O    1 
ATOM   19543 C  CB   . SER   D  4  7   ? 22.024  -57.217 -53.187  1.00 77.27  ? 7    SER   D CB   1 
ATOM   19544 O  OG   . SER   D  4  7   ? 20.845  -58.000 -53.128  1.00 80.31  ? 7    SER   D OG   1 
ATOM   19545 H  H    . SER   D  4  7   ? 20.443  -55.373 -53.364  1.00 85.92  ? 7    SER   D H    1 
ATOM   19546 H  HA   . SER   D  4  7   ? 22.821  -55.768 -54.398  1.00 86.67  ? 7    SER   D HA   1 
ATOM   19547 H  HB2  . SER   D  4  7   ? 22.782  -57.803 -53.337  1.00 92.70  ? 7    SER   D HB2  1 
ATOM   19548 H  HB3  . SER   D  4  7   ? 22.130  -56.745 -52.346  1.00 92.70  ? 7    SER   D HB3  1 
ATOM   19549 H  HG   . SER   D  4  7   ? 20.924  -58.594 -52.540  1.00 96.35  ? 7    SER   D HG   1 
ATOM   19550 N  N    . GLY   D  4  8   ? 22.531  -57.783 -56.058  1.00 71.47  ? 8    GLY   D N    1 
ATOM   19551 C  CA   . GLY   D  4  8   ? 22.406  -58.459 -57.330  1.00 72.86  ? 8    GLY   D CA   1 
ATOM   19552 C  C    . GLY   D  4  8   ? 21.430  -59.619 -57.292  1.00 70.42  ? 8    GLY   D C    1 
ATOM   19553 O  O    . GLY   D  4  8   ? 20.879  -59.989 -56.254  1.00 70.42  ? 8    GLY   D O    1 
ATOM   19554 H  H    . GLY   D  4  8   ? 23.223  -58.018 -55.605  1.00 85.75  ? 8    GLY   D H    1 
ATOM   19555 H  HA2  . GLY   D  4  8   ? 22.098  -57.826 -57.998  1.00 87.42  ? 8    GLY   D HA2  1 
ATOM   19556 H  HA3  . GLY   D  4  8   ? 23.273  -58.801 -57.596  1.00 87.42  ? 8    GLY   D HA3  1 
ATOM   19557 N  N    . ALA   D  4  9   ? 21.224  -60.207 -58.469  1.00 68.55  ? 9    ALA   D N    1 
ATOM   19558 C  CA   . ALA   D  4  9   ? 20.275  -61.303 -58.609  1.00 68.56  ? 9    ALA   D CA   1 
ATOM   19559 C  C    . ALA   D  4  9   ? 20.603  -62.435 -57.644  1.00 74.32  ? 9    ALA   D C    1 
ATOM   19560 O  O    . ALA   D  4  9   ? 21.772  -62.738 -57.386  1.00 77.71  ? 9    ALA   D O    1 
ATOM   19561 C  CB   . ALA   D  4  9   ? 20.281  -61.822 -60.046  1.00 65.90  ? 9    ALA   D CB   1 
ATOM   19562 H  H    . ALA   D  4  9   ? 21.621  -59.989 -59.199  1.00 82.24  ? 9    ALA   D H    1 
ATOM   19563 H  HA   . ALA   D  4  9   ? 19.384  -60.979 -58.401  1.00 82.26  ? 9    ALA   D HA   1 
ATOM   19564 H  HB1  . ALA   D  4  9   ? 19.649  -62.554 -60.120  1.00 79.06  ? 9    ALA   D HB1  1 
ATOM   19565 H  HB2  . ALA   D  4  9   ? 20.025  -61.102 -60.644  1.00 79.06  ? 9    ALA   D HB2  1 
ATOM   19566 H  HB3  . ALA   D  4  9   ? 21.173  -62.133 -60.266  1.00 79.06  ? 9    ALA   D HB3  1 
ATOM   19567 N  N    . GLU   D  4  10  ? 19.558  -63.063 -57.113  1.00 73.99  ? 10   GLU   D N    1 
ATOM   19568 C  CA   . GLU   D  4  10  ? 19.682  -64.178 -56.187  1.00 74.64  ? 10   GLU   D CA   1 
ATOM   19569 C  C    . GLU   D  4  10  ? 19.154  -65.450 -56.836  1.00 75.34  ? 10   GLU   D C    1 
ATOM   19570 O  O    . GLU   D  4  10  ? 18.132  -65.427 -57.530  1.00 76.09  ? 10   GLU   D O    1 
ATOM   19571 C  CB   . GLU   D  4  10  ? 18.912  -63.904 -54.891  1.00 76.89  ? 10   GLU   D CB   1 
ATOM   19572 C  CG   . GLU   D  4  10  ? 19.458  -62.753 -54.059  1.00 77.40  ? 10   GLU   D CG   1 
ATOM   19573 C  CD   . GLU   D  4  10  ? 20.672  -63.144 -53.238  1.00 81.98  ? 10   GLU   D CD   1 
ATOM   19574 O  OE1  . GLU   D  4  10  ? 21.194  -64.262 -53.436  1.00 84.34  ? 10   GLU   D OE1  1 
ATOM   19575 O  OE2  . GLU   D  4  10  ? 21.102  -62.334 -52.389  1.00 83.24  ? 10   GLU   D OE2  1 
ATOM   19576 H  H    . GLU   D  4  10  ? 18.741  -62.852 -57.282  1.00 88.77  ? 10   GLU   D H    1 
ATOM   19577 H  HA   . GLU   D  4  10  ? 20.617  -64.310 -55.966  1.00 89.55  ? 10   GLU   D HA   1 
ATOM   19578 H  HB2  . GLU   D  4  10  ? 17.993  -63.691 -55.117  1.00 92.25  ? 10   GLU   D HB2  1 
ATOM   19579 H  HB3  . GLU   D  4  10  ? 18.942  -64.702 -54.340  1.00 92.25  ? 10   GLU   D HB3  1 
ATOM   19580 H  HG2  . GLU   D  4  10  ? 19.717  -62.030 -54.651  1.00 92.86  ? 10   GLU   D HG2  1 
ATOM   19581 H  HG3  . GLU   D  4  10  ? 18.768  -62.450 -53.448  1.00 92.86  ? 10   GLU   D HG3  1 
ATOM   19582 N  N    . LEU   D  4  11  ? 19.860  -66.555 -56.612  1.00 74.57  ? 11   LEU   D N    1 
ATOM   19583 C  CA   . LEU   D  4  11  ? 19.421  -67.882 -57.019  1.00 72.52  ? 11   LEU   D CA   1 
ATOM   19584 C  C    . LEU   D  4  11  ? 19.357  -68.771 -55.785  1.00 73.88  ? 11   LEU   D C    1 
ATOM   19585 O  O    . LEU   D  4  11  ? 20.221  -68.683 -54.906  1.00 76.11  ? 11   LEU   D O    1 
ATOM   19586 C  CB   . LEU   D  4  11  ? 20.370  -68.498 -58.053  1.00 74.23  ? 11   LEU   D CB   1 
ATOM   19587 C  CG   . LEU   D  4  11  ? 20.896  -67.584 -59.162  1.00 75.02  ? 11   LEU   D CG   1 
ATOM   19588 C  CD1  . LEU   D  4  11  ? 22.021  -68.279 -59.915  1.00 77.17  ? 11   LEU   D CD1  1 
ATOM   19589 C  CD2  . LEU   D  4  11  ? 19.789  -67.175 -60.122  1.00 75.11  ? 11   LEU   D CD2  1 
ATOM   19590 H  H    . LEU   D  4  11  ? 20.622  -66.559 -56.212  1.00 89.46  ? 11   LEU   D H    1 
ATOM   19591 H  HA   . LEU   D  4  11  ? 18.540  -67.829 -57.423  1.00 87.01  ? 11   LEU   D HA   1 
ATOM   19592 H  HB2  . LEU   D  4  11  ? 21.144  -68.838 -57.579  1.00 89.06  ? 11   LEU   D HB2  1 
ATOM   19593 H  HB3  . LEU   D  4  11  ? 19.901  -69.227 -58.489  1.00 89.06  ? 11   LEU   D HB3  1 
ATOM   19594 H  HG   . LEU   D  4  11  ? 21.241  -66.772 -58.758  1.00 90.01  ? 11   LEU   D HG   1 
ATOM   19595 H  HD11 . LEU   D  4  11  ? 22.389  -67.665 -60.570  1.00 92.59  ? 11   LEU   D HD11 1 
ATOM   19596 H  HD12 . LEU   D  4  11  ? 22.709  -68.541 -59.283  1.00 92.59  ? 11   LEU   D HD12 1 
ATOM   19597 H  HD13 . LEU   D  4  11  ? 21.665  -69.063 -60.360  1.00 92.59  ? 11   LEU   D HD13 1 
ATOM   19598 H  HD21 . LEU   D  4  11  ? 20.157  -66.578 -60.792  1.00 90.11  ? 11   LEU   D HD21 1 
ATOM   19599 H  HD22 . LEU   D  4  11  ? 19.431  -67.969 -60.547  1.00 90.11  ? 11   LEU   D HD22 1 
ATOM   19600 H  HD23 . LEU   D  4  11  ? 19.091  -66.723 -59.623  1.00 90.11  ? 11   LEU   D HD23 1 
ATOM   19601 N  N    . ALA   D  4  12  ? 18.337  -69.622 -55.714  1.00 74.51  ? 12   ALA   D N    1 
ATOM   19602 C  CA   . ALA   D  4  12  ? 18.189  -70.497 -54.559  1.00 77.18  ? 12   ALA   D CA   1 
ATOM   19603 C  C    . ALA   D  4  12  ? 17.339  -71.701 -54.932  1.00 81.58  ? 12   ALA   D C    1 
ATOM   19604 O  O    . ALA   D  4  12  ? 16.450  -71.612 -55.780  1.00 81.22  ? 12   ALA   D O    1 
ATOM   19605 C  CB   . ALA   D  4  12  ? 17.564  -69.752 -53.374  1.00 74.83  ? 12   ALA   D CB   1 
ATOM   19606 H  H    . ALA   D  4  12  ? 17.728  -69.710 -56.314  1.00 89.39  ? 12   ALA   D H    1 
ATOM   19607 H  HA   . ALA   D  4  12  ? 19.065  -70.823 -54.298  1.00 92.60  ? 12   ALA   D HA   1 
ATOM   19608 H  HB1  . ALA   D  4  12  ? 17.471  -70.367 -52.629  1.00 89.78  ? 12   ALA   D HB1  1 
ATOM   19609 H  HB2  . ALA   D  4  12  ? 18.141  -69.014 -53.124  1.00 89.78  ? 12   ALA   D HB2  1 
ATOM   19610 H  HB3  . ALA   D  4  12  ? 16.692  -69.416 -53.636  1.00 89.78  ? 12   ALA   D HB3  1 
ATOM   19611 N  N    . GLU   D  4  13  ? 17.627  -72.825 -54.285  1.00 85.25  ? 13   GLU   D N    1 
ATOM   19612 C  CA   . GLU   D  4  13  ? 16.852  -74.037 -54.477  1.00 84.50  ? 13   GLU   D CA   1 
ATOM   19613 C  C    . GLU   D  4  13  ? 15.536  -73.957 -53.709  1.00 82.36  ? 13   GLU   D C    1 
ATOM   19614 O  O    . GLU   D  4  13  ? 15.396  -73.159 -52.780  1.00 79.31  ? 13   GLU   D O    1 
ATOM   19615 C  CB   . GLU   D  4  13  ? 17.650  -75.249 -54.011  1.00 92.02  ? 13   GLU   D CB   1 
ATOM   19616 C  CG   . GLU   D  4  13  ? 18.924  -75.500 -54.797  1.00 96.70  ? 13   GLU   D CG   1 
ATOM   19617 C  CD   . GLU   D  4  13  ? 19.762  -76.612 -54.199  1.00 103.39 ? 13   GLU   D CD   1 
ATOM   19618 O  OE1  . GLU   D  4  13  ? 20.010  -76.578 -52.974  1.00 106.57 ? 13   GLU   D OE1  1 
ATOM   19619 O  OE2  . GLU   D  4  13  ? 20.164  -77.523 -54.952  1.00 107.86 ? 13   GLU   D OE2  1 
ATOM   19620 H  H    . GLU   D  4  13  ? 18.274  -72.909 -53.724  1.00 102.28 ? 13   GLU   D H    1 
ATOM   19621 H  HA   . GLU   D  4  13  ? 16.651  -74.149 -55.420  1.00 101.38 ? 13   GLU   D HA   1 
ATOM   19622 H  HB2  . GLU   D  4  13  ? 17.899  -75.117 -53.083  1.00 110.41 ? 13   GLU   D HB2  1 
ATOM   19623 H  HB3  . GLU   D  4  13  ? 17.093  -76.038 -54.095  1.00 110.41 ? 13   GLU   D HB3  1 
ATOM   19624 H  HG2  . GLU   D  4  13  ? 18.693  -75.752 -55.704  1.00 116.02 ? 13   GLU   D HG2  1 
ATOM   19625 H  HG3  . GLU   D  4  13  ? 19.458  -74.690 -54.803  1.00 116.02 ? 13   GLU   D HG3  1 
ATOM   19626 N  N    . PRO   D  4  14  ? 14.550  -74.775 -54.080  1.00 86.95  ? 14   PRO   D N    1 
ATOM   19627 C  CA   . PRO   D  4  14  ? 13.285  -74.776 -53.336  1.00 90.19  ? 14   PRO   D CA   1 
ATOM   19628 C  C    . PRO   D  4  14  ? 13.507  -75.076 -51.861  1.00 95.23  ? 14   PRO   D C    1 
ATOM   19629 O  O    . PRO   D  4  14  ? 14.290  -75.956 -51.496  1.00 97.74  ? 14   PRO   D O    1 
ATOM   19630 C  CB   . PRO   D  4  14  ? 12.470  -75.880 -54.021  1.00 94.16  ? 14   PRO   D CB   1 
ATOM   19631 C  CG   . PRO   D  4  14  ? 13.046  -75.985 -55.390  1.00 92.55  ? 14   PRO   D CG   1 
ATOM   19632 C  CD   . PRO   D  4  14  ? 14.509  -75.684 -55.240  1.00 90.66  ? 14   PRO   D CD   1 
ATOM   19633 H  HA   . PRO   D  4  14  ? 12.829  -73.925 -53.431  1.00 108.21 ? 14   PRO   D HA   1 
ATOM   19634 H  HB2  . PRO   D  4  14  ? 12.571  -76.715 -53.537  1.00 112.98 ? 14   PRO   D HB2  1 
ATOM   19635 H  HB3  . PRO   D  4  14  ? 11.534  -75.628 -54.056  1.00 112.98 ? 14   PRO   D HB3  1 
ATOM   19636 H  HG2  . PRO   D  4  14  ? 12.912  -76.882 -55.734  1.00 111.04 ? 14   PRO   D HG2  1 
ATOM   19637 H  HG3  . PRO   D  4  14  ? 12.620  -75.339 -55.974  1.00 111.04 ? 14   PRO   D HG3  1 
ATOM   19638 H  HD2  . PRO   D  4  14  ? 15.012  -76.494 -55.061  1.00 108.77 ? 14   PRO   D HD2  1 
ATOM   19639 H  HD3  . PRO   D  4  14  ? 14.855  -75.247 -56.034  1.00 108.77 ? 14   PRO   D HD3  1 
ATOM   19640 N  N    . GLY   D  4  15  ? 12.806  -74.328 -51.009  1.00 96.80  ? 15   GLY   D N    1 
ATOM   19641 C  CA   . GLY   D  4  15  ? 12.901  -74.488 -49.577  1.00 100.50 ? 15   GLY   D CA   1 
ATOM   19642 C  C    . GLY   D  4  15  ? 14.005  -73.689 -48.916  1.00 98.74  ? 15   GLY   D C    1 
ATOM   19643 O  O    . GLY   D  4  15  ? 13.985  -73.529 -47.690  1.00 103.22 ? 15   GLY   D O    1 
ATOM   19644 H  H    . GLY   D  4  15  ? 12.259  -73.709 -51.251  1.00 116.14 ? 15   GLY   D H    1 
ATOM   19645 H  HA2  . GLY   D  4  15  ? 12.060  -74.215 -49.178  1.00 120.58 ? 15   GLY   D HA2  1 
ATOM   19646 H  HA3  . GLY   D  4  15  ? 13.056  -75.425 -49.379  1.00 120.58 ? 15   GLY   D HA3  1 
ATOM   19647 N  N    . ALA   D  4  16  ? 14.960  -73.180 -49.688  1.00 91.30  ? 16   ALA   D N    1 
ATOM   19648 C  CA   . ALA   D  4  16  ? 16.067  -72.410 -49.139  1.00 87.33  ? 16   ALA   D CA   1 
ATOM   19649 C  C    . ALA   D  4  16  ? 15.597  -70.984 -48.857  1.00 82.17  ? 16   ALA   D C    1 
ATOM   19650 O  O    . ALA   D  4  16  ? 14.401  -70.681 -48.881  1.00 85.24  ? 16   ALA   D O    1 
ATOM   19651 C  CB   . ALA   D  4  16  ? 17.257  -72.442 -50.093  1.00 85.92  ? 16   ALA   D CB   1 
ATOM   19652 H  H    . ALA   D  4  16  ? 14.988  -73.268 -50.543  1.00 109.54 ? 16   ALA   D H    1 
ATOM   19653 H  HA   . ALA   D  4  16  ? 16.338  -72.818 -48.301  1.00 104.77 ? 16   ALA   D HA   1 
ATOM   19654 H  HB1  . ALA   D  4  16  ? 17.989  -71.938 -49.703  1.00 103.08 ? 16   ALA   D HB1  1 
ATOM   19655 H  HB2  . ALA   D  4  16  ? 17.527  -73.363 -50.231  1.00 103.08 ? 16   ALA   D HB2  1 
ATOM   19656 H  HB3  . ALA   D  4  16  ? 16.995  -72.044 -50.938  1.00 103.08 ? 16   ALA   D HB3  1 
ATOM   19657 N  N    . SER   D  4  17  ? 16.541  -70.087 -48.580  1.00 79.73  ? 17   SER   D N    1 
ATOM   19658 C  CA   . SER   D  4  17  ? 16.228  -68.690 -48.323  1.00 81.64  ? 17   SER   D CA   1 
ATOM   19659 C  C    . SER   D  4  17  ? 17.280  -67.809 -48.979  1.00 77.28  ? 17   SER   D C    1 
ATOM   19660 O  O    . SER   D  4  17  ? 18.398  -68.244 -49.266  1.00 78.44  ? 17   SER   D O    1 
ATOM   19661 C  CB   . SER   D  4  17  ? 16.162  -68.390 -46.819  1.00 93.14  ? 17   SER   D CB   1 
ATOM   19662 O  OG   . SER   D  4  17  ? 17.455  -68.398 -46.239  1.00 102.02 ? 17   SER   D OG   1 
ATOM   19663 H  H    . SER   D  4  17  ? 17.381  -70.269 -48.535  1.00 95.66  ? 17   SER   D H    1 
ATOM   19664 H  HA   . SER   D  4  17  ? 15.366  -68.482 -48.715  1.00 97.95  ? 17   SER   D HA   1 
ATOM   19665 H  HB2  . SER   D  4  17  ? 15.765  -67.514 -46.690  1.00 111.75 ? 17   SER   D HB2  1 
ATOM   19666 H  HB3  . SER   D  4  17  ? 15.618  -69.067 -46.386  1.00 111.75 ? 17   SER   D HB3  1 
ATOM   19667 H  HG   . SER   D  4  17  ? 17.400  -68.261 -45.412  1.00 122.41 ? 17   SER   D HG   1 
ATOM   19668 N  N    . VAL   D  4  18  ? 16.900  -66.554 -49.218  1.00 75.44  ? 18   VAL   D N    1 
ATOM   19669 C  CA   . VAL   D  4  18  ? 17.796  -65.548 -49.767  1.00 76.07  ? 18   VAL   D CA   1 
ATOM   19670 C  C    . VAL   D  4  18  ? 17.644  -64.276 -48.947  1.00 73.43  ? 18   VAL   D C    1 
ATOM   19671 O  O    . VAL   D  4  18  ? 16.611  -64.031 -48.319  1.00 73.48  ? 18   VAL   D O    1 
ATOM   19672 C  CB   . VAL   D  4  18  ? 17.522  -65.261 -51.260  1.00 75.39  ? 18   VAL   D CB   1 
ATOM   19673 C  CG1  . VAL   D  4  18  ? 17.820  -66.492 -52.099  1.00 77.96  ? 18   VAL   D CG1  1 
ATOM   19674 C  CG2  . VAL   D  4  18  ? 16.084  -64.802 -51.465  1.00 71.32  ? 18   VAL   D CG2  1 
ATOM   19675 H  H    . VAL   D  4  18  ? 16.107  -66.258 -49.064  1.00 90.51  ? 18   VAL   D H    1 
ATOM   19676 H  HA   . VAL   D  4  18  ? 18.711  -65.860 -49.690  1.00 91.27  ? 18   VAL   D HA   1 
ATOM   19677 H  HB   . VAL   D  4  18  ? 18.107  -64.545 -51.554  1.00 90.45  ? 18   VAL   D HB   1 
ATOM   19678 H  HG11 . VAL   D  4  18  ? 17.618  -66.298 -53.028  1.00 93.54  ? 18   VAL   D HG11 1 
ATOM   19679 H  HG12 . VAL   D  4  18  ? 18.759  -66.718 -52.006  1.00 93.54  ? 18   VAL   D HG12 1 
ATOM   19680 H  HG13 . VAL   D  4  18  ? 17.270  -67.228 -51.788  1.00 93.54  ? 18   VAL   D HG13 1 
ATOM   19681 H  HG21 . VAL   D  4  18  ? 15.930  -64.660 -52.412  1.00 85.57  ? 18   VAL   D HG21 1 
ATOM   19682 H  HG22 . VAL   D  4  18  ? 15.483  -65.486 -51.132  1.00 85.57  ? 18   VAL   D HG22 1 
ATOM   19683 H  HG23 . VAL   D  4  18  ? 15.944  -63.974 -50.980  1.00 85.57  ? 18   VAL   D HG23 1 
ATOM   19684 N  N    . LYS   D  4  19  ? 18.698  -63.465 -48.956  1.00 71.46  ? 19   LYS   D N    1 
ATOM   19685 C  CA   . LYS   D  4  19  ? 18.717  -62.186 -48.259  1.00 67.70  ? 19   LYS   D CA   1 
ATOM   19686 C  C    . LYS   D  4  19  ? 19.271  -61.139 -49.211  1.00 67.70  ? 19   LYS   D C    1 
ATOM   19687 O  O    . LYS   D  4  19  ? 20.382  -61.293 -49.727  1.00 73.88  ? 19   LYS   D O    1 
ATOM   19688 C  CB   . LYS   D  4  19  ? 19.561  -62.262 -46.984  1.00 70.52  ? 19   LYS   D CB   1 
ATOM   19689 C  CG   . LYS   D  4  19  ? 19.366  -61.088 -46.036  1.00 73.36  ? 19   LYS   D CG   1 
ATOM   19690 C  CD   . LYS   D  4  19  ? 20.272  -61.208 -44.821  1.00 76.04  ? 19   LYS   D CD   1 
ATOM   19691 C  CE   . LYS   D  4  19  ? 19.989  -60.120 -43.796  1.00 77.32  ? 19   LYS   D CE   1 
ATOM   19692 N  NZ   . LYS   D  4  19  ? 20.952  -60.159 -42.661  1.00 82.52  ? 19   LYS   D NZ   1 
ATOM   19693 H  H    . LYS   D  4  19  ? 19.432  -63.640 -49.369  1.00 85.73  ? 19   LYS   D H    1 
ATOM   19694 H  HA   . LYS   D  4  19  ? 17.816  -61.932 -48.007  1.00 81.22  ? 19   LYS   D HA   1 
ATOM   19695 H  HB2  . LYS   D  4  19  ? 19.325  -63.070 -46.503  1.00 84.60  ? 19   LYS   D HB2  1 
ATOM   19696 H  HB3  . LYS   D  4  19  ? 20.499  -62.286 -47.233  1.00 84.60  ? 19   LYS   D HB3  1 
ATOM   19697 H  HG2  . LYS   D  4  19  ? 19.580  -60.261 -46.497  1.00 88.01  ? 19   LYS   D HG2  1 
ATOM   19698 H  HG3  . LYS   D  4  19  ? 18.445  -61.069 -45.731  1.00 88.01  ? 19   LYS   D HG3  1 
ATOM   19699 H  HD2  . LYS   D  4  19  ? 20.128  -62.068 -44.397  1.00 91.23  ? 19   LYS   D HD2  1 
ATOM   19700 H  HD3  . LYS   D  4  19  ? 21.197  -61.127 -45.101  1.00 91.23  ? 19   LYS   D HD3  1 
ATOM   19701 H  HE2  . LYS   D  4  19  ? 20.060  -59.252 -44.224  1.00 92.76  ? 19   LYS   D HE2  1 
ATOM   19702 H  HE3  . LYS   D  4  19  ? 19.095  -60.242 -43.440  1.00 92.76  ? 19   LYS   D HE3  1 
ATOM   19703 H  HZ1  . LYS   D  4  19  ? 20.760  -59.516 -42.077  1.00 99.00  ? 19   LYS   D HZ1  1 
ATOM   19704 H  HZ2  . LYS   D  4  19  ? 20.906  -60.947 -42.250  1.00 99.00  ? 19   LYS   D HZ2  1 
ATOM   19705 H  HZ3  . LYS   D  4  19  ? 21.781  -60.038 -42.961  1.00 99.00  ? 19   LYS   D HZ3  1 
ATOM   19706 N  N    . MET   D  4  20  ? 18.497  -60.084 -49.447  1.00 64.98  ? 20   MET   D N    1 
ATOM   19707 C  CA   . MET   D  4  20  ? 18.871  -59.019 -50.363  1.00 65.20  ? 20   MET   D CA   1 
ATOM   19708 C  C    . MET   D  4  20  ? 18.965  -57.704 -49.603  1.00 66.70  ? 20   MET   D C    1 
ATOM   19709 O  O    . MET   D  4  20  ? 18.327  -57.522 -48.562  1.00 66.52  ? 20   MET   D O    1 
ATOM   19710 C  CB   . MET   D  4  20  ? 17.860  -58.899 -51.511  1.00 64.01  ? 20   MET   D CB   1 
ATOM   19711 C  CG   . MET   D  4  20  ? 16.449  -58.550 -51.070  1.00 64.25  ? 20   MET   D CG   1 
ATOM   19712 S  SD   . MET   D  4  20  ? 15.236  -58.767 -52.387  1.00 65.77  ? 20   MET   D SD   1 
ATOM   19713 C  CE   . MET   D  4  20  ? 15.170  -60.554 -52.489  1.00 63.47  ? 20   MET   D CE   1 
ATOM   19714 H  H    . MET   D  4  20  ? 17.730  -59.963 -49.076  1.00 77.96  ? 20   MET   D H    1 
ATOM   19715 H  HA   . MET   D  4  20  ? 19.737  -59.215 -50.755  1.00 78.22  ? 20   MET   D HA   1 
ATOM   19716 H  HB2  . MET   D  4  20  ? 18.160  -58.203 -52.115  1.00 76.80  ? 20   MET   D HB2  1 
ATOM   19717 H  HB3  . MET   D  4  20  ? 17.820  -59.749 -51.978  1.00 76.80  ? 20   MET   D HB3  1 
ATOM   19718 H  HG2  . MET   D  4  20  ? 16.197  -59.125 -50.331  1.00 77.08  ? 20   MET   D HG2  1 
ATOM   19719 H  HG3  . MET   D  4  20  ? 16.426  -57.621 -50.790  1.00 77.08  ? 20   MET   D HG3  1 
ATOM   19720 H  HE1  . MET   D  4  20  ? 14.491  -60.809 -53.133  1.00 76.15  ? 20   MET   D HE1  1 
ATOM   19721 H  HE2  . MET   D  4  20  ? 16.036  -60.887 -52.772  1.00 76.15  ? 20   MET   D HE2  1 
ATOM   19722 H  HE3  . MET   D  4  20  ? 14.948  -60.912 -51.615  1.00 76.15  ? 20   MET   D HE3  1 
ATOM   19723 N  N    . SER   D  4  21  ? 19.771  -56.788 -50.132  1.00 66.51  ? 21   SER   D N    1 
ATOM   19724 C  CA   . SER   D  4  21  ? 20.060  -55.531 -49.465  1.00 65.86  ? 21   SER   D CA   1 
ATOM   19725 C  C    . SER   D  4  21  ? 19.549  -54.359 -50.291  1.00 63.22  ? 21   SER   D C    1 
ATOM   19726 O  O    . SER   D  4  21  ? 19.231  -54.491 -51.476  1.00 61.14  ? 21   SER   D O    1 
ATOM   19727 C  CB   . SER   D  4  21  ? 21.565  -55.369 -49.215  1.00 68.69  ? 21   SER   D CB   1 
ATOM   19728 O  OG   . SER   D  4  21  ? 22.260  -55.150 -50.430  1.00 72.88  ? 21   SER   D OG   1 
ATOM   19729 H  H    . SER   D  4  21  ? 20.166  -56.877 -50.891  1.00 79.79  ? 21   SER   D H    1 
ATOM   19730 H  HA   . SER   D  4  21  ? 19.602  -55.516 -48.610  1.00 79.01  ? 21   SER   D HA   1 
ATOM   19731 H  HB2  . SER   D  4  21  ? 21.707  -54.609 -48.630  1.00 82.41  ? 21   SER   D HB2  1 
ATOM   19732 H  HB3  . SER   D  4  21  ? 21.905  -56.176 -48.799  1.00 82.41  ? 21   SER   D HB3  1 
ATOM   19733 H  HG   . SER   D  4  21  ? 23.087  -55.124 -50.288  1.00 87.44  ? 21   SER   D HG   1 
ATOM   19734 N  N    . CYS   D  4  22  ? 19.481  -53.200 -49.635  1.00 63.45  ? 22   CYS   D N    1 
ATOM   19735 C  CA   . CYS   D  4  22  ? 18.994  -51.970 -50.258  1.00 63.75  ? 22   CYS   D CA   1 
ATOM   19736 C  C    . CYS   D  4  22  ? 19.671  -50.811 -49.530  1.00 61.05  ? 22   CYS   D C    1 
ATOM   19737 O  O    . CYS   D  4  22  ? 19.223  -50.410 -48.452  1.00 58.50  ? 22   CYS   D O    1 
ATOM   19738 C  CB   . CYS   D  4  22  ? 17.476  -51.884 -50.171  1.00 64.42  ? 22   CYS   D CB   1 
ATOM   19739 S  SG   . CYS   D  4  22  ? 16.742  -50.284 -50.602  1.00 68.42  ? 22   CYS   D SG   1 
ATOM   19740 H  H    . CYS   D  4  22  ? 19.715  -53.099 -48.814  1.00 76.12  ? 22   CYS   D H    1 
ATOM   19741 H  HA   . CYS   D  4  22  ? 19.249  -51.944 -51.194  1.00 76.48  ? 22   CYS   D HA   1 
ATOM   19742 H  HB2  . CYS   D  4  22  ? 17.101  -52.543 -50.776  1.00 77.28  ? 22   CYS   D HB2  1 
ATOM   19743 H  HB3  . CYS   D  4  22  ? 17.213  -52.083 -49.259  1.00 77.28  ? 22   CYS   D HB3  1 
ATOM   19744 N  N    . LYS   D  4  23  ? 20.743  -50.286 -50.118  1.00 59.75  ? 23   LYS   D N    1 
ATOM   19745 C  CA   . LYS   D  4  23  ? 21.514  -49.216 -49.499  1.00 63.48  ? 23   LYS   D CA   1 
ATOM   19746 C  C    . LYS   D  4  23  ? 20.982  -47.868 -49.965  1.00 63.51  ? 23   LYS   D C    1 
ATOM   19747 O  O    . LYS   D  4  23  ? 20.813  -47.641 -51.168  1.00 68.21  ? 23   LYS   D O    1 
ATOM   19748 C  CB   . LYS   D  4  23  ? 22.999  -49.346 -49.837  1.00 71.90  ? 23   LYS   D CB   1 
ATOM   19749 C  CG   . LYS   D  4  23  ? 23.879  -48.311 -49.145  1.00 81.13  ? 23   LYS   D CG   1 
ATOM   19750 C  CD   . LYS   D  4  23  ? 25.338  -48.455 -49.545  1.00 91.35  ? 23   LYS   D CD   1 
ATOM   19751 C  CE   . LYS   D  4  23  ? 26.203  -47.376 -48.910  1.00 97.08  ? 23   LYS   D CE   1 
ATOM   19752 N  NZ   . LYS   D  4  23  ? 26.202  -47.445 -47.422  1.00 98.59  ? 23   LYS   D NZ   1 
ATOM   19753 H  H    . LYS   D  4  23  ? 21.046  -50.537 -50.883  1.00 71.68  ? 23   LYS   D H    1 
ATOM   19754 H  HA   . LYS   D  4  23  ? 21.420  -49.270 -48.535  1.00 76.16  ? 23   LYS   D HA   1 
ATOM   19755 H  HB2  . LYS   D  4  23  ? 23.306  -50.225 -49.565  1.00 86.26  ? 23   LYS   D HB2  1 
ATOM   19756 H  HB3  . LYS   D  4  23  ? 23.112  -49.237 -50.794  1.00 86.26  ? 23   LYS   D HB3  1 
ATOM   19757 H  HG2  . LYS   D  4  23  ? 23.582  -47.421 -49.392  1.00 97.33  ? 23   LYS   D HG2  1 
ATOM   19758 H  HG3  . LYS   D  4  23  ? 23.814  -48.427 -48.184  1.00 97.33  ? 23   LYS   D HG3  1 
ATOM   19759 H  HD2  . LYS   D  4  23  ? 25.667  -49.320 -49.253  1.00 109.59 ? 23   LYS   D HD2  1 
ATOM   19760 H  HD3  . LYS   D  4  23  ? 25.415  -48.379 -50.509  1.00 109.59 ? 23   LYS   D HD3  1 
ATOM   19761 H  HE2  . LYS   D  4  23  ? 27.118  -47.482 -49.215  1.00 116.47 ? 23   LYS   D HE2  1 
ATOM   19762 H  HE3  . LYS   D  4  23  ? 25.865  -46.505 -49.171  1.00 116.47 ? 23   LYS   D HE3  1 
ATOM   19763 H  HZ1  . LYS   D  4  23  ? 26.782  -46.857 -47.089  1.00 118.29 ? 23   LYS   D HZ1  1 
ATOM   19764 H  HZ2  . LYS   D  4  23  ? 25.390  -47.259 -47.109  1.00 118.29 ? 23   LYS   D HZ2  1 
ATOM   19765 H  HZ3  . LYS   D  4  23  ? 26.434  -48.262 -47.155  1.00 118.29 ? 23   LYS   D HZ3  1 
ATOM   19766 N  N    . ALA   D  4  24  ? 20.729  -46.976 -49.013  1.00 62.12  ? 24   ALA   D N    1 
ATOM   19767 C  CA   . ALA   D  4  24  ? 20.139  -45.677 -49.293  1.00 62.88  ? 24   ALA   D CA   1 
ATOM   19768 C  C    . ALA   D  4  24  ? 21.187  -44.575 -49.209  1.00 67.44  ? 24   ALA   D C    1 
ATOM   19769 O  O    . ALA   D  4  24  ? 22.128  -44.641 -48.414  1.00 72.01  ? 24   ALA   D O    1 
ATOM   19770 C  CB   . ALA   D  4  24  ? 18.998  -45.378 -48.319  1.00 61.48  ? 24   ALA   D CB   1 
ATOM   19771 H  H    . ALA   D  4  24  ? 20.895  -47.106 -48.179  1.00 74.52  ? 24   ALA   D H    1 
ATOM   19772 H  HA   . ALA   D  4  24  ? 19.783  -45.682 -50.195  1.00 75.43  ? 24   ALA   D HA   1 
ATOM   19773 H  HB1  . ALA   D  4  24  ? 18.632  -44.502 -48.521  1.00 73.76  ? 24   ALA   D HB1  1 
ATOM   19774 H  HB2  . ALA   D  4  24  ? 18.310  -46.055 -48.421  1.00 73.76  ? 24   ALA   D HB2  1 
ATOM   19775 H  HB3  . ALA   D  4  24  ? 19.344  -45.391 -47.413  1.00 73.76  ? 24   ALA   D HB3  1 
ATOM   19776 N  N    . SER   D  4  25  ? 21.008  -43.555 -50.045  1.00 67.26  ? 25   SER   D N    1 
ATOM   19777 C  CA   . SER   D  4  25  ? 21.871  -42.385 -50.046  1.00 70.51  ? 25   SER   D CA   1 
ATOM   19778 C  C    . SER   D  4  25  ? 21.053  -41.191 -50.512  1.00 69.90  ? 25   SER   D C    1 
ATOM   19779 O  O    . SER   D  4  25  ? 20.047  -41.340 -51.211  1.00 70.25  ? 25   SER   D O    1 
ATOM   19780 C  CB   . SER   D  4  25  ? 23.096  -42.583 -50.945  1.00 75.45  ? 25   SER   D CB   1 
ATOM   19781 O  OG   . SER   D  4  25  ? 22.705  -42.817 -52.286  1.00 79.20  ? 25   SER   D OG   1 
ATOM   19782 H  H    . SER   D  4  25  ? 20.380  -43.520 -50.632  1.00 80.69  ? 25   SER   D H    1 
ATOM   19783 H  HA   . SER   D  4  25  ? 22.189  -42.213 -49.146  1.00 84.60  ? 25   SER   D HA   1 
ATOM   19784 H  HB2  . SER   D  4  25  ? 23.645  -41.784 -50.912  1.00 90.52  ? 25   SER   D HB2  1 
ATOM   19785 H  HB3  . SER   D  4  25  ? 23.602  -43.347 -50.626  1.00 90.52  ? 25   SER   D HB3  1 
ATOM   19786 H  HG   . SER   D  4  25  ? 23.383  -42.922 -52.770  1.00 95.02  ? 25   SER   D HG   1 
ATOM   19787 N  N    . GLY   D  4  26  ? 21.493  -40.001 -50.113  1.00 69.86  ? 26   GLY   D N    1 
ATOM   19788 C  CA   . GLY   D  4  26  ? 20.811  -38.778 -50.474  1.00 68.88  ? 26   GLY   D CA   1 
ATOM   19789 C  C    . GLY   D  4  26  ? 19.793  -38.291 -49.468  1.00 66.87  ? 26   GLY   D C    1 
ATOM   19790 O  O    . GLY   D  4  26  ? 19.218  -37.213 -49.666  1.00 69.59  ? 26   GLY   D O    1 
ATOM   19791 H  H    . GLY   D  4  26  ? 22.192  -39.882 -49.627  1.00 83.81  ? 26   GLY   D H    1 
ATOM   19792 H  HA2  . GLY   D  4  26  ? 21.472  -38.077 -50.587  1.00 82.64  ? 26   GLY   D HA2  1 
ATOM   19793 H  HA3  . GLY   D  4  26  ? 20.351  -38.917 -51.316  1.00 82.64  ? 26   GLY   D HA3  1 
ATOM   19794 N  N    . TYR   D  4  27  ? 19.543  -39.047 -48.402  1.00 63.21  ? 27   TYR   D N    1 
ATOM   19795 C  CA   . TYR   D  4  27  ? 18.629  -38.617 -47.354  1.00 61.84  ? 27   TYR   D CA   1 
ATOM   19796 C  C    . TYR   D  4  27  ? 18.992  -39.352 -46.073  1.00 65.18  ? 27   TYR   D C    1 
ATOM   19797 O  O    . TYR   D  4  27  ? 19.803  -40.281 -46.073  1.00 68.52  ? 27   TYR   D O    1 
ATOM   19798 C  CB   . TYR   D  4  27  ? 17.168  -38.871 -47.743  1.00 56.31  ? 27   TYR   D CB   1 
ATOM   19799 C  CG   . TYR   D  4  27  ? 16.757  -40.326 -47.707  1.00 56.83  ? 27   TYR   D CG   1 
ATOM   19800 C  CD1  . TYR   D  4  27  ? 17.019  -41.171 -48.778  1.00 59.47  ? 27   TYR   D CD1  1 
ATOM   19801 C  CD2  . TYR   D  4  27  ? 16.098  -40.854 -46.605  1.00 58.86  ? 27   TYR   D CD2  1 
ATOM   19802 C  CE1  . TYR   D  4  27  ? 16.642  -42.501 -48.749  1.00 60.49  ? 27   TYR   D CE1  1 
ATOM   19803 C  CE2  . TYR   D  4  27  ? 15.717  -42.181 -46.567  1.00 61.76  ? 27   TYR   D CE2  1 
ATOM   19804 C  CZ   . TYR   D  4  27  ? 15.991  -43.000 -47.641  1.00 63.37  ? 27   TYR   D CZ   1 
ATOM   19805 O  OH   . TYR   D  4  27  ? 15.612  -44.322 -47.605  1.00 63.99  ? 27   TYR   D OH   1 
ATOM   19806 H  H    . TYR   D  4  27  ? 19.895  -39.819 -48.264  1.00 75.83  ? 27   TYR   D H    1 
ATOM   19807 H  HA   . TYR   D  4  27  ? 18.738  -37.665 -47.204  1.00 74.19  ? 27   TYR   D HA   1 
ATOM   19808 H  HB2  . TYR   D  4  27  ? 16.595  -38.389 -47.126  1.00 67.55  ? 27   TYR   D HB2  1 
ATOM   19809 H  HB3  . TYR   D  4  27  ? 17.027  -38.548 -48.647  1.00 67.55  ? 27   TYR   D HB3  1 
ATOM   19810 H  HD1  . TYR   D  4  27  ? 17.456  -40.836 -49.528  1.00 71.34  ? 27   TYR   D HD1  1 
ATOM   19811 H  HD2  . TYR   D  4  27  ? 15.910  -40.304 -45.879  1.00 70.62  ? 27   TYR   D HD2  1 
ATOM   19812 H  HE1  . TYR   D  4  27  ? 16.826  -43.056 -49.473  1.00 72.57  ? 27   TYR   D HE1  1 
ATOM   19813 H  HE2  . TYR   D  4  27  ? 15.278  -42.520 -45.821  1.00 74.10  ? 27   TYR   D HE2  1 
ATOM   19814 H  HH   . TYR   D  4  27  ? 15.201  -44.484 -46.891  1.00 76.77  ? 27   TYR   D HH   1 
ATOM   19815 N  N    . THR   D  4  28  ? 18.378  -38.921 -44.974  1.00 62.89  ? 28   THR   D N    1 
ATOM   19816 C  CA   . THR   D  4  28  ? 18.627  -39.529 -43.671  1.00 62.81  ? 28   THR   D CA   1 
ATOM   19817 C  C    . THR   D  4  28  ? 17.836  -40.829 -43.587  1.00 63.65  ? 28   THR   D C    1 
ATOM   19818 O  O    . THR   D  4  28  ? 16.611  -40.815 -43.425  1.00 59.63  ? 28   THR   D O    1 
ATOM   19819 C  CB   . THR   D  4  28  ? 18.252  -38.567 -42.548  1.00 58.26  ? 28   THR   D CB   1 
ATOM   19820 O  OG1  . THR   D  4  28  ? 19.005  -37.355 -42.691  1.00 56.50  ? 28   THR   D OG1  1 
ATOM   19821 C  CG2  . THR   D  4  28  ? 18.550  -39.191 -41.188  1.00 55.67  ? 28   THR   D CG2  1 
ATOM   19822 H  H    . THR   D  4  28  ? 17.811  -38.274 -44.957  1.00 75.45  ? 28   THR   D H    1 
ATOM   19823 H  HA   . THR   D  4  28  ? 19.570  -39.734 -43.578  1.00 75.35  ? 28   THR   D HA   1 
ATOM   19824 H  HB   . THR   D  4  28  ? 17.304  -38.368 -42.591  1.00 69.90  ? 28   THR   D HB   1 
ATOM   19825 H  HG1  . THR   D  4  28  ? 18.727  -36.778 -42.147  1.00 67.78  ? 28   THR   D HG1  1 
ATOM   19826 H  HG21 . THR   D  4  28  ? 18.341  -38.560 -40.481  1.00 66.79  ? 28   THR   D HG21 1 
ATOM   19827 H  HG22 . THR   D  4  28  ? 18.014  -39.990 -41.065  1.00 66.79  ? 28   THR   D HG22 1 
ATOM   19828 H  HG23 . THR   D  4  28  ? 19.488  -39.429 -41.131  1.00 66.79  ? 28   THR   D HG23 1 
ATOM   19829 N  N    . PHE   D  4  29  ? 18.548  -41.952 -43.697  1.00 64.94  ? 29   PHE   D N    1 
ATOM   19830 C  CA   . PHE   D  4  29  ? 17.905  -43.259 -43.779  1.00 62.17  ? 29   PHE   D CA   1 
ATOM   19831 C  C    . PHE   D  4  29  ? 17.029  -43.536 -42.563  1.00 61.50  ? 29   PHE   D C    1 
ATOM   19832 O  O    . PHE   D  4  29  ? 15.951  -44.130 -42.688  1.00 62.61  ? 29   PHE   D O    1 
ATOM   19833 C  CB   . PHE   D  4  29  ? 18.989  -44.329 -43.930  1.00 60.90  ? 29   PHE   D CB   1 
ATOM   19834 C  CG   . PHE   D  4  29  ? 18.474  -45.737 -43.930  1.00 58.50  ? 29   PHE   D CG   1 
ATOM   19835 C  CD1  . PHE   D  4  29  ? 17.834  -46.257 -45.041  1.00 56.09  ? 29   PHE   D CD1  1 
ATOM   19836 C  CD2  . PHE   D  4  29  ? 18.663  -46.553 -42.828  1.00 60.72  ? 29   PHE   D CD2  1 
ATOM   19837 C  CE1  . PHE   D  4  29  ? 17.373  -47.559 -45.045  1.00 59.22  ? 29   PHE   D CE1  1 
ATOM   19838 C  CE2  . PHE   D  4  29  ? 18.210  -47.855 -42.826  1.00 58.84  ? 29   PHE   D CE2  1 
ATOM   19839 C  CZ   . PHE   D  4  29  ? 17.562  -48.360 -43.935  1.00 60.73  ? 29   PHE   D CZ   1 
ATOM   19840 H  H    . PHE   D  4  29  ? 19.407  -41.983 -43.726  1.00 77.91  ? 29   PHE   D H    1 
ATOM   19841 H  HA   . PHE   D  4  29  ? 17.325  -43.288 -44.556  1.00 74.59  ? 29   PHE   D HA   1 
ATOM   19842 H  HB2  . PHE   D  4  29  ? 19.450  -44.185 -44.772  1.00 73.06  ? 29   PHE   D HB2  1 
ATOM   19843 H  HB3  . PHE   D  4  29  ? 19.612  -44.244 -43.192  1.00 73.06  ? 29   PHE   D HB3  1 
ATOM   19844 H  HD1  . PHE   D  4  29  ? 17.712  -45.724 -45.793  1.00 67.29  ? 29   PHE   D HD1  1 
ATOM   19845 H  HD2  . PHE   D  4  29  ? 19.100  -46.218 -42.079  1.00 72.84  ? 29   PHE   D HD2  1 
ATOM   19846 H  HE1  . PHE   D  4  29  ? 16.935  -47.896 -45.793  1.00 71.05  ? 29   PHE   D HE1  1 
ATOM   19847 H  HE2  . PHE   D  4  29  ? 18.341  -48.393 -42.079  1.00 70.59  ? 29   PHE   D HE2  1 
ATOM   19848 H  HZ   . PHE   D  4  29  ? 17.254  -49.238 -43.935  1.00 72.85  ? 29   PHE   D HZ   1 
ATOM   19849 N  N    . SER   D  4  30  ? 17.465  -43.101 -41.380  1.00 60.87  ? 30   SER   D N    1 
ATOM   19850 C  CA   . SER   D  4  30  ? 16.781  -43.470 -40.146  1.00 63.27  ? 30   SER   D CA   1 
ATOM   19851 C  C    . SER   D  4  30  ? 15.423  -42.797 -39.990  1.00 61.91  ? 30   SER   D C    1 
ATOM   19852 O  O    . SER   D  4  30  ? 14.599  -43.277 -39.204  1.00 62.04  ? 30   SER   D O    1 
ATOM   19853 C  CB   . SER   D  4  30  ? 17.659  -43.119 -38.944  1.00 67.80  ? 30   SER   D CB   1 
ATOM   19854 O  OG   . SER   D  4  30  ? 18.941  -43.708 -39.059  1.00 77.34  ? 30   SER   D OG   1 
ATOM   19855 H  H    . SER   D  4  30  ? 18.151  -42.594 -41.268  1.00 73.03  ? 30   SER   D H    1 
ATOM   19856 H  HA   . SER   D  4  30  ? 16.634  -44.429 -40.160  1.00 75.90  ? 30   SER   D HA   1 
ATOM   19857 H  HB2  . SER   D  4  30  ? 17.758  -42.155 -38.898  1.00 81.34  ? 30   SER   D HB2  1 
ATOM   19858 H  HB3  . SER   D  4  30  ? 17.233  -43.448 -38.137  1.00 81.34  ? 30   SER   D HB3  1 
ATOM   19859 H  HG   . SER   D  4  30  ? 19.392  -43.553 -38.368  1.00 92.79  ? 30   SER   D HG   1 
ATOM   19860 N  N    . SER   D  4  31  ? 15.167  -41.707 -40.709  1.00 58.65  ? 31   SER   D N    1 
ATOM   19861 C  CA   . SER   D  4  31  ? 13.977  -40.897 -40.490  1.00 57.47  ? 31   SER   D CA   1 
ATOM   19862 C  C    . SER   D  4  31  ? 12.821  -41.255 -41.414  1.00 57.40  ? 31   SER   D C    1 
ATOM   19863 O  O    . SER   D  4  31  ? 11.776  -40.600 -41.352  1.00 57.38  ? 31   SER   D O    1 
ATOM   19864 C  CB   . SER   D  4  31  ? 14.318  -39.412 -40.658  1.00 56.54  ? 31   SER   D CB   1 
ATOM   19865 O  OG   . SER   D  4  31  ? 15.221  -38.981 -39.656  1.00 60.51  ? 31   SER   D OG   1 
ATOM   19866 H  H    . SER   D  4  31  ? 15.677  -41.414 -41.337  1.00 70.36  ? 31   SER   D H    1 
ATOM   19867 H  HA   . SER   D  4  31  ? 13.677  -41.043 -39.580  1.00 68.94  ? 31   SER   D HA   1 
ATOM   19868 H  HB2  . SER   D  4  31  ? 14.726  -39.279 -41.528  1.00 67.83  ? 31   SER   D HB2  1 
ATOM   19869 H  HB3  . SER   D  4  31  ? 13.501  -38.892 -40.591  1.00 67.83  ? 31   SER   D HB3  1 
ATOM   19870 H  HG   . SER   D  4  31  ? 15.386  -38.162 -39.751  1.00 72.60  ? 31   SER   D HG   1 
ATOM   19871 N  N    . PHE   D  4  32  ? 12.971  -42.272 -42.261  1.00 57.10  ? 32   PHE   D N    1 
ATOM   19872 C  CA   . PHE   D  4  32  ? 11.933  -42.619 -43.220  1.00 55.11  ? 32   PHE   D CA   1 
ATOM   19873 C  C    . PHE   D  4  32  ? 11.783  -44.127 -43.318  1.00 51.12  ? 32   PHE   D C    1 
ATOM   19874 O  O    . PHE   D  4  32  ? 12.772  -44.864 -43.305  1.00 52.23  ? 32   PHE   D O    1 
ATOM   19875 C  CB   . PHE   D  4  32  ? 12.244  -42.033 -44.602  1.00 56.47  ? 32   PHE   D CB   1 
ATOM   19876 C  CG   . PHE   D  4  32  ? 12.278  -40.536 -44.623  1.00 59.29  ? 32   PHE   D CG   1 
ATOM   19877 C  CD1  . PHE   D  4  32  ? 11.121  -39.807 -44.846  1.00 59.32  ? 32   PHE   D CD1  1 
ATOM   19878 C  CD2  . PHE   D  4  32  ? 13.463  -39.855 -44.406  1.00 62.22  ? 32   PHE   D CD2  1 
ATOM   19879 C  CE1  . PHE   D  4  32  ? 11.149  -38.429 -44.861  1.00 60.15  ? 32   PHE   D CE1  1 
ATOM   19880 C  CE2  . PHE   D  4  32  ? 13.498  -38.477 -44.419  1.00 61.71  ? 32   PHE   D CE2  1 
ATOM   19881 C  CZ   . PHE   D  4  32  ? 12.338  -37.761 -44.646  1.00 60.74  ? 32   PHE   D CZ   1 
ATOM   19882 H  H    . PHE   D  4  32  ? 13.667  -42.775 -42.296  1.00 68.50  ? 32   PHE   D H    1 
ATOM   19883 H  HA   . PHE   D  4  32  ? 11.085  -42.263 -42.912  1.00 66.11  ? 32   PHE   D HA   1 
ATOM   19884 H  HB2  . PHE   D  4  32  ? 13.113  -42.354 -44.889  1.00 67.74  ? 32   PHE   D HB2  1 
ATOM   19885 H  HB3  . PHE   D  4  32  ? 11.560  -42.324 -45.225  1.00 67.74  ? 32   PHE   D HB3  1 
ATOM   19886 H  HD1  . PHE   D  4  32  ? 10.318  -40.253 -44.989  1.00 71.16  ? 32   PHE   D HD1  1 
ATOM   19887 H  HD2  . PHE   D  4  32  ? 14.246  -40.333 -44.251  1.00 74.65  ? 32   PHE   D HD2  1 
ATOM   19888 H  HE1  . PHE   D  4  32  ? 10.367  -37.949 -45.015  1.00 72.16  ? 32   PHE   D HE1  1 
ATOM   19889 H  HE2  . PHE   D  4  32  ? 14.300  -38.030 -44.275  1.00 74.04  ? 32   PHE   D HE2  1 
ATOM   19890 H  HZ   . PHE   D  4  32  ? 12.359  -36.832 -44.655  1.00 72.87  ? 32   PHE   D HZ   1 
ATOM   19891 N  N    . TRP   D  4  33  ? 10.534  -44.575 -43.411  1.00 50.74  ? 33   TRP   D N    1 
ATOM   19892 C  CA   . TRP   D  4  33  ? 10.250  -45.988 -43.581  1.00 51.73  ? 33   TRP   D CA   1 
ATOM   19893 C  C    . TRP   D  4  33  ? 10.771  -46.483 -44.927  1.00 50.45  ? 33   TRP   D C    1 
ATOM   19894 O  O    . TRP   D  4  33  ? 10.945  -45.719 -45.881  1.00 50.90  ? 33   TRP   D O    1 
ATOM   19895 C  CB   . TRP   D  4  33  ? 8.747   -46.249 -43.494  1.00 52.21  ? 33   TRP   D CB   1 
ATOM   19896 C  CG   . TRP   D  4  33  ? 8.134   -45.909 -42.175  1.00 58.46  ? 33   TRP   D CG   1 
ATOM   19897 C  CD1  . TRP   D  4  33  ? 8.777   -45.478 -41.051  1.00 60.08  ? 33   TRP   D CD1  1 
ATOM   19898 C  CD2  . TRP   D  4  33  ? 6.744   -45.973 -41.843  1.00 64.56  ? 33   TRP   D CD2  1 
ATOM   19899 N  NE1  . TRP   D  4  33  ? 7.871   -45.270 -40.039  1.00 63.53  ? 33   TRP   D NE1  1 
ATOM   19900 C  CE2  . TRP   D  4  33  ? 6.615   -45.568 -40.500  1.00 65.88  ? 33   TRP   D CE2  1 
ATOM   19901 C  CE3  . TRP   D  4  33  ? 5.594   -46.335 -42.552  1.00 65.80  ? 33   TRP   D CE3  1 
ATOM   19902 C  CZ2  . TRP   D  4  33  ? 5.384   -45.515 -39.852  1.00 69.32  ? 33   TRP   D CZ2  1 
ATOM   19903 C  CZ3  . TRP   D  4  33  ? 4.374   -46.282 -41.908  1.00 68.21  ? 33   TRP   D CZ3  1 
ATOM   19904 C  CH2  . TRP   D  4  33  ? 4.278   -45.875 -40.571  1.00 70.95  ? 33   TRP   D CH2  1 
ATOM   19905 H  H    . TRP   D  4  33  ? 9.834   -44.077 -43.378  1.00 60.87  ? 33   TRP   D H    1 
ATOM   19906 H  HA   . TRP   D  4  33  ? 10.690  -46.486 -42.875  1.00 62.06  ? 33   TRP   D HA   1 
ATOM   19907 H  HB2  . TRP   D  4  33  ? 8.302   -45.715 -44.171  1.00 62.63  ? 33   TRP   D HB2  1 
ATOM   19908 H  HB3  . TRP   D  4  33  ? 8.588   -47.191 -43.657  1.00 62.63  ? 33   TRP   D HB3  1 
ATOM   19909 H  HD1  . TRP   D  4  33  ? 9.695   -45.344 -40.980  1.00 72.07  ? 33   TRP   D HD1  1 
ATOM   19910 H  HE1  . TRP   D  4  33  ? 8.060   -44.998 -39.246  1.00 76.21  ? 33   TRP   D HE1  1 
ATOM   19911 H  HE3  . TRP   D  4  33  ? 5.650   -46.606 -43.440  1.00 78.94  ? 33   TRP   D HE3  1 
ATOM   19912 H  HZ2  . TRP   D  4  33  ? 5.317   -45.245 -38.965  1.00 83.16  ? 33   TRP   D HZ2  1 
ATOM   19913 H  HZ3  . TRP   D  4  33  ? 3.603   -46.521 -42.369  1.00 81.84  ? 33   TRP   D HZ3  1 
ATOM   19914 H  HH2  . TRP   D  4  33  ? 3.442   -45.849 -40.163  1.00 85.13  ? 33   TRP   D HH2  1 
ATOM   19915 N  N    . MET   D  4  34  ? 11.018  -47.788 -44.993  1.00 57.14  ? 34   MET   D N    1 
ATOM   19916 C  CA   . MET   D  4  34  ? 11.397  -48.458 -46.230  1.00 58.99  ? 34   MET   D CA   1 
ATOM   19917 C  C    . MET   D  4  34  ? 10.338  -49.502 -46.551  1.00 62.71  ? 34   MET   D C    1 
ATOM   19918 O  O    . MET   D  4  34  ? 10.042  -50.365 -45.718  1.00 64.27  ? 34   MET   D O    1 
ATOM   19919 C  CB   . MET   D  4  34  ? 12.775  -49.110 -46.110  1.00 57.23  ? 34   MET   D CB   1 
ATOM   19920 C  CG   . MET   D  4  34  ? 13.320  -49.632 -47.429  1.00 58.25  ? 34   MET   D CG   1 
ATOM   19921 S  SD   . MET   D  4  34  ? 13.699  -48.314 -48.600  1.00 60.42  ? 34   MET   D SD   1 
ATOM   19922 C  CE   . MET   D  4  34  ? 15.136  -47.579 -47.826  1.00 64.31  ? 34   MET   D CE   1 
ATOM   19923 H  H    . MET   D  4  34  ? 10.970  -48.318 -44.318  1.00 68.55  ? 34   MET   D H    1 
ATOM   19924 H  HA   . MET   D  4  34  ? 11.439  -47.806 -46.948  1.00 70.77  ? 34   MET   D HA   1 
ATOM   19925 H  HB2  . MET   D  4  34  ? 13.402  -48.453 -45.769  1.00 68.66  ? 34   MET   D HB2  1 
ATOM   19926 H  HB3  . MET   D  4  34  ? 12.713  -49.859 -45.497  1.00 68.66  ? 34   MET   D HB3  1 
ATOM   19927 H  HG2  . MET   D  4  34  ? 14.137  -50.127 -47.259  1.00 69.89  ? 34   MET   D HG2  1 
ATOM   19928 H  HG3  . MET   D  4  34  ? 12.659  -50.214 -47.835  1.00 69.89  ? 34   MET   D HG3  1 
ATOM   19929 H  HE1  . MET   D  4  34  ? 15.466  -46.861 -48.390  1.00 77.15  ? 34   MET   D HE1  1 
ATOM   19930 H  HE2  . MET   D  4  34  ? 14.883  -47.228 -46.958  1.00 77.15  ? 34   MET   D HE2  1 
ATOM   19931 H  HE3  . MET   D  4  34  ? 15.821  -48.258 -47.721  1.00 77.15  ? 34   MET   D HE3  1 
ATOM   19932 N  N    . HIS   D  4  35  ? 9.768   -49.416 -47.747  1.00 63.93  ? 35   HIS   D N    1 
ATOM   19933 C  CA   . HIS   D  4  35  ? 8.779   -50.371 -48.219  1.00 62.86  ? 35   HIS   D CA   1 
ATOM   19934 C  C    . HIS   D  4  35  ? 9.425   -51.370 -49.171  1.00 64.16  ? 35   HIS   D C    1 
ATOM   19935 O  O    . HIS   D  4  35  ? 10.476  -51.113 -49.763  1.00 68.54  ? 35   HIS   D O    1 
ATOM   19936 C  CB   . HIS   D  4  35  ? 7.623   -49.653 -48.919  1.00 59.73  ? 35   HIS   D CB   1 
ATOM   19937 C  CG   . HIS   D  4  35  ? 6.825   -48.771 -48.010  1.00 59.90  ? 35   HIS   D CG   1 
ATOM   19938 N  ND1  . HIS   D  4  35  ? 5.499   -49.006 -47.721  1.00 62.40  ? 35   HIS   D ND1  1 
ATOM   19939 C  CD2  . HIS   D  4  35  ? 7.170   -47.660 -47.318  1.00 61.74  ? 35   HIS   D CD2  1 
ATOM   19940 C  CE1  . HIS   D  4  35  ? 5.058   -48.074 -46.895  1.00 65.03  ? 35   HIS   D CE1  1 
ATOM   19941 N  NE2  . HIS   D  4  35  ? 6.052   -47.246 -46.634  1.00 62.79  ? 35   HIS   D NE2  1 
ATOM   19942 H  H    . HIS   D  4  35  ? 9.944   -48.797 -48.317  1.00 76.70  ? 35   HIS   D H    1 
ATOM   19943 H  HA   . HIS   D  4  35  ? 8.415   -50.859 -47.464  1.00 75.41  ? 35   HIS   D HA   1 
ATOM   19944 H  HB2  . HIS   D  4  35  ? 7.984   -49.098 -49.628  1.00 71.66  ? 35   HIS   D HB2  1 
ATOM   19945 H  HB3  . HIS   D  4  35  ? 7.022   -50.317 -49.290  1.00 71.66  ? 35   HIS   D HB3  1 
ATOM   19946 H  HD2  . HIS   D  4  35  ? 8.006   -47.253 -47.308  1.00 74.07  ? 35   HIS   D HD2  1 
ATOM   19947 H  HE1  . HIS   D  4  35  ? 4.194   -48.012 -46.556  1.00 78.01  ? 35   HIS   D HE1  1 
ATOM   19948 H  HE2  . HIS   D  4  35  ? 6.008   -46.558 -46.119  1.00 75.33  ? 35   HIS   D HE2  1 
ATOM   19949 N  N    . TRP   D  4  36  ? 8.780   -52.525 -49.306  1.00 61.73  ? 36   TRP   D N    1 
ATOM   19950 C  CA   . TRP   D  4  36  ? 9.220   -53.567 -50.221  1.00 58.42  ? 36   TRP   D CA   1 
ATOM   19951 C  C    . TRP   D  4  36  ? 8.047   -54.002 -51.085  1.00 59.60  ? 36   TRP   D C    1 
ATOM   19952 O  O    . TRP   D  4  36  ? 6.916   -54.111 -50.603  1.00 62.63  ? 36   TRP   D O    1 
ATOM   19953 C  CB   . TRP   D  4  36  ? 9.798   -54.767 -49.465  1.00 57.39  ? 36   TRP   D CB   1 
ATOM   19954 C  CG   . TRP   D  4  36  ? 11.106  -54.469 -48.793  1.00 55.31  ? 36   TRP   D CG   1 
ATOM   19955 C  CD1  . TRP   D  4  36  ? 11.286  -53.941 -47.546  1.00 54.35  ? 36   TRP   D CD1  1 
ATOM   19956 C  CD2  . TRP   D  4  36  ? 12.417  -54.679 -49.332  1.00 55.57  ? 36   TRP   D CD2  1 
ATOM   19957 N  NE1  . TRP   D  4  36  ? 12.627  -53.810 -47.276  1.00 55.51  ? 36   TRP   D NE1  1 
ATOM   19958 C  CE2  . TRP   D  4  36  ? 13.342  -54.257 -48.356  1.00 54.91  ? 36   TRP   D CE2  1 
ATOM   19959 C  CE3  . TRP   D  4  36  ? 12.898  -55.184 -50.544  1.00 59.81  ? 36   TRP   D CE3  1 
ATOM   19960 C  CZ2  . TRP   D  4  36  ? 14.719  -54.324 -48.555  1.00 54.72  ? 36   TRP   D CZ2  1 
ATOM   19961 C  CZ3  . TRP   D  4  36  ? 14.266  -55.249 -50.739  1.00 60.86  ? 36   TRP   D CZ3  1 
ATOM   19962 C  CH2  . TRP   D  4  36  ? 15.160  -54.821 -49.750  1.00 57.91  ? 36   TRP   D CH2  1 
ATOM   19963 H  H    . TRP   D  4  36  ? 8.069   -52.731 -48.867  1.00 74.06  ? 36   TRP   D H    1 
ATOM   19964 H  HA   . TRP   D  4  36  ? 9.914   -53.222 -50.804  1.00 70.08  ? 36   TRP   D HA   1 
ATOM   19965 H  HB2  . TRP   D  4  36  ? 9.167   -55.041 -48.781  1.00 68.85  ? 36   TRP   D HB2  1 
ATOM   19966 H  HB3  . TRP   D  4  36  ? 9.944   -55.493 -50.092  1.00 68.85  ? 36   TRP   D HB3  1 
ATOM   19967 H  HD1  . TRP   D  4  36  ? 10.601  -53.703 -46.965  1.00 65.20  ? 36   TRP   D HD1  1 
ATOM   19968 H  HE1  . TRP   D  4  36  ? 12.962  -53.499 -46.548  1.00 66.59  ? 36   TRP   D HE1  1 
ATOM   19969 H  HE3  . TRP   D  4  36  ? 12.311  -55.469 -51.205  1.00 71.75  ? 36   TRP   D HE3  1 
ATOM   19970 H  HZ2  . TRP   D  4  36  ? 15.316  -54.041 -47.900  1.00 65.65  ? 36   TRP   D HZ2  1 
ATOM   19971 H  HZ3  . TRP   D  4  36  ? 14.597  -55.583 -51.541  1.00 73.02  ? 36   TRP   D HZ3  1 
ATOM   19972 H  HH2  . TRP   D  4  36  ? 16.074  -54.877 -49.909  1.00 69.47  ? 36   TRP   D HH2  1 
ATOM   19973 N  N    . VAL   D  4  37  ? 8.324   -54.245 -52.364  1.00 60.25  ? 37   VAL   D N    1 
ATOM   19974 C  CA   . VAL   D  4  37  ? 7.302   -54.584 -53.345  1.00 62.94  ? 37   VAL   D CA   1 
ATOM   19975 C  C    . VAL   D  4  37  ? 7.771   -55.788 -54.146  1.00 61.24  ? 37   VAL   D C    1 
ATOM   19976 O  O    . VAL   D  4  37  ? 8.962   -55.920 -54.452  1.00 62.47  ? 37   VAL   D O    1 
ATOM   19977 C  CB   . VAL   D  4  37  ? 6.996   -53.393 -54.278  1.00 67.54  ? 37   VAL   D CB   1 
ATOM   19978 C  CG1  . VAL   D  4  37  ? 5.926   -53.764 -55.296  1.00 69.62  ? 37   VAL   D CG1  1 
ATOM   19979 C  CG2  . VAL   D  4  37  ? 6.564   -52.182 -53.463  1.00 66.92  ? 37   VAL   D CG2  1 
ATOM   19980 H  H    . VAL   D  4  37  ? 9.118   -54.219 -52.693  1.00 72.28  ? 37   VAL   D H    1 
ATOM   19981 H  HA   . VAL   D  4  37  ? 6.485   -54.829 -52.883  1.00 75.51  ? 37   VAL   D HA   1 
ATOM   19982 H  HB   . VAL   D  4  37  ? 7.802   -53.162 -54.766  1.00 81.03  ? 37   VAL   D HB   1 
ATOM   19983 H  HG11 . VAL   D  4  37  ? 5.709   -52.982 -55.827  1.00 83.52  ? 37   VAL   D HG11 1 
ATOM   19984 H  HG12 . VAL   D  4  37  ? 6.266   -54.468 -55.870  1.00 83.52  ? 37   VAL   D HG12 1 
ATOM   19985 H  HG13 . VAL   D  4  37  ? 5.136   -54.074 -54.825  1.00 83.52  ? 37   VAL   D HG13 1 
ATOM   19986 H  HG21 . VAL   D  4  37  ? 6.357   -51.452 -54.067  1.00 80.28  ? 37   VAL   D HG21 1 
ATOM   19987 H  HG22 . VAL   D  4  37  ? 5.779   -52.415 -52.944  1.00 80.28  ? 37   VAL   D HG22 1 
ATOM   19988 H  HG23 . VAL   D  4  37  ? 7.289   -51.925 -52.871  1.00 80.28  ? 37   VAL   D HG23 1 
ATOM   19989 N  N    . LYS   D  4  38  ? 6.830   -56.664 -54.485  1.00 63.08  ? 38   LYS   D N    1 
ATOM   19990 C  CA   . LYS   D  4  38  ? 7.088   -57.865 -55.267  1.00 64.89  ? 38   LYS   D CA   1 
ATOM   19991 C  C    . LYS   D  4  38  ? 6.398   -57.746 -56.619  1.00 67.72  ? 38   LYS   D C    1 
ATOM   19992 O  O    . LYS   D  4  38  ? 5.266   -57.259 -56.708  1.00 68.67  ? 38   LYS   D O    1 
ATOM   19993 C  CB   . LYS   D  4  38  ? 6.587   -59.109 -54.525  1.00 66.77  ? 38   LYS   D CB   1 
ATOM   19994 C  CG   . LYS   D  4  38  ? 6.677   -60.415 -55.305  1.00 70.18  ? 38   LYS   D CG   1 
ATOM   19995 C  CD   . LYS   D  4  38  ? 5.974   -61.532 -54.546  1.00 72.14  ? 38   LYS   D CD   1 
ATOM   19996 C  CE   . LYS   D  4  38  ? 6.027   -62.853 -55.294  1.00 75.67  ? 38   LYS   D CE   1 
ATOM   19997 N  NZ   . LYS   D  4  38  ? 5.250   -63.910 -54.590  1.00 81.57  ? 38   LYS   D NZ   1 
ATOM   19998 H  H    . LYS   D  4  38  ? 6.003   -56.580 -54.264  1.00 75.68  ? 38   LYS   D H    1 
ATOM   19999 H  HA   . LYS   D  4  38  ? 8.041   -57.966 -55.419  1.00 77.84  ? 38   LYS   D HA   1 
ATOM   20000 H  HB2  . LYS   D  4  38  ? 7.115   -59.217 -53.719  1.00 80.11  ? 38   LYS   D HB2  1 
ATOM   20001 H  HB3  . LYS   D  4  38  ? 5.655   -58.973 -54.296  1.00 80.11  ? 38   LYS   D HB3  1 
ATOM   20002 H  HG2  . LYS   D  4  38  ? 6.248   -60.309 -56.169  1.00 84.19  ? 38   LYS   D HG2  1 
ATOM   20003 H  HG3  . LYS   D  4  38  ? 7.608   -60.660 -55.425  1.00 84.19  ? 38   LYS   D HG3  1 
ATOM   20004 H  HD2  . LYS   D  4  38  ? 6.405   -61.654 -53.686  1.00 86.55  ? 38   LYS   D HD2  1 
ATOM   20005 H  HD3  . LYS   D  4  38  ? 5.042   -61.294 -54.419  1.00 86.55  ? 38   LYS   D HD3  1 
ATOM   20006 H  HE2  . LYS   D  4  38  ? 5.649   -62.736 -56.180  1.00 90.78  ? 38   LYS   D HE2  1 
ATOM   20007 H  HE3  . LYS   D  4  38  ? 6.949   -63.146 -55.363  1.00 90.78  ? 38   LYS   D HE3  1 
ATOM   20008 H  HZ1  . LYS   D  4  38  ? 5.394   -64.700 -54.973  1.00 97.86  ? 38   LYS   D HZ1  1 
ATOM   20009 H  HZ2  . LYS   D  4  38  ? 5.498   -63.953 -53.736  1.00 97.86  ? 38   LYS   D HZ2  1 
ATOM   20010 H  HZ3  . LYS   D  4  38  ? 4.380   -63.726 -54.629  1.00 97.86  ? 38   LYS   D HZ3  1 
ATOM   20011 N  N    . GLN   D  4  39  ? 7.085   -58.190 -57.671  1.00 68.54  ? 39   GLN   D N    1 
ATOM   20012 C  CA   . GLN   D  4  39  ? 6.542   -58.159 -59.027  1.00 69.69  ? 39   GLN   D CA   1 
ATOM   20013 C  C    . GLN   D  4  39  ? 6.961   -59.434 -59.744  1.00 72.67  ? 39   GLN   D C    1 
ATOM   20014 O  O    . GLN   D  4  39  ? 8.133   -59.591 -60.099  1.00 71.08  ? 39   GLN   D O    1 
ATOM   20015 C  CB   . GLN   D  4  39  ? 7.027   -56.926 -59.789  1.00 68.84  ? 39   GLN   D CB   1 
ATOM   20016 C  CG   . GLN   D  4  39  ? 6.471   -56.818 -61.201  1.00 71.77  ? 39   GLN   D CG   1 
ATOM   20017 C  CD   . GLN   D  4  39  ? 6.873   -55.532 -61.895  1.00 69.07  ? 39   GLN   D CD   1 
ATOM   20018 O  OE1  . GLN   D  4  39  ? 7.946   -54.984 -61.641  1.00 67.62  ? 39   GLN   D OE1  1 
ATOM   20019 N  NE2  . GLN   D  4  39  ? 6.010   -55.043 -62.777  1.00 67.46  ? 39   GLN   D NE2  1 
ATOM   20020 H  H    . GLN   D  4  39  ? 7.879   -58.519 -57.623  1.00 82.23  ? 39   GLN   D H    1 
ATOM   20021 H  HA   . GLN   D  4  39  ? 5.574   -58.137 -58.981  1.00 83.61  ? 39   GLN   D HA   1 
ATOM   20022 H  HB2  . GLN   D  4  39  ? 6.756   -56.132 -59.303  1.00 82.59  ? 39   GLN   D HB2  1 
ATOM   20023 H  HB3  . GLN   D  4  39  ? 7.995   -56.960 -59.855  1.00 82.59  ? 39   GLN   D HB3  1 
ATOM   20024 H  HG2  . GLN   D  4  39  ? 6.803   -57.561 -61.729  1.00 86.10  ? 39   GLN   D HG2  1 
ATOM   20025 H  HG3  . GLN   D  4  39  ? 5.502   -56.846 -61.161  1.00 86.10  ? 39   GLN   D HG3  1 
ATOM   20026 H  HE21 . GLN   D  4  39  ? 5.270   -55.454 -62.928  1.00 80.94  ? 39   GLN   D HE21 1 
ATOM   20027 H  HE22 . GLN   D  4  39  ? 6.192   -54.316 -63.198  1.00 80.94  ? 39   GLN   D HE22 1 
ATOM   20028 N  N    . ARG   D  4  40  ? 6.009   -60.338 -59.967  1.00 79.52  ? 40   ARG   D N    1 
ATOM   20029 C  CA   . ARG   D  4  40  ? 6.313   -61.553 -60.702  1.00 88.89  ? 40   ARG   D CA   1 
ATOM   20030 C  C    . ARG   D  4  40  ? 6.519   -61.233 -62.182  1.00 92.61  ? 40   ARG   D C    1 
ATOM   20031 O  O    . ARG   D  4  40  ? 5.974   -60.252 -62.695  1.00 93.10  ? 40   ARG   D O    1 
ATOM   20032 C  CB   . ARG   D  4  40  ? 5.193   -62.577 -60.552  1.00 96.82  ? 40   ARG   D CB   1 
ATOM   20033 C  CG   . ARG   D  4  40  ? 5.282   -63.433 -59.304  1.00 103.33 ? 40   ARG   D CG   1 
ATOM   20034 C  CD   . ARG   D  4  40  ? 4.545   -64.748 -59.498  1.00 116.89 ? 40   ARG   D CD   1 
ATOM   20035 N  NE   . ARG   D  4  40  ? 4.049   -65.287 -58.236  1.00 125.81 ? 40   ARG   D NE   1 
ATOM   20036 C  CZ   . ARG   D  4  40  ? 2.872   -64.978 -57.698  1.00 132.98 ? 40   ARG   D CZ   1 
ATOM   20037 N  NH1  . ARG   D  4  40  ? 2.054   -64.129 -58.309  1.00 132.92 ? 40   ARG   D NH1  1 
ATOM   20038 N  NH2  . ARG   D  4  40  ? 2.511   -65.521 -56.544  1.00 138.71 ? 40   ARG   D NH2  1 
ATOM   20039 H  H    . ARG   D  4  40  ? 5.193   -60.269 -59.705  1.00 95.41  ? 40   ARG   D H    1 
ATOM   20040 H  HA   . ARG   D  4  40  ? 7.127   -61.946 -60.349  1.00 106.65 ? 40   ARG   D HA   1 
ATOM   20041 H  HB2  . ARG   D  4  40  ? 4.345   -62.105 -60.523  1.00 116.17 ? 40   ARG   D HB2  1 
ATOM   20042 H  HB3  . ARG   D  4  40  ? 5.215   -63.172 -61.317  1.00 116.17 ? 40   ARG   D HB3  1 
ATOM   20043 H  HG2  . ARG   D  4  40  ? 6.213   -63.627 -59.110  1.00 123.98 ? 40   ARG   D HG2  1 
ATOM   20044 H  HG3  . ARG   D  4  40  ? 4.879   -62.962 -58.558  1.00 123.98 ? 40   ARG   D HG3  1 
ATOM   20045 H  HD2  . ARG   D  4  40  ? 3.787   -64.606 -60.086  1.00 140.25 ? 40   ARG   D HD2  1 
ATOM   20046 H  HD3  . ARG   D  4  40  ? 5.150   -65.399 -59.888  1.00 140.25 ? 40   ARG   D HD3  1 
ATOM   20047 H  HE   . ARG   D  4  40  ? 4.551   -65.841 -57.811  1.00 150.95 ? 40   ARG   D HE   1 
ATOM   20048 H  HH11 . ARG   D  4  40  ? 2.284   -63.774 -59.057  1.00 159.49 ? 40   ARG   D HH11 1 
ATOM   20049 H  HH12 . ARG   D  4  40  ? 1.295   -63.934 -57.955  1.00 159.49 ? 40   ARG   D HH12 1 
ATOM   20050 H  HH21 . ARG   D  4  40  ? 3.038   -66.072 -56.145  1.00 166.44 ? 40   ARG   D HH21 1 
ATOM   20051 H  HH22 . ARG   D  4  40  ? 1.751   -65.323 -56.195  1.00 166.44 ? 40   ARG   D HH22 1 
ATOM   20052 N  N    . PRO   D  4  41  ? 7.305   -62.048 -62.892  1.00 95.61  ? 41   PRO   D N    1 
ATOM   20053 C  CA   . PRO   D  4  41  ? 7.511   -61.803 -64.327  1.00 98.19  ? 41   PRO   D CA   1 
ATOM   20054 C  C    . PRO   D  4  41  ? 6.206   -61.638 -65.088  1.00 102.89 ? 41   PRO   D C    1 
ATOM   20055 O  O    . PRO   D  4  41  ? 5.345   -62.524 -65.064  1.00 102.93 ? 41   PRO   D O    1 
ATOM   20056 C  CB   . PRO   D  4  41  ? 8.277   -63.050 -64.786  1.00 102.50 ? 41   PRO   D CB   1 
ATOM   20057 C  CG   . PRO   D  4  41  ? 8.989   -63.519 -63.566  1.00 101.25 ? 41   PRO   D CG   1 
ATOM   20058 C  CD   . PRO   D  4  41  ? 8.078   -63.207 -62.412  1.00 97.11  ? 41   PRO   D CD   1 
ATOM   20059 H  HA   . PRO   D  4  41  ? 8.061   -61.016 -64.460  1.00 117.81 ? 41   PRO   D HA   1 
ATOM   20060 H  HB2  . PRO   D  4  41  ? 7.656   -63.723 -65.107  1.00 122.98 ? 41   PRO   D HB2  1 
ATOM   20061 H  HB3  . PRO   D  4  41  ? 8.904   -62.816 -65.488  1.00 122.98 ? 41   PRO   D HB3  1 
ATOM   20062 H  HG2  . PRO   D  4  41  ? 9.151   -64.473 -63.628  1.00 121.48 ? 41   PRO   D HG2  1 
ATOM   20063 H  HG3  . PRO   D  4  41  ? 9.831   -63.045 -63.476  1.00 121.48 ? 41   PRO   D HG3  1 
ATOM   20064 H  HD2  . PRO   D  4  41  ? 7.493   -63.958 -62.222  1.00 116.51 ? 41   PRO   D HD2  1 
ATOM   20065 H  HD3  . PRO   D  4  41  ? 8.590   -62.977 -61.620  1.00 116.51 ? 41   PRO   D HD3  1 
ATOM   20066 N  N    . GLY   D  4  42  ? 6.050   -60.501 -65.763  1.00 108.11 ? 42   GLY   D N    1 
ATOM   20067 C  CA   . GLY   D  4  42  ? 4.848   -60.235 -66.527  1.00 114.17 ? 42   GLY   D CA   1 
ATOM   20068 C  C    . GLY   D  4  42  ? 3.613   -59.952 -65.705  1.00 112.68 ? 42   GLY   D C    1 
ATOM   20069 O  O    . GLY   D  4  42  ? 2.523   -59.840 -66.275  1.00 112.67 ? 42   GLY   D O    1 
ATOM   20070 H  H    . GLY   D  4  42  ? 6.631   -59.868 -65.791  1.00 129.71 ? 42   GLY   D H    1 
ATOM   20071 H  HA2  . GLY   D  4  42  ? 5.007   -59.465 -67.094  1.00 136.98 ? 42   GLY   D HA2  1 
ATOM   20072 H  HA3  . GLY   D  4  42  ? 4.660   -61.005 -67.085  1.00 136.98 ? 42   GLY   D HA3  1 
ATOM   20073 N  N    . GLN   D  4  43  ? 3.744   -59.828 -64.389  1.00 109.19 ? 43   GLN   D N    1 
ATOM   20074 C  CA   . GLN   D  4  43  ? 2.625   -59.588 -63.490  1.00 105.09 ? 43   GLN   D CA   1 
ATOM   20075 C  C    . GLN   D  4  43  ? 2.687   -58.162 -62.947  1.00 100.33 ? 43   GLN   D C    1 
ATOM   20076 O  O    . GLN   D  4  43  ? 3.546   -57.360 -63.323  1.00 96.18  ? 43   GLN   D O    1 
ATOM   20077 C  CB   . GLN   D  4  43  ? 2.628   -60.615 -62.355  1.00 101.77 ? 43   GLN   D CB   1 
ATOM   20078 C  CG   . GLN   D  4  43  ? 2.191   -62.007 -62.789  1.00 102.59 ? 43   GLN   D CG   1 
ATOM   20079 C  CD   . GLN   D  4  43  ? 0.759   -62.038 -63.297  1.00 103.47 ? 43   GLN   D CD   1 
ATOM   20080 O  OE1  . GLN   D  4  43  ? 0.473   -62.607 -64.350  1.00 108.73 ? 43   GLN   D OE1  1 
ATOM   20081 N  NE2  . GLN   D  4  43  ? -0.149  -61.425 -62.545  1.00 101.09 ? 43   GLN   D NE2  1 
ATOM   20082 H  H    . GLN   D  4  43  ? 4.499   -59.881 -63.981  1.00 131.00 ? 43   GLN   D H    1 
ATOM   20083 H  HA   . GLN   D  4  43  ? 1.797   -59.682 -63.986  1.00 126.08 ? 43   GLN   D HA   1 
ATOM   20084 H  HB2  . GLN   D  4  43  ? 3.527   -60.684 -61.999  1.00 122.11 ? 43   GLN   D HB2  1 
ATOM   20085 H  HB3  . GLN   D  4  43  ? 2.018   -60.316 -61.662  1.00 122.11 ? 43   GLN   D HB3  1 
ATOM   20086 H  HG2  . GLN   D  4  43  ? 2.770   -62.312 -63.505  1.00 123.09 ? 43   GLN   D HG2  1 
ATOM   20087 H  HG3  . GLN   D  4  43  ? 2.254   -62.610 -62.032  1.00 123.09 ? 43   GLN   D HG3  1 
ATOM   20088 H  HE21 . GLN   D  4  43  ? 0.088   -61.039 -61.814  1.00 121.29 ? 43   GLN   D HE21 1 
ATOM   20089 H  HE22 . GLN   D  4  43  ? -0.973  -61.415 -62.789  1.00 121.29 ? 43   GLN   D HE22 1 
ATOM   20090 N  N    . GLY   D  4  44  ? 1.753   -57.851 -62.053  1.00 98.88  ? 44   GLY   D N    1 
ATOM   20091 C  CA   . GLY   D  4  44  ? 1.660   -56.540 -61.449  1.00 90.59  ? 44   GLY   D CA   1 
ATOM   20092 C  C    . GLY   D  4  44  ? 2.512   -56.417 -60.204  1.00 80.24  ? 44   GLY   D C    1 
ATOM   20093 O  O    . GLY   D  4  44  ? 3.414   -57.219 -59.948  1.00 81.15  ? 44   GLY   D O    1 
ATOM   20094 H  H    . GLY   D  4  44  ? 1.151   -58.400 -61.778  1.00 118.64 ? 44   GLY   D H    1 
ATOM   20095 H  HA2  . GLY   D  4  44  ? 1.953   -55.871 -62.087  1.00 108.69 ? 44   GLY   D HA2  1 
ATOM   20096 H  HA3  . GLY   D  4  44  ? 0.738   -56.363 -61.207  1.00 108.69 ? 44   GLY   D HA3  1 
ATOM   20097 N  N    . LEU   D  4  45  ? 2.209   -55.392 -59.414  1.00 70.63  ? 45   LEU   D N    1 
ATOM   20098 C  CA   . LEU   D  4  45  ? 2.970   -55.069 -58.216  1.00 66.41  ? 45   LEU   D CA   1 
ATOM   20099 C  C    . LEU   D  4  45  ? 2.227   -55.541 -56.974  1.00 66.96  ? 45   LEU   D C    1 
ATOM   20100 O  O    . LEU   D  4  45  ? 1.008   -55.383 -56.866  1.00 66.44  ? 45   LEU   D O    1 
ATOM   20101 C  CB   . LEU   D  4  45  ? 3.228   -53.564 -58.135  1.00 62.20  ? 45   LEU   D CB   1 
ATOM   20102 C  CG   . LEU   D  4  45  ? 3.981   -52.981 -59.333  1.00 61.73  ? 45   LEU   D CG   1 
ATOM   20103 C  CD1  . LEU   D  4  45  ? 4.049   -51.467 -59.240  1.00 58.74  ? 45   LEU   D CD1  1 
ATOM   20104 C  CD2  . LEU   D  4  45  ? 5.378   -53.574 -59.429  1.00 60.62  ? 45   LEU   D CD2  1 
ATOM   20105 H  H    . LEU   D  4  45  ? 1.551   -54.857 -59.556  1.00 84.73  ? 45   LEU   D H    1 
ATOM   20106 H  HA   . LEU   D  4  45  ? 3.825   -55.526 -58.243  1.00 79.67  ? 45   LEU   D HA   1 
ATOM   20107 H  HB2  . LEU   D  4  45  ? 2.373   -53.108 -58.076  1.00 74.62  ? 45   LEU   D HB2  1 
ATOM   20108 H  HB3  . LEU   D  4  45  ? 3.755   -53.384 -57.341  1.00 74.62  ? 45   LEU   D HB3  1 
ATOM   20109 H  HG   . LEU   D  4  45  ? 3.501   -53.210 -60.144  1.00 74.06  ? 45   LEU   D HG   1 
ATOM   20110 H  HD11 . LEU   D  4  45  ? 4.531   -51.125 -60.009  1.00 70.47  ? 45   LEU   D HD11 1 
ATOM   20111 H  HD12 . LEU   D  4  45  ? 3.146   -51.111 -59.231  1.00 70.47  ? 45   LEU   D HD12 1 
ATOM   20112 H  HD13 . LEU   D  4  45  ? 4.510   -51.221 -58.424  1.00 70.47  ? 45   LEU   D HD13 1 
ATOM   20113 H  HD21 . LEU   D  4  45  ? 5.853   -53.147 -60.159  1.00 72.73  ? 45   LEU   D HD21 1 
ATOM   20114 H  HD22 . LEU   D  4  45  ? 5.846   -53.417 -58.594  1.00 72.73  ? 45   LEU   D HD22 1 
ATOM   20115 H  HD23 . LEU   D  4  45  ? 5.306   -54.527 -59.594  1.00 72.73  ? 45   LEU   D HD23 1 
ATOM   20116 N  N    . GLU   D  4  46  ? 2.976   -56.119 -56.037  1.00 67.36  ? 46   GLU   D N    1 
ATOM   20117 C  CA   . GLU   D  4  46  ? 2.426   -56.667 -54.804  1.00 69.90  ? 46   GLU   D CA   1 
ATOM   20118 C  C    . GLU   D  4  46  ? 3.196   -56.084 -53.628  1.00 69.20  ? 46   GLU   D C    1 
ATOM   20119 O  O    . GLU   D  4  46  ? 4.429   -56.157 -53.591  1.00 66.73  ? 46   GLU   D O    1 
ATOM   20120 C  CB   . GLU   D  4  46  ? 2.507   -58.197 -54.800  1.00 72.74  ? 46   GLU   D CB   1 
ATOM   20121 C  CG   . GLU   D  4  46  ? 1.431   -58.875 -53.966  1.00 82.62  ? 46   GLU   D CG   1 
ATOM   20122 C  CD   . GLU   D  4  46  ? 1.357   -60.367 -54.218  1.00 93.51  ? 46   GLU   D CD   1 
ATOM   20123 O  OE1  . GLU   D  4  46  ? 2.347   -60.936 -54.724  1.00 97.25  ? 46   GLU   D OE1  1 
ATOM   20124 O  OE2  . GLU   D  4  46  ? 0.304   -60.970 -53.918  1.00 99.52  ? 46   GLU   D OE2  1 
ATOM   20125 H  H    . GLU   D  4  46  ? 3.829   -56.208 -56.096  1.00 80.82  ? 46   GLU   D H    1 
ATOM   20126 H  HA   . GLU   D  4  46  ? 1.494   -56.415 -54.712  1.00 83.86  ? 46   GLU   D HA   1 
ATOM   20127 H  HB2  . GLU   D  4  46  ? 2.417   -58.514 -55.712  1.00 87.27  ? 46   GLU   D HB2  1 
ATOM   20128 H  HB3  . GLU   D  4  46  ? 3.368   -58.461 -54.440  1.00 87.27  ? 46   GLU   D HB3  1 
ATOM   20129 H  HG2  . GLU   D  4  46  ? 1.626   -58.738 -53.026  1.00 99.13  ? 46   GLU   D HG2  1 
ATOM   20130 H  HG3  . GLU   D  4  46  ? 0.569   -58.489 -54.187  1.00 99.13  ? 46   GLU   D HG3  1 
ATOM   20131 N  N    . TRP   D  4  47  ? 2.468   -55.507 -52.677  1.00 67.82  ? 47   TRP   D N    1 
ATOM   20132 C  CA   . TRP   D  4  47  ? 3.064   -54.826 -51.534  1.00 65.60  ? 47   TRP   D CA   1 
ATOM   20133 C  C    . TRP   D  4  47  ? 3.327   -55.832 -50.419  1.00 66.89  ? 47   TRP   D C    1 
ATOM   20134 O  O    . TRP   D  4  47  ? 2.408   -56.527 -49.972  1.00 72.20  ? 47   TRP   D O    1 
ATOM   20135 C  CB   . TRP   D  4  47  ? 2.141   -53.710 -51.049  1.00 67.78  ? 47   TRP   D CB   1 
ATOM   20136 C  CG   . TRP   D  4  47  ? 2.683   -52.915 -49.908  1.00 66.71  ? 47   TRP   D CG   1 
ATOM   20137 C  CD1  . TRP   D  4  47  ? 3.583   -51.894 -49.976  1.00 64.40  ? 47   TRP   D CD1  1 
ATOM   20138 C  CD2  . TRP   D  4  47  ? 2.345   -53.061 -48.523  1.00 67.92  ? 47   TRP   D CD2  1 
ATOM   20139 N  NE1  . TRP   D  4  47  ? 3.833   -51.400 -48.720  1.00 63.66  ? 47   TRP   D NE1  1 
ATOM   20140 C  CE2  . TRP   D  4  47  ? 3.085   -52.099 -47.810  1.00 65.13  ? 47   TRP   D CE2  1 
ATOM   20141 C  CE3  . TRP   D  4  47  ? 1.491   -53.915 -47.819  1.00 69.10  ? 47   TRP   D CE3  1 
ATOM   20142 C  CZ2  . TRP   D  4  47  ? 2.997   -51.965 -46.425  1.00 65.29  ? 47   TRP   D CZ2  1 
ATOM   20143 C  CZ3  . TRP   D  4  47  ? 1.406   -53.783 -46.444  1.00 69.40  ? 47   TRP   D CZ3  1 
ATOM   20144 C  CH2  . TRP   D  4  47  ? 2.153   -52.814 -45.762  1.00 67.05  ? 47   TRP   D CH2  1 
ATOM   20145 H  H    . TRP   D  4  47  ? 1.608   -55.496 -52.671  1.00 81.37  ? 47   TRP   D H    1 
ATOM   20146 H  HA   . TRP   D  4  47  ? 3.914   -54.438 -51.793  1.00 78.70  ? 47   TRP   D HA   1 
ATOM   20147 H  HB2  . TRP   D  4  47  ? 1.984   -53.097 -51.784  1.00 81.31  ? 47   TRP   D HB2  1 
ATOM   20148 H  HB3  . TRP   D  4  47  ? 1.303   -54.104 -50.760  1.00 81.31  ? 47   TRP   D HB3  1 
ATOM   20149 H  HD1  . TRP   D  4  47  ? 3.972   -51.579 -50.759  1.00 77.26  ? 47   TRP   D HD1  1 
ATOM   20150 H  HE1  . TRP   D  4  47  ? 4.371   -50.756 -48.534  1.00 76.38  ? 47   TRP   D HE1  1 
ATOM   20151 H  HE3  . TRP   D  4  47  ? 0.989   -54.559 -48.265  1.00 82.90  ? 47   TRP   D HE3  1 
ATOM   20152 H  HZ2  . TRP   D  4  47  ? 3.492   -51.324 -45.970  1.00 78.33  ? 47   TRP   D HZ2  1 
ATOM   20153 H  HZ3  . TRP   D  4  47  ? 0.843   -54.348 -45.965  1.00 83.26  ? 47   TRP   D HZ3  1 
ATOM   20154 H  HH2  . TRP   D  4  47  ? 2.074   -52.747 -44.838  1.00 80.44  ? 47   TRP   D HH2  1 
ATOM   20155 N  N    . ILE   D  4  48  ? 4.579   -55.900 -49.968  1.00 65.29  ? 48   ILE   D N    1 
ATOM   20156 C  CA   . ILE   D  4  48  ? 4.983   -56.845 -48.934  1.00 65.91  ? 48   ILE   D CA   1 
ATOM   20157 C  C    . ILE   D  4  48  ? 4.796   -56.213 -47.561  1.00 67.08  ? 48   ILE   D C    1 
ATOM   20158 O  O    . ILE   D  4  48  ? 4.097   -56.764 -46.704  1.00 66.38  ? 48   ILE   D O    1 
ATOM   20159 C  CB   . ILE   D  4  48  ? 6.441   -57.297 -49.140  1.00 61.40  ? 48   ILE   D CB   1 
ATOM   20160 C  CG1  . ILE   D  4  48  ? 6.616   -57.882 -50.545  1.00 60.21  ? 48   ILE   D CG1  1 
ATOM   20161 C  CG2  . ILE   D  4  48  ? 6.836   -58.326 -48.085  1.00 63.21  ? 48   ILE   D CG2  1 
ATOM   20162 C  CD1  . ILE   D  4  48  ? 8.041   -58.248 -50.890  1.00 59.25  ? 48   ILE   D CD1  1 
ATOM   20163 H  H    . ILE   D  4  48  ? 5.220   -55.401 -50.251  1.00 78.33  ? 48   ILE   D H    1 
ATOM   20164 H  HA   . ILE   D  4  48  ? 4.409   -57.625 -48.983  1.00 79.07  ? 48   ILE   D HA   1 
ATOM   20165 H  HB   . ILE   D  4  48  ? 7.018   -56.524 -49.047  1.00 73.66  ? 48   ILE   D HB   1 
ATOM   20166 H  HG12 . ILE   D  4  48  ? 6.080   -58.688 -50.615  1.00 72.23  ? 48   ILE   D HG12 1 
ATOM   20167 H  HG13 . ILE   D  4  48  ? 6.315   -57.226 -51.194  1.00 72.23  ? 48   ILE   D HG13 1 
ATOM   20168 H  HG21 . ILE   D  4  48  ? 7.761   -58.583 -48.226  1.00 75.83  ? 48   ILE   D HG21 1 
ATOM   20169 H  HG22 . ILE   D  4  48  ? 6.734   -57.931 -47.205  1.00 75.83  ? 48   ILE   D HG22 1 
ATOM   20170 H  HG23 . ILE   D  4  48  ? 6.260   -59.102 -48.169  1.00 75.83  ? 48   ILE   D HG23 1 
ATOM   20171 H  HD11 . ILE   D  4  48  ? 8.082   -58.514 -51.822  1.00 71.08  ? 48   ILE   D HD11 1 
ATOM   20172 H  HD12 . ILE   D  4  48  ? 8.610   -57.477 -50.740  1.00 71.08  ? 48   ILE   D HD12 1 
ATOM   20173 H  HD13 . ILE   D  4  48  ? 8.324   -58.983 -50.324  1.00 71.08  ? 48   ILE   D HD13 1 
ATOM   20174 N  N    . GLY   D  4  49  ? 5.415   -55.059 -47.340  1.00 68.79  ? 49   GLY   D N    1 
ATOM   20175 C  CA   . GLY   D  4  49  ? 5.348   -54.417 -46.044  1.00 70.66  ? 49   GLY   D CA   1 
ATOM   20176 C  C    . GLY   D  4  49  ? 6.300   -53.239 -45.980  1.00 68.24  ? 49   GLY   D C    1 
ATOM   20177 O  O    . GLY   D  4  49  ? 6.866   -52.817 -46.991  1.00 66.37  ? 49   GLY   D O    1 
ATOM   20178 H  H    . GLY   D  4  49  ? 5.878   -54.632 -47.926  1.00 82.53  ? 49   GLY   D H    1 
ATOM   20179 H  HA2  . GLY   D  4  49  ? 4.446   -54.098 -45.882  1.00 84.77  ? 49   GLY   D HA2  1 
ATOM   20180 H  HA3  . GLY   D  4  49  ? 5.588   -55.051 -45.351  1.00 84.77  ? 49   GLY   D HA3  1 
ATOM   20181 N  N    . TYR   D  4  50  ? 6.465   -52.717 -44.765  1.00 66.98  ? 50   TYR   D N    1 
ATOM   20182 C  CA   . TYR   D  4  50  ? 7.402   -51.633 -44.512  1.00 64.32  ? 50   TYR   D CA   1 
ATOM   20183 C  C    . TYR   D  4  50  ? 8.122   -51.897 -43.198  1.00 63.56  ? 50   TYR   D C    1 
ATOM   20184 O  O    . TYR   D  4  50  ? 7.713   -52.740 -42.396  1.00 64.75  ? 50   TYR   D O    1 
ATOM   20185 C  CB   . TYR   D  4  50  ? 6.702   -50.265 -44.469  1.00 65.70  ? 50   TYR   D CB   1 
ATOM   20186 C  CG   . TYR   D  4  50  ? 6.040   -49.943 -43.143  1.00 68.10  ? 50   TYR   D CG   1 
ATOM   20187 C  CD1  . TYR   D  4  50  ? 6.771   -49.404 -42.090  1.00 66.37  ? 50   TYR   D CD1  1 
ATOM   20188 C  CD2  . TYR   D  4  50  ? 4.684   -50.166 -42.949  1.00 72.52  ? 50   TYR   D CD2  1 
ATOM   20189 C  CE1  . TYR   D  4  50  ? 6.174   -49.111 -40.880  1.00 69.80  ? 50   TYR   D CE1  1 
ATOM   20190 C  CE2  . TYR   D  4  50  ? 4.078   -49.869 -41.743  1.00 75.44  ? 50   TYR   D CE2  1 
ATOM   20191 C  CZ   . TYR   D  4  50  ? 4.828   -49.344 -40.713  1.00 72.98  ? 50   TYR   D CZ   1 
ATOM   20192 O  OH   . TYR   D  4  50  ? 4.230   -49.048 -39.510  1.00 76.06  ? 50   TYR   D OH   1 
ATOM   20193 H  H    . TYR   D  4  50  ? 6.038   -52.979 -44.066  1.00 80.36  ? 50   TYR   D H    1 
ATOM   20194 H  HA   . TYR   D  4  50  ? 8.057   -51.614 -45.227  1.00 77.17  ? 50   TYR   D HA   1 
ATOM   20195 H  HB2  . TYR   D  4  50  ? 7.360   -49.574 -44.644  1.00 78.82  ? 50   TYR   D HB2  1 
ATOM   20196 H  HB3  . TYR   D  4  50  ? 6.013   -50.248 -45.152  1.00 78.82  ? 50   TYR   D HB3  1 
ATOM   20197 H  HD1  . TYR   D  4  50  ? 7.679   -49.237 -42.202  1.00 79.63  ? 50   TYR   D HD1  1 
ATOM   20198 H  HD2  . TYR   D  4  50  ? 4.176   -50.522 -43.641  1.00 87.01  ? 50   TYR   D HD2  1 
ATOM   20199 H  HE1  . TYR   D  4  50  ? 6.678   -48.758 -40.183  1.00 83.74  ? 50   TYR   D HE1  1 
ATOM   20200 H  HE2  . TYR   D  4  50  ? 3.168   -50.022 -41.627  1.00 90.51  ? 50   TYR   D HE2  1 
ATOM   20201 H  HH   . TYR   D  4  50  ? 3.462   -49.388 -39.480  1.00 91.26  ? 50   TYR   D HH   1 
ATOM   20202 N  N    . ILE   D  4  51  ? 9.200   -51.149 -42.977  1.00 64.76  ? 51   ILE   D N    1 
ATOM   20203 C  CA   . ILE   D  4  51  ? 9.975   -51.228 -41.745  1.00 63.16  ? 51   ILE   D CA   1 
ATOM   20204 C  C    . ILE   D  4  51  ? 10.363  -49.819 -41.323  1.00 62.79  ? 51   ILE   D C    1 
ATOM   20205 O  O    . ILE   D  4  51  ? 10.726  -48.986 -42.160  1.00 62.01  ? 51   ILE   D O    1 
ATOM   20206 C  CB   . ILE   D  4  51  ? 11.232  -52.106 -41.914  1.00 59.57  ? 51   ILE   D CB   1 
ATOM   20207 C  CG1  . ILE   D  4  51  ? 12.086  -52.059 -40.643  1.00 61.11  ? 51   ILE   D CG1  1 
ATOM   20208 C  CG2  . ILE   D  4  51  ? 12.044  -51.645 -43.118  1.00 59.17  ? 51   ILE   D CG2  1 
ATOM   20209 C  CD1  . ILE   D  4  51  ? 13.208  -53.074 -40.618  1.00 61.50  ? 51   ILE   D CD1  1 
ATOM   20210 H  H    . ILE   D  4  51  ? 9.509   -50.576 -43.540  1.00 77.69  ? 51   ILE   D H    1 
ATOM   20211 H  HA   . ILE   D  4  51  ? 9.421   -51.617 -41.050  1.00 75.78  ? 51   ILE   D HA   1 
ATOM   20212 H  HB   . ILE   D  4  51  ? 10.950  -53.022 -42.063  1.00 71.47  ? 51   ILE   D HB   1 
ATOM   20213 H  HG12 . ILE   D  4  51  ? 12.484  -51.178 -40.567  1.00 73.31  ? 51   ILE   D HG12 1 
ATOM   20214 H  HG13 . ILE   D  4  51  ? 11.515  -52.232 -39.878  1.00 73.31  ? 51   ILE   D HG13 1 
ATOM   20215 H  HG21 . ILE   D  4  51  ? 12.813  -52.226 -43.222  1.00 70.98  ? 51   ILE   D HG21 1 
ATOM   20216 H  HG22 . ILE   D  4  51  ? 11.486  -51.689 -43.911  1.00 70.98  ? 51   ILE   D HG22 1 
ATOM   20217 H  HG23 . ILE   D  4  51  ? 12.336  -50.732 -42.971  1.00 70.98  ? 51   ILE   D HG23 1 
ATOM   20218 H  HD11 . ILE   D  4  51  ? 13.655  -53.030 -39.758  1.00 73.78  ? 51   ILE   D HD11 1 
ATOM   20219 H  HD12 . ILE   D  4  51  ? 12.836  -53.960 -40.753  1.00 73.78  ? 51   ILE   D HD12 1 
ATOM   20220 H  HD13 . ILE   D  4  51  ? 13.836  -52.868 -41.328  1.00 73.78  ? 51   ILE   D HD13 1 
ATOM   20221 N  N    . ASN   D  4  52  ? 10.277  -49.552 -40.022  1.00 62.32  ? 52   ASN   D N    1 
ATOM   20222 C  CA   . ASN   D  4  52  ? 10.819  -48.329 -39.444  1.00 62.75  ? 52   ASN   D CA   1 
ATOM   20223 C  C    . ASN   D  4  52  ? 12.295  -48.571 -39.147  1.00 64.68  ? 52   ASN   D C    1 
ATOM   20224 O  O    . ASN   D  4  52  ? 12.621  -49.255 -38.167  1.00 68.95  ? 52   ASN   D O    1 
ATOM   20225 C  CB   . ASN   D  4  52  ? 10.055  -47.938 -38.178  1.00 66.46  ? 52   ASN   D CB   1 
ATOM   20226 C  CG   . ASN   D  4  52  ? 10.526  -46.619 -37.592  1.00 72.45  ? 52   ASN   D CG   1 
ATOM   20227 O  OD1  . ASN   D  4  52  ? 11.704  -46.272 -37.674  1.00 74.33  ? 52   ASN   D OD1  1 
ATOM   20228 N  ND2  . ASN   D  4  52  ? 9.601   -45.875 -36.996  1.00 77.60  ? 52   ASN   D ND2  1 
ATOM   20229 H  H    . ASN   D  4  52  ? 9.905   -50.072 -39.446  1.00 74.77  ? 52   ASN   D H    1 
ATOM   20230 H  HA   . ASN   D  4  52  ? 10.733  -47.586 -40.062  1.00 75.28  ? 52   ASN   D HA   1 
ATOM   20231 H  HB2  . ASN   D  4  52  ? 9.112   -47.853 -38.392  1.00 79.73  ? 52   ASN   D HB2  1 
ATOM   20232 H  HB3  . ASN   D  4  52  ? 10.181  -48.627 -37.507  1.00 79.73  ? 52   ASN   D HB3  1 
ATOM   20233 H  HD21 . ASN   D  4  52  ? 9.817   -45.119 -36.648  1.00 93.10  ? 52   ASN   D HD21 1 
ATOM   20234 H  HD22 . ASN   D  4  52  ? 8.787   -46.150 -36.958  1.00 93.10  ? 52   ASN   D HD22 1 
ATOM   20235 N  N    . PRO   D  4  53  ? 13.217  -48.037 -39.957  1.00 64.47  ? 53   PRO   D N    1 
ATOM   20236 C  CA   . PRO   D  4  53  ? 14.625  -48.444 -39.808  1.00 63.22  ? 53   PRO   D CA   1 
ATOM   20237 C  C    . PRO   D  4  53  ? 15.199  -48.160 -38.432  1.00 61.10  ? 53   PRO   D C    1 
ATOM   20238 O  O    . PRO   D  4  53  ? 15.967  -48.974 -37.906  1.00 62.11  ? 53   PRO   D O    1 
ATOM   20239 C  CB   . PRO   D  4  53  ? 15.346  -47.632 -40.897  1.00 66.01  ? 53   PRO   D CB   1 
ATOM   20240 C  CG   . PRO   D  4  53  ? 14.280  -47.182 -41.836  1.00 66.79  ? 53   PRO   D CG   1 
ATOM   20241 C  CD   . PRO   D  4  53  ? 13.049  -47.017 -41.007  1.00 65.75  ? 53   PRO   D CD   1 
ATOM   20242 H  HA   . PRO   D  4  53  ? 14.706  -49.391 -40.001  1.00 75.85  ? 53   PRO   D HA   1 
ATOM   20243 H  HB2  . PRO   D  4  53  ? 15.795  -46.872 -40.495  1.00 79.19  ? 53   PRO   D HB2  1 
ATOM   20244 H  HB3  . PRO   D  4  53  ? 15.991  -48.196 -41.352  1.00 79.19  ? 53   PRO   D HB3  1 
ATOM   20245 H  HG2  . PRO   D  4  53  ? 14.536  -46.339 -42.242  1.00 80.12  ? 53   PRO   D HG2  1 
ATOM   20246 H  HG3  . PRO   D  4  53  ? 14.144  -47.853 -42.522  1.00 80.12  ? 53   PRO   D HG3  1 
ATOM   20247 H  HD2  . PRO   D  4  53  ? 13.008  -46.128 -40.622  1.00 78.88  ? 53   PRO   D HD2  1 
ATOM   20248 H  HD3  . PRO   D  4  53  ? 12.252  -47.189 -41.533  1.00 78.88  ? 53   PRO   D HD3  1 
ATOM   20249 N  N    . ASN   D  4  54  ? 14.848  -47.023 -37.831  1.00 62.91  ? 54   ASN   D N    1 
ATOM   20250 C  CA   . ASN   D  4  54  ? 15.451  -46.646 -36.559  1.00 67.98  ? 54   ASN   D CA   1 
ATOM   20251 C  C    . ASN   D  4  54  ? 14.942  -47.493 -35.401  1.00 69.07  ? 54   ASN   D C    1 
ATOM   20252 O  O    . ASN   D  4  54  ? 15.641  -47.615 -34.389  1.00 70.68  ? 54   ASN   D O    1 
ATOM   20253 C  CB   . ASN   D  4  54  ? 15.185  -45.166 -36.274  1.00 73.06  ? 54   ASN   D CB   1 
ATOM   20254 C  CG   . ASN   D  4  54  ? 16.278  -44.528 -35.440  1.00 79.43  ? 54   ASN   D CG   1 
ATOM   20255 O  OD1  . ASN   D  4  54  ? 17.452  -44.874 -35.564  1.00 78.11  ? 54   ASN   D OD1  1 
ATOM   20256 N  ND2  . ASN   D  4  54  ? 15.896  -43.589 -34.583  1.00 88.90  ? 54   ASN   D ND2  1 
ATOM   20257 H  H    . ASN   D  4  54  ? 14.272  -46.462 -38.136  1.00 75.47  ? 54   ASN   D H    1 
ATOM   20258 H  HA   . ASN   D  4  54  ? 16.410  -46.774 -36.622  1.00 81.56  ? 54   ASN   D HA   1 
ATOM   20259 H  HB2  . ASN   D  4  54  ? 15.130  -44.686 -37.115  1.00 87.66  ? 54   ASN   D HB2  1 
ATOM   20260 H  HB3  . ASN   D  4  54  ? 14.349  -45.083 -35.789  1.00 87.66  ? 54   ASN   D HB3  1 
ATOM   20261 H  HD21 . ASN   D  4  54  ? 16.478  -43.196 -34.087  1.00 106.66 ? 54   ASN   D HD21 1 
ATOM   20262 H  HD22 . ASN   D  4  54  ? 15.065  -43.373 -34.524  1.00 106.66 ? 54   ASN   D HD22 1 
ATOM   20263 N  N    . SER   D  4  55  ? 13.751  -48.084 -35.526  1.00 68.13  ? 55   SER   D N    1 
ATOM   20264 C  CA   . SER   D  4  55  ? 13.147  -48.854 -34.450  1.00 67.56  ? 55   SER   D CA   1 
ATOM   20265 C  C    . SER   D  4  55  ? 12.984  -50.333 -34.764  1.00 71.14  ? 55   SER   D C    1 
ATOM   20266 O  O    . SER   D  4  55  ? 12.682  -51.108 -33.849  1.00 73.32  ? 55   SER   D O    1 
ATOM   20267 C  CB   . SER   D  4  55  ? 11.767  -48.278 -34.091  1.00 66.85  ? 55   SER   D CB   1 
ATOM   20268 O  OG   . SER   D  4  55  ? 10.816  -48.570 -35.100  1.00 66.26  ? 55   SER   D OG   1 
ATOM   20269 H  H    . SER   D  4  55  ? 13.270  -48.050 -36.238  1.00 81.74  ? 55   SER   D H    1 
ATOM   20270 H  HA   . SER   D  4  55  ? 13.718  -48.780 -33.669  1.00 81.05  ? 55   SER   D HA   1 
ATOM   20271 H  HB2  . SER   D  4  55  ? 11.470  -48.670 -33.255  1.00 80.20  ? 55   SER   D HB2  1 
ATOM   20272 H  HB3  . SER   D  4  55  ? 11.842  -47.315 -33.997  1.00 80.20  ? 55   SER   D HB3  1 
ATOM   20273 H  HG   . SER   D  4  55  ? 10.053  -48.315 -34.859  1.00 79.49  ? 55   SER   D HG   1 
ATOM   20274 N  N    . GLY   D  4  56  ? 13.167  -50.751 -36.016  1.00 72.32  ? 56   GLY   D N    1 
ATOM   20275 C  CA   . GLY   D  4  56  ? 13.001  -52.139 -36.391  1.00 71.35  ? 56   GLY   D CA   1 
ATOM   20276 C  C    . GLY   D  4  56  ? 11.567  -52.611 -36.488  1.00 70.56  ? 56   GLY   D C    1 
ATOM   20277 O  O    . GLY   D  4  56  ? 11.335  -53.745 -36.926  1.00 73.43  ? 56   GLY   D O    1 
ATOM   20278 H  H    . GLY   D  4  56  ? 13.390  -50.238 -36.669  1.00 86.77  ? 56   GLY   D H    1 
ATOM   20279 H  HA2  . GLY   D  4  56  ? 13.416  -52.278 -37.257  1.00 85.60  ? 56   GLY   D HA2  1 
ATOM   20280 H  HA3  . GLY   D  4  56  ? 13.449  -52.693 -35.733  1.00 85.60  ? 56   GLY   D HA3  1 
ATOM   20281 N  N    . TYR   D  4  57  ? 10.598  -51.788 -36.093  1.00 69.64  ? 57   TYR   D N    1 
ATOM   20282 C  CA   . TYR   D  4  57  ? 9.195   -52.160 -36.214  1.00 69.71  ? 57   TYR   D CA   1 
ATOM   20283 C  C    . TYR   D  4  57  ? 8.828   -52.381 -37.676  1.00 69.19  ? 57   TYR   D C    1 
ATOM   20284 O  O    . TYR   D  4  57  ? 9.294   -51.663 -38.566  1.00 67.14  ? 57   TYR   D O    1 
ATOM   20285 C  CB   . TYR   D  4  57  ? 8.315   -51.069 -35.602  1.00 74.55  ? 57   TYR   D CB   1 
ATOM   20286 C  CG   . TYR   D  4  57  ? 6.832   -51.300 -35.773  1.00 80.40  ? 57   TYR   D CG   1 
ATOM   20287 C  CD1  . TYR   D  4  57  ? 6.151   -52.191 -34.956  1.00 85.31  ? 57   TYR   D CD1  1 
ATOM   20288 C  CD2  . TYR   D  4  57  ? 6.112   -50.620 -36.745  1.00 82.09  ? 57   TYR   D CD2  1 
ATOM   20289 C  CE1  . TYR   D  4  57  ? 4.796   -52.404 -35.107  1.00 89.98  ? 57   TYR   D CE1  1 
ATOM   20290 C  CE2  . TYR   D  4  57  ? 4.755   -50.825 -36.903  1.00 87.54  ? 57   TYR   D CE2  1 
ATOM   20291 C  CZ   . TYR   D  4  57  ? 4.102   -51.718 -36.081  1.00 92.50  ? 57   TYR   D CZ   1 
ATOM   20292 O  OH   . TYR   D  4  57  ? 2.751   -51.928 -36.233  1.00 98.20  ? 57   TYR   D OH   1 
ATOM   20293 H  H    . TYR   D  4  57  ? 10.728  -51.009 -35.752  1.00 83.55  ? 57   TYR   D H    1 
ATOM   20294 H  HA   . TYR   D  4  57  ? 9.033   -52.987 -35.734  1.00 83.63  ? 57   TYR   D HA   1 
ATOM   20295 H  HB2  . TYR   D  4  57  ? 8.497   -51.021 -34.651  1.00 89.44  ? 57   TYR   D HB2  1 
ATOM   20296 H  HB3  . TYR   D  4  57  ? 8.531   -50.223 -36.025  1.00 89.44  ? 57   TYR   D HB3  1 
ATOM   20297 H  HD1  . TYR   D  4  57  ? 6.616   -52.653 -34.296  1.00 102.36 ? 57   TYR   D HD1  1 
ATOM   20298 H  HD2  . TYR   D  4  57  ? 6.550   -50.016 -37.300  1.00 98.49  ? 57   TYR   D HD2  1 
ATOM   20299 H  HE1  . TYR   D  4  57  ? 4.353   -53.006 -34.554  1.00 107.96 ? 57   TYR   D HE1  1 
ATOM   20300 H  HE2  . TYR   D  4  57  ? 4.285   -50.364 -37.559  1.00 105.03 ? 57   TYR   D HE2  1 
ATOM   20301 H  HH   . TYR   D  4  57  ? 2.451   -51.437 -36.844  1.00 117.83 ? 57   TYR   D HH   1 
ATOM   20302 N  N    . THR   D  4  58  ? 7.990   -53.387 -37.923  1.00 73.39  ? 58   THR   D N    1 
ATOM   20303 C  CA   . THR   D  4  58  ? 7.580   -53.736 -39.274  1.00 71.44  ? 58   THR   D CA   1 
ATOM   20304 C  C    . THR   D  4  58  ? 6.089   -54.038 -39.304  1.00 72.38  ? 58   THR   D C    1 
ATOM   20305 O  O    . THR   D  4  58  ? 5.500   -54.451 -38.302  1.00 73.80  ? 58   THR   D O    1 
ATOM   20306 C  CB   . THR   D  4  58  ? 8.343   -54.959 -39.811  1.00 69.90  ? 58   THR   D CB   1 
ATOM   20307 O  OG1  . THR   D  4  58  ? 7.957   -56.128 -39.077  1.00 71.46  ? 58   THR   D OG1  1 
ATOM   20308 C  CG2  . THR   D  4  58  ? 9.843   -54.763 -39.683  1.00 69.96  ? 58   THR   D CG2  1 
ATOM   20309 H  H    . THR   D  4  58  ? 7.644   -53.887 -37.315  1.00 88.05  ? 58   THR   D H    1 
ATOM   20310 H  HA   . THR   D  4  58  ? 7.755   -52.976 -39.852  1.00 85.71  ? 58   THR   D HA   1 
ATOM   20311 H  HB   . THR   D  4  58  ? 8.132   -55.077 -40.751  1.00 83.86  ? 58   THR   D HB   1 
ATOM   20312 H  HG1  . THR   D  4  58  ? 8.323   -56.808 -39.407  1.00 85.73  ? 58   THR   D HG1  1 
ATOM   20313 H  HG21 . THR   D  4  58  ? 10.311  -55.522 -40.065  1.00 83.93  ? 58   THR   D HG21 1 
ATOM   20314 H  HG22 . THR   D  4  58  ? 10.114  -53.958 -40.150  1.00 83.93  ? 58   THR   D HG22 1 
ATOM   20315 H  HG23 . THR   D  4  58  ? 10.088  -54.681 -38.748  1.00 83.93  ? 58   THR   D HG23 1 
ATOM   20316 N  N    . GLU   D  4  59  ? 5.487   -53.823 -40.472  1.00 70.27  ? 59   GLU   D N    1 
ATOM   20317 C  CA   . GLU   D  4  59  ? 4.144   -54.293 -40.777  1.00 73.16  ? 59   GLU   D CA   1 
ATOM   20318 C  C    . GLU   D  4  59  ? 4.173   -54.949 -42.149  1.00 72.90  ? 59   GLU   D C    1 
ATOM   20319 O  O    . GLU   D  4  59  ? 4.768   -54.413 -43.088  1.00 69.62  ? 59   GLU   D O    1 
ATOM   20320 C  CB   . GLU   D  4  59  ? 3.112   -53.158 -40.764  1.00 75.70  ? 59   GLU   D CB   1 
ATOM   20321 C  CG   . GLU   D  4  59  ? 2.835   -52.574 -39.387  1.00 82.81  ? 59   GLU   D CG   1 
ATOM   20322 C  CD   . GLU   D  4  59  ? 1.603   -51.693 -39.369  1.00 87.23  ? 59   GLU   D CD   1 
ATOM   20323 O  OE1  . GLU   D  4  59  ? 0.621   -52.028 -40.065  1.00 88.01  ? 59   GLU   D OE1  1 
ATOM   20324 O  OE2  . GLU   D  4  59  ? 1.618   -50.664 -38.661  1.00 88.84  ? 59   GLU   D OE2  1 
ATOM   20325 H  H    . GLU   D  4  59  ? 5.851   -53.394 -41.123  1.00 84.31  ? 59   GLU   D H    1 
ATOM   20326 H  HA   . GLU   D  4  59  ? 3.863   -54.940 -40.112  1.00 87.77  ? 59   GLU   D HA   1 
ATOM   20327 H  HB2  . GLU   D  4  59  ? 3.437   -52.439 -41.328  1.00 90.82  ? 59   GLU   D HB2  1 
ATOM   20328 H  HB3  . GLU   D  4  59  ? 2.273   -53.499 -41.112  1.00 90.82  ? 59   GLU   D HB3  1 
ATOM   20329 H  HG2  . GLU   D  4  59  ? 2.697   -53.298 -38.757  1.00 99.35  ? 59   GLU   D HG2  1 
ATOM   20330 H  HG3  . GLU   D  4  59  ? 3.594   -52.035 -39.113  1.00 99.35  ? 59   GLU   D HG3  1 
ATOM   20331 N  N    . CYS   D  4  60  ? 3.535   -56.110 -42.258  1.00 78.08  ? 60   CYS   D N    1 
ATOM   20332 C  CA   . CYS   D  4  60  ? 3.537   -56.896 -43.481  1.00 79.24  ? 60   CYS   D CA   1 
ATOM   20333 C  C    . CYS   D  4  60  ? 2.116   -57.098 -43.983  1.00 77.05  ? 60   CYS   D C    1 
ATOM   20334 O  O    . CYS   D  4  60  ? 1.155   -57.071 -43.210  1.00 78.35  ? 60   CYS   D O    1 
ATOM   20335 C  CB   . CYS   D  4  60  ? 4.187   -58.270 -43.264  1.00 86.04  ? 60   CYS   D CB   1 
ATOM   20336 S  SG   . CYS   D  4  60  ? 5.967   -58.232 -42.966  1.00 90.69  ? 60   CYS   D SG   1 
ATOM   20337 H  H    . CYS   D  4  60  ? 3.084   -56.470 -41.620  1.00 93.68  ? 60   CYS   D H    1 
ATOM   20338 H  HA   . CYS   D  4  60  ? 4.039   -56.414 -44.157  1.00 95.07  ? 60   CYS   D HA   1 
ATOM   20339 H  HB2  . CYS   D  4  60  ? 3.771   -58.688 -42.494  1.00 103.23 ? 60   CYS   D HB2  1 
ATOM   20340 H  HB3  . CYS   D  4  60  ? 4.035   -58.809 -44.056  1.00 103.23 ? 60   CYS   D HB3  1 
ATOM   20341 H  HG   . CYS   D  4  60  ? 6.360   -59.355 -42.805  1.00 108.81 ? 60   CYS   D HG   1 
ATOM   20342 N  N    . ASN   D  4  61  ? 1.996   -57.294 -45.293  1.00 73.58  ? 61   ASN   D N    1 
ATOM   20343 C  CA   . ASN   D  4  61  ? 0.771   -57.850 -45.849  1.00 74.36  ? 61   ASN   D CA   1 
ATOM   20344 C  C    . ASN   D  4  61  ? 0.561   -59.247 -45.279  1.00 77.90  ? 61   ASN   D C    1 
ATOM   20345 O  O    . ASN   D  4  61  ? 1.514   -60.010 -45.100  1.00 74.12  ? 61   ASN   D O    1 
ATOM   20346 C  CB   . ASN   D  4  61  ? 0.860   -57.898 -47.375  1.00 73.66  ? 61   ASN   D CB   1 
ATOM   20347 C  CG   . ASN   D  4  61  ? -0.437  -58.340 -48.027  1.00 77.31  ? 61   ASN   D CG   1 
ATOM   20348 O  OD1  . ASN   D  4  61  ? -1.308  -58.923 -47.381  1.00 80.70  ? 61   ASN   D OD1  1 
ATOM   20349 N  ND2  . ASN   D  4  61  ? -0.567  -58.069 -49.321  1.00 76.47  ? 61   ASN   D ND2  1 
ATOM   20350 H  H    . ASN   D  4  61  ? 2.603   -57.114 -45.875  1.00 88.28  ? 61   ASN   D H    1 
ATOM   20351 H  HA   . ASN   D  4  61  ? 0.009   -57.295 -45.619  1.00 89.21  ? 61   ASN   D HA   1 
ATOM   20352 H  HB2  . ASN   D  4  61  ? 1.075   -57.012 -47.707  1.00 88.37  ? 61   ASN   D HB2  1 
ATOM   20353 H  HB3  . ASN   D  4  61  ? 1.553   -58.525 -47.632  1.00 88.37  ? 61   ASN   D HB3  1 
ATOM   20354 H  HD21 . ASN   D  4  61  ? -1.283  -58.299 -49.738  1.00 91.74  ? 61   ASN   D HD21 1 
ATOM   20355 H  HD22 . ASN   D  4  61  ? 0.065   -57.665 -49.741  1.00 91.74  ? 61   ASN   D HD22 1 
ATOM   20356 N  N    . GLU   D  4  62  ? -0.698  -59.581 -44.982  1.00 84.19  ? 62   GLU   D N    1 
ATOM   20357 C  CA   . GLU   D  4  62  ? -0.990  -60.885 -44.395  1.00 93.13  ? 62   GLU   D CA   1 
ATOM   20358 C  C    . GLU   D  4  62  ? -0.403  -62.020 -45.225  1.00 90.77  ? 62   GLU   D C    1 
ATOM   20359 O  O    . GLU   D  4  62  ? -0.063  -63.077 -44.682  1.00 91.95  ? 62   GLU   D O    1 
ATOM   20360 C  CB   . GLU   D  4  62  ? -2.501  -61.074 -44.247  1.00 107.28 ? 62   GLU   D CB   1 
ATOM   20361 C  CG   . GLU   D  4  62  ? -3.143  -60.159 -43.217  1.00 115.75 ? 62   GLU   D CG   1 
ATOM   20362 C  CD   . GLU   D  4  62  ? -4.628  -60.416 -43.056  1.00 125.54 ? 62   GLU   D CD   1 
ATOM   20363 O  OE1  . GLU   D  4  62  ? -5.168  -61.271 -43.791  1.00 129.23 ? 62   GLU   D OE1  1 
ATOM   20364 O  OE2  . GLU   D  4  62  ? -5.253  -59.764 -42.194  1.00 128.36 ? 62   GLU   D OE2  1 
ATOM   20365 H  H    . GLU   D  4  62  ? -1.385  -59.079 -45.107  1.00 101.01 ? 62   GLU   D H    1 
ATOM   20366 H  HA   . GLU   D  4  62  ? -0.594  -60.921 -43.510  1.00 111.73 ? 62   GLU   D HA   1 
ATOM   20367 H  HB2  . GLU   D  4  62  ? -2.921  -60.894 -45.102  1.00 128.72 ? 62   GLU   D HB2  1 
ATOM   20368 H  HB3  . GLU   D  4  62  ? -2.675  -61.989 -43.977  1.00 128.72 ? 62   GLU   D HB3  1 
ATOM   20369 H  HG2  . GLU   D  4  62  ? -2.719  -60.303 -42.357  1.00 138.88 ? 62   GLU   D HG2  1 
ATOM   20370 H  HG3  . GLU   D  4  62  ? -3.026  -59.237 -43.494  1.00 138.88 ? 62   GLU   D HG3  1 
ATOM   20371 N  N    . ILE   D  4  63  ? -0.269  -61.818 -46.537  1.00 89.09  ? 63   ILE   D N    1 
ATOM   20372 C  CA   . ILE   D  4  63  ? 0.274   -62.861 -47.404  1.00 92.38  ? 63   ILE   D CA   1 
ATOM   20373 C  C    . ILE   D  4  63  ? 1.682   -63.240 -46.962  1.00 91.76  ? 63   ILE   D C    1 
ATOM   20374 O  O    . ILE   D  4  63  ? 1.980   -64.415 -46.714  1.00 100.82 ? 63   ILE   D O    1 
ATOM   20375 C  CB   . ILE   D  4  63  ? 0.256   -62.398 -48.873  1.00 92.60  ? 63   ILE   D CB   1 
ATOM   20376 C  CG1  . ILE   D  4  63  ? -1.181  -62.140 -49.333  1.00 94.52  ? 63   ILE   D CG1  1 
ATOM   20377 C  CG2  . ILE   D  4  63  ? 0.933   -63.433 -49.770  1.00 95.46  ? 63   ILE   D CG2  1 
ATOM   20378 C  CD1  . ILE   D  4  63  ? -1.286  -61.434 -50.672  1.00 92.66  ? 63   ILE   D CD1  1 
ATOM   20379 H  H    . ILE   D  4  63  ? -0.483  -61.092 -46.946  1.00 106.89 ? 63   ILE   D H    1 
ATOM   20380 H  HA   . ILE   D  4  63  ? -0.288  -63.648 -47.326  1.00 110.84 ? 63   ILE   D HA   1 
ATOM   20381 H  HB   . ILE   D  4  63  ? 0.752   -61.567 -48.938  1.00 111.11 ? 63   ILE   D HB   1 
ATOM   20382 H  HG12 . ILE   D  4  63  ? -1.639  -62.991 -49.412  1.00 113.41 ? 63   ILE   D HG12 1 
ATOM   20383 H  HG13 . ILE   D  4  63  ? -1.624  -61.584 -48.672  1.00 113.41 ? 63   ILE   D HG13 1 
ATOM   20384 H  HG21 . ILE   D  4  63  ? 0.842   -63.156 -50.695  1.00 114.53 ? 63   ILE   D HG21 1 
ATOM   20385 H  HG22 . ILE   D  4  63  ? 1.871   -63.491 -49.532  1.00 114.53 ? 63   ILE   D HG22 1 
ATOM   20386 H  HG23 . ILE   D  4  63  ? 0.504   -64.293 -49.638  1.00 114.53 ? 63   ILE   D HG23 1 
ATOM   20387 H  HD11 . ILE   D  4  63  ? -2.220  -61.257 -50.863  1.00 111.18 ? 63   ILE   D HD11 1 
ATOM   20388 H  HD12 . ILE   D  4  63  ? -0.793  -60.600 -50.629  1.00 111.18 ? 63   ILE   D HD12 1 
ATOM   20389 H  HD13 . ILE   D  4  63  ? -0.910  -62.006 -51.360  1.00 111.18 ? 63   ILE   D HD13 1 
ATOM   20390 N  N    . PHE   D  4  64  ? 2.567   -62.250 -46.857  1.00 85.02  ? 64   PHE   D N    1 
ATOM   20391 C  CA   . PHE   D  4  64  ? 3.987   -62.482 -46.635  1.00 85.69  ? 64   PHE   D CA   1 
ATOM   20392 C  C    . PHE   D  4  64  ? 4.366   -62.500 -45.158  1.00 87.03  ? 64   PHE   D C    1 
ATOM   20393 O  O    . PHE   D  4  64  ? 5.551   -62.359 -44.834  1.00 85.24  ? 64   PHE   D O    1 
ATOM   20394 C  CB   . PHE   D  4  64  ? 4.808   -61.413 -47.363  1.00 83.08  ? 64   PHE   D CB   1 
ATOM   20395 C  CG   . PHE   D  4  64  ? 4.422   -61.230 -48.802  1.00 84.47  ? 64   PHE   D CG   1 
ATOM   20396 C  CD1  . PHE   D  4  64  ? 4.995   -62.011 -49.791  1.00 86.19  ? 64   PHE   D CD1  1 
ATOM   20397 C  CD2  . PHE   D  4  64  ? 3.482   -60.279 -49.165  1.00 83.71  ? 64   PHE   D CD2  1 
ATOM   20398 C  CE1  . PHE   D  4  64  ? 4.639   -61.847 -51.114  1.00 86.44  ? 64   PHE   D CE1  1 
ATOM   20399 C  CE2  . PHE   D  4  64  ? 3.122   -60.111 -50.488  1.00 84.28  ? 64   PHE   D CE2  1 
ATOM   20400 C  CZ   . PHE   D  4  64  ? 3.701   -60.895 -51.463  1.00 84.95  ? 64   PHE   D CZ   1 
ATOM   20401 H  H    . PHE   D  4  64  ? 2.361   -61.417 -46.913  1.00 102.00 ? 64   PHE   D H    1 
ATOM   20402 H  HA   . PHE   D  4  64  ? 4.211   -63.349 -47.006  1.00 102.81 ? 64   PHE   D HA   1 
ATOM   20403 H  HB2  . PHE   D  4  64  ? 4.683   -60.563 -46.913  1.00 99.68  ? 64   PHE   D HB2  1 
ATOM   20404 H  HB3  . PHE   D  4  64  ? 5.744   -61.668 -47.338  1.00 99.68  ? 64   PHE   D HB3  1 
ATOM   20405 H  HD1  . PHE   D  4  64  ? 5.626   -62.654 -49.561  1.00 103.40 ? 64   PHE   D HD1  1 
ATOM   20406 H  HD2  . PHE   D  4  64  ? 3.089   -59.748 -48.511  1.00 100.43 ? 64   PHE   D HD2  1 
ATOM   20407 H  HE1  . PHE   D  4  64  ? 5.030   -62.377 -51.770  1.00 103.71 ? 64   PHE   D HE1  1 
ATOM   20408 H  HE2  . PHE   D  4  64  ? 2.490   -59.469 -50.720  1.00 101.12 ? 64   PHE   D HE2  1 
ATOM   20409 H  HZ   . PHE   D  4  64  ? 3.460   -60.784 -52.354  1.00 101.92 ? 64   PHE   D HZ   1 
ATOM   20410 N  N    . ARG   D  4  65  ? 3.396   -62.673 -44.257  1.00 92.21  ? 65   ARG   D N    1 
ATOM   20411 C  CA   . ARG   D  4  65  ? 3.705   -62.602 -42.831  1.00 96.85  ? 65   ARG   D CA   1 
ATOM   20412 C  C    . ARG   D  4  65  ? 4.741   -63.649 -42.437  1.00 93.14  ? 65   ARG   D C    1 
ATOM   20413 O  O    . ARG   D  4  65  ? 5.656   -63.363 -41.656  1.00 90.34  ? 65   ARG   D O    1 
ATOM   20414 C  CB   . ARG   D  4  65  ? 2.428   -62.760 -42.002  1.00 108.07 ? 65   ARG   D CB   1 
ATOM   20415 C  CG   . ARG   D  4  65  ? 1.784   -64.139 -42.046  1.00 118.83 ? 65   ARG   D CG   1 
ATOM   20416 C  CD   . ARG   D  4  65  ? 0.512   -64.168 -41.209  1.00 123.52 ? 65   ARG   D CD   1 
ATOM   20417 N  NE   . ARG   D  4  65  ? 0.044   -65.526 -40.936  1.00 128.85 ? 65   ARG   D NE   1 
ATOM   20418 C  CZ   . ARG   D  4  65  ? -0.764  -66.223 -41.730  1.00 132.10 ? 65   ARG   D CZ   1 
ATOM   20419 N  NH1  . ARG   D  4  65  ? -1.207  -65.705 -42.869  1.00 129.37 ? 65   ARG   D NH1  1 
ATOM   20420 N  NH2  . ARG   D  4  65  ? -1.131  -67.449 -41.384  1.00 138.64 ? 65   ARG   D NH2  1 
ATOM   20421 H  H    . ARG   D  4  65  ? 2.570   -62.829 -44.441  1.00 110.63 ? 65   ARG   D H    1 
ATOM   20422 H  HA   . ARG   D  4  65  ? 4.077   -61.728 -42.637  1.00 116.20 ? 65   ARG   D HA   1 
ATOM   20423 H  HB2  . ARG   D  4  65  ? 2.641   -62.570 -41.075  1.00 129.67 ? 65   ARG   D HB2  1 
ATOM   20424 H  HB3  . ARG   D  4  65  ? 1.771   -62.125 -42.329  1.00 129.67 ? 65   ARG   D HB3  1 
ATOM   20425 H  HG2  . ARG   D  4  65  ? 1.556   -64.362 -42.962  1.00 142.57 ? 65   ARG   D HG2  1 
ATOM   20426 H  HG3  . ARG   D  4  65  ? 2.402   -64.797 -41.689  1.00 142.57 ? 65   ARG   D HG3  1 
ATOM   20427 H  HD2  . ARG   D  4  65  ? 0.682   -63.734 -40.359  1.00 148.20 ? 65   ARG   D HD2  1 
ATOM   20428 H  HD3  . ARG   D  4  65  ? -0.191  -63.700 -41.686  1.00 148.20 ? 65   ARG   D HD3  1 
ATOM   20429 H  HE   . ARG   D  4  65  ? 0.312   -65.901 -40.210  1.00 154.60 ? 65   ARG   D HE   1 
ATOM   20430 H  HH11 . ARG   D  4  65  ? -0.972  -64.911 -43.100  1.00 155.23 ? 65   ARG   D HH11 1 
ATOM   20431 H  HH12 . ARG   D  4  65  ? -1.729  -66.163 -43.375  1.00 155.23 ? 65   ARG   D HH12 1 
ATOM   20432 H  HH21 . ARG   D  4  65  ? -0.846  -67.791 -40.648  1.00 166.35 ? 65   ARG   D HH21 1 
ATOM   20433 H  HH22 . ARG   D  4  65  ? -1.653  -67.902 -41.895  1.00 166.35 ? 65   ARG   D HH22 1 
ATOM   20434 N  N    . ASP   D  4  66  ? 4.621   -64.865 -42.972  1.00 94.35  ? 66   ASP   D N    1 
ATOM   20435 C  CA   . ASP   D  4  66  ? 5.571   -65.934 -42.699  1.00 96.70  ? 66   ASP   D CA   1 
ATOM   20436 C  C    . ASP   D  4  66  ? 6.625   -66.086 -43.787  1.00 94.41  ? 66   ASP   D C    1 
ATOM   20437 O  O    . ASP   D  4  66  ? 7.548   -66.892 -43.624  1.00 96.30  ? 66   ASP   D O    1 
ATOM   20438 C  CB   . ASP   D  4  66  ? 4.830   -67.266 -42.522  1.00 104.42 ? 66   ASP   D CB   1 
ATOM   20439 C  CG   . ASP   D  4  66  ? 4.153   -67.380 -41.171  1.00 108.65 ? 66   ASP   D CG   1 
ATOM   20440 O  OD1  . ASP   D  4  66  ? 4.749   -66.936 -40.167  1.00 107.53 ? 66   ASP   D OD1  1 
ATOM   20441 O  OD2  . ASP   D  4  66  ? 3.027   -67.915 -41.113  1.00 113.57 ? 66   ASP   D OD2  1 
ATOM   20442 H  H    . ASP   D  4  66  ? 3.985   -65.095 -43.504  1.00 113.20 ? 66   ASP   D H    1 
ATOM   20443 H  HA   . ASP   D  4  66  ? 6.030   -65.737 -41.868  1.00 116.03 ? 66   ASP   D HA   1 
ATOM   20444 H  HB2  . ASP   D  4  66  ? 4.147   -67.342 -43.207  1.00 125.29 ? 66   ASP   D HB2  1 
ATOM   20445 H  HB3  . ASP   D  4  66  ? 5.464   -67.995 -42.603  1.00 125.29 ? 66   ASP   D HB3  1 
ATOM   20446 N  N    . LYS   D  4  67  ? 6.519   -65.336 -44.883  1.00 92.86  ? 67   LYS   D N    1 
ATOM   20447 C  CA   . LYS   D  4  67  ? 7.470   -65.451 -45.981  1.00 96.24  ? 67   LYS   D CA   1 
ATOM   20448 C  C    . LYS   D  4  67  ? 8.679   -64.541 -45.793  1.00 89.66  ? 67   LYS   D C    1 
ATOM   20449 O  O    . LYS   D  4  67  ? 9.822   -65.003 -45.856  1.00 88.33  ? 67   LYS   D O    1 
ATOM   20450 C  CB   . LYS   D  4  67  ? 6.782   -65.127 -47.311  1.00 105.32 ? 67   LYS   D CB   1 
ATOM   20451 C  CG   . LYS   D  4  67  ? 5.709   -66.120 -47.726  1.00 119.48 ? 67   LYS   D CG   1 
ATOM   20452 C  CD   . LYS   D  4  67  ? 5.047   -65.697 -49.029  1.00 123.02 ? 67   LYS   D CD   1 
ATOM   20453 C  CE   . LYS   D  4  67  ? 3.983   -66.691 -49.472  1.00 127.89 ? 67   LYS   D CE   1 
ATOM   20454 N  NZ   . LYS   D  4  67  ? 3.319   -66.265 -50.736  1.00 126.05 ? 67   LYS   D NZ   1 
ATOM   20455 H  H    . LYS   D  4  67  ? 5.901   -64.752 -45.012  1.00 111.41 ? 67   LYS   D H    1 
ATOM   20456 H  HA   . LYS   D  4  67  ? 7.784   -66.368 -46.015  1.00 115.47 ? 67   LYS   D HA   1 
ATOM   20457 H  HB2  . LYS   D  4  67  ? 6.361   -64.256 -47.237  1.00 126.37 ? 67   LYS   D HB2  1 
ATOM   20458 H  HB3  . LYS   D  4  67  ? 7.453   -65.113 -48.011  1.00 126.37 ? 67   LYS   D HB3  1 
ATOM   20459 H  HG2  . LYS   D  4  67  ? 6.110   -66.994 -47.855  1.00 143.35 ? 67   LYS   D HG2  1 
ATOM   20460 H  HG3  . LYS   D  4  67  ? 5.028   -66.166 -47.036  1.00 143.35 ? 67   LYS   D HG3  1 
ATOM   20461 H  HD2  . LYS   D  4  67  ? 4.623   -64.833 -48.907  1.00 147.60 ? 67   LYS   D HD2  1 
ATOM   20462 H  HD3  . LYS   D  4  67  ? 5.719   -65.641 -49.726  1.00 147.60 ? 67   LYS   D HD3  1 
ATOM   20463 H  HE2  . LYS   D  4  67  ? 4.396   -67.555 -49.622  1.00 153.45 ? 67   LYS   D HE2  1 
ATOM   20464 H  HE3  . LYS   D  4  67  ? 3.305   -66.762 -48.782  1.00 153.45 ? 67   LYS   D HE3  1 
ATOM   20465 H  HZ1  . LYS   D  4  67  ? 2.707   -66.864 -50.975  1.00 151.24 ? 67   LYS   D HZ1  1 
ATOM   20466 H  HZ2  . LYS   D  4  67  ? 2.922   -65.476 -50.621  1.00 151.24 ? 67   LYS   D HZ2  1 
ATOM   20467 H  HZ3  . LYS   D  4  67  ? 3.922   -66.192 -51.387  1.00 151.24 ? 67   LYS   D HZ3  1 
ATOM   20468 N  N    . ALA   D  4  68  ? 8.444   -63.253 -45.557  1.00 86.73  ? 68   ALA   D N    1 
ATOM   20469 C  CA   . ALA   D  4  68  ? 9.499   -62.252 -45.548  1.00 86.32  ? 68   ALA   D CA   1 
ATOM   20470 C  C    . ALA   D  4  68  ? 9.770   -61.747 -44.137  1.00 85.65  ? 68   ALA   D C    1 
ATOM   20471 O  O    . ALA   D  4  68  ? 8.875   -61.698 -43.289  1.00 90.07  ? 68   ALA   D O    1 
ATOM   20472 C  CB   . ALA   D  4  68  ? 9.136   -61.068 -46.450  1.00 84.94  ? 68   ALA   D CB   1 
ATOM   20473 H  H    . ALA   D  4  68  ? 7.664   -62.930 -45.397  1.00 104.06 ? 68   ALA   D H    1 
ATOM   20474 H  HA   . ALA   D  4  68  ? 10.316  -62.660 -45.876  1.00 103.56 ? 68   ALA   D HA   1 
ATOM   20475 H  HB1  . ALA   D  4  68  ? 9.856   -60.419 -46.425  1.00 101.90 ? 68   ALA   D HB1  1 
ATOM   20476 H  HB2  . ALA   D  4  68  ? 9.011   -61.388 -47.357  1.00 101.90 ? 68   ALA   D HB2  1 
ATOM   20477 H  HB3  . ALA   D  4  68  ? 8.315   -60.664 -46.126  1.00 101.90 ? 68   ALA   D HB3  1 
ATOM   20478 N  N    . THR   D  4  69  ? 11.026  -61.373 -43.901  1.00 82.08  ? 69   THR   D N    1 
ATOM   20479 C  CA   . THR   D  4  69  ? 11.450  -60.712 -42.674  1.00 79.81  ? 69   THR   D CA   1 
ATOM   20480 C  C    . THR   D  4  69  ? 12.322  -59.525 -43.055  1.00 74.86  ? 69   THR   D C    1 
ATOM   20481 O  O    . THR   D  4  69  ? 13.264  -59.672 -43.840  1.00 71.90  ? 69   THR   D O    1 
ATOM   20482 C  CB   . THR   D  4  69  ? 12.219  -61.666 -41.755  1.00 81.35  ? 69   THR   D CB   1 
ATOM   20483 O  OG1  . THR   D  4  69  ? 13.408  -62.119 -42.414  1.00 87.64  ? 69   THR   D OG1  1 
ATOM   20484 C  CG2  . THR   D  4  69  ? 11.357  -62.866 -41.389  1.00 82.86  ? 69   THR   D CG2  1 
ATOM   20485 H  H    . THR   D  4  69  ? 11.671  -61.497 -44.457  1.00 98.48  ? 69   THR   D H    1 
ATOM   20486 H  HA   . THR   D  4  69  ? 10.675  -60.393 -42.185  1.00 95.75  ? 69   THR   D HA   1 
ATOM   20487 H  HB   . THR   D  4  69  ? 12.461  -61.201 -40.939  1.00 97.60  ? 69   THR   D HB   1 
ATOM   20488 H  HG1  . THR   D  4  69  ? 13.876  -61.462 -42.646  1.00 105.15 ? 69   THR   D HG1  1 
ATOM   20489 H  HG21 . THR   D  4  69  ? 11.843  -63.452 -40.788  1.00 99.41  ? 69   THR   D HG21 1 
ATOM   20490 H  HG22 . THR   D  4  69  ? 10.545  -62.569 -40.949  1.00 99.41  ? 69   THR   D HG22 1 
ATOM   20491 H  HG23 . THR   D  4  69  ? 11.120  -63.360 -42.188  1.00 99.41  ? 69   THR   D HG23 1 
ATOM   20492 N  N    . MET   D  4  70  ? 12.008  -58.355 -42.505  1.00 71.53  ? 70   MET   D N    1 
ATOM   20493 C  CA   . MET   D  4  70  ? 12.692  -57.116 -42.844  1.00 66.36  ? 70   MET   D CA   1 
ATOM   20494 C  C    . MET   D  4  70  ? 13.565  -56.660 -41.683  1.00 67.62  ? 70   MET   D C    1 
ATOM   20495 O  O    . MET   D  4  70  ? 13.158  -56.734 -40.519  1.00 69.54  ? 70   MET   D O    1 
ATOM   20496 C  CB   . MET   D  4  70  ? 11.683  -56.020 -43.197  1.00 64.93  ? 70   MET   D CB   1 
ATOM   20497 C  CG   . MET   D  4  70  ? 10.764  -56.387 -44.345  1.00 64.49  ? 70   MET   D CG   1 
ATOM   20498 S  SD   . MET   D  4  70  ? 9.358   -55.275 -44.503  1.00 64.90  ? 70   MET   D SD   1 
ATOM   20499 C  CE   . MET   D  4  70  ? 8.481   -56.076 -45.840  1.00 72.88  ? 70   MET   D CE   1 
ATOM   20500 H  H    . MET   D  4  70  ? 11.386  -58.254 -41.920  1.00 85.81  ? 70   MET   D H    1 
ATOM   20501 H  HA   . MET   D  4  70  ? 13.260  -57.268 -43.616  1.00 79.62  ? 70   MET   D HA   1 
ATOM   20502 H  HB2  . MET   D  4  70  ? 11.130  -55.842 -42.419  1.00 77.90  ? 70   MET   D HB2  1 
ATOM   20503 H  HB3  . MET   D  4  70  ? 12.168  -55.219 -43.449  1.00 77.90  ? 70   MET   D HB3  1 
ATOM   20504 H  HG2  . MET   D  4  70  ? 11.266  -56.354 -45.174  1.00 77.37  ? 70   MET   D HG2  1 
ATOM   20505 H  HG3  . MET   D  4  70  ? 10.421  -57.283 -44.201  1.00 77.37  ? 70   MET   D HG3  1 
ATOM   20506 H  HE1  . MET   D  4  70  ? 7.700   -55.547 -46.068  1.00 87.44  ? 70   MET   D HE1  1 
ATOM   20507 H  HE2  . MET   D  4  70  ? 9.070   -56.144 -46.608  1.00 87.44  ? 70   MET   D HE2  1 
ATOM   20508 H  HE3  . MET   D  4  70  ? 8.209   -56.962 -45.553  1.00 87.44  ? 70   MET   D HE3  1 
ATOM   20509 N  N    . THR   D  4  71  ? 14.767  -56.191 -42.008  1.00 69.92  ? 71   THR   D N    1 
ATOM   20510 C  CA   . THR   D  4  71  ? 15.695  -55.660 -41.021  1.00 72.53  ? 71   THR   D CA   1 
ATOM   20511 C  C    . THR   D  4  71  ? 16.366  -54.426 -41.604  1.00 64.83  ? 71   THR   D C    1 
ATOM   20512 O  O    . THR   D  4  71  ? 16.186  -54.091 -42.778  1.00 59.90  ? 71   THR   D O    1 
ATOM   20513 C  CB   . THR   D  4  71  ? 16.742  -56.703 -40.609  1.00 80.37  ? 71   THR   D CB   1 
ATOM   20514 O  OG1  . THR   D  4  71  ? 17.464  -57.144 -41.765  1.00 85.16  ? 71   THR   D OG1  1 
ATOM   20515 C  CG2  . THR   D  4  71  ? 16.075  -57.899 -39.945  1.00 82.39  ? 71   THR   D CG2  1 
ATOM   20516 H  H    . THR   D  4  71  ? 15.073  -56.170 -42.811  1.00 83.88  ? 71   THR   D H    1 
ATOM   20517 H  HA   . THR   D  4  71  ? 15.206  -55.399 -40.225  1.00 87.01  ? 71   THR   D HA   1 
ATOM   20518 H  HB   . THR   D  4  71  ? 17.359  -56.306 -39.975  1.00 96.42  ? 71   THR   D HB   1 
ATOM   20519 H  HG1  . THR   D  4  71  ? 18.191  -56.727 -41.825  1.00 102.18 ? 71   THR   D HG1  1 
ATOM   20520 H  HG21 . THR   D  4  71  ? 16.747  -58.543 -39.670  1.00 98.85  ? 71   THR   D HG21 1 
ATOM   20521 H  HG22 . THR   D  4  71  ? 15.578  -57.610 -39.163  1.00 98.85  ? 71   THR   D HG22 1 
ATOM   20522 H  HG23 . THR   D  4  71  ? 15.465  -58.326 -40.566  1.00 98.85  ? 71   THR   D HG23 1 
ATOM   20523 N  N    . ALA   D  4  72  ? 17.150  -53.743 -40.772  1.00 60.84  ? 72   ALA   D N    1 
ATOM   20524 C  CA   . ALA   D  4  72  ? 17.817  -52.522 -41.197  1.00 59.89  ? 72   ALA   D CA   1 
ATOM   20525 C  C    . ALA   D  4  72  ? 19.071  -52.300 -40.367  1.00 64.48  ? 72   ALA   D C    1 
ATOM   20526 O  O    . ALA   D  4  72  ? 19.068  -52.508 -39.151  1.00 64.51  ? 72   ALA   D O    1 
ATOM   20527 C  CB   . ALA   D  4  72  ? 16.891  -51.307 -41.073  1.00 57.75  ? 72   ALA   D CB   1 
ATOM   20528 H  H    . ALA   D  4  72  ? 17.309  -53.968 -39.957  1.00 72.99  ? 72   ALA   D H    1 
ATOM   20529 H  HA   . ALA   D  4  72  ? 18.086  -52.620 -42.124  1.00 71.85  ? 72   ALA   D HA   1 
ATOM   20530 H  HB1  . ALA   D  4  72  ? 17.369  -50.514 -41.364  1.00 69.28  ? 72   ALA   D HB1  1 
ATOM   20531 H  HB2  . ALA   D  4  72  ? 16.110  -51.446 -41.632  1.00 69.28  ? 72   ALA   D HB2  1 
ATOM   20532 H  HB3  . ALA   D  4  72  ? 16.621  -51.208 -40.147  1.00 69.28  ? 72   ALA   D HB3  1 
ATOM   20533 N  N    . ASP   D  4  73  ? 20.139  -51.876 -41.039  1.00 68.45  ? 73   ASP   D N    1 
ATOM   20534 C  CA   . ASP   D  4  73  ? 21.389  -51.481 -40.399  1.00 74.00  ? 73   ASP   D CA   1 
ATOM   20535 C  C    . ASP   D  4  73  ? 21.520  -49.970 -40.552  1.00 69.52  ? 73   ASP   D C    1 
ATOM   20536 O  O    . ASP   D  4  73  ? 21.726  -49.468 -41.662  1.00 68.37  ? 73   ASP   D O    1 
ATOM   20537 C  CB   . ASP   D  4  73  ? 22.578  -52.210 -41.021  1.00 82.95  ? 73   ASP   D CB   1 
ATOM   20538 C  CG   . ASP   D  4  73  ? 23.895  -51.876 -40.339  1.00 93.41  ? 73   ASP   D CG   1 
ATOM   20539 O  OD1  . ASP   D  4  73  ? 23.907  -51.008 -39.441  1.00 96.20  ? 73   ASP   D OD1  1 
ATOM   20540 O  OD2  . ASP   D  4  73  ? 24.922  -52.487 -40.703  1.00 99.81  ? 73   ASP   D OD2  1 
ATOM   20541 H  H    . ASP   D  4  73  ? 20.163  -51.806 -41.896  1.00 82.12  ? 73   ASP   D H    1 
ATOM   20542 H  HA   . ASP   D  4  73  ? 21.366  -51.703 -39.455  1.00 88.78  ? 73   ASP   D HA   1 
ATOM   20543 H  HB2  . ASP   D  4  73  ? 22.436  -53.167 -40.947  1.00 99.52  ? 73   ASP   D HB2  1 
ATOM   20544 H  HB3  . ASP   D  4  73  ? 22.651  -51.957 -41.954  1.00 99.52  ? 73   ASP   D HB3  1 
ATOM   20545 N  N    . THR   D  4  74  ? 21.397  -49.249 -39.436  1.00 72.35  ? 74   THR   D N    1 
ATOM   20546 C  CA   . THR   D  4  74  ? 21.425  -47.791 -39.490  1.00 73.56  ? 74   THR   D CA   1 
ATOM   20547 C  C    . THR   D  4  74  ? 22.817  -47.272 -39.828  1.00 79.27  ? 74   THR   D C    1 
ATOM   20548 O  O    . THR   D  4  74  ? 22.958  -46.322 -40.607  1.00 82.80  ? 74   THR   D O    1 
ATOM   20549 C  CB   . THR   D  4  74  ? 20.943  -47.210 -38.158  1.00 76.01  ? 74   THR   D CB   1 
ATOM   20550 O  OG1  . THR   D  4  74  ? 19.513  -47.284 -38.086  1.00 76.14  ? 74   THR   D OG1  1 
ATOM   20551 C  CG2  . THR   D  4  74  ? 21.390  -45.760 -37.999  1.00 79.35  ? 74   THR   D CG2  1 
ATOM   20552 H  H    . THR   D  4  74  ? 21.299  -49.575 -38.647  1.00 86.81  ? 74   THR   D H    1 
ATOM   20553 H  HA   . THR   D  4  74  ? 20.819  -47.493 -40.187  1.00 88.26  ? 74   THR   D HA   1 
ATOM   20554 H  HB   . THR   D  4  74  ? 21.328  -47.722 -37.430  1.00 91.19  ? 74   THR   D HB   1 
ATOM   20555 H  HG1  . THR   D  4  74  ? 19.242  -46.938 -37.370  1.00 91.35  ? 74   THR   D HG1  1 
ATOM   20556 H  HG21 . THR   D  4  74  ? 20.898  -45.338 -37.277  1.00 95.20  ? 74   THR   D HG21 1 
ATOM   20557 H  HG22 . THR   D  4  74  ? 22.338  -45.725 -37.796  1.00 95.20  ? 74   THR   D HG22 1 
ATOM   20558 H  HG23 . THR   D  4  74  ? 21.226  -45.270 -38.820  1.00 95.20  ? 74   THR   D HG23 1 
ATOM   20559 N  N    . SER   D  4  75  ? 23.858  -47.879 -39.253  1.00 83.71  ? 75   SER   D N    1 
ATOM   20560 C  CA   . SER   D  4  75  ? 25.214  -47.388 -39.476  1.00 87.93  ? 75   SER   D CA   1 
ATOM   20561 C  C    . SER   D  4  75  ? 25.569  -47.358 -40.957  1.00 86.63  ? 75   SER   D C    1 
ATOM   20562 O  O    . SER   D  4  75  ? 26.321  -46.481 -41.396  1.00 91.66  ? 75   SER   D O    1 
ATOM   20563 C  CB   . SER   D  4  75  ? 26.216  -48.253 -38.711  1.00 95.75  ? 75   SER   D CB   1 
ATOM   20564 O  OG   . SER   D  4  75  ? 26.182  -49.594 -39.165  1.00 101.69 ? 75   SER   D OG   1 
ATOM   20565 H  H    . SER   D  4  75  ? 23.805  -48.566 -38.739  1.00 100.44 ? 75   SER   D H    1 
ATOM   20566 H  HA   . SER   D  4  75  ? 25.274  -46.481 -39.137  1.00 105.50 ? 75   SER   D HA   1 
ATOM   20567 H  HB2  . SER   D  4  75  ? 27.108  -47.896 -38.848  1.00 114.88 ? 75   SER   D HB2  1 
ATOM   20568 H  HB3  . SER   D  4  75  ? 25.992  -48.234 -37.768  1.00 114.88 ? 75   SER   D HB3  1 
ATOM   20569 H  HG   . SER   D  4  75  ? 25.404  -49.902 -39.094  1.00 122.00 ? 75   SER   D HG   1 
ATOM   20570 N  N    . SER   D  4  76  ? 25.040  -48.298 -41.741  1.00 80.58  ? 76   SER   D N    1 
ATOM   20571 C  CA   . SER   D  4  76  ? 25.339  -48.387 -43.164  1.00 79.60  ? 76   SER   D CA   1 
ATOM   20572 C  C    . SER   D  4  76  ? 24.174  -47.946 -44.041  1.00 74.14  ? 76   SER   D C    1 
ATOM   20573 O  O    . SER   D  4  76  ? 24.251  -48.077 -45.267  1.00 72.91  ? 76   SER   D O    1 
ATOM   20574 C  CB   . SER   D  4  76  ? 25.750  -49.817 -43.526  1.00 82.10  ? 76   SER   D CB   1 
ATOM   20575 O  OG   . SER   D  4  76  ? 24.687  -50.729 -43.312  1.00 80.49  ? 76   SER   D OG   1 
ATOM   20576 H  H    . SER   D  4  76  ? 24.496  -48.904 -41.464  1.00 96.68  ? 76   SER   D H    1 
ATOM   20577 H  HA   . SER   D  4  76  ? 26.088  -47.800 -43.354  1.00 95.50  ? 76   SER   D HA   1 
ATOM   20578 H  HB2  . SER   D  4  76  ? 26.002  -49.843 -44.463  1.00 98.50  ? 76   SER   D HB2  1 
ATOM   20579 H  HB3  . SER   D  4  76  ? 26.503  -50.077 -42.973  1.00 98.50  ? 76   SER   D HB3  1 
ATOM   20580 H  HG   . SER   D  4  76  ? 24.153  -50.705 -43.960  1.00 96.57  ? 76   SER   D HG   1 
ATOM   20581 N  N    . SER   D  4  77  ? 23.101  -47.424 -43.448  1.00 71.79  ? 77   SER   D N    1 
ATOM   20582 C  CA   . SER   D  4  77  ? 21.938  -46.954 -44.199  1.00 69.14  ? 77   SER   D CA   1 
ATOM   20583 C  C    . SER   D  4  77  ? 21.471  -48.014 -45.193  1.00 70.45  ? 77   SER   D C    1 
ATOM   20584 O  O    . SER   D  4  77  ? 21.242  -47.742 -46.374  1.00 73.01  ? 77   SER   D O    1 
ATOM   20585 C  CB   . SER   D  4  77  ? 22.246  -45.637 -44.911  1.00 68.72  ? 77   SER   D CB   1 
ATOM   20586 O  OG   . SER   D  4  77  ? 22.513  -44.602 -43.981  1.00 73.25  ? 77   SER   D OG   1 
ATOM   20587 H  H    . SER   D  4  77  ? 23.021  -47.330 -42.596  1.00 86.13  ? 77   SER   D H    1 
ATOM   20588 H  HA   . SER   D  4  77  ? 21.213  -46.795 -43.574  1.00 82.95  ? 77   SER   D HA   1 
ATOM   20589 H  HB2  . SER   D  4  77  ? 23.025  -45.760 -45.477  1.00 82.45  ? 77   SER   D HB2  1 
ATOM   20590 H  HB3  . SER   D  4  77  ? 21.481  -45.385 -45.451  1.00 82.45  ? 77   SER   D HB3  1 
ATOM   20591 H  HG   . SER   D  4  77  ? 22.700  -43.892 -44.388  1.00 87.88  ? 77   SER   D HG   1 
ATOM   20592 N  N    . THR   D  4  78  ? 21.330  -49.242 -44.699  1.00 69.92  ? 78   THR   D N    1 
ATOM   20593 C  CA   . THR   D  4  78  ? 20.995  -50.388 -45.532  1.00 68.88  ? 78   THR   D CA   1 
ATOM   20594 C  C    . THR   D  4  78  ? 19.784  -51.102 -44.954  1.00 61.98  ? 78   THR   D C    1 
ATOM   20595 O  O    . THR   D  4  78  ? 19.756  -51.421 -43.761  1.00 61.51  ? 78   THR   D O    1 
ATOM   20596 C  CB   . THR   D  4  78  ? 22.176  -51.362 -45.633  1.00 72.93  ? 78   THR   D CB   1 
ATOM   20597 O  OG1  . THR   D  4  78  ? 23.349  -50.655 -46.054  1.00 77.27  ? 78   THR   D OG1  1 
ATOM   20598 C  CG2  . THR   D  4  78  ? 21.873  -52.474 -46.631  1.00 68.48  ? 78   THR   D CG2  1 
ATOM   20599 H  H    . THR   D  4  78  ? 21.425  -49.437 -43.867  1.00 83.88  ? 78   THR   D H    1 
ATOM   20600 H  HA   . THR   D  4  78  ? 20.769  -50.078 -46.423  1.00 82.64  ? 78   THR   D HA   1 
ATOM   20601 H  HB   . THR   D  4  78  ? 22.334  -51.766 -44.766  1.00 87.49  ? 78   THR   D HB   1 
ATOM   20602 H  HG1  . THR   D  4  78  ? 23.987  -51.192 -46.157  1.00 92.71  ? 78   THR   D HG1  1 
ATOM   20603 H  HG21 . THR   D  4  78  ? 22.645  -53.054 -46.725  1.00 82.16  ? 78   THR   D HG21 1 
ATOM   20604 H  HG22 . THR   D  4  78  ? 21.119  -53.000 -46.322  1.00 82.16  ? 78   THR   D HG22 1 
ATOM   20605 H  HG23 . THR   D  4  78  ? 21.657  -52.093 -47.496  1.00 82.16  ? 78   THR   D HG23 1 
ATOM   20606 N  N    . ALA   D  4  79  ? 18.788  -51.344 -45.801  1.00 58.54  ? 79   ALA   D N    1 
ATOM   20607 C  CA   . ALA   D  4  79  ? 17.639  -52.166 -45.453  1.00 61.60  ? 79   ALA   D CA   1 
ATOM   20608 C  C    . ALA   D  4  79  ? 17.810  -53.548 -46.068  1.00 66.36  ? 79   ALA   D C    1 
ATOM   20609 O  O    . ALA   D  4  79  ? 18.327  -53.684 -47.182  1.00 68.70  ? 79   ALA   D O    1 
ATOM   20610 C  CB   . ALA   D  4  79  ? 16.337  -51.531 -45.943  1.00 58.48  ? 79   ALA   D CB   1 
ATOM   20611 H  H    . ALA   D  4  79  ? 18.757  -51.035 -46.602  1.00 70.23  ? 79   ALA   D H    1 
ATOM   20612 H  HA   . ALA   D  4  79  ? 17.578  -52.256 -44.489  1.00 73.90  ? 79   ALA   D HA   1 
ATOM   20613 H  HB1  . ALA   D  4  79  ? 15.593  -52.099 -45.689  1.00 70.15  ? 79   ALA   D HB1  1 
ATOM   20614 H  HB2  . ALA   D  4  79  ? 16.239  -50.656 -45.535  1.00 70.15  ? 79   ALA   D HB2  1 
ATOM   20615 H  HB3  . ALA   D  4  79  ? 16.372  -51.443 -46.908  1.00 70.15  ? 79   ALA   D HB3  1 
ATOM   20616 N  N    . TYR   D  4  80  ? 17.381  -54.571 -45.337  1.00 66.39  ? 80   TYR   D N    1 
ATOM   20617 C  CA   . TYR   D  4  80  ? 17.503  -55.950 -45.778  1.00 65.83  ? 80   TYR   D CA   1 
ATOM   20618 C  C    . TYR   D  4  80  ? 16.136  -56.617 -45.756  1.00 65.73  ? 80   TYR   D C    1 
ATOM   20619 O  O    . TYR   D  4  80  ? 15.279  -56.286 -44.931  1.00 68.54  ? 80   TYR   D O    1 
ATOM   20620 C  CB   . TYR   D  4  80  ? 18.465  -56.750 -44.888  1.00 64.88  ? 80   TYR   D CB   1 
ATOM   20621 C  CG   . TYR   D  4  80  ? 19.876  -56.207 -44.820  1.00 63.77  ? 80   TYR   D CG   1 
ATOM   20622 C  CD1  . TYR   D  4  80  ? 20.229  -55.249 -43.877  1.00 62.67  ? 80   TYR   D CD1  1 
ATOM   20623 C  CD2  . TYR   D  4  80  ? 20.861  -56.667 -45.686  1.00 62.79  ? 80   TYR   D CD2  1 
ATOM   20624 C  CE1  . TYR   D  4  80  ? 21.519  -54.756 -43.806  1.00 66.23  ? 80   TYR   D CE1  1 
ATOM   20625 C  CE2  . TYR   D  4  80  ? 22.154  -56.180 -45.622  1.00 63.98  ? 80   TYR   D CE2  1 
ATOM   20626 C  CZ   . TYR   D  4  80  ? 22.477  -55.226 -44.680  1.00 67.69  ? 80   TYR   D CZ   1 
ATOM   20627 O  OH   . TYR   D  4  80  ? 23.763  -54.738 -44.612  1.00 73.09  ? 80   TYR   D OH   1 
ATOM   20628 H  H    . TYR   D  4  80  ? 17.009  -54.487 -44.566  1.00 79.65  ? 80   TYR   D H    1 
ATOM   20629 H  HA   . TYR   D  4  80  ? 17.846  -55.963 -46.685  1.00 78.97  ? 80   TYR   D HA   1 
ATOM   20630 H  HB2  . TYR   D  4  80  ? 18.113  -56.758 -43.984  1.00 77.84  ? 80   TYR   D HB2  1 
ATOM   20631 H  HB3  . TYR   D  4  80  ? 18.519  -57.656 -45.230  1.00 77.84  ? 80   TYR   D HB3  1 
ATOM   20632 H  HD1  . TYR   D  4  80  ? 19.586  -54.933 -43.284  1.00 75.19  ? 80   TYR   D HD1  1 
ATOM   20633 H  HD2  . TYR   D  4  80  ? 20.648  -57.313 -46.319  1.00 75.33  ? 80   TYR   D HD2  1 
ATOM   20634 H  HE1  . TYR   D  4  80  ? 21.739  -54.112 -43.172  1.00 79.46  ? 80   TYR   D HE1  1 
ATOM   20635 H  HE2  . TYR   D  4  80  ? 22.802  -56.494 -46.210  1.00 76.75  ? 80   TYR   D HE2  1 
ATOM   20636 H  HH   . TYR   D  4  80  ? 24.249  -55.130 -45.174  1.00 87.69  ? 80   TYR   D HH   1 
ATOM   20637 N  N    . MET   D  4  81  ? 15.937  -57.557 -46.675  1.00 63.09  ? 81   MET   D N    1 
ATOM   20638 C  CA   . MET   D  4  81  ? 14.779  -58.439 -46.650  1.00 64.36  ? 81   MET   D CA   1 
ATOM   20639 C  C    . MET   D  4  81  ? 15.245  -59.865 -46.894  1.00 65.52  ? 81   MET   D C    1 
ATOM   20640 O  O    . MET   D  4  81  ? 16.058  -60.113 -47.789  1.00 63.74  ? 81   MET   D O    1 
ATOM   20641 C  CB   . MET   D  4  81  ? 13.734  -58.056 -47.700  1.00 63.90  ? 81   MET   D CB   1 
ATOM   20642 C  CG   . MET   D  4  81  ? 12.493  -58.937 -47.643  1.00 71.17  ? 81   MET   D CG   1 
ATOM   20643 S  SD   . MET   D  4  81  ? 11.197  -58.430 -48.783  1.00 86.91  ? 81   MET   D SD   1 
ATOM   20644 C  CE   . MET   D  4  81  ? 11.996  -58.762 -50.350  1.00 91.18  ? 81   MET   D CE   1 
ATOM   20645 H  H    . MET   D  4  81  ? 16.469  -57.705 -47.335  1.00 75.69  ? 81   MET   D H    1 
ATOM   20646 H  HA   . MET   D  4  81  ? 14.353  -58.372 -45.782  1.00 77.22  ? 81   MET   D HA   1 
ATOM   20647 H  HB2  . MET   D  4  81  ? 13.459  -57.138 -47.552  1.00 76.66  ? 81   MET   D HB2  1 
ATOM   20648 H  HB3  . MET   D  4  81  ? 14.126  -58.146 -48.583  1.00 76.66  ? 81   MET   D HB3  1 
ATOM   20649 H  HG2  . MET   D  4  81  ? 12.745  -59.847 -47.865  1.00 85.38  ? 81   MET   D HG2  1 
ATOM   20650 H  HG3  . MET   D  4  81  ? 12.128  -58.904 -46.745  1.00 85.38  ? 81   MET   D HG3  1 
ATOM   20651 H  HE1  . MET   D  4  81  ? 11.388  -58.531 -51.070  1.00 109.39 ? 81   MET   D HE1  1 
ATOM   20652 H  HE2  . MET   D  4  81  ? 12.802  -58.225 -50.414  1.00 109.39 ? 81   MET   D HE2  1 
ATOM   20653 H  HE3  . MET   D  4  81  ? 12.222  -59.704 -50.396  1.00 109.39 ? 81   MET   D HE3  1 
ATOM   20654 N  N    . GLN   D  4  82  ? 14.722  -60.795 -46.101  1.00 66.55  ? 82   GLN   D N    1 
ATOM   20655 C  CA   . GLN   D  4  82  ? 15.030  -62.210 -46.235  1.00 70.33  ? 82   GLN   D CA   1 
ATOM   20656 C  C    . GLN   D  4  82  ? 13.759  -62.961 -46.599  1.00 75.65  ? 82   GLN   D C    1 
ATOM   20657 O  O    . GLN   D  4  82  ? 12.732  -62.812 -45.929  1.00 78.77  ? 82   GLN   D O    1 
ATOM   20658 C  CB   . GLN   D  4  82  ? 15.626  -62.770 -44.943  1.00 71.57  ? 82   GLN   D CB   1 
ATOM   20659 C  CG   . GLN   D  4  82  ? 16.169  -64.179 -45.082  1.00 75.30  ? 82   GLN   D CG   1 
ATOM   20660 C  CD   . GLN   D  4  82  ? 16.799  -64.689 -43.801  1.00 78.34  ? 82   GLN   D CD   1 
ATOM   20661 O  OE1  . GLN   D  4  82  ? 16.221  -64.573 -42.720  1.00 77.51  ? 82   GLN   D OE1  1 
ATOM   20662 N  NE2  . GLN   D  4  82  ? 17.997  -65.250 -43.915  1.00 81.14  ? 82   GLN   D NE2  1 
ATOM   20663 H  H    . GLN   D  4  82  ? 14.173  -60.624 -45.461  1.00 79.84  ? 82   GLN   D H    1 
ATOM   20664 H  HA   . GLN   D  4  82  ? 15.677  -62.338 -46.947  1.00 84.37  ? 82   GLN   D HA   1 
ATOM   20665 H  HB2  . GLN   D  4  82  ? 16.356  -62.197 -44.662  1.00 85.86  ? 82   GLN   D HB2  1 
ATOM   20666 H  HB3  . GLN   D  4  82  ? 14.935  -62.785 -44.262  1.00 85.86  ? 82   GLN   D HB3  1 
ATOM   20667 H  HG2  . GLN   D  4  82  ? 15.443  -64.777 -45.318  1.00 90.34  ? 82   GLN   D HG2  1 
ATOM   20668 H  HG3  . GLN   D  4  82  ? 16.847  -64.190 -45.776  1.00 90.34  ? 82   GLN   D HG3  1 
ATOM   20669 H  HE21 . GLN   D  4  82  ? 18.372  -65.308 -44.687  1.00 97.35  ? 82   GLN   D HE21 1 
ATOM   20670 H  HE22 . GLN   D  4  82  ? 18.397  -65.555 -43.218  1.00 97.35  ? 82   GLN   D HE22 1 
ATOM   20671 N  N    . LEU   D  4  83  ? 13.832  -63.758 -47.660  1.00 76.78  ? 83   LEU   D N    1 
ATOM   20672 C  CA   . LEU   D  4  83  ? 12.735  -64.610 -48.098  1.00 75.73  ? 83   LEU   D CA   1 
ATOM   20673 C  C    . LEU   D  4  83  ? 13.073  -66.047 -47.730  1.00 76.92  ? 83   LEU   D C    1 
ATOM   20674 O  O    . LEU   D  4  83  ? 14.072  -66.593 -48.210  1.00 79.38  ? 83   LEU   D O    1 
ATOM   20675 C  CB   . LEU   D  4  83  ? 12.506  -64.473 -49.601  1.00 72.64  ? 83   LEU   D CB   1 
ATOM   20676 C  CG   . LEU   D  4  83  ? 12.203  -63.052 -50.079  1.00 71.17  ? 83   LEU   D CG   1 
ATOM   20677 C  CD1  . LEU   D  4  83  ? 12.210  -62.984 -51.595  1.00 71.33  ? 83   LEU   D CD1  1 
ATOM   20678 C  CD2  . LEU   D  4  83  ? 10.869  -62.574 -49.524  1.00 68.88  ? 83   LEU   D CD2  1 
ATOM   20679 H  H    . LEU   D  4  83  ? 14.531  -63.823 -48.158  1.00 92.12  ? 83   LEU   D H    1 
ATOM   20680 H  HA   . LEU   D  4  83  ? 11.916  -64.357 -47.644  1.00 90.86  ? 83   LEU   D HA   1 
ATOM   20681 H  HB2  . LEU   D  4  83  ? 13.305  -64.772 -50.062  1.00 87.15  ? 83   LEU   D HB2  1 
ATOM   20682 H  HB3  . LEU   D  4  83  ? 11.752  -65.030 -49.849  1.00 87.15  ? 83   LEU   D HB3  1 
ATOM   20683 H  HG   . LEU   D  4  83  ? 12.895  -62.455 -49.751  1.00 85.38  ? 83   LEU   D HG   1 
ATOM   20684 H  HD11 . LEU   D  4  83  ? 12.016  -62.074 -51.871  1.00 85.58  ? 83   LEU   D HD11 1 
ATOM   20685 H  HD12 . LEU   D  4  83  ? 13.086  -63.248 -51.919  1.00 85.58  ? 83   LEU   D HD12 1 
ATOM   20686 H  HD13 . LEU   D  4  83  ? 11.534  -63.586 -51.941  1.00 85.58  ? 83   LEU   D HD13 1 
ATOM   20687 H  HD21 . LEU   D  4  83  ? 10.688  -61.682 -49.860  1.00 82.63  ? 83   LEU   D HD21 1 
ATOM   20688 H  HD22 . LEU   D  4  83  ? 10.172  -63.184 -49.811  1.00 82.63  ? 83   LEU   D HD22 1 
ATOM   20689 H  HD23 . LEU   D  4  83  ? 10.917  -62.560 -48.555  1.00 82.63  ? 83   LEU   D HD23 1 
ATOM   20690 N  N    . SER   D  4  84  ? 12.248  -66.652 -46.881  1.00 77.99  ? 84   SER   D N    1 
ATOM   20691 C  CA   . SER   D  4  84  ? 12.487  -67.991 -46.368  1.00 83.79  ? 84   SER   D CA   1 
ATOM   20692 C  C    . SER   D  4  84  ? 11.453  -68.968 -46.914  1.00 83.37  ? 84   SER   D C    1 
ATOM   20693 O  O    . SER   D  4  84  ? 10.367  -68.582 -47.354  1.00 79.32  ? 84   SER   D O    1 
ATOM   20694 C  CB   . SER   D  4  84  ? 12.460  -67.996 -44.835  1.00 90.68  ? 84   SER   D CB   1 
ATOM   20695 O  OG   . SER   D  4  84  ? 11.308  -67.334 -44.342  1.00 95.06  ? 84   SER   D OG   1 
ATOM   20696 H  H    . SER   D  4  84  ? 11.525  -66.295 -46.582  1.00 93.57  ? 84   SER   D H    1 
ATOM   20697 H  HA   . SER   D  4  84  ? 13.361  -68.295 -46.659  1.00 100.53 ? 84   SER   D HA   1 
ATOM   20698 H  HB2  . SER   D  4  84  ? 12.453  -68.914 -44.523  1.00 108.80 ? 84   SER   D HB2  1 
ATOM   20699 H  HB3  . SER   D  4  84  ? 13.250  -67.540 -44.505  1.00 108.80 ? 84   SER   D HB3  1 
ATOM   20700 H  HG   . SER   D  4  84  ? 11.330  -67.306 -43.502  1.00 114.05 ? 84   SER   D HG   1 
ATOM   20701 N  N    . GLY   D  4  85  ? 11.811  -70.251 -46.879  1.00 87.82  ? 85   GLY   D N    1 
ATOM   20702 C  CA   . GLY   D  4  85  ? 10.945  -71.299 -47.385  1.00 89.62  ? 85   GLY   D CA   1 
ATOM   20703 C  C    . GLY   D  4  85  ? 10.572  -71.081 -48.837  1.00 87.82  ? 85   GLY   D C    1 
ATOM   20704 O  O    . GLY   D  4  85  ? 9.390   -71.095 -49.195  1.00 88.90  ? 85   GLY   D O    1 
ATOM   20705 H  H    . GLY   D  4  85  ? 12.558  -70.538 -46.563  1.00 105.36 ? 85   GLY   D H    1 
ATOM   20706 H  HA2  . GLY   D  4  85  ? 11.396  -72.154 -47.310  1.00 107.52 ? 85   GLY   D HA2  1 
ATOM   20707 H  HA3  . GLY   D  4  85  ? 10.130  -71.325 -46.860  1.00 107.52 ? 85   GLY   D HA3  1 
ATOM   20708 N  N    . LEU   D  4  86  ? 11.579  -70.893 -49.683  1.00 86.81  ? 86   LEU   D N    1 
ATOM   20709 C  CA   . LEU   D  4  86  ? 11.348  -70.434 -51.044  1.00 86.63  ? 86   LEU   D CA   1 
ATOM   20710 C  C    . LEU   D  4  86  ? 10.620  -71.479 -51.882  1.00 91.01  ? 86   LEU   D C    1 
ATOM   20711 O  O    . LEU   D  4  86  ? 10.776  -72.689 -51.693  1.00 92.72  ? 86   LEU   D O    1 
ATOM   20712 C  CB   . LEU   D  4  86  ? 12.675  -70.074 -51.711  1.00 86.97  ? 86   LEU   D CB   1 
ATOM   20713 C  CG   . LEU   D  4  86  ? 13.317  -68.772 -51.229  1.00 87.12  ? 86   LEU   D CG   1 
ATOM   20714 C  CD1  . LEU   D  4  86  ? 14.755  -68.680 -51.705  1.00 86.01  ? 86   LEU   D CD1  1 
ATOM   20715 C  CD2  . LEU   D  4  86  ? 12.518  -67.572 -51.713  1.00 84.52  ? 86   LEU   D CD2  1 
ATOM   20716 H  H    . LEU   D  4  86  ? 12.408  -71.025 -49.493  1.00 104.15 ? 86   LEU   D H    1 
ATOM   20717 H  HA   . LEU   D  4  86  ? 10.786  -69.644 -51.014  1.00 103.94 ? 86   LEU   D HA   1 
ATOM   20718 H  HB2  . LEU   D  4  86  ? 13.307  -70.790 -51.540  1.00 104.34 ? 86   LEU   D HB2  1 
ATOM   20719 H  HB3  . LEU   D  4  86  ? 12.523  -69.986 -52.665  1.00 104.34 ? 86   LEU   D HB3  1 
ATOM   20720 H  HG   . LEU   D  4  86  ? 13.320  -68.762 -50.259  1.00 104.53 ? 86   LEU   D HG   1 
ATOM   20721 H  HD11 . LEU   D  4  86  ? 15.145  -67.855 -51.376  1.00 103.19 ? 86   LEU   D HD11 1 
ATOM   20722 H  HD12 . LEU   D  4  86  ? 15.251  -69.440 -51.362  1.00 103.19 ? 86   LEU   D HD12 1 
ATOM   20723 H  HD13 . LEU   D  4  86  ? 14.768  -68.688 -52.675  1.00 103.19 ? 86   LEU   D HD13 1 
ATOM   20724 H  HD21 . LEU   D  4  86  ? 12.960  -66.759 -51.421  1.00 101.41 ? 86   LEU   D HD21 1 
ATOM   20725 H  HD22 . LEU   D  4  86  ? 12.471  -67.593 -52.682  1.00 101.41 ? 86   LEU   D HD22 1 
ATOM   20726 H  HD23 . LEU   D  4  86  ? 11.625  -67.615 -51.338  1.00 101.41 ? 86   LEU   D HD23 1 
ATOM   20727 N  N    . THR   D  4  87  ? 9.813   -70.986 -52.821  1.00 92.43  ? 87   THR   D N    1 
ATOM   20728 C  CA   . THR   D  4  87  ? 9.135   -71.823 -53.801  1.00 94.37  ? 87   THR   D CA   1 
ATOM   20729 C  C    . THR   D  4  87  ? 9.297   -71.192 -55.179  1.00 94.69  ? 87   THR   D C    1 
ATOM   20730 O  O    . THR   D  4  87  ? 10.045  -70.222 -55.334  1.00 91.21  ? 87   THR   D O    1 
ATOM   20731 C  CB   . THR   D  4  87  ? 7.652   -71.980 -53.460  1.00 92.25  ? 87   THR   D CB   1 
ATOM   20732 O  OG1  . THR   D  4  87  ? 6.971   -70.743 -53.698  1.00 90.50  ? 87   THR   D OG1  1 
ATOM   20733 C  CG2  . THR   D  4  87  ? 7.471   -72.378 -52.000  1.00 93.53  ? 87   THR   D CG2  1 
ATOM   20734 H  H    . THR   D  4  87  ? 9.640   -70.149 -52.912  1.00 110.89 ? 87   THR   D H    1 
ATOM   20735 H  HA   . THR   D  4  87  ? 9.521   -72.713 -53.800  1.00 113.22 ? 87   THR   D HA   1 
ATOM   20736 H  HB   . THR   D  4  87  ? 7.268   -72.677 -54.015  1.00 110.68 ? 87   THR   D HB   1 
ATOM   20737 H  HG1  . THR   D  4  87  ? 6.155   -70.825 -53.520  1.00 108.58 ? 87   THR   D HG1  1 
ATOM   20738 H  HG21 . THR   D  4  87  ? 6.529   -72.497 -51.803  1.00 112.22 ? 87   THR   D HG21 1 
ATOM   20739 H  HG22 . THR   D  4  87  ? 7.938   -73.209 -51.823  1.00 112.22 ? 87   THR   D HG22 1 
ATOM   20740 H  HG23 . THR   D  4  87  ? 7.829   -71.686 -51.421  1.00 112.22 ? 87   THR   D HG23 1 
ATOM   20741 N  N    . SER   D  4  88  ? 8.603   -71.728 -56.185  1.00 97.58  ? 88   SER   D N    1 
ATOM   20742 C  CA   . SER   D  4  88  ? 8.638   -71.105 -57.504  1.00 92.85  ? 88   SER   D CA   1 
ATOM   20743 C  C    . SER   D  4  88  ? 7.798   -69.835 -57.540  1.00 88.94  ? 88   SER   D C    1 
ATOM   20744 O  O    . SER   D  4  88  ? 8.070   -68.935 -58.344  1.00 85.50  ? 88   SER   D O    1 
ATOM   20745 C  CB   . SER   D  4  88  ? 8.153   -72.089 -58.567  1.00 93.80  ? 88   SER   D CB   1 
ATOM   20746 O  OG   . SER   D  4  88  ? 6.797   -72.440 -58.357  1.00 96.84  ? 88   SER   D OG   1 
ATOM   20747 H  H    . SER   D  4  88  ? 8.116   -72.434 -56.130  1.00 117.08 ? 88   SER   D H    1 
ATOM   20748 H  HA   . SER   D  4  88  ? 9.555   -70.868 -57.713  1.00 111.41 ? 88   SER   D HA   1 
ATOM   20749 H  HB2  . SER   D  4  88  ? 8.240   -71.677 -59.440  1.00 112.54 ? 88   SER   D HB2  1 
ATOM   20750 H  HB3  . SER   D  4  88  ? 8.697   -72.892 -58.523  1.00 112.54 ? 88   SER   D HB3  1 
ATOM   20751 H  HG   . SER   D  4  88  ? 6.551   -72.994 -58.939  1.00 116.19 ? 88   SER   D HG   1 
ATOM   20752 N  N    . GLU   D  4  89  ? 6.777   -69.744 -56.684  1.00 88.92  ? 89   GLU   D N    1 
ATOM   20753 C  CA   . GLU   D  4  89  ? 5.954   -68.542 -56.621  1.00 88.39  ? 89   GLU   D CA   1 
ATOM   20754 C  C    . GLU   D  4  89  ? 6.712   -67.351 -56.052  1.00 84.95  ? 89   GLU   D C    1 
ATOM   20755 O  O    . GLU   D  4  89  ? 6.269   -66.211 -56.226  1.00 84.50  ? 89   GLU   D O    1 
ATOM   20756 C  CB   . GLU   D  4  89  ? 4.704   -68.811 -55.781  1.00 96.42  ? 89   GLU   D CB   1 
ATOM   20757 C  CG   . GLU   D  4  89  ? 3.713   -69.759 -56.436  1.00 108.93 ? 89   GLU   D CG   1 
ATOM   20758 C  CD   . GLU   D  4  89  ? 2.544   -69.034 -57.070  1.00 119.88 ? 89   GLU   D CD   1 
ATOM   20759 O  OE1  . GLU   D  4  89  ? 1.815   -68.329 -56.341  1.00 124.09 ? 89   GLU   D OE1  1 
ATOM   20760 O  OE2  . GLU   D  4  89  ? 2.359   -69.162 -58.298  1.00 124.14 ? 89   GLU   D OE2  1 
ATOM   20761 H  H    . GLU   D  4  89  ? 6.545   -70.361 -56.133  1.00 106.69 ? 89   GLU   D H    1 
ATOM   20762 H  HA   . GLU   D  4  89  ? 5.670   -68.312 -57.519  1.00 106.05 ? 89   GLU   D HA   1 
ATOM   20763 H  HB2  . GLU   D  4  89  ? 4.974   -69.203 -54.937  1.00 115.68 ? 89   GLU   D HB2  1 
ATOM   20764 H  HB3  . GLU   D  4  89  ? 4.247   -67.969 -55.625  1.00 115.68 ? 89   GLU   D HB3  1 
ATOM   20765 H  HG2  . GLU   D  4  89  ? 4.168   -70.262 -57.130  1.00 130.70 ? 89   GLU   D HG2  1 
ATOM   20766 H  HG3  . GLU   D  4  89  ? 3.363   -70.365 -55.764  1.00 130.70 ? 89   GLU   D HG3  1 
ATOM   20767 N  N    . ASP   D  4  90  ? 7.835   -67.586 -55.375  1.00 83.33  ? 90   ASP   D N    1 
ATOM   20768 C  CA   . ASP   D  4  90  ? 8.665   -66.505 -54.862  1.00 80.29  ? 90   ASP   D CA   1 
ATOM   20769 C  C    . ASP   D  4  90  ? 9.652   -65.978 -55.894  1.00 77.44  ? 90   ASP   D C    1 
ATOM   20770 O  O    . ASP   D  4  90  ? 10.272  -64.935 -55.657  1.00 77.00  ? 90   ASP   D O    1 
ATOM   20771 C  CB   . ASP   D  4  90  ? 9.433   -66.971 -53.620  1.00 83.61  ? 90   ASP   D CB   1 
ATOM   20772 C  CG   . ASP   D  4  90  ? 8.516   -67.302 -52.461  1.00 88.57  ? 90   ASP   D CG   1 
ATOM   20773 O  OD1  . ASP   D  4  90  ? 7.464   -66.643 -52.327  1.00 89.41  ? 90   ASP   D OD1  1 
ATOM   20774 O  OD2  . ASP   D  4  90  ? 8.849   -68.222 -51.685  1.00 91.52  ? 90   ASP   D OD2  1 
ATOM   20775 H  H    . ASP   D  4  90  ? 8.138   -68.371 -55.199  1.00 99.98  ? 90   ASP   D H    1 
ATOM   20776 H  HA   . ASP   D  4  90  ? 8.089   -65.771 -54.597  1.00 96.32  ? 90   ASP   D HA   1 
ATOM   20777 H  HB2  . ASP   D  4  90  ? 9.939   -67.768 -53.841  1.00 100.31 ? 90   ASP   D HB2  1 
ATOM   20778 H  HB3  . ASP   D  4  90  ? 10.033  -66.264 -53.336  1.00 100.31 ? 90   ASP   D HB3  1 
ATOM   20779 N  N    . SER   D  4  91  ? 9.817   -66.665 -57.022  1.00 75.52  ? 91   SER   D N    1 
ATOM   20780 C  CA   . SER   D  4  91  ? 10.683  -66.182 -58.092  1.00 74.14  ? 91   SER   D CA   1 
ATOM   20781 C  C    . SER   D  4  91  ? 10.074  -64.918 -58.688  1.00 74.03  ? 91   SER   D C    1 
ATOM   20782 O  O    . SER   D  4  91  ? 9.017   -64.971 -59.323  1.00 74.13  ? 91   SER   D O    1 
ATOM   20783 C  CB   . SER   D  4  91  ? 10.858  -67.260 -59.156  1.00 74.80  ? 91   SER   D CB   1 
ATOM   20784 O  OG   . SER   D  4  91  ? 11.469  -68.418 -58.614  1.00 80.12  ? 91   SER   D OG   1 
ATOM   20785 H  H    . SER   D  4  91  ? 9.436   -67.418 -57.191  1.00 90.61  ? 91   SER   D H    1 
ATOM   20786 H  HA   . SER   D  4  91  ? 11.558  -65.970 -57.732  1.00 88.94  ? 91   SER   D HA   1 
ATOM   20787 H  HB2  . SER   D  4  91  ? 9.986   -67.500 -59.508  1.00 89.74  ? 91   SER   D HB2  1 
ATOM   20788 H  HB3  . SER   D  4  91  ? 11.419  -66.912 -59.867  1.00 89.74  ? 91   SER   D HB3  1 
ATOM   20789 H  HG   . SER   D  4  91  ? 11.455  -69.041 -59.178  1.00 96.13  ? 91   SER   D HG   1 
ATOM   20790 N  N    . ALA   D  4  92  ? 10.731  -63.782 -58.484  1.00 74.33  ? 92   ALA   D N    1 
ATOM   20791 C  CA   . ALA   D  4  92  ? 10.200  -62.499 -58.930  1.00 75.47  ? 92   ALA   D CA   1 
ATOM   20792 C  C    . ALA   D  4  92  ? 11.250  -61.426 -58.667  1.00 69.57  ? 92   ALA   D C    1 
ATOM   20793 O  O    . ALA   D  4  92  ? 12.319  -61.696 -58.109  1.00 69.05  ? 92   ALA   D O    1 
ATOM   20794 C  CB   . ALA   D  4  92  ? 8.884   -62.171 -58.222  1.00 81.75  ? 92   ALA   D CB   1 
ATOM   20795 H  H    . ALA   D  4  92  ? 11.492  -63.728 -58.086  1.00 89.18  ? 92   ALA   D H    1 
ATOM   20796 H  HA   . ALA   D  4  92  ? 10.044  -62.539 -59.886  1.00 90.54  ? 92   ALA   D HA   1 
ATOM   20797 H  HB1  . ALA   D  4  92  ? 8.581   -61.295 -58.508  1.00 98.08  ? 92   ALA   D HB1  1 
ATOM   20798 H  HB2  . ALA   D  4  92  ? 8.224   -62.842 -58.456  1.00 98.08  ? 92   ALA   D HB2  1 
ATOM   20799 H  HB3  . ALA   D  4  92  ? 9.032   -62.173 -57.263  1.00 98.08  ? 92   ALA   D HB3  1 
ATOM   20800 N  N    . VAL   D  4  93  ? 10.932  -60.202 -59.078  1.00 65.80  ? 93   VAL   D N    1 
ATOM   20801 C  CA   . VAL   D  4  93  ? 11.759  -59.036 -58.788  1.00 68.46  ? 93   VAL   D CA   1 
ATOM   20802 C  C    . VAL   D  4  93  ? 11.219  -58.370 -57.531  1.00 63.93  ? 93   VAL   D C    1 
ATOM   20803 O  O    . VAL   D  4  93  ? 10.005  -58.185 -57.388  1.00 62.38  ? 93   VAL   D O    1 
ATOM   20804 C  CB   . VAL   D  4  93  ? 11.766  -58.057 -59.974  1.00 77.67  ? 93   VAL   D CB   1 
ATOM   20805 C  CG1  . VAL   D  4  93  ? 12.530  -56.784 -59.620  1.00 80.13  ? 93   VAL   D CG1  1 
ATOM   20806 C  CG2  . VAL   D  4  93  ? 12.371  -58.717 -61.203  1.00 81.52  ? 93   VAL   D CG2  1 
ATOM   20807 H  H    . VAL   D  4  93  ? 10.228  -60.018 -59.536  1.00 78.94  ? 93   VAL   D H    1 
ATOM   20808 H  HA   . VAL   D  4  93  ? 12.673  -59.318 -58.624  1.00 82.14  ? 93   VAL   D HA   1 
ATOM   20809 H  HB   . VAL   D  4  93  ? 10.851  -57.810 -60.179  1.00 93.19  ? 93   VAL   D HB   1 
ATOM   20810 H  HG11 . VAL   D  4  93  ? 12.599  -56.227 -60.411  1.00 96.14  ? 93   VAL   D HG11 1 
ATOM   20811 H  HG12 . VAL   D  4  93  ? 12.050  -56.311 -58.922  1.00 96.14  ? 93   VAL   D HG12 1 
ATOM   20812 H  HG13 . VAL   D  4  93  ? 13.416  -57.024 -59.307  1.00 96.14  ? 93   VAL   D HG13 1 
ATOM   20813 H  HG21 . VAL   D  4  93  ? 12.372  -58.080 -61.935  1.00 97.80  ? 93   VAL   D HG21 1 
ATOM   20814 H  HG22 . VAL   D  4  93  ? 13.279  -58.990 -61.000  1.00 97.80  ? 93   VAL   D HG22 1 
ATOM   20815 H  HG23 . VAL   D  4  93  ? 11.837  -59.492 -61.440  1.00 97.80  ? 93   VAL   D HG23 1 
ATOM   20816 N  N    . TYR   D  4  94  ? 12.119  -58.007 -56.620  1.00 63.15  ? 94   TYR   D N    1 
ATOM   20817 C  CA   . TYR   D  4  94  ? 11.753  -57.414 -55.340  1.00 65.00  ? 94   TYR   D CA   1 
ATOM   20818 C  C    . TYR   D  4  94  ? 12.363  -56.023 -55.246  1.00 68.47  ? 94   TYR   D C    1 
ATOM   20819 O  O    . TYR   D  4  94  ? 13.588  -55.875 -55.292  1.00 68.85  ? 94   TYR   D O    1 
ATOM   20820 C  CB   . TYR   D  4  94  ? 12.218  -58.295 -54.179  1.00 64.00  ? 94   TYR   D CB   1 
ATOM   20821 C  CG   . TYR   D  4  94  ? 11.492  -59.620 -54.106  1.00 64.59  ? 94   TYR   D CG   1 
ATOM   20822 C  CD1  . TYR   D  4  94  ? 11.957  -60.731 -54.799  1.00 64.33  ? 94   TYR   D CD1  1 
ATOM   20823 C  CD2  . TYR   D  4  94  ? 10.336  -59.758 -53.349  1.00 66.25  ? 94   TYR   D CD2  1 
ATOM   20824 C  CE1  . TYR   D  4  94  ? 11.292  -61.942 -54.736  1.00 67.20  ? 94   TYR   D CE1  1 
ATOM   20825 C  CE2  . TYR   D  4  94  ? 9.665   -60.964 -53.280  1.00 68.37  ? 94   TYR   D CE2  1 
ATOM   20826 C  CZ   . TYR   D  4  94  ? 10.147  -62.052 -53.974  1.00 69.61  ? 94   TYR   D CZ   1 
ATOM   20827 O  OH   . TYR   D  4  94  ? 9.479   -63.253 -53.906  1.00 73.39  ? 94   TYR   D OH   1 
ATOM   20828 H  H    . TYR   D  4  94  ? 12.968  -58.097 -56.725  1.00 75.76  ? 94   TYR   D H    1 
ATOM   20829 H  HA   . TYR   D  4  94  ? 10.788  -57.321 -55.287  1.00 77.98  ? 94   TYR   D HA   1 
ATOM   20830 H  HB2  . TYR   D  4  94  ? 13.165  -58.479 -54.286  1.00 76.78  ? 94   TYR   D HB2  1 
ATOM   20831 H  HB3  . TYR   D  4  94  ? 12.064  -57.823 -53.346  1.00 76.78  ? 94   TYR   D HB3  1 
ATOM   20832 H  HD1  . TYR   D  4  94  ? 12.728  -60.659 -55.313  1.00 77.18  ? 94   TYR   D HD1  1 
ATOM   20833 H  HD2  . TYR   D  4  94  ? 10.007  -59.024 -52.881  1.00 79.48  ? 94   TYR   D HD2  1 
ATOM   20834 H  HE1  . TYR   D  4  94  ? 11.615  -62.678 -55.204  1.00 80.62  ? 94   TYR   D HE1  1 
ATOM   20835 H  HE2  . TYR   D  4  94  ? 8.894   -61.041 -52.767  1.00 82.02  ? 94   TYR   D HE2  1 
ATOM   20836 H  HH   . TYR   D  4  94  ? 9.787   -63.786 -54.477  1.00 88.05  ? 94   TYR   D HH   1 
ATOM   20837 N  N    . TYR   D  4  95  ? 11.508  -55.013 -55.116  1.00 69.38  ? 95   TYR   D N    1 
ATOM   20838 C  CA   . TYR   D  4  95  ? 11.932  -53.625 -55.035  1.00 65.81  ? 95   TYR   D CA   1 
ATOM   20839 C  C    . TYR   D  4  95  ? 11.918  -53.145 -53.591  1.00 62.02  ? 95   TYR   D C    1 
ATOM   20840 O  O    . TYR   D  4  95  ? 11.123  -53.608 -52.770  1.00 62.38  ? 95   TYR   D O    1 
ATOM   20841 C  CB   . TYR   D  4  95  ? 11.017  -52.721 -55.865  1.00 64.84  ? 95   TYR   D CB   1 
ATOM   20842 C  CG   . TYR   D  4  95  ? 11.055  -52.966 -57.355  1.00 60.75  ? 95   TYR   D CG   1 
ATOM   20843 C  CD1  . TYR   D  4  95  ? 11.974  -52.310 -58.162  1.00 59.94  ? 95   TYR   D CD1  1 
ATOM   20844 C  CD2  . TYR   D  4  95  ? 10.159  -53.838 -57.958  1.00 60.45  ? 95   TYR   D CD2  1 
ATOM   20845 C  CE1  . TYR   D  4  95  ? 12.008  -52.523 -59.528  1.00 60.94  ? 95   TYR   D CE1  1 
ATOM   20846 C  CE2  . TYR   D  4  95  ? 10.185  -54.059 -59.322  1.00 60.99  ? 95   TYR   D CE2  1 
ATOM   20847 C  CZ   . TYR   D  4  95  ? 11.111  -53.400 -60.101  1.00 61.85  ? 95   TYR   D CZ   1 
ATOM   20848 O  OH   . TYR   D  4  95  ? 11.137  -53.616 -61.460  1.00 67.77  ? 95   TYR   D OH   1 
ATOM   20849 H  H    . TYR   D  4  95  ? 10.655  -55.113 -55.071  1.00 83.24  ? 95   TYR   D H    1 
ATOM   20850 H  HA   . TYR   D  4  95  ? 12.836  -53.557 -55.380  1.00 78.95  ? 95   TYR   D HA   1 
ATOM   20851 H  HB2  . TYR   D  4  95  ? 10.103  -52.857 -55.572  1.00 77.79  ? 95   TYR   D HB2  1 
ATOM   20852 H  HB3  . TYR   D  4  95  ? 11.280  -51.799 -55.716  1.00 77.79  ? 95   TYR   D HB3  1 
ATOM   20853 H  HD1  . TYR   D  4  95  ? 12.578  -51.716 -57.778  1.00 71.91  ? 95   TYR   D HD1  1 
ATOM   20854 H  HD2  . TYR   D  4  95  ? 9.531   -54.282 -57.435  1.00 72.52  ? 95   TYR   D HD2  1 
ATOM   20855 H  HE1  . TYR   D  4  95  ? 12.631  -52.079 -60.056  1.00 73.10  ? 95   TYR   D HE1  1 
ATOM   20856 H  HE2  . TYR   D  4  95  ? 9.581   -54.649 -59.711  1.00 73.17  ? 95   TYR   D HE2  1 
ATOM   20857 H  HH   . TYR   D  4  95  ? 11.557  -52.996 -61.842  1.00 81.31  ? 95   TYR   D HH   1 
ATOM   20858 N  N    . CYS   D  4  96  ? 12.810  -52.206 -53.289  1.00 59.99  ? 96   CYS   D N    1 
ATOM   20859 C  CA   . CYS   D  4  96  ? 12.742  -51.416 -52.069  1.00 61.72  ? 96   CYS   D CA   1 
ATOM   20860 C  C    . CYS   D  4  96  ? 12.407  -49.979 -52.442  1.00 62.16  ? 96   CYS   D C    1 
ATOM   20861 O  O    . CYS   D  4  96  ? 12.934  -49.446 -53.424  1.00 60.99  ? 96   CYS   D O    1 
ATOM   20862 C  CB   . CYS   D  4  96  ? 14.056  -51.463 -51.288  1.00 64.69  ? 96   CYS   D CB   1 
ATOM   20863 S  SG   . CYS   D  4  96  ? 15.475  -50.725 -52.128  1.00 68.91  ? 96   CYS   D SG   1 
ATOM   20864 H  H    . CYS   D  4  96  ? 13.479  -52.005 -53.790  1.00 71.97  ? 96   CYS   D H    1 
ATOM   20865 H  HA   . CYS   D  4  96  ? 12.051  -51.767 -51.486  1.00 74.04  ? 96   CYS   D HA   1 
ATOM   20866 H  HB2  . CYS   D  4  96  ? 13.933  -50.987 -50.452  1.00 77.61  ? 96   CYS   D HB2  1 
ATOM   20867 H  HB3  . CYS   D  4  96  ? 14.274  -52.392 -51.112  1.00 77.61  ? 96   CYS   D HB3  1 
ATOM   20868 N  N    . ALA   D  4  97  ? 11.526  -49.358 -51.662  1.00 62.15  ? 97   ALA   D N    1 
ATOM   20869 C  CA   . ALA   D  4  97  ? 11.051  -48.015 -51.962  1.00 59.98  ? 97   ALA   D CA   1 
ATOM   20870 C  C    . ALA   D  4  97  ? 10.922  -47.219 -50.674  1.00 62.22  ? 97   ALA   D C    1 
ATOM   20871 O  O    . ALA   D  4  97  ? 10.273  -47.669 -49.725  1.00 66.26  ? 97   ALA   D O    1 
ATOM   20872 C  CB   . ALA   D  4  97  ? 9.705   -48.060 -52.696  1.00 58.03  ? 97   ALA   D CB   1 
ATOM   20873 H  H    . ALA   D  4  97  ? 11.188  -49.698 -50.949  1.00 74.57  ? 97   ALA   D H    1 
ATOM   20874 H  HA   . ALA   D  4  97  ? 11.697  -47.563 -52.527  1.00 71.96  ? 97   ALA   D HA   1 
ATOM   20875 H  HB1  . ALA   D  4  97  ? 9.438   -47.155 -52.922  1.00 69.62  ? 97   ALA   D HB1  1 
ATOM   20876 H  HB2  . ALA   D  4  97  ? 9.803   -48.587 -53.504  1.00 69.62  ? 97   ALA   D HB2  1 
ATOM   20877 H  HB3  . ALA   D  4  97  ? 9.042   -48.465 -52.116  1.00 69.62  ? 97   ALA   D HB3  1 
ATOM   20878 N  N    . SER   D  4  98  ? 11.539  -46.041 -50.646  1.00 58.42  ? 98   SER   D N    1 
ATOM   20879 C  CA   . SER   D  4  98  ? 11.450  -45.176 -49.479  1.00 57.79  ? 98   SER   D CA   1 
ATOM   20880 C  C    . SER   D  4  98  ? 10.045  -44.597 -49.354  1.00 55.36  ? 98   SER   D C    1 
ATOM   20881 O  O    . SER   D  4  98  ? 9.332   -44.413 -50.344  1.00 53.48  ? 98   SER   D O    1 
ATOM   20882 C  CB   . SER   D  4  98  ? 12.478  -44.048 -49.569  1.00 61.10  ? 98   SER   D CB   1 
ATOM   20883 O  OG   . SER   D  4  98  ? 12.206  -43.190 -50.663  1.00 63.37  ? 98   SER   D OG   1 
ATOM   20884 H  H    . SER   D  4  98  ? 12.013  -45.721 -51.289  1.00 70.09  ? 98   SER   D H    1 
ATOM   20885 H  HA   . SER   D  4  98  ? 11.641  -45.690 -48.679  1.00 69.33  ? 98   SER   D HA   1 
ATOM   20886 H  HB2  . SER   D  4  98  ? 12.448  -43.530 -48.749  1.00 73.30  ? 98   SER   D HB2  1 
ATOM   20887 H  HB3  . SER   D  4  98  ? 13.360  -44.435 -49.685  1.00 73.30  ? 98   SER   D HB3  1 
ATOM   20888 H  HG   . SER   D  4  98  ? 11.476  -42.792 -50.543  1.00 76.03  ? 98   SER   D HG   1 
ATOM   20889 N  N    . PHE   D  4  99  ? 9.649   -44.309 -48.117  1.00 53.43  ? 99   PHE   D N    1 
ATOM   20890 C  CA   . PHE   D  4  99  ? 8.304   -43.829 -47.826  1.00 51.67  ? 99   PHE   D CA   1 
ATOM   20891 C  C    . PHE   D  4  99  ? 8.276   -42.308 -47.917  1.00 54.30  ? 99   PHE   D C    1 
ATOM   20892 O  O    . PHE   D  4  99  ? 8.977   -41.619 -47.168  1.00 54.19  ? 99   PHE   D O    1 
ATOM   20893 C  CB   . PHE   D  4  99  ? 7.851   -44.298 -46.443  1.00 56.23  ? 99   PHE   D CB   1 
ATOM   20894 C  CG   . PHE   D  4  99  ? 6.379   -44.098 -46.177  1.00 58.11  ? 99   PHE   D CG   1 
ATOM   20895 C  CD1  . PHE   D  4  99  ? 5.437   -44.302 -47.175  1.00 59.91  ? 99   PHE   D CD1  1 
ATOM   20896 C  CD2  . PHE   D  4  99  ? 5.936   -43.733 -44.916  1.00 58.18  ? 99   PHE   D CD2  1 
ATOM   20897 C  CE1  . PHE   D  4  99  ? 4.089   -44.129 -46.924  1.00 61.93  ? 99   PHE   D CE1  1 
ATOM   20898 C  CE2  . PHE   D  4  99  ? 4.588   -43.558 -44.661  1.00 58.68  ? 99   PHE   D CE2  1 
ATOM   20899 C  CZ   . PHE   D  4  99  ? 3.665   -43.756 -45.665  1.00 61.20  ? 99   PHE   D CZ   1 
ATOM   20900 H  H    . PHE   D  4  99  ? 10.149  -44.385 -47.421  1.00 64.10  ? 99   PHE   D H    1 
ATOM   20901 H  HA   . PHE   D  4  99  ? 7.687   -44.183 -48.485  1.00 61.99  ? 99   PHE   D HA   1 
ATOM   20902 H  HB2  . PHE   D  4  99  ? 8.040   -45.245 -46.359  1.00 67.46  ? 99   PHE   D HB2  1 
ATOM   20903 H  HB3  . PHE   D  4  99  ? 8.342   -43.801 -45.770  1.00 67.46  ? 99   PHE   D HB3  1 
ATOM   20904 H  HD1  . PHE   D  4  99  ? 5.716   -44.559 -48.024  1.00 71.88  ? 99   PHE   D HD1  1 
ATOM   20905 H  HD2  . PHE   D  4  99  ? 6.554   -43.603 -44.233  1.00 69.80  ? 99   PHE   D HD2  1 
ATOM   20906 H  HE1  . PHE   D  4  99  ? 3.468   -44.262 -47.603  1.00 74.29  ? 99   PHE   D HE1  1 
ATOM   20907 H  HE2  . PHE   D  4  99  ? 4.305   -43.307 -43.811  1.00 70.39  ? 99   PHE   D HE2  1 
ATOM   20908 H  HZ   . PHE   D  4  99  ? 2.758   -43.640 -45.494  1.00 73.42  ? 99   PHE   D HZ   1 
ATOM   20909 N  N    . LEU   D  4  100 ? 7.466   -41.791 -48.841  1.00 59.13  ? 100  LEU   D N    1 
ATOM   20910 C  CA   . LEU   D  4  100 ? 7.313   -40.349 -48.982  1.00 60.50  ? 100  LEU   D CA   1 
ATOM   20911 C  C    . LEU   D  4  100 ? 6.495   -39.754 -47.848  1.00 60.22  ? 100  LEU   D C    1 
ATOM   20912 O  O    . LEU   D  4  100 ? 6.718   -38.601 -47.460  1.00 61.45  ? 100  LEU   D O    1 
ATOM   20913 C  CB   . LEU   D  4  100 ? 6.631   -40.032 -50.314  1.00 63.87  ? 100  LEU   D CB   1 
ATOM   20914 C  CG   . LEU   D  4  100 ? 6.261   -38.572 -50.591  1.00 66.73  ? 100  LEU   D CG   1 
ATOM   20915 C  CD1  . LEU   D  4  100 ? 7.499   -37.734 -50.843  1.00 69.77  ? 100  LEU   D CD1  1 
ATOM   20916 C  CD2  . LEU   D  4  100 ? 5.295   -38.482 -51.767  1.00 65.86  ? 100  LEU   D CD2  1 
ATOM   20917 H  H    . LEU   D  4  100 ? 6.997   -42.253 -49.395  1.00 70.94  ? 100  LEU   D H    1 
ATOM   20918 H  HA   . LEU   D  4  100 ? 8.194   -39.944 -48.971  1.00 72.58  ? 100  LEU   D HA   1 
ATOM   20919 H  HB2  . LEU   D  4  100 ? 7.229   -40.310 -51.026  1.00 76.62  ? 100  LEU   D HB2  1 
ATOM   20920 H  HB3  . LEU   D  4  100 ? 5.808   -40.543 -50.355  1.00 76.62  ? 100  LEU   D HB3  1 
ATOM   20921 H  HG   . LEU   D  4  100 ? 5.818   -38.208 -49.808  1.00 80.06  ? 100  LEU   D HG   1 
ATOM   20922 H  HD11 . LEU   D  4  100 ? 7.358   -36.845 -50.482  1.00 83.70  ? 100  LEU   D HD11 1 
ATOM   20923 H  HD12 . LEU   D  4  100 ? 8.258   -38.152 -50.405  1.00 83.70  ? 100  LEU   D HD12 1 
ATOM   20924 H  HD13 . LEU   D  4  100 ? 7.657   -37.683 -51.799  1.00 83.70  ? 100  LEU   D HD13 1 
ATOM   20925 H  HD21 . LEU   D  4  100 ? 5.229   -37.557 -52.051  1.00 79.01  ? 100  LEU   D HD21 1 
ATOM   20926 H  HD22 . LEU   D  4  100 ? 5.632   -39.028 -52.495  1.00 79.01  ? 100  LEU   D HD22 1 
ATOM   20927 H  HD23 . LEU   D  4  100 ? 4.425   -38.805 -51.486  1.00 79.01  ? 100  LEU   D HD23 1 
ATOM   20928 N  N    . GLY   D  4  101 ? 5.561   -40.521 -47.303  1.00 59.31  ? 101  GLY   D N    1 
ATOM   20929 C  CA   . GLY   D  4  101 ? 4.415   -39.964 -46.624  1.00 58.13  ? 101  GLY   D CA   1 
ATOM   20930 C  C    . GLY   D  4  101 ? 3.245   -39.847 -47.583  1.00 58.85  ? 101  GLY   D C    1 
ATOM   20931 O  O    . GLY   D  4  101 ? 3.351   -40.106 -48.785  1.00 58.58  ? 101  GLY   D O    1 
ATOM   20932 H  H    . GLY   D  4  101 ? 5.574   -41.381 -47.316  1.00 71.15  ? 101  GLY   D H    1 
ATOM   20933 H  HA2  . GLY   D  4  101 ? 4.160   -40.536 -45.884  1.00 69.74  ? 101  GLY   D HA2  1 
ATOM   20934 H  HA3  . GLY   D  4  101 ? 4.631   -39.082 -46.282  1.00 69.74  ? 101  GLY   D HA3  1 
ATOM   20935 N  N    . ARG   D  4  102 ? 2.098   -39.450 -47.040  1.00 55.89  ? 102  ARG   D N    1 
ATOM   20936 C  CA   . ARG   D  4  102 ? 0.880   -39.319 -47.837  1.00 56.16  ? 102  ARG   D CA   1 
ATOM   20937 C  C    . ARG   D  4  102 ? 0.546   -40.626 -48.555  1.00 58.81  ? 102  ARG   D C    1 
ATOM   20938 O  O    . ARG   D  4  102 ? 0.009   -40.618 -49.666  1.00 60.48  ? 102  ARG   D O    1 
ATOM   20939 C  CB   . ARG   D  4  102 ? 1.003   -38.177 -48.851  1.00 55.04  ? 102  ARG   D CB   1 
ATOM   20940 C  CG   . ARG   D  4  102 ? 1.723   -36.938 -48.326  1.00 52.93  ? 102  ARG   D CG   1 
ATOM   20941 C  CD   . ARG   D  4  102 ? 0.899   -36.176 -47.293  1.00 55.09  ? 102  ARG   D CD   1 
ATOM   20942 N  NE   . ARG   D  4  102 ? -0.061  -35.272 -47.926  1.00 62.28  ? 102  ARG   D NE   1 
ATOM   20943 C  CZ   . ARG   D  4  102 ? -1.379  -35.292 -47.735  1.00 74.14  ? 102  ARG   D CZ   1 
ATOM   20944 N  NH1  . ARG   D  4  102 ? -1.942  -36.163 -46.907  1.00 81.33  ? 102  ARG   D NH1  1 
ATOM   20945 N  NH2  . ARG   D  4  102 ? -2.141  -34.417 -48.374  1.00 80.00  ? 102  ARG   D NH2  1 
ATOM   20946 H  H    . ARG   D  4  102 ? 1.998   -39.250 -46.209  1.00 67.05  ? 102  ARG   D H    1 
ATOM   20947 H  HA   . ARG   D  4  102 ? 0.144   -39.112 -47.240  1.00 67.37  ? 102  ARG   D HA   1 
ATOM   20948 H  HB2  . ARG   D  4  102 ? 1.498   -38.499 -49.621  1.00 66.03  ? 102  ARG   D HB2  1 
ATOM   20949 H  HB3  . ARG   D  4  102 ? 0.112   -37.905 -49.121  1.00 66.03  ? 102  ARG   D HB3  1 
ATOM   20950 H  HG2  . ARG   D  4  102 ? 2.555   -37.209 -47.906  1.00 63.50  ? 102  ARG   D HG2  1 
ATOM   20951 H  HG3  . ARG   D  4  102 ? 1.906   -36.338 -49.066  1.00 63.50  ? 102  ARG   D HG3  1 
ATOM   20952 H  HD2  . ARG   D  4  102 ? 0.407   -36.808 -46.746  1.00 66.09  ? 102  ARG   D HD2  1 
ATOM   20953 H  HD3  . ARG   D  4  102 ? 1.493   -35.648 -46.736  1.00 66.09  ? 102  ARG   D HD3  1 
ATOM   20954 H  HE   . ARG   D  4  102 ? 0.251   -34.679 -48.465  1.00 74.72  ? 102  ARG   D HE   1 
ATOM   20955 H  HH11 . ARG   D  4  102 ? -1.454  -36.728 -46.481  1.00 97.58  ? 102  ARG   D HH11 1 
ATOM   20956 H  HH12 . ARG   D  4  102 ? -2.795  -36.161 -46.796  1.00 97.58  ? 102  ARG   D HH12 1 
ATOM   20957 H  HH21 . ARG   D  4  102 ? -1.785  -33.844 -48.906  1.00 95.98  ? 102  ARG   D HH21 1 
ATOM   20958 H  HH22 . ARG   D  4  102 ? -2.993  -34.423 -48.257  1.00 95.98  ? 102  ARG   D HH22 1 
ATOM   20959 N  N    . GLY   D  4  103 ? 0.878   -41.755 -47.932  1.00 58.86  ? 103  GLY   D N    1 
ATOM   20960 C  CA   . GLY   D  4  103 ? 0.561   -43.055 -48.501  1.00 56.95  ? 103  GLY   D CA   1 
ATOM   20961 C  C    . GLY   D  4  103 ? 1.185   -43.319 -49.852  1.00 56.82  ? 103  GLY   D C    1 
ATOM   20962 O  O    . GLY   D  4  103 ? 0.586   -44.018 -50.677  1.00 58.90  ? 103  GLY   D O    1 
ATOM   20963 H  H    . GLY   D  4  103 ? 1.287   -41.792 -47.177  1.00 70.61  ? 103  GLY   D H    1 
ATOM   20964 H  HA2  . GLY   D  4  103 ? 0.869   -43.745 -47.892  1.00 68.32  ? 103  GLY   D HA2  1 
ATOM   20965 H  HA3  . GLY   D  4  103 ? -0.401  -43.126 -48.599  1.00 68.32  ? 103  GLY   D HA3  1 
ATOM   20966 N  N    . ALA   D  4  104 ? 2.380   -42.789 -50.103  1.00 57.95  ? 104  ALA   D N    1 
ATOM   20967 C  CA   . ALA   D  4  104 ? 3.069   -42.977 -51.371  1.00 55.49  ? 104  ALA   D CA   1 
ATOM   20968 C  C    . ALA   D  4  104 ? 4.532   -43.313 -51.117  1.00 53.68  ? 104  ALA   D C    1 
ATOM   20969 O  O    . ALA   D  4  104 ? 5.063   -43.095 -50.026  1.00 54.86  ? 104  ALA   D O    1 
ATOM   20970 C  CB   . ALA   D  4  104 ? 2.964   -41.728 -52.258  1.00 56.39  ? 104  ALA   D CB   1 
ATOM   20971 H  H    . ALA   D  4  104 ? 2.818   -42.306 -49.542  1.00 69.52  ? 104  ALA   D H    1 
ATOM   20972 H  HA   . ALA   D  4  104 ? 2.668   -43.722 -51.845  1.00 66.57  ? 104  ALA   D HA   1 
ATOM   20973 H  HB1  . ALA   D  4  104 ? 3.419   -41.898 -53.097  1.00 67.64  ? 104  ALA   D HB1  1 
ATOM   20974 H  HB2  . ALA   D  4  104 ? 2.027   -41.536 -52.423  1.00 67.64  ? 104  ALA   D HB2  1 
ATOM   20975 H  HB3  . ALA   D  4  104 ? 3.379   -40.980 -51.801  1.00 67.64  ? 104  ALA   D HB3  1 
ATOM   20976 N  N    . MET   D  4  105 ? 5.180   -43.850 -52.148  1.00 53.34  ? 105  MET   D N    1 
ATOM   20977 C  CA   . MET   D  4  105 ? 6.582   -44.248 -52.094  1.00 56.13  ? 105  MET   D CA   1 
ATOM   20978 C  C    . MET   D  4  105 ? 7.327   -43.502 -53.193  1.00 57.51  ? 105  MET   D C    1 
ATOM   20979 O  O    . MET   D  4  105 ? 7.045   -43.697 -54.380  1.00 57.62  ? 105  MET   D O    1 
ATOM   20980 C  CB   . MET   D  4  105 ? 6.715   -45.764 -52.249  1.00 61.10  ? 105  MET   D CB   1 
ATOM   20981 C  CG   . MET   D  4  105 ? 6.054   -46.540 -51.110  1.00 67.16  ? 105  MET   D CG   1 
ATOM   20982 S  SD   . MET   D  4  105 ? 5.505   -48.199 -51.564  1.00 72.94  ? 105  MET   D SD   1 
ATOM   20983 C  CE   . MET   D  4  105 ? 4.137   -47.833 -52.663  1.00 73.77  ? 105  MET   D CE   1 
ATOM   20984 H  H    . MET   D  4  105 ? 4.816   -43.998 -52.913  1.00 63.99  ? 105  MET   D H    1 
ATOM   20985 H  HA   . MET   D  4  105 ? 6.970   -44.007 -51.238  1.00 67.34  ? 105  MET   D HA   1 
ATOM   20986 H  HB2  . MET   D  4  105 ? 6.293   -46.034 -53.079  1.00 73.30  ? 105  MET   D HB2  1 
ATOM   20987 H  HB3  . MET   D  4  105 ? 7.656   -45.998 -52.264  1.00 73.30  ? 105  MET   D HB3  1 
ATOM   20988 H  HG2  . MET   D  4  105 ? 6.692   -46.630 -50.385  1.00 80.58  ? 105  MET   D HG2  1 
ATOM   20989 H  HG3  . MET   D  4  105 ? 5.276   -46.046 -50.808  1.00 80.58  ? 105  MET   D HG3  1 
ATOM   20990 H  HE1  . MET   D  4  105 ? 3.746   -48.666 -52.969  1.00 88.50  ? 105  MET   D HE1  1 
ATOM   20991 H  HE2  . MET   D  4  105 ? 3.475   -47.314 -52.181  1.00 88.50  ? 105  MET   D HE2  1 
ATOM   20992 H  HE3  . MET   D  4  105 ? 4.468   -47.325 -53.420  1.00 88.50  ? 105  MET   D HE3  1 
ATOM   20993 N  N    . ASP   D  4  106 ? 8.278   -42.652 -52.796  1.00 57.40  ? 106  ASP   D N    1 
ATOM   20994 C  CA   . ASP   D  4  106 ? 8.820   -41.646 -53.704  1.00 60.55  ? 106  ASP   D CA   1 
ATOM   20995 C  C    . ASP   D  4  106 ? 10.054  -42.099 -54.471  1.00 56.33  ? 106  ASP   D C    1 
ATOM   20996 O  O    . ASP   D  4  106 ? 10.287  -41.608 -55.582  1.00 57.03  ? 106  ASP   D O    1 
ATOM   20997 C  CB   . ASP   D  4  106 ? 9.162   -40.363 -52.936  1.00 64.30  ? 106  ASP   D CB   1 
ATOM   20998 C  CG   . ASP   D  4  106 ? 9.942   -40.628 -51.661  1.00 64.03  ? 106  ASP   D CG   1 
ATOM   20999 O  OD1  . ASP   D  4  106 ? 10.210  -41.809 -51.355  1.00 62.63  ? 106  ASP   D OD1  1 
ATOM   21000 O  OD2  . ASP   D  4  106 ? 10.283  -39.649 -50.964  1.00 63.18  ? 106  ASP   D OD2  1 
ATOM   21001 H  H    . ASP   D  4  106 ? 8.622   -42.640 -52.008  1.00 68.85  ? 106  ASP   D H    1 
ATOM   21002 H  HA   . ASP   D  4  106 ? 8.130   -41.445 -54.355  1.00 72.64  ? 106  ASP   D HA   1 
ATOM   21003 H  HB2  . ASP   D  4  106 ? 9.702   -39.790 -53.503  1.00 77.14  ? 106  ASP   D HB2  1 
ATOM   21004 H  HB3  . ASP   D  4  106 ? 8.339   -39.910 -52.695  1.00 77.14  ? 106  ASP   D HB3  1 
ATOM   21005 N  N    . TYR   D  4  107 ? 10.858  -43.002 -53.919  1.00 56.43  ? 107  TYR   D N    1 
ATOM   21006 C  CA   . TYR   D  4  107 ? 12.087  -43.425 -54.578  1.00 57.92  ? 107  TYR   D CA   1 
ATOM   21007 C  C    . TYR   D  4  107 ? 12.208  -44.938 -54.515  1.00 56.32  ? 107  TYR   D C    1 
ATOM   21008 O  O    . TYR   D  4  107 ? 11.971  -45.546 -53.469  1.00 56.61  ? 107  TYR   D O    1 
ATOM   21009 C  CB   . TYR   D  4  107 ? 13.308  -42.751 -53.945  1.00 59.98  ? 107  TYR   D CB   1 
ATOM   21010 C  CG   . TYR   D  4  107 ? 13.308  -41.252 -54.148  1.00 61.15  ? 107  TYR   D CG   1 
ATOM   21011 C  CD1  . TYR   D  4  107 ? 13.737  -40.696 -55.346  1.00 60.77  ? 107  TYR   D CD1  1 
ATOM   21012 C  CD2  . TYR   D  4  107 ? 12.861  -40.395 -53.150  1.00 60.96  ? 107  TYR   D CD2  1 
ATOM   21013 C  CE1  . TYR   D  4  107 ? 13.730  -39.329 -55.542  1.00 63.10  ? 107  TYR   D CE1  1 
ATOM   21014 C  CE2  . TYR   D  4  107 ? 12.851  -39.027 -53.338  1.00 62.21  ? 107  TYR   D CE2  1 
ATOM   21015 C  CZ   . TYR   D  4  107 ? 13.286  -38.500 -54.536  1.00 61.77  ? 107  TYR   D CZ   1 
ATOM   21016 O  OH   . TYR   D  4  107 ? 13.278  -37.139 -54.728  1.00 60.94  ? 107  TYR   D OH   1 
ATOM   21017 H  H    . TYR   D  4  107 ? 10.713  -43.384 -53.163  1.00 67.70  ? 107  TYR   D H    1 
ATOM   21018 H  HA   . TYR   D  4  107 ? 12.062  -43.178 -55.515  1.00 69.49  ? 107  TYR   D HA   1 
ATOM   21019 H  HB2  . TYR   D  4  107 ? 13.309  -42.926 -52.990  1.00 71.95  ? 107  TYR   D HB2  1 
ATOM   21020 H  HB3  . TYR   D  4  107 ? 14.114  -43.110 -54.348  1.00 71.95  ? 107  TYR   D HB3  1 
ATOM   21021 H  HD1  . TYR   D  4  107 ? 14.033  -41.254 -56.028  1.00 72.90  ? 107  TYR   D HD1  1 
ATOM   21022 H  HD2  . TYR   D  4  107 ? 12.564  -40.748 -52.343  1.00 73.14  ? 107  TYR   D HD2  1 
ATOM   21023 H  HE1  . TYR   D  4  107 ? 14.023  -38.971 -56.348  1.00 75.70  ? 107  TYR   D HE1  1 
ATOM   21024 H  HE2  . TYR   D  4  107 ? 12.553  -38.464 -52.660  1.00 74.63  ? 107  TYR   D HE2  1 
ATOM   21025 H  HH   . TYR   D  4  107 ? 12.961  -36.755 -54.052  1.00 73.11  ? 107  TYR   D HH   1 
ATOM   21026 N  N    . TRP   D  4  108 ? 12.582  -45.534 -55.645  1.00 57.27  ? 108  TRP   D N    1 
ATOM   21027 C  CA   . TRP   D  4  108 ? 12.593  -46.977 -55.822  1.00 56.24  ? 108  TRP   D CA   1 
ATOM   21028 C  C    . TRP   D  4  108 ? 13.984  -47.451 -56.211  1.00 58.09  ? 108  TRP   D C    1 
ATOM   21029 O  O    . TRP   D  4  108 ? 14.695  -46.772 -56.959  1.00 57.75  ? 108  TRP   D O    1 
ATOM   21030 C  CB   . TRP   D  4  108 ? 11.599  -47.399 -56.907  1.00 58.64  ? 108  TRP   D CB   1 
ATOM   21031 C  CG   . TRP   D  4  108 ? 10.172  -47.198 -56.532  1.00 59.24  ? 108  TRP   D CG   1 
ATOM   21032 C  CD1  . TRP   D  4  108 ? 9.566   -46.021 -56.205  1.00 61.44  ? 108  TRP   D CD1  1 
ATOM   21033 C  CD2  . TRP   D  4  108 ? 9.160   -48.206 -56.457  1.00 57.66  ? 108  TRP   D CD2  1 
ATOM   21034 N  NE1  . TRP   D  4  108 ? 8.239   -46.236 -55.923  1.00 63.52  ? 108  TRP   D NE1  1 
ATOM   21035 C  CE2  . TRP   D  4  108 ? 7.965   -47.570 -56.072  1.00 60.71  ? 108  TRP   D CE2  1 
ATOM   21036 C  CE3  . TRP   D  4  108 ? 9.150   -49.587 -56.677  1.00 56.65  ? 108  TRP   D CE3  1 
ATOM   21037 C  CZ2  . TRP   D  4  108 ? 6.771   -48.266 -55.901  1.00 62.61  ? 108  TRP   D CZ2  1 
ATOM   21038 C  CZ3  . TRP   D  4  108 ? 7.966   -50.276 -56.508  1.00 58.65  ? 108  TRP   D CZ3  1 
ATOM   21039 C  CH2  . TRP   D  4  108 ? 6.792   -49.616 -56.124  1.00 62.02  ? 108  TRP   D CH2  1 
ATOM   21040 H  H    . TRP   D  4  108 ? 12.841  -45.106 -56.345  1.00 68.70  ? 108  TRP   D H    1 
ATOM   21041 H  HA   . TRP   D  4  108 ? 12.351  -47.400 -54.984  1.00 67.47  ? 108  TRP   D HA   1 
ATOM   21042 H  HB2  . TRP   D  4  108 ? 11.770  -46.877 -57.706  1.00 70.35  ? 108  TRP   D HB2  1 
ATOM   21043 H  HB3  . TRP   D  4  108 ? 11.725  -48.343 -57.094  1.00 70.35  ? 108  TRP   D HB3  1 
ATOM   21044 H  HD1  . TRP   D  4  108 ? 9.990   -45.194 -56.176  1.00 73.71  ? 108  TRP   D HD1  1 
ATOM   21045 H  HE1  . TRP   D  4  108 ? 7.673   -45.631 -55.690  1.00 76.20  ? 108  TRP   D HE1  1 
ATOM   21046 H  HE3  . TRP   D  4  108 ? 9.925   -50.032 -56.933  1.00 67.96  ? 108  TRP   D HE3  1 
ATOM   21047 H  HZ2  . TRP   D  4  108 ? 5.990   -47.830 -55.646  1.00 75.11  ? 108  TRP   D HZ2  1 
ATOM   21048 H  HZ3  . TRP   D  4  108 ? 7.947   -51.195 -56.651  1.00 70.36  ? 108  TRP   D HZ3  1 
ATOM   21049 H  HH2  . TRP   D  4  108 ? 6.009   -50.106 -56.017  1.00 74.41  ? 108  TRP   D HH2  1 
ATOM   21050 N  N    . GLY   D  4  109 ? 14.365  -48.623 -55.704  1.00 61.66  ? 109  GLY   D N    1 
ATOM   21051 C  CA   . GLY   D  4  109 ? 15.567  -49.277 -56.169  1.00 59.85  ? 109  GLY   D CA   1 
ATOM   21052 C  C    . GLY   D  4  109 ? 15.370  -49.908 -57.533  1.00 58.80  ? 109  GLY   D C    1 
ATOM   21053 O  O    . GLY   D  4  109 ? 14.264  -49.972 -58.069  1.00 57.69  ? 109  GLY   D O    1 
ATOM   21054 H  H    . GLY   D  4  109 ? 13.940  -49.053 -55.093  1.00 73.97  ? 109  GLY   D H    1 
ATOM   21055 H  HA2  . GLY   D  4  109 ? 16.285  -48.628 -56.230  1.00 71.80  ? 109  GLY   D HA2  1 
ATOM   21056 H  HA3  . GLY   D  4  109 ? 15.822  -49.971 -55.541  1.00 71.80  ? 109  GLY   D HA3  1 
ATOM   21057 N  N    . GLN   D  4  110 ? 16.475  -50.388 -58.107  1.00 62.41  ? 110  GLN   D N    1 
ATOM   21058 C  CA   . GLN   D  4  110 ? 16.401  -50.982 -59.437  1.00 64.70  ? 110  GLN   D CA   1 
ATOM   21059 C  C    . GLN   D  4  110 ? 15.730  -52.349 -59.419  1.00 63.49  ? 110  GLN   D C    1 
ATOM   21060 O  O    . GLN   D  4  110 ? 15.290  -52.821 -60.473  1.00 65.45  ? 110  GLN   D O    1 
ATOM   21061 C  CB   . GLN   D  4  110 ? 17.800  -51.089 -60.055  1.00 71.51  ? 110  GLN   D CB   1 
ATOM   21062 C  CG   . GLN   D  4  110 ? 18.673  -52.241 -59.549  1.00 78.60  ? 110  GLN   D CG   1 
ATOM   21063 C  CD   . GLN   D  4  110 ? 19.328  -51.954 -58.214  1.00 83.43  ? 110  GLN   D CD   1 
ATOM   21064 O  OE1  . GLN   D  4  110 ? 19.071  -50.926 -57.588  1.00 78.78  ? 110  GLN   D OE1  1 
ATOM   21065 N  NE2  . GLN   D  4  110 ? 20.190  -52.865 -57.773  1.00 91.02  ? 110  GLN   D NE2  1 
ATOM   21066 H  H    . GLN   D  4  110 ? 17.259  -50.382 -57.754  1.00 74.87  ? 110  GLN   D H    1 
ATOM   21067 H  HA   . GLN   D  4  110 ? 15.875  -50.399 -60.006  1.00 77.62  ? 110  GLN   D HA   1 
ATOM   21068 H  HB2  . GLN   D  4  110 ? 17.699  -51.205 -61.013  1.00 85.79  ? 110  GLN   D HB2  1 
ATOM   21069 H  HB3  . GLN   D  4  110 ? 18.277  -50.265 -59.869  1.00 85.79  ? 110  GLN   D HB3  1 
ATOM   21070 H  HG2  . GLN   D  4  110 ? 18.120  -53.032 -59.446  1.00 94.30  ? 110  GLN   D HG2  1 
ATOM   21071 H  HG3  . GLN   D  4  110 ? 19.376  -52.409 -60.196  1.00 94.30  ? 110  GLN   D HG3  1 
ATOM   21072 H  HE21 . GLN   D  4  110 ? 20.347  -53.569 -58.241  1.00 109.21 ? 110  GLN   D HE21 1 
ATOM   21073 H  HE22 . GLN   D  4  110 ? 20.589  -52.750 -57.020  1.00 109.21 ? 110  GLN   D HE22 1 
ATOM   21074 N  N    . GLY   D  4  111 ? 15.644  -52.989 -58.256  1.00 62.47  ? 111  GLY   D N    1 
ATOM   21075 C  CA   . GLY   D  4  111 ? 15.035  -54.299 -58.154  1.00 65.10  ? 111  GLY   D CA   1 
ATOM   21076 C  C    . GLY   D  4  111 ? 16.053  -55.415 -58.045  1.00 67.12  ? 111  GLY   D C    1 
ATOM   21077 O  O    . GLY   D  4  111 ? 17.103  -55.377 -58.695  1.00 67.33  ? 111  GLY   D O    1 
ATOM   21078 H  H    . GLY   D  4  111 ? 15.935  -52.680 -57.509  1.00 74.94  ? 111  GLY   D H    1 
ATOM   21079 H  HA2  . GLY   D  4  111 ? 14.468  -54.327 -57.368  1.00 78.10  ? 111  GLY   D HA2  1 
ATOM   21080 H  HA3  . GLY   D  4  111 ? 14.491  -54.461 -58.941  1.00 78.10  ? 111  GLY   D HA3  1 
ATOM   21081 N  N    . THR   D  4  112 ? 15.755  -56.412 -57.216  1.00 67.78  ? 112  THR   D N    1 
ATOM   21082 C  CA   . THR   D  4  112 ? 16.575  -57.609 -57.074  1.00 65.93  ? 112  THR   D CA   1 
ATOM   21083 C  C    . THR   D  4  112 ? 15.756  -58.791 -57.574  1.00 70.22  ? 112  THR   D C    1 
ATOM   21084 O  O    . THR   D  4  112 ? 14.728  -59.134 -56.979  1.00 75.99  ? 112  THR   D O    1 
ATOM   21085 C  CB   . THR   D  4  112 ? 17.003  -57.821 -55.623  1.00 62.62  ? 112  THR   D CB   1 
ATOM   21086 O  OG1  . THR   D  4  112 ? 17.871  -56.758 -55.212  1.00 65.20  ? 112  THR   D OG1  1 
ATOM   21087 C  CG2  . THR   D  4  112 ? 17.727  -59.155 -55.466  1.00 62.69  ? 112  THR   D CG2  1 
ATOM   21088 H  H    . THR   D  4  112 ? 15.059  -56.416 -56.711  1.00 81.31  ? 112  THR   D H    1 
ATOM   21089 H  HA   . THR   D  4  112 ? 17.376  -57.518 -57.615  1.00 79.10  ? 112  THR   D HA   1 
ATOM   21090 H  HB   . THR   D  4  112 ? 16.217  -57.832 -55.056  1.00 75.12  ? 112  THR   D HB   1 
ATOM   21091 H  HG1  . THR   D  4  112 ? 18.580  -56.776 -55.662  1.00 78.22  ? 112  THR   D HG1  1 
ATOM   21092 H  HG21 . THR   D  4  112 ? 18.105  -59.224 -54.575  1.00 75.21  ? 112  THR   D HG21 1 
ATOM   21093 H  HG22 . THR   D  4  112 ? 17.107  -59.887 -55.603  1.00 75.21  ? 112  THR   D HG22 1 
ATOM   21094 H  HG23 . THR   D  4  112 ? 18.443  -59.223 -56.117  1.00 75.21  ? 112  THR   D HG23 1 
ATOM   21095 N  N    . SER   D  4  113 ? 16.204  -59.407 -58.663  1.00 68.99  ? 113  SER   D N    1 
ATOM   21096 C  CA   . SER   D  4  113 ? 15.540  -60.595 -59.176  1.00 71.10  ? 113  SER   D CA   1 
ATOM   21097 C  C    . SER   D  4  113 ? 15.911  -61.805 -58.330  1.00 70.48  ? 113  SER   D C    1 
ATOM   21098 O  O    . SER   D  4  113 ? 17.068  -61.977 -57.936  1.00 68.22  ? 113  SER   D O    1 
ATOM   21099 C  CB   . SER   D  4  113 ? 15.921  -60.841 -60.636  1.00 75.38  ? 113  SER   D CB   1 
ATOM   21100 O  OG   . SER   D  4  113 ? 17.308  -61.099 -60.770  1.00 82.79  ? 113  SER   D OG   1 
ATOM   21101 H  H    . SER   D  4  113 ? 16.888  -59.156 -59.120  1.00 82.77  ? 113  SER   D H    1 
ATOM   21102 H  HA   . SER   D  4  113 ? 14.579  -60.471 -59.138  1.00 85.30  ? 113  SER   D HA   1 
ATOM   21103 H  HB2  . SER   D  4  113 ? 15.426  -61.608 -60.964  1.00 90.44  ? 113  SER   D HB2  1 
ATOM   21104 H  HB3  . SER   D  4  113 ? 15.697  -60.054 -61.156  1.00 90.44  ? 113  SER   D HB3  1 
ATOM   21105 H  HG   . SER   D  4  113 ? 17.490  -61.283 -61.569  1.00 99.32  ? 113  SER   D HG   1 
ATOM   21106 N  N    . VAL   D  4  114 ? 14.915  -62.637 -58.042  1.00 70.58  ? 114  VAL   D N    1 
ATOM   21107 C  CA   . VAL   D  4  114 ? 15.100  -63.884 -57.311  1.00 73.04  ? 114  VAL   D CA   1 
ATOM   21108 C  C    . VAL   D  4  114 ? 14.559  -65.010 -58.178  1.00 70.75  ? 114  VAL   D C    1 
ATOM   21109 O  O    . VAL   D  4  114 ? 13.431  -64.928 -58.676  1.00 66.89  ? 114  VAL   D O    1 
ATOM   21110 C  CB   . VAL   D  4  114 ? 14.394  -63.854 -55.943  1.00 77.28  ? 114  VAL   D CB   1 
ATOM   21111 C  CG1  . VAL   D  4  114 ? 14.502  -65.207 -55.251  1.00 81.14  ? 114  VAL   D CG1  1 
ATOM   21112 C  CG2  . VAL   D  4  114 ? 14.984  -62.758 -55.067  1.00 77.44  ? 114  VAL   D CG2  1 
ATOM   21113 H  H    . VAL   D  4  114 ? 14.097  -62.494 -58.267  1.00 84.67  ? 114  VAL   D H    1 
ATOM   21114 H  HA   . VAL   D  4  114 ? 16.045  -64.036 -57.156  1.00 87.63  ? 114  VAL   D HA   1 
ATOM   21115 H  HB   . VAL   D  4  114 ? 13.454  -63.661 -56.080  1.00 92.72  ? 114  VAL   D HB   1 
ATOM   21116 H  HG11 . VAL   D  4  114 ? 14.152  -65.130 -54.350  1.00 97.35  ? 114  VAL   D HG11 1 
ATOM   21117 H  HG12 . VAL   D  4  114 ? 13.986  -65.859 -55.751  1.00 97.35  ? 114  VAL   D HG12 1 
ATOM   21118 H  HG13 . VAL   D  4  114 ? 15.434  -65.474 -55.222  1.00 97.35  ? 114  VAL   D HG13 1 
ATOM   21119 H  HG21 . VAL   D  4  114 ? 14.531  -62.762 -54.209  1.00 92.91  ? 114  VAL   D HG21 1 
ATOM   21120 H  HG22 . VAL   D  4  114 ? 15.930  -62.929 -54.942  1.00 92.91  ? 114  VAL   D HG22 1 
ATOM   21121 H  HG23 . VAL   D  4  114 ? 14.857  -61.902 -55.504  1.00 92.91  ? 114  VAL   D HG23 1 
ATOM   21122 N  N    . THR   D  4  115 ? 15.366  -66.051 -58.366  1.00 72.51  ? 115  THR   D N    1 
ATOM   21123 C  CA   . THR   D  4  115 ? 14.993  -67.201 -59.178  1.00 73.95  ? 115  THR   D CA   1 
ATOM   21124 C  C    . THR   D  4  115 ? 15.130  -68.463 -58.339  1.00 75.72  ? 115  THR   D C    1 
ATOM   21125 O  O    . THR   D  4  115 ? 16.176  -68.692 -57.722  1.00 76.76  ? 115  THR   D O    1 
ATOM   21126 C  CB   . THR   D  4  115 ? 15.865  -67.299 -60.433  1.00 74.50  ? 115  THR   D CB   1 
ATOM   21127 O  OG1  . THR   D  4  115 ? 15.957  -66.012 -61.057  1.00 71.90  ? 115  THR   D OG1  1 
ATOM   21128 C  CG2  . THR   D  4  115 ? 15.265  -68.289 -61.419  1.00 78.17  ? 115  THR   D CG2  1 
ATOM   21129 H  H    . THR   D  4  115 ? 16.152  -66.114 -58.024  1.00 86.99  ? 115  THR   D H    1 
ATOM   21130 H  HA   . THR   D  4  115 ? 14.069  -67.116 -59.460  1.00 88.72  ? 115  THR   D HA   1 
ATOM   21131 H  HB   . THR   D  4  115 ? 16.752  -67.605 -60.187  1.00 89.38  ? 115  THR   D HB   1 
ATOM   21132 H  HG1  . THR   D  4  115 ? 16.467  -66.052 -61.724  1.00 86.26  ? 115  THR   D HG1  1 
ATOM   21133 H  HG21 . THR   D  4  115 ? 15.828  -68.355 -62.206  1.00 93.78  ? 115  THR   D HG21 1 
ATOM   21134 H  HG22 . THR   D  4  115 ? 15.194  -69.165 -61.008  1.00 93.78  ? 115  THR   D HG22 1 
ATOM   21135 H  HG23 . THR   D  4  115 ? 14.381  -67.994 -61.688  1.00 93.78  ? 115  THR   D HG23 1 
ATOM   21136 N  N    . VAL   D  4  116 ? 14.078  -69.276 -58.321  1.00 77.93  ? 116  VAL   D N    1 
ATOM   21137 C  CA   . VAL   D  4  116 ? 14.013  -70.474 -57.492  1.00 81.72  ? 116  VAL   D CA   1 
ATOM   21138 C  C    . VAL   D  4  116 ? 13.839  -71.671 -58.415  1.00 86.03  ? 116  VAL   D C    1 
ATOM   21139 O  O    . VAL   D  4  116 ? 12.747  -71.896 -58.953  1.00 88.70  ? 116  VAL   D O    1 
ATOM   21140 C  CB   . VAL   D  4  116 ? 12.875  -70.402 -56.465  1.00 82.66  ? 116  VAL   D CB   1 
ATOM   21141 C  CG1  . VAL   D  4  116 ? 12.872  -71.646 -55.586  1.00 87.79  ? 116  VAL   D CG1  1 
ATOM   21142 C  CG2  . VAL   D  4  116 ? 13.006  -69.145 -55.616  1.00 79.63  ? 116  VAL   D CG2  1 
ATOM   21143 H  H    . VAL   D  4  116 ? 13.370  -69.150 -58.794  1.00 93.50  ? 116  VAL   D H    1 
ATOM   21144 H  HA   . VAL   D  4  116 ? 14.853  -70.576 -57.018  1.00 98.04  ? 116  VAL   D HA   1 
ATOM   21145 H  HB   . VAL   D  4  116 ? 12.027  -70.363 -56.935  1.00 99.18  ? 116  VAL   D HB   1 
ATOM   21146 H  HG11 . VAL   D  4  116 ? 12.191  -71.547 -54.902  1.00 105.33 ? 116  VAL   D HG11 1 
ATOM   21147 H  HG12 . VAL   D  4  116 ? 12.677  -72.421 -56.137  1.00 105.33 ? 116  VAL   D HG12 1 
ATOM   21148 H  HG13 . VAL   D  4  116 ? 13.744  -71.743 -55.174  1.00 105.33 ? 116  VAL   D HG13 1 
ATOM   21149 H  HG21 . VAL   D  4  116 ? 12.293  -69.133 -54.959  1.00 95.54  ? 116  VAL   D HG21 1 
ATOM   21150 H  HG22 . VAL   D  4  116 ? 13.867  -69.154 -55.170  1.00 95.54  ? 116  VAL   D HG22 1 
ATOM   21151 H  HG23 . VAL   D  4  116 ? 12.939  -68.367 -56.192  1.00 95.54  ? 116  VAL   D HG23 1 
ATOM   21152 N  N    . SER   D  4  117 ? 14.910  -72.438 -58.596  1.00 86.35  ? 117  SER   D N    1 
ATOM   21153 C  CA   . SER   D  4  117 ? 14.847  -73.675 -59.358  1.00 88.12  ? 117  SER   D CA   1 
ATOM   21154 C  C    . SER   D  4  117 ? 15.875  -74.644 -58.796  1.00 87.56  ? 117  SER   D C    1 
ATOM   21155 O  O    . SER   D  4  117 ? 16.812  -74.251 -58.095  1.00 84.50  ? 117  SER   D O    1 
ATOM   21156 C  CB   . SER   D  4  117 ? 15.100  -73.442 -60.851  1.00 91.03  ? 117  SER   D CB   1 
ATOM   21157 O  OG   . SER   D  4  117 ? 16.474  -73.203 -61.100  1.00 93.73  ? 117  SER   D OG   1 
ATOM   21158 H  H    . SER   D  4  117 ? 15.692  -72.260 -58.285  1.00 103.60 ? 117  SER   D H    1 
ATOM   21159 H  HA   . SER   D  4  117 ? 13.964  -74.064 -59.260  1.00 105.73 ? 117  SER   D HA   1 
ATOM   21160 H  HB2  . SER   D  4  117 ? 14.822  -74.229 -61.345  1.00 109.21 ? 117  SER   D HB2  1 
ATOM   21161 H  HB3  . SER   D  4  117 ? 14.589  -72.671 -61.141  1.00 109.21 ? 117  SER   D HB3  1 
ATOM   21162 H  HG   . SER   D  4  117 ? 16.577  -72.894 -61.874  1.00 112.46 ? 117  SER   D HG   1 
ATOM   21163 N  N    . SER   D  4  118 ? 15.684  -75.923 -59.112  1.00 87.21  ? 118  SER   D N    1 
ATOM   21164 C  CA   . SER   D  4  118 ? 16.617  -76.961 -58.699  1.00 90.20  ? 118  SER   D CA   1 
ATOM   21165 C  C    . SER   D  4  118 ? 17.784  -77.116 -59.662  1.00 96.94  ? 118  SER   D C    1 
ATOM   21166 O  O    . SER   D  4  118 ? 18.807  -77.700 -59.287  1.00 102.49 ? 118  SER   D O    1 
ATOM   21167 C  CB   . SER   D  4  118 ? 15.885  -78.300 -58.572  1.00 89.40  ? 118  SER   D CB   1 
ATOM   21168 O  OG   . SER   D  4  118 ? 14.688  -78.155 -57.827  1.00 87.87  ? 118  SER   D OG   1 
ATOM   21169 H  H    . SER   D  4  118 ? 15.016  -76.215 -59.569  1.00 104.63 ? 118  SER   D H    1 
ATOM   21170 H  HA   . SER   D  4  118 ? 16.977  -76.734 -57.828  1.00 108.22 ? 118  SER   D HA   1 
ATOM   21171 H  HB2  . SER   D  4  118 ? 15.667  -78.626 -59.459  1.00 107.26 ? 118  SER   D HB2  1 
ATOM   21172 H  HB3  . SER   D  4  118 ? 16.463  -78.934 -58.119  1.00 107.26 ? 118  SER   D HB3  1 
ATOM   21173 H  HG   . SER   D  4  118 ? 14.215  -78.845 -57.906  1.00 105.43 ? 118  SER   D HG   1 
ATOM   21174 N  N    . ALA   D  4  119 ? 17.656  -76.604 -60.884  1.00 97.57  ? 119  ALA   D N    1 
ATOM   21175 C  CA   . ALA   D  4  119 ? 18.705  -76.762 -61.880  1.00 100.00 ? 119  ALA   D CA   1 
ATOM   21176 C  C    . ALA   D  4  119 ? 20.008  -76.141 -61.394  1.00 97.95  ? 119  ALA   D C    1 
ATOM   21177 O  O    . ALA   D  4  119 ? 20.018  -75.159 -60.647  1.00 95.16  ? 119  ALA   D O    1 
ATOM   21178 C  CB   . ALA   D  4  119 ? 18.282  -76.120 -63.203  1.00 98.98  ? 119  ALA   D CB   1 
ATOM   21179 H  H    . ALA   D  4  119 ? 16.972  -76.162 -61.160  1.00 117.06 ? 119  ALA   D H    1 
ATOM   21180 H  HA   . ALA   D  4  119 ? 18.859  -77.707 -62.035  1.00 119.98 ? 119  ALA   D HA   1 
ATOM   21181 H  HB1  . ALA   D  4  119 ? 18.993  -76.238 -63.852  1.00 118.76 ? 119  ALA   D HB1  1 
ATOM   21182 H  HB2  . ALA   D  4  119 ? 17.471  -76.549 -63.517  1.00 118.76 ? 119  ALA   D HB2  1 
ATOM   21183 H  HB3  . ALA   D  4  119 ? 18.121  -75.174 -63.057  1.00 118.76 ? 119  ALA   D HB3  1 
ATOM   21184 N  N    . LYS   D  4  120 ? 21.117  -76.730 -61.826  1.00 99.22  ? 120  LYS   D N    1 
ATOM   21185 C  CA   . LYS   D  4  120 ? 22.448  -76.219 -61.542  1.00 97.85  ? 120  LYS   D CA   1 
ATOM   21186 C  C    . LYS   D  4  120 ? 23.021  -75.566 -62.794  1.00 91.84  ? 120  LYS   D C    1 
ATOM   21187 O  O    . LYS   D  4  120 ? 22.506  -75.731 -63.903  1.00 88.86  ? 120  LYS   D O    1 
ATOM   21188 C  CB   . LYS   D  4  120 ? 23.366  -77.341 -61.043  1.00 102.95 ? 120  LYS   D CB   1 
ATOM   21189 C  CG   . LYS   D  4  120 ? 22.868  -78.021 -59.776  1.00 106.68 ? 120  LYS   D CG   1 
ATOM   21190 C  CD   . LYS   D  4  120 ? 23.989  -78.749 -59.052  1.00 113.43 ? 120  LYS   D CD   1 
ATOM   21191 C  CE   . LYS   D  4  120 ? 23.503  -79.365 -57.748  1.00 118.72 ? 120  LYS   D CE   1 
ATOM   21192 N  NZ   . LYS   D  4  120 ? 24.617  -79.965 -56.962  1.00 125.03 ? 120  LYS   D NZ   1 
ATOM   21193 H  H    . LYS   D  4  120 ? 21.121  -77.447 -62.300  1.00 119.05 ? 120  LYS   D H    1 
ATOM   21194 H  HA   . LYS   D  4  120 ? 22.398  -75.548 -60.844  1.00 117.40 ? 120  LYS   D HA   1 
ATOM   21195 H  HB2  . LYS   D  4  120 ? 23.437  -78.017 -61.734  1.00 123.52 ? 120  LYS   D HB2  1 
ATOM   21196 H  HB3  . LYS   D  4  120 ? 24.241  -76.967 -60.854  1.00 123.52 ? 120  LYS   D HB3  1 
ATOM   21197 H  HG2  . LYS   D  4  120 ? 22.502  -77.352 -59.175  1.00 128.00 ? 120  LYS   D HG2  1 
ATOM   21198 H  HG3  . LYS   D  4  120 ? 22.184  -78.668 -60.007  1.00 128.00 ? 120  LYS   D HG3  1 
ATOM   21199 H  HD2  . LYS   D  4  120 ? 24.328  -79.461 -59.617  1.00 136.09 ? 120  LYS   D HD2  1 
ATOM   21200 H  HD3  . LYS   D  4  120 ? 24.700  -78.122 -58.847  1.00 136.09 ? 120  LYS   D HD3  1 
ATOM   21201 H  HE2  . LYS   D  4  120 ? 23.087  -78.676 -57.206  1.00 142.45 ? 120  LYS   D HE2  1 
ATOM   21202 H  HE3  . LYS   D  4  120 ? 22.861  -80.065 -57.946  1.00 142.45 ? 120  LYS   D HE3  1 
ATOM   21203 H  HZ1  . LYS   D  4  120 ? 24.299  -80.332 -56.216  1.00 150.02 ? 120  LYS   D HZ1  1 
ATOM   21204 H  HZ2  . LYS   D  4  120 ? 25.025  -80.593 -57.442  1.00 150.02 ? 120  LYS   D HZ2  1 
ATOM   21205 H  HZ3  . LYS   D  4  120 ? 25.209  -79.337 -56.745  1.00 150.02 ? 120  LYS   D HZ3  1 
ATOM   21206 N  N    . THR   D  4  121 ? 24.100  -74.811 -62.597  1.00 89.85  ? 121  THR   D N    1 
ATOM   21207 C  CA   . THR   D  4  121 ? 24.707  -74.060 -63.689  1.00 85.67  ? 121  THR   D CA   1 
ATOM   21208 C  C    . THR   D  4  121 ? 24.985  -74.967 -64.883  1.00 82.56  ? 121  THR   D C    1 
ATOM   21209 O  O    . THR   D  4  121 ? 25.616  -76.018 -64.749  1.00 81.83  ? 121  THR   D O    1 
ATOM   21210 C  CB   . THR   D  4  121 ? 26.001  -73.392 -63.213  1.00 89.27  ? 121  THR   D CB   1 
ATOM   21211 O  OG1  . THR   D  4  121 ? 26.667  -72.781 -64.326  1.00 86.69  ? 121  THR   D OG1  1 
ATOM   21212 C  CG2  . THR   D  4  121 ? 26.938  -74.400 -62.554  1.00 98.53  ? 121  THR   D CG2  1 
ATOM   21213 H  H    . THR   D  4  121 ? 24.498  -74.717 -61.841  1.00 107.80 ? 121  THR   D H    1 
ATOM   21214 H  HA   . THR   D  4  121 ? 24.095  -73.364 -63.975  1.00 102.79 ? 121  THR   D HA   1 
ATOM   21215 H  HB   . THR   D  4  121 ? 25.781  -72.716 -62.553  1.00 107.10 ? 121  THR   D HB   1 
ATOM   21216 H  HG1  . THR   D  4  121 ? 27.379  -72.416 -64.070  1.00 104.00 ? 121  THR   D HG1  1 
ATOM   21217 H  HG21 . THR   D  4  121 ? 27.771  -73.968 -62.309  1.00 118.21 ? 121  THR   D HG21 1 
ATOM   21218 H  HG22 . THR   D  4  121 ? 26.525  -74.763 -61.755  1.00 118.21 ? 121  THR   D HG22 1 
ATOM   21219 H  HG23 . THR   D  4  121 ? 27.129  -75.126 -63.168  1.00 118.21 ? 121  THR   D HG23 1 
ATOM   21220 N  N    . THR   D  4  122 ? 24.500  -74.552 -66.053  1.00 80.68  ? 122  THR   D N    1 
ATOM   21221 C  CA   . THR   D  4  122 ? 24.619  -75.337 -67.274  1.00 79.43  ? 122  THR   D CA   1 
ATOM   21222 C  C    . THR   D  4  122 ? 24.998  -74.423 -68.430  1.00 82.09  ? 122  THR   D C    1 
ATOM   21223 O  O    . THR   D  4  122 ? 24.457  -73.322 -68.564  1.00 84.40  ? 122  THR   D O    1 
ATOM   21224 C  CB   . THR   D  4  122 ? 23.308  -76.068 -67.600  1.00 72.86  ? 122  THR   D CB   1 
ATOM   21225 O  OG1  . THR   D  4  122 ? 22.869  -76.807 -66.453  1.00 71.67  ? 122  THR   D OG1  1 
ATOM   21226 C  CG2  . THR   D  4  122 ? 23.504  -77.023 -68.770  1.00 73.66  ? 122  THR   D CG2  1 
ATOM   21227 H  H    . THR   D  4  122 ? 24.089  -73.805 -66.164  1.00 96.80  ? 122  THR   D H    1 
ATOM   21228 H  HA   . THR   D  4  122 ? 25.321  -75.997 -67.165  1.00 95.30  ? 122  THR   D HA   1 
ATOM   21229 H  HB   . THR   D  4  122 ? 22.630  -75.419 -67.845  1.00 87.42  ? 122  THR   D HB   1 
ATOM   21230 H  HG1  . THR   D  4  122 ? 22.690  -76.280 -65.824  1.00 85.99  ? 122  THR   D HG1  1 
ATOM   21231 H  HG21 . THR   D  4  122 ? 22.701  -77.551 -68.906  1.00 88.38  ? 122  THR   D HG21 1 
ATOM   21232 H  HG22 . THR   D  4  122 ? 23.692  -76.522 -69.580  1.00 88.38  ? 122  THR   D HG22 1 
ATOM   21233 H  HG23 . THR   D  4  122 ? 24.247  -77.620 -68.590  1.00 88.38  ? 122  THR   D HG23 1 
ATOM   21234 N  N    . ALA   D  4  123 ? 25.926  -74.890 -69.267  1.00 83.34  ? 123  ALA   D N    1 
ATOM   21235 C  CA   . ALA   D  4  123 ? 26.380  -74.102 -70.401  1.00 82.09  ? 123  ALA   D CA   1 
ATOM   21236 C  C    . ALA   D  4  123 ? 25.388  -74.195 -71.560  1.00 79.93  ? 123  ALA   D C    1 
ATOM   21237 O  O    . ALA   D  4  123 ? 24.692  -75.202 -71.713  1.00 80.72  ? 123  ALA   D O    1 
ATOM   21238 C  CB   . ALA   D  4  123 ? 27.753  -74.579 -70.864  1.00 84.90  ? 123  ALA   D CB   1 
ATOM   21239 H  H    . ALA   D  4  123 ? 26.304  -75.659 -69.197  1.00 99.99  ? 123  ALA   D H    1 
ATOM   21240 H  HA   . ALA   D  4  123 ? 26.452  -73.171 -70.138  1.00 98.49  ? 123  ALA   D HA   1 
ATOM   21241 H  HB1  . ALA   D  4  123 ? 28.027  -74.054 -71.632  1.00 101.86 ? 123  ALA   D HB1  1 
ATOM   21242 H  HB2  . ALA   D  4  123 ? 28.388  -74.462 -70.140  1.00 101.86 ? 123  ALA   D HB2  1 
ATOM   21243 H  HB3  . ALA   D  4  123 ? 27.696  -75.516 -71.107  1.00 101.86 ? 123  ALA   D HB3  1 
ATOM   21244 N  N    . PRO   D  4  124 ? 25.306  -73.157 -72.391  1.00 78.47  ? 124  PRO   D N    1 
ATOM   21245 C  CA   . PRO   D  4  124 ? 24.381  -73.193 -73.527  1.00 75.56  ? 124  PRO   D CA   1 
ATOM   21246 C  C    . PRO   D  4  124 ? 24.894  -74.037 -74.681  1.00 80.83  ? 124  PRO   D C    1 
ATOM   21247 O  O    . PRO   D  4  124 ? 26.098  -74.228 -74.866  1.00 80.50  ? 124  PRO   D O    1 
ATOM   21248 C  CB   . PRO   D  4  124 ? 24.278  -71.720 -73.945  1.00 70.60  ? 124  PRO   D CB   1 
ATOM   21249 C  CG   . PRO   D  4  124 ? 25.564  -71.119 -73.514  1.00 74.52  ? 124  PRO   D CG   1 
ATOM   21250 C  CD   . PRO   D  4  124 ? 25.968  -71.846 -72.260  1.00 78.76  ? 124  PRO   D CD   1 
ATOM   21251 H  HA   . PRO   D  4  124 ? 23.515  -73.526 -73.243  1.00 90.66  ? 124  PRO   D HA   1 
ATOM   21252 H  HB2  . PRO   D  4  124 ? 24.167  -71.654 -74.906  1.00 84.70  ? 124  PRO   D HB2  1 
ATOM   21253 H  HB3  . PRO   D  4  124 ? 23.528  -71.299 -73.495  1.00 84.70  ? 124  PRO   D HB3  1 
ATOM   21254 H  HG2  . PRO   D  4  124 ? 26.230  -71.241 -74.209  1.00 89.41  ? 124  PRO   D HG2  1 
ATOM   21255 H  HG3  . PRO   D  4  124 ? 25.439  -70.174 -73.337  1.00 89.41  ? 124  PRO   D HG3  1 
ATOM   21256 H  HD2  . PRO   D  4  124 ? 26.932  -71.950 -72.217  1.00 94.49  ? 124  PRO   D HD2  1 
ATOM   21257 H  HD3  . PRO   D  4  124 ? 25.650  -71.377 -71.473  1.00 94.49  ? 124  PRO   D HD3  1 
ATOM   21258 N  N    . SER   D  4  125 ? 23.945  -74.545 -75.462  1.00 64.27  ? 125  SER   D N    1 
ATOM   21259 C  CA   . SER   D  4  125 ? 24.222  -75.134 -76.765  1.00 70.74  ? 125  SER   D CA   1 
ATOM   21260 C  C    . SER   D  4  125 ? 23.820  -74.120 -77.829  1.00 73.17  ? 125  SER   D C    1 
ATOM   21261 O  O    . SER   D  4  125 ? 22.637  -73.783 -77.951  1.00 74.40  ? 125  SER   D O    1 
ATOM   21262 C  CB   . SER   D  4  125 ? 23.460  -76.444 -76.959  1.00 71.83  ? 125  SER   D CB   1 
ATOM   21263 O  OG   . SER   D  4  125 ? 23.849  -77.414 -76.003  1.00 75.74  ? 125  SER   D OG   1 
ATOM   21264 H  H    . SER   D  4  125 ? 23.111  -74.559 -75.252  1.00 77.11  ? 125  SER   D H    1 
ATOM   21265 H  HA   . SER   D  4  125 ? 25.169  -75.331 -76.843  1.00 84.87  ? 125  SER   D HA   1 
ATOM   21266 H  HB2  . SER   D  4  125 ? 22.511  -76.272 -76.862  1.00 86.17  ? 125  SER   D HB2  1 
ATOM   21267 H  HB3  . SER   D  4  125 ? 23.647  -76.787 -77.847  1.00 86.17  ? 125  SER   D HB3  1 
ATOM   21268 H  HG   . SER   D  4  125 ? 23.448  -78.137 -76.148  1.00 90.87  ? 125  SER   D HG   1 
ATOM   21269 N  N    . VAL   D  4  126 ? 24.797  -73.630 -78.583  1.00 72.17  ? 126  VAL   D N    1 
ATOM   21270 C  CA   . VAL   D  4  126 ? 24.567  -72.617 -79.606  1.00 72.12  ? 126  VAL   D CA   1 
ATOM   21271 C  C    . VAL   D  4  126 ? 24.418  -73.324 -80.945  1.00 74.88  ? 126  VAL   D C    1 
ATOM   21272 O  O    . VAL   D  4  126 ? 25.319  -74.053 -81.379  1.00 79.02  ? 126  VAL   D O    1 
ATOM   21273 C  CB   . VAL   D  4  126 ? 25.704  -71.584 -79.644  1.00 70.40  ? 126  VAL   D CB   1 
ATOM   21274 C  CG1  . VAL   D  4  126 ? 25.402  -70.499 -80.669  1.00 69.16  ? 126  VAL   D CG1  1 
ATOM   21275 C  CG2  . VAL   D  4  126 ? 25.904  -70.973 -78.267  1.00 67.72  ? 126  VAL   D CG2  1 
ATOM   21276 H  H    . VAL   D  4  126 ? 25.620  -73.873 -78.519  1.00 86.58  ? 126  VAL   D H    1 
ATOM   21277 H  HA   . VAL   D  4  126 ? 23.740  -72.149 -79.414  1.00 86.53  ? 126  VAL   D HA   1 
ATOM   21278 H  HB   . VAL   D  4  126 ? 26.526  -72.028 -79.905  1.00 84.46  ? 126  VAL   D HB   1 
ATOM   21279 H  HG11 . VAL   D  4  126 ? 26.114  -69.841 -80.651  1.00 82.98  ? 126  VAL   D HG11 1 
ATOM   21280 H  HG12 . VAL   D  4  126 ? 25.348  -70.903 -81.550  1.00 82.98  ? 126  VAL   D HG12 1 
ATOM   21281 H  HG13 . VAL   D  4  126 ? 24.557  -70.080 -80.445  1.00 82.98  ? 126  VAL   D HG13 1 
ATOM   21282 H  HG21 . VAL   D  4  126 ? 26.603  -70.302 -78.318  1.00 81.25  ? 126  VAL   D HG21 1 
ATOM   21283 H  HG22 . VAL   D  4  126 ? 25.073  -70.563 -77.979  1.00 81.25  ? 126  VAL   D HG22 1 
ATOM   21284 H  HG23 . VAL   D  4  126 ? 26.161  -71.672 -77.645  1.00 81.25  ? 126  VAL   D HG23 1 
ATOM   21285 N  N    . TYR   D  4  127 ? 23.280  -73.106 -81.599  1.00 72.92  ? 127  TYR   D N    1 
ATOM   21286 C  CA   . TYR   D  4  127 ? 22.972  -73.722 -82.873  1.00 72.58  ? 127  TYR   D CA   1 
ATOM   21287 C  C    . TYR   D  4  127 ? 22.795  -72.645 -83.934  1.00 77.47  ? 127  TYR   D C    1 
ATOM   21288 O  O    . TYR   D  4  127 ? 21.997  -71.717 -83.737  1.00 77.91  ? 127  TYR   D O    1 
ATOM   21289 C  CB   . TYR   D  4  127 ? 21.690  -74.562 -82.772  1.00 65.67  ? 127  TYR   D CB   1 
ATOM   21290 C  CG   . TYR   D  4  127 ? 21.776  -75.703 -81.788  1.00 63.20  ? 127  TYR   D CG   1 
ATOM   21291 C  CD1  . TYR   D  4  127 ? 22.874  -76.553 -81.774  1.00 64.38  ? 127  TYR   D CD1  1 
ATOM   21292 C  CD2  . TYR   D  4  127 ? 20.761  -75.927 -80.868  1.00 63.10  ? 127  TYR   D CD2  1 
ATOM   21293 C  CE1  . TYR   D  4  127 ? 22.957  -77.597 -80.875  1.00 65.56  ? 127  TYR   D CE1  1 
ATOM   21294 C  CE2  . TYR   D  4  127 ? 20.834  -76.967 -79.963  1.00 63.50  ? 127  TYR   D CE2  1 
ATOM   21295 C  CZ   . TYR   D  4  127 ? 21.933  -77.800 -79.971  1.00 66.23  ? 127  TYR   D CZ   1 
ATOM   21296 O  OH   . TYR   D  4  127 ? 22.008  -78.839 -79.070  1.00 70.93  ? 127  TYR   D OH   1 
ATOM   21297 H  H    . TYR   D  4  127 ? 22.656  -72.590 -81.311  1.00 87.49  ? 127  TYR   D H    1 
ATOM   21298 H  HA   . TYR   D  4  127 ? 23.702  -74.303 -83.138  1.00 87.07  ? 127  TYR   D HA   1 
ATOM   21299 H  HB2  . TYR   D  4  127 ? 20.962  -73.985 -82.492  1.00 78.79  ? 127  TYR   D HB2  1 
ATOM   21300 H  HB3  . TYR   D  4  127 ? 21.497  -74.939 -83.645  1.00 78.79  ? 127  TYR   D HB3  1 
ATOM   21301 H  HD1  . TYR   D  4  127 ? 23.566  -76.416 -82.380  1.00 77.24  ? 127  TYR   D HD1  1 
ATOM   21302 H  HD2  . TYR   D  4  127 ? 20.019  -75.367 -80.861  1.00 75.70  ? 127  TYR   D HD2  1 
ATOM   21303 H  HE1  . TYR   D  4  127 ? 23.697  -78.161 -80.879  1.00 78.65  ? 127  TYR   D HE1  1 
ATOM   21304 H  HE2  . TYR   D  4  127 ? 20.146  -77.105 -79.353  1.00 76.18  ? 127  TYR   D HE2  1 
ATOM   21305 H  HH   . TYR   D  4  127 ? 21.308  -78.870 -78.608  1.00 85.10  ? 127  TYR   D HH   1 
ATOM   21306 N  N    . PRO   D  4  128 ? 23.504  -72.719 -85.058  1.00 79.68  ? 128  PRO   D N    1 
ATOM   21307 C  CA   . PRO   D  4  128 ? 23.238  -71.773 -86.144  1.00 81.54  ? 128  PRO   D CA   1 
ATOM   21308 C  C    . PRO   D  4  128 ? 21.929  -72.109 -86.837  1.00 85.05  ? 128  PRO   D C    1 
ATOM   21309 O  O    . PRO   D  4  128 ? 21.488  -73.260 -86.859  1.00 90.13  ? 128  PRO   D O    1 
ATOM   21310 C  CB   . PRO   D  4  128 ? 24.434  -71.963 -87.081  1.00 84.34  ? 128  PRO   D CB   1 
ATOM   21311 C  CG   . PRO   D  4  128 ? 24.842  -73.376 -86.867  1.00 85.64  ? 128  PRO   D CG   1 
ATOM   21312 C  CD   . PRO   D  4  128 ? 24.566  -73.678 -85.414  1.00 82.79  ? 128  PRO   D CD   1 
ATOM   21313 H  HA   . PRO   D  4  128 ? 23.222  -70.857 -85.826  1.00 97.83  ? 128  PRO   D HA   1 
ATOM   21314 H  HB2  . PRO   D  4  128 ? 24.165  -71.811 -88.001  1.00 101.19 ? 128  PRO   D HB2  1 
ATOM   21315 H  HB3  . PRO   D  4  128 ? 25.147  -71.351 -86.840  1.00 101.19 ? 128  PRO   D HB3  1 
ATOM   21316 H  HG2  . PRO   D  4  128 ? 24.320  -73.957 -87.442  1.00 102.75 ? 128  PRO   D HG2  1 
ATOM   21317 H  HG3  . PRO   D  4  128 ? 25.786  -73.476 -87.064  1.00 102.75 ? 128  PRO   D HG3  1 
ATOM   21318 H  HD2  . PRO   D  4  128 ? 24.257  -74.591 -85.305  1.00 99.33  ? 128  PRO   D HD2  1 
ATOM   21319 H  HD3  . PRO   D  4  128 ? 25.359  -73.530 -84.875  1.00 99.33  ? 128  PRO   D HD3  1 
ATOM   21320 N  N    . LEU   D  4  129 ? 21.301  -71.081 -87.404  1.00 81.69  ? 129  LEU   D N    1 
ATOM   21321 C  CA   . LEU   D  4  129 ? 20.030  -71.233 -88.109  1.00 79.47  ? 129  LEU   D CA   1 
ATOM   21322 C  C    . LEU   D  4  129 ? 20.168  -70.588 -89.484  1.00 80.11  ? 129  LEU   D C    1 
ATOM   21323 O  O    . LEU   D  4  129 ? 20.064  -69.365 -89.618  1.00 82.75  ? 129  LEU   D O    1 
ATOM   21324 C  CB   . LEU   D  4  129 ? 18.880  -70.615 -87.320  1.00 78.75  ? 129  LEU   D CB   1 
ATOM   21325 C  CG   . LEU   D  4  129 ? 18.650  -71.154 -85.906  1.00 77.95  ? 129  LEU   D CG   1 
ATOM   21326 C  CD1  . LEU   D  4  129 ? 17.505  -70.409 -85.236  1.00 74.07  ? 129  LEU   D CD1  1 
ATOM   21327 C  CD2  . LEU   D  4  129 ? 18.374  -72.651 -85.923  1.00 82.07  ? 129  LEU   D CD2  1 
ATOM   21328 H  H    . LEU   D  4  129 ? 21.597  -70.274 -87.394  1.00 98.01  ? 129  LEU   D H    1 
ATOM   21329 H  HA   . LEU   D  4  129 ? 19.846  -72.178 -88.231  1.00 95.35  ? 129  LEU   D HA   1 
ATOM   21330 H  HB2  . LEU   D  4  129 ? 19.049  -69.664 -87.238  1.00 94.49  ? 129  LEU   D HB2  1 
ATOM   21331 H  HB3  . LEU   D  4  129 ? 18.060  -70.764 -87.818  1.00 94.49  ? 129  LEU   D HB3  1 
ATOM   21332 H  HG   . LEU   D  4  129 ? 19.456  -71.011 -85.386  1.00 93.52  ? 129  LEU   D HG   1 
ATOM   21333 H  HD11 . LEU   D  4  129 ? 17.355  -70.786 -84.355  1.00 88.86  ? 129  LEU   D HD11 1 
ATOM   21334 H  HD12 . LEU   D  4  129 ? 17.741  -69.471 -85.159  1.00 88.86  ? 129  LEU   D HD12 1 
ATOM   21335 H  HD13 . LEU   D  4  129 ? 16.706  -70.505 -85.777  1.00 88.86  ? 129  LEU   D HD13 1 
ATOM   21336 H  HD21 . LEU   D  4  129 ? 18.200  -72.950 -85.017  1.00 98.47  ? 129  LEU   D HD21 1 
ATOM   21337 H  HD22 . LEU   D  4  129 ? 17.602  -72.823 -86.484  1.00 98.47  ? 129  LEU   D HD22 1 
ATOM   21338 H  HD23 . LEU   D  4  129 ? 19.151  -73.111 -86.279  1.00 98.47  ? 129  LEU   D HD23 1 
ATOM   21339 N  N    . ALA   D  4  130 ? 20.410  -71.419 -90.509  1.00 79.48  ? 130  ALA   D N    1 
ATOM   21340 C  CA   . ALA   D  4  130 ? 20.466  -70.966 -91.887  1.00 82.89  ? 130  ALA   D CA   1 
ATOM   21341 C  C    . ALA   D  4  130 ? 19.130  -71.206 -92.580  1.00 83.33  ? 130  ALA   D C    1 
ATOM   21342 O  O    . ALA   D  4  130 ? 18.382  -72.112 -92.201  1.00 84.49  ? 130  ALA   D O    1 
ATOM   21343 C  CB   . ALA   D  4  130 ? 21.569  -71.697 -92.658  1.00 89.03  ? 130  ALA   D CB   1 
ATOM   21344 H  H    . ALA   D  4  130 ? 20.546  -72.264 -90.421  1.00 95.36  ? 130  ALA   D H    1 
ATOM   21345 H  HA   . ALA   D  4  130 ? 20.665  -70.016 -91.909  1.00 99.45  ? 130  ALA   D HA   1 
ATOM   21346 H  HB1  . ALA   D  4  130 ? 21.611  -71.344 -93.560  1.00 106.82 ? 130  ALA   D HB1  1 
ATOM   21347 H  HB2  . ALA   D  4  130 ? 22.416  -71.557 -92.207  1.00 106.82 ? 130  ALA   D HB2  1 
ATOM   21348 H  HB3  . ALA   D  4  130 ? 21.361  -72.645 -92.684  1.00 106.82 ? 130  ALA   D HB3  1 
ATOM   21349 N  N    . PRO   D  4  131 ? 18.797  -70.416 -93.597  1.00 82.10  ? 131  PRO   D N    1 
ATOM   21350 C  CA   . PRO   D  4  131 ? 17.553  -70.657 -94.336  1.00 85.90  ? 131  PRO   D CA   1 
ATOM   21351 C  C    . PRO   D  4  131 ? 17.641  -71.930 -95.166  1.00 97.31  ? 131  PRO   D C    1 
ATOM   21352 O  O    . PRO   D  4  131 ? 18.723  -72.449 -95.451  1.00 105.55 ? 131  PRO   D O    1 
ATOM   21353 C  CB   . PRO   D  4  131 ? 17.416  -69.416 -95.224  1.00 84.94  ? 131  PRO   D CB   1 
ATOM   21354 C  CG   . PRO   D  4  131 ? 18.809  -68.909 -95.388  1.00 84.18  ? 131  PRO   D CG   1 
ATOM   21355 C  CD   . PRO   D  4  131 ? 19.535  -69.249 -94.115  1.00 80.13  ? 131  PRO   D CD   1 
ATOM   21356 H  HA   . PRO   D  4  131 ? 16.794  -70.710 -93.735  1.00 103.07 ? 131  PRO   D HA   1 
ATOM   21357 H  HB2  . PRO   D  4  131 ? 17.033  -69.662 -96.081  1.00 101.91 ? 131  PRO   D HB2  1 
ATOM   21358 H  HB3  . PRO   D  4  131 ? 16.855  -68.756 -94.787  1.00 101.91 ? 131  PRO   D HB3  1 
ATOM   21359 H  HG2  . PRO   D  4  131 ? 19.227  -69.346 -96.146  1.00 100.99 ? 131  PRO   D HG2  1 
ATOM   21360 H  HG3  . PRO   D  4  131 ? 18.792  -67.949 -95.526  1.00 100.99 ? 131  PRO   D HG3  1 
ATOM   21361 H  HD2  . PRO   D  4  131 ? 20.459  -69.479 -94.296  1.00 96.14  ? 131  PRO   D HD2  1 
ATOM   21362 H  HD3  . PRO   D  4  131 ? 19.494  -68.510 -93.488  1.00 96.14  ? 131  PRO   D HD3  1 
ATOM   21363 N  N    . VAL   D  4  132 ? 16.468  -72.435 -95.553  1.00 98.43  ? 132  VAL   D N    1 
ATOM   21364 C  CA   . VAL   D  4  132 ? 16.414  -73.679 -96.311  1.00 106.10 ? 132  VAL   D CA   1 
ATOM   21365 C  C    . VAL   D  4  132 ? 16.856  -73.419 -97.746  1.00 113.59 ? 132  VAL   D C    1 
ATOM   21366 O  O    . VAL   D  4  132 ? 16.674  -72.322 -98.292  1.00 115.54 ? 132  VAL   D O    1 
ATOM   21367 C  CB   . VAL   D  4  132 ? 15.002  -74.295 -96.277  1.00 108.95 ? 132  VAL   D CB   1 
ATOM   21368 C  CG1  . VAL   D  4  132 ? 15.055  -75.757 -96.708  1.00 113.65 ? 132  VAL   D CG1  1 
ATOM   21369 C  CG2  . VAL   D  4  132 ? 14.379  -74.153 -94.897  1.00 103.86 ? 132  VAL   D CG2  1 
ATOM   21370 H  H    . VAL   D  4  132 ? 15.702  -72.081 -95.390  1.00 118.09 ? 132  VAL   D H    1 
ATOM   21371 H  HA   . VAL   D  4  132 ? 17.023  -74.314 -95.903  1.00 127.30 ? 132  VAL   D HA   1 
ATOM   21372 H  HB   . VAL   D  4  132 ? 14.436  -73.815 -96.901  1.00 130.72 ? 132  VAL   D HB   1 
ATOM   21373 H  HG11 . VAL   D  4  132 ? 14.184  -76.160 -96.567  1.00 136.36 ? 132  VAL   D HG11 1 
ATOM   21374 H  HG12 . VAL   D  4  132 ? 15.292  -75.802 -97.647  1.00 136.36 ? 132  VAL   D HG12 1 
ATOM   21375 H  HG13 . VAL   D  4  132 ? 15.723  -76.219 -96.176  1.00 136.36 ? 132  VAL   D HG13 1 
ATOM   21376 H  HG21 . VAL   D  4  132 ? 13.828  -74.931 -94.717  1.00 124.61 ? 132  VAL   D HG21 1 
ATOM   21377 H  HG22 . VAL   D  4  132 ? 15.086  -74.088 -94.236  1.00 124.61 ? 132  VAL   D HG22 1 
ATOM   21378 H  HG23 . VAL   D  4  132 ? 13.834  -73.351 -94.877  1.00 124.61 ? 132  VAL   D HG23 1 
ATOM   21379 N  N    . CYS   D  4  133 ? 17.442  -74.439 -98.366  1.00 120.38 ? 133  CYS   D N    1 
ATOM   21380 C  CA   . CYS   D  4  133 ? 17.904  -74.331 -99.745  1.00 131.85 ? 133  CYS   D CA   1 
ATOM   21381 C  C    . CYS   D  4  133 ? 16.754  -73.925 -100.662 1.00 127.80 ? 133  CYS   D C    1 
ATOM   21382 O  O    . CYS   D  4  133 ? 16.869  -72.974 -101.434 1.00 124.91 ? 133  CYS   D O    1 
ATOM   21383 C  CB   . CYS   D  4  133 ? 18.509  -75.654 -100.221 1.00 149.66 ? 133  CYS   D CB   1 
ATOM   21384 S  SG   . CYS   D  4  133 ? 18.761  -76.891 -98.923  1.00 154.83 ? 133  CYS   D SG   1 
ATOM   21385 H  H    . CYS   D  4  133 ? 17.584  -75.208 -98.008  1.00 144.44 ? 133  CYS   D H    1 
ATOM   21386 H  HA   . CYS   D  4  133 ? 18.596  -73.654 -99.797  1.00 158.20 ? 133  CYS   D HA   1 
ATOM   21387 H  HB2  . CYS   D  4  133 ? 17.915  -76.042 -100.882 1.00 179.58 ? 133  CYS   D HB2  1 
ATOM   21388 H  HB3  . CYS   D  4  133 ? 19.374  -75.469 -100.619 1.00 179.58 ? 133  CYS   D HB3  1 
ATOM   21389 N  N    . GLY   D  4  138 ? 14.067  -61.914 -103.344 1.00 136.68 ? 138  GLY   D N    1 
ATOM   21390 C  CA   . GLY   D  4  138 ? 15.198  -62.217 -102.487 1.00 131.41 ? 138  GLY   D CA   1 
ATOM   21391 C  C    . GLY   D  4  138 ? 16.133  -61.037 -102.309 1.00 130.18 ? 138  GLY   D C    1 
ATOM   21392 O  O    . GLY   D  4  138 ? 17.282  -61.071 -102.751 1.00 136.13 ? 138  GLY   D O    1 
ATOM   21393 H  HA2  . GLY   D  4  138 ? 14.874  -62.483 -101.612 1.00 157.67 ? 138  GLY   D HA2  1 
ATOM   21394 H  HA3  . GLY   D  4  138 ? 15.704  -62.950 -102.872 1.00 157.67 ? 138  GLY   D HA3  1 
ATOM   21395 N  N    . SER   D  4  139 ? 15.638  -59.986 -101.657 1.00 122.49 ? 139  SER   D N    1 
ATOM   21396 C  CA   . SER   D  4  139 ? 16.416  -58.776 -101.419 1.00 118.02 ? 139  SER   D CA   1 
ATOM   21397 C  C    . SER   D  4  139 ? 17.090  -58.765 -100.054 1.00 112.66 ? 139  SER   D C    1 
ATOM   21398 O  O    . SER   D  4  139 ? 18.207  -58.253 -99.927  1.00 116.01 ? 139  SER   D O    1 
ATOM   21399 C  CB   . SER   D  4  139 ? 15.523  -57.538 -101.552 1.00 115.81 ? 139  SER   D CB   1 
ATOM   21400 O  OG   . SER   D  4  139 ? 14.478  -57.555 -100.596 1.00 110.23 ? 139  SER   D OG   1 
ATOM   21401 H  H    . SER   D  4  139 ? 14.840  -59.951 -101.338 1.00 146.97 ? 139  SER   D H    1 
ATOM   21402 H  HA   . SER   D  4  139 ? 17.111  -58.715 -102.093 1.00 141.60 ? 139  SER   D HA   1 
ATOM   21403 H  HB2  . SER   D  4  139 ? 16.064  -56.745 -101.414 1.00 138.95 ? 139  SER   D HB2  1 
ATOM   21404 H  HB3  . SER   D  4  139 ? 15.136  -57.525 -102.441 1.00 138.95 ? 139  SER   D HB3  1 
ATOM   21405 H  HG   . SER   D  4  139 ? 14.004  -56.866 -100.677 1.00 132.25 ? 139  SER   D HG   1 
ATOM   21406 N  N    . SER   D  4  140 ? 16.439  -59.315 -99.032  1.00 106.90 ? 140  SER   D N    1 
ATOM   21407 C  CA   . SER   D  4  140 ? 17.016  -59.433 -97.704  1.00 102.74 ? 140  SER   D CA   1 
ATOM   21408 C  C    . SER   D  4  140 ? 16.983  -60.889 -97.259  1.00 97.99  ? 140  SER   D C    1 
ATOM   21409 O  O    . SER   D  4  140 ? 16.156  -61.684 -97.716  1.00 96.36  ? 140  SER   D O    1 
ATOM   21410 C  CB   . SER   D  4  140 ? 16.271  -58.563 -96.682  1.00 101.96 ? 140  SER   D CB   1 
ATOM   21411 O  OG   . SER   D  4  140 ? 15.176  -59.264 -96.117  1.00 100.43 ? 140  SER   D OG   1 
ATOM   21412 H  H    . SER   D  4  140 ? 15.642  -59.633 -99.089  1.00 128.26 ? 140  SER   D H    1 
ATOM   21413 H  HA   . SER   D  4  140 ? 17.940  -59.137 -97.730  1.00 123.27 ? 140  SER   D HA   1 
ATOM   21414 H  HB2  . SER   D  4  140 ? 16.884  -58.314 -95.974  1.00 122.34 ? 140  SER   D HB2  1 
ATOM   21415 H  HB3  . SER   D  4  140 ? 15.939  -57.768 -97.129  1.00 122.34 ? 140  SER   D HB3  1 
ATOM   21416 H  HG   . SER   D  4  140 ? 14.831  -58.809 -95.500  1.00 120.49 ? 140  SER   D HG   1 
ATOM   21417 N  N    . VAL   D  4  141 ? 17.895  -61.227 -96.353  1.00 96.77  ? 141  VAL   D N    1 
ATOM   21418 C  CA   . VAL   D  4  141 ? 18.038  -62.581 -95.838  1.00 99.12  ? 141  VAL   D CA   1 
ATOM   21419 C  C    . VAL   D  4  141 ? 18.009  -62.524 -94.319  1.00 94.79  ? 141  VAL   D C    1 
ATOM   21420 O  O    . VAL   D  4  141 ? 18.641  -61.654 -93.709  1.00 94.30  ? 141  VAL   D O    1 
ATOM   21421 C  CB   . VAL   D  4  141 ? 19.342  -63.241 -96.336  1.00 105.52 ? 141  VAL   D CB   1 
ATOM   21422 C  CG1  . VAL   D  4  141 ? 20.546  -62.369 -95.996  1.00 105.34 ? 141  VAL   D CG1  1 
ATOM   21423 C  CG2  . VAL   D  4  141 ? 19.497  -64.632 -95.743  1.00 105.74 ? 141  VAL   D CG2  1 
ATOM   21424 H  H    . VAL   D  4  141 ? 18.457  -60.672 -96.013  1.00 116.10 ? 141  VAL   D H    1 
ATOM   21425 H  HA   . VAL   D  4  141 ? 17.291  -63.123 -96.136  1.00 118.93 ? 141  VAL   D HA   1 
ATOM   21426 H  HB   . VAL   D  4  141 ? 19.300  -63.330 -97.301  1.00 126.60 ? 141  VAL   D HB   1 
ATOM   21427 H  HG11 . VAL   D  4  141 ? 21.348  -62.789 -96.343  1.00 126.38 ? 141  VAL   D HG11 1 
ATOM   21428 H  HG12 . VAL   D  4  141 ? 20.428  -61.496 -96.402  1.00 126.38 ? 141  VAL   D HG12 1 
ATOM   21429 H  HG13 . VAL   D  4  141 ? 20.609  -62.280 -95.032  1.00 126.38 ? 141  VAL   D HG13 1 
ATOM   21430 H  HG21 . VAL   D  4  141 ? 20.257  -65.069 -96.159  1.00 126.86 ? 141  VAL   D HG21 1 
ATOM   21431 H  HG22 . VAL   D  4  141 ? 19.643  -64.554 -94.788  1.00 126.86 ? 141  VAL   D HG22 1 
ATOM   21432 H  HG23 . VAL   D  4  141 ? 18.689  -65.140 -95.915  1.00 126.86 ? 141  VAL   D HG23 1 
ATOM   21433 N  N    . THR   D  4  142 ? 17.272  -63.448 -93.709  1.00 91.20  ? 142  THR   D N    1 
ATOM   21434 C  CA   . THR   D  4  142 ? 17.159  -63.538 -92.259  1.00 83.87  ? 142  THR   D CA   1 
ATOM   21435 C  C    . THR   D  4  142 ? 17.900  -64.780 -91.785  1.00 82.05  ? 142  THR   D C    1 
ATOM   21436 O  O    . THR   D  4  142 ? 17.566  -65.899 -92.188  1.00 82.79  ? 142  THR   D O    1 
ATOM   21437 C  CB   . THR   D  4  142 ? 15.695  -63.586 -91.820  1.00 81.75  ? 142  THR   D CB   1 
ATOM   21438 O  OG1  . THR   D  4  142 ? 15.043  -62.365 -92.192  1.00 85.00  ? 142  THR   D OG1  1 
ATOM   21439 C  CG2  . THR   D  4  142 ? 15.592  -63.772 -90.308  1.00 76.47  ? 142  THR   D CG2  1 
ATOM   21440 H  H    . THR   D  4  142 ? 16.818  -64.047 -94.126  1.00 109.41 ? 142  THR   D H    1 
ATOM   21441 H  HA   . THR   D  4  142 ? 17.572  -62.758 -91.857  1.00 100.62 ? 142  THR   D HA   1 
ATOM   21442 H  HB   . THR   D  4  142 ? 15.254  -64.335 -92.250  1.00 98.08  ? 142  THR   D HB   1 
ATOM   21443 H  HG1  . THR   D  4  142 ? 15.402  -61.716 -91.797  1.00 101.98 ? 142  THR   D HG1  1 
ATOM   21444 H  HG21 . THR   D  4  142 ? 14.665  -63.704 -90.028  1.00 91.75  ? 142  THR   D HG21 1 
ATOM   21445 H  HG22 . THR   D  4  142 ? 15.933  -64.644 -90.057  1.00 91.75  ? 142  THR   D HG22 1 
ATOM   21446 H  HG23 . THR   D  4  142 ? 16.109  -63.088 -89.854  1.00 91.75  ? 142  THR   D HG23 1 
ATOM   21447 N  N    . LEU   D  4  143 ? 18.903  -64.577 -90.939  1.00 79.65  ? 143  LEU   D N    1 
ATOM   21448 C  CA   . LEU   D  4  143 ? 19.615  -65.654 -90.271  1.00 78.91  ? 143  LEU   D CA   1 
ATOM   21449 C  C    . LEU   D  4  143 ? 19.212  -65.675 -88.803  1.00 77.47  ? 143  LEU   D C    1 
ATOM   21450 O  O    . LEU   D  4  143 ? 18.626  -64.720 -88.286  1.00 77.51  ? 143  LEU   D O    1 
ATOM   21451 C  CB   . LEU   D  4  143 ? 21.129  -65.477 -90.410  1.00 79.27  ? 143  LEU   D CB   1 
ATOM   21452 C  CG   . LEU   D  4  143 ? 21.669  -65.243 -91.823  1.00 80.64  ? 143  LEU   D CG   1 
ATOM   21453 C  CD1  . LEU   D  4  143 ? 23.183  -65.076 -91.789  1.00 82.14  ? 143  LEU   D CD1  1 
ATOM   21454 C  CD2  . LEU   D  4  143 ? 21.277  -66.377 -92.757  1.00 82.08  ? 143  LEU   D CD2  1 
ATOM   21455 H  H    . LEU   D  4  143 ? 19.197  -63.796 -90.731  1.00 95.56  ? 143  LEU   D H    1 
ATOM   21456 H  HA   . LEU   D  4  143 ? 19.382  -66.504 -90.676  1.00 94.67  ? 143  LEU   D HA   1 
ATOM   21457 H  HB2  . LEU   D  4  143 ? 21.392  -64.712 -89.875  1.00 95.11  ? 143  LEU   D HB2  1 
ATOM   21458 H  HB3  . LEU   D  4  143 ? 21.556  -66.280 -90.073  1.00 95.11  ? 143  LEU   D HB3  1 
ATOM   21459 H  HG   . LEU   D  4  143 ? 21.278  -64.427 -92.173  1.00 96.75  ? 143  LEU   D HG   1 
ATOM   21460 H  HD11 . LEU   D  4  143 ? 23.493  -64.831 -92.675  1.00 98.55  ? 143  LEU   D HD11 1 
ATOM   21461 H  HD12 . LEU   D  4  143 ? 23.410  -64.379 -91.154  1.00 98.55  ? 143  LEU   D HD12 1 
ATOM   21462 H  HD13 . LEU   D  4  143 ? 23.587  -65.915 -91.517  1.00 98.55  ? 143  LEU   D HD13 1 
ATOM   21463 H  HD21 . LEU   D  4  143 ? 21.679  -66.223 -93.626  1.00 98.48  ? 143  LEU   D HD21 1 
ATOM   21464 H  HD22 . LEU   D  4  143 ? 21.598  -67.215 -92.388  1.00 98.48  ? 143  LEU   D HD22 1 
ATOM   21465 H  HD23 . LEU   D  4  143 ? 20.311  -66.399 -92.839  1.00 98.48  ? 143  LEU   D HD23 1 
ATOM   21466 N  N    . GLY   D  4  144 ? 19.534  -66.780 -88.124  1.00 75.32  ? 144  GLY   D N    1 
ATOM   21467 C  CA   . GLY   D  4  144 ? 19.106  -66.967 -86.755  1.00 70.77  ? 144  GLY   D CA   1 
ATOM   21468 C  C    . GLY   D  4  144 ? 20.161  -67.669 -85.924  1.00 71.53  ? 144  GLY   D C    1 
ATOM   21469 O  O    . GLY   D  4  144 ? 21.130  -68.227 -86.445  1.00 74.60  ? 144  GLY   D O    1 
ATOM   21470 H  H    . GLY   D  4  144 ? 20.000  -67.430 -88.442  1.00 90.37  ? 144  GLY   D H    1 
ATOM   21471 H  HA2  . GLY   D  4  144 ? 18.923  -66.103 -86.353  1.00 84.91  ? 144  GLY   D HA2  1 
ATOM   21472 H  HA3  . GLY   D  4  144 ? 18.297  -67.501 -86.739  1.00 84.91  ? 144  GLY   D HA3  1 
ATOM   21473 N  N    . CYS   D  4  145 ? 19.947  -67.634 -84.610  1.00 68.76  ? 145  CYS   D N    1 
ATOM   21474 C  CA   . CYS   D  4  145 ? 20.840  -68.281 -83.658  1.00 68.96  ? 145  CYS   D CA   1 
ATOM   21475 C  C    . CYS   D  4  145 ? 20.016  -68.766 -82.476  1.00 67.06  ? 145  CYS   D C    1 
ATOM   21476 O  O    . CYS   D  4  145 ? 19.237  -67.998 -81.904  1.00 64.65  ? 145  CYS   D O    1 
ATOM   21477 C  CB   . CYS   D  4  145 ? 21.937  -67.324 -83.185  1.00 73.14  ? 145  CYS   D CB   1 
ATOM   21478 S  SG   . CYS   D  4  145 ? 23.296  -68.117 -82.294  1.00 80.43  ? 145  CYS   D SG   1 
ATOM   21479 H  H    . CYS   D  4  145 ? 19.280  -67.234 -84.241  1.00 82.49  ? 145  CYS   D H    1 
ATOM   21480 H  HA   . CYS   D  4  145 ? 21.265  -69.046 -84.076  1.00 82.73  ? 145  CYS   D HA   1 
ATOM   21481 H  HB2  . CYS   D  4  145 ? 22.315  -66.880 -83.961  1.00 87.74  ? 145  CYS   D HB2  1 
ATOM   21482 H  HB3  . CYS   D  4  145 ? 21.540  -66.669 -82.590  1.00 87.74  ? 145  CYS   D HB3  1 
ATOM   21483 N  N    . LEU   D  4  146 ? 20.196  -70.033 -82.115  1.00 67.29  ? 146  LEU   D N    1 
ATOM   21484 C  CA   . LEU   D  4  146 ? 19.421  -70.681 -81.065  1.00 64.76  ? 146  LEU   D CA   1 
ATOM   21485 C  C    . LEU   D  4  146 ? 20.347  -71.024 -79.905  1.00 64.78  ? 146  LEU   D C    1 
ATOM   21486 O  O    . LEU   D  4  146 ? 21.267  -71.835 -80.058  1.00 66.41  ? 146  LEU   D O    1 
ATOM   21487 C  CB   . LEU   D  4  146 ? 18.735  -71.937 -81.603  1.00 69.50  ? 146  LEU   D CB   1 
ATOM   21488 C  CG   . LEU   D  4  146 ? 17.877  -72.731 -80.617  1.00 73.29  ? 146  LEU   D CG   1 
ATOM   21489 C  CD1  . LEU   D  4  146 ? 16.724  -71.885 -80.101  1.00 75.76  ? 146  LEU   D CD1  1 
ATOM   21490 C  CD2  . LEU   D  4  146 ? 17.362  -74.001 -81.276  1.00 76.71  ? 146  LEU   D CD2  1 
ATOM   21491 H  H    . LEU   D  4  146 ? 20.780  -70.552 -82.476  1.00 80.73  ? 146  LEU   D H    1 
ATOM   21492 H  HA   . LEU   D  4  146 ? 18.741  -70.073 -80.737  1.00 77.69  ? 146  LEU   D HA   1 
ATOM   21493 H  HB2  . LEU   D  4  146 ? 18.155  -71.671 -82.333  1.00 83.38  ? 146  LEU   D HB2  1 
ATOM   21494 H  HB3  . LEU   D  4  146 ? 19.423  -72.538 -81.927  1.00 83.38  ? 146  LEU   D HB3  1 
ATOM   21495 H  HG   . LEU   D  4  146 ? 18.419  -72.983 -79.854  1.00 87.93  ? 146  LEU   D HG   1 
ATOM   21496 H  HD11 . LEU   D  4  146 ? 16.175  -72.426 -79.512  1.00 90.90  ? 146  LEU   D HD11 1 
ATOM   21497 H  HD12 . LEU   D  4  146 ? 17.083  -71.126 -79.615  1.00 90.90  ? 146  LEU   D HD12 1 
ATOM   21498 H  HD13 . LEU   D  4  146 ? 16.197  -71.577 -80.855  1.00 90.90  ? 146  LEU   D HD13 1 
ATOM   21499 H  HD21 . LEU   D  4  146 ? 16.826  -74.494 -80.636  1.00 92.03  ? 146  LEU   D HD21 1 
ATOM   21500 H  HD22 . LEU   D  4  146 ? 16.821  -73.761 -82.045  1.00 92.03  ? 146  LEU   D HD22 1 
ATOM   21501 H  HD23 . LEU   D  4  146 ? 18.118  -74.539 -81.559  1.00 92.03  ? 146  LEU   D HD23 1 
ATOM   21502 N  N    . VAL   D  4  147 ? 20.102  -70.406 -78.754  1.00 64.65  ? 147  VAL   D N    1 
ATOM   21503 C  CA   . VAL   D  4  147 ? 20.885  -70.623 -77.543  1.00 67.04  ? 147  VAL   D CA   1 
ATOM   21504 C  C    . VAL   D  4  147 ? 19.982  -71.387 -76.581  1.00 66.87  ? 147  VAL   D C    1 
ATOM   21505 O  O    . VAL   D  4  147 ? 19.077  -70.810 -75.968  1.00 70.16  ? 147  VAL   D O    1 
ATOM   21506 C  CB   . VAL   D  4  147 ? 21.377  -69.304 -76.938  1.00 67.15  ? 147  VAL   D CB   1 
ATOM   21507 C  CG1  . VAL   D  4  147 ? 22.307  -69.565 -75.767  1.00 71.59  ? 147  VAL   D CG1  1 
ATOM   21508 C  CG2  . VAL   D  4  147 ? 22.070  -68.463 -78.005  1.00 64.25  ? 147  VAL   D CG2  1 
ATOM   21509 H  H    . VAL   D  4  147 ? 19.466  -69.837 -78.648  1.00 77.57  ? 147  VAL   D H    1 
ATOM   21510 H  HA   . VAL   D  4  147 ? 21.660  -71.172 -77.742  1.00 80.43  ? 147  VAL   D HA   1 
ATOM   21511 H  HB   . VAL   D  4  147 ? 20.614  -68.805 -76.606  1.00 80.56  ? 147  VAL   D HB   1 
ATOM   21512 H  HG11 . VAL   D  4  147 ? 22.617  -68.716 -75.415  1.00 85.88  ? 147  VAL   D HG11 1 
ATOM   21513 H  HG12 . VAL   D  4  147 ? 21.822  -70.050 -75.081  1.00 85.88  ? 147  VAL   D HG12 1 
ATOM   21514 H  HG13 . VAL   D  4  147 ? 23.061  -70.091 -76.075  1.00 85.88  ? 147  VAL   D HG13 1 
ATOM   21515 H  HG21 . VAL   D  4  147 ? 22.393  -67.643 -77.600  1.00 77.08  ? 147  VAL   D HG21 1 
ATOM   21516 H  HG22 . VAL   D  4  147 ? 22.815  -68.967 -78.370  1.00 77.08  ? 147  VAL   D HG22 1 
ATOM   21517 H  HG23 . VAL   D  4  147 ? 21.435  -68.257 -78.708  1.00 77.08  ? 147  VAL   D HG23 1 
ATOM   21518 N  N    . LYS   D  4  148 ? 20.225  -72.688 -76.445  1.00 65.18  ? 148  LYS   D N    1 
ATOM   21519 C  CA   . LYS   D  4  148 ? 19.284  -73.599 -75.810  1.00 65.26  ? 148  LYS   D CA   1 
ATOM   21520 C  C    . LYS   D  4  148 ? 19.926  -74.332 -74.641  1.00 68.59  ? 148  LYS   D C    1 
ATOM   21521 O  O    . LYS   D  4  148 ? 21.057  -74.818 -74.742  1.00 69.58  ? 148  LYS   D O    1 
ATOM   21522 C  CB   . LYS   D  4  148 ? 18.760  -74.617 -76.829  1.00 62.74  ? 148  LYS   D CB   1 
ATOM   21523 C  CG   . LYS   D  4  148 ? 17.604  -75.462 -76.333  1.00 67.26  ? 148  LYS   D CG   1 
ATOM   21524 C  CD   . LYS   D  4  148 ? 17.113  -76.403 -77.423  1.00 72.20  ? 148  LYS   D CD   1 
ATOM   21525 C  CE   . LYS   D  4  148 ? 15.910  -77.209 -76.966  1.00 78.83  ? 148  LYS   D CE   1 
ATOM   21526 N  NZ   . LYS   D  4  148 ? 16.213  -78.025 -75.759  1.00 85.92  ? 148  LYS   D NZ   1 
ATOM   21527 H  H    . LYS   D  4  148 ? 20.943  -73.073 -76.719  1.00 78.20  ? 148  LYS   D H    1 
ATOM   21528 H  HA   . LYS   D  4  148 ? 18.543  -73.086 -75.451  1.00 78.29  ? 148  LYS   D HA   1 
ATOM   21529 H  HB2  . LYS   D  4  148 ? 18.456  -74.138 -77.616  1.00 75.26  ? 148  LYS   D HB2  1 
ATOM   21530 H  HB3  . LYS   D  4  148 ? 19.483  -75.218 -77.065  1.00 75.26  ? 148  LYS   D HB3  1 
ATOM   21531 H  HG2  . LYS   D  4  148 ? 17.894  -75.994 -75.576  1.00 80.69  ? 148  LYS   D HG2  1 
ATOM   21532 H  HG3  . LYS   D  4  148 ? 16.870  -74.885 -76.072  1.00 80.69  ? 148  LYS   D HG3  1 
ATOM   21533 H  HD2  . LYS   D  4  148 ? 16.854  -75.885 -78.201  1.00 86.62  ? 148  LYS   D HD2  1 
ATOM   21534 H  HD3  . LYS   D  4  148 ? 17.823  -77.021 -77.656  1.00 86.62  ? 148  LYS   D HD3  1 
ATOM   21535 H  HE2  . LYS   D  4  148 ? 15.184  -76.604 -76.749  1.00 94.57  ? 148  LYS   D HE2  1 
ATOM   21536 H  HE3  . LYS   D  4  148 ? 15.640  -77.810 -77.678  1.00 94.57  ? 148  LYS   D HE3  1 
ATOM   21537 H  HZ1  . LYS   D  4  148 ? 15.863  -78.838 -75.846  1.00 103.08 ? 148  LYS   D HZ1  1 
ATOM   21538 H  HZ2  . LYS   D  4  148 ? 17.094  -78.098 -75.655  1.00 103.08 ? 148  LYS   D HZ2  1 
ATOM   21539 H  HZ3  . LYS   D  4  148 ? 15.868  -77.637 -75.036  1.00 103.08 ? 148  LYS   D HZ3  1 
ATOM   21540 N  N    . GLY   D  4  149 ? 19.190  -74.408 -73.534  1.00 73.29  ? 149  GLY   D N    1 
ATOM   21541 C  CA   . GLY   D  4  149 ? 19.559  -75.254 -72.416  1.00 74.57  ? 149  GLY   D CA   1 
ATOM   21542 C  C    . GLY   D  4  149 ? 20.695  -74.737 -71.559  1.00 75.43  ? 149  GLY   D C    1 
ATOM   21543 O  O    . GLY   D  4  149 ? 21.640  -75.478 -71.269  1.00 79.12  ? 149  GLY   D O    1 
ATOM   21544 H  H    . GLY   D  4  149 ? 18.461  -73.970 -73.408  1.00 87.93  ? 149  GLY   D H    1 
ATOM   21545 H  HA2  . GLY   D  4  149 ? 18.785  -75.364 -71.842  1.00 89.47  ? 149  GLY   D HA2  1 
ATOM   21546 H  HA3  . GLY   D  4  149 ? 19.823  -76.122 -72.760  1.00 89.47  ? 149  GLY   D HA3  1 
ATOM   21547 N  N    . TYR   D  4  150 ? 20.617  -73.479 -71.136  1.00 74.59  ? 150  TYR   D N    1 
ATOM   21548 C  CA   . TYR   D  4  150 ? 21.613  -72.896 -70.253  1.00 75.83  ? 150  TYR   D CA   1 
ATOM   21549 C  C    . TYR   D  4  150 ? 20.961  -72.450 -68.952  1.00 75.53  ? 150  TYR   D C    1 
ATOM   21550 O  O    . TYR   D  4  150 ? 19.745  -72.254 -68.872  1.00 73.55  ? 150  TYR   D O    1 
ATOM   21551 C  CB   . TYR   D  4  150 ? 22.324  -71.706 -70.908  1.00 76.74  ? 150  TYR   D CB   1 
ATOM   21552 C  CG   . TYR   D  4  150 ? 21.432  -70.513 -71.175  1.00 74.65  ? 150  TYR   D CG   1 
ATOM   21553 C  CD1  . TYR   D  4  150 ? 20.705  -70.417 -72.353  1.00 69.90  ? 150  TYR   D CD1  1 
ATOM   21554 C  CD2  . TYR   D  4  150 ? 21.327  -69.478 -70.254  1.00 75.73  ? 150  TYR   D CD2  1 
ATOM   21555 C  CE1  . TYR   D  4  150 ? 19.892  -69.326 -72.605  1.00 68.17  ? 150  TYR   D CE1  1 
ATOM   21556 C  CE2  . TYR   D  4  150 ? 20.517  -68.383 -70.497  1.00 73.78  ? 150  TYR   D CE2  1 
ATOM   21557 C  CZ   . TYR   D  4  150 ? 19.802  -68.312 -71.674  1.00 70.06  ? 150  TYR   D CZ   1 
ATOM   21558 O  OH   . TYR   D  4  150 ? 18.996  -67.223 -71.919  1.00 67.31  ? 150  TYR   D OH   1 
ATOM   21559 H  H    . TYR   D  4  150 ? 19.984  -72.937 -71.352  1.00 89.48  ? 150  TYR   D H    1 
ATOM   21560 H  HA   . TYR   D  4  150 ? 22.279  -73.570 -70.046  1.00 90.97  ? 150  TYR   D HA   1 
ATOM   21561 H  HB2  . TYR   D  4  150 ? 23.038  -71.412 -70.321  1.00 92.07  ? 150  TYR   D HB2  1 
ATOM   21562 H  HB3  . TYR   D  4  150 ? 22.690  -71.994 -71.758  1.00 92.07  ? 150  TYR   D HB3  1 
ATOM   21563 H  HD1  . TYR   D  4  150 ? 20.765  -71.097 -72.984  1.00 83.86  ? 150  TYR   D HD1  1 
ATOM   21564 H  HD2  . TYR   D  4  150 ? 21.810  -69.522 -69.461  1.00 90.86  ? 150  TYR   D HD2  1 
ATOM   21565 H  HE1  . TYR   D  4  150 ? 19.409  -69.276 -73.399  1.00 81.79  ? 150  TYR   D HE1  1 
ATOM   21566 H  HE2  . TYR   D  4  150 ? 20.455  -67.699 -69.870  1.00 88.52  ? 150  TYR   D HE2  1 
ATOM   21567 H  HH   . TYR   D  4  150 ? 18.995  -66.710 -71.254  1.00 80.75  ? 150  TYR   D HH   1 
ATOM   21568 N  N    . PHE   D  4  151 ? 21.799  -72.289 -67.926  1.00 77.05  ? 151  PHE   D N    1 
ATOM   21569 C  CA   . PHE   D  4  151 ? 21.333  -71.814 -66.634  1.00 77.16  ? 151  PHE   D CA   1 
ATOM   21570 C  C    . PHE   D  4  151 ? 22.536  -71.359 -65.830  1.00 79.32  ? 151  PHE   D C    1 
ATOM   21571 O  O    . PHE   D  4  151 ? 23.584  -72.016 -65.893  1.00 79.24  ? 151  PHE   D O    1 
ATOM   21572 C  CB   . PHE   D  4  151 ? 20.576  -72.906 -65.871  1.00 76.66  ? 151  PHE   D CB   1 
ATOM   21573 C  CG   . PHE   D  4  151 ? 20.053  -72.455 -64.538  1.00 79.89  ? 151  PHE   D CG   1 
ATOM   21574 C  CD1  . PHE   D  4  151 ? 20.820  -72.592 -63.392  1.00 86.34  ? 151  PHE   D CD1  1 
ATOM   21575 C  CD2  . PHE   D  4  151 ? 18.796  -71.884 -64.432  1.00 79.69  ? 151  PHE   D CD2  1 
ATOM   21576 C  CE1  . PHE   D  4  151 ? 20.341  -72.173 -62.165  1.00 91.33  ? 151  PHE   D CE1  1 
ATOM   21577 C  CE2  . PHE   D  4  151 ? 18.312  -71.462 -63.210  1.00 84.28  ? 151  PHE   D CE2  1 
ATOM   21578 C  CZ   . PHE   D  4  151 ? 19.085  -71.607 -62.074  1.00 90.41  ? 151  PHE   D CZ   1 
ATOM   21579 H  H    . PHE   D  4  151 ? 22.643  -72.450 -67.958  1.00 92.45  ? 151  PHE   D H    1 
ATOM   21580 H  HA   . PHE   D  4  151 ? 20.737  -71.060 -66.764  1.00 92.58  ? 151  PHE   D HA   1 
ATOM   21581 H  HB2  . PHE   D  4  151 ? 19.819  -73.193 -66.406  1.00 91.97  ? 151  PHE   D HB2  1 
ATOM   21582 H  HB3  . PHE   D  4  151 ? 21.176  -73.653 -65.717  1.00 91.97  ? 151  PHE   D HB3  1 
ATOM   21583 H  HD1  . PHE   D  4  151 ? 21.667  -72.971 -63.449  1.00 103.59 ? 151  PHE   D HD1  1 
ATOM   21584 H  HD2  . PHE   D  4  151 ? 18.271  -71.784 -65.194  1.00 95.61  ? 151  PHE   D HD2  1 
ATOM   21585 H  HE1  . PHE   D  4  151 ? 20.864  -72.272 -61.403  1.00 109.57 ? 151  PHE   D HE1  1 
ATOM   21586 H  HE2  . PHE   D  4  151 ? 17.466  -71.080 -63.151  1.00 101.11 ? 151  PHE   D HE2  1 
ATOM   21587 H  HZ   . PHE   D  4  151 ? 18.760  -71.324 -61.250  1.00 108.47 ? 151  PHE   D HZ   1 
ATOM   21588 N  N    . PRO   D  4  152 ? 22.440  -70.253 -65.075  1.00 81.05  ? 152  PRO   D N    1 
ATOM   21589 C  CA   . PRO   D  4  152 ? 21.289  -69.351 -64.994  1.00 79.15  ? 152  PRO   D CA   1 
ATOM   21590 C  C    . PRO   D  4  152 ? 21.377  -68.226 -66.010  1.00 76.33  ? 152  PRO   D C    1 
ATOM   21591 O  O    . PRO   D  4  152 ? 22.363  -68.138 -66.744  1.00 74.30  ? 152  PRO   D O    1 
ATOM   21592 C  CB   . PRO   D  4  152 ? 21.390  -68.801 -63.576  1.00 83.69  ? 152  PRO   D CB   1 
ATOM   21593 C  CG   . PRO   D  4  152 ? 22.864  -68.704 -63.354  1.00 86.10  ? 152  PRO   D CG   1 
ATOM   21594 C  CD   . PRO   D  4  152 ? 23.488  -69.863 -64.114  1.00 85.08  ? 152  PRO   D CD   1 
ATOM   21595 H  HA   . PRO   D  4  152 ? 20.452  -69.830 -65.104  1.00 94.96  ? 152  PRO   D HA   1 
ATOM   21596 H  HB2  . PRO   D  4  152 ? 20.966  -67.931 -63.520  1.00 100.41 ? 152  PRO   D HB2  1 
ATOM   21597 H  HB3  . PRO   D  4  152 ? 20.977  -69.413 -62.946  1.00 100.41 ? 152  PRO   D HB3  1 
ATOM   21598 H  HG2  . PRO   D  4  152 ? 23.189  -67.857 -63.696  1.00 103.30 ? 152  PRO   D HG2  1 
ATOM   21599 H  HG3  . PRO   D  4  152 ? 23.055  -68.775 -62.406  1.00 103.30 ? 152  PRO   D HG3  1 
ATOM   21600 H  HD2  . PRO   D  4  152 ? 24.291  -69.578 -64.578  1.00 102.08 ? 152  PRO   D HD2  1 
ATOM   21601 H  HD3  . PRO   D  4  152 ? 23.695  -70.597 -63.514  1.00 102.08 ? 152  PRO   D HD3  1 
ATOM   21602 N  N    . GLU   D  4  153 ? 20.354  -67.380 -66.061  1.00 76.52  ? 153  GLU   D N    1 
ATOM   21603 C  CA   . GLU   D  4  153 ? 20.511  -66.099 -66.721  1.00 76.89  ? 153  GLU   D CA   1 
ATOM   21604 C  C    . GLU   D  4  153 ? 21.660  -65.345 -66.052  1.00 75.87  ? 153  GLU   D C    1 
ATOM   21605 O  O    . GLU   D  4  153 ? 21.959  -65.574 -64.876  1.00 75.40  ? 153  GLU   D O    1 
ATOM   21606 C  CB   . GLU   D  4  153 ? 19.219  -65.289 -66.637  1.00 85.37  ? 153  GLU   D CB   1 
ATOM   21607 C  CG   . GLU   D  4  153 ? 18.084  -65.838 -67.491  1.00 90.42  ? 153  GLU   D CG   1 
ATOM   21608 C  CD   . GLU   D  4  153 ? 18.002  -65.179 -68.854  1.00 94.07  ? 153  GLU   D CD   1 
ATOM   21609 O  OE1  . GLU   D  4  153 ? 17.392  -64.094 -68.953  1.00 96.47  ? 153  GLU   D OE1  1 
ATOM   21610 O  OE2  . GLU   D  4  153 ? 18.552  -65.741 -69.825  1.00 93.79  ? 153  GLU   D OE2  1 
ATOM   21611 H  H    . GLU   D  4  153 ? 19.575  -67.525 -65.727  1.00 91.80  ? 153  GLU   D H    1 
ATOM   21612 H  HA   . GLU   D  4  153 ? 20.713  -66.221 -67.661  1.00 92.25  ? 153  GLU   D HA   1 
ATOM   21613 H  HB2  . GLU   D  4  153 ? 18.917  -65.280 -65.715  1.00 102.43 ? 153  GLU   D HB2  1 
ATOM   21614 H  HB3  . GLU   D  4  153 ? 19.401  -64.384 -66.935  1.00 102.43 ? 153  GLU   D HB3  1 
ATOM   21615 H  HG2  . GLU   D  4  153 ? 18.221  -66.789 -67.625  1.00 108.49 ? 153  GLU   D HG2  1 
ATOM   21616 H  HG3  . GLU   D  4  153 ? 17.242  -65.686 -67.033  1.00 108.49 ? 153  GLU   D HG3  1 
ATOM   21617 N  N    . PRO   D  4  154 ? 22.330  -64.437 -66.774  1.00 79.03  ? 154  PRO   D N    1 
ATOM   21618 C  CA   . PRO   D  4  154 ? 22.084  -64.032 -68.157  1.00 80.33  ? 154  PRO   D CA   1 
ATOM   21619 C  C    . PRO   D  4  154 ? 22.998  -64.695 -69.179  1.00 86.72  ? 154  PRO   D C    1 
ATOM   21620 O  O    . PRO   D  4  154 ? 23.975  -65.357 -68.826  1.00 92.88  ? 154  PRO   D O    1 
ATOM   21621 C  CB   . PRO   D  4  154 ? 22.360  -62.532 -68.112  1.00 80.22  ? 154  PRO   D CB   1 
ATOM   21622 C  CG   . PRO   D  4  154 ? 23.504  -62.429 -67.137  1.00 83.95  ? 154  PRO   D CG   1 
ATOM   21623 C  CD   . PRO   D  4  154 ? 23.330  -63.562 -66.135  1.00 83.37  ? 154  PRO   D CD   1 
ATOM   21624 H  HA   . PRO   D  4  154 ? 21.163  -64.217 -68.399  1.00 96.37  ? 154  PRO   D HA   1 
ATOM   21625 H  HB2  . PRO   D  4  154 ? 22.613  -62.207 -68.990  1.00 96.25  ? 154  PRO   D HB2  1 
ATOM   21626 H  HB3  . PRO   D  4  154 ? 21.579  -62.053 -67.793  1.00 96.25  ? 154  PRO   D HB3  1 
ATOM   21627 H  HG2  . PRO   D  4  154 ? 24.344  -62.522 -67.613  1.00 100.72 ? 154  PRO   D HG2  1 
ATOM   21628 H  HG3  . PRO   D  4  154 ? 23.470  -61.570 -66.688  1.00 100.72 ? 154  PRO   D HG3  1 
ATOM   21629 H  HD2  . PRO   D  4  154 ? 24.166  -64.036 -66.002  1.00 100.02 ? 154  PRO   D HD2  1 
ATOM   21630 H  HD3  . PRO   D  4  154 ? 23.001  -63.225 -65.287  1.00 100.02 ? 154  PRO   D HD3  1 
ATOM   21631 N  N    . VAL   D  4  155 ? 22.657  -64.508 -70.450  1.00 85.63  ? 155  VAL   D N    1 
ATOM   21632 C  CA   . VAL   D  4  155 ? 23.531  -64.819 -71.570  1.00 84.38  ? 155  VAL   D CA   1 
ATOM   21633 C  C    . VAL   D  4  155 ? 23.577  -63.586 -72.460  1.00 82.91  ? 155  VAL   D C    1 
ATOM   21634 O  O    . VAL   D  4  155 ? 22.580  -62.863 -72.590  1.00 87.95  ? 155  VAL   D O    1 
ATOM   21635 C  CB   . VAL   D  4  155 ? 23.055  -66.054 -72.365  1.00 83.55  ? 155  VAL   D CB   1 
ATOM   21636 C  CG1  . VAL   D  4  155 ? 21.727  -65.770 -73.052  1.00 83.76  ? 155  VAL   D CG1  1 
ATOM   21637 C  CG2  . VAL   D  4  155 ? 24.110  -66.480 -73.380  1.00 82.46  ? 155  VAL   D CG2  1 
ATOM   21638 H  H    . VAL   D  4  155 ? 21.896  -64.190 -70.695  1.00 102.74 ? 155  VAL   D H    1 
ATOM   21639 H  HA   . VAL   D  4  155 ? 24.423  -65.016 -71.244  1.00 101.23 ? 155  VAL   D HA   1 
ATOM   21640 H  HB   . VAL   D  4  155 ? 22.921  -66.790 -71.747  1.00 100.24 ? 155  VAL   D HB   1 
ATOM   21641 H  HG11 . VAL   D  4  155 ? 21.400  -66.588 -73.458  1.00 100.50 ? 155  VAL   D HG11 1 
ATOM   21642 H  HG12 . VAL   D  4  155 ? 21.091  -65.452 -72.392  1.00 100.50 ? 155  VAL   D HG12 1 
ATOM   21643 H  HG13 . VAL   D  4  155 ? 21.862  -65.094 -73.734  1.00 100.50 ? 155  VAL   D HG13 1 
ATOM   21644 H  HG21 . VAL   D  4  155 ? 23.770  -67.229 -73.894  1.00 98.94  ? 155  VAL   D HG21 1 
ATOM   21645 H  HG22 . VAL   D  4  155 ? 24.301  -65.734 -73.969  1.00 98.94  ? 155  VAL   D HG22 1 
ATOM   21646 H  HG23 . VAL   D  4  155 ? 24.916  -66.742 -72.907  1.00 98.94  ? 155  VAL   D HG23 1 
ATOM   21647 N  N    . THR   D  4  156 ? 24.732  -63.338 -73.058  1.00 78.48  ? 156  THR   D N    1 
ATOM   21648 C  CA   . THR   D  4  156 ? 24.921  -62.207 -73.955  1.00 79.26  ? 156  THR   D CA   1 
ATOM   21649 C  C    . THR   D  4  156 ? 25.148  -62.721 -75.370  1.00 79.26  ? 156  THR   D C    1 
ATOM   21650 O  O    . THR   D  4  156 ? 25.923  -63.662 -75.579  1.00 83.90  ? 156  THR   D O    1 
ATOM   21651 C  CB   . THR   D  4  156 ? 26.097  -61.334 -73.513  1.00 83.11  ? 156  THR   D CB   1 
ATOM   21652 O  OG1  . THR   D  4  156 ? 27.325  -62.047 -73.699  1.00 86.27  ? 156  THR   D OG1  1 
ATOM   21653 C  CG2  . THR   D  4  156 ? 25.958  -60.946 -72.045  1.00 85.92  ? 156  THR   D CG2  1 
ATOM   21654 H  H    . THR   D  4  156 ? 25.437  -63.820 -72.958  1.00 94.16  ? 156  THR   D H    1 
ATOM   21655 H  HA   . THR   D  4  156 ? 24.122  -61.657 -73.951  1.00 95.10  ? 156  THR   D HA   1 
ATOM   21656 H  HB   . THR   D  4  156 ? 26.111  -60.522 -74.044  1.00 99.72  ? 156  THR   D HB   1 
ATOM   21657 H  HG1  . THR   D  4  156 ? 27.922  -61.725 -73.204  1.00 103.50 ? 156  THR   D HG1  1 
ATOM   21658 H  HG21 . THR   D  4  156 ? 26.695  -60.374 -71.782  1.00 103.09 ? 156  THR   D HG21 1 
ATOM   21659 H  HG22 . THR   D  4  156 ? 25.124  -60.470 -71.906  1.00 103.09 ? 156  THR   D HG22 1 
ATOM   21660 H  HG23 . THR   D  4  156 ? 25.963  -61.742 -71.490  1.00 103.09 ? 156  THR   D HG23 1 
ATOM   21661 N  N    . LEU   D  4  157 ? 24.468  -62.106 -76.332  1.00 75.55  ? 157  LEU   D N    1 
ATOM   21662 C  CA   . LEU   D  4  157 ? 24.529  -62.525 -77.725  1.00 72.45  ? 157  LEU   D CA   1 
ATOM   21663 C  C    . LEU   D  4  157 ? 24.745  -61.311 -78.614  1.00 74.79  ? 157  LEU   D C    1 
ATOM   21664 O  O    . LEU   D  4  157 ? 24.092  -60.277 -78.436  1.00 75.78  ? 157  LEU   D O    1 
ATOM   21665 C  CB   . LEU   D  4  157 ? 23.248  -63.264 -78.139  1.00 70.35  ? 157  LEU   D CB   1 
ATOM   21666 C  CG   . LEU   D  4  157 ? 23.169  -63.759 -79.587  1.00 71.16  ? 157  LEU   D CG   1 
ATOM   21667 C  CD1  . LEU   D  4  157 ? 22.349  -65.038 -79.657  1.00 67.27  ? 157  LEU   D CD1  1 
ATOM   21668 C  CD2  . LEU   D  4  157 ? 22.570  -62.706 -80.512  1.00 72.30  ? 157  LEU   D CD2  1 
ATOM   21669 H  H    . LEU   D  4  157 ? 23.955  -61.429 -76.199  1.00 90.64  ? 157  LEU   D H    1 
ATOM   21670 H  HA   . LEU   D  4  157 ? 25.283  -63.124 -77.845  1.00 86.92  ? 157  LEU   D HA   1 
ATOM   21671 H  HB2  . LEU   D  4  157 ? 23.155  -64.043 -77.569  1.00 84.41  ? 157  LEU   D HB2  1 
ATOM   21672 H  HB3  . LEU   D  4  157 ? 22.499  -62.662 -78.005  1.00 84.41  ? 157  LEU   D HB3  1 
ATOM   21673 H  HG   . LEU   D  4  157 ? 24.070  -63.940 -79.897  1.00 85.37  ? 157  LEU   D HG   1 
ATOM   21674 H  HD11 . LEU   D  4  157 ? 22.296  -65.329 -80.581  1.00 80.71  ? 157  LEU   D HD11 1 
ATOM   21675 H  HD12 . LEU   D  4  157 ? 22.782  -65.720 -79.120  1.00 80.71  ? 157  LEU   D HD12 1 
ATOM   21676 H  HD13 . LEU   D  4  157 ? 21.459  -64.861 -79.313  1.00 80.71  ? 157  LEU   D HD13 1 
ATOM   21677 H  HD21 . LEU   D  4  157 ? 22.448  -63.091 -81.394  1.00 86.74  ? 157  LEU   D HD21 1 
ATOM   21678 H  HD22 . LEU   D  4  157 ? 21.714  -62.421 -80.154  1.00 86.74  ? 157  LEU   D HD22 1 
ATOM   21679 H  HD23 . LEU   D  4  157 ? 23.175  -61.949 -80.563  1.00 86.74  ? 157  LEU   D HD23 1 
ATOM   21680 N  N    . THR   D  4  158 ? 25.659  -61.446 -79.570  1.00 76.47  ? 158  THR   D N    1 
ATOM   21681 C  CA   . THR   D  4  158 ? 25.920  -60.405 -80.551  1.00 78.80  ? 158  THR   D CA   1 
ATOM   21682 C  C    . THR   D  4  158 ? 26.139  -61.054 -81.910  1.00 80.23  ? 158  THR   D C    1 
ATOM   21683 O  O    . THR   D  4  158 ? 26.360  -62.263 -82.017  1.00 79.53  ? 158  THR   D O    1 
ATOM   21684 C  CB   . THR   D  4  158 ? 27.140  -59.553 -80.172  1.00 80.50  ? 158  THR   D CB   1 
ATOM   21685 O  OG1  . THR   D  4  158 ? 28.291  -60.395 -80.030  1.00 81.48  ? 158  THR   D OG1  1 
ATOM   21686 C  CG2  . THR   D  4  158 ? 26.889  -58.810 -78.869  1.00 81.02  ? 158  THR   D CG2  1 
ATOM   21687 H  H    . THR   D  4  158 ? 26.149  -62.145 -79.671  1.00 91.75  ? 158  THR   D H    1 
ATOM   21688 H  HA   . THR   D  4  158 ? 25.150  -59.818 -80.609  1.00 94.54  ? 158  THR   D HA   1 
ATOM   21689 H  HB   . THR   D  4  158 ? 27.306  -58.898 -80.868  1.00 96.58  ? 158  THR   D HB   1 
ATOM   21690 H  HG1  . THR   D  4  158 ? 28.960  -59.933 -79.817  1.00 97.75  ? 158  THR   D HG1  1 
ATOM   21691 H  HG21 . THR   D  4  158 ? 27.658  -58.263 -78.645  1.00 97.21  ? 158  THR   D HG21 1 
ATOM   21692 H  HG22 . THR   D  4  158 ? 26.111  -58.238 -78.958  1.00 97.21  ? 158  THR   D HG22 1 
ATOM   21693 H  HG23 . THR   D  4  158 ? 26.734  -59.444 -78.151  1.00 97.21  ? 158  THR   D HG23 1 
ATOM   21694 N  N    . TRP   D  4  159 ? 26.072  -60.231 -82.954  1.00 82.58  ? 159  TRP   D N    1 
ATOM   21695 C  CA   . TRP   D  4  159 ? 26.295  -60.667 -84.327  1.00 85.44  ? 159  TRP   D CA   1 
ATOM   21696 C  C    . TRP   D  4  159 ? 27.522  -59.947 -84.866  1.00 90.48  ? 159  TRP   D C    1 
ATOM   21697 O  O    . TRP   D  4  159 ? 27.563  -58.712 -84.879  1.00 90.49  ? 159  TRP   D O    1 
ATOM   21698 C  CB   . TRP   D  4  159 ? 25.071  -60.387 -85.200  1.00 84.66  ? 159  TRP   D CB   1 
ATOM   21699 C  CG   . TRP   D  4  159 ? 23.886  -61.244 -84.869  1.00 81.16  ? 159  TRP   D CG   1 
ATOM   21700 C  CD1  . TRP   D  4  159 ? 22.850  -60.928 -84.037  1.00 78.34  ? 159  TRP   D CD1  1 
ATOM   21701 C  CD2  . TRP   D  4  159 ? 23.614  -62.561 -85.364  1.00 80.89  ? 159  TRP   D CD2  1 
ATOM   21702 N  NE1  . TRP   D  4  159 ? 21.951  -61.966 -83.985  1.00 76.35  ? 159  TRP   D NE1  1 
ATOM   21703 C  CE2  . TRP   D  4  159 ? 22.398  -62.980 -84.790  1.00 77.61  ? 159  TRP   D CE2  1 
ATOM   21704 C  CE3  . TRP   D  4  159 ? 24.283  -63.426 -86.236  1.00 83.48  ? 159  TRP   D CE3  1 
ATOM   21705 C  CZ2  . TRP   D  4  159 ? 21.835  -64.226 -85.061  1.00 76.88  ? 159  TRP   D CZ2  1 
ATOM   21706 C  CZ3  . TRP   D  4  159 ? 23.722  -64.661 -86.503  1.00 83.43  ? 159  TRP   D CZ3  1 
ATOM   21707 C  CH2  . TRP   D  4  159 ? 22.511  -65.049 -85.919  1.00 79.16  ? 159  TRP   D CH2  1 
ATOM   21708 H  H    . TRP   D  4  159 ? 25.893  -59.392 -82.888  1.00 99.08  ? 159  TRP   D H    1 
ATOM   21709 H  HA   . TRP   D  4  159 ? 26.466  -61.622 -84.344  1.00 102.50 ? 159  TRP   D HA   1 
ATOM   21710 H  HB2  . TRP   D  4  159 ? 24.809  -59.460 -85.083  1.00 101.57 ? 159  TRP   D HB2  1 
ATOM   21711 H  HB3  . TRP   D  4  159 ? 25.305  -60.551 -86.127  1.00 101.57 ? 159  TRP   D HB3  1 
ATOM   21712 H  HD1  . TRP   D  4  159 ? 22.765  -60.126 -83.573  1.00 93.99  ? 159  TRP   D HD1  1 
ATOM   21713 H  HE1  . TRP   D  4  159 ? 21.226  -61.977 -83.522  1.00 91.60  ? 159  TRP   D HE1  1 
ATOM   21714 H  HE3  . TRP   D  4  159 ? 25.088  -63.175 -86.628  1.00 100.16 ? 159  TRP   D HE3  1 
ATOM   21715 H  HZ2  . TRP   D  4  159 ? 21.032  -64.487 -84.673  1.00 92.24  ? 159  TRP   D HZ2  1 
ATOM   21716 H  HZ3  . TRP   D  4  159 ? 24.158  -65.245 -87.081  1.00 100.09 ? 159  TRP   D HZ3  1 
ATOM   21717 H  HH2  . TRP   D  4  159 ? 22.157  -65.885 -86.119  1.00 94.98  ? 159  TRP   D HH2  1 
ATOM   21718 N  N    . ASN   D  4  160 ? 28.512  -60.717 -85.313  1.00 94.61  ? 160  ASN   D N    1 
ATOM   21719 C  CA   . ASN   D  4  160 ? 29.790  -60.172 -85.763  1.00 98.96  ? 160  ASN   D CA   1 
ATOM   21720 C  C    . ASN   D  4  160 ? 30.354  -59.197 -84.731  1.00 103.40 ? 160  ASN   D C    1 
ATOM   21721 O  O    . ASN   D  4  160 ? 30.765  -58.078 -85.046  1.00 108.83 ? 160  ASN   D O    1 
ATOM   21722 C  CB   . ASN   D  4  160 ? 29.652  -59.505 -87.133  1.00 97.35  ? 160  ASN   D CB   1 
ATOM   21723 C  CG   . ASN   D  4  160 ? 29.630  -60.510 -88.268  1.00 95.57  ? 160  ASN   D CG   1 
ATOM   21724 O  OD1  . ASN   D  4  160 ? 30.221  -61.585 -88.172  1.00 93.56  ? 160  ASN   D OD1  1 
ATOM   21725 N  ND2  . ASN   D  4  160 ? 28.951  -60.162 -89.354  1.00 98.19  ? 160  ASN   D ND2  1 
ATOM   21726 H  H    . ASN   D  4  160 ? 28.466  -61.574 -85.366  1.00 113.51 ? 160  ASN   D H    1 
ATOM   21727 H  HA   . ASN   D  4  160 ? 30.421  -60.903 -85.853  1.00 118.73 ? 160  ASN   D HA   1 
ATOM   21728 H  HB2  . ASN   D  4  160 ? 28.822  -59.004 -87.159  1.00 116.81 ? 160  ASN   D HB2  1 
ATOM   21729 H  HB3  . ASN   D  4  160 ? 30.405  -58.909 -87.272  1.00 116.81 ? 160  ASN   D HB3  1 
ATOM   21730 H  HD21 . ASN   D  4  160 ? 28.909  -60.698 -90.025  1.00 117.81 ? 160  ASN   D HD21 1 
ATOM   21731 H  HD22 . ASN   D  4  160 ? 28.552  -59.400 -89.387  1.00 117.81 ? 160  ASN   D HD22 1 
ATOM   21732 N  N    . SER   D  4  161 ? 30.363  -59.638 -83.473  1.00 100.79 ? 161  SER   D N    1 
ATOM   21733 C  CA   . SER   D  4  161 ? 30.941  -58.868 -82.374  1.00 103.02 ? 161  SER   D CA   1 
ATOM   21734 C  C    . SER   D  4  161 ? 30.227  -57.533 -82.177  1.00 101.03 ? 161  SER   D C    1 
ATOM   21735 O  O    . SER   D  4  161 ? 30.848  -56.528 -81.829  1.00 104.75 ? 161  SER   D O    1 
ATOM   21736 C  CB   . SER   D  4  161 ? 32.437  -58.634 -82.599  1.00 108.28 ? 161  SER   D CB   1 
ATOM   21737 O  OG   . SER   D  4  161 ? 33.091  -59.844 -82.936  1.00 106.83 ? 161  SER   D OG   1 
ATOM   21738 H  H    . SER   D  4  161 ? 30.035  -60.394 -83.228  1.00 120.93 ? 161  SER   D H    1 
ATOM   21739 H  HA   . SER   D  4  161 ? 30.824  -59.381 -81.559  1.00 123.61 ? 161  SER   D HA   1 
ATOM   21740 H  HB2  . SER   D  4  161 ? 32.552  -58.000 -83.324  1.00 129.92 ? 161  SER   D HB2  1 
ATOM   21741 H  HB3  . SER   D  4  161 ? 32.828  -58.281 -81.784  1.00 129.92 ? 161  SER   D HB3  1 
ATOM   21742 H  HG   . SER   D  4  161 ? 33.901  -59.696 -83.103  1.00 128.17 ? 161  SER   D HG   1 
ATOM   21743 N  N    . GLY   D  4  162 ? 28.913  -57.517 -82.397  1.00 95.33  ? 162  GLY   D N    1 
ATOM   21744 C  CA   . GLY   D  4  162 ? 28.129  -56.312 -82.232  1.00 93.07  ? 162  GLY   D CA   1 
ATOM   21745 C  C    . GLY   D  4  162 ? 28.169  -55.355 -83.402  1.00 93.68  ? 162  GLY   D C    1 
ATOM   21746 O  O    . GLY   D  4  162 ? 27.482  -54.326 -83.360  1.00 92.36  ? 162  GLY   D O    1 
ATOM   21747 H  H    . GLY   D  4  162 ? 28.455  -58.202 -82.645  1.00 114.38 ? 162  GLY   D H    1 
ATOM   21748 H  HA2  . GLY   D  4  162 ? 27.203  -56.562 -82.087  1.00 111.66 ? 162  GLY   D HA2  1 
ATOM   21749 H  HA3  . GLY   D  4  162 ? 28.454  -55.836 -81.452  1.00 111.66 ? 162  GLY   D HA3  1 
ATOM   21750 N  N    . SER   D  4  163 ? 28.948  -55.656 -84.443  1.00 96.93  ? 163  SER   D N    1 
ATOM   21751 C  CA   . SER   D  4  163 ? 28.984  -54.788 -85.615  1.00 102.61 ? 163  SER   D CA   1 
ATOM   21752 C  C    . SER   D  4  163 ? 27.613  -54.672 -86.266  1.00 97.87  ? 163  SER   D C    1 
ATOM   21753 O  O    . SER   D  4  163 ? 27.307  -53.651 -86.893  1.00 96.85  ? 163  SER   D O    1 
ATOM   21754 C  CB   . SER   D  4  163 ? 30.003  -55.316 -86.624  1.00 112.91 ? 163  SER   D CB   1 
ATOM   21755 O  OG   . SER   D  4  163 ? 29.861  -54.675 -87.879  1.00 123.60 ? 163  SER   D OG   1 
ATOM   21756 H  H    . SER   D  4  163 ? 29.459  -56.346 -84.494  1.00 116.30 ? 163  SER   D H    1 
ATOM   21757 H  HA   . SER   D  4  163 ? 29.262  -53.901 -85.340  1.00 123.11 ? 163  SER   D HA   1 
ATOM   21758 H  HB2  . SER   D  4  163 ? 30.897  -55.149 -86.285  1.00 135.47 ? 163  SER   D HB2  1 
ATOM   21759 H  HB3  . SER   D  4  163 ? 29.866  -56.270 -86.740  1.00 135.47 ? 163  SER   D HB3  1 
ATOM   21760 H  HG   . SER   D  4  163 ? 30.405  -54.999 -88.431  1.00 148.30 ? 163  SER   D HG   1 
ATOM   21761 N  N    . LEU   D  4  164 ? 26.781  -55.700 -86.134  1.00 94.84  ? 164  LEU   D N    1 
ATOM   21762 C  CA   . LEU   D  4  164 ? 25.429  -55.712 -86.685  1.00 93.75  ? 164  LEU   D CA   1 
ATOM   21763 C  C    . LEU   D  4  164 ? 24.455  -55.521 -85.526  1.00 96.12  ? 164  LEU   D C    1 
ATOM   21764 O  O    . LEU   D  4  164 ? 24.189  -56.459 -84.769  1.00 100.11 ? 164  LEU   D O    1 
ATOM   21765 C  CB   . LEU   D  4  164 ? 25.153  -57.014 -87.429  1.00 87.78  ? 164  LEU   D CB   1 
ATOM   21766 C  CG   . LEU   D  4  164 ? 26.173  -57.432 -88.488  1.00 88.89  ? 164  LEU   D CG   1 
ATOM   21767 C  CD1  . LEU   D  4  164 ? 25.843  -58.821 -89.016  1.00 87.24  ? 164  LEU   D CD1  1 
ATOM   21768 C  CD2  . LEU   D  4  164 ? 26.222  -56.425 -89.624  1.00 92.81  ? 164  LEU   D CD2  1 
ATOM   21769 H  H    . LEU   D  4  164 ? 26.983  -56.425 -85.717  1.00 113.79 ? 164  LEU   D H    1 
ATOM   21770 H  HA   . LEU   D  4  164 ? 25.327  -54.974 -87.306  1.00 112.48 ? 164  LEU   D HA   1 
ATOM   21771 H  HB2  . LEU   D  4  164 ? 25.114  -57.730 -86.775  1.00 105.32 ? 164  LEU   D HB2  1 
ATOM   21772 H  HB3  . LEU   D  4  164 ? 24.297  -56.927 -87.877  1.00 105.32 ? 164  LEU   D HB3  1 
ATOM   21773 H  HG   . LEU   D  4  164 ? 27.054  -57.459 -88.083  1.00 106.65 ? 164  LEU   D HG   1 
ATOM   21774 H  HD11 . LEU   D  4  164 ? 26.490  -59.062 -89.698  1.00 104.67 ? 164  LEU   D HD11 1 
ATOM   21775 H  HD12 . LEU   D  4  164 ? 25.883  -59.455 -88.284  1.00 104.67 ? 164  LEU   D HD12 1 
ATOM   21776 H  HD13 . LEU   D  4  164 ? 24.951  -58.810 -89.397  1.00 104.67 ? 164  LEU   D HD13 1 
ATOM   21777 H  HD21 . LEU   D  4  164 ? 26.866  -56.725 -90.285  1.00 111.35 ? 164  LEU   D HD21 1 
ATOM   21778 H  HD22 . LEU   D  4  164 ? 25.341  -56.360 -90.026  1.00 111.35 ? 164  LEU   D HD22 1 
ATOM   21779 H  HD23 . LEU   D  4  164 ? 26.488  -55.562 -89.270  1.00 111.35 ? 164  LEU   D HD23 1 
ATOM   21780 N  N    . SER   D  4  165 ? 23.933  -54.305 -85.386  1.00 96.83  ? 165  SER   D N    1 
ATOM   21781 C  CA   . SER   D  4  165 ? 22.926  -53.990 -84.380  1.00 95.66  ? 165  SER   D CA   1 
ATOM   21782 C  C    . SER   D  4  165 ? 21.555  -53.754 -84.994  1.00 91.97  ? 165  SER   D C    1 
ATOM   21783 O  O    . SER   D  4  165 ? 20.571  -54.364 -84.567  1.00 85.96  ? 165  SER   D O    1 
ATOM   21784 C  CB   . SER   D  4  165 ? 23.352  -52.756 -83.572  1.00 108.00 ? 165  SER   D CB   1 
ATOM   21785 O  OG   . SER   D  4  165 ? 23.420  -51.603 -84.393  1.00 119.44 ? 165  SER   D OG   1 
ATOM   21786 H  H    . SER   D  4  165 ? 24.152  -53.631 -85.873  1.00 116.17 ? 165  SER   D H    1 
ATOM   21787 H  HA   . SER   D  4  165 ? 22.856  -54.735 -83.763  1.00 114.78 ? 165  SER   D HA   1 
ATOM   21788 H  HB2  . SER   D  4  165 ? 22.702  -52.602 -82.868  1.00 129.58 ? 165  SER   D HB2  1 
ATOM   21789 H  HB3  . SER   D  4  165 ? 24.227  -52.920 -83.186  1.00 129.58 ? 165  SER   D HB3  1 
ATOM   21790 H  HG   . SER   D  4  165 ? 23.672  -50.943 -83.940  1.00 143.30 ? 165  SER   D HG   1 
ATOM   21791 N  N    . ALA   D  4  166 ? 21.467  -52.876 -85.991  1.00 98.06  ? 166  ALA   D N    1 
ATOM   21792 C  CA   . ALA   D  4  166 ? 20.216  -52.698 -86.712  1.00 100.52 ? 166  ALA   D CA   1 
ATOM   21793 C  C    . ALA   D  4  166 ? 19.859  -53.981 -87.454  1.00 102.94 ? 166  ALA   D C    1 
ATOM   21794 O  O    . ALA   D  4  166 ? 20.735  -54.695 -87.950  1.00 102.05 ? 166  ALA   D O    1 
ATOM   21795 C  CB   . ALA   D  4  166 ? 20.328  -51.531 -87.693  1.00 102.92 ? 166  ALA   D CB   1 
ATOM   21796 H  H    . ALA   D  4  166 ? 22.111  -52.378 -86.265  1.00 117.66 ? 166  ALA   D H    1 
ATOM   21797 H  HA   . ALA   D  4  166 ? 19.503  -52.492 -86.088  1.00 120.61 ? 166  ALA   D HA   1 
ATOM   21798 H  HB1  . ALA   D  4  166 ? 19.487  -51.433 -88.165  1.00 123.48 ? 166  ALA   D HB1  1 
ATOM   21799 H  HB2  . ALA   D  4  166 ? 20.526  -50.721 -87.197  1.00 123.48 ? 166  ALA   D HB2  1 
ATOM   21800 H  HB3  . ALA   D  4  166 ? 21.042  -51.716 -88.323  1.00 123.48 ? 166  ALA   D HB3  1 
ATOM   21801 N  N    . GLY   D  4  167 ? 18.564  -54.272 -87.525  1.00 104.51 ? 167  GLY   D N    1 
ATOM   21802 C  CA   . GLY   D  4  167 ? 18.117  -55.504 -88.139  1.00 103.05 ? 167  GLY   D CA   1 
ATOM   21803 C  C    . GLY   D  4  167 ? 18.327  -56.737 -87.293  1.00 97.16  ? 167  GLY   D C    1 
ATOM   21804 O  O    . GLY   D  4  167 ? 18.275  -57.852 -87.821  1.00 95.91  ? 167  GLY   D O    1 
ATOM   21805 H  H    . GLY   D  4  167 ? 17.932  -53.772 -87.226  1.00 125.39 ? 167  GLY   D H    1 
ATOM   21806 H  HA2  . GLY   D  4  167 ? 17.168  -55.432 -88.329  1.00 123.64 ? 167  GLY   D HA2  1 
ATOM   21807 H  HA3  . GLY   D  4  167 ? 18.596  -55.630 -88.972  1.00 123.64 ? 167  GLY   D HA3  1 
ATOM   21808 N  N    . VAL   D  4  168 ? 18.569  -56.572 -85.995  1.00 93.12  ? 168  VAL   D N    1 
ATOM   21809 C  CA   . VAL   D  4  168 ? 18.752  -57.681 -85.066  1.00 85.39  ? 168  VAL   D CA   1 
ATOM   21810 C  C    . VAL   D  4  168 ? 17.580  -57.685 -84.096  1.00 83.74  ? 168  VAL   D C    1 
ATOM   21811 O  O    . VAL   D  4  168 ? 17.193  -56.632 -83.575  1.00 90.31  ? 168  VAL   D O    1 
ATOM   21812 C  CB   . VAL   D  4  168 ? 20.088  -57.570 -84.310  1.00 81.29  ? 168  VAL   D CB   1 
ATOM   21813 C  CG1  . VAL   D  4  168 ? 20.225  -58.688 -83.284  1.00 73.01  ? 168  VAL   D CG1  1 
ATOM   21814 C  CG2  . VAL   D  4  168 ? 21.251  -57.599 -85.286  1.00 85.15  ? 168  VAL   D CG2  1 
ATOM   21815 H  H    . VAL   D  4  168 ? 18.633  -55.802 -85.618  1.00 111.72 ? 168  VAL   D H    1 
ATOM   21816 H  HA   . VAL   D  4  168 ? 18.749  -58.517 -85.558  1.00 102.45 ? 168  VAL   D HA   1 
ATOM   21817 H  HB   . VAL   D  4  168 ? 20.107  -56.724 -83.836  1.00 97.53  ? 168  VAL   D HB   1 
ATOM   21818 H  HG11 . VAL   D  4  168 ? 21.110  -58.649 -82.890  1.00 87.59  ? 168  VAL   D HG11 1 
ATOM   21819 H  HG12 . VAL   D  4  168 ? 19.551  -58.569 -82.596  1.00 87.59  ? 168  VAL   D HG12 1 
ATOM   21820 H  HG13 . VAL   D  4  168 ? 20.097  -59.541 -83.727  1.00 87.59  ? 168  VAL   D HG13 1 
ATOM   21821 H  HG21 . VAL   D  4  168 ? 22.082  -57.556 -84.788  1.00 102.16 ? 168  VAL   D HG21 1 
ATOM   21822 H  HG22 . VAL   D  4  168 ? 21.214  -58.424 -85.796  1.00 102.16 ? 168  VAL   D HG22 1 
ATOM   21823 H  HG23 . VAL   D  4  168 ? 21.182  -56.838 -85.883  1.00 102.16 ? 168  VAL   D HG23 1 
ATOM   21824 N  N    . HIS   D  4  169 ? 17.016  -58.868 -83.856  1.00 76.89  ? 169  HIS   D N    1 
ATOM   21825 C  CA   . HIS   D  4  169 ? 15.924  -59.046 -82.901  1.00 75.10  ? 169  HIS   D CA   1 
ATOM   21826 C  C    . HIS   D  4  169 ? 16.289  -60.206 -81.979  1.00 77.08  ? 169  HIS   D C    1 
ATOM   21827 O  O    . HIS   D  4  169 ? 16.060  -61.371 -82.317  1.00 81.28  ? 169  HIS   D O    1 
ATOM   21828 C  CB   . HIS   D  4  169 ? 14.599  -59.303 -83.613  1.00 74.44  ? 169  HIS   D CB   1 
ATOM   21829 C  CG   . HIS   D  4  169 ? 14.055  -58.107 -84.328  1.00 80.61  ? 169  HIS   D CG   1 
ATOM   21830 N  ND1  . HIS   D  4  169 ? 13.690  -56.951 -83.672  1.00 83.76  ? 169  HIS   D ND1  1 
ATOM   21831 C  CD2  . HIS   D  4  169 ? 13.805  -57.889 -85.641  1.00 85.33  ? 169  HIS   D CD2  1 
ATOM   21832 C  CE1  . HIS   D  4  169 ? 13.243  -56.071 -84.551  1.00 88.29  ? 169  HIS   D CE1  1 
ATOM   21833 N  NE2  . HIS   D  4  169 ? 13.302  -56.616 -85.752  1.00 89.00  ? 169  HIS   D NE2  1 
ATOM   21834 H  H    . HIS   D  4  169 ? 17.255  -59.597 -84.243  1.00 92.25  ? 169  HIS   D H    1 
ATOM   21835 H  HA   . HIS   D  4  169 ? 15.834  -58.242 -82.367  1.00 90.10  ? 169  HIS   D HA   1 
ATOM   21836 H  HB2  . HIS   D  4  169 ? 14.729  -60.006 -84.269  1.00 89.30  ? 169  HIS   D HB2  1 
ATOM   21837 H  HB3  . HIS   D  4  169 ? 13.941  -59.580 -82.956  1.00 89.30  ? 169  HIS   D HB3  1 
ATOM   21838 H  HD1  . HIS   D  4  169 ? 13.744  -56.822 -82.824  1.00 100.50 ? 169  HIS   D HD1  1 
ATOM   21839 H  HD2  . HIS   D  4  169 ? 13.946  -58.490 -86.337  1.00 102.38 ? 169  HIS   D HD2  1 
ATOM   21840 H  HE1  . HIS   D  4  169 ? 12.939  -55.214 -84.356  1.00 105.92 ? 169  HIS   D HE1  1 
ATOM   21841 N  N    . THR   D  4  170 ? 16.861  -59.886 -80.821  1.00 74.61  ? 170  THR   D N    1 
ATOM   21842 C  CA   . THR   D  4  170 ? 17.160  -60.885 -79.804  1.00 72.25  ? 170  THR   D CA   1 
ATOM   21843 C  C    . THR   D  4  170 ? 15.987  -60.967 -78.838  1.00 72.86  ? 170  THR   D C    1 
ATOM   21844 O  O    . THR   D  4  170 ? 15.541  -59.946 -78.305  1.00 76.82  ? 170  THR   D O    1 
ATOM   21845 C  CB   . THR   D  4  170 ? 18.445  -60.539 -79.052  1.00 70.16  ? 170  THR   D CB   1 
ATOM   21846 O  OG1  . THR   D  4  170 ? 19.533  -60.449 -79.980  1.00 67.96  ? 170  THR   D OG1  1 
ATOM   21847 C  CG2  . THR   D  4  170 ? 18.760  -61.606 -78.007  1.00 68.17  ? 170  THR   D CG2  1 
ATOM   21848 H  H    . THR   D  4  170 ? 17.088  -59.087 -80.600  1.00 89.51  ? 170  THR   D H    1 
ATOM   21849 H  HA   . THR   D  4  170 ? 17.290  -61.750 -80.223  1.00 86.68  ? 170  THR   D HA   1 
ATOM   21850 H  HB   . THR   D  4  170 ? 18.335  -59.690 -78.597  1.00 84.17  ? 170  THR   D HB   1 
ATOM   21851 H  HG1  . THR   D  4  170 ? 20.242  -60.253 -79.574  1.00 81.53  ? 170  THR   D HG1  1 
ATOM   21852 H  HG21 . THR   D  4  170 ? 19.608  -61.411 -77.578  1.00 81.78  ? 170  THR   D HG21 1 
ATOM   21853 H  HG22 . THR   D  4  170 ? 18.063  -61.625 -77.332  1.00 81.78  ? 170  THR   D HG22 1 
ATOM   21854 H  HG23 . THR   D  4  170 ? 18.814  -62.478 -78.429  1.00 81.78  ? 170  THR   D HG23 1 
ATOM   21855 N  N    . PHE   D  4  171 ? 15.498  -62.171 -78.615  1.00 69.46  ? 171  PHE   D N    1 
ATOM   21856 C  CA   . PHE   D  4  171 ? 14.283  -62.345 -77.838  1.00 66.78  ? 171  PHE   D CA   1 
ATOM   21857 C  C    . PHE   D  4  171 ? 14.604  -62.744 -76.403  1.00 64.28  ? 171  PHE   D C    1 
ATOM   21858 O  O    . PHE   D  4  171 ? 15.610  -63.412 -76.146  1.00 60.42  ? 171  PHE   D O    1 
ATOM   21859 C  CB   . PHE   D  4  171 ? 13.393  -63.414 -78.479  1.00 66.90  ? 171  PHE   D CB   1 
ATOM   21860 C  CG   . PHE   D  4  171 ? 12.990  -63.092 -79.890  1.00 69.86  ? 171  PHE   D CG   1 
ATOM   21861 C  CD1  . PHE   D  4  171 ? 13.852  -63.343 -80.946  1.00 69.28  ? 171  PHE   D CD1  1 
ATOM   21862 C  CD2  . PHE   D  4  171 ? 11.753  -62.533 -80.160  1.00 71.58  ? 171  PHE   D CD2  1 
ATOM   21863 C  CE1  . PHE   D  4  171 ? 13.487  -63.044 -82.244  1.00 71.34  ? 171  PHE   D CE1  1 
ATOM   21864 C  CE2  . PHE   D  4  171 ? 11.380  -62.233 -81.456  1.00 73.09  ? 171  PHE   D CE2  1 
ATOM   21865 C  CZ   . PHE   D  4  171 ? 12.247  -62.489 -82.500  1.00 73.74  ? 171  PHE   D CZ   1 
ATOM   21866 H  H    . PHE   D  4  171 ? 15.848  -62.903 -78.901  1.00 83.33  ? 171  PHE   D H    1 
ATOM   21867 H  HA   . PHE   D  4  171 ? 13.789  -61.511 -77.812  1.00 80.12  ? 171  PHE   D HA   1 
ATOM   21868 H  HB2  . PHE   D  4  171 ? 13.876  -64.255 -78.493  1.00 80.26  ? 171  PHE   D HB2  1 
ATOM   21869 H  HB3  . PHE   D  4  171 ? 12.584  -63.504 -77.953  1.00 80.26  ? 171  PHE   D HB3  1 
ATOM   21870 H  HD1  . PHE   D  4  171 ? 14.687  -63.718 -80.778  1.00 83.11  ? 171  PHE   D HD1  1 
ATOM   21871 H  HD2  . PHE   D  4  171 ? 11.165  -62.358 -79.460  1.00 85.88  ? 171  PHE   D HD2  1 
ATOM   21872 H  HE1  . PHE   D  4  171 ? 14.073  -63.217 -82.945  1.00 85.58  ? 171  PHE   D HE1  1 
ATOM   21873 H  HE2  . PHE   D  4  171 ? 10.545  -61.858 -81.625  1.00 87.68  ? 171  PHE   D HE2  1 
ATOM   21874 H  HZ   . PHE   D  4  171 ? 11.998  -62.287 -83.373  1.00 88.46  ? 171  PHE   D HZ   1 
ATOM   21875 N  N    . PRO   D  4  172 ? 13.770  -62.343 -75.443  1.00 67.93  ? 172  PRO   D N    1 
ATOM   21876 C  CA   . PRO   D  4  172 ? 14.011  -62.743 -74.053  1.00 70.43  ? 172  PRO   D CA   1 
ATOM   21877 C  C    . PRO   D  4  172 ? 13.917  -64.252 -73.886  1.00 71.64  ? 172  PRO   D C    1 
ATOM   21878 O  O    . PRO   D  4  172 ? 13.241  -64.946 -74.650  1.00 72.16  ? 172  PRO   D O    1 
ATOM   21879 C  CB   . PRO   D  4  172 ? 12.907  -62.017 -73.273  1.00 73.53  ? 172  PRO   D CB   1 
ATOM   21880 C  CG   . PRO   D  4  172 ? 11.850  -61.717 -74.285  1.00 71.68  ? 172  PRO   D CG   1 
ATOM   21881 C  CD   . PRO   D  4  172 ? 12.577  -61.486 -75.573  1.00 68.57  ? 172  PRO   D CD   1 
ATOM   21882 H  HA   . PRO   D  4  172 ? 14.879  -62.435 -73.749  1.00 84.49  ? 172  PRO   D HA   1 
ATOM   21883 H  HB2  . PRO   D  4  172 ? 12.563  -62.595 -72.573  1.00 88.22  ? 172  PRO   D HB2  1 
ATOM   21884 H  HB3  . PRO   D  4  172 ? 13.259  -61.201 -72.886  1.00 88.22  ? 172  PRO   D HB3  1 
ATOM   21885 H  HG2  . PRO   D  4  172 ? 11.245  -62.472 -74.362  1.00 85.99  ? 172  PRO   D HG2  1 
ATOM   21886 H  HG3  . PRO   D  4  172 ? 11.358  -60.924 -74.020  1.00 85.99  ? 172  PRO   D HG3  1 
ATOM   21887 H  HD2  . PRO   D  4  172 ? 12.035  -61.760 -76.330  1.00 82.26  ? 172  PRO   D HD2  1 
ATOM   21888 H  HD3  . PRO   D  4  172 ? 12.829  -60.554 -75.665  1.00 82.26  ? 172  PRO   D HD3  1 
ATOM   21889 N  N    . ALA   D  4  173 ? 14.609  -64.756 -72.869  1.00 73.52  ? 173  ALA   D N    1 
ATOM   21890 C  CA   . ALA   D  4  173 ? 14.686  -66.191 -72.648  1.00 74.88  ? 173  ALA   D CA   1 
ATOM   21891 C  C    . ALA   D  4  173 ? 13.378  -66.724 -72.068  1.00 78.95  ? 173  ALA   D C    1 
ATOM   21892 O  O    . ALA   D  4  173 ? 12.585  -65.995 -71.467  1.00 83.75  ? 173  ALA   D O    1 
ATOM   21893 C  CB   . ALA   D  4  173 ? 15.847  -66.523 -71.710  1.00 73.28  ? 173  ALA   D CB   1 
ATOM   21894 H  H    . ALA   D  4  173 ? 15.043  -64.287 -72.293  1.00 88.21  ? 173  ALA   D H    1 
ATOM   21895 H  HA   . ALA   D  4  173 ? 14.840  -66.636 -73.495  1.00 89.84  ? 173  ALA   D HA   1 
ATOM   21896 H  HB1  . ALA   D  4  173 ? 15.871  -67.482 -71.566  1.00 87.92  ? 173  ALA   D HB1  1 
ATOM   21897 H  HB2  . ALA   D  4  173 ? 16.676  -66.228 -72.118  1.00 87.92  ? 173  ALA   D HB2  1 
ATOM   21898 H  HB3  . ALA   D  4  173 ? 15.712  -66.065 -70.866  1.00 87.92  ? 173  ALA   D HB3  1 
ATOM   21899 N  N    . VAL   D  4  174 ? 13.163  -68.025 -72.259  1.00 79.39  ? 174  VAL   D N    1 
ATOM   21900 C  CA   . VAL   D  4  174 ? 11.991  -68.719 -71.742  1.00 81.68  ? 174  VAL   D CA   1 
ATOM   21901 C  C    . VAL   D  4  174 ? 12.459  -69.949 -70.979  1.00 80.13  ? 174  VAL   D C    1 
ATOM   21902 O  O    . VAL   D  4  174 ? 13.535  -70.494 -71.243  1.00 77.32  ? 174  VAL   D O    1 
ATOM   21903 C  CB   . VAL   D  4  174 ? 11.013  -69.127 -72.867  1.00 82.29  ? 174  VAL   D CB   1 
ATOM   21904 C  CG1  . VAL   D  4  174 ? 9.666   -69.538 -72.284  1.00 88.99  ? 174  VAL   D CG1  1 
ATOM   21905 C  CG2  . VAL   D  4  174 ? 10.843  -67.998 -73.871  1.00 77.36  ? 174  VAL   D CG2  1 
ATOM   21906 H  H    . VAL   D  4  174 ? 13.697  -68.538 -72.696  1.00 95.25  ? 174  VAL   D H    1 
ATOM   21907 H  HA   . VAL   D  4  174 ? 11.520  -68.132 -71.130  1.00 98.00  ? 174  VAL   D HA   1 
ATOM   21908 H  HB   . VAL   D  4  174 ? 11.382  -69.890 -73.338  1.00 98.73  ? 174  VAL   D HB   1 
ATOM   21909 H  HG11 . VAL   D  4  174 ? 9.054   -69.734 -73.011  1.00 106.77 ? 174  VAL   D HG11 1 
ATOM   21910 H  HG12 . VAL   D  4  174 ? 9.789   -70.327 -71.733  1.00 106.77 ? 174  VAL   D HG12 1 
ATOM   21911 H  HG13 . VAL   D  4  174 ? 9.319   -68.810 -71.746  1.00 106.77 ? 174  VAL   D HG13 1 
ATOM   21912 H  HG21 . VAL   D  4  174 ? 10.181  -68.258 -74.530  1.00 92.81  ? 174  VAL   D HG21 1 
ATOM   21913 H  HG22 . VAL   D  4  174 ? 10.549  -67.201 -73.403  1.00 92.81  ? 174  VAL   D HG22 1 
ATOM   21914 H  HG23 . VAL   D  4  174 ? 11.694  -67.831 -74.305  1.00 92.81  ? 174  VAL   D HG23 1 
ATOM   21915 N  N    . LEU   D  4  175 ? 11.640  -70.388 -70.026  1.00 83.38  ? 175  LEU   D N    1 
ATOM   21916 C  CA   . LEU   D  4  175 ? 11.916  -71.620 -69.302  1.00 86.06  ? 175  LEU   D CA   1 
ATOM   21917 C  C    . LEU   D  4  175 ? 11.480  -72.821 -70.130  1.00 88.13  ? 175  LEU   D C    1 
ATOM   21918 O  O    . LEU   D  4  175 ? 10.415  -72.814 -70.754  1.00 90.17  ? 175  LEU   D O    1 
ATOM   21919 C  CB   . LEU   D  4  175 ? 11.200  -71.627 -67.951  1.00 91.29  ? 175  LEU   D CB   1 
ATOM   21920 C  CG   . LEU   D  4  175 ? 11.820  -70.773 -66.843  1.00 94.33  ? 175  LEU   D CG   1 
ATOM   21921 C  CD1  . LEU   D  4  175 ? 10.961  -70.841 -65.590  1.00 103.62 ? 175  LEU   D CD1  1 
ATOM   21922 C  CD2  . LEU   D  4  175 ? 13.245  -71.215 -66.536  1.00 91.94  ? 175  LEU   D CD2  1 
ATOM   21923 H  H    . LEU   D  4  175 ? 10.919  -69.988 -69.782  1.00 100.04 ? 175  LEU   D H    1 
ATOM   21924 H  HA   . LEU   D  4  175 ? 12.868  -71.689 -69.132  1.00 103.25 ? 175  LEU   D HA   1 
ATOM   21925 H  HB2  . LEU   D  4  175 ? 10.297  -71.302 -68.089  1.00 109.53 ? 175  LEU   D HB2  1 
ATOM   21926 H  HB3  . LEU   D  4  175 ? 11.179  -72.541 -67.628  1.00 109.53 ? 175  LEU   D HB3  1 
ATOM   21927 H  HG   . LEU   D  4  175 ? 11.860  -69.851 -67.143  1.00 113.17 ? 175  LEU   D HG   1 
ATOM   21928 H  HD11 . LEU   D  4  175 ? 11.380  -70.315 -64.891  1.00 124.32 ? 175  LEU   D HD11 1 
ATOM   21929 H  HD12 . LEU   D  4  175 ? 10.082  -70.484 -65.791  1.00 124.32 ? 175  LEU   D HD12 1 
ATOM   21930 H  HD13 . LEU   D  4  175 ? 10.886  -71.766 -65.309  1.00 124.32 ? 175  LEU   D HD13 1 
ATOM   21931 H  HD21 . LEU   D  4  175 ? 13.566  -70.729 -65.760  1.00 110.31 ? 175  LEU   D HD21 1 
ATOM   21932 H  HD22 . LEU   D  4  175 ? 13.248  -72.168 -66.354  1.00 110.31 ? 175  LEU   D HD22 1 
ATOM   21933 H  HD23 . LEU   D  4  175 ? 13.807  -71.023 -67.303  1.00 110.31 ? 175  LEU   D HD23 1 
ATOM   21934 N  N    . GLN   D  4  176 ? 12.314  -73.861 -70.126  1.00 91.59  ? 176  GLN   D N    1 
ATOM   21935 C  CA   . GLN   D  4  176 ? 12.104  -75.026 -70.982  1.00 100.18 ? 176  GLN   D CA   1 
ATOM   21936 C  C    . GLN   D  4  176 ? 12.705  -76.229 -70.262  1.00 110.39 ? 176  GLN   D C    1 
ATOM   21937 O  O    . GLN   D  4  176 ? 13.926  -76.411 -70.268  1.00 109.49 ? 176  GLN   D O    1 
ATOM   21938 C  CB   . GLN   D  4  176 ? 12.739  -74.808 -72.348  1.00 99.11  ? 176  GLN   D CB   1 
ATOM   21939 C  CG   . GLN   D  4  176 ? 12.546  -75.941 -73.336  1.00 105.87 ? 176  GLN   D CG   1 
ATOM   21940 C  CD   . GLN   D  4  176 ? 13.307  -75.704 -74.624  1.00 107.25 ? 176  GLN   D CD   1 
ATOM   21941 O  OE1  . GLN   D  4  176 ? 14.535  -75.628 -74.625  1.00 106.02 ? 176  GLN   D OE1  1 
ATOM   21942 N  NE2  . GLN   D  4  176 ? 12.581  -75.572 -75.727  1.00 110.34 ? 176  GLN   D NE2  1 
ATOM   21943 H  H    . GLN   D  4  176 ? 13.015  -73.915 -69.631  1.00 109.89 ? 176  GLN   D H    1 
ATOM   21944 H  HA   . GLN   D  4  176 ? 11.154  -75.184 -71.104  1.00 120.20 ? 176  GLN   D HA   1 
ATOM   21945 H  HB2  . GLN   D  4  176 ? 12.353  -74.010 -72.742  1.00 118.92 ? 176  GLN   D HB2  1 
ATOM   21946 H  HB3  . GLN   D  4  176 ? 13.694  -74.688 -72.226  1.00 118.92 ? 176  GLN   D HB3  1 
ATOM   21947 H  HG2  . GLN   D  4  176 ? 12.867  -76.767 -72.941  1.00 127.03 ? 176  GLN   D HG2  1 
ATOM   21948 H  HG3  . GLN   D  4  176 ? 11.603  -76.020 -73.551  1.00 127.03 ? 176  GLN   D HG3  1 
ATOM   21949 H  HE21 . GLN   D  4  176 ? 11.723  -75.622 -75.686  1.00 132.39 ? 176  GLN   D HE21 1 
ATOM   21950 H  HE22 . GLN   D  4  176 ? 12.968  -75.436 -76.483  1.00 132.39 ? 176  GLN   D HE22 1 
ATOM   21951 N  N    . SER   D  4  177 ? 11.845  -77.041 -69.647  1.00 121.66 ? 177  SER   D N    1 
ATOM   21952 C  CA   . SER   D  4  177 ? 12.290  -78.176 -68.840  1.00 127.69 ? 177  SER   D CA   1 
ATOM   21953 C  C    . SER   D  4  177 ? 13.244  -77.718 -67.739  1.00 119.38 ? 177  SER   D C    1 
ATOM   21954 O  O    . SER   D  4  177 ? 14.241  -78.377 -67.441  1.00 120.57 ? 177  SER   D O    1 
ATOM   21955 C  CB   . SER   D  4  177 ? 12.945  -79.249 -69.711  1.00 133.88 ? 177  SER   D CB   1 
ATOM   21956 O  OG   . SER   D  4  177 ? 12.040  -79.737 -70.684  1.00 138.41 ? 177  SER   D OG   1 
ATOM   21957 H  H    . SER   D  4  177 ? 10.990  -76.954 -69.682  1.00 145.98 ? 177  SER   D H    1 
ATOM   21958 H  HA   . SER   D  4  177 ? 11.515  -78.574 -68.414  1.00 153.20 ? 177  SER   D HA   1 
ATOM   21959 H  HB2  . SER   D  4  177 ? 13.714  -78.863 -70.160  1.00 160.64 ? 177  SER   D HB2  1 
ATOM   21960 H  HB3  . SER   D  4  177 ? 13.227  -79.985 -69.145  1.00 160.64 ? 177  SER   D HB3  1 
ATOM   21961 H  HG   . SER   D  4  177 ? 12.423  -80.300 -71.176  1.00 166.07 ? 177  SER   D HG   1 
ATOM   21962 N  N    . SER   D  4  178 ? 12.934  -76.565 -67.143  1.00 108.55 ? 178  SER   D N    1 
ATOM   21963 C  CA   . SER   D  4  178 ? 13.714  -75.966 -66.062  1.00 99.05  ? 178  SER   D CA   1 
ATOM   21964 C  C    . SER   D  4  178 ? 15.062  -75.428 -66.536  1.00 89.07  ? 178  SER   D C    1 
ATOM   21965 O  O    . SER   D  4  178 ? 15.998  -75.315 -65.742  1.00 85.35  ? 178  SER   D O    1 
ATOM   21966 C  CB   . SER   D  4  178 ? 13.926  -76.955 -64.910  1.00 103.39 ? 178  SER   D CB   1 
ATOM   21967 O  OG   . SER   D  4  178 ? 12.686  -77.397 -64.383  1.00 108.58 ? 178  SER   D OG   1 
ATOM   21968 H  H    . SER   D  4  178 ? 12.248  -76.093 -67.357  1.00 130.25 ? 178  SER   D H    1 
ATOM   21969 H  HA   . SER   D  4  178 ? 13.208  -75.210 -65.726  1.00 118.84 ? 178  SER   D HA   1 
ATOM   21970 H  HB2  . SER   D  4  178 ? 14.419  -77.722 -65.240  1.00 124.04 ? 178  SER   D HB2  1 
ATOM   21971 H  HB3  . SER   D  4  178 ? 14.428  -76.515 -64.206  1.00 124.04 ? 178  SER   D HB3  1 
ATOM   21972 H  HG   . SER   D  4  178 ? 12.818  -77.940 -63.755  1.00 130.27 ? 178  SER   D HG   1 
ATOM   21973 N  N    . LEU   D  4  179 ? 15.177  -75.084 -67.818  1.00 85.91  ? 179  LEU   D N    1 
ATOM   21974 C  CA   . LEU   D  4  179 ? 16.382  -74.461 -68.348  1.00 81.68  ? 179  LEU   D CA   1 
ATOM   21975 C  C    . LEU   D  4  179 ? 15.989  -73.347 -69.306  1.00 82.33  ? 179  LEU   D C    1 
ATOM   21976 O  O    . LEU   D  4  179 ? 14.919  -73.382 -69.920  1.00 83.92  ? 179  LEU   D O    1 
ATOM   21977 C  CB   . LEU   D  4  179 ? 17.283  -75.474 -69.066  1.00 79.21  ? 179  LEU   D CB   1 
ATOM   21978 C  CG   . LEU   D  4  179 ? 18.002  -76.494 -68.181  1.00 80.20  ? 179  LEU   D CG   1 
ATOM   21979 C  CD1  . LEU   D  4  179 ? 18.810  -77.449 -69.040  1.00 78.26  ? 179  LEU   D CD1  1 
ATOM   21980 C  CD2  . LEU   D  4  179 ? 18.901  -75.804 -67.164  1.00 80.63  ? 179  LEU   D CD2  1 
ATOM   21981 H  H    . LEU   D  4  179 ? 14.562  -75.204 -68.406  1.00 103.07 ? 179  LEU   D H    1 
ATOM   21982 H  HA   . LEU   D  4  179 ? 16.890  -74.073 -67.618  1.00 97.99  ? 179  LEU   D HA   1 
ATOM   21983 H  HB2  . LEU   D  4  179 ? 16.735  -75.974 -69.690  1.00 95.04  ? 179  LEU   D HB2  1 
ATOM   21984 H  HB3  . LEU   D  4  179 ? 17.967  -74.980 -69.545  1.00 95.04  ? 179  LEU   D HB3  1 
ATOM   21985 H  HG   . LEU   D  4  179 ? 17.339  -77.002 -67.687  1.00 96.22  ? 179  LEU   D HG   1 
ATOM   21986 H  HD11 . LEU   D  4  179 ? 19.276  -78.075 -68.464  1.00 93.90  ? 179  LEU   D HD11 1 
ATOM   21987 H  HD12 . LEU   D  4  179 ? 18.209  -77.928 -69.632  1.00 93.90  ? 179  LEU   D HD12 1 
ATOM   21988 H  HD13 . LEU   D  4  179 ? 19.451  -76.940 -69.561  1.00 93.90  ? 179  LEU   D HD13 1 
ATOM   21989 H  HD21 . LEU   D  4  179 ? 19.403  -76.477 -66.678  1.00 96.74  ? 179  LEU   D HD21 1 
ATOM   21990 H  HD22 . LEU   D  4  179 ? 19.509  -75.210 -67.631  1.00 96.74  ? 179  LEU   D HD22 1 
ATOM   21991 H  HD23 . LEU   D  4  179 ? 18.350  -75.295 -66.548  1.00 96.74  ? 179  LEU   D HD23 1 
ATOM   21992 N  N    . TYR   D  4  180 ? 16.870  -72.358 -69.429  1.00 81.63  ? 180  TYR   D N    1 
ATOM   21993 C  CA   . TYR   D  4  180 ? 16.589  -71.194 -70.255  1.00 78.48  ? 180  TYR   D CA   1 
ATOM   21994 C  C    . TYR   D  4  180 ? 16.920  -71.472 -71.713  1.00 78.62  ? 180  TYR   D C    1 
ATOM   21995 O  O    . TYR   D  4  180 ? 17.913  -72.136 -72.027  1.00 81.49  ? 180  TYR   D O    1 
ATOM   21996 C  CB   . TYR   D  4  180 ? 17.388  -69.984 -69.772  1.00 73.75  ? 180  TYR   D CB   1 
ATOM   21997 C  CG   . TYR   D  4  180 ? 16.917  -69.428 -68.451  1.00 76.64  ? 180  TYR   D CG   1 
ATOM   21998 C  CD1  . TYR   D  4  180 ? 15.676  -68.816 -68.339  1.00 77.62  ? 180  TYR   D CD1  1 
ATOM   21999 C  CD2  . TYR   D  4  180 ? 17.714  -69.507 -67.318  1.00 78.57  ? 180  TYR   D CD2  1 
ATOM   22000 C  CE1  . TYR   D  4  180 ? 15.238  -68.305 -67.132  1.00 79.72  ? 180  TYR   D CE1  1 
ATOM   22001 C  CE2  . TYR   D  4  180 ? 17.287  -68.996 -66.108  1.00 82.06  ? 180  TYR   D CE2  1 
ATOM   22002 C  CZ   . TYR   D  4  180 ? 16.048  -68.395 -66.021  1.00 83.22  ? 180  TYR   D CZ   1 
ATOM   22003 O  OH   . TYR   D  4  180 ? 15.618  -67.886 -64.816  1.00 90.01  ? 180  TYR   D OH   1 
ATOM   22004 H  H    . TYR   D  4  180 ? 17.638  -72.339 -69.042  1.00 97.94  ? 180  TYR   D H    1 
ATOM   22005 H  HA   . TYR   D  4  180 ? 15.644  -70.985 -70.190  1.00 94.15  ? 180  TYR   D HA   1 
ATOM   22006 H  HB2  . TYR   D  4  180 ? 18.316  -70.245 -69.668  1.00 88.48  ? 180  TYR   D HB2  1 
ATOM   22007 H  HB3  . TYR   D  4  180 ? 17.314  -69.278 -70.433  1.00 88.48  ? 180  TYR   D HB3  1 
ATOM   22008 H  HD1  . TYR   D  4  180 ? 15.130  -68.750 -69.088  1.00 93.12  ? 180  TYR   D HD1  1 
ATOM   22009 H  HD2  . TYR   D  4  180 ? 18.551  -69.910 -67.375  1.00 94.26  ? 180  TYR   D HD2  1 
ATOM   22010 H  HE1  . TYR   D  4  180 ? 14.402  -67.902 -67.071  1.00 95.65  ? 180  TYR   D HE1  1 
ATOM   22011 H  HE2  . TYR   D  4  180 ? 17.832  -69.056 -65.356  1.00 98.45  ? 180  TYR   D HE2  1 
ATOM   22012 H  HH   . TYR   D  4  180 ? 14.797  -67.714 -64.854  1.00 108.00 ? 180  TYR   D HH   1 
ATOM   22013 N  N    . THR   D  4  181 ? 16.079  -70.954 -72.604  1.00 73.33  ? 181  THR   D N    1 
ATOM   22014 C  CA   . THR   D  4  181 ? 16.301  -71.028 -74.039  1.00 69.74  ? 181  THR   D CA   1 
ATOM   22015 C  C    . THR   D  4  181 ? 16.065  -69.651 -74.641  1.00 67.64  ? 181  THR   D C    1 
ATOM   22016 O  O    . THR   D  4  181 ? 15.116  -68.955 -74.270  1.00 67.83  ? 181  THR   D O    1 
ATOM   22017 C  CB   . THR   D  4  181 ? 15.382  -72.062 -74.699  1.00 69.59  ? 181  THR   D CB   1 
ATOM   22018 O  OG1  . THR   D  4  181 ? 15.623  -73.352 -74.122  1.00 75.70  ? 181  THR   D OG1  1 
ATOM   22019 C  CG2  . THR   D  4  181 ? 15.632  -72.127 -76.202  1.00 65.90  ? 181  THR   D CG2  1 
ATOM   22020 H  H    . THR   D  4  181 ? 15.354  -70.544 -72.392  1.00 87.98  ? 181  THR   D H    1 
ATOM   22021 H  HA   . THR   D  4  181 ? 17.216  -71.293 -74.221  1.00 83.67  ? 181  THR   D HA   1 
ATOM   22022 H  HB   . THR   D  4  181 ? 14.456  -71.809 -74.557  1.00 83.48  ? 181  THR   D HB   1 
ATOM   22023 H  HG1  . THR   D  4  181 ? 15.170  -73.935 -74.523  1.00 90.82  ? 181  THR   D HG1  1 
ATOM   22024 H  HG21 . THR   D  4  181 ? 15.087  -72.824 -76.600  1.00 79.06  ? 181  THR   D HG21 1 
ATOM   22025 H  HG22 . THR   D  4  181 ? 15.406  -71.278 -76.613  1.00 79.06  ? 181  THR   D HG22 1 
ATOM   22026 H  HG23 . THR   D  4  181 ? 16.567  -72.321 -76.375  1.00 79.06  ? 181  THR   D HG23 1 
ATOM   22027 N  N    . LEU   D  4  182 ? 16.935  -69.268 -75.571  1.00 65.94  ? 182  LEU   D N    1 
ATOM   22028 C  CA   . LEU   D  4  182 ? 16.920  -67.940 -76.161  1.00 66.99  ? 182  LEU   D CA   1 
ATOM   22029 C  C    . LEU   D  4  182 ? 17.229  -68.055 -77.645  1.00 70.74  ? 182  LEU   D C    1 
ATOM   22030 O  O    . LEU   D  4  182 ? 17.934  -68.970 -78.078  1.00 79.18  ? 182  LEU   D O    1 
ATOM   22031 C  CB   . LEU   D  4  182 ? 17.933  -67.019 -75.461  1.00 68.04  ? 182  LEU   D CB   1 
ATOM   22032 C  CG   . LEU   D  4  182 ? 18.310  -65.700 -76.135  1.00 69.42  ? 182  LEU   D CG   1 
ATOM   22033 C  CD1  . LEU   D  4  182 ? 18.597  -64.645 -75.078  1.00 69.86  ? 182  LEU   D CD1  1 
ATOM   22034 C  CD2  . LEU   D  4  182 ? 19.520  -65.874 -77.040  1.00 70.42  ? 182  LEU   D CD2  1 
ATOM   22035 H  H    . LEU   D  4  182 ? 17.556  -69.774 -75.882  1.00 79.11  ? 182  LEU   D H    1 
ATOM   22036 H  HA   . LEU   D  4  182 ? 16.041  -67.538 -76.076  1.00 80.37  ? 182  LEU   D HA   1 
ATOM   22037 H  HB2  . LEU   D  4  182 ? 17.568  -66.791 -74.592  1.00 81.63  ? 182  LEU   D HB2  1 
ATOM   22038 H  HB3  . LEU   D  4  182 ? 18.757  -67.520 -75.354  1.00 81.63  ? 182  LEU   D HB3  1 
ATOM   22039 H  HG   . LEU   D  4  182 ? 17.567  -65.404 -76.685  1.00 83.29  ? 182  LEU   D HG   1 
ATOM   22040 H  HD11 . LEU   D  4  182 ? 18.868  -63.824 -75.518  1.00 83.82  ? 182  LEU   D HD11 1 
ATOM   22041 H  HD12 . LEU   D  4  182 ? 17.793  -64.492 -74.558  1.00 83.82  ? 182  LEU   D HD12 1 
ATOM   22042 H  HD13 . LEU   D  4  182 ? 19.310  -64.962 -74.501  1.00 83.82  ? 182  LEU   D HD13 1 
ATOM   22043 H  HD21 . LEU   D  4  182 ? 19.777  -65.008 -77.393  1.00 84.48  ? 182  LEU   D HD21 1 
ATOM   22044 H  HD22 . LEU   D  4  182 ? 20.249  -66.249 -76.523  1.00 84.48  ? 182  LEU   D HD22 1 
ATOM   22045 H  HD23 . LEU   D  4  182 ? 19.287  -66.472 -77.767  1.00 84.48  ? 182  LEU   D HD23 1 
ATOM   22046 N  N    . SER   D  4  183 ? 16.690  -67.118 -78.421  1.00 66.12  ? 183  SER   D N    1 
ATOM   22047 C  CA   . SER   D  4  183 ? 16.913  -67.086 -79.857  1.00 66.54  ? 183  SER   D CA   1 
ATOM   22048 C  C    . SER   D  4  183 ? 17.134  -65.648 -80.299  1.00 65.39  ? 183  SER   D C    1 
ATOM   22049 O  O    . SER   D  4  183 ? 16.775  -64.697 -79.600  1.00 63.41  ? 183  SER   D O    1 
ATOM   22050 C  CB   . SER   D  4  183 ? 15.737  -67.705 -80.626  1.00 68.76  ? 183  SER   D CB   1 
ATOM   22051 O  OG   . SER   D  4  183 ? 14.526  -67.026 -80.342  1.00 71.17  ? 183  SER   D OG   1 
ATOM   22052 H  H    . SER   D  4  183 ? 16.187  -66.483 -78.132  1.00 79.33  ? 183  SER   D H    1 
ATOM   22053 H  HA   . SER   D  4  183 ? 17.713  -67.593 -80.070  1.00 79.83  ? 183  SER   D HA   1 
ATOM   22054 H  HB2  . SER   D  4  183 ? 15.916  -67.644 -81.577  1.00 82.49  ? 183  SER   D HB2  1 
ATOM   22055 H  HB3  . SER   D  4  183 ? 15.645  -68.634 -80.364  1.00 82.49  ? 183  SER   D HB3  1 
ATOM   22056 H  HG   . SER   D  4  183 ? 14.567  -66.235 -80.622  1.00 85.39  ? 183  SER   D HG   1 
ATOM   22057 N  N    . SER   D  4  184 ? 17.737  -65.501 -81.477  1.00 66.13  ? 184  SER   D N    1 
ATOM   22058 C  CA   . SER   D  4  184 ? 18.021  -64.190 -82.039  1.00 69.82  ? 184  SER   D CA   1 
ATOM   22059 C  C    . SER   D  4  184 ? 18.026  -64.295 -83.555  1.00 71.08  ? 184  SER   D C    1 
ATOM   22060 O  O    . SER   D  4  184 ? 18.542  -65.267 -84.114  1.00 71.65  ? 184  SER   D O    1 
ATOM   22061 C  CB   . SER   D  4  184 ? 19.367  -63.648 -81.543  1.00 73.01  ? 184  SER   D CB   1 
ATOM   22062 O  OG   . SER   D  4  184 ? 19.648  -62.379 -82.107  1.00 76.80  ? 184  SER   D OG   1 
ATOM   22063 H  H    . SER   D  4  184 ? 17.993  -66.155 -81.973  1.00 79.33  ? 184  SER   D H    1 
ATOM   22064 H  HA   . SER   D  4  184 ? 17.327  -63.566 -81.777  1.00 83.76  ? 184  SER   D HA   1 
ATOM   22065 H  HB2  . SER   D  4  184 ? 19.335  -63.562 -80.577  1.00 87.59  ? 184  SER   D HB2  1 
ATOM   22066 H  HB3  . SER   D  4  184 ? 20.069  -64.267 -81.797  1.00 87.59  ? 184  SER   D HB3  1 
ATOM   22067 H  HG   . SER   D  4  184 ? 19.492  -61.774 -81.545  1.00 92.14  ? 184  SER   D HG   1 
ATOM   22068 N  N    . SER   D  4  185 ? 17.449  -63.293 -84.212  1.00 72.23  ? 185  SER   D N    1 
ATOM   22069 C  CA   . SER   D  4  185 ? 17.417  -63.217 -85.664  1.00 74.67  ? 185  SER   D CA   1 
ATOM   22070 C  C    . SER   D  4  185 ? 18.181  -61.983 -86.120  1.00 76.75  ? 185  SER   D C    1 
ATOM   22071 O  O    . SER   D  4  185 ? 18.122  -60.930 -85.477  1.00 77.82  ? 185  SER   D O    1 
ATOM   22072 C  CB   . SER   D  4  185 ? 15.980  -63.154 -86.188  1.00 76.51  ? 185  SER   D CB   1 
ATOM   22073 O  OG   . SER   D  4  185 ? 15.440  -61.856 -86.015  1.00 78.76  ? 185  SER   D OG   1 
ATOM   22074 H  H    . SER   D  4  185 ? 17.061  -62.630 -83.825  1.00 86.66  ? 185  SER   D H    1 
ATOM   22075 H  HA   . SER   D  4  185 ? 17.841  -64.004 -86.039  1.00 89.58  ? 185  SER   D HA   1 
ATOM   22076 H  HB2  . SER   D  4  185 ? 15.978  -63.375 -87.132  1.00 91.79  ? 185  SER   D HB2  1 
ATOM   22077 H  HB3  . SER   D  4  185 ? 15.436  -63.791 -85.697  1.00 91.79  ? 185  SER   D HB3  1 
ATOM   22078 H  HG   . SER   D  4  185 ? 14.611  -61.869 -86.152  1.00 94.50  ? 185  SER   D HG   1 
ATOM   22079 N  N    . VAL   D  4  186 ? 18.902  -62.123 -87.228  1.00 77.32  ? 186  VAL   D N    1 
ATOM   22080 C  CA   . VAL   D  4  186 ? 19.609  -61.017 -87.861  1.00 79.56  ? 186  VAL   D CA   1 
ATOM   22081 C  C    . VAL   D  4  186 ? 19.193  -60.971 -89.323  1.00 82.87  ? 186  VAL   D C    1 
ATOM   22082 O  O    . VAL   D  4  186 ? 19.079  -62.013 -89.978  1.00 85.54  ? 186  VAL   D O    1 
ATOM   22083 C  CB   . VAL   D  4  186 ? 21.141  -61.162 -87.727  1.00 78.92  ? 186  VAL   D CB   1 
ATOM   22084 C  CG1  . VAL   D  4  186 ? 21.622  -62.446 -88.389  1.00 79.74  ? 186  VAL   D CG1  1 
ATOM   22085 C  CG2  . VAL   D  4  186 ? 21.846  -59.950 -88.320  1.00 81.87  ? 186  VAL   D CG2  1 
ATOM   22086 H  H    . VAL   D  4  186 ? 18.998  -62.870 -87.643  1.00 92.76  ? 186  VAL   D H    1 
ATOM   22087 H  HA   . VAL   D  4  186 ? 19.354  -60.182 -87.438  1.00 95.46  ? 186  VAL   D HA   1 
ATOM   22088 H  HB   . VAL   D  4  186 ? 21.368  -61.211 -86.785  1.00 94.69  ? 186  VAL   D HB   1 
ATOM   22089 H  HG11 . VAL   D  4  186 ? 22.578  -62.534 -88.251  1.00 95.67  ? 186  VAL   D HG11 1 
ATOM   22090 H  HG12 . VAL   D  4  186 ? 21.159  -63.200 -87.989  1.00 95.67  ? 186  VAL   D HG12 1 
ATOM   22091 H  HG13 . VAL   D  4  186 ? 21.427  -62.404 -89.338  1.00 95.67  ? 186  VAL   D HG13 1 
ATOM   22092 H  HG21 . VAL   D  4  186 ? 22.800  -60.033 -88.165  1.00 98.23  ? 186  VAL   D HG21 1 
ATOM   22093 H  HG22 . VAL   D  4  186 ? 21.667  -59.915 -89.272  1.00 98.23  ? 186  VAL   D HG22 1 
ATOM   22094 H  HG23 . VAL   D  4  186 ? 21.510  -59.148 -87.891  1.00 98.23  ? 186  VAL   D HG23 1 
ATOM   22095 N  N    . THR   D  4  187 ? 18.960  -59.764 -89.832  1.00 84.61  ? 187  THR   D N    1 
ATOM   22096 C  CA   . THR   D  4  187 ? 18.512  -59.560 -91.204  1.00 91.31  ? 187  THR   D CA   1 
ATOM   22097 C  C    . THR   D  4  187 ? 19.480  -58.617 -91.900  1.00 95.97  ? 187  THR   D C    1 
ATOM   22098 O  O    . THR   D  4  187 ? 19.682  -57.484 -91.449  1.00 96.37  ? 187  THR   D O    1 
ATOM   22099 C  CB   . THR   D  4  187 ? 17.090  -58.997 -91.243  1.00 91.97  ? 187  THR   D CB   1 
ATOM   22100 O  OG1  . THR   D  4  187 ? 16.199  -59.899 -90.575  1.00 89.70  ? 187  THR   D OG1  1 
ATOM   22101 C  CG2  . THR   D  4  187 ? 16.627  -58.807 -92.681  1.00 96.46  ? 187  THR   D CG2  1 
ATOM   22102 H  H    . THR   D  4  187 ? 19.058  -59.033 -89.391  1.00 101.51 ? 187  THR   D H    1 
ATOM   22103 H  HA   . THR   D  4  187 ? 18.517  -60.408 -91.674  1.00 109.56 ? 187  THR   D HA   1 
ATOM   22104 H  HB   . THR   D  4  187 ? 17.072  -58.134 -90.800  1.00 110.34 ? 187  THR   D HB   1 
ATOM   22105 H  HG1  . THR   D  4  187 ? 15.414  -59.602 -90.605  1.00 107.62 ? 187  THR   D HG1  1 
ATOM   22106 H  HG21 . THR   D  4  187 ? 15.699  -58.527 -92.697  1.00 115.73 ? 187  THR   D HG21 1 
ATOM   22107 H  HG22 . THR   D  4  187 ? 17.168  -58.130 -93.117  1.00 115.73 ? 187  THR   D HG22 1 
ATOM   22108 H  HG23 . THR   D  4  187 ? 16.713  -59.641 -93.169  1.00 115.73 ? 187  THR   D HG23 1 
ATOM   22109 N  N    . VAL   D  4  188 ? 20.073  -59.085 -92.998  1.00 98.33  ? 188  VAL   D N    1 
ATOM   22110 C  CA   . VAL   D  4  188 ? 21.019  -58.307 -93.781  1.00 99.80  ? 188  VAL   D CA   1 
ATOM   22111 C  C    . VAL   D  4  188 ? 20.576  -58.328 -95.238  1.00 102.44 ? 188  VAL   D C    1 
ATOM   22112 O  O    . VAL   D  4  188 ? 19.625  -59.013 -95.616  1.00 101.30 ? 188  VAL   D O    1 
ATOM   22113 C  CB   . VAL   D  4  188 ? 22.462  -58.837 -93.649  1.00 97.65  ? 188  VAL   D CB   1 
ATOM   22114 C  CG1  . VAL   D  4  188 ? 22.951  -58.690 -92.218  1.00 92.22  ? 188  VAL   D CG1  1 
ATOM   22115 C  CG2  . VAL   D  4  188 ? 22.542  -60.292 -94.101  1.00 96.75  ? 188  VAL   D CG2  1 
ATOM   22116 H  H    . VAL   D  4  188 ? 19.936  -59.873 -93.314  1.00 117.98 ? 188  VAL   D H    1 
ATOM   22117 H  HA   . VAL   D  4  188 ? 21.005  -57.388 -93.473  1.00 119.74 ? 188  VAL   D HA   1 
ATOM   22118 H  HB   . VAL   D  4  188 ? 23.044  -58.314 -94.223  1.00 117.16 ? 188  VAL   D HB   1 
ATOM   22119 H  HG11 . VAL   D  4  188 ? 23.865  -59.012 -92.162  1.00 110.65 ? 188  VAL   D HG11 1 
ATOM   22120 H  HG12 . VAL   D  4  188 ? 22.914  -57.754 -91.966  1.00 110.65 ? 188  VAL   D HG12 1 
ATOM   22121 H  HG13 . VAL   D  4  188 ? 22.380  -59.213 -91.634  1.00 110.65 ? 188  VAL   D HG13 1 
ATOM   22122 H  HG21 . VAL   D  4  188 ? 23.464  -60.590 -94.045  1.00 116.08 ? 188  VAL   D HG21 1 
ATOM   22123 H  HG22 . VAL   D  4  188 ? 21.983  -60.834 -93.523  1.00 116.08 ? 188  VAL   D HG22 1 
ATOM   22124 H  HG23 . VAL   D  4  188 ? 22.229  -60.356 -95.017  1.00 116.08 ? 188  VAL   D HG23 1 
ATOM   22125 N  N    . VAL   D  4  189 ? 21.292  -57.562 -96.062  1.00 106.53 ? 189  VAL   D N    1 
ATOM   22126 C  CA   . VAL   D  4  189 ? 21.002  -57.524 -97.488  1.00 112.78 ? 189  VAL   D CA   1 
ATOM   22127 C  C    . VAL   D  4  189 ? 21.321  -58.882 -98.099  1.00 117.36 ? 189  VAL   D C    1 
ATOM   22128 O  O    . VAL   D  4  189 ? 22.290  -59.548 -97.710  1.00 119.29 ? 189  VAL   D O    1 
ATOM   22129 C  CB   . VAL   D  4  189 ? 21.803  -56.403 -98.172  1.00 114.69 ? 189  VAL   D CB   1 
ATOM   22130 C  CG1  . VAL   D  4  189 ? 21.362  -56.235 -99.618  1.00 121.58 ? 189  VAL   D CG1  1 
ATOM   22131 C  CG2  . VAL   D  4  189 ? 21.649  -55.090 -97.413  1.00 112.36 ? 189  VAL   D CG2  1 
ATOM   22132 H  H    . VAL   D  4  189 ? 21.945  -57.058 -95.818  1.00 127.82 ? 189  VAL   D H    1 
ATOM   22133 H  HA   . VAL   D  4  189 ? 20.059  -57.338 -97.619  1.00 135.32 ? 189  VAL   D HA   1 
ATOM   22134 H  HB   . VAL   D  4  189 ? 22.742  -56.647 -98.166  1.00 137.61 ? 189  VAL   D HB   1 
ATOM   22135 H  HG11 . VAL   D  4  189 ? 21.867  -55.511 -100.020 1.00 145.87 ? 189  VAL   D HG11 1 
ATOM   22136 H  HG12 . VAL   D  4  189 ? 21.530  -57.061 -100.097 1.00 145.87 ? 189  VAL   D HG12 1 
ATOM   22137 H  HG13 . VAL   D  4  189 ? 20.415  -56.028 -99.637  1.00 145.87 ? 189  VAL   D HG13 1 
ATOM   22138 H  HG21 . VAL   D  4  189 ? 22.078  -54.381 -97.918  1.00 134.82 ? 189  VAL   D HG21 1 
ATOM   22139 H  HG22 . VAL   D  4  189 ? 20.705  -54.895 -97.306  1.00 134.82 ? 189  VAL   D HG22 1 
ATOM   22140 H  HG23 . VAL   D  4  189 ? 22.069  -55.177 -96.543  1.00 134.82 ? 189  VAL   D HG23 1 
ATOM   22141 N  N    . ALA   D  4  190 ? 20.499  -59.304 -99.063  1.00 118.52 ? 190  ALA   D N    1 
ATOM   22142 C  CA   . ALA   D  4  190 ? 20.705  -60.609 -99.683  1.00 115.71 ? 190  ALA   D CA   1 
ATOM   22143 C  C    . ALA   D  4  190 ? 22.067  -60.703 -100.356 1.00 120.98 ? 190  ALA   D C    1 
ATOM   22144 O  O    . ALA   D  4  190 ? 22.648  -61.791 -100.433 1.00 120.38 ? 190  ALA   D O    1 
ATOM   22145 C  CB   . ALA   D  4  190 ? 19.595  -60.892 -100.695 1.00 117.20 ? 190  ALA   D CB   1 
ATOM   22146 H  H    . ALA   D  4  190 ? 19.828  -58.861 -99.370  1.00 142.21 ? 190  ALA   D H    1 
ATOM   22147 H  HA   . ALA   D  4  190 ? 20.663  -61.290 -98.993  1.00 138.84 ? 190  ALA   D HA   1 
ATOM   22148 H  HB1  . ALA   D  4  190 ? 19.762  -61.750 -101.115 1.00 140.63 ? 190  ALA   D HB1  1 
ATOM   22149 H  HB2  . ALA   D  4  190 ? 18.742  -60.911 -100.232 1.00 140.63 ? 190  ALA   D HB2  1 
ATOM   22150 H  HB3  . ALA   D  4  190 ? 19.592  -60.190 -101.365 1.00 140.63 ? 190  ALA   D HB3  1 
ATOM   22151 N  N    . SER   D  4  191 ? 22.591  -59.579 -100.847 1.00 126.98 ? 191  SER   D N    1 
ATOM   22152 C  CA   . SER   D  4  191 ? 23.890  -59.564 -101.506 1.00 132.49 ? 191  SER   D CA   1 
ATOM   22153 C  C    . SER   D  4  191 ? 25.056  -59.586 -100.526 1.00 134.32 ? 191  SER   D C    1 
ATOM   22154 O  O    . SER   D  4  191 ? 26.187  -59.857 -100.944 1.00 138.06 ? 191  SER   D O    1 
ATOM   22155 C  CB   . SER   D  4  191 ? 24.007  -58.328 -102.402 1.00 135.89 ? 191  SER   D CB   1 
ATOM   22156 O  OG   . SER   D  4  191 ? 23.908  -57.135 -101.643 1.00 131.10 ? 191  SER   D OG   1 
ATOM   22157 H  H    . SER   D  4  191 ? 22.210  -58.809 -100.810 1.00 152.36 ? 191  SER   D H    1 
ATOM   22158 H  HA   . SER   D  4  191 ? 23.959  -60.355 -102.064 1.00 158.97 ? 191  SER   D HA   1 
ATOM   22159 H  HB2  . SER   D  4  191 ? 24.866  -58.345 -102.851 1.00 163.05 ? 191  SER   D HB2  1 
ATOM   22160 H  HB3  . SER   D  4  191 ? 23.290  -58.345 -103.056 1.00 163.05 ? 191  SER   D HB3  1 
ATOM   22161 H  HG   . SER   D  4  191 ? 23.962  -56.467 -102.149 1.00 157.31 ? 191  SER   D HG   1 
ATOM   22162 N  N    . THR   D  4  192 ? 24.815  -59.311 -99.245  1.00 132.40 ? 192  THR   D N    1 
ATOM   22163 C  CA   . THR   D  4  192 ? 25.867  -59.295 -98.238  1.00 130.03 ? 192  THR   D CA   1 
ATOM   22164 C  C    . THR   D  4  192 ? 25.975  -60.613 -97.482  1.00 122.99 ? 192  THR   D C    1 
ATOM   22165 O  O    . THR   D  4  192 ? 26.680  -60.679 -96.470  1.00 117.45 ? 192  THR   D O    1 
ATOM   22166 C  CB   . THR   D  4  192 ? 25.637  -58.148 -97.250  1.00 126.02 ? 192  THR   D CB   1 
ATOM   22167 O  OG1  . THR   D  4  192 ? 24.371  -58.314 -96.599  1.00 119.95 ? 192  THR   D OG1  1 
ATOM   22168 C  CG2  . THR   D  4  192 ? 25.671  -56.808 -97.972  1.00 132.03 ? 192  THR   D CG2  1 
ATOM   22169 H  H    . THR   D  4  192 ? 24.035  -59.128 -98.932  1.00 158.86 ? 192  THR   D H    1 
ATOM   22170 H  HA   . THR   D  4  192 ? 26.713  -59.138 -98.685  1.00 156.02 ? 192  THR   D HA   1 
ATOM   22171 H  HB   . THR   D  4  192 ? 26.340  -58.151 -96.581  1.00 151.20 ? 192  THR   D HB   1 
ATOM   22172 H  HG1  . THR   D  4  192 ? 23.910  -58.884 -97.008  1.00 143.92 ? 192  THR   D HG1  1 
ATOM   22173 H  HG21 . THR   D  4  192 ? 25.522  -56.087 -97.341  1.00 158.42 ? 192  THR   D HG21 1 
ATOM   22174 H  HG22 . THR   D  4  192 ? 26.534  -56.682 -98.397  1.00 158.42 ? 192  THR   D HG22 1 
ATOM   22175 H  HG23 . THR   D  4  192 ? 24.979  -56.780 -98.651  1.00 158.42 ? 192  THR   D HG23 1 
ATOM   22176 N  N    . TRP   D  4  193 ? 25.287  -61.660 -97.944  1.00 122.24 ? 193  TRP   D N    1 
ATOM   22177 C  CA   . TRP   D  4  193 ? 25.427  -62.986 -97.361  1.00 115.92 ? 193  TRP   D CA   1 
ATOM   22178 C  C    . TRP   D  4  193 ? 25.040  -64.002 -98.420  1.00 116.73 ? 193  TRP   D C    1 
ATOM   22179 O  O    . TRP   D  4  193 ? 24.032  -63.794 -99.109  1.00 119.32 ? 193  TRP   D O    1 
ATOM   22180 C  CB   . TRP   D  4  193 ? 24.551  -63.155 -96.114  1.00 109.84 ? 193  TRP   D CB   1 
ATOM   22181 C  CG   . TRP   D  4  193 ? 24.792  -64.453 -95.418  1.00 106.99 ? 193  TRP   D CG   1 
ATOM   22182 C  CD1  . TRP   D  4  193 ? 25.759  -64.720 -94.493  1.00 104.61 ? 193  TRP   D CD1  1 
ATOM   22183 C  CD2  . TRP   D  4  193 ? 24.066  -65.674 -95.604  1.00 104.73 ? 193  TRP   D CD2  1 
ATOM   22184 N  NE1  . TRP   D  4  193 ? 25.679  -66.031 -94.090  1.00 99.40  ? 193  TRP   D NE1  1 
ATOM   22185 C  CE2  . TRP   D  4  193 ? 24.646  -66.637 -94.757  1.00 98.58  ? 193  TRP   D CE2  1 
ATOM   22186 C  CE3  . TRP   D  4  193 ? 22.981  -66.045 -96.404  1.00 106.28 ? 193  TRP   D CE3  1 
ATOM   22187 C  CZ2  . TRP   D  4  193 ? 24.177  -67.946 -94.686  1.00 93.90  ? 193  TRP   D CZ2  1 
ATOM   22188 C  CZ3  . TRP   D  4  193 ? 22.516  -67.346 -96.329  1.00 102.19 ? 193  TRP   D CZ3  1 
ATOM   22189 C  CH2  . TRP   D  4  193 ? 23.113  -68.279 -95.476  1.00 95.65  ? 193  TRP   D CH2  1 
ATOM   22190 H  H    . TRP   D  4  193 ? 24.730  -61.623 -98.598  1.00 146.67 ? 193  TRP   D H    1 
ATOM   22191 H  HA   . TRP   D  4  193 ? 26.350  -63.134 -97.099  1.00 139.09 ? 193  TRP   D HA   1 
ATOM   22192 H  HB2  . TRP   D  4  193 ? 24.746  -62.438 -95.490  1.00 131.79 ? 193  TRP   D HB2  1 
ATOM   22193 H  HB3  . TRP   D  4  193 ? 23.618  -63.122 -96.376  1.00 131.79 ? 193  TRP   D HB3  1 
ATOM   22194 H  HD1  . TRP   D  4  193 ? 26.382  -64.104 -94.181  1.00 125.52 ? 193  TRP   D HD1  1 
ATOM   22195 H  HE1  . TRP   D  4  193 ? 26.192  -66.409 -93.513  1.00 119.26 ? 193  TRP   D HE1  1 
ATOM   22196 H  HE3  . TRP   D  4  193 ? 22.579  -65.429 -96.974  1.00 127.52 ? 193  TRP   D HE3  1 
ATOM   22197 H  HZ2  . TRP   D  4  193 ? 24.574  -68.570 -94.122  1.00 112.66 ? 193  TRP   D HZ2  1 
ATOM   22198 H  HZ3  . TRP   D  4  193 ? 21.793  -67.604 -96.855  1.00 122.60 ? 193  TRP   D HZ3  1 
ATOM   22199 H  HH2  . TRP   D  4  193 ? 22.779  -69.147 -95.446  1.00 114.76 ? 193  TRP   D HH2  1 
ATOM   22200 N  N    . PRO   D  4  194 ? 25.790  -65.109 -98.580  1.00 114.90 ? 194  PRO   D N    1 
ATOM   22201 C  CA   . PRO   D  4  194 ? 26.972  -65.526 -97.814  1.00 110.64 ? 194  PRO   D CA   1 
ATOM   22202 C  C    . PRO   D  4  194 ? 28.294  -64.939 -98.309  1.00 115.92 ? 194  PRO   D C    1 
ATOM   22203 O  O    . PRO   D  4  194 ? 29.348  -65.470 -97.962  1.00 115.79 ? 194  PRO   D O    1 
ATOM   22204 C  CB   . PRO   D  4  194 ? 26.983  -67.058 -97.984  1.00 109.62 ? 194  PRO   D CB   1 
ATOM   22205 C  CG   . PRO   D  4  194 ? 25.735  -67.406 -98.772  1.00 111.85 ? 194  PRO   D CG   1 
ATOM   22206 C  CD   . PRO   D  4  194 ? 25.359  -66.167 -99.506  1.00 116.40 ? 194  PRO   D CD   1 
ATOM   22207 H  HA   . PRO   D  4  194 ? 26.850  -65.280 -96.884  1.00 132.75 ? 194  PRO   D HA   1 
ATOM   22208 H  HB2  . PRO   D  4  194 ? 27.780  -67.326 -98.469  1.00 131.53 ? 194  PRO   D HB2  1 
ATOM   22209 H  HB3  . PRO   D  4  194 ? 26.968  -67.482 -97.112  1.00 131.53 ? 194  PRO   D HB3  1 
ATOM   22210 H  HG2  . PRO   D  4  194 ? 25.929  -68.127 -99.391  1.00 134.20 ? 194  PRO   D HG2  1 
ATOM   22211 H  HG3  . PRO   D  4  194 ? 25.028  -67.673 -98.163  1.00 134.20 ? 194  PRO   D HG3  1 
ATOM   22212 H  HD2  . PRO   D  4  194 ? 25.833  -66.105 -100.351 1.00 139.66 ? 194  PRO   D HD2  1 
ATOM   22213 H  HD3  . PRO   D  4  194 ? 24.402  -66.128 -99.659  1.00 139.66 ? 194  PRO   D HD3  1 
ATOM   22214 N  N    . SER   D  4  195 ? 28.245  -63.867 -99.103  1.00 120.82 ? 195  SER   D N    1 
ATOM   22215 C  CA   . SER   D  4  195 ? 29.484  -63.255 -99.575  1.00 125.86 ? 195  SER   D CA   1 
ATOM   22216 C  C    . SER   D  4  195 ? 30.346  -62.794 -98.406  1.00 121.07 ? 195  SER   D C    1 
ATOM   22217 O  O    . SER   D  4  195 ? 31.578  -62.898 -98.452  1.00 120.98 ? 195  SER   D O    1 
ATOM   22218 C  CB   . SER   D  4  195 ? 29.171  -62.085 -100.507 1.00 132.75 ? 195  SER   D CB   1 
ATOM   22219 O  OG   . SER   D  4  195 ? 28.426  -61.086 -99.836  1.00 129.53 ? 195  SER   D OG   1 
ATOM   22220 H  H    . SER   D  4  195 ? 27.525  -63.484 -99.375  1.00 144.97 ? 195  SER   D H    1 
ATOM   22221 H  HA   . SER   D  4  195 ? 29.987  -63.912 -100.081 1.00 151.02 ? 195  SER   D HA   1 
ATOM   22222 H  HB2  . SER   D  4  195 ? 30.005  -61.700 -100.820 1.00 159.28 ? 195  SER   D HB2  1 
ATOM   22223 H  HB3  . SER   D  4  195 ? 28.653  -62.412 -101.260 1.00 159.28 ? 195  SER   D HB3  1 
ATOM   22224 H  HG   . SER   D  4  195 ? 27.991  -60.630 -100.391 1.00 155.42 ? 195  SER   D HG   1 
ATOM   22225 N  N    . GLN   D  4  196 ? 29.717  -62.281 -97.353  1.00 117.78 ? 196  GLN   D N    1 
ATOM   22226 C  CA   . GLN   D  4  196 ? 30.389  -61.904 -96.120  1.00 115.89 ? 196  GLN   D CA   1 
ATOM   22227 C  C    . GLN   D  4  196 ? 29.925  -62.821 -94.994  1.00 108.12 ? 196  GLN   D C    1 
ATOM   22228 O  O    . GLN   D  4  196 ? 28.775  -63.269 -94.972  1.00 103.90 ? 196  GLN   D O    1 
ATOM   22229 C  CB   . GLN   D  4  196 ? 30.105  -60.442 -95.764  1.00 119.59 ? 196  GLN   D CB   1 
ATOM   22230 C  CG   . GLN   D  4  196 ? 30.582  -59.447 -96.812  1.00 133.22 ? 196  GLN   D CG   1 
ATOM   22231 C  CD   . GLN   D  4  196 ? 29.971  -58.072 -96.627  1.00 141.07 ? 196  GLN   D CD   1 
ATOM   22232 O  OE1  . GLN   D  4  196 ? 28.766  -57.889 -96.801  1.00 143.47 ? 196  GLN   D OE1  1 
ATOM   22233 N  NE2  . GLN   D  4  196 ? 30.799  -57.098 -96.271  1.00 145.61 ? 196  GLN   D NE2  1 
ATOM   22234 H  H    . GLN   D  4  196 ? 28.869  -62.138 -97.331  1.00 141.32 ? 196  GLN   D H    1 
ATOM   22235 H  HA   . GLN   D  4  196 ? 31.349  -62.000 -96.219  1.00 139.05 ? 196  GLN   D HA   1 
ATOM   22236 H  HB2  . GLN   D  4  196 ? 29.147  -60.328 -95.662  1.00 143.49 ? 196  GLN   D HB2  1 
ATOM   22237 H  HB3  . GLN   D  4  196 ? 30.554  -60.232 -94.930  1.00 143.49 ? 196  GLN   D HB3  1 
ATOM   22238 H  HG2  . GLN   D  4  196 ? 31.546  -59.359 -96.749  1.00 159.84 ? 196  GLN   D HG2  1 
ATOM   22239 H  HG3  . GLN   D  4  196 ? 30.334  -59.771 -97.692  1.00 159.84 ? 196  GLN   D HG3  1 
ATOM   22240 H  HE21 . GLN   D  4  196 ? 31.635  -57.265 -96.156  1.00 174.72 ? 196  GLN   D HE21 1 
ATOM   22241 H  HE22 . GLN   D  4  196 ? 30.500  -56.301 -96.154  1.00 174.72 ? 196  GLN   D HE22 1 
ATOM   22242 N  N    . SER   D  4  197 ? 30.831  -63.099 -94.059  1.00 108.21 ? 197  SER   D N    1 
ATOM   22243 C  CA   . SER   D  4  197 ? 30.565  -64.067 -93.003  1.00 107.69 ? 197  SER   D CA   1 
ATOM   22244 C  C    . SER   D  4  197 ? 29.824  -63.402 -91.852  1.00 104.64 ? 197  SER   D C    1 
ATOM   22245 O  O    . SER   D  4  197 ? 30.207  -62.319 -91.398  1.00 105.82 ? 197  SER   D O    1 
ATOM   22246 C  CB   . SER   D  4  197 ? 31.870  -64.684 -92.496  1.00 112.49 ? 197  SER   D CB   1 
ATOM   22247 O  OG   . SER   D  4  197 ? 32.414  -63.923 -91.432  1.00 114.69 ? 197  SER   D OG   1 
ATOM   22248 H  H    . SER   D  4  197 ? 31.610  -62.738 -94.016  1.00 129.83 ? 197  SER   D H    1 
ATOM   22249 H  HA   . SER   D  4  197 ? 30.008  -64.778 -93.360  1.00 129.21 ? 197  SER   D HA   1 
ATOM   22250 H  HB2  . SER   D  4  197 ? 31.691  -65.584 -92.180  1.00 134.97 ? 197  SER   D HB2  1 
ATOM   22251 H  HB3  . SER   D  4  197 ? 32.510  -64.710 -93.225  1.00 134.97 ? 197  SER   D HB3  1 
ATOM   22252 H  HG   . SER   D  4  197 ? 33.075  -64.323 -91.101  1.00 137.61 ? 197  SER   D HG   1 
ATOM   22253 N  N    . ILE   D  4  198 ? 28.764  -64.056 -91.382  1.00 101.50 ? 198  ILE   D N    1 
ATOM   22254 C  CA   . ILE   D  4  198 ? 28.004  -63.621 -90.217  1.00 96.01  ? 198  ILE   D CA   1 
ATOM   22255 C  C    . ILE   D  4  198 ? 28.167  -64.679 -89.136  1.00 93.47  ? 198  ILE   D C    1 
ATOM   22256 O  O    . ILE   D  4  198 ? 27.986  -65.874 -89.399  1.00 93.73  ? 198  ILE   D O    1 
ATOM   22257 C  CB   . ILE   D  4  198 ? 26.519  -63.397 -90.555  1.00 92.07  ? 198  ILE   D CB   1 
ATOM   22258 C  CG1  . ILE   D  4  198 ? 26.389  -62.251 -91.563  1.00 92.20  ? 198  ILE   D CG1  1 
ATOM   22259 C  CG2  . ILE   D  4  198 ? 25.715  -63.104 -89.289  1.00 89.32  ? 198  ILE   D CG2  1 
ATOM   22260 C  CD1  . ILE   D  4  198 ? 24.970  -61.943 -91.985  1.00 90.55  ? 198  ILE   D CD1  1 
ATOM   22261 H  H    . ILE   D  4  198 ? 28.457  -64.778 -91.735  1.00 121.78 ? 198  ILE   D H    1 
ATOM   22262 H  HA   . ILE   D  4  198 ? 28.363  -62.783 -89.885  1.00 115.20 ? 198  ILE   D HA   1 
ATOM   22263 H  HB   . ILE   D  4  198 ? 26.160  -64.206 -90.953  1.00 110.47 ? 198  ILE   D HB   1 
ATOM   22264 H  HG12 . ILE   D  4  198 ? 26.758  -61.447 -91.166  1.00 110.63 ? 198  ILE   D HG12 1 
ATOM   22265 H  HG13 . ILE   D  4  198 ? 26.888  -62.485 -92.362  1.00 110.63 ? 198  ILE   D HG13 1 
ATOM   22266 H  HG21 . ILE   D  4  198 ? 24.785  -62.971 -89.528  1.00 107.17 ? 198  ILE   D HG21 1 
ATOM   22267 H  HG22 . ILE   D  4  198 ? 25.797  -63.856 -88.682  1.00 107.17 ? 198  ILE   D HG22 1 
ATOM   22268 H  HG23 . ILE   D  4  198 ? 26.067  -62.302 -88.870  1.00 107.17 ? 198  ILE   D HG23 1 
ATOM   22269 H  HD11 . ILE   D  4  198 ? 24.987  -61.255 -92.668  1.00 108.64 ? 198  ILE   D HD11 1 
ATOM   22270 H  HD12 . ILE   D  4  198 ? 24.564  -62.750 -92.338  1.00 108.64 ? 198  ILE   D HD12 1 
ATOM   22271 H  HD13 . ILE   D  4  198 ? 24.472  -61.632 -91.213  1.00 108.64 ? 198  ILE   D HD13 1 
ATOM   22272 N  N    . THR   D  4  199 ? 28.507  -64.240 -87.928  1.00 91.40  ? 199  THR   D N    1 
ATOM   22273 C  CA   . THR   D  4  199 ? 28.795  -65.140 -86.822  1.00 88.53  ? 199  THR   D CA   1 
ATOM   22274 C  C    . THR   D  4  199 ? 27.959  -64.758 -85.612  1.00 86.40  ? 199  THR   D C    1 
ATOM   22275 O  O    . THR   D  4  199 ? 27.795  -63.574 -85.303  1.00 86.42  ? 199  THR   D O    1 
ATOM   22276 C  CB   . THR   D  4  199 ? 30.286  -65.109 -86.454  1.00 89.71  ? 199  THR   D CB   1 
ATOM   22277 O  OG1  . THR   D  4  199 ? 31.066  -65.537 -87.578  1.00 94.73  ? 199  THR   D OG1  1 
ATOM   22278 C  CG2  . THR   D  4  199 ? 30.573  -66.016 -85.261  1.00 86.47  ? 199  THR   D CG2  1 
ATOM   22279 H  H    . THR   D  4  199 ? 28.577  -63.408 -87.722  1.00 109.66 ? 199  THR   D H    1 
ATOM   22280 H  HA   . THR   D  4  199 ? 28.559  -66.046 -87.077  1.00 106.22 ? 199  THR   D HA   1 
ATOM   22281 H  HB   . THR   D  4  199 ? 30.536  -64.204 -86.211  1.00 107.64 ? 199  THR   D HB   1 
ATOM   22282 H  HG1  . THR   D  4  199 ? 31.884  -65.494 -87.392  1.00 113.65 ? 199  THR   D HG1  1 
ATOM   22283 H  HG21 . THR   D  4  199 ? 31.527  -66.041 -85.086  1.00 103.74 ? 199  THR   D HG21 1 
ATOM   22284 H  HG22 . THR   D  4  199 ? 30.117  -65.681 -84.473  1.00 103.74 ? 199  THR   D HG22 1 
ATOM   22285 H  HG23 . THR   D  4  199 ? 30.262  -66.916 -85.447  1.00 103.74 ? 199  THR   D HG23 1 
ATOM   22286 N  N    . CYS   D  4  200 ? 27.436  -65.774 -84.932  1.00 85.78  ? 200  CYS   D N    1 
ATOM   22287 C  CA   . CYS   D  4  200 ? 26.673  -65.592 -83.703  1.00 85.85  ? 200  CYS   D CA   1 
ATOM   22288 C  C    . CYS   D  4  200 ? 27.621  -65.751 -82.519  1.00 85.75  ? 200  CYS   D C    1 
ATOM   22289 O  O    . CYS   D  4  200 ? 28.113  -66.852 -82.253  1.00 87.78  ? 200  CYS   D O    1 
ATOM   22290 C  CB   . CYS   D  4  200 ? 25.531  -66.600 -83.631  1.00 85.83  ? 200  CYS   D CB   1 
ATOM   22291 S  SG   . CYS   D  4  200 ? 24.653  -66.625 -82.056  1.00 84.00  ? 200  CYS   D SG   1 
ATOM   22292 H  H    . CYS   D  4  200 ? 27.511  -66.597 -85.168  1.00 102.92 ? 200  CYS   D H    1 
ATOM   22293 H  HA   . CYS   D  4  200 ? 26.296  -64.698 -83.680  1.00 103.00 ? 200  CYS   D HA   1 
ATOM   22294 H  HB2  . CYS   D  4  200 ? 24.885  -66.385 -84.323  1.00 102.97 ? 200  CYS   D HB2  1 
ATOM   22295 H  HB3  . CYS   D  4  200 ? 25.892  -67.488 -83.779  1.00 102.97 ? 200  CYS   D HB3  1 
ATOM   22296 N  N    . ASN   D  4  201 ? 27.881  -64.653 -81.815  1.00 84.58  ? 201  ASN   D N    1 
ATOM   22297 C  CA   . ASN   D  4  201 ? 28.741  -64.664 -80.638  1.00 83.88  ? 201  ASN   D CA   1 
ATOM   22298 C  C    . ASN   D  4  201 ? 27.865  -64.809 -79.401  1.00 79.47  ? 201  ASN   D C    1 
ATOM   22299 O  O    . ASN   D  4  201 ? 26.969  -63.989 -79.173  1.00 79.76  ? 201  ASN   D O    1 
ATOM   22300 C  CB   . ASN   D  4  201 ? 29.577  -63.387 -80.555  1.00 88.69  ? 201  ASN   D CB   1 
ATOM   22301 C  CG   . ASN   D  4  201 ? 30.066  -62.919 -81.911  1.00 92.49  ? 201  ASN   D CG   1 
ATOM   22302 O  OD1  . ASN   D  4  201 ? 29.515  -61.985 -82.493  1.00 93.51  ? 201  ASN   D OD1  1 
ATOM   22303 N  ND2  . ASN   D  4  201 ? 31.105  -63.569 -82.423  1.00 94.36  ? 201  ASN   D ND2  1 
ATOM   22304 H  H    . ASN   D  4  201 ? 27.565  -63.876 -82.003  1.00 101.48 ? 201  ASN   D H    1 
ATOM   22305 H  HA   . ASN   D  4  201 ? 29.352  -65.417 -80.688  1.00 100.64 ? 201  ASN   D HA   1 
ATOM   22306 H  HB2  . ASN   D  4  201 ? 29.036  -62.680 -80.171  1.00 106.41 ? 201  ASN   D HB2  1 
ATOM   22307 H  HB3  . ASN   D  4  201 ? 30.352  -63.552 -79.997  1.00 106.41 ? 201  ASN   D HB3  1 
ATOM   22308 H  HD21 . ASN   D  4  201 ? 31.419  -63.340 -83.191  1.00 113.21 ? 201  ASN   D HD21 1 
ATOM   22309 H  HD22 . ASN   D  4  201 ? 31.463  -64.218 -81.988  1.00 113.21 ? 201  ASN   D HD22 1 
ATOM   22310 N  N    . VAL   D  4  202 ? 28.120  -65.848 -78.610  1.00 78.37  ? 202  VAL   D N    1 
ATOM   22311 C  CA   . VAL   D  4  202 ? 27.352  -66.136 -77.406  1.00 77.68  ? 202  VAL   D CA   1 
ATOM   22312 C  C    . VAL   D  4  202 ? 28.318  -66.280 -76.241  1.00 80.84  ? 202  VAL   D C    1 
ATOM   22313 O  O    . VAL   D  4  202 ? 29.393  -66.874 -76.383  1.00 84.59  ? 202  VAL   D O    1 
ATOM   22314 C  CB   . VAL   D  4  202 ? 26.499  -67.412 -77.563  1.00 77.55  ? 202  VAL   D CB   1 
ATOM   22315 C  CG1  . VAL   D  4  202 ? 25.746  -67.719 -76.274  1.00 78.95  ? 202  VAL   D CG1  1 
ATOM   22316 C  CG2  . VAL   D  4  202 ? 25.531  -67.264 -78.727  1.00 74.48  ? 202  VAL   D CG2  1 
ATOM   22317 H  H    . VAL   D  4  202 ? 28.751  -66.414 -78.755  1.00 94.02  ? 202  VAL   D H    1 
ATOM   22318 H  HA   . VAL   D  4  202 ? 26.756  -65.393 -77.223  1.00 93.20  ? 202  VAL   D HA   1 
ATOM   22319 H  HB   . VAL   D  4  202 ? 27.087  -68.160 -77.751  1.00 93.04  ? 202  VAL   D HB   1 
ATOM   22320 H  HG11 . VAL   D  4  202 ? 25.152  -68.471 -76.426  1.00 94.73  ? 202  VAL   D HG11 1 
ATOM   22321 H  HG12 . VAL   D  4  202 ? 26.387  -67.939 -75.579  1.00 94.73  ? 202  VAL   D HG12 1 
ATOM   22322 H  HG13 . VAL   D  4  202 ? 25.232  -66.938 -76.014  1.00 94.73  ? 202  VAL   D HG13 1 
ATOM   22323 H  HG21 . VAL   D  4  202 ? 25.010  -68.078 -78.810  1.00 89.36  ? 202  VAL   D HG21 1 
ATOM   22324 H  HG22 . VAL   D  4  202 ? 24.944  -66.511 -78.555  1.00 89.36  ? 202  VAL   D HG22 1 
ATOM   22325 H  HG23 . VAL   D  4  202 ? 26.037  -67.111 -79.540  1.00 89.36  ? 202  VAL   D HG23 1 
ATOM   22326 N  N    . ALA   D  4  203 ? 27.932  -65.740 -75.088  1.00 81.24  ? 203  ALA   D N    1 
ATOM   22327 C  CA   . ALA   D  4  203 ? 28.749  -65.813 -73.885  1.00 84.35  ? 203  ALA   D CA   1 
ATOM   22328 C  C    . ALA   D  4  203 ? 27.856  -66.097 -72.690  1.00 82.57  ? 203  ALA   D C    1 
ATOM   22329 O  O    . ALA   D  4  203 ? 26.864  -65.395 -72.472  1.00 83.20  ? 203  ALA   D O    1 
ATOM   22330 C  CB   . ALA   D  4  203 ? 29.528  -64.512 -73.661  1.00 89.23  ? 203  ALA   D CB   1 
ATOM   22331 H  H    . ALA   D  4  203 ? 27.189  -65.320 -74.977  1.00 97.47  ? 203  ALA   D H    1 
ATOM   22332 H  HA   . ALA   D  4  203 ? 29.384  -66.540 -73.973  1.00 101.20 ? 203  ALA   D HA   1 
ATOM   22333 H  HB1  . ALA   D  4  203 ? 30.062  -64.599 -72.856  1.00 107.06 ? 203  ALA   D HB1  1 
ATOM   22334 H  HB2  . ALA   D  4  203 ? 30.104  -64.354 -74.425  1.00 107.06 ? 203  ALA   D HB2  1 
ATOM   22335 H  HB3  . ALA   D  4  203 ? 28.899  -63.780 -73.564  1.00 107.06 ? 203  ALA   D HB3  1 
ATOM   22336 N  N    . HIS   D  4  204 ? 28.213  -67.122 -71.922  1.00 81.84  ? 204  HIS   D N    1 
ATOM   22337 C  CA   . HIS   D  4  204 ? 27.512  -67.465 -70.684  1.00 80.79  ? 204  HIS   D CA   1 
ATOM   22338 C  C    . HIS   D  4  204 ? 28.494  -67.320 -69.530  1.00 81.15  ? 204  HIS   D C    1 
ATOM   22339 O  O    . HIS   D  4  204 ? 29.278  -68.248 -69.259  1.00 81.21  ? 204  HIS   D O    1 
ATOM   22340 C  CB   . HIS   D  4  204 ? 26.948  -68.884 -70.746  1.00 79.16  ? 204  HIS   D CB   1 
ATOM   22341 C  CG   . HIS   D  4  204 ? 25.947  -69.181 -69.673  1.00 82.56  ? 204  HIS   D CG   1 
ATOM   22342 N  ND1  . HIS   D  4  204 ? 26.026  -70.298 -68.869  1.00 85.88  ? 204  HIS   D ND1  1 
ATOM   22343 C  CD2  . HIS   D  4  204 ? 24.846  -68.505 -69.270  1.00 83.15  ? 204  HIS   D CD2  1 
ATOM   22344 C  CE1  . HIS   D  4  204 ? 25.016  -70.298 -68.018  1.00 87.56  ? 204  HIS   D CE1  1 
ATOM   22345 N  NE2  . HIS   D  4  204 ? 24.285  -69.220 -68.240  1.00 86.07  ? 204  HIS   D NE2  1 
ATOM   22346 H  H    . HIS   D  4  204 ? 28.871  -67.646 -72.099  1.00 98.19  ? 204  HIS   D H    1 
ATOM   22347 H  HA   . HIS   D  4  204 ? 26.766  -66.861 -70.546  1.00 96.93  ? 204  HIS   D HA   1 
ATOM   22348 H  HB2  . HIS   D  4  204 ? 26.511  -69.009 -71.603  1.00 94.97  ? 204  HIS   D HB2  1 
ATOM   22349 H  HB3  . HIS   D  4  204 ? 27.679  -69.515 -70.652  1.00 94.97  ? 204  HIS   D HB3  1 
ATOM   22350 H  HD2  . HIS   D  4  204 ? 24.528  -67.705 -69.623  1.00 99.76  ? 204  HIS   D HD2  1 
ATOM   22351 H  HE1  . HIS   D  4  204 ? 24.849  -70.946 -67.373  1.00 105.06 ? 204  HIS   D HE1  1 
ATOM   22352 H  HE2  . HIS   D  4  204 ? 23.573  -69.002 -67.809  1.00 103.27 ? 204  HIS   D HE2  1 
ATOM   22353 N  N    . PRO   D  4  205 ? 28.497  -66.188 -68.821  1.00 80.06  ? 205  PRO   D N    1 
ATOM   22354 C  CA   . PRO   D  4  205 ? 29.537  -65.976 -67.800  1.00 83.65  ? 205  PRO   D CA   1 
ATOM   22355 C  C    . PRO   D  4  205 ? 29.488  -66.984 -66.667  1.00 90.21  ? 205  PRO   D C    1 
ATOM   22356 O  O    . PRO   D  4  205 ? 30.543  -67.363 -66.143  1.00 97.89  ? 205  PRO   D O    1 
ATOM   22357 C  CB   . PRO   D  4  205 ? 29.252  -64.551 -67.304  1.00 81.21  ? 205  PRO   D CB   1 
ATOM   22358 C  CG   . PRO   D  4  205 ? 27.800  -64.348 -67.562  1.00 78.04  ? 205  PRO   D CG   1 
ATOM   22359 C  CD   . PRO   D  4  205 ? 27.499  -65.103 -68.827  1.00 75.83  ? 205  PRO   D CD   1 
ATOM   22360 H  HA   . PRO   D  4  205 ? 30.414  -66.005 -68.212  1.00 100.36 ? 205  PRO   D HA   1 
ATOM   22361 H  HB2  . PRO   D  4  205 ? 29.451  -64.483 -66.357  1.00 97.43  ? 205  PRO   D HB2  1 
ATOM   22362 H  HB3  . PRO   D  4  205 ? 29.787  -63.914 -67.802  1.00 97.43  ? 205  PRO   D HB3  1 
ATOM   22363 H  HG2  . PRO   D  4  205 ? 27.284  -64.700 -66.820  1.00 93.62  ? 205  PRO   D HG2  1 
ATOM   22364 H  HG3  . PRO   D  4  205 ? 27.617  -63.402 -67.674  1.00 93.62  ? 205  PRO   D HG3  1 
ATOM   22365 H  HD2  . PRO   D  4  205 ? 26.599  -65.462 -68.808  1.00 90.98  ? 205  PRO   D HD2  1 
ATOM   22366 H  HD3  . PRO   D  4  205 ? 27.613  -64.533 -69.604  1.00 90.98  ? 205  PRO   D HD3  1 
ATOM   22367 N  N    . ALA   D  4  206 ? 28.296  -67.432 -66.270  1.00 89.49  ? 206  ALA   D N    1 
ATOM   22368 C  CA   . ALA   D  4  206 ? 28.190  -68.392 -65.179  1.00 93.34  ? 206  ALA   D CA   1 
ATOM   22369 C  C    . ALA   D  4  206 ? 28.903  -69.701 -65.491  1.00 91.66  ? 206  ALA   D C    1 
ATOM   22370 O  O    . ALA   D  4  206 ? 29.205  -70.464 -64.566  1.00 93.17  ? 206  ALA   D O    1 
ATOM   22371 C  CB   . ALA   D  4  206 ? 26.720  -68.663 -64.865  1.00 96.00  ? 206  ALA   D CB   1 
ATOM   22372 H  H    . ALA   D  4  206 ? 27.543  -67.198 -66.614  1.00 107.37 ? 206  ALA   D H    1 
ATOM   22373 H  HA   . ALA   D  4  206 ? 28.603  -68.011 -64.389  1.00 111.99 ? 206  ALA   D HA   1 
ATOM   22374 H  HB1  . ALA   D  4  206 ? 26.665  -69.303 -64.138  1.00 115.18 ? 206  ALA   D HB1  1 
ATOM   22375 H  HB2  . ALA   D  4  206 ? 26.294  -67.831 -64.606  1.00 115.18 ? 206  ALA   D HB2  1 
ATOM   22376 H  HB3  . ALA   D  4  206 ? 26.289  -69.024 -65.656  1.00 115.18 ? 206  ALA   D HB3  1 
ATOM   22377 N  N    . SER   D  4  207 ? 29.175  -69.979 -66.766  1.00 89.50  ? 207  SER   D N    1 
ATOM   22378 C  CA   . SER   D  4  207 ? 29.885  -71.186 -67.171  1.00 91.22  ? 207  SER   D CA   1 
ATOM   22379 C  C    . SER   D  4  207 ? 31.230  -70.882 -67.818  1.00 89.35  ? 207  SER   D C    1 
ATOM   22380 O  O    . SER   D  4  207 ? 31.876  -71.800 -68.338  1.00 87.46  ? 207  SER   D O    1 
ATOM   22381 C  CB   . SER   D  4  207 ? 29.027  -72.011 -68.136  1.00 93.43  ? 207  SER   D CB   1 
ATOM   22382 O  OG   . SER   D  4  207 ? 27.813  -72.414 -67.529  1.00 99.13  ? 207  SER   D OG   1 
ATOM   22383 H  H    . SER   D  4  207 ? 28.953  -69.474 -67.426  1.00 107.38 ? 207  SER   D H    1 
ATOM   22384 H  HA   . SER   D  4  207 ? 30.050  -71.722 -66.379  1.00 109.44 ? 207  SER   D HA   1 
ATOM   22385 H  HB2  . SER   D  4  207 ? 28.824  -71.471 -68.916  1.00 112.10 ? 207  SER   D HB2  1 
ATOM   22386 H  HB3  . SER   D  4  207 ? 29.523  -72.802 -68.400  1.00 112.10 ? 207  SER   D HB3  1 
ATOM   22387 H  HG   . SER   D  4  207 ? 27.272  -71.771 -67.514  1.00 118.94 ? 207  SER   D HG   1 
ATOM   22388 N  N    . SER   D  4  208 ? 31.673  -69.624 -67.799  1.00 92.24  ? 208  SER   D N    1 
ATOM   22389 C  CA   . SER   D  4  208 ? 32.902  -69.223 -68.484  1.00 97.30  ? 208  SER   D CA   1 
ATOM   22390 C  C    . SER   D  4  208 ? 32.884  -69.700 -69.934  1.00 99.10  ? 208  SER   D C    1 
ATOM   22391 O  O    . SER   D  4  208 ? 33.898  -70.133 -70.486  1.00 103.70 ? 208  SER   D O    1 
ATOM   22392 C  CB   . SER   D  4  208 ? 34.136  -69.748 -67.749  1.00 99.08  ? 208  SER   D CB   1 
ATOM   22393 O  OG   . SER   D  4  208 ? 34.251  -69.160 -66.465  1.00 100.40 ? 208  SER   D OG   1 
ATOM   22394 H  H    . SER   D  4  208 ? 31.276  -68.979 -67.393  1.00 110.67 ? 208  SER   D H    1 
ATOM   22395 H  HA   . SER   D  4  208 ? 32.954  -68.255 -68.490  1.00 116.74 ? 208  SER   D HA   1 
ATOM   22396 H  HB2  . SER   D  4  208 ? 34.057  -70.710 -67.648  1.00 118.88 ? 208  SER   D HB2  1 
ATOM   22397 H  HB3  . SER   D  4  208 ? 34.927  -69.532 -68.267  1.00 118.88 ? 208  SER   D HB3  1 
ATOM   22398 H  HG   . SER   D  4  208 ? 34.938  -69.448 -66.077  1.00 120.47 ? 208  SER   D HG   1 
ATOM   22399 N  N    . THR   D  4  209 ? 31.711  -69.617 -70.555  1.00 94.26  ? 209  THR   D N    1 
ATOM   22400 C  CA   . THR   D  4  209 ? 31.498  -70.090 -71.915  1.00 88.42  ? 209  THR   D CA   1 
ATOM   22401 C  C    . THR   D  4  209 ? 31.569  -68.926 -72.893  1.00 86.07  ? 209  THR   D C    1 
ATOM   22402 O  O    . THR   D  4  209 ? 31.020  -67.850 -72.637  1.00 86.82  ? 209  THR   D O    1 
ATOM   22403 C  CB   . THR   D  4  209 ? 30.140  -70.786 -72.041  1.00 85.44  ? 209  THR   D CB   1 
ATOM   22404 O  OG1  . THR   D  4  209 ? 30.040  -71.832 -71.065  1.00 91.30  ? 209  THR   D OG1  1 
ATOM   22405 C  CG2  . THR   D  4  209 ? 29.958  -71.380 -73.433  1.00 79.32  ? 209  THR   D CG2  1 
ATOM   22406 H  H    . THR   D  4  209 ? 31.004  -69.282 -70.197  1.00 113.10 ? 209  THR   D H    1 
ATOM   22407 H  HA   . THR   D  4  209 ? 32.194  -70.726 -72.145  1.00 106.08 ? 209  THR   D HA   1 
ATOM   22408 H  HB   . THR   D  4  209 ? 29.436  -70.136 -71.894  1.00 102.51 ? 209  THR   D HB   1 
ATOM   22409 H  HG1  . THR   D  4  209 ? 29.294  -72.213 -71.129  1.00 109.54 ? 209  THR   D HG1  1 
ATOM   22410 H  HG21 . THR   D  4  209 ? 29.134  -71.890 -73.471  1.00 95.17  ? 209  THR   D HG21 1 
ATOM   22411 H  HG22 . THR   D  4  209 ? 29.919  -70.670 -74.093  1.00 95.17  ? 209  THR   D HG22 1 
ATOM   22412 H  HG23 . THR   D  4  209 ? 30.701  -71.966 -73.643  1.00 95.17  ? 209  THR   D HG23 1 
ATOM   22413 N  N    . LYS   D  4  210 ? 32.251  -69.148 -74.014  1.00 87.43  ? 210  LYS   D N    1 
ATOM   22414 C  CA   . LYS   D  4  210 ? 32.293  -68.186 -75.113  1.00 93.73  ? 210  LYS   D CA   1 
ATOM   22415 C  C    . LYS   D  4  210 ? 32.330  -68.977 -76.412  1.00 99.29  ? 210  LYS   D C    1 
ATOM   22416 O  O    . LYS   D  4  210 ? 33.324  -69.650 -76.704  1.00 108.91 ? 210  LYS   D O    1 
ATOM   22417 C  CB   . LYS   D  4  210 ? 33.499  -67.254 -75.004  1.00 99.52  ? 210  LYS   D CB   1 
ATOM   22418 C  CG   . LYS   D  4  210 ? 33.178  -65.895 -74.396  1.00 102.74 ? 210  LYS   D CG   1 
ATOM   22419 C  CD   . LYS   D  4  210 ? 34.375  -64.958 -74.461  1.00 110.30 ? 210  LYS   D CD   1 
ATOM   22420 C  CE   . LYS   D  4  210 ? 34.039  -63.576 -73.919  1.00 116.04 ? 210  LYS   D CE   1 
ATOM   22421 N  NZ   . LYS   D  4  210 ? 33.609  -63.619 -72.495  1.00 119.96 ? 210  LYS   D NZ   1 
ATOM   22422 H  H    . LYS   D  4  210 ? 32.707  -69.861 -74.164  1.00 104.90 ? 210  LYS   D H    1 
ATOM   22423 H  HA   . LYS   D  4  210 ? 31.492  -67.640 -75.098  1.00 112.46 ? 210  LYS   D HA   1 
ATOM   22424 H  HB2  . LYS   D  4  210 ? 34.169  -67.676 -74.444  1.00 119.41 ? 210  LYS   D HB2  1 
ATOM   22425 H  HB3  . LYS   D  4  210 ? 33.857  -67.102 -75.892  1.00 119.41 ? 210  LYS   D HB3  1 
ATOM   22426 H  HG2  . LYS   D  4  210 ? 32.446  -65.489 -74.885  1.00 123.27 ? 210  LYS   D HG2  1 
ATOM   22427 H  HG3  . LYS   D  4  210 ? 32.931  -66.010 -73.465  1.00 123.27 ? 210  LYS   D HG3  1 
ATOM   22428 H  HD2  . LYS   D  4  210 ? 35.099  -65.325 -73.929  1.00 132.34 ? 210  LYS   D HD2  1 
ATOM   22429 H  HD3  . LYS   D  4  210 ? 34.657  -64.862 -75.384  1.00 132.34 ? 210  LYS   D HD3  1 
ATOM   22430 H  HE2  . LYS   D  4  210 ? 34.824  -63.010 -73.981  1.00 139.23 ? 210  LYS   D HE2  1 
ATOM   22431 H  HE3  . LYS   D  4  210 ? 33.315  -63.197 -74.442  1.00 139.23 ? 210  LYS   D HE3  1 
ATOM   22432 H  HZ1  . LYS   D  4  210 ? 33.564  -62.794 -72.165  1.00 143.93 ? 210  LYS   D HZ1  1 
ATOM   22433 H  HZ2  . LYS   D  4  210 ? 32.807  -64.000 -72.430  1.00 143.93 ? 210  LYS   D HZ2  1 
ATOM   22434 H  HZ3  . LYS   D  4  210 ? 34.192  -64.091 -72.015  1.00 143.93 ? 210  LYS   D HZ3  1 
ATOM   22435 N  N    . VAL   D  4  211 ? 31.251  -68.896 -77.187  1.00 93.23  ? 211  VAL   D N    1 
ATOM   22436 C  CA   . VAL   D  4  211 ? 31.091  -69.669 -78.411  1.00 88.31  ? 211  VAL   D CA   1 
ATOM   22437 C  C    . VAL   D  4  211 ? 30.836  -68.716 -79.568  1.00 91.70  ? 211  VAL   D C    1 
ATOM   22438 O  O    . VAL   D  4  211 ? 30.118  -67.720 -79.421  1.00 93.04  ? 211  VAL   D O    1 
ATOM   22439 C  CB   . VAL   D  4  211 ? 29.941  -70.691 -78.285  1.00 77.46  ? 211  VAL   D CB   1 
ATOM   22440 C  CG1  . VAL   D  4  211 ? 29.710  -71.409 -79.605  1.00 74.26  ? 211  VAL   D CG1  1 
ATOM   22441 C  CG2  . VAL   D  4  211 ? 30.238  -71.691 -77.181  1.00 75.19  ? 211  VAL   D CG2  1 
ATOM   22442 H  H    . VAL   D  4  211 ? 30.581  -68.384 -77.018  1.00 111.85 ? 211  VAL   D H    1 
ATOM   22443 H  HA   . VAL   D  4  211 ? 31.914  -70.150 -78.593  1.00 105.95 ? 211  VAL   D HA   1 
ATOM   22444 H  HB   . VAL   D  4  211 ? 29.127  -70.215 -78.055  1.00 92.94  ? 211  VAL   D HB   1 
ATOM   22445 H  HG11 . VAL   D  4  211 ? 29.036  -72.095 -79.478  1.00 89.09  ? 211  VAL   D HG11 1 
ATOM   22446 H  HG12 . VAL   D  4  211 ? 29.407  -70.766 -80.265  1.00 89.09  ? 211  VAL   D HG12 1 
ATOM   22447 H  HG13 . VAL   D  4  211 ? 30.543  -71.813 -79.895  1.00 89.09  ? 211  VAL   D HG13 1 
ATOM   22448 H  HG21 . VAL   D  4  211 ? 29.507  -72.326 -77.125  1.00 90.21  ? 211  VAL   D HG21 1 
ATOM   22449 H  HG22 . VAL   D  4  211 ? 31.064  -72.156 -77.390  1.00 90.21  ? 211  VAL   D HG22 1 
ATOM   22450 H  HG23 . VAL   D  4  211 ? 30.330  -71.216 -76.340  1.00 90.21  ? 211  VAL   D HG23 1 
ATOM   22451 N  N    . ASP   D  4  212 ? 31.425  -69.028 -80.721  1.00 92.82  ? 212  ASP   D N    1 
ATOM   22452 C  CA   . ASP   D  4  212 ? 31.202  -68.290 -81.958  1.00 91.55  ? 212  ASP   D CA   1 
ATOM   22453 C  C    . ASP   D  4  212 ? 30.758  -69.280 -83.023  1.00 87.06  ? 212  ASP   D C    1 
ATOM   22454 O  O    . ASP   D  4  212 ? 31.506  -70.204 -83.361  1.00 87.39  ? 212  ASP   D O    1 
ATOM   22455 C  CB   . ASP   D  4  212 ? 32.468  -67.553 -82.400  1.00 95.28  ? 212  ASP   D CB   1 
ATOM   22456 C  CG   . ASP   D  4  212 ? 32.956  -66.559 -81.366  1.00 96.71  ? 212  ASP   D CG   1 
ATOM   22457 O  OD1  . ASP   D  4  212 ? 32.109  -65.891 -80.736  1.00 94.01  ? 212  ASP   D OD1  1 
ATOM   22458 O  OD2  . ASP   D  4  212 ? 34.186  -66.449 -81.178  1.00 102.00 ? 212  ASP   D OD2  1 
ATOM   22459 H  H    . ASP   D  4  212 ? 31.975  -69.683 -80.812  1.00 111.37 ? 212  ASP   D H    1 
ATOM   22460 H  HA   . ASP   D  4  212 ? 30.500  -67.633 -81.828  1.00 109.85 ? 212  ASP   D HA   1 
ATOM   22461 H  HB2  . ASP   D  4  212 ? 33.175  -68.200 -82.552  1.00 114.31 ? 212  ASP   D HB2  1 
ATOM   22462 H  HB3  . ASP   D  4  212 ? 32.282  -67.067 -83.219  1.00 114.31 ? 212  ASP   D HB3  1 
ATOM   22463 N  N    . LYS   D  4  213 ? 29.548  -69.093 -83.546  1.00 82.28  ? 213  LYS   D N    1 
ATOM   22464 C  CA   . LYS   D  4  213 ? 28.977  -69.978 -84.551  1.00 81.86  ? 213  LYS   D CA   1 
ATOM   22465 C  C    . LYS   D  4  213 ? 28.710  -69.204 -85.833  1.00 83.28  ? 213  LYS   D C    1 
ATOM   22466 O  O    . LYS   D  4  213 ? 28.189  -68.084 -85.797  1.00 84.07  ? 213  LYS   D O    1 
ATOM   22467 C  CB   . LYS   D  4  213 ? 27.674  -70.619 -84.055  1.00 79.65  ? 213  LYS   D CB   1 
ATOM   22468 C  CG   . LYS   D  4  213 ? 27.841  -71.546 -82.859  1.00 81.02  ? 213  LYS   D CG   1 
ATOM   22469 C  CD   . LYS   D  4  213 ? 28.796  -72.692 -83.158  1.00 88.15  ? 213  LYS   D CD   1 
ATOM   22470 C  CE   . LYS   D  4  213 ? 28.706  -73.777 -82.096  1.00 91.80  ? 213  LYS   D CE   1 
ATOM   22471 N  NZ   . LYS   D  4  213 ? 29.828  -74.751 -82.184  1.00 97.16  ? 213  LYS   D NZ   1 
ATOM   22472 H  H    . LYS   D  4  213 ? 29.029  -68.444 -83.327  1.00 98.72  ? 213  LYS   D H    1 
ATOM   22473 H  HA   . LYS   D  4  213 ? 29.610  -70.686 -84.748  1.00 98.21  ? 213  LYS   D HA   1 
ATOM   22474 H  HB2  . LYS   D  4  213 ? 27.062  -69.913 -83.796  1.00 95.56  ? 213  LYS   D HB2  1 
ATOM   22475 H  HB3  . LYS   D  4  213 ? 27.292  -71.140 -84.779  1.00 95.56  ? 213  LYS   D HB3  1 
ATOM   22476 H  HG2  . LYS   D  4  213 ? 28.198  -71.041 -82.112  1.00 97.20  ? 213  LYS   D HG2  1 
ATOM   22477 H  HG3  . LYS   D  4  213 ? 26.979  -71.923 -82.625  1.00 97.20  ? 213  LYS   D HG3  1 
ATOM   22478 H  HD2  . LYS   D  4  213 ? 28.571  -73.084 -84.016  1.00 105.76 ? 213  LYS   D HD2  1 
ATOM   22479 H  HD3  . LYS   D  4  213 ? 29.706  -72.356 -83.175  1.00 105.76 ? 213  LYS   D HD3  1 
ATOM   22480 H  HE2  . LYS   D  4  213 ? 28.732  -73.366 -81.218  1.00 110.14 ? 213  LYS   D HE2  1 
ATOM   22481 H  HE3  . LYS   D  4  213 ? 27.875  -74.264 -82.209  1.00 110.14 ? 213  LYS   D HE3  1 
ATOM   22482 H  HZ1  . LYS   D  4  213 ? 29.750  -75.364 -81.543  1.00 116.57 ? 213  LYS   D HZ1  1 
ATOM   22483 H  HZ2  . LYS   D  4  213 ? 29.816  -75.158 -82.975  1.00 116.57 ? 213  LYS   D HZ2  1 
ATOM   22484 H  HZ3  . LYS   D  4  213 ? 30.606  -74.329 -82.087  1.00 116.57 ? 213  LYS   D HZ3  1 
ATOM   22485 N  N    . LYS   D  4  214 ? 29.060  -69.811 -86.964  1.00 85.71  ? 214  LYS   D N    1 
ATOM   22486 C  CA   . LYS   D  4  214 ? 28.894  -69.207 -88.276  1.00 90.71  ? 214  LYS   D CA   1 
ATOM   22487 C  C    . LYS   D  4  214 ? 27.760  -69.897 -89.026  1.00 93.18  ? 214  LYS   D C    1 
ATOM   22488 O  O    . LYS   D  4  214 ? 27.449  -71.066 -88.779  1.00 94.65  ? 214  LYS   D O    1 
ATOM   22489 C  CB   . LYS   D  4  214 ? 30.191  -69.294 -89.088  1.00 96.39  ? 214  LYS   D CB   1 
ATOM   22490 C  CG   . LYS   D  4  214 ? 30.234  -68.353 -90.284  1.00 101.42 ? 214  LYS   D CG   1 
ATOM   22491 C  CD   . LYS   D  4  214 ? 31.543  -68.462 -91.059  1.00 108.86 ? 214  LYS   D CD   1 
ATOM   22492 C  CE   . LYS   D  4  214 ? 32.696  -67.782 -90.332  1.00 111.98 ? 214  LYS   D CE   1 
ATOM   22493 N  NZ   . LYS   D  4  214 ? 33.732  -67.275 -91.279  1.00 119.25 ? 214  LYS   D NZ   1 
ATOM   22494 H  H    . LYS   D  4  214 ? 29.406  -70.598 -86.994  1.00 102.83 ? 214  LYS   D H    1 
ATOM   22495 H  HA   . LYS   D  4  214 ? 28.663  -68.270 -88.179  1.00 108.84 ? 214  LYS   D HA   1 
ATOM   22496 H  HB2  . LYS   D  4  214 ? 30.936  -69.070 -88.509  1.00 115.65 ? 214  LYS   D HB2  1 
ATOM   22497 H  HB3  . LYS   D  4  214 ? 30.291  -70.199 -89.421  1.00 115.65 ? 214  LYS   D HB3  1 
ATOM   22498 H  HG2  . LYS   D  4  214 ? 29.507  -68.572 -90.888  1.00 121.68 ? 214  LYS   D HG2  1 
ATOM   22499 H  HG3  . LYS   D  4  214 ? 30.143  -67.439 -89.973  1.00 121.68 ? 214  LYS   D HG3  1 
ATOM   22500 H  HD2  . LYS   D  4  214 ? 31.768  -69.398 -91.176  1.00 130.62 ? 214  LYS   D HD2  1 
ATOM   22501 H  HD3  . LYS   D  4  214 ? 31.438  -68.036 -91.925  1.00 130.62 ? 214  LYS   D HD3  1 
ATOM   22502 H  HE2  . LYS   D  4  214 ? 32.354  -67.029 -89.825  1.00 134.35 ? 214  LYS   D HE2  1 
ATOM   22503 H  HE3  . LYS   D  4  214 ? 33.117  -68.420 -89.736  1.00 134.35 ? 214  LYS   D HE3  1 
ATOM   22504 H  HZ1  . LYS   D  4  214 ? 34.313  -66.757 -90.847  1.00 143.09 ? 214  LYS   D HZ1  1 
ATOM   22505 H  HZ2  . LYS   D  4  214 ? 34.171  -67.957 -91.644  1.00 143.09 ? 214  LYS   D HZ2  1 
ATOM   22506 H  HZ3  . LYS   D  4  214 ? 33.347  -66.800 -91.926  1.00 143.09 ? 214  LYS   D HZ3  1 
ATOM   22507 N  N    . ILE   D  4  215 ? 27.144  -69.157 -89.947  1.00 94.00  ? 215  ILE   D N    1 
ATOM   22508 C  CA   . ILE   D  4  215 ? 25.971  -69.627 -90.679  1.00 93.80  ? 215  ILE   D CA   1 
ATOM   22509 C  C    . ILE   D  4  215 ? 26.340  -69.817 -92.144  1.00 97.93  ? 215  ILE   D C    1 
ATOM   22510 O  O    . ILE   D  4  215 ? 26.315  -68.865 -92.931  1.00 102.68 ? 215  ILE   D O    1 
ATOM   22511 C  CB   . ILE   D  4  215 ? 24.804  -68.637 -90.510  1.00 91.08  ? 215  ILE   D CB   1 
ATOM   22512 C  CG1  . ILE   D  4  215 ? 24.432  -68.520 -89.029  1.00 85.59  ? 215  ILE   D CG1  1 
ATOM   22513 C  CG2  . ILE   D  4  215 ? 23.606  -69.077 -91.324  1.00 93.72  ? 215  ILE   D CG2  1 
ATOM   22514 C  CD1  . ILE   D  4  215 ? 23.473  -67.405 -88.727  1.00 86.79  ? 215  ILE   D CD1  1 
ATOM   22515 H  H    . ILE   D  4  215 ? 27.391  -68.364 -90.170  1.00 112.78 ? 215  ILE   D H    1 
ATOM   22516 H  HA   . ILE   D  4  215 ? 25.691  -70.489 -90.334  1.00 112.54 ? 215  ILE   D HA   1 
ATOM   22517 H  HB   . ILE   D  4  215 ? 25.088  -67.768 -90.834  1.00 109.28 ? 215  ILE   D HB   1 
ATOM   22518 H  HG12 . ILE   D  4  215 ? 24.018  -69.350 -88.746  1.00 102.69 ? 215  ILE   D HG12 1 
ATOM   22519 H  HG13 . ILE   D  4  215 ? 25.240  -68.360 -88.517  1.00 102.69 ? 215  ILE   D HG13 1 
ATOM   22520 H  HG21 . ILE   D  4  215 ? 22.826  -68.579 -91.032  1.00 112.45 ? 215  ILE   D HG21 1 
ATOM   22521 H  HG22 . ILE   D  4  215 ? 23.779  -68.900 -92.262  1.00 112.45 ? 215  ILE   D HG22 1 
ATOM   22522 H  HG23 . ILE   D  4  215 ? 23.462  -70.026 -91.187  1.00 112.45 ? 215  ILE   D HG23 1 
ATOM   22523 H  HD11 . ILE   D  4  215 ? 23.606  -67.112 -87.812  1.00 104.12 ? 215  ILE   D HD11 1 
ATOM   22524 H  HD12 . ILE   D  4  215 ? 23.640  -66.669 -89.337  1.00 104.12 ? 215  ILE   D HD12 1 
ATOM   22525 H  HD13 . ILE   D  4  215 ? 22.565  -67.729 -88.841  1.00 104.12 ? 215  ILE   D HD13 1 
ATOM   22526 N  N    . GLU   D  4  216 ? 26.718  -71.042 -92.513  1.00 97.89  ? 216  GLU   D N    1 
ATOM   22527 C  CA   . GLU   D  4  216 ? 27.288  -71.296 -93.832  1.00 106.55 ? 216  GLU   D CA   1 
ATOM   22528 C  C    . GLU   D  4  216 ? 26.265  -71.519 -94.943  1.00 114.48 ? 216  GLU   D C    1 
ATOM   22529 O  O    . GLU   D  4  216 ? 26.361  -70.867 -95.992  1.00 118.85 ? 216  GLU   D O    1 
ATOM   22530 C  CB   . GLU   D  4  216 ? 28.241  -72.493 -93.742  1.00 108.75 ? 216  GLU   D CB   1 
ATOM   22531 C  CG   . GLU   D  4  216 ? 29.640  -72.091 -93.309  1.00 111.81 ? 216  GLU   D CG   1 
ATOM   22532 C  CD   . GLU   D  4  216 ? 30.273  -73.078 -92.349  1.00 115.16 ? 216  GLU   D CD   1 
ATOM   22533 O  OE1  . GLU   D  4  216 ? 30.648  -74.186 -92.789  1.00 121.35 ? 216  GLU   D OE1  1 
ATOM   22534 O  OE2  . GLU   D  4  216 ? 30.392  -72.746 -91.151  1.00 112.48 ? 216  GLU   D OE2  1 
ATOM   22535 H  H    . GLU   D  4  216 ? 26.654  -71.741 -92.016  1.00 117.45 ? 216  GLU   D H    1 
ATOM   22536 H  HA   . GLU   D  4  216 ? 27.757  -70.490 -94.096  1.00 127.84 ? 216  GLU   D HA   1 
ATOM   22537 H  HB2  . GLU   D  4  216 ? 27.895  -73.125 -93.094  1.00 130.49 ? 216  GLU   D HB2  1 
ATOM   22538 H  HB3  . GLU   D  4  216 ? 28.304  -72.912 -94.614  1.00 130.49 ? 216  GLU   D HB3  1 
ATOM   22539 H  HG2  . GLU   D  4  216 ? 30.208  -72.032 -94.093  1.00 134.16 ? 216  GLU   D HG2  1 
ATOM   22540 H  HG3  . GLU   D  4  216 ? 29.597  -71.229 -92.865  1.00 134.16 ? 216  GLU   D HG3  1 
ATOM   22541 N  N    . PRO   D  4  217 ? 25.274  -72.415 -94.776  1.00 117.73 ? 217  PRO   D N    1 
ATOM   22542 C  CA   . PRO   D  4  217 ? 24.413  -72.695 -95.930  1.00 124.17 ? 217  PRO   D CA   1 
ATOM   22543 C  C    . PRO   D  4  217 ? 23.064  -71.980 -95.871  1.00 127.43 ? 217  PRO   D C    1 
ATOM   22544 O  O    . PRO   D  4  217 ? 22.022  -72.631 -95.950  1.00 131.95 ? 217  PRO   D O    1 
ATOM   22545 C  CB   . PRO   D  4  217 ? 24.235  -74.211 -95.845  1.00 123.77 ? 217  PRO   D CB   1 
ATOM   22546 C  CG   . PRO   D  4  217 ? 24.194  -74.475 -94.363  1.00 119.92 ? 217  PRO   D CG   1 
ATOM   22547 C  CD   . PRO   D  4  217 ? 25.018  -73.372 -93.684  1.00 115.53 ? 217  PRO   D CD   1 
ATOM   22548 H  HA   . PRO   D  4  217 ? 24.854  -72.454 -96.759  1.00 148.98 ? 217  PRO   D HA   1 
ATOM   22549 H  HB2  . PRO   D  4  217 ? 23.406  -74.478 -96.274  1.00 148.51 ? 217  PRO   D HB2  1 
ATOM   22550 H  HB3  . PRO   D  4  217 ? 24.985  -74.662 -96.264  1.00 148.51 ? 217  PRO   D HB3  1 
ATOM   22551 H  HG2  . PRO   D  4  217 ? 23.275  -74.447 -94.056  1.00 143.88 ? 217  PRO   D HG2  1 
ATOM   22552 H  HG3  . PRO   D  4  217 ? 24.579  -75.346 -94.180  1.00 143.88 ? 217  PRO   D HG3  1 
ATOM   22553 H  HD2  . PRO   D  4  217 ? 24.512  -72.954 -92.970  1.00 138.61 ? 217  PRO   D HD2  1 
ATOM   22554 H  HD3  . PRO   D  4  217 ? 25.851  -73.729 -93.336  1.00 138.61 ? 217  PRO   D HD3  1 
HETATM 22555 C  C1   . NAG   E  5  .   ? -4.994  -14.895 -25.483  1.00 53.07  ? 1    NAG   I C1   1 
HETATM 22556 C  C2   . NAG   E  5  .   ? -4.632  -14.375 -24.097  1.00 64.21  ? 1    NAG   I C2   1 
HETATM 22557 C  C3   . NAG   E  5  .   ? -5.119  -15.350 -23.028  1.00 67.26  ? 1    NAG   I C3   1 
HETATM 22558 C  C4   . NAG   E  5  .   ? -6.586  -15.710 -23.234  1.00 73.82  ? 1    NAG   I C4   1 
HETATM 22559 C  C5   . NAG   E  5  .   ? -6.863  -16.104 -24.683  1.00 71.81  ? 1    NAG   I C5   1 
HETATM 22560 C  C6   . NAG   E  5  .   ? -8.334  -16.286 -24.982  1.00 78.21  ? 1    NAG   I C6   1 
HETATM 22561 C  C7   . NAG   E  5  .   ? -2.600  -12.997 -24.199  1.00 75.67  ? 1    NAG   I C7   1 
HETATM 22562 C  C8   . NAG   E  5  .   ? -1.111  -12.976 -24.028  1.00 76.29  ? 1    NAG   I C8   1 
HETATM 22563 N  N2   . NAG   E  5  .   ? -3.198  -14.172 -23.979  1.00 70.44  ? 1    NAG   I N2   1 
HETATM 22564 O  O3   . NAG   E  5  .   ? -4.936  -14.769 -21.742  1.00 64.55  ? 1    NAG   I O3   1 
HETATM 22565 O  O4   . NAG   E  5  .   ? -6.900  -16.824 -22.405  1.00 83.96  ? 1    NAG   I O4   1 
HETATM 22566 O  O5   . NAG   E  5  .   ? -6.390  -15.082 -25.569  1.00 62.02  ? 1    NAG   I O5   1 
HETATM 22567 O  O6   . NAG   E  5  .   ? -8.584  -16.239 -26.380  1.00 83.37  ? 1    NAG   I O6   1 
HETATM 22568 O  O7   . NAG   E  5  .   ? -3.232  -11.996 -24.521  1.00 80.23  ? 1    NAG   I O7   1 
HETATM 22569 H  H4   . NAG   E  5  .   ? -7.137  -14.936 -23.010  1.00 88.56  ? 1    NAG   I H4   1 
HETATM 22570 H  H5   . NAG   E  5  .   ? -6.392  -16.936 -24.876  1.00 86.15  ? 1    NAG   I H5   1 
HETATM 22571 H  H61  . NAG   E  5  .   ? -8.840  -15.577 -24.542  1.00 93.84  ? 1    NAG   I H61  1 
HETATM 22572 H  H62  . NAG   E  5  .   ? -8.626  -17.150 -24.634  1.00 93.84  ? 1    NAG   I H62  1 
HETATM 22573 H  H81  . NAG   E  5  .   ? -0.775  -12.079 -24.211  1.00 91.53  ? 1    NAG   I H81  1 
HETATM 22574 H  H82  . NAG   E  5  .   ? -0.704  -13.609 -24.649  1.00 91.53  ? 1    NAG   I H82  1 
HETATM 22575 H  H83  . NAG   E  5  .   ? -0.885  -13.227 -23.112  1.00 91.53  ? 1    NAG   I H83  1 
HETATM 22576 H  HN2  . NAG   E  5  .   ? -2.678  -14.884 -23.742  1.00 84.51  ? 1    NAG   I HN2  1 
HETATM 22577 H  HO6  . NAG   E  5  .   ? -7.889  -15.869 -26.791  1.00 100.02 ? 1    NAG   I HO6  1 
HETATM 22578 C  C1   . NAG   E  5  .   ? -8.109  -16.603 -21.662  1.00 94.24  ? 2    NAG   I C1   1 
HETATM 22579 C  C2   . NAG   E  5  .   ? -8.565  -17.940 -21.112  1.00 99.56  ? 2    NAG   I C2   1 
HETATM 22580 C  C3   . NAG   E  5  .   ? -9.412  -17.723 -19.874  1.00 101.02 ? 2    NAG   I C3   1 
HETATM 22581 C  C4   . NAG   E  5  .   ? -8.525  -17.211 -18.751  1.00 105.93 ? 2    NAG   I C4   1 
HETATM 22582 C  C5   . NAG   E  5  .   ? -7.553  -16.148 -19.269  1.00 101.94 ? 2    NAG   I C5   1 
HETATM 22583 C  C6   . NAG   E  5  .   ? -6.130  -16.650 -19.396  1.00 99.48  ? 2    NAG   I C6   1 
HETATM 22584 C  C7   . NAG   E  5  .   ? -8.747  -19.709 -22.802  1.00 101.25 ? 2    NAG   I C7   1 
HETATM 22585 C  C8   . NAG   E  5  .   ? -7.312  -20.013 -22.493  1.00 98.10  ? 2    NAG   I C8   1 
HETATM 22586 N  N2   . NAG   E  5  .   ? -9.296  -18.705 -22.110  1.00 102.23 ? 2    NAG   I N2   1 
HETATM 22587 O  O3   . NAG   E  5  .   ? -10.023 -18.950 -19.493  1.00 99.09  ? 2    NAG   I O3   1 
HETATM 22588 O  O4   . NAG   E  5  .   ? -9.317  -16.660 -17.705  1.00 114.51 ? 2    NAG   I O4   1 
HETATM 22589 O  O5   . NAG   E  5  .   ? -7.941  -15.643 -20.563  1.00 99.90  ? 2    NAG   I O5   1 
HETATM 22590 O  O6   . NAG   E  5  .   ? -5.207  -15.736 -18.821  1.00 97.29  ? 2    NAG   I O6   1 
HETATM 22591 O  O7   . NAG   E  5  .   ? -9.380  -20.343 -23.640  1.00 102.69 ? 2    NAG   I O7   1 
HETATM 22592 H  H4   . NAG   E  5  .   ? -8.010  -17.960 -18.397  1.00 127.09 ? 2    NAG   I H4   1 
HETATM 22593 H  H5   . NAG   E  5  .   ? -7.580  -15.397 -18.646  1.00 122.31 ? 2    NAG   I H5   1 
HETATM 22594 H  H61  . NAG   E  5  .   ? -5.916  -16.768 -20.341  1.00 119.36 ? 2    NAG   I H61  1 
HETATM 22595 H  H62  . NAG   E  5  .   ? -6.053  -17.510 -18.942  1.00 119.36 ? 2    NAG   I H62  1 
HETATM 22596 H  H81  . NAG   E  5  .   ? -7.013  -20.764 -23.040  1.00 117.70 ? 2    NAG   I H81  1 
HETATM 22597 H  H82  . NAG   E  5  .   ? -7.224  -20.244 -21.548  1.00 117.70 ? 2    NAG   I H82  1 
HETATM 22598 H  H83  . NAG   E  5  .   ? -6.763  -19.230 -22.689  1.00 117.70 ? 2    NAG   I H83  1 
HETATM 22599 H  HN2  . NAG   E  5  .   ? -10.167 -18.489 -22.271  1.00 122.66 ? 2    NAG   I HN2  1 
HETATM 22600 H  HO6  . NAG   E  5  .   ? -4.933  -15.164 -19.444  1.00 116.73 ? 2    NAG   I HO6  1 
HETATM 22601 C  C1   . BMA   E  5  .   ? -8.891  -17.312 -16.489  1.00 120.04 ? 3    BMA   I C1   1 
HETATM 22602 C  C2   . BMA   E  5  .   ? -9.386  -16.501 -15.276  1.00 121.69 ? 3    BMA   I C2   1 
HETATM 22603 C  C3   . BMA   E  5  .   ? -8.969  -17.223 -13.995  1.00 121.70 ? 3    BMA   I C3   1 
HETATM 22604 C  C4   . BMA   E  5  .   ? -9.362  -18.717 -14.019  1.00 122.67 ? 3    BMA   I C4   1 
HETATM 22605 C  C5   . BMA   E  5  .   ? -8.921  -19.394 -15.334  1.00 123.98 ? 3    BMA   I C5   1 
HETATM 22606 C  C6   . BMA   E  5  .   ? -9.474  -20.800 -15.482  1.00 125.66 ? 3    BMA   I C6   1 
HETATM 22607 O  O2   . BMA   E  5  .   ? -10.802 -16.429 -15.265  1.00 121.79 ? 3    BMA   I O2   1 
HETATM 22608 O  O3   . BMA   E  5  .   ? -9.519  -16.598 -12.837  1.00 120.61 ? 3    BMA   I O3   1 
HETATM 22609 O  O4   . BMA   E  5  .   ? -8.748  -19.386 -12.925  1.00 121.98 ? 3    BMA   I O4   1 
HETATM 22610 O  O5   . BMA   E  5  .   ? -9.413  -18.628 -16.438  1.00 123.08 ? 3    BMA   I O5   1 
HETATM 22611 O  O6   . BMA   E  5  .   ? -10.845 -20.695 -15.849  1.00 126.60 ? 3    BMA   I O6   1 
HETATM 22612 H  H4   . BMA   E  5  .   ? -10.462 -18.769 -13.984  1.00 147.18 ? 3    BMA   I H4   1 
HETATM 22613 H  H5   . BMA   E  5  .   ? -7.819  -19.429 -15.363  1.00 148.76 ? 3    BMA   I H5   1 
HETATM 22614 H  H61  . BMA   E  5  .   ? -9.348  -21.327 -14.524  1.00 150.77 ? 3    BMA   I H61  1 
HETATM 22615 H  H62  . BMA   E  5  .   ? -8.886  -21.327 -16.249  1.00 150.77 ? 3    BMA   I H62  1 
HETATM 22616 H  HO4  . BMA   E  5  .   ? -9.293  -20.171 -12.759  1.00 146.36 ? 3    BMA   I HO4  1 
HETATM 22617 H  HO6  . BMA   E  5  .   ? -10.928 -19.951 -16.458  1.00 151.90 ? 3    BMA   I HO6  1 
HETATM 22618 C  C1   . NAG   F  6  .   ? 34.989  -35.875 -40.003  1.00 75.93  ? 1    NAG   E C1   1 
HETATM 22619 C  C2   . NAG   F  6  .   ? 35.888  -37.092 -40.233  1.00 84.15  ? 1    NAG   E C2   1 
HETATM 22620 C  C3   . NAG   F  6  .   ? 37.301  -36.811 -39.728  1.00 91.92  ? 1    NAG   E C3   1 
HETATM 22621 C  C4   . NAG   F  6  .   ? 37.843  -35.540 -40.366  1.00 96.93  ? 1    NAG   E C4   1 
HETATM 22622 C  C5   . NAG   F  6  .   ? 36.883  -34.384 -40.102  1.00 91.09  ? 1    NAG   E C5   1 
HETATM 22623 C  C6   . NAG   F  6  .   ? 37.301  -33.102 -40.782  1.00 89.52  ? 1    NAG   E C6   1 
HETATM 22624 C  C7   . NAG   F  6  .   ? 34.516  -39.127 -40.215  1.00 85.69  ? 1    NAG   E C7   1 
HETATM 22625 C  C8   . NAG   F  6  .   ? 34.043  -40.298 -39.404  1.00 87.17  ? 1    NAG   E C8   1 
HETATM 22626 N  N2   . NAG   F  6  .   ? 35.339  -38.276 -39.592  1.00 84.48  ? 1    NAG   E N2   1 
HETATM 22627 O  O3   . NAG   F  6  .   ? 38.151  -37.909 -40.039  1.00 94.10  ? 1    NAG   E O3   1 
HETATM 22628 O  O4   . NAG   F  6  .   ? 39.128  -35.227 -39.839  1.00 105.68 ? 1    NAG   E O4   1 
HETATM 22629 O  O5   . NAG   F  6  .   ? 35.581  -34.714 -40.608  1.00 84.67  ? 1    NAG   E O5   1 
HETATM 22630 O  O6   . NAG   F  6  .   ? 37.054  -33.158 -42.180  1.00 89.81  ? 1    NAG   E O6   1 
HETATM 22631 O  O7   . NAG   F  6  .   ? 34.168  -38.960 -41.379  1.00 85.63  ? 1    NAG   E O7   1 
HETATM 22632 H  H4   . NAG   F  6  .   ? 37.931  -35.673 -41.328  1.00 116.29 ? 1    NAG   E H4   1 
HETATM 22633 H  H5   . NAG   F  6  .   ? 36.825  -34.231 -39.140  1.00 109.29 ? 1    NAG   E H5   1 
HETATM 22634 H  H61  . NAG   F  6  .   ? 38.254  -32.955 -40.631  1.00 107.41 ? 1    NAG   E H61  1 
HETATM 22635 H  H62  . NAG   F  6  .   ? 36.798  -32.359 -40.399  1.00 107.41 ? 1    NAG   E H62  1 
HETATM 22636 H  H81  . NAG   F  6  .   ? 33.463  -40.860 -39.952  1.00 104.58 ? 1    NAG   E H81  1 
HETATM 22637 H  H82  . NAG   F  6  .   ? 33.547  -39.977 -38.628  1.00 104.58 ? 1    NAG   E H82  1 
HETATM 22638 H  H83  . NAG   F  6  .   ? 34.813  -40.818 -39.106  1.00 104.58 ? 1    NAG   E H83  1 
HETATM 22639 H  HN2  . NAG   F  6  .   ? 35.567  -38.447 -38.726  1.00 101.36 ? 1    NAG   E HN2  1 
HETATM 22640 H  HO6  . NAG   F  6  .   ? 36.305  -33.610 -42.331  1.00 107.75 ? 1    NAG   E HO6  1 
HETATM 22641 C  C1   . NAG   F  6  .   ? 40.090  -35.292 -40.916  1.00 111.44 ? 2    NAG   E C1   1 
HETATM 22642 C  C2   . NAG   F  6  .   ? 41.296  -34.421 -40.555  1.00 111.53 ? 2    NAG   E C2   1 
HETATM 22643 C  C3   . NAG   F  6  .   ? 42.354  -34.508 -41.652  1.00 113.13 ? 2    NAG   E C3   1 
HETATM 22644 C  C4   . NAG   F  6  .   ? 42.714  -35.961 -41.932  1.00 118.02 ? 2    NAG   E C4   1 
HETATM 22645 C  C5   . NAG   F  6  .   ? 41.455  -36.773 -42.224  1.00 116.67 ? 2    NAG   E C5   1 
HETATM 22646 C  C6   . NAG   F  6  .   ? 41.728  -38.250 -42.385  1.00 115.61 ? 2    NAG   E C6   1 
HETATM 22647 C  C7   . NAG   F  6  .   ? 40.702  -32.511 -39.127  1.00 107.18 ? 2    NAG   E C7   1 
HETATM 22648 C  C8   . NAG   F  6  .   ? 40.927  -33.430 -37.963  1.00 107.23 ? 2    NAG   E C8   1 
HETATM 22649 N  N2   . NAG   F  6  .   ? 40.893  -33.040 -40.341  1.00 108.92 ? 2    NAG   E N2   1 
HETATM 22650 O  O3   . NAG   F  6  .   ? 43.514  -33.788 -41.250  1.00 110.37 ? 2    NAG   E O3   1 
HETATM 22651 O  O4   . NAG   F  6  .   ? 43.592  -36.039 -43.051  1.00 122.97 ? 2    NAG   E O4   1 
HETATM 22652 O  O5   . NAG   F  6  .   ? 40.524  -36.642 -41.139  1.00 115.33 ? 2    NAG   E O5   1 
HETATM 22653 O  O6   . NAG   F  6  .   ? 41.528  -38.951 -41.165  1.00 114.75 ? 2    NAG   E O6   1 
HETATM 22654 O  O7   . NAG   F  6  .   ? 40.363  -31.341 -38.975  1.00 105.86 ? 2    NAG   E O7   1 
HETATM 22655 H  H4   . NAG   F  6  .   ? 43.160  -36.335 -41.148  1.00 141.61 ? 2    NAG   E H4   1 
HETATM 22656 H  H5   . NAG   F  6  .   ? 41.041  -36.431 -43.039  1.00 139.98 ? 2    NAG   E H5   1 
HETATM 22657 H  H61  . NAG   F  6  .   ? 42.652  -38.373 -42.675  1.00 138.71 ? 2    NAG   E H61  1 
HETATM 22658 H  H62  . NAG   F  6  .   ? 41.128  -38.613 -43.063  1.00 138.71 ? 2    NAG   E H62  1 
HETATM 22659 H  H81  . NAG   F  6  .   ? 40.745  -32.953 -37.132  1.00 128.66 ? 2    NAG   E H81  1 
HETATM 22660 H  H82  . NAG   F  6  .   ? 41.854  -33.737 -37.966  1.00 128.66 ? 2    NAG   E H82  1 
HETATM 22661 H  H83  . NAG   F  6  .   ? 40.330  -34.198 -38.035  1.00 128.66 ? 2    NAG   E H83  1 
HETATM 22662 H  HN2  . NAG   F  6  .   ? 40.764  -32.509 -41.070  1.00 130.68 ? 2    NAG   E HN2  1 
HETATM 22663 H  HO6  . NAG   F  6  .   ? 41.070  -38.440 -40.601  1.00 137.68 ? 2    NAG   E HO6  1 
HETATM 22664 C  C1   . BMA   F  6  .   ? 44.817  -36.680 -42.630  1.00 126.94 ? 3    BMA   E C1   1 
HETATM 22665 C  C2   . BMA   F  6  .   ? 45.449  -37.403 -43.837  1.00 127.30 ? 3    BMA   E C2   1 
HETATM 22666 C  C3   . BMA   F  6  .   ? 46.744  -38.070 -43.381  1.00 126.46 ? 3    BMA   E C3   1 
HETATM 22667 C  C4   . BMA   F  6  .   ? 47.674  -37.077 -42.654  1.00 130.36 ? 3    BMA   E C4   1 
HETATM 22668 C  C5   . BMA   F  6  .   ? 46.910  -36.325 -41.542  1.00 130.88 ? 3    BMA   E C5   1 
HETATM 22669 C  C6   . BMA   F  6  .   ? 47.721  -35.206 -40.899  1.00 131.38 ? 3    BMA   E C6   1 
HETATM 22670 O  O2   . BMA   F  6  .   ? 45.802  -36.478 -44.857  1.00 127.76 ? 3    BMA   E O2   1 
HETATM 22671 O  O3   . BMA   F  6  .   ? 47.432  -38.669 -44.469  1.00 122.10 ? 3    BMA   E O3   1 
HETATM 22672 O  O4   . BMA   F  6  .   ? 48.767  -37.785 -42.080  1.00 131.85 ? 3    BMA   E O4   1 
HETATM 22673 O  O5   . BMA   F  6  .   ? 45.733  -35.730 -42.109  1.00 129.23 ? 3    BMA   E O5   1 
HETATM 22674 O  O6   . BMA   F  6  .   ? 46.913  -34.024 -40.879  1.00 132.19 ? 3    BMA   E O6   1 
HETATM 22675 H  H4   . BMA   F  6  .   ? 48.007  -36.324 -43.387  1.00 156.41 ? 3    BMA   E H4   1 
HETATM 22676 H  H5   . BMA   F  6  .   ? 46.628  -37.051 -40.761  1.00 157.04 ? 3    BMA   E H5   1 
HETATM 22677 H  H61  . BMA   F  6  .   ? 48.640  -35.061 -41.488  1.00 157.64 ? 3    BMA   E H61  1 
HETATM 22678 H  H62  . BMA   F  6  .   ? 48.005  -35.522 -39.884  1.00 157.64 ? 3    BMA   E H62  1 
HETATM 22679 H  HO4  . BMA   F  6  .   ? 49.361  -37.104 -41.726  1.00 158.21 ? 3    BMA   E HO4  1 
HETATM 22680 C  C1   . MAN   F  6  .   ? 47.692  -32.931 -40.339  1.00 134.22 ? 4    MAN   E C1   1 
HETATM 22681 C  C2   . MAN   F  6  .   ? 46.991  -32.432 -39.040  1.00 135.36 ? 4    MAN   E C2   1 
HETATM 22682 C  C3   . MAN   F  6  .   ? 45.710  -31.666 -39.362  1.00 135.75 ? 4    MAN   E C3   1 
HETATM 22683 C  C4   . MAN   F  6  .   ? 45.921  -30.629 -40.472  1.00 135.79 ? 4    MAN   E C4   1 
HETATM 22684 C  C5   . MAN   F  6  .   ? 46.605  -31.246 -41.698  1.00 137.86 ? 4    MAN   E C5   1 
HETATM 22685 C  C6   . MAN   F  6  .   ? 46.960  -30.200 -42.753  1.00 142.63 ? 4    MAN   E C6   1 
HETATM 22686 O  O2   . MAN   F  6  .   ? 47.819  -31.511 -38.326  1.00 135.89 ? 4    MAN   E O2   1 
HETATM 22687 O  O3   . MAN   F  6  .   ? 45.216  -30.986 -38.214  1.00 135.72 ? 4    MAN   E O3   1 
HETATM 22688 O  O4   . MAN   F  6  .   ? 44.661  -30.101 -40.865  1.00 134.42 ? 4    MAN   E O4   1 
HETATM 22689 O  O5   . MAN   F  6  .   ? 47.828  -31.881 -41.292  1.00 135.61 ? 4    MAN   E O5   1 
HETATM 22690 O  O6   . MAN   F  6  .   ? 47.056  -28.921 -42.114  1.00 145.93 ? 4    MAN   E O6   1 
HETATM 22691 H  H3   . MAN   F  6  .   ? 44.962  -32.393 -39.697  1.00 162.89 ? 4    MAN   E H3   1 
HETATM 22692 H  H4   . MAN   F  6  .   ? 46.603  -29.858 -40.077  1.00 162.93 ? 4    MAN   E H4   1 
HETATM 22693 H  H5   . MAN   F  6  .   ? 45.936  -31.995 -42.143  1.00 165.41 ? 4    MAN   E H5   1 
HETATM 22694 H  H61  . MAN   F  6  .   ? 46.175  -30.206 -43.526  1.00 171.14 ? 4    MAN   E H61  1 
HETATM 22695 H  H62  . MAN   F  6  .   ? 47.913  -30.488 -43.222  1.00 171.14 ? 4    MAN   E H62  1 
HETATM 22696 H  HO4  . MAN   F  6  .   ? 44.508  -30.440 -41.763  1.00 161.29 ? 4    MAN   E HO4  1 
HETATM 22697 C  C1   . MAN   F  6  .   ? 44.079  -31.659 -37.647  1.00 135.40 ? 5    MAN   E C1   1 
HETATM 22698 C  C2   . MAN   F  6  .   ? 43.270  -30.592 -36.902  1.00 133.92 ? 5    MAN   E C2   1 
HETATM 22699 C  C3   . MAN   F  6  .   ? 44.133  -30.006 -35.788  1.00 132.22 ? 5    MAN   E C3   1 
HETATM 22700 C  C4   . MAN   F  6  .   ? 44.729  -31.119 -34.898  1.00 134.32 ? 5    MAN   E C4   1 
HETATM 22701 C  C5   . MAN   F  6  .   ? 45.419  -32.199 -35.759  1.00 136.85 ? 5    MAN   E C5   1 
HETATM 22702 C  C6   . MAN   F  6  .   ? 45.850  -33.419 -34.962  1.00 139.29 ? 5    MAN   E C6   1 
HETATM 22703 O  O2   . MAN   F  6  .   ? 42.129  -31.155 -36.249  1.00 134.06 ? 5    MAN   E O2   1 
HETATM 22704 O  O3   . MAN   F  6  .   ? 43.404  -29.072 -34.994  1.00 129.25 ? 5    MAN   E O3   1 
HETATM 22705 O  O4   . MAN   F  6  .   ? 45.685  -30.551 -34.015  1.00 133.87 ? 5    MAN   E O4   1 
HETATM 22706 O  O5   . MAN   F  6  .   ? 44.508  -32.658 -36.774  1.00 136.30 ? 5    MAN   E O5   1 
HETATM 22707 O  O6   . MAN   F  6  .   ? 44.686  -34.033 -34.420  1.00 140.91 ? 5    MAN   E O6   1 
HETATM 22708 H  H3   . MAN   F  6  .   ? 44.964  -29.454 -36.239  1.00 158.64 ? 5    MAN   E H3   1 
HETATM 22709 H  H4   . MAN   F  6  .   ? 43.898  -31.606 -34.360  1.00 161.17 ? 5    MAN   E H4   1 
HETATM 22710 H  H5   . MAN   F  6  .   ? 46.306  -31.751 -36.226  1.00 164.20 ? 5    MAN   E H5   1 
HETATM 22711 H  H61  . MAN   F  6  .   ? 46.540  -33.092 -34.169  1.00 167.13 ? 5    MAN   E H61  1 
HETATM 22712 H  H62  . MAN   F  6  .   ? 46.391  -34.102 -35.635  1.00 167.13 ? 5    MAN   E H62  1 
HETATM 22713 H  HO3  . MAN   F  6  .   ? 42.579  -29.525 -34.752  1.00 155.08 ? 5    MAN   E HO3  1 
HETATM 22714 H  HO4  . MAN   F  6  .   ? 45.880  -31.242 -33.364  1.00 160.62 ? 5    MAN   E HO4  1 
HETATM 22715 H  HO6  . MAN   F  6  .   ? 43.998  -34.000 -35.096  1.00 169.07 ? 5    MAN   E HO6  1 
HETATM 22716 C  C1   . MAN   F  6  .   ? 46.465  -27.906 -42.949  1.00 147.30 ? 6    MAN   E C1   1 
HETATM 22717 C  C2   . MAN   F  6  .   ? 47.254  -26.574 -42.729  1.00 144.68 ? 6    MAN   E C2   1 
HETATM 22718 C  C3   . MAN   F  6  .   ? 46.844  -25.902 -41.415  1.00 142.29 ? 6    MAN   E C3   1 
HETATM 22719 C  C4   . MAN   F  6  .   ? 45.321  -25.785 -41.317  1.00 142.54 ? 6    MAN   E C4   1 
HETATM 22720 C  C5   . MAN   F  6  .   ? 44.707  -27.183 -41.415  1.00 146.26 ? 6    MAN   E C5   1 
HETATM 22721 C  C6   . MAN   F  6  .   ? 43.188  -27.174 -41.335  1.00 144.45 ? 6    MAN   E C6   1 
HETATM 22722 O  O2   . MAN   F  6  .   ? 46.973  -25.616 -43.752  1.00 144.34 ? 6    MAN   E O2   1 
HETATM 22723 O  O3   . MAN   F  6  .   ? 47.446  -24.618 -41.263  1.00 140.41 ? 6    MAN   E O3   1 
HETATM 22724 O  O4   . MAN   F  6  .   ? 44.957  -25.195 -40.077  1.00 139.44 ? 6    MAN   E O4   1 
HETATM 22725 O  O5   . MAN   F  6  .   ? 45.069  -27.769 -42.692  1.00 149.18 ? 6    MAN   E O5   1 
HETATM 22726 O  O6   . MAN   F  6  .   ? 42.799  -27.858 -40.148  1.00 142.70 ? 6    MAN   E O6   1 
HETATM 22727 H  H3   . MAN   F  6  .   ? 47.199  -26.513 -40.579  1.00 170.72 ? 6    MAN   E H3   1 
HETATM 22728 H  H4   . MAN   F  6  .   ? 44.955  -25.180 -42.163  1.00 171.03 ? 6    MAN   E H4   1 
HETATM 22729 H  H5   . MAN   F  6  .   ? 45.099  -27.799 -40.595  1.00 175.49 ? 6    MAN   E H5   1 
HETATM 22730 H  H61  . MAN   F  6  .   ? 42.788  -27.666 -42.234  1.00 173.32 ? 6    MAN   E H61  1 
HETATM 22731 H  H62  . MAN   F  6  .   ? 42.846  -26.127 -41.328  1.00 173.32 ? 6    MAN   E H62  1 
HETATM 22732 H  HO3  . MAN   F  6  .   ? 47.470  -24.234 -42.155  1.00 168.47 ? 6    MAN   E HO3  1 
HETATM 22733 H  HO4  . MAN   F  6  .   ? 45.573  -24.455 -39.954  1.00 167.31 ? 6    MAN   E HO4  1 
HETATM 22734 H  HO6  . MAN   F  6  .   ? 43.166  -28.750 -40.192  1.00 171.22 ? 6    MAN   E HO6  1 
HETATM 22735 C  C1   . NAG   G  7  .   ? 31.771  -37.636 -25.590  1.00 43.32  ? 1    NAG   F C1   1 
HETATM 22736 C  C2   . NAG   G  7  .   ? 32.512  -38.764 -26.299  1.00 54.59  ? 1    NAG   F C2   1 
HETATM 22737 C  C3   . NAG   G  7  .   ? 31.526  -39.635 -27.071  1.00 59.20  ? 1    NAG   F C3   1 
HETATM 22738 C  C4   . NAG   G  7  .   ? 30.383  -40.095 -26.175  1.00 57.90  ? 1    NAG   F C4   1 
HETATM 22739 C  C5   . NAG   G  7  .   ? 29.769  -38.927 -25.408  1.00 60.41  ? 1    NAG   F C5   1 
HETATM 22740 C  C6   . NAG   G  7  .   ? 28.787  -39.372 -24.348  1.00 66.77  ? 1    NAG   F C6   1 
HETATM 22741 C  C7   . NAG   G  7  .   ? 34.729  -37.816 -26.775  1.00 71.27  ? 1    NAG   F C7   1 
HETATM 22742 C  C8   . NAG   G  7  .   ? 35.661  -37.325 -27.841  1.00 73.76  ? 1    NAG   F C8   1 
HETATM 22743 N  N2   . NAG   G  7  .   ? 33.535  -38.245 -27.194  1.00 65.98  ? 1    NAG   F N2   1 
HETATM 22744 O  O3   . NAG   G  7  .   ? 32.210  -40.766 -27.598  1.00 65.72  ? 1    NAG   F O3   1 
HETATM 22745 O  O4   . NAG   G  7  .   ? 29.358  -40.663 -26.984  1.00 58.13  ? 1    NAG   F O4   1 
HETATM 22746 O  O5   . NAG   G  7  .   ? 30.789  -38.184 -24.727  1.00 52.92  ? 1    NAG   F O5   1 
HETATM 22747 O  O6   . NAG   G  7  .   ? 29.422  -40.165 -23.354  1.00 70.67  ? 1    NAG   F O6   1 
HETATM 22748 O  O7   . NAG   G  7  .   ? 35.042  -37.818 -25.589  1.00 71.53  ? 1    NAG   F O7   1 
HETATM 22749 H  H4   . NAG   G  7  .   ? 30.734  -40.746 -25.538  1.00 69.46  ? 1    NAG   F H4   1 
HETATM 22750 H  H5   . NAG   G  7  .   ? 29.322  -38.336 -26.043  1.00 72.48  ? 1    NAG   F H5   1 
HETATM 22751 H  H61  . NAG   G  7  .   ? 28.079  -39.896 -24.770  1.00 80.11  ? 1    NAG   F H61  1 
HETATM 22752 H  H62  . NAG   G  7  .   ? 28.394  -38.585 -23.926  1.00 80.11  ? 1    NAG   F H62  1 
HETATM 22753 H  H81  . NAG   G  7  .   ? 35.323  -36.486 -28.208  1.00 88.49  ? 1    NAG   F H81  1 
HETATM 22754 H  H82  . NAG   G  7  .   ? 35.720  -37.991 -28.553  1.00 88.49  ? 1    NAG   F H82  1 
HETATM 22755 H  H83  . NAG   G  7  .   ? 36.547  -37.180 -27.458  1.00 88.49  ? 1    NAG   F H83  1 
HETATM 22756 H  HN2  . NAG   G  7  .   ? 33.352  -38.212 -28.086  1.00 79.16  ? 1    NAG   F HN2  1 
HETATM 22757 H  HO6  . NAG   G  7  .   ? 28.999  -40.068 -22.579  1.00 84.79  ? 1    NAG   F HO6  1 
HETATM 22758 C  C1   . NAG   G  7  .   ? 29.236  -42.069 -26.736  1.00 57.99  ? 2    NAG   F C1   1 
HETATM 22759 C  C2   . NAG   G  7  .   ? 28.050  -42.570 -27.550  1.00 60.13  ? 2    NAG   F C2   1 
HETATM 22760 C  C3   . NAG   G  7  .   ? 27.892  -44.077 -27.384  1.00 59.39  ? 2    NAG   F C3   1 
HETATM 22761 C  C4   . NAG   G  7  .   ? 29.198  -44.783 -27.722  1.00 60.31  ? 2    NAG   F C4   1 
HETATM 22762 C  C5   . NAG   G  7  .   ? 30.347  -44.189 -26.912  1.00 58.15  ? 2    NAG   F C5   1 
HETATM 22763 C  C6   . NAG   G  7  .   ? 31.696  -44.746 -27.306  1.00 57.42  ? 2    NAG   F C6   1 
HETATM 22764 C  C7   . NAG   G  7  .   ? 26.330  -40.851 -27.866  1.00 68.88  ? 2    NAG   F C7   1 
HETATM 22765 C  C8   . NAG   G  7  .   ? 25.059  -40.254 -27.338  1.00 69.70  ? 2    NAG   F C8   1 
HETATM 22766 N  N2   . NAG   G  7  .   ? 26.826  -41.882 -27.174  1.00 63.75  ? 2    NAG   F N2   1 
HETATM 22767 O  O3   . NAG   G  7  .   ? 26.858  -44.540 -28.243  1.00 58.52  ? 2    NAG   F O3   1 
HETATM 22768 O  O4   . NAG   G  7  .   ? 29.085  -46.170 -27.429  1.00 64.05  ? 2    NAG   F O4   1 
HETATM 22769 O  O5   . NAG   G  7  .   ? 30.414  -42.771 -27.121  1.00 57.01  ? 2    NAG   F O5   1 
HETATM 22770 O  O6   . NAG   G  7  .   ? 31.970  -44.504 -28.680  1.00 58.70  ? 2    NAG   F O6   1 
HETATM 22771 O  O7   . NAG   G  7  .   ? 26.884  -40.416 -28.870  1.00 70.91  ? 2    NAG   F O7   1 
HETATM 22772 H  H4   . NAG   G  7  .   ? 29.388  -44.668 -28.673  1.00 72.36  ? 2    NAG   F H4   1 
HETATM 22773 H  H5   . NAG   G  7  .   ? 30.189  -44.364 -25.965  1.00 69.76  ? 2    NAG   F H5   1 
HETATM 22774 H  H61  . NAG   G  7  .   ? 31.705  -45.708 -27.143  1.00 68.88  ? 2    NAG   F H61  1 
HETATM 22775 H  H62  . NAG   G  7  .   ? 32.388  -44.323 -26.763  1.00 68.88  ? 2    NAG   F H62  1 
HETATM 22776 H  H81  . NAG   G  7  .   ? 25.261  -39.680 -26.576  1.00 83.62  ? 2    NAG   F H81  1 
HETATM 22777 H  H82  . NAG   G  7  .   ? 24.457  -40.969 -27.057  1.00 83.62  ? 2    NAG   F H82  1 
HETATM 22778 H  H83  . NAG   G  7  .   ? 24.632  -39.726 -28.039  1.00 83.62  ? 2    NAG   F H83  1 
HETATM 22779 H  HN2  . NAG   G  7  .   ? 26.377  -42.165 -26.432  1.00 76.48  ? 2    NAG   F HN2  1 
HETATM 22780 H  HO6  . NAG   G  7  .   ? 32.796  -44.765 -28.872  1.00 70.42  ? 2    NAG   F HO6  1 
HETATM 22781 C  C1   . BMA   G  7  .   ? 29.496  -46.934 -28.579  1.00 69.38  ? 3    BMA   F C1   1 
HETATM 22782 C  C2   . BMA   G  7  .   ? 30.324  -48.133 -28.053  1.00 76.46  ? 3    BMA   F C2   1 
HETATM 22783 C  C3   . BMA   G  7  .   ? 30.557  -49.177 -29.151  1.00 81.77  ? 3    BMA   F C3   1 
HETATM 22784 C  C4   . BMA   G  7  .   ? 29.274  -49.472 -29.927  1.00 79.52  ? 3    BMA   F C4   1 
HETATM 22785 C  C5   . BMA   G  7  .   ? 28.683  -48.170 -30.464  1.00 73.32  ? 3    BMA   F C5   1 
HETATM 22786 C  C6   . BMA   G  7  .   ? 27.415  -48.390 -31.261  1.00 72.91  ? 3    BMA   F C6   1 
HETATM 22787 O  O2   . BMA   G  7  .   ? 29.633  -48.793 -27.005  1.00 75.52  ? 3    BMA   F O2   1 
HETATM 22788 O  O3   . BMA   G  7  .   ? 31.052  -50.388 -28.606  1.00 85.84  ? 3    BMA   F O3   1 
HETATM 22789 O  O4   . BMA   G  7  .   ? 29.552  -50.352 -31.004  1.00 83.16  ? 3    BMA   F O4   1 
HETATM 22790 O  O5   . BMA   G  7  .   ? 28.364  -47.347 -29.335  1.00 69.42  ? 3    BMA   F O5   1 
HETATM 22791 O  O6   . BMA   G  7  .   ? 26.420  -48.851 -30.366  1.00 74.46  ? 3    BMA   F O6   1 
HETATM 22792 H  H4   . BMA   G  7  .   ? 28.542  -49.912 -29.231  1.00 95.41  ? 3    BMA   F H4   1 
HETATM 22793 H  H5   . BMA   G  7  .   ? 29.415  -47.662 -31.113  1.00 87.97  ? 3    BMA   F H5   1 
HETATM 22794 H  H61  . BMA   G  7  .   ? 27.623  -49.124 -32.055  1.00 87.47  ? 3    BMA   F H61  1 
HETATM 22795 H  H62  . BMA   G  7  .   ? 27.130  -47.438 -31.734  1.00 87.47  ? 3    BMA   F H62  1 
HETATM 22796 H  HO4  . BMA   G  7  .   ? 30.118  -51.043 -30.626  1.00 99.78  ? 3    BMA   F HO4  1 
HETATM 22797 C  C1   . MAN   G  7  .   ? 32.468  -50.493 -28.851  1.00 89.49  ? 4    MAN   F C1   1 
HETATM 22798 C  C2   . MAN   G  7  .   ? 32.766  -51.983 -29.114  1.00 91.17  ? 4    MAN   F C2   1 
HETATM 22799 C  C3   . MAN   G  7  .   ? 32.534  -52.792 -27.836  1.00 90.24  ? 4    MAN   F C3   1 
HETATM 22800 C  C4   . MAN   G  7  .   ? 33.249  -52.155 -26.631  1.00 90.50  ? 4    MAN   F C4   1 
HETATM 22801 C  C5   . MAN   G  7  .   ? 32.869  -50.673 -26.508  1.00 93.49  ? 4    MAN   F C5   1 
HETATM 22802 C  C6   . MAN   G  7  .   ? 33.620  -49.962 -25.398  1.00 98.15  ? 4    MAN   F C6   1 
HETATM 22803 O  O2   . MAN   G  7  .   ? 34.135  -52.194 -29.469  1.00 92.06  ? 4    MAN   F O2   1 
HETATM 22804 O  O3   . MAN   G  7  .   ? 32.952  -54.143 -27.992  1.00 90.99  ? 4    MAN   F O3   1 
HETATM 22805 O  O4   . MAN   G  7  .   ? 32.873  -52.826 -25.439  1.00 89.31  ? 4    MAN   F O4   1 
HETATM 22806 O  O5   . MAN   G  7  .   ? 33.184  -50.010 -27.742  1.00 90.61  ? 4    MAN   F O5   1 
HETATM 22807 O  O6   . MAN   G  7  .   ? 33.304  -50.612 -24.173  1.00 100.90 ? 4    MAN   F O6   1 
HETATM 22808 H  H3   . MAN   G  7  .   ? 31.461  -52.808 -27.621  1.00 108.27 ? 4    MAN   F H3   1 
HETATM 22809 H  H4   . MAN   G  7  .   ? 34.335  -52.214 -26.812  1.00 108.58 ? 4    MAN   F H4   1 
HETATM 22810 H  H5   . MAN   G  7  .   ? 31.793  -50.591 -26.307  1.00 112.17 ? 4    MAN   F H5   1 
HETATM 22811 H  H61  . MAN   G  7  .   ? 33.313  -48.905 -25.387  1.00 117.76 ? 4    MAN   F H61  1 
HETATM 22812 H  H62  . MAN   G  7  .   ? 34.698  -50.010 -25.616  1.00 117.76 ? 4    MAN   F H62  1 
HETATM 22813 H  HO3  . MAN   G  7  .   ? 32.320  -54.539 -28.614  1.00 109.17 ? 4    MAN   F HO3  1 
HETATM 22814 H  HO4  . MAN   G  7  .   ? 33.245  -53.718 -25.517  1.00 107.16 ? 4    MAN   F HO4  1 
HETATM 22815 H  HO6  . MAN   G  7  .   ? 33.942  -50.315 -23.514  1.00 121.06 ? 4    MAN   F HO6  1 
HETATM 22816 C  C1   . NAG   H  5  .   ? 66.154  24.339  -5.818   1.00 114.76 ? 1    NAG   G C1   1 
HETATM 22817 C  C2   . NAG   H  5  .   ? 67.362  23.947  -6.674   1.00 116.60 ? 1    NAG   G C2   1 
HETATM 22818 C  C3   . NAG   H  5  .   ? 67.431  24.818  -7.918   1.00 118.88 ? 1    NAG   G C3   1 
HETATM 22819 C  C4   . NAG   H  5  .   ? 66.055  24.887  -8.562   1.00 121.58 ? 1    NAG   G C4   1 
HETATM 22820 C  C5   . NAG   H  5  .   ? 65.089  25.603  -7.626   1.00 119.82 ? 1    NAG   G C5   1 
HETATM 22821 C  C6   . NAG   H  5  .   ? 63.731  24.941  -7.564   1.00 120.57 ? 1    NAG   G C6   1 
HETATM 22822 C  C7   . NAG   H  5  .   ? 69.787  23.671  -6.404   1.00 119.45 ? 1    NAG   G C7   1 
HETATM 22823 C  C8   . NAG   H  5  .   ? 70.956  23.826  -5.478   1.00 118.44 ? 1    NAG   G C8   1 
HETATM 22824 N  N2   . NAG   H  5  .   ? 68.598  24.036  -5.913   1.00 117.75 ? 1    NAG   G N2   1 
HETATM 22825 O  O3   . NAG   H  5  .   ? 68.372  24.268  -8.832   1.00 119.14 ? 1    NAG   G O3   1 
HETATM 22826 O  O4   . NAG   H  5  .   ? 66.117  25.571  -9.808   1.00 124.47 ? 1    NAG   G O4   1 
HETATM 22827 O  O5   . NAG   H  5  .   ? 65.608  25.605  -6.286   1.00 116.12 ? 1    NAG   G O5   1 
HETATM 22828 O  O6   . NAG   H  5  .   ? 62.742  25.825  -7.054   1.00 120.23 ? 1    NAG   G O6   1 
HETATM 22829 O  O7   . NAG   H  5  .   ? 69.914  23.238  -7.545   1.00 121.59 ? 1    NAG   G O7   1 
HETATM 22830 H  H4   . NAG   H  5  .   ? 65.732  23.981  -8.731   1.00 145.88 ? 1    NAG   G H4   1 
HETATM 22831 H  H5   . NAG   H  5  .   ? 64.985  26.526  -7.925   1.00 143.77 ? 1    NAG   G H5   1 
HETATM 22832 H  H61  . NAG   H  5  .   ? 63.785  24.156  -6.987   1.00 144.66 ? 1    NAG   G H61  1 
HETATM 22833 H  H62  . NAG   H  5  .   ? 63.473  24.659  -8.463   1.00 144.66 ? 1    NAG   G H62  1 
HETATM 22834 H  H81  . NAG   H  5  .   ? 71.743  23.405  -5.874   1.00 142.11 ? 1    NAG   G H81  1 
HETATM 22835 H  H82  . NAG   H  5  .   ? 70.754  23.399  -4.624   1.00 142.11 ? 1    NAG   G H82  1 
HETATM 22836 H  H83  . NAG   H  5  .   ? 71.133  24.775  -5.333   1.00 142.11 ? 1    NAG   G H83  1 
HETATM 22837 H  HN2  . NAG   H  5  .   ? 68.560  24.357  -5.060   1.00 141.28 ? 1    NAG   G HN2  1 
HETATM 22838 H  HO6  . NAG   H  5  .   ? 62.915  26.003  -6.201   1.00 144.26 ? 1    NAG   G HO6  1 
HETATM 22839 C  C1   . NAG   H  5  .   ? 65.506  24.693  -10.777  1.00 125.67 ? 2    NAG   G C1   1 
HETATM 22840 C  C2   . NAG   H  5  .   ? 65.375  25.420  -12.119  1.00 125.29 ? 2    NAG   G C2   1 
HETATM 22841 C  C3   . NAG   H  5  .   ? 64.801  24.481  -13.183  1.00 123.83 ? 2    NAG   G C3   1 
HETATM 22842 C  C4   . NAG   H  5  .   ? 65.569  23.164  -13.222  1.00 124.71 ? 2    NAG   G C4   1 
HETATM 22843 C  C5   . NAG   H  5  .   ? 65.674  22.572  -11.820  1.00 124.22 ? 2    NAG   G C5   1 
HETATM 22844 C  C6   . NAG   H  5  .   ? 66.500  21.309  -11.759  1.00 122.15 ? 2    NAG   G C6   1 
HETATM 22845 C  C7   . NAG   H  5  .   ? 63.356  26.599  -11.367  1.00 127.59 ? 2    NAG   G C7   1 
HETATM 22846 C  C8   . NAG   H  5  .   ? 62.635  27.912  -11.314  1.00 124.76 ? 2    NAG   G C8   1 
HETATM 22847 N  N2   . NAG   H  5  .   ? 64.544  26.606  -11.984  1.00 126.73 ? 2    NAG   G N2   1 
HETATM 22848 O  O3   . NAG   H  5  .   ? 64.871  25.121  -14.452  1.00 121.71 ? 2    NAG   G O3   1 
HETATM 22849 O  O4   . NAG   H  5  .   ? 64.886  22.212  -14.031  1.00 125.74 ? 2    NAG   G O4   1 
HETATM 22850 O  O5   . NAG   H  5  .   ? 66.293  23.519  -10.943  1.00 125.76 ? 2    NAG   G O5   1 
HETATM 22851 O  O6   . NAG   H  5  .   ? 66.119  20.495  -10.658  1.00 120.50 ? 2    NAG   G O6   1 
HETATM 22852 O  O7   . NAG   H  5  .   ? 62.885  25.578  -10.875  1.00 130.54 ? 2    NAG   G O7   1 
HETATM 22853 H  H4   . NAG   H  5  .   ? 66.456  23.341  -13.587  1.00 149.63 ? 2    NAG   G H4   1 
HETATM 22854 H  H5   . NAG   H  5  .   ? 64.776  22.371  -11.493  1.00 149.05 ? 2    NAG   G H5   1 
HETATM 22855 H  H61  . NAG   H  5  .   ? 67.442  21.548  -11.669  1.00 146.56 ? 2    NAG   G H61  1 
HETATM 22856 H  H62  . NAG   H  5  .   ? 66.376  20.805  -12.586  1.00 146.56 ? 2    NAG   G H62  1 
HETATM 22857 H  H81  . NAG   H  5  .   ? 61.741  27.777  -10.947  1.00 149.69 ? 2    NAG   G H81  1 
HETATM 22858 H  H82  . NAG   H  5  .   ? 62.564  28.280  -12.215  1.00 149.69 ? 2    NAG   G H82  1 
HETATM 22859 H  H83  . NAG   H  5  .   ? 63.130  28.533  -10.747  1.00 149.69 ? 2    NAG   G H83  1 
HETATM 22860 H  HN2  . NAG   H  5  .   ? 64.847  27.391  -12.335  1.00 152.05 ? 2    NAG   G HN2  1 
HETATM 22861 H  HO6  . NAG   H  5  .   ? 65.929  19.676  -10.942  1.00 144.58 ? 2    NAG   G HO6  1 
HETATM 22862 C  C1   . BMA   H  5  .   ? 65.234  22.252  -15.431  1.00 125.10 ? 3    BMA   G C1   1 
HETATM 22863 C  C2   . BMA   H  5  .   ? 66.697  21.842  -15.621  1.00 125.73 ? 3    BMA   G C2   1 
HETATM 22864 C  C3   . BMA   H  5  .   ? 67.001  21.678  -17.111  1.00 120.83 ? 3    BMA   G C3   1 
HETATM 22865 C  C4   . BMA   H  5  .   ? 65.806  22.063  -18.015  1.00 117.62 ? 3    BMA   G C4   1 
HETATM 22866 C  C5   . BMA   H  5  .   ? 64.484  21.399  -17.558  1.00 115.85 ? 3    BMA   G C5   1 
HETATM 22867 C  C6   . BMA   H  5  .   ? 64.335  19.963  -18.051  1.00 107.44 ? 3    BMA   G C6   1 
HETATM 22868 O  O2   . BMA   H  5  .   ? 66.948  20.581  -15.015  1.00 129.30 ? 3    BMA   G O2   1 
HETATM 22869 O  O3   . BMA   H  5  .   ? 67.457  20.362  -17.418  1.00 119.53 ? 3    BMA   G O3   1 
HETATM 22870 O  O4   . BMA   H  5  .   ? 65.653  23.481  -18.018  1.00 116.65 ? 3    BMA   G O4   1 
HETATM 22871 O  O5   . BMA   H  5  .   ? 64.397  21.357  -16.125  1.00 121.53 ? 3    BMA   G O5   1 
HETATM 22872 O  O6   . BMA   H  5  .   ? 63.301  19.338  -17.293  1.00 101.64 ? 3    BMA   G O6   1 
HETATM 22873 H  H4   . BMA   H  5  .   ? 66.017  21.656  -19.017  1.00 141.12 ? 3    BMA   G H4   1 
HETATM 22874 H  H5   . BMA   H  5  .   ? 63.660  22.020  -17.947  1.00 139.00 ? 3    BMA   G H5   1 
HETATM 22875 H  H61  . BMA   H  5  .   ? 65.300  19.449  -17.923  1.00 128.91 ? 3    BMA   G H61  1 
HETATM 22876 H  H62  . BMA   H  5  .   ? 64.094  19.987  -19.125  1.00 128.91 ? 3    BMA   G H62  1 
HETATM 22877 H  HO4  . BMA   H  5  .   ? 64.828  23.655  -18.494  1.00 139.97 ? 3    BMA   G HO4  1 
HETATM 22878 H  HO6  . BMA   H  5  .   ? 63.557  19.362  -16.360  1.00 121.94 ? 3    BMA   G HO6  1 
HETATM 22879 CA CA   . CA    I  8  .   ? 35.397  -27.213 -37.785  1.00 62.78  ? 2001 CA    A CA   1 
HETATM 22880 CA CA   . CA    J  8  .   ? 36.768  -5.514  -25.140  1.00 74.24  ? 2002 CA    A CA   1 
HETATM 22881 CA CA   . CA    K  8  .   ? 26.584  1.058   -30.998  1.00 74.33  ? 2003 CA    A CA   1 
HETATM 22882 CA CA   . CA    L  8  .   ? 40.433  -17.595 -27.825  1.00 63.68  ? 2004 CA    A CA   1 
HETATM 22883 C  C1   . MAN   M  9  .   ? 24.358  -49.508 -32.690  1.00 111.31 ? 2005 MAN   A C1   1 
HETATM 22884 C  C2   . MAN   M  9  .   ? 23.197  -48.919 -31.870  1.00 113.17 ? 2005 MAN   A C2   1 
HETATM 22885 C  C3   . MAN   M  9  .   ? 23.232  -49.462 -30.442  1.00 111.94 ? 2005 MAN   A C3   1 
HETATM 22886 C  C4   . MAN   M  9  .   ? 23.364  -50.993 -30.432  1.00 109.81 ? 2005 MAN   A C4   1 
HETATM 22887 C  C5   . MAN   M  9  .   ? 24.593  -51.416 -31.243  1.00 108.21 ? 2005 MAN   A C5   1 
HETATM 22888 C  C6   . MAN   M  9  .   ? 24.748  -52.924 -31.343  1.00 104.48 ? 2005 MAN   A C6   1 
HETATM 22889 O  O2   . MAN   M  9  .   ? 21.929  -49.312 -32.403  1.00 114.24 ? 2005 MAN   A O2   1 
HETATM 22890 O  O3   . MAN   M  9  .   ? 22.080  -49.064 -29.703  1.00 110.48 ? 2005 MAN   A O3   1 
HETATM 22891 O  O4   . MAN   M  9  .   ? 23.505  -51.457 -29.099  1.00 108.92 ? 2005 MAN   A O4   1 
HETATM 22892 O  O5   . MAN   M  9  .   ? 24.457  -50.906 -32.584  1.00 110.23 ? 2005 MAN   A O5   1 
HETATM 22893 O  O6   . MAN   M  9  .   ? 26.036  -53.275 -30.845  1.00 100.73 ? 2005 MAN   A O6   1 
HETATM 22894 H  H3   . MAN   M  9  .   ? 24.102  -49.044 -29.926  1.00 134.31 ? 2005 MAN   A H3   1 
HETATM 22895 H  H4   . MAN   M  9  .   ? 22.469  -51.418 -30.917  1.00 131.75 ? 2005 MAN   A H4   1 
HETATM 22896 H  H5   . MAN   M  9  .   ? 25.494  -51.004 -30.771  1.00 129.83 ? 2005 MAN   A H5   1 
HETATM 22897 H  H61  . MAN   M  9  .   ? 24.630  -53.217 -32.398  1.00 125.36 ? 2005 MAN   A H61  1 
HETATM 22898 H  H62  . MAN   M  9  .   ? 23.946  -53.397 -30.757  1.00 125.36 ? 2005 MAN   A H62  1 
HETATM 22899 H  HO3  . MAN   M  9  .   ? 22.004  -48.105 -29.841  1.00 132.56 ? 2005 MAN   A HO3  1 
HETATM 22900 H  HO4  . MAN   M  9  .   ? 23.189  -50.731 -28.539  1.00 130.68 ? 2005 MAN   A HO4  1 
HETATM 22901 H  HO6  . MAN   M  9  .   ? 26.684  -52.704 -31.278  1.00 120.85 ? 2005 MAN   A HO6  1 
HETATM 22902 C  C1   . MAN   N  9  .   ? 25.302  -54.580 -28.011  1.00 103.67 ? 2006 MAN   A C1   1 
HETATM 22903 C  C2   . MAN   N  9  .   ? 25.761  -53.290 -27.318  1.00 105.44 ? 2006 MAN   A C2   1 
HETATM 22904 C  C3   . MAN   N  9  .   ? 24.974  -53.088 -26.030  1.00 103.46 ? 2006 MAN   A C3   1 
HETATM 22905 C  C4   . MAN   N  9  .   ? 23.461  -53.193 -26.288  1.00 105.33 ? 2006 MAN   A C4   1 
HETATM 22906 C  C5   . MAN   N  9  .   ? 23.132  -54.521 -26.987  1.00 105.16 ? 2006 MAN   A C5   1 
HETATM 22907 C  C6   . MAN   N  9  .   ? 21.671  -54.629 -27.385  1.00 105.22 ? 2006 MAN   A C6   1 
HETATM 22908 O  O2   . MAN   N  9  .   ? 25.479  -52.142 -28.124  1.00 109.26 ? 2006 MAN   A O2   1 
HETATM 22909 O  O3   . MAN   N  9  .   ? 25.284  -51.840 -25.417  1.00 100.14 ? 2006 MAN   A O3   1 
HETATM 22910 O  O4   . MAN   N  9  .   ? 22.761  -53.132 -25.058  1.00 106.07 ? 2006 MAN   A O4   1 
HETATM 22911 O  O5   . MAN   N  9  .   ? 23.913  -54.633 -28.192  1.00 104.20 ? 2006 MAN   A O5   1 
HETATM 22912 O  O6   . MAN   N  9  .   ? 21.590  -55.416 -28.569  1.00 104.11 ? 2006 MAN   A O6   1 
HETATM 22913 C  C1   . GOL   O  10 .   ? 12.633  -35.000 -42.116  1.00 61.70  ? 2007 GOL   A C1   1 
HETATM 22914 O  O1   . GOL   O  10 .   ? 12.034  -33.742 -42.169  1.00 65.90  ? 2007 GOL   A O1   1 
HETATM 22915 C  C2   . GOL   O  10 .   ? 14.162  -34.768 -42.025  1.00 58.00  ? 2007 GOL   A C2   1 
HETATM 22916 O  O2   . GOL   O  10 .   ? 14.527  -34.142 -40.841  1.00 59.21  ? 2007 GOL   A O2   1 
HETATM 22917 C  C3   . GOL   O  10 .   ? 14.782  -36.174 -42.156  1.00 60.04  ? 2007 GOL   A C3   1 
HETATM 22918 O  O3   . GOL   O  10 .   ? 15.796  -36.077 -43.106  1.00 62.40  ? 2007 GOL   A O3   1 
HETATM 22919 H  H31  . GOL   O  10 .   ? 14.085  -36.804 -42.398  1.00 72.02  ? 2007 GOL   A H31  1 
HETATM 22920 H  H32  . GOL   O  10 .   ? 15.096  -36.462 -41.284  1.00 72.02  ? 2007 GOL   A H32  1 
HETATM 22921 H  HO3  . GOL   O  10 .   ? 16.502  -35.859 -42.689  1.00 74.87  ? 2007 GOL   A HO3  1 
HETATM 22922 C  C1   . GOL   P  10 .   ? 9.842   -24.158 -25.570  1.00 62.19  ? 2008 GOL   A C1   1 
HETATM 22923 O  O1   . GOL   P  10 .   ? 8.650   -24.372 -24.881  1.00 65.82  ? 2008 GOL   A O1   1 
HETATM 22924 C  C2   . GOL   P  10 .   ? 10.574  -22.996 -24.864  1.00 67.10  ? 2008 GOL   A C2   1 
HETATM 22925 O  O2   . GOL   P  10 .   ? 10.408  -23.047 -23.490  1.00 68.19  ? 2008 GOL   A O2   1 
HETATM 22926 C  C3   . GOL   P  10 .   ? 12.055  -23.165 -25.269  1.00 77.09  ? 2008 GOL   A C3   1 
HETATM 22927 O  O3   . GOL   P  10 .   ? 12.585  -21.886 -25.410  1.00 83.08  ? 2008 GOL   A O3   1 
HETATM 22928 H  H31  . GOL   P  10 .   ? 12.099  -23.691 -26.082  1.00 92.49  ? 2008 GOL   A H31  1 
HETATM 22929 H  H32  . GOL   P  10 .   ? 12.506  -23.696 -24.594  1.00 92.49  ? 2008 GOL   A H32  1 
HETATM 22930 H  HO3  . GOL   P  10 .   ? 13.412  -21.983 -25.581  1.00 99.67  ? 2008 GOL   A HO3  1 
HETATM 22931 C  C1   . GOL   Q  10 .   ? 25.282  -42.797 -31.834  1.00 79.13  ? 2009 GOL   A C1   1 
HETATM 22932 O  O1   . GOL   Q  10 .   ? 26.178  -41.731 -31.850  1.00 76.81  ? 2009 GOL   A O1   1 
HETATM 22933 C  C2   . GOL   Q  10 .   ? 26.121  -44.092 -31.974  1.00 82.04  ? 2009 GOL   A C2   1 
HETATM 22934 O  O2   . GOL   Q  10 .   ? 27.053  -44.224 -30.954  1.00 81.56  ? 2009 GOL   A O2   1 
HETATM 22935 C  C3   . GOL   Q  10 .   ? 25.085  -45.237 -31.974  1.00 85.82  ? 2009 GOL   A C3   1 
HETATM 22936 O  O3   . GOL   Q  10 .   ? 24.739  -45.467 -33.305  1.00 88.89  ? 2009 GOL   A O3   1 
HETATM 22937 H  H31  . GOL   Q  10 .   ? 24.332  -44.980 -31.419  1.00 102.97 ? 2009 GOL   A H31  1 
HETATM 22938 H  H32  . GOL   Q  10 .   ? 25.473  -46.011 -31.537  1.00 102.97 ? 2009 GOL   A H32  1 
HETATM 22939 H  HO3  . GOL   Q  10 .   ? 24.051  -45.968 -33.296  1.00 106.65 ? 2009 GOL   A HO3  1 
HETATM 22940 C  C1   . GOL   R  10 .   ? 12.671  -17.406 -7.492   1.00 82.19  ? 2010 GOL   A C1   1 
HETATM 22941 O  O1   . GOL   R  10 .   ? 11.952  -17.969 -6.438   1.00 83.13  ? 2010 GOL   A O1   1 
HETATM 22942 C  C2   . GOL   R  10 .   ? 14.160  -17.399 -7.070   1.00 80.89  ? 2010 GOL   A C2   1 
HETATM 22943 O  O2   . GOL   R  10 .   ? 14.627  -16.118 -6.807   1.00 84.08  ? 2010 GOL   A O2   1 
HETATM 22944 C  C3   . GOL   R  10 .   ? 14.908  -18.067 -8.244   1.00 76.88  ? 2010 GOL   A C3   1 
HETATM 22945 O  O3   . GOL   R  10 .   ? 15.448  -19.252 -7.750   1.00 74.94  ? 2010 GOL   A O3   1 
HETATM 22946 H  H31  . GOL   R  10 .   ? 15.575  -17.450 -8.584   1.00 92.24  ? 2010 GOL   A H31  1 
HETATM 22947 H  H32  . GOL   R  10 .   ? 14.287  -18.202 -8.977   1.00 92.24  ? 2010 GOL   A H32  1 
HETATM 22948 H  HO3  . GOL   R  10 .   ? 16.294  -19.163 -7.778   1.00 89.91  ? 2010 GOL   A HO3  1 
HETATM 22949 MG MG   . MG    S  11 .   ? 7.704   -44.203 -13.155  1.00 43.74  ? 2001 MG    B MG   1 
HETATM 22950 CA CA   . CA    T  8  .   ? 8.325   -38.707 -15.591  1.00 49.05  ? 2002 CA    B CA   1 
HETATM 22951 CA CA   . CA    U  8  .   ? 7.817   -52.157 -8.782   1.00 61.12  ? 2003 CA    B CA   1 
HETATM 22952 C  C13  . A1A6I V  12 .   ? 12.708  -47.219 -21.636  1.00 56.97  ? 2004 A1A6I B C13  1 
HETATM 22953 C  C14  . A1A6I V  12 .   ? 14.226  -47.120 -21.946  1.00 59.24  ? 2004 A1A6I B C14  1 
HETATM 22954 C  C15  . A1A6I V  12 .   ? 14.466  -47.150 -23.477  1.00 64.94  ? 2004 A1A6I B C15  1 
HETATM 22955 C  C19  . A1A6I V  12 .   ? 15.165  -47.152 -27.735  1.00 78.84  ? 2004 A1A6I B C19  1 
HETATM 22956 C  C20  . A1A6I V  12 .   ? 15.973  -45.951 -28.223  1.00 79.66  ? 2004 A1A6I B C20  1 
HETATM 22957 C  C21  . A1A6I V  12 .   ? 15.897  -44.752 -27.293  1.00 79.66  ? 2004 A1A6I B C21  1 
HETATM 22958 C  C23  . A1A6I V  12 .   ? 14.112  -48.185 -25.630  1.00 71.97  ? 2004 A1A6I B C23  1 
HETATM 22959 C  C24  . A1A6I V  12 .   ? 13.892  -48.171 -24.247  1.00 67.64  ? 2004 A1A6I B C24  1 
HETATM 22960 C  C25  . A1A6I V  12 .   ? 5.621   -46.892 -17.220  1.00 60.97  ? 2004 A1A6I B C25  1 
HETATM 22961 C  C26  . A1A6I V  12 .   ? 6.193   -47.789 -16.326  1.00 59.22  ? 2004 A1A6I B C26  1 
HETATM 22962 C  C27  . A1A6I V  12 .   ? 5.741   -49.105 -16.277  1.00 57.16  ? 2004 A1A6I B C27  1 
HETATM 22963 C  C02  . A1A6I V  12 .   ? 5.843   -44.735 -15.962  1.00 71.23  ? 2004 A1A6I B C02  1 
HETATM 22964 C  C04  . A1A6I V  12 .   ? 6.116   -45.437 -17.280  1.00 70.04  ? 2004 A1A6I B C04  1 
HETATM 22965 C  C06  . A1A6I V  12 .   ? 8.071   -43.938 -17.710  1.00 68.39  ? 2004 A1A6I B C06  1 
HETATM 22966 C  C07  . A1A6I V  12 .   ? 9.072   -43.948 -18.969  1.00 63.96  ? 2004 A1A6I B C07  1 
HETATM 22967 C  C08  . A1A6I V  12 .   ? 8.878   -45.090 -19.618  1.00 63.07  ? 2004 A1A6I B C08  1 
HETATM 22968 C  C09  . A1A6I V  12 .   ? 7.754   -46.015 -18.753  1.00 66.41  ? 2004 A1A6I B C09  1 
HETATM 22969 C  C11  . A1A6I V  12 .   ? 10.598  -45.831 -21.087  1.00 57.91  ? 2004 A1A6I B C11  1 
HETATM 22970 C  C12  . A1A6I V  12 .   ? 12.151  -45.890 -21.053  1.00 55.30  ? 2004 A1A6I B C12  1 
HETATM 22971 C  C17  . A1A6I V  12 .   ? 15.440  -46.181 -25.368  1.00 74.72  ? 2004 A1A6I B C17  1 
HETATM 22972 C  C18  . A1A6I V  12 .   ? 14.904  -47.168 -26.194  1.00 76.20  ? 2004 A1A6I B C18  1 
HETATM 22973 C  C29  . A1A6I V  12 .   ? 4.717   -49.528 -17.124  1.00 54.94  ? 2004 A1A6I B C29  1 
HETATM 22974 C  C30  . A1A6I V  12 .   ? 4.143   -48.630 -18.022  1.00 56.02  ? 2004 A1A6I B C30  1 
HETATM 22975 C  C31  . A1A6I V  12 .   ? 4.594   -47.316 -18.069  1.00 55.58  ? 2004 A1A6I B C31  1 
HETATM 22976 C  C32  . A1A6I V  12 .   ? 3.976   -46.331 -19.047  1.00 51.35  ? 2004 A1A6I B C32  1 
HETATM 22977 C  C33  . A1A6I V  12 .   ? 2.535   -46.732 -19.353  1.00 52.30  ? 2004 A1A6I B C33  1 
HETATM 22978 C  C34  . A1A6I V  12 .   ? 1.913   -45.859 -20.369  1.00 54.83  ? 2004 A1A6I B C34  1 
HETATM 22979 C  C35  . A1A6I V  12 .   ? 2.753   -45.601 -21.544  1.00 57.17  ? 2004 A1A6I B C35  1 
HETATM 22980 C  C36  . A1A6I V  12 .   ? 2.510   -46.465 -22.789  1.00 58.71  ? 2004 A1A6I B C36  1 
HETATM 22981 C  C37  . A1A6I V  12 .   ? 2.182   -44.972 -22.824  1.00 59.68  ? 2004 A1A6I B C37  1 
HETATM 22982 C  C38  . A1A6I V  12 .   ? 4.221   -45.337 -21.208  1.00 53.05  ? 2004 A1A6I B C38  1 
HETATM 22983 F  F28  . A1A6I V  12 .   ? 6.304   -49.983 -15.393  1.00 58.33  ? 2004 A1A6I B F28  1 
HETATM 22984 N  N05  . A1A6I V  12 .   ? 7.557   -45.434 -17.564  1.00 71.29  ? 2004 A1A6I B N05  1 
HETATM 22985 N  N16  . A1A6I V  12 .   ? 15.204  -46.207 -24.049  1.00 67.32  ? 2004 A1A6I B N16  1 
HETATM 22986 N  N22  . A1A6I V  12 .   ? 16.278  -45.091 -25.937  1.00 77.96  ? 2004 A1A6I B N22  1 
HETATM 22987 O  O01  . A1A6I V  12 .   ? 6.784   -44.528 -15.143  1.00 70.92  ? 2004 A1A6I B O01  1 
HETATM 22988 O  O03  . A1A6I V  12 .   ? 4.669   -44.356 -15.685  1.00 70.66  ? 2004 A1A6I B O03  1 
HETATM 22989 O  O10  . A1A6I V  12 .   ? 10.108  -45.795 -19.746  1.00 61.88  ? 2004 A1A6I B O10  1 
HETATM 22990 O  O39  . A1A6I V  12 .   ? 4.772   -46.316 -20.263  1.00 51.13  ? 2004 A1A6I B O39  1 
HETATM 22991 C  C1   . GOL   W  10 .   ? 25.161  -34.472 5.573    1.00 89.34  ? 2005 GOL   B C1   1 
HETATM 22992 O  O1   . GOL   W  10 .   ? 24.327  -34.703 4.480    1.00 89.60  ? 2005 GOL   B O1   1 
HETATM 22993 C  C2   . GOL   W  10 .   ? 24.931  -35.630 6.571    1.00 90.35  ? 2005 GOL   B C2   1 
HETATM 22994 O  O2   . GOL   W  10 .   ? 24.731  -36.836 5.921    1.00 88.71  ? 2005 GOL   B O2   1 
HETATM 22995 C  C3   . GOL   W  10 .   ? 26.204  -35.659 7.441    1.00 94.49  ? 2005 GOL   B C3   1 
HETATM 22996 O  O3   . GOL   W  10 .   ? 26.182  -36.867 8.127    1.00 98.86  ? 2005 GOL   B O3   1 
HETATM 22997 H  H31  . GOL   W  10 .   ? 26.207  -34.884 8.024    1.00 113.37 ? 2005 GOL   B H31  1 
HETATM 22998 H  H32  . GOL   W  10 .   ? 26.981  -35.553 6.870    1.00 113.37 ? 2005 GOL   B H32  1 
HETATM 22999 H  HO3  . GOL   W  10 .   ? 25.874  -37.447 7.586    1.00 118.61 ? 2005 GOL   B HO3  1 
HETATM 23000 C  C1   . GOL   X  10 .   ? 28.821  -22.212 26.646   1.00 82.89  ? 2006 GOL   B C1   1 
HETATM 23001 O  O1   . GOL   X  10 .   ? 28.878  -23.195 27.631   1.00 80.69  ? 2006 GOL   B O1   1 
HETATM 23002 C  C2   . GOL   X  10 .   ? 30.223  -21.565 26.577   1.00 86.90  ? 2006 GOL   B C2   1 
HETATM 23003 O  O2   . GOL   X  10 .   ? 31.235  -22.511 26.646   1.00 90.33  ? 2006 GOL   B O2   1 
HETATM 23004 C  C3   . GOL   X  10 .   ? 30.266  -20.568 27.759   1.00 87.87  ? 2006 GOL   B C3   1 
HETATM 23005 O  O3   . GOL   X  10 .   ? 31.568  -20.073 27.815   1.00 90.98  ? 2006 GOL   B O3   1 
HETATM 23006 H  H31  . GOL   X  10 .   ? 29.992  -21.027 28.569   1.00 105.43 ? 2006 GOL   B H31  1 
HETATM 23007 H  H32  . GOL   X  10 .   ? 29.597  -19.880 27.616   1.00 105.43 ? 2006 GOL   B H32  1 
HETATM 23008 H  HO3  . GOL   X  10 .   ? 32.084  -20.728 27.644   1.00 109.16 ? 2006 GOL   B HO3  1 
HETATM 23009 C  C    . ACT   Y  13 .   ? 9.531   -46.222 24.742   1.00 73.29  ? 2007 ACT   B C    1 
HETATM 23010 O  O    . ACT   Y  13 .   ? 10.725  -45.881 24.514   1.00 72.84  ? 2007 ACT   B O    1 
HETATM 23011 O  OXT  . ACT   Y  13 .   ? 8.850   -47.132 24.190   1.00 72.17  ? 2007 ACT   B OXT  1 
HETATM 23012 C  CH3  . ACT   Y  13 .   ? 8.780   -45.418 25.855   1.00 73.81  ? 2007 ACT   B CH3  1 
HETATM 23013 C  C1   . NAG   Z  14 .   ? 5.341   -24.251 17.921   1.00 94.64  ? 2008 NAG   B C1   1 
HETATM 23014 C  C2   . NAG   Z  14 .   ? 6.070   -23.340 16.926   1.00 104.80 ? 2008 NAG   B C2   1 
HETATM 23015 C  C3   . NAG   Z  14 .   ? 5.486   -21.923 16.982   1.00 109.02 ? 2008 NAG   B C3   1 
HETATM 23016 C  C4   . NAG   Z  14 .   ? 3.964   -21.947 16.883   1.00 113.26 ? 2008 NAG   B C4   1 
HETATM 23017 C  C5   . NAG   Z  14 .   ? 3.375   -22.943 17.876   1.00 112.63 ? 2008 NAG   B C5   1 
HETATM 23018 C  C6   . NAG   Z  14 .   ? 1.878   -23.101 17.754   1.00 116.26 ? 2008 NAG   B C6   1 
HETATM 23019 C  C7   . NAG   Z  14 .   ? 8.354   -22.477 16.607   1.00 111.73 ? 2008 NAG   B C7   1 
HETATM 23020 C  C8   . NAG   Z  14 .   ? 9.786   -22.584 17.036   1.00 111.96 ? 2008 NAG   B C8   1 
HETATM 23021 N  N2   . NAG   Z  14 .   ? 7.497   -23.310 17.211   1.00 109.45 ? 2008 NAG   B N2   1 
HETATM 23022 O  O3   . NAG   Z  14 .   ? 6.020   -21.138 15.922   1.00 109.51 ? 2008 NAG   B O3   1 
HETATM 23023 O  O4   . NAG   Z  14 .   ? 3.447   -20.651 17.166   1.00 116.69 ? 2008 NAG   B O4   1 
HETATM 23024 O  O5   . NAG   Z  14 .   ? 3.948   -24.236 17.649   1.00 106.50 ? 2008 NAG   B O5   1 
HETATM 23025 O  O6   . NAG   Z  14 .   ? 1.456   -24.368 18.240   1.00 118.24 ? 2008 NAG   B O6   1 
HETATM 23026 O  O7   . NAG   Z  14 .   ? 7.990   -21.674 15.753   1.00 111.56 ? 2008 NAG   B O7   1 
HETATM 23027 H  H4   . NAG   Z  14 .   ? 3.710   -22.214 15.979   1.00 135.89 ? 2008 NAG   B H4   1 
HETATM 23028 H  H5   . NAG   Z  14 .   ? 3.584   -22.648 18.783   1.00 135.13 ? 2008 NAG   B H5   1 
HETATM 23029 H  H61  . NAG   Z  14 .   ? 1.623   -23.018 16.816   1.00 139.49 ? 2008 NAG   B H61  1 
HETATM 23030 H  H62  . NAG   Z  14 .   ? 1.438   -22.398 18.269   1.00 139.49 ? 2008 NAG   B H62  1 
HETATM 23031 H  H81  . NAG   Z  14 .   ? 9.914   -22.092 17.869   1.00 134.34 ? 2008 NAG   B H81  1 
HETATM 23032 H  H82  . NAG   Z  14 .   ? 10.362  -22.207 16.344   1.00 134.34 ? 2008 NAG   B H82  1 
HETATM 23033 H  H83  . NAG   Z  14 .   ? 10.015  -23.523 17.174   1.00 134.34 ? 2008 NAG   B H83  1 
HETATM 23034 H  HN2  . NAG   Z  14 .   ? 7.825   -23.889 17.834   1.00 131.32 ? 2008 NAG   B HN2  1 
HETATM 23035 H  HO4  . NAG   Z  14 .   ? 2.561   -20.685 17.221   1.00 140.01 ? 2008 NAG   B HO4  1 
HETATM 23036 H  HO6  . NAG   Z  14 .   ? 0.570   -24.385 18.294   1.00 141.87 ? 2008 NAG   B HO6  1 
HETATM 23037 CL CL   . CL    AA 15 .   ? 1.232   -52.724 -15.483  1.00 87.45  ? 2009 CL    B CL   1 
HETATM 23038 C  C1   . GOL   BA 10 .   ? -3.391  -43.229 -43.840  1.00 88.90  ? 301  GOL   C C1   1 
HETATM 23039 O  O1   . GOL   BA 10 .   ? -4.767  -43.047 -43.964  1.00 91.12  ? 301  GOL   C O1   1 
HETATM 23040 C  C2   . GOL   BA 10 .   ? -2.730  -42.410 -44.974  1.00 85.36  ? 301  GOL   C C2   1 
HETATM 23041 O  O2   . GOL   BA 10 .   ? -2.934  -41.046 -44.819  1.00 81.60  ? 301  GOL   C O2   1 
HETATM 23042 C  C3   . GOL   BA 10 .   ? -1.234  -42.789 -44.919  1.00 86.33  ? 301  GOL   C C3   1 
HETATM 23043 O  O3   . GOL   BA 10 .   ? -1.169  -44.184 -44.947  1.00 85.26  ? 301  GOL   C O3   1 
HETATM 23044 H  H31  . GOL   BA 10 .   ? -0.841  -42.401 -44.121  1.00 103.57 ? 301  GOL   C H31  1 
HETATM 23045 H  H32  . GOL   BA 10 .   ? -0.775  -42.367 -45.662  1.00 103.57 ? 301  GOL   C H32  1 
HETATM 23046 H  HO3  . GOL   BA 10 .   ? -1.653  -44.438 -45.596  1.00 102.30 ? 301  GOL   C HO3  1 
HETATM 23047 C  C1   . GOL   CA 10 .   ? 14.950  -55.791 -61.847  1.00 82.64  ? 301  GOL   D C1   1 
HETATM 23048 O  O1   . GOL   CA 10 .   ? 14.105  -55.292 -62.837  1.00 83.33  ? 301  GOL   D O1   1 
HETATM 23049 C  C2   . GOL   CA 10 .   ? 16.279  -56.177 -62.539  1.00 81.44  ? 301  GOL   D C2   1 
HETATM 23050 O  O2   . GOL   CA 10 .   ? 16.766  -57.395 -62.085  1.00 81.04  ? 301  GOL   D O2   1 
HETATM 23051 C  C3   . GOL   CA 10 .   ? 17.244  -55.014 -62.223  1.00 82.14  ? 301  GOL   D C3   1 
HETATM 23052 O  O3   . GOL   CA 10 .   ? 18.355  -55.181 -63.048  1.00 83.97  ? 301  GOL   D O3   1 
HETATM 23053 H  H31  . GOL   CA 10 .   ? 17.459  -55.031 -61.277  1.00 98.55  ? 301  GOL   D H31  1 
HETATM 23054 H  H32  . GOL   CA 10 .   ? 16.781  -54.173 -62.365  1.00 98.55  ? 301  GOL   D H32  1 
HETATM 23055 H  HO3  . GOL   CA 10 .   ? 18.930  -54.604 -62.805  1.00 100.75 ? 301  GOL   D HO3  1 
HETATM 23056 C  C    . ACT   DA 13 .   ? 10.870  -35.394 -51.253  1.00 70.91  ? 302  ACT   D C    1 
HETATM 23057 O  O    . ACT   DA 13 .   ? 10.930  -35.254 -50.000  1.00 69.08  ? 302  ACT   D O    1 
HETATM 23058 O  OXT  . ACT   DA 13 .   ? 11.093  -34.539 -52.156  1.00 78.46  ? 302  ACT   D OXT  1 
HETATM 23059 C  CH3  . ACT   DA 13 .   ? 10.466  -36.813 -51.771  1.00 62.89  ? 302  ACT   D CH3  1 
HETATM 23060 O  O    . HOH   EA 16 .   ? 4.253   -45.968 -30.386  1.00 68.20  ? 2101 HOH   A O    1 
HETATM 23061 O  O    . HOH   EA 16 .   ? 13.102  -11.882 -12.068  1.00 64.45  ? 2102 HOH   A O    1 
HETATM 23062 O  O    . HOH   EA 16 .   ? 11.872  -27.312 -45.700  1.00 56.54  ? 2103 HOH   A O    1 
HETATM 23063 O  O    . HOH   EA 16 .   ? 41.978  -19.395 -27.320  1.00 68.41  ? 2104 HOH   A O    1 
HETATM 23064 O  O    . HOH   EA 16 .   ? 16.740  -36.517 -45.215  1.00 57.63  ? 2105 HOH   A O    1 
HETATM 23065 O  O    . HOH   EA 16 .   ? 34.935  -28.982 -39.297  1.00 47.67  ? 2106 HOH   A O    1 
HETATM 23066 O  O    . HOH   EA 16 .   ? 11.258  -10.124 -42.992  1.00 63.22  ? 2107 HOH   A O    1 
HETATM 23067 O  O    . HOH   EA 16 .   ? 25.951  2.832   -29.498  1.00 84.87  ? 2108 HOH   A O    1 
HETATM 23068 O  O    . HOH   EA 16 .   ? 38.233  -6.171  -23.266  1.00 84.02  ? 2109 HOH   A O    1 
HETATM 23069 O  O    . HOH   EA 16 .   ? 3.979   -31.874 -54.350  1.00 50.12  ? 2110 HOH   A O    1 
HETATM 23070 O  O    . HOH   EA 16 .   ? -6.197  -35.192 -35.138  1.00 58.16  ? 2111 HOH   A O    1 
HETATM 23071 O  O    . HOH   EA 16 .   ? 30.940  -34.747 -28.240  1.00 52.90  ? 2112 HOH   A O    1 
HETATM 23072 O  O    . HOH   EA 16 .   ? 3.481   -16.589 -16.125  1.00 54.88  ? 2113 HOH   A O    1 
HETATM 23073 O  O    . HOH   EA 16 .   ? 10.298  -33.542 -25.206  1.00 47.80  ? 2114 HOH   A O    1 
HETATM 23074 O  O    . HOH   EA 16 .   ? 5.843   -37.909 -35.216  1.00 48.82  ? 2115 HOH   A O    1 
HETATM 23075 O  O    . HOH   EA 16 .   ? 19.636  -28.037 -8.458   1.00 48.84  ? 2116 HOH   A O    1 
HETATM 23076 O  O    . HOH   EA 16 .   ? 0.924   -36.773 -26.544  1.00 53.73  ? 2117 HOH   A O    1 
HETATM 23077 O  O    . HOH   EA 16 .   ? 16.666  -21.596 -8.119   1.00 53.21  ? 2118 HOH   A O    1 
HETATM 23078 O  O    . HOH   EA 16 .   ? 9.340   -37.642 -47.917  1.00 56.17  ? 2119 HOH   A O    1 
HETATM 23079 O  O    . HOH   EA 16 .   ? 11.190  -38.112 -29.020  1.00 40.77  ? 2120 HOH   A O    1 
HETATM 23080 O  O    . HOH   EA 16 .   ? 25.419  -39.236 -32.504  1.00 54.64  ? 2121 HOH   A O    1 
HETATM 23081 O  O    . HOH   EA 16 .   ? 25.346  -38.444 -30.164  1.00 52.35  ? 2122 HOH   A O    1 
HETATM 23082 O  O    . HOH   EA 16 .   ? 9.719   -32.197 -42.282  1.00 53.80  ? 2123 HOH   A O    1 
HETATM 23083 O  O    . HOH   EA 16 .   ? 21.284  -19.634 -8.637   1.00 63.89  ? 2124 HOH   A O    1 
HETATM 23084 O  O    . HOH   EA 16 .   ? 22.288  -39.936 -28.951  1.00 63.83  ? 2125 HOH   A O    1 
HETATM 23085 O  O    . HOH   EA 16 .   ? 45.731  -20.426 -23.338  1.00 56.44  ? 2126 HOH   A O    1 
HETATM 23086 O  O    . HOH   EA 16 .   ? 13.773  -12.353 -21.211  1.00 47.41  ? 2127 HOH   A O    1 
HETATM 23087 O  O    . HOH   EA 16 .   ? 21.013  -26.193 -6.774   1.00 55.11  ? 2128 HOH   A O    1 
HETATM 23088 O  O    . HOH   EA 16 .   ? 30.966  -22.660 -40.970  1.00 55.19  ? 2129 HOH   A O    1 
HETATM 23089 O  O    . HOH   EA 16 .   ? 23.751  -38.085 -23.984  1.00 50.93  ? 2130 HOH   A O    1 
HETATM 23090 O  O    . HOH   EA 16 .   ? -4.449  -26.265 -31.667  1.00 35.62  ? 2131 HOH   A O    1 
HETATM 23091 O  O    . HOH   EA 16 .   ? 11.009  -30.389 -36.113  1.00 53.50  ? 2132 HOH   A O    1 
HETATM 23092 O  O    . HOH   EA 16 .   ? 5.422   -36.681 -45.429  1.00 57.03  ? 2133 HOH   A O    1 
HETATM 23093 O  O    . HOH   EA 16 .   ? 4.659   -11.989 -18.810  1.00 48.04  ? 2134 HOH   A O    1 
HETATM 23094 O  O    . HOH   EA 16 .   ? 20.554  -49.810 -24.742  1.00 46.50  ? 2135 HOH   A O    1 
HETATM 23095 O  O    . HOH   EA 16 .   ? 28.804  -26.333 -40.035  1.00 59.86  ? 2136 HOH   A O    1 
HETATM 23096 O  O    . HOH   EA 16 .   ? 5.356   -20.425 -17.372  1.00 46.48  ? 2137 HOH   A O    1 
HETATM 23097 O  O    . HOH   EA 16 .   ? 27.474  -19.100 -31.545  1.00 59.46  ? 2138 HOH   A O    1 
HETATM 23098 O  O    . HOH   EA 16 .   ? 5.215   -38.658 -43.040  1.00 51.11  ? 2139 HOH   A O    1 
HETATM 23099 O  O    . HOH   EA 16 .   ? 2.009   -20.489 -25.771  1.00 49.60  ? 2140 HOH   A O    1 
HETATM 23100 O  O    . HOH   EA 16 .   ? 34.888  -19.581 -34.869  1.00 51.32  ? 2141 HOH   A O    1 
HETATM 23101 O  O    . HOH   EA 16 .   ? 3.804   -40.314 -39.869  1.00 71.34  ? 2142 HOH   A O    1 
HETATM 23102 O  O    . HOH   EA 16 .   ? 29.218  -39.155 -30.104  1.00 51.81  ? 2143 HOH   A O    1 
HETATM 23103 O  O    . HOH   FA 16 .   ? 12.545  -23.115 -16.864  1.00 60.99  ? 2101 HOH   B O    1 
HETATM 23104 O  O    . HOH   FA 16 .   ? -1.497  -45.507 -22.919  1.00 58.23  ? 2102 HOH   B O    1 
HETATM 23105 O  O    . HOH   FA 16 .   ? 11.182  -16.777 -14.955  1.00 59.69  ? 2103 HOH   B O    1 
HETATM 23106 O  O    . HOH   FA 16 .   ? 6.711   -26.742 -9.008   1.00 46.30  ? 2104 HOH   B O    1 
HETATM 23107 O  O    . HOH   FA 16 .   ? 8.973   -44.506 -11.407  1.00 46.67  ? 2105 HOH   B O    1 
HETATM 23108 O  O    . HOH   FA 16 .   ? 7.422   -39.618 22.507   1.00 58.72  ? 2106 HOH   B O    1 
HETATM 23109 O  O    . HOH   FA 16 .   ? 10.952  -37.799 -8.528   1.00 47.89  ? 2107 HOH   B O    1 
HETATM 23110 O  O    . HOH   FA 16 .   ? 12.530  -24.034 -9.522   1.00 52.35  ? 2108 HOH   B O    1 
HETATM 23111 O  O    . HOH   FA 16 .   ? 4.969   -34.483 -9.578   1.00 50.65  ? 2109 HOH   B O    1 
HETATM 23112 O  O    . HOH   FA 16 .   ? 8.451   -46.131 -13.896  1.00 48.96  ? 2110 HOH   B O    1 
HETATM 23113 O  O    . HOH   FA 16 .   ? 4.304   -31.583 -9.971   1.00 55.81  ? 2111 HOH   B O    1 
HETATM 23114 O  O    . HOH   FA 16 .   ? 11.268  -40.470 -8.944   1.00 48.25  ? 2112 HOH   B O    1 
HETATM 23115 O  O    . HOH   FA 16 .   ? 17.664  -36.897 -11.440  1.00 57.80  ? 2113 HOH   B O    1 
HETATM 23116 O  O    . HOH   FA 16 .   ? 8.922   -59.307 -1.658   1.00 60.08  ? 2114 HOH   B O    1 
HETATM 23117 O  O    . HOH   FA 16 .   ? 3.240   -28.293 -22.281  1.00 45.35  ? 2115 HOH   B O    1 
HETATM 23118 O  O    . HOH   FA 16 .   ? -0.430  -31.787 -8.203   1.00 51.32  ? 2116 HOH   B O    1 
HETATM 23119 O  O    . HOH   FA 16 .   ? -3.597  -38.434 -17.524  1.00 57.41  ? 2117 HOH   B O    1 
HETATM 23120 O  O    . HOH   FA 16 .   ? 11.186  -34.437 -9.354   1.00 51.36  ? 2118 HOH   B O    1 
HETATM 23121 O  O    . HOH   FA 16 .   ? 9.480   -43.899 -14.280  1.00 45.51  ? 2119 HOH   B O    1 
HETATM 23122 O  O    . HOH   FA 16 .   ? 14.492  -20.288 -15.027  1.00 59.02  ? 2120 HOH   B O    1 
HETATM 23123 O  O    . HOH   FA 16 .   ? 9.750   -50.639 -8.659   1.00 51.75  ? 2121 HOH   B O    1 
HETATM 23124 O  O    . HOH   FA 16 .   ? 3.836   -20.251 -15.259  1.00 53.31  ? 2122 HOH   B O    1 
HETATM 23125 O  O    . HOH   FA 16 .   ? -6.040  -40.111 17.888   1.00 61.88  ? 2123 HOH   B O    1 
HETATM 23126 O  O    . HOH   FA 16 .   ? 12.337  -41.384 -20.450  1.00 46.04  ? 2124 HOH   B O    1 
HETATM 23127 O  O    . HOH   FA 16 .   ? 36.086  -25.383 17.740   1.00 63.05  ? 2125 HOH   B O    1 
HETATM 23128 O  O    . HOH   FA 16 .   ? 8.493   -54.244 4.487    1.00 48.78  ? 2126 HOH   B O    1 
HETATM 23129 O  O    . HOH   FA 16 .   ? 10.432  -50.299 -6.408   1.00 52.98  ? 2127 HOH   B O    1 
HETATM 23130 O  O    . HOH   FA 16 .   ? 14.518  -43.385 -20.041  1.00 57.83  ? 2128 HOH   B O    1 
HETATM 23131 O  O    . HOH   FA 16 .   ? 8.736   -53.340 -10.646  1.00 75.88  ? 2129 HOH   B O    1 
HETATM 23132 O  O    . HOH   FA 16 .   ? 2.877   -23.993 -21.555  1.00 46.38  ? 2130 HOH   B O    1 
HETATM 23133 O  O    . HOH   FA 16 .   ? 11.492  -46.156 -13.762  1.00 53.77  ? 2131 HOH   B O    1 
HETATM 23134 O  O    . HOH   FA 16 .   ? 13.341  -19.672 -3.623   1.00 59.96  ? 2132 HOH   B O    1 
HETATM 23135 O  O    . HOH   GA 16 .   ? 17.500  -64.323 -60.142  1.00 74.58  ? 401  HOH   D O    1 
HETATM 23136 O  O    . HOH   GA 16 .   ? 17.510  -56.010 -52.826  1.00 60.36  ? 402  HOH   D O    1 
HETATM 23137 O  O    . HOH   GA 16 .   ? 14.228  -53.772 -44.538  1.00 53.31  ? 403  HOH   D O    1 
HETATM 23138 O  O    . HOH   GA 16 .   ? 21.332  -41.954 -44.026  1.00 49.74  ? 404  HOH   D O    1 
HETATM 23139 O  O    . HOH   GA 16 .   ? 19.317  -74.829 -92.517  1.00 67.02  ? 405  HOH   D O    1 
HETATM 23140 O  O    . HOH   GA 16 .   ? 20.179  -57.872 -40.995  1.00 55.12  ? 406  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   ? 0.9651 0.6531 1.0303 -0.3001 -0.2531 0.0544  1   PHE A N   
2     C CA  . PHE A 1   ? 1.0101 0.6508 1.0678 -0.3054 -0.2701 0.0380  1   PHE A CA  
3     C C   . PHE A 1   ? 1.0902 0.6701 1.1359 -0.3076 -0.2791 0.0454  1   PHE A C   
4     O O   . PHE A 1   ? 1.1405 0.6740 1.1769 -0.3049 -0.2929 0.0304  1   PHE A O   
5     C CB  . PHE A 1   ? 1.0129 0.6663 1.0832 -0.3341 -0.2784 0.0363  1   PHE A CB  
6     C CG  . PHE A 1   ? 1.0526 0.7135 1.1338 -0.3632 -0.2763 0.0601  1   PHE A CG  
7     C CD1 . PHE A 1   ? 1.1441 0.7536 1.2192 -0.3825 -0.2874 0.0690  1   PHE A CD1 
8     C CD2 . PHE A 1   ? 1.0646 0.7837 1.1615 -0.3713 -0.2631 0.0735  1   PHE A CD2 
9     C CE1 . PHE A 1   ? 1.2288 0.8463 1.3127 -0.4111 -0.2846 0.0920  1   PHE A CE1 
10    C CE2 . PHE A 1   ? 1.1469 0.8769 1.2539 -0.3985 -0.2598 0.0950  1   PHE A CE2 
11    C CZ  . PHE A 1   ? 1.2303 0.9101 1.3304 -0.4193 -0.2701 0.1049  1   PHE A CZ  
23    N N   . ASN A 2   ? 1.0921 0.6713 1.1366 -0.3117 -0.2719 0.0682  2   ASN A N   
24    C CA  . ASN A 2   ? 1.1418 0.6650 1.1753 -0.3190 -0.2812 0.0804  2   ASN A CA  
25    C C   . ASN A 2   ? 1.1643 0.6625 1.1845 -0.2905 -0.2796 0.0801  2   ASN A C   
26    O O   . ASN A 2   ? 1.2225 0.6755 1.2326 -0.2933 -0.2872 0.0922  2   ASN A O   
27    C CB  . ASN A 2   ? 1.1291 0.6647 1.1684 -0.3469 -0.2760 0.1082  2   ASN A CB  
28    C CG  . ASN A 2   ? 1.0666 0.6557 1.1113 -0.3392 -0.2575 0.1219  2   ASN A CG  
29    O OD1 . ASN A 2   ? 1.0048 0.6391 1.0574 -0.3250 -0.2480 0.1112  2   ASN A OD1 
30    N ND2 . ASN A 2   ? 1.0971 0.6798 1.1361 -0.3484 -0.2527 0.1455  2   ASN A ND2 
37    N N   . LEU A 3   ? 1.1211 0.6473 1.1412 -0.2636 -0.2707 0.0671  3   LEU A N   
38    C CA  . LEU A 3   ? 1.1138 0.6197 1.1235 -0.2365 -0.2696 0.0651  3   LEU A CA  
39    C C   . LEU A 3   ? 1.1970 0.6451 1.1968 -0.2256 -0.2856 0.0484  3   LEU A C   
40    O O   . LEU A 3   ? 1.2326 0.6718 1.2329 -0.2261 -0.2931 0.0280  3   LEU A O   
41    C CB  . LEU A 3   ? 0.9961 0.5468 1.0091 -0.2124 -0.2563 0.0541  3   LEU A CB  
42    C CG  . LEU A 3   ? 0.9667 0.5651 0.9855 -0.2128 -0.2402 0.0712  3   LEU A CG  
43    C CD1 . LEU A 3   ? 0.8963 0.5341 0.9180 -0.1906 -0.2291 0.0579  3   LEU A CD1 
44    C CD2 . LEU A 3   ? 0.9739 0.5529 0.9847 -0.2093 -0.2392 0.0902  3   LEU A CD2 
56    N N   . ASP A 4   ? 1.2321 0.6409 1.2222 -0.2147 -0.2914 0.0567  4   ASP A N   
57    C CA  . ASP A 4   ? 1.2552 0.6059 1.2360 -0.2016 -0.3072 0.0420  4   ASP A CA  
58    C C   . ASP A 4   ? 1.2582 0.6213 1.2382 -0.1678 -0.3029 0.0198  4   ASP A C   
59    O O   . ASP A 4   ? 1.2065 0.5814 1.1853 -0.1489 -0.2959 0.0259  4   ASP A O   
60    C CB  . ASP A 4   ? 1.2583 0.5605 1.2293 -0.2049 -0.3167 0.0620  4   ASP A CB  
61    C CG  . ASP A 4   ? 1.3026 0.5421 1.2642 -0.1885 -0.3341 0.0467  4   ASP A CG  
62    O OD1 . ASP A 4   ? 1.2800 0.5219 1.2412 -0.1583 -0.3331 0.0277  4   ASP A OD1 
63    O OD2 . ASP A 4   ? 1.4018 0.5897 1.3570 -0.2060 -0.3489 0.0535  4   ASP A OD2 
68    N N   . VAL A 5   ? 1.3105 0.6720 1.2906 -0.1609 -0.3069 -0.0060 5   VAL A N   
69    C CA  . VAL A 5   ? 1.3114 0.6852 1.2901 -0.1304 -0.3026 -0.0288 5   VAL A CA  
70    C C   . VAL A 5   ? 1.4182 0.7372 1.3890 -0.1125 -0.3173 -0.0460 5   VAL A C   
71    O O   . VAL A 5   ? 1.4825 0.8090 1.4526 -0.0851 -0.3140 -0.0643 5   VAL A O   
72    C CB  . VAL A 5   ? 1.2170 0.6303 1.1991 -0.1312 -0.2958 -0.0476 5   VAL A CB  
73    C CG1 . VAL A 5   ? 1.1063 0.5736 1.0972 -0.1466 -0.2821 -0.0314 5   VAL A CG1 
74    C CG2 . VAL A 5   ? 1.2378 0.6198 1.2159 -0.1453 -0.3100 -0.0633 5   VAL A CG2 
84    N N   . ASP A 6   ? 1.4483 0.7124 1.4134 -0.1269 -0.3334 -0.0408 6   ASP A N   
85    C CA  . ASP A 6   ? 1.4921 0.7000 1.4494 -0.1095 -0.3490 -0.0592 6   ASP A CA  
86    C C   . ASP A 6   ? 1.4949 0.6866 1.4505 -0.0837 -0.3502 -0.0531 6   ASP A C   
87    O O   . ASP A 6   ? 1.5137 0.6891 1.4676 -0.0561 -0.3549 -0.0747 6   ASP A O   
88    C CB  . ASP A 6   ? 1.5562 0.7067 1.5074 -0.1338 -0.3668 -0.0534 6   ASP A CB  
89    C CG  . ASP A 6   ? 1.6115 0.7774 1.5657 -0.1597 -0.3677 -0.0609 6   ASP A CG  
90    O OD1 . ASP A 6   ? 1.5992 0.7996 1.5555 -0.1504 -0.3610 -0.0826 6   ASP A OD1 
91    O OD2 . ASP A 6   ? 1.6731 0.8177 1.6275 -0.1899 -0.3752 -0.0448 6   ASP A OD2 
96    N N   . SER A 7   ? 1.4793 0.6770 1.4353 -0.0919 -0.3462 -0.0246 7   SER A N   
97    C CA  . SER A 7   ? 1.4605 0.6417 1.4140 -0.0699 -0.3492 -0.0157 7   SER A CA  
98    C C   . SER A 7   ? 1.3723 0.6001 1.3297 -0.0747 -0.3342 0.0081  7   SER A C   
99    O O   . SER A 7   ? 1.3558 0.5676 1.3076 -0.0887 -0.3373 0.0345  7   SER A O   
100   C CB  . SER A 7   ? 1.5664 0.6764 1.5097 -0.0757 -0.3691 -0.0041 7   SER A CB  
101   O OG  . SER A 7   ? 1.6389 0.7365 1.5783 -0.1113 -0.3716 0.0187  7   SER A OG  
107   N N   . PRO A 8   ? 1.3122 0.5973 1.2777 -0.0637 -0.3178 -0.0006 8   PRO A N   
108   C CA  . PRO A 8   ? 1.2569 0.5859 1.2259 -0.0655 -0.3038 0.0191  8   PRO A CA  
109   C C   . PRO A 8   ? 1.2553 0.5808 1.2239 -0.0393 -0.3050 0.0214  8   PRO A C   
110   O O   . PRO A 8   ? 1.3061 0.6136 1.2762 -0.0146 -0.3118 0.0024  8   PRO A O   
111   C CB  . PRO A 8   ? 1.1976 0.5841 1.1750 -0.0644 -0.2876 0.0060  8   PRO A CB  
112   C CG  . PRO A 8   ? 1.1997 0.5753 1.1777 -0.0457 -0.2922 -0.0239 8   PRO A CG  
113   C CD  . PRO A 8   ? 1.2757 0.5881 1.2463 -0.0508 -0.3113 -0.0288 8   PRO A CD  
121   N N   . ALA A 9   ? 1.1983 0.5435 1.1655 -0.0448 -0.2984 0.0446  9   ALA A N   
122   C CA  . ALA A 9   ? 1.1812 0.5292 1.1484 -0.0217 -0.2993 0.0486  9   ALA A CA  
123   C C   . ALA A 9   ? 1.1697 0.5674 1.1480 -0.0014 -0.2859 0.0302  9   ALA A C   
124   O O   . ALA A 9   ? 1.1405 0.5831 1.1238 -0.0108 -0.2712 0.0294  9   ALA A O   
125   C CB  . ALA A 9   ? 1.1819 0.5381 1.1423 -0.0347 -0.2961 0.0782  9   ALA A CB  
131   N N   . GLU A 10  ? 1.1987 0.5884 1.1812 0.0262  -0.2912 0.0159  10  GLU A N   
132   C CA  . GLU A 10  ? 1.1956 0.6284 1.1891 0.0461  -0.2797 -0.0040 10  GLU A CA  
133   C C   . GLU A 10  ? 1.1499 0.5964 1.1479 0.0658  -0.2796 0.0017  10  GLU A C   
134   O O   . GLU A 10  ? 1.1806 0.5911 1.1761 0.0792  -0.2939 0.0049  10  GLU A O   
135   C CB  . GLU A 10  ? 1.2722 0.6883 1.2688 0.0617  -0.2851 -0.0327 10  GLU A CB  
136   C CG  . GLU A 10  ? 1.3247 0.7823 1.3321 0.0838  -0.2741 -0.0541 10  GLU A CG  
137   C CD  . GLU A 10  ? 1.3958 0.8379 1.4044 0.0981  -0.2788 -0.0829 10  GLU A CD  
138   O OE1 . GLU A 10  ? 1.4151 0.8211 1.4157 0.0865  -0.2881 -0.0872 10  GLU A OE1 
139   O OE2 . GLU A 10  ? 1.4036 0.8702 1.4209 0.1205  -0.2732 -0.1016 10  GLU A OE2 
146   N N   . TYR A 11  ? 1.0880 0.5856 1.0928 0.0675  -0.2645 0.0028  11  TYR A N   
147   C CA  . TYR A 11  ? 1.0965 0.6148 1.1067 0.0837  -0.2630 0.0079  11  TYR A CA  
148   C C   . TYR A 11  ? 1.0755 0.6369 1.0991 0.1006  -0.2514 -0.0132 11  TYR A C   
149   O O   . TYR A 11  ? 1.0444 0.6343 1.0703 0.0923  -0.2388 -0.0221 11  TYR A O   
150   C CB  . TYR A 11  ? 1.1021 0.6415 1.1065 0.0673  -0.2558 0.0323  11  TYR A CB  
151   C CG  . TYR A 11  ? 1.1356 0.6371 1.1260 0.0493  -0.2657 0.0554  11  TYR A CG  
152   C CD1 . TYR A 11  ? 1.1689 0.6598 1.1533 0.0251  -0.2637 0.0617  11  TYR A CD1 
153   C CD2 . TYR A 11  ? 1.1725 0.6499 1.1554 0.0556  -0.2772 0.0714  11  TYR A CD2 
154   C CE1 . TYR A 11  ? 1.2222 0.6805 1.1943 0.0065  -0.2719 0.0835  11  TYR A CE1 
155   C CE2 . TYR A 11  ? 1.2507 0.6932 1.2189 0.0377  -0.2858 0.0941  11  TYR A CE2 
156   C CZ  . TYR A 11  ? 1.2521 0.6855 1.2152 0.0125  -0.2825 0.1001  11  TYR A CZ  
157   O OH  . TYR A 11  ? 1.2509 0.6514 1.1998 -0.0074 -0.2902 0.1233  11  TYR A OH  
167   N N   . SER A 12  ? 1.0643 0.6311 1.0967 0.1239  -0.2559 -0.0205 12  SER A N   
168   C CA  . SER A 12  ? 1.0359 0.6434 1.0825 0.1407  -0.2456 -0.0407 12  SER A CA  
169   C C   . SER A 12  ? 0.9800 0.6200 1.0343 0.1486  -0.2415 -0.0324 12  SER A C   
170   O O   . SER A 12  ? 0.9883 0.6117 1.0379 0.1495  -0.2512 -0.0153 12  SER A O   
171   C CB  . SER A 12  ? 1.0903 0.6787 1.1443 0.1643  -0.2545 -0.0639 12  SER A CB  
172   O OG  . SER A 12  ? 1.1799 0.7430 1.2368 0.1817  -0.2698 -0.0589 12  SER A OG  
178   N N   . GLY A 13  ? 0.9302 0.6165 0.9956 0.1535  -0.2274 -0.0442 13  GLY A N   
179   C CA  . GLY A 13  ? 0.8758 0.5965 0.9506 0.1608  -0.2230 -0.0399 13  GLY A CA  
180   C C   . GLY A 13  ? 0.8782 0.6309 0.9706 0.1807  -0.2175 -0.0620 13  GLY A C   
181   O O   . GLY A 13  ? 0.9474 0.6969 1.0436 0.1892  -0.2160 -0.0813 13  GLY A O   
185   N N   . PRO A 14  ? 0.8490 0.6347 0.9526 0.1880  -0.2142 -0.0601 14  PRO A N   
186   C CA  . PRO A 14  ? 0.8447 0.6661 0.9674 0.2057  -0.2082 -0.0806 14  PRO A CA  
187   C C   . PRO A 14  ? 0.8202 0.6678 0.9440 0.1984  -0.1917 -0.0951 14  PRO A C   
188   O O   . PRO A 14  ? 0.7867 0.6446 0.9009 0.1789  -0.1812 -0.0865 14  PRO A O   
189   C CB  . PRO A 14  ? 0.8189 0.6734 0.9504 0.2061  -0.2058 -0.0715 14  PRO A CB  
190   C CG  . PRO A 14  ? 0.8204 0.6454 0.9380 0.1982  -0.2173 -0.0486 14  PRO A CG  
191   C CD  . PRO A 14  ? 0.8373 0.6292 0.9366 0.1806  -0.2168 -0.0397 14  PRO A CD  
199   N N   . GLU A 15  ? 0.8361 0.6948 0.9711 0.2153  -0.1898 -0.1175 15  GLU A N   
200   C CA  . GLU A 15  ? 0.8929 0.7765 1.0273 0.2099  -0.1746 -0.1323 15  GLU A CA  
201   C C   . GLU A 15  ? 0.8748 0.8048 1.0147 0.1990  -0.1590 -0.1279 15  GLU A C   
202   O O   . GLU A 15  ? 0.8763 0.8345 1.0315 0.2072  -0.1578 -0.1287 15  GLU A O   
203   C CB  . GLU A 15  ? 0.9689 0.8600 1.1152 0.2322  -0.1752 -0.1580 15  GLU A CB  
204   C CG  . GLU A 15  ? 1.0399 0.9579 1.1837 0.2278  -0.1594 -0.1746 15  GLU A CG  
205   C CD  . GLU A 15  ? 1.1613 1.0869 1.3157 0.2507  -0.1597 -0.2012 15  GLU A CD  
206   O OE1 . GLU A 15  ? 1.2165 1.1199 1.3598 0.2522  -0.1612 -0.2140 15  GLU A OE1 
207   O OE2 . GLU A 15  ? 1.1757 1.1307 1.3502 0.2675  -0.1586 -0.2103 15  GLU A OE2 
214   N N   . GLY A 16  ? 0.8661 0.8032 0.9938 0.1803  -0.1478 -0.1234 16  GLY A N   
215   C CA  . GLY A 16  ? 0.8508 0.8263 0.9810 0.1685  -0.1333 -0.1187 16  GLY A CA  
216   C C   . GLY A 16  ? 0.8285 0.8032 0.9541 0.1551  -0.1344 -0.0974 16  GLY A C   
217   O O   . GLY A 16  ? 0.7803 0.7840 0.9078 0.1454  -0.1235 -0.0932 16  GLY A O   
221   N N   . SER A 17  ? 0.8481 0.7900 0.9666 0.1538  -0.1470 -0.0840 17  SER A N   
222   C CA  . SER A 17  ? 0.8177 0.7584 0.9300 0.1418  -0.1484 -0.0643 17  SER A CA  
223   C C   . SER A 17  ? 0.8139 0.7429 0.9101 0.1221  -0.1434 -0.0524 17  SER A C   
224   O O   . SER A 17  ? 0.8038 0.7329 0.8937 0.1115  -0.1431 -0.0367 17  SER A O   
225   C CB  . SER A 17  ? 0.8594 0.7728 0.9710 0.1502  -0.1644 -0.0544 17  SER A CB  
226   O OG  . SER A 17  ? 0.8822 0.7549 0.9828 0.1490  -0.1739 -0.0517 17  SER A OG  
232   N N   . TYR A 18  ? 0.8371 0.7577 0.9267 0.1175  -0.1397 -0.0602 18  TYR A N   
233   C CA  . TYR A 18  ? 0.8386 0.7492 0.9147 0.0998  -0.1363 -0.0501 18  TYR A CA  
234   C C   . TYR A 18  ? 0.8119 0.6913 0.8796 0.0929  -0.1471 -0.0338 18  TYR A C   
235   O O   . TYR A 18  ? 0.7544 0.6344 0.8143 0.0784  -0.1440 -0.0199 18  TYR A O   
236   C CB  . TYR A 18  ? 0.8173 0.7570 0.8919 0.0884  -0.1238 -0.0436 18  TYR A CB  
237   C CG  . TYR A 18  ? 0.7906 0.7568 0.8681 0.0893  -0.1121 -0.0568 18  TYR A CG  
238   C CD1 . TYR A 18  ? 0.7583 0.7275 0.8409 0.1012  -0.1119 -0.0745 18  TYR A CD1 
239   C CD2 . TYR A 18  ? 0.7777 0.7651 0.8514 0.0782  -0.1014 -0.0514 18  TYR A CD2 
240   C CE1 . TYR A 18  ? 0.7554 0.7503 0.8386 0.1008  -0.1004 -0.0856 18  TYR A CE1 
241   C CE2 . TYR A 18  ? 0.7558 0.7657 0.8298 0.0776  -0.0909 -0.0614 18  TYR A CE2 
242   C CZ  . TYR A 18  ? 0.7575 0.7721 0.8358 0.0883  -0.0900 -0.0781 18  TYR A CZ  
243   O OH  . TYR A 18  ? 0.7263 0.7648 0.8030 0.0867  -0.0787 -0.0873 18  TYR A OH  
253   N N   . PHE A 19  ? 0.8473 0.6997 0.9167 0.1038  -0.1598 -0.0356 19  PHE A N   
254   C CA  . PHE A 19  ? 0.8493 0.6676 0.9090 0.0966  -0.1709 -0.0201 19  PHE A CA  
255   C C   . PHE A 19  ? 0.8161 0.6196 0.8657 0.0801  -0.1694 -0.0168 19  PHE A C   
256   O O   . PHE A 19  ? 0.8159 0.6086 0.8649 0.0823  -0.1707 -0.0302 19  PHE A O   
257   C CB  . PHE A 19  ? 0.8981 0.6860 0.9607 0.1124  -0.1856 -0.0251 19  PHE A CB  
258   C CG  . PHE A 19  ? 0.9245 0.6724 0.9757 0.1044  -0.1981 -0.0088 19  PHE A CG  
259   C CD1 . PHE A 19  ? 0.9300 0.6468 0.9734 0.0958  -0.2034 -0.0101 19  PHE A CD1 
260   C CD2 . PHE A 19  ? 0.9148 0.6561 0.9621 0.1047  -0.2047 0.0079  19  PHE A CD2 
261   C CE1 . PHE A 19  ? 0.9380 0.6175 0.9708 0.0864  -0.2147 0.0059  19  PHE A CE1 
262   C CE2 . PHE A 19  ? 0.9399 0.6443 0.9749 0.0960  -0.2158 0.0244  19  PHE A CE2 
263   C CZ  . PHE A 19  ? 0.9475 0.6207 0.9757 0.0863  -0.2205 0.0238  19  PHE A CZ  
273   N N   . GLY A 20  ? 0.7855 0.5905 0.8277 0.0638  -0.1666 0.0003  20  GLY A N   
274   C CA  . GLY A 20  ? 0.7723 0.5701 0.8073 0.0470  -0.1645 0.0047  20  GLY A CA  
275   C C   . GLY A 20  ? 0.7482 0.5785 0.7832 0.0374  -0.1512 0.0058  20  GLY A C   
276   O O   . GLY A 20  ? 0.6911 0.5202 0.7217 0.0241  -0.1493 0.0090  20  GLY A O   
280   N N   . PHE A 21  ? 0.7514 0.6103 0.7916 0.0438  -0.1428 0.0033  21  PHE A N   
281   C CA  . PHE A 21  ? 0.7482 0.6347 0.7875 0.0353  -0.1311 0.0055  21  PHE A CA  
282   C C   . PHE A 21  ? 0.7347 0.6213 0.7682 0.0211  -0.1298 0.0222  21  PHE A C   
283   O O   . PHE A 21  ? 0.7095 0.6105 0.7412 0.0119  -0.1230 0.0244  21  PHE A O   
284   C CB  . PHE A 21  ? 0.7446 0.6572 0.7903 0.0437  -0.1238 0.0012  21  PHE A CB  
285   C CG  . PHE A 21  ? 0.6939 0.6317 0.7384 0.0370  -0.1124 0.0011  21  PHE A CG  
286   C CD1 . PHE A 21  ? 0.6987 0.6473 0.7433 0.0382  -0.1066 -0.0106 21  PHE A CD1 
287   C CD2 . PHE A 21  ? 0.6864 0.6361 0.7285 0.0299  -0.1078 0.0126  21  PHE A CD2 
288   C CE1 . PHE A 21  ? 0.6735 0.6421 0.7154 0.0321  -0.0972 -0.0093 21  PHE A CE1 
289   C CE2 . PHE A 21  ? 0.6753 0.6446 0.7160 0.0249  -0.0984 0.0125  21  PHE A CE2 
290   C CZ  . PHE A 21  ? 0.6483 0.6261 0.6887 0.0258  -0.0935 0.0023  21  PHE A CZ  
300   N N   . ALA A 22  ? 0.7369 0.6088 0.7673 0.0198  -0.1364 0.0342  22  ALA A N   
301   C CA  . ALA A 22  ? 0.7538 0.6259 0.7779 0.0062  -0.1352 0.0504  22  ALA A CA  
302   C C   . ALA A 22  ? 0.7606 0.6013 0.7790 0.0021  -0.1464 0.0602  22  ALA A C   
303   O O   . ALA A 22  ? 0.7737 0.5967 0.7923 0.0130  -0.1549 0.0585  22  ALA A O   
304   C CB  . ALA A 22  ? 0.7075 0.6007 0.7304 0.0075  -0.1291 0.0577  22  ALA A CB  
310   N N   . VAL A 23  ? 0.7249 0.5589 0.7387 -0.0136 -0.1467 0.0707  23  VAL A N   
311   C CA  . VAL A 23  ? 0.7796 0.5823 0.7868 -0.0213 -0.1570 0.0821  23  VAL A CA  
312   C C   . VAL A 23  ? 0.8039 0.6160 0.8052 -0.0380 -0.1525 0.0996  23  VAL A C   
313   O O   . VAL A 23  ? 0.8422 0.6803 0.8469 -0.0460 -0.1430 0.0999  23  VAL A O   
314   C CB  . VAL A 23  ? 0.7779 0.5551 0.7864 -0.0255 -0.1646 0.0739  23  VAL A CB  
315   C CG1 . VAL A 23  ? 0.7857 0.5492 0.7983 -0.0075 -0.1705 0.0571  23  VAL A CG1 
316   C CG2 . VAL A 23  ? 0.7528 0.5499 0.7656 -0.0363 -0.1573 0.0686  23  VAL A CG2 
326   N N   . ASP A 24  ? 0.8244 0.6158 0.8165 -0.0426 -0.1594 0.1143  24  ASP A N   
327   C CA  . ASP A 24  ? 0.8424 0.6409 0.8275 -0.0599 -0.1554 0.1320  24  ASP A CA  
328   C C   . ASP A 24  ? 0.8329 0.5952 0.8070 -0.0667 -0.1670 0.1467  24  ASP A C   
329   O O   . ASP A 24  ? 0.8162 0.5488 0.7883 -0.0555 -0.1783 0.1431  24  ASP A O   
330   C CB  . ASP A 24  ? 0.8323 0.6620 0.8142 -0.0571 -0.1456 0.1372  24  ASP A CB  
331   C CG  . ASP A 24  ? 0.8965 0.7456 0.8748 -0.0743 -0.1373 0.1502  24  ASP A CG  
332   O OD1 . ASP A 24  ? 0.9610 0.7980 0.9388 -0.0899 -0.1400 0.1580  24  ASP A OD1 
333   O OD2 . ASP A 24  ? 0.9267 0.8040 0.9034 -0.0724 -0.1279 0.1518  24  ASP A OD2 
338   N N   . PHE A 25  ? 0.8382 0.6035 0.8053 -0.0853 -0.1639 0.1636  25  PHE A N   
339   C CA  . PHE A 25  ? 0.9003 0.6337 0.8539 -0.0952 -0.1733 0.1817  25  PHE A CA  
340   C C   . PHE A 25  ? 0.9368 0.6809 0.8774 -0.0920 -0.1709 0.1952  25  PHE A C   
341   O O   . PHE A 25  ? 0.9047 0.6851 0.8468 -0.0893 -0.1594 0.1930  25  PHE A O   
342   C CB  . PHE A 25  ? 0.9064 0.6377 0.8595 -0.1203 -0.1712 0.1934  25  PHE A CB  
343   C CG  . PHE A 25  ? 0.9100 0.6174 0.8713 -0.1264 -0.1788 0.1839  25  PHE A CG  
344   C CD1 . PHE A 25  ? 0.9539 0.6131 0.9080 -0.1290 -0.1936 0.1886  25  PHE A CD1 
345   C CD2 . PHE A 25  ? 0.8815 0.6132 0.8565 -0.1294 -0.1720 0.1701  25  PHE A CD2 
346   C CE1 . PHE A 25  ? 0.9640 0.5996 0.9247 -0.1347 -0.2012 0.1784  25  PHE A CE1 
347   C CE2 . PHE A 25  ? 0.8883 0.5986 0.8695 -0.1354 -0.1796 0.1605  25  PHE A CE2 
348   C CZ  . PHE A 25  ? 0.9389 0.6011 0.9130 -0.1383 -0.1941 0.1641  25  PHE A CZ  
358   N N   . PHE A 26  ? 0.9990 0.7098 0.9256 -0.0921 -0.1825 0.2089  26  PHE A N   
359   C CA  . PHE A 26  ? 1.0072 0.7240 0.9178 -0.0908 -0.1823 0.2240  26  PHE A CA  
360   C C   . PHE A 26  ? 1.0603 0.7546 0.9545 -0.1116 -0.1864 0.2476  26  PHE A C   
361   O O   . PHE A 26  ? 1.0752 0.7271 0.9649 -0.1156 -0.1994 0.2538  26  PHE A O   
362   C CB  . PHE A 26  ? 1.0550 0.7545 0.9623 -0.0684 -0.1939 0.2193  26  PHE A CB  
363   C CG  . PHE A 26  ? 1.0637 0.7746 0.9551 -0.0650 -0.1939 0.2320  26  PHE A CG  
364   C CD1 . PHE A 26  ? 1.0238 0.7719 0.9098 -0.0739 -0.1798 0.2370  26  PHE A CD1 
365   C CD2 . PHE A 26  ? 1.0868 0.7711 0.9679 -0.0520 -0.2086 0.2383  26  PHE A CD2 
366   C CE1 . PHE A 26  ? 1.0210 0.7796 0.8905 -0.0707 -0.1801 0.2474  26  PHE A CE1 
367   C CE2 . PHE A 26  ? 1.0792 0.7745 0.9441 -0.0489 -0.2096 0.2499  26  PHE A CE2 
368   C CZ  . PHE A 26  ? 1.0523 0.7846 0.9106 -0.0588 -0.1951 0.2542  26  PHE A CZ  
378   N N   . VAL A 27  ? 1.0953 0.8176 0.9800 -0.1248 -0.1752 0.2607  27  VAL A N   
379   C CA  . VAL A 27  ? 1.1628 0.8706 1.0308 -0.1471 -0.1763 0.2846  27  VAL A CA  
380   C C   . VAL A 27  ? 1.1292 0.8481 0.9759 -0.1452 -0.1744 0.2995  27  VAL A C   
381   O O   . VAL A 27  ? 1.0026 0.7594 0.8452 -0.1544 -0.1602 0.3042  27  VAL A O   
382   C CB  . VAL A 27  ? 1.2475 0.9824 1.1247 -0.1696 -0.1632 0.2873  27  VAL A CB  
383   C CG1 . VAL A 27  ? 1.2248 0.9368 1.1170 -0.1767 -0.1696 0.2787  27  VAL A CG1 
384   C CG2 . VAL A 27  ? 1.2922 1.0797 1.1811 -0.1632 -0.1469 0.2739  27  VAL A CG2 
394   N N   . PRO A 28  ? 1.2819 0.9701 1.1145 -0.1329 -0.1887 0.3065  28  PRO A N   
395   C CA  . PRO A 28  ? 1.3763 1.0737 1.1859 -0.1320 -0.1883 0.3217  28  PRO A CA  
396   C C   . PRO A 28  ? 1.4666 1.1748 1.2598 -0.1584 -0.1789 0.3436  28  PRO A C   
397   O O   . PRO A 28  ? 1.4803 1.1654 1.2720 -0.1777 -0.1815 0.3556  28  PRO A O   
398   C CB  . PRO A 28  ? 1.4491 1.0999 1.2464 -0.1194 -0.2090 0.3298  28  PRO A CB  
399   C CG  . PRO A 28  ? 1.4214 1.0536 1.2409 -0.1035 -0.2170 0.3091  28  PRO A CG  
400   C CD  . PRO A 28  ? 1.3488 0.9927 1.1855 -0.1185 -0.2065 0.3005  28  PRO A CD  
408   N N   . SER A 29  ? 1.5485 1.2931 1.3294 -0.1595 -0.1677 0.3480  29  SER A N   
409   C CA  . SER A 29  ? 1.6521 1.4189 1.4195 -0.1835 -0.1548 0.3655  29  SER A CA  
410   C C   . SER A 29  ? 1.7402 1.4759 1.4765 -0.1950 -0.1645 0.3934  29  SER A C   
411   O O   . SER A 29  ? 1.7703 1.5253 1.4841 -0.1999 -0.1585 0.4061  29  SER A O   
412   C CB  . SER A 29  ? 1.6673 1.4874 1.4346 -0.1787 -0.1380 0.3562  29  SER A CB  
413   O OG  . SER A 29  ? 1.7015 1.5481 1.4579 -0.2009 -0.1239 0.3709  29  SER A OG  
419   N N   . ALA A 30  ? 1.7841 1.4688 1.5183 -0.1990 -0.1805 0.4028  30  ALA A N   
420   C CA  . ALA A 30  ? 1.8511 1.4996 1.5567 -0.2145 -0.1904 0.4318  30  ALA A CA  
421   C C   . ALA A 30  ? 1.9970 1.6047 1.7083 -0.2335 -0.1981 0.4412  30  ALA A C   
422   O O   . ALA A 30  ? 2.1225 1.6845 1.8139 -0.2411 -0.2118 0.4614  30  ALA A O   
423   C CB  . ALA A 30  ? 1.7895 1.4053 1.4772 -0.1933 -0.2092 0.4370  30  ALA A CB  
429   N N   . SER A 31  ? 1.9550 1.5781 1.6931 -0.2408 -0.1898 0.4259  31  SER A N   
430   C CA  . SER A 31  ? 1.9203 1.5036 1.6674 -0.2561 -0.1988 0.4294  31  SER A CA  
431   C C   . SER A 31  ? 1.9166 1.4406 1.6603 -0.2379 -0.2217 0.4268  31  SER A C   
432   O O   . SER A 31  ? 1.9248 1.4001 1.6626 -0.2502 -0.2344 0.4384  31  SER A O   
433   C CB  . SER A 31  ? 1.9083 1.4828 1.6384 -0.2902 -0.1950 0.4576  31  SER A CB  
434   O OG  . SER A 31  ? 1.8969 1.4565 1.6000 -0.2872 -0.1995 0.4730  31  SER A OG  
440   N N   . SER A 32  ? 1.8841 1.4135 1.6329 -0.2078 -0.2269 0.4101  32  SER A N   
441   C CA  . SER A 32  ? 1.8772 1.3576 1.6240 -0.1862 -0.2481 0.4059  32  SER A CA  
442   C C   . SER A 32  ? 1.8346 1.2979 1.6075 -0.1784 -0.2531 0.3829  32  SER A C   
443   O O   . SER A 32  ? 1.8531 1.3344 1.6421 -0.1936 -0.2426 0.3748  32  SER A O   
444   C CB  . SER A 32  ? 1.8270 1.3257 1.5702 -0.1583 -0.2510 0.3970  32  SER A CB  
445   O OG  . SER A 32  ? 1.8251 1.3406 1.5424 -0.1654 -0.2468 0.4170  32  SER A OG  
451   N N   . ARG A 33  ? 1.7383 1.1676 1.5153 -0.1539 -0.2696 0.3718  33  ARG A N   
452   C CA  . ARG A 33  ? 1.5689 0.9854 1.3696 -0.1423 -0.2740 0.3471  33  ARG A CA  
453   C C   . ARG A 33  ? 1.4083 0.8815 1.2315 -0.1365 -0.2560 0.3240  33  ARG A C   
454   O O   . ARG A 33  ? 1.3303 0.8481 1.1520 -0.1335 -0.2433 0.3238  33  ARG A O   
455   C CB  . ARG A 33  ? 1.5263 0.9080 1.3288 -0.1125 -0.2925 0.3367  33  ARG A CB  
456   C CG  . ARG A 33  ? 1.5568 0.8914 1.3339 -0.1101 -0.3108 0.3605  33  ARG A CG  
457   C CD  . ARG A 33  ? 1.5739 0.8772 1.3565 -0.0782 -0.3295 0.3477  33  ARG A CD  
458   N NE  . ARG A 33  ? 1.6278 0.9207 1.3911 -0.0681 -0.3385 0.3623  33  ARG A NE  
459   C CZ  . ARG A 33  ? 1.6913 0.9513 1.4369 -0.0784 -0.3450 0.3788  33  ARG A CZ  
460   N NH1 . ARG A 33  ? 1.7219 0.9771 1.4507 -0.0675 -0.3524 0.3906  33  ARG A NH1 
461   N NH2 . ARG A 33  ? 1.7045 0.9367 1.4490 -0.1000 -0.3446 0.3838  33  ARG A NH2 
475   N N   . MET A 34  ? 1.3414 0.8107 1.1845 -0.1349 -0.2556 0.3043  34  MET A N   
476   C CA  . MET A 34  ? 1.2350 0.7512 1.0993 -0.1276 -0.2410 0.2815  34  MET A CA  
477   C C   . MET A 34  ? 1.1488 0.6558 1.0272 -0.0996 -0.2488 0.2574  34  MET A C   
478   O O   . MET A 34  ? 1.1787 0.6402 1.0554 -0.0902 -0.2649 0.2547  34  MET A O   
479   C CB  . MET A 34  ? 1.2922 0.8194 1.1681 -0.1499 -0.2325 0.2778  34  MET A CB  
480   C CG  . MET A 34  ? 1.3702 0.9185 1.2366 -0.1777 -0.2215 0.2992  34  MET A CG  
481   S SD  . MET A 34  ? 1.4536 1.0131 1.3357 -0.2048 -0.2142 0.2955  34  MET A SD  
482   C CE  . MET A 34  ? 1.4966 1.0901 1.3671 -0.2328 -0.1996 0.3211  34  MET A CE  
492   N N   . PHE A 35  ? 1.0471 0.5979 0.9394 -0.0865 -0.2371 0.2398  35  PHE A N   
493   C CA  . PHE A 35  ? 1.0097 0.5617 0.9160 -0.0605 -0.2415 0.2170  35  PHE A CA  
494   C C   . PHE A 35  ? 0.9881 0.5767 0.9127 -0.0601 -0.2278 0.1966  35  PHE A C   
495   O O   . PHE A 35  ? 0.9572 0.5727 0.8840 -0.0775 -0.2154 0.2003  35  PHE A O   
496   C CB  . PHE A 35  ? 0.9989 0.5670 0.9014 -0.0409 -0.2432 0.2173  35  PHE A CB  
497   C CG  . PHE A 35  ? 1.0836 0.6201 0.9659 -0.0406 -0.2566 0.2388  35  PHE A CG  
498   C CD1 . PHE A 35  ? 1.1424 0.6883 1.0065 -0.0582 -0.2514 0.2613  35  PHE A CD1 
499   C CD2 . PHE A 35  ? 1.1544 0.6527 1.0354 -0.0219 -0.2747 0.2364  35  PHE A CD2 
500   C CE1 . PHE A 35  ? 1.2358 0.7523 1.0786 -0.0585 -0.2640 0.2824  35  PHE A CE1 
501   C CE2 . PHE A 35  ? 1.2580 0.7255 1.1191 -0.0208 -0.2884 0.2573  35  PHE A CE2 
502   C CZ  . PHE A 35  ? 1.2972 0.7732 1.1381 -0.0397 -0.2832 0.2810  35  PHE A CZ  
512   N N   . LEU A 36  ? 1.0191 0.6092 0.9567 -0.0395 -0.2305 0.1752  36  LEU A N   
513   C CA  . LEU A 36  ? 1.0102 0.6358 0.9634 -0.0353 -0.2182 0.1556  36  LEU A CA  
514   C C   . LEU A 36  ? 1.0010 0.6591 0.9601 -0.0170 -0.2123 0.1468  36  LEU A C   
515   O O   . LEU A 36  ? 1.0853 0.7312 1.0435 0.0002  -0.2217 0.1452  36  LEU A O   
516   C CB  . LEU A 36  ? 1.0503 0.6550 1.0134 -0.0279 -0.2243 0.1363  36  LEU A CB  
517   C CG  . LEU A 36  ? 1.1303 0.7059 1.0909 -0.0465 -0.2297 0.1394  36  LEU A CG  
518   C CD1 . LEU A 36  ? 1.2188 0.7450 1.1658 -0.0522 -0.2451 0.1561  36  LEU A CD1 
519   C CD2 . LEU A 36  ? 1.1338 0.7024 1.1051 -0.0376 -0.2319 0.1157  36  LEU A CD2 
531   N N   . LEU A 37  ? 0.8835 0.5825 0.8490 -0.0209 -0.1975 0.1413  37  LEU A N   
532   C CA  . LEU A 37  ? 0.8435 0.5745 0.8161 -0.0059 -0.1908 0.1310  37  LEU A CA  
533   C C   . LEU A 37  ? 0.8470 0.5925 0.8343 0.0023  -0.1852 0.1095  37  LEU A C   
534   O O   . LEU A 37  ? 0.8564 0.6112 0.8473 -0.0087 -0.1780 0.1054  37  LEU A O   
535   C CB  . LEU A 37  ? 0.8659 0.6307 0.8336 -0.0153 -0.1785 0.1401  37  LEU A CB  
536   C CG  . LEU A 37  ? 0.9332 0.6899 0.8839 -0.0252 -0.1815 0.1617  37  LEU A CG  
537   C CD1 . LEU A 37  ? 0.9153 0.7093 0.8623 -0.0317 -0.1682 0.1661  37  LEU A CD1 
538   C CD2 . LEU A 37  ? 1.0124 0.7482 0.9557 -0.0111 -0.1949 0.1668  37  LEU A CD2 
550   N N   . VAL A 38  ? 0.8505 0.5994 0.8462 0.0215  -0.1885 0.0960  38  VAL A N   
551   C CA  . VAL A 38  ? 0.8272 0.5898 0.8355 0.0304  -0.1834 0.0754  38  VAL A CA  
552   C C   . VAL A 38  ? 0.8102 0.6049 0.8268 0.0431  -0.1769 0.0669  38  VAL A C   
553   O O   . VAL A 38  ? 0.8111 0.6036 0.8290 0.0554  -0.1840 0.0681  38  VAL A O   
554   C CB  . VAL A 38  ? 0.8443 0.5757 0.8564 0.0416  -0.1947 0.0638  38  VAL A CB  
555   C CG1 . VAL A 38  ? 0.8341 0.5830 0.8571 0.0494  -0.1878 0.0424  38  VAL A CG1 
556   C CG2 . VAL A 38  ? 0.8816 0.5768 0.8847 0.0276  -0.2029 0.0731  38  VAL A CG2 
566   N N   . GLY A 39  ? 0.7480 0.5720 0.7703 0.0396  -0.1644 0.0586  39  GLY A N   
567   C CA  . GLY A 39  ? 0.7496 0.6037 0.7802 0.0491  -0.1575 0.0499  39  GLY A CA  
568   C C   . GLY A 39  ? 0.8103 0.6689 0.8527 0.0631  -0.1577 0.0311  39  GLY A C   
569   O O   . GLY A 39  ? 0.8473 0.6985 0.8910 0.0617  -0.1565 0.0217  39  GLY A O   
573   N N   . ALA A 40  ? 0.8106 0.6835 0.8616 0.0764  -0.1595 0.0251  40  ALA A N   
574   C CA  . ALA A 40  ? 0.7792 0.6646 0.8436 0.0905  -0.1580 0.0067  40  ALA A CA  
575   C C   . ALA A 40  ? 0.7446 0.6664 0.8172 0.0919  -0.1486 0.0027  40  ALA A C   
576   O O   . ALA A 40  ? 0.7559 0.6885 0.8364 0.1020  -0.1532 0.0013  40  ALA A O   
577   C CB  . ALA A 40  ? 0.7231 0.5884 0.7931 0.1072  -0.1717 0.0022  40  ALA A CB  
583   N N   . PRO A 41  ? 0.7577 0.6984 0.8287 0.0815  -0.1363 0.0008  41  PRO A N   
584   C CA  . PRO A 41  ? 0.7427 0.7132 0.8185 0.0792  -0.1280 0.0004  41  PRO A CA  
585   C C   . PRO A 41  ? 0.7275 0.7214 0.8187 0.0903  -0.1252 -0.0139 41  PRO A C   
586   O O   . PRO A 41  ? 0.7201 0.7373 0.8167 0.0885  -0.1204 -0.0141 41  PRO A O   
587   C CB  . PRO A 41  ? 0.7185 0.6969 0.7873 0.0659  -0.1169 0.0023  41  PRO A CB  
588   C CG  . PRO A 41  ? 0.7303 0.6928 0.7960 0.0650  -0.1178 -0.0034 41  PRO A CG  
589   C CD  . PRO A 41  ? 0.7603 0.6945 0.8243 0.0712  -0.1305 -0.0003 41  PRO A CD  
597   N N   . LYS A 42  ? 0.7139 0.7035 0.8126 0.1014  -0.1280 -0.0265 42  LYS A N   
598   C CA  . LYS A 42  ? 0.7283 0.7436 0.8435 0.1129  -0.1251 -0.0410 42  LYS A CA  
599   C C   . LYS A 42  ? 0.7887 0.7970 0.9143 0.1301  -0.1379 -0.0448 42  LYS A C   
600   O O   . LYS A 42  ? 0.8217 0.8513 0.9634 0.1423  -0.1369 -0.0585 42  LYS A O   
601   C CB  . LYS A 42  ? 0.7473 0.7699 0.8643 0.1142  -0.1167 -0.0552 42  LYS A CB  
602   C CG  . LYS A 42  ? 0.7412 0.7829 0.8528 0.1003  -0.1028 -0.0544 42  LYS A CG  
603   C CD  . LYS A 42  ? 0.8214 0.8758 0.9350 0.1032  -0.0944 -0.0695 42  LYS A CD  
604   C CE  . LYS A 42  ? 0.9393 1.0132 1.0469 0.0899  -0.0812 -0.0675 42  LYS A CE  
605   N NZ  . LYS A 42  ? 1.0483 1.1357 1.1551 0.0918  -0.0727 -0.0811 42  LYS A NZ  
619   N N   . ALA A 43  ? 0.8005 0.7805 0.9174 0.1314  -0.1501 -0.0327 43  ALA A N   
620   C CA  . ALA A 43  ? 0.7762 0.7441 0.9009 0.1487  -0.1643 -0.0350 43  ALA A CA  
621   C C   . ALA A 43  ? 0.7228 0.7180 0.8598 0.1553  -0.1671 -0.0348 43  ALA A C   
622   O O   . ALA A 43  ? 0.6931 0.7006 0.8248 0.1442  -0.1635 -0.0250 43  ALA A O   
623   C CB  . ALA A 43  ? 0.8359 0.7632 0.9450 0.1461  -0.1768 -0.0198 43  ALA A CB  
629   N N   . ASN A 44  ? 0.7694 0.7747 0.9235 0.1739  -0.1742 -0.0466 44  ASN A N   
630   C CA  . ASN A 44  ? 0.7191 0.7503 0.8870 0.1819  -0.1796 -0.0470 44  ASN A CA  
631   C C   . ASN A 44  ? 0.7718 0.7779 0.9280 0.1845  -0.1953 -0.0306 44  ASN A C   
632   O O   . ASN A 44  ? 0.8282 0.7963 0.9724 0.1882  -0.2054 -0.0232 44  ASN A O   
633   C CB  . ASN A 44  ? 0.6732 0.7258 0.8649 0.2022  -0.1826 -0.0655 44  ASN A CB  
634   C CG  . ASN A 44  ? 0.7273 0.8191 0.9329 0.1978  -0.1658 -0.0803 44  ASN A CG  
635   O OD1 . ASN A 44  ? 0.6625 0.7786 0.8684 0.1834  -0.1559 -0.0767 44  ASN A OD1 
636   N ND2 . ASN A 44  ? 0.9605 1.0577 1.1765 0.2097  -0.1624 -0.0970 44  ASN A ND2 
642   N N   . THR A 45  ? 0.7791 0.8062 0.9377 0.1817  -0.1976 -0.0247 45  THR A N   
643   C CA  . THR A 45  ? 0.7784 0.7868 0.9233 0.1823  -0.2113 -0.0083 45  THR A CA  
644   C C   . THR A 45  ? 0.7506 0.7831 0.9124 0.1974  -0.2225 -0.0131 45  THR A C   
645   O O   . THR A 45  ? 0.7457 0.8127 0.9308 0.2050  -0.2180 -0.0288 45  THR A O   
646   C CB  . THR A 45  ? 0.7870 0.7958 0.9132 0.1620  -0.2039 0.0054  45  THR A CB  
647   O OG1 . THR A 45  ? 0.7709 0.8178 0.9080 0.1561  -0.1952 -0.0014 45  THR A OG1 
648   C CG2 . THR A 45  ? 0.7786 0.7694 0.8915 0.1475  -0.1924 0.0089  45  THR A CG2 
656   N N   . THR A 46  ? 0.7790 0.7947 0.9287 0.2012  -0.2374 0.0010  46  THR A N   
657   C CA  . THR A 46  ? 0.7816 0.8192 0.9444 0.2147  -0.2503 -0.0012 46  THR A CA  
658   C C   . THR A 46  ? 0.7736 0.8437 0.9365 0.2021  -0.2447 0.0004  46  THR A C   
659   O O   . THR A 46  ? 0.8089 0.9018 0.9833 0.2111  -0.2550 -0.0021 46  THR A O   
660   C CB  . THR A 46  ? 0.8143 0.8174 0.9616 0.2250  -0.2705 0.0141  46  THR A CB  
661   O OG1 . THR A 46  ? 0.8202 0.8004 0.9382 0.2075  -0.2691 0.0334  46  THR A OG1 
662   C CG2 . THR A 46  ? 0.8681 0.8369 1.0172 0.2394  -0.2783 0.0110  46  THR A CG2 
670   N N   . GLN A 47  ? 0.7936 0.8657 0.9442 0.1821  -0.2295 0.0040  47  GLN A N   
671   C CA  . GLN A 47  ? 0.7818 0.8809 0.9312 0.1695  -0.2238 0.0043  47  GLN A CA  
672   C C   . GLN A 47  ? 0.7911 0.9330 0.9698 0.1756  -0.2219 -0.0123 47  GLN A C   
673   O O   . GLN A 47  ? 0.8159 0.9724 1.0113 0.1767  -0.2110 -0.0252 47  GLN A O   
674   C CB  . GLN A 47  ? 0.7272 0.8217 0.8630 0.1496  -0.2067 0.0074  47  GLN A CB  
675   C CG  . GLN A 47  ? 0.7406 0.7990 0.8488 0.1413  -0.2074 0.0239  47  GLN A CG  
676   C CD  . GLN A 47  ? 0.7410 0.7970 0.8393 0.1241  -0.1907 0.0252  47  GLN A CD  
677   O OE1 . GLN A 47  ? 0.7851 0.8335 0.8872 0.1223  -0.1824 0.0202  47  GLN A OE1 
678   N NE2 . GLN A 47  ? 0.7223 0.7849 0.8073 0.1121  -0.1864 0.0313  47  GLN A NE2 
687   N N   . PRO A 48  ? 0.7740 0.9385 0.9597 0.1791  -0.2320 -0.0128 48  PRO A N   
688   C CA  . PRO A 48  ? 0.7494 0.9574 0.9661 0.1851  -0.2313 -0.0288 48  PRO A CA  
689   C C   . PRO A 48  ? 0.7112 0.9423 0.9372 0.1691  -0.2116 -0.0385 48  PRO A C   
690   O O   . PRO A 48  ? 0.6919 0.9200 0.9029 0.1514  -0.2031 -0.0331 48  PRO A O   
691   C CB  . PRO A 48  ? 0.7243 0.9484 0.9397 0.1857  -0.2450 -0.0246 48  PRO A CB  
692   C CG  . PRO A 48  ? 0.7568 0.9431 0.9438 0.1893  -0.2576 -0.0071 48  PRO A CG  
693   C CD  . PRO A 48  ? 0.7794 0.9324 0.9451 0.1778  -0.2451 0.0011  48  PRO A CD  
701   N N   . GLY A 49  ? 0.6917 0.9457 0.9420 0.1759  -0.2046 -0.0529 49  GLY A N   
702   C CA  . GLY A 49  ? 0.6055 0.8855 0.8668 0.1614  -0.1868 -0.0623 49  GLY A CA  
703   C C   . GLY A 49  ? 0.6015 0.8578 0.8442 0.1482  -0.1716 -0.0580 49  GLY A C   
704   O O   . GLY A 49  ? 0.5993 0.8733 0.8469 0.1345  -0.1571 -0.0633 49  GLY A O   
708   N N   . ILE A 50  ? 0.6186 0.8359 0.8405 0.1512  -0.1749 -0.0481 50  ILE A N   
709   C CA  . ILE A 50  ? 0.6007 0.7954 0.8045 0.1388  -0.1622 -0.0432 50  ILE A CA  
710   C C   . ILE A 50  ? 0.6397 0.8258 0.8497 0.1488  -0.1584 -0.0514 50  ILE A C   
711   O O   . ILE A 50  ? 0.6870 0.8566 0.8989 0.1648  -0.1699 -0.0518 50  ILE A O   
712   C CB  . ILE A 50  ? 0.5921 0.7517 0.7684 0.1325  -0.1673 -0.0267 50  ILE A CB  
713   C CG1 . ILE A 50  ? 0.6257 0.7947 0.7947 0.1245  -0.1719 -0.0203 50  ILE A CG1 
714   C CG2 . ILE A 50  ? 0.5243 0.6649 0.6846 0.1197  -0.1544 -0.0224 50  ILE A CG2 
715   C CD1 . ILE A 50  ? 0.6169 0.8129 0.7938 0.1106  -0.1606 -0.0272 50  ILE A CD1 
727   N N   . VAL A 51  ? 0.6426 0.8383 0.8542 0.1395  -0.1430 -0.0580 51  VAL A N   
728   C CA  . VAL A 51  ? 0.6278 0.8165 0.8422 0.1467  -0.1375 -0.0669 51  VAL A CA  
729   C C   . VAL A 51  ? 0.6785 0.8356 0.8693 0.1353  -0.1315 -0.0578 51  VAL A C   
730   O O   . VAL A 51  ? 0.6572 0.8162 0.8376 0.1191  -0.1221 -0.0519 51  VAL A O   
731   C CB  . VAL A 51  ? 0.5774 0.8040 0.8108 0.1450  -0.1244 -0.0817 51  VAL A CB  
732   C CG1 . VAL A 51  ? 0.6217 0.8413 0.8555 0.1529  -0.1186 -0.0919 51  VAL A CG1 
733   C CG2 . VAL A 51  ? 0.5271 0.7899 0.7869 0.1553  -0.1303 -0.0909 51  VAL A CG2 
743   N N   . GLU A 52  ? 0.7045 0.8324 0.8876 0.1440  -0.1376 -0.0571 52  GLU A N   
744   C CA  . GLU A 52  ? 0.6904 0.7892 0.8533 0.1340  -0.1332 -0.0496 52  GLU A CA  
745   C C   . GLU A 52  ? 0.6471 0.7354 0.7931 0.1188  -0.1321 -0.0340 52  GLU A C   
746   O O   . GLU A 52  ? 0.6312 0.7173 0.7666 0.1054  -0.1220 -0.0304 52  GLU A O   
747   C CB  . GLU A 52  ? 0.7222 0.8332 0.8863 0.1281  -0.1189 -0.0596 52  GLU A CB  
748   C CG  . GLU A 52  ? 0.8006 0.9183 0.9776 0.1433  -0.1192 -0.0759 52  GLU A CG  
749   C CD  . GLU A 52  ? 0.8151 0.9378 0.9867 0.1369  -0.1062 -0.0841 52  GLU A CD  
750   O OE1 . GLU A 52  ? 0.8102 0.9340 0.9700 0.1207  -0.0970 -0.0769 52  GLU A OE1 
751   O OE2 . GLU A 52  ? 0.8150 0.9401 0.9935 0.1488  -0.1058 -0.0982 52  GLU A OE2 
758   N N   . GLY A 53  ? 0.6609 0.7435 0.8039 0.1219  -0.1431 -0.0251 53  GLY A N   
759   C CA  . GLY A 53  ? 0.6835 0.7546 0.8088 0.1095  -0.1430 -0.0108 53  GLY A CA  
760   C C   . GLY A 53  ? 0.7125 0.7519 0.8199 0.1033  -0.1435 -0.0006 53  GLY A C   
761   O O   . GLY A 53  ? 0.7066 0.7402 0.7999 0.0911  -0.1392 0.0094  53  GLY A O   
765   N N   . GLY A 54  ? 0.6947 0.7141 0.8028 0.1114  -0.1487 -0.0037 54  GLY A N   
766   C CA  . GLY A 54  ? 0.7187 0.7075 0.8114 0.1048  -0.1504 0.0055  54  GLY A CA  
767   C C   . GLY A 54  ? 0.7459 0.7114 0.8263 0.1054  -0.1626 0.0205  54  GLY A C   
768   O O   . GLY A 54  ? 0.7398 0.7140 0.8198 0.1086  -0.1685 0.0257  54  GLY A O   
772   N N   . GLN A 55  ? 0.7925 0.7278 0.8617 0.1013  -0.1666 0.0280  55  GLN A N   
773   C CA  . GLN A 55  ? 0.8259 0.7361 0.8813 0.0999  -0.1779 0.0440  55  GLN A CA  
774   C C   . GLN A 55  ? 0.8021 0.6853 0.8448 0.0879  -0.1771 0.0528  55  GLN A C   
775   O O   . GLN A 55  ? 0.8019 0.6822 0.8483 0.0846  -0.1712 0.0444  55  GLN A O   
776   C CB  . GLN A 55  ? 0.7992 0.6951 0.8609 0.1176  -0.1933 0.0419  55  GLN A CB  
777   C CG  . GLN A 55  ? 0.7445 0.6247 0.8160 0.1286  -0.1971 0.0289  55  GLN A CG  
778   C CD  . GLN A 55  ? 0.7801 0.6495 0.8603 0.1490  -0.2125 0.0249  55  GLN A CD  
779   O OE1 . GLN A 55  ? 0.8024 0.6815 0.8838 0.1554  -0.2200 0.0306  55  GLN A OE1 
780   N NE2 . GLN A 55  ? 0.7676 0.6167 0.8539 0.1600  -0.2180 0.0145  55  GLN A NE2 
789   N N   . VAL A 56  ? 0.7872 0.6523 0.8143 0.0805  -0.1832 0.0701  56  VAL A N   
790   C CA  . VAL A 56  ? 0.7643 0.6038 0.7791 0.0672  -0.1837 0.0812  56  VAL A CA  
791   C C   . VAL A 56  ? 0.8450 0.6483 0.8526 0.0734  -0.1998 0.0902  56  VAL A C   
792   O O   . VAL A 56  ? 0.8798 0.6800 0.8826 0.0809  -0.2090 0.0979  56  VAL A O   
793   C CB  . VAL A 56  ? 0.7490 0.5995 0.7506 0.0509  -0.1756 0.0951  56  VAL A CB  
794   C CG1 . VAL A 56  ? 0.7750 0.6025 0.7660 0.0359  -0.1760 0.1068  56  VAL A CG1 
795   C CG2 . VAL A 56  ? 0.6976 0.5810 0.7061 0.0466  -0.1611 0.0860  56  VAL A CG2 
805   N N   . LEU A 57  ? 0.8715 0.6461 0.8778 0.0702  -0.2041 0.0893  57  LEU A N   
806   C CA  . LEU A 57  ? 0.9191 0.6537 0.9190 0.0765  -0.2203 0.0964  57  LEU A CA  
807   C C   . LEU A 57  ? 0.8716 0.5792 0.8546 0.0573  -0.2226 0.1151  57  LEU A C   
808   O O   . LEU A 57  ? 0.7751 0.4880 0.7572 0.0417  -0.2130 0.1153  57  LEU A O   
809   C CB  . LEU A 57  ? 0.9668 0.6846 0.9789 0.0899  -0.2259 0.0786  57  LEU A CB  
810   C CG  . LEU A 57  ? 0.9761 0.7198 1.0064 0.1102  -0.2247 0.0594  57  LEU A CG  
811   C CD1 . LEU A 57  ? 0.9985 0.7752 1.0391 0.1058  -0.2085 0.0444  57  LEU A CD1 
812   C CD2 . LEU A 57  ? 0.9931 0.7094 1.0308 0.1293  -0.2384 0.0485  57  LEU A CD2 
824   N N   . LYS A 58  ? 0.8820 0.5618 0.8516 0.0581  -0.2355 0.1315  58  LYS A N   
825   C CA  . LYS A 58  ? 0.8926 0.5404 0.8455 0.0404  -0.2403 0.1505  58  LYS A CA  
826   C C   . LYS A 58  ? 0.9468 0.5482 0.9003 0.0476  -0.2554 0.1474  58  LYS A C   
827   O O   . LYS A 58  ? 0.9940 0.5791 0.9506 0.0674  -0.2684 0.1431  58  LYS A O   
828   C CB  . LYS A 58  ? 0.9804 0.6255 0.9148 0.0349  -0.2448 0.1725  58  LYS A CB  
829   C CG  . LYS A 58  ? 1.1443 0.7586 1.0598 0.0144  -0.2488 0.1946  58  LYS A CG  
830   C CD  . LYS A 58  ? 1.2360 0.8621 1.1321 0.0049  -0.2466 0.2153  58  LYS A CD  
831   C CE  . LYS A 58  ? 1.3094 0.9228 1.1968 0.0221  -0.2616 0.2220  58  LYS A CE  
832   N NZ  . LYS A 58  ? 1.3383 0.9712 1.2068 0.0142  -0.2579 0.2387  58  LYS A NZ  
846   N N   . CYS A 59  ? 0.9852 0.5656 0.9362 0.0321  -0.2543 0.1488  59  CYS A N   
847   C CA  . CYS A 59  ? 1.0734 0.6096 1.0260 0.0378  -0.2676 0.1420  59  CYS A CA  
848   C C   . CYS A 59  ? 1.1077 0.6023 1.0429 0.0182  -0.2763 0.1637  59  CYS A C   
849   O O   . CYS A 59  ? 1.0637 0.5679 0.9935 -0.0054 -0.2669 0.1738  59  CYS A O   
850   C CB  . CYS A 59  ? 1.0938 0.6404 1.0604 0.0376  -0.2598 0.1200  59  CYS A CB  
851   S SG  . CYS A 59  ? 1.0689 0.6655 1.0552 0.0570  -0.2476 0.0952  59  CYS A SG  
856   N N   . ASP A 60  ? 1.1793 0.6281 1.1061 0.0279  -0.2946 0.1709  60  ASP A N   
857   C CA  . ASP A 60  ? 1.2737 0.6758 1.1835 0.0092  -0.3048 0.1912  60  ASP A CA  
858   C C   . ASP A 60  ? 1.2346 0.6193 1.1500 -0.0052 -0.3032 0.1815  60  ASP A C   
859   O O   . ASP A 60  ? 1.1763 0.5678 1.1067 0.0068  -0.3011 0.1572  60  ASP A O   
860   C CB  . ASP A 60  ? 1.4243 0.7762 1.3250 0.0257  -0.3267 0.1983  60  ASP A CB  
861   C CG  . ASP A 60  ? 1.5007 0.8645 1.3915 0.0364  -0.3311 0.2129  60  ASP A CG  
862   O OD1 . ASP A 60  ? 1.5048 0.9165 1.3966 0.0320  -0.3169 0.2151  60  ASP A OD1 
863   O OD2 . ASP A 60  ? 1.5765 0.9006 1.4579 0.0494  -0.3497 0.2219  60  ASP A OD2 
868   N N   . TRP A 61  ? 1.2853 0.6482 1.1880 -0.0320 -0.3042 0.2006  61  TRP A N   
869   C CA  . TRP A 61  ? 1.3407 0.6831 1.2473 -0.0490 -0.3049 0.1939  61  TRP A CA  
870   C C   . TRP A 61  ? 1.4807 0.7549 1.3763 -0.0496 -0.3257 0.2011  61  TRP A C   
871   O O   . TRP A 61  ? 1.4993 0.7442 1.3776 -0.0664 -0.3328 0.2266  61  TRP A O   
872   C CB  . TRP A 61  ? 1.2924 0.6599 1.1956 -0.0804 -0.2915 0.2087  61  TRP A CB  
873   C CG  . TRP A 61  ? 1.3149 0.6553 1.2203 -0.1002 -0.2956 0.2055  61  TRP A CG  
874   C CD1 . TRP A 61  ? 1.2806 0.6289 1.2003 -0.0980 -0.2928 0.1819  61  TRP A CD1 
875   C CD2 . TRP A 61  ? 1.4433 0.7440 1.3357 -0.1261 -0.3041 0.2264  61  TRP A CD2 
876   N NE1 . TRP A 61  ? 1.3596 0.6759 1.2767 -0.1205 -0.2996 0.1858  61  TRP A NE1 
877   C CE2 . TRP A 61  ? 1.4451 0.7317 1.3463 -0.1388 -0.3064 0.2132  61  TRP A CE2 
878   C CE3 . TRP A 61  ? 1.5647 0.8406 1.4379 -0.1408 -0.3100 0.2555  61  TRP A CE3 
879   C CZ2 . TRP A 61  ? 1.5521 0.8008 1.4453 -0.1663 -0.3146 0.2276  61  TRP A CZ2 
880   C CZ3 . TRP A 61  ? 1.6471 0.8851 1.5114 -0.1684 -0.3173 0.2710  61  TRP A CZ3 
881   C CH2 . TRP A 61  ? 1.6543 0.8790 1.5295 -0.1813 -0.3196 0.2568  61  TRP A CH2 
892   N N   . SER A 62  ? 1.5985 0.8468 1.5033 -0.0308 -0.3356 0.1784  62  SER A N   
893   C CA  . SER A 62  ? 1.7345 0.9160 1.6314 -0.0322 -0.3550 0.1794  62  SER A CA  
894   C C   . SER A 62  ? 1.8338 0.9706 1.7155 -0.0205 -0.3729 0.1975  62  SER A C   
895   O O   . SER A 62  ? 1.8843 0.9716 1.7601 -0.0173 -0.3874 0.1958  62  SER A O   
896   C CB  . SER A 62  ? 1.7911 0.9548 1.6811 -0.0677 -0.3537 0.1924  62  SER A CB  
897   O OG  . SER A 62  ? 1.8739 0.9725 1.7579 -0.0701 -0.3722 0.1895  62  SER A OG  
903   N N   . SER A 63  ? 1.8887 1.0532 1.7648 -0.0134 -0.3688 0.2117  63  SER A N   
904   C CA  . SER A 63  ? 1.9969 1.1314 1.8610 0.0029  -0.3838 0.2239  63  SER A CA  
905   C C   . SER A 63  ? 1.9921 1.1199 1.8708 0.0396  -0.3935 0.1982  63  SER A C   
906   O O   . SER A 63  ? 2.0100 1.1013 1.8857 0.0516  -0.4061 0.1935  63  SER A O   
907   C CB  . SER A 63  ? 2.0129 1.1797 1.8661 0.0003  -0.3777 0.2454  63  SER A CB  
908   O OG  . SER A 63  ? 2.0321 1.2038 1.8697 -0.0330 -0.3690 0.2700  63  SER A OG  
914   N N   . THR A 64  ? 1.9424 1.1151 1.8387 0.0569  -0.3841 0.1794  64  THR A N   
915   C CA  . THR A 64  ? 1.8760 1.0510 1.7898 0.0903  -0.3901 0.1516  64  THR A CA  
916   C C   . THR A 64  ? 1.7750 0.9980 1.7087 0.0936  -0.3724 0.1240  64  THR A C   
917   O O   . THR A 64  ? 1.8075 1.0323 1.7560 0.1186  -0.3758 0.0985  64  THR A O   
918   C CB  . THR A 64  ? 1.8228 1.0175 1.7394 0.1151  -0.3956 0.1552  64  THR A CB  
919   O OG1 . THR A 64  ? 1.8140 1.0740 1.7377 0.1102  -0.3763 0.1550  64  THR A OG1 
920   C CG2 . THR A 64  ? 1.7703 0.9379 1.6660 0.1081  -0.4055 0.1819  64  THR A CG2 
928   N N   . ARG A 65  ? 1.6365 0.8986 1.5707 0.0700  -0.3539 0.1280  65  ARG A N   
929   C CA  . ARG A 65  ? 1.5266 0.8392 1.4778 0.0726  -0.3363 0.1051  65  ARG A CA  
930   C C   . ARG A 65  ? 1.4145 0.7719 1.3794 0.0970  -0.3300 0.0932  65  ARG A C   
931   O O   . ARG A 65  ? 1.3549 0.7428 1.3354 0.1095  -0.3210 0.0692  65  ARG A O   
932   C CB  . ARG A 65  ? 1.5848 0.8756 1.5436 0.0777  -0.3399 0.0806  65  ARG A CB  
933   C CG  . ARG A 65  ? 1.6811 0.9404 1.6300 0.0495  -0.3421 0.0882  65  ARG A CG  
934   C CD  . ARG A 65  ? 1.7560 1.0262 1.7149 0.0487  -0.3354 0.0619  65  ARG A CD  
935   N NE  . ARG A 65  ? 1.8447 1.1065 1.8138 0.0789  -0.3419 0.0348  65  ARG A NE  
936   C CZ  . ARG A 65  ? 1.8826 1.1455 1.8581 0.0836  -0.3395 0.0091  65  ARG A CZ  
937   N NH1 . ARG A 65  ? 1.8608 1.1315 1.8338 0.0600  -0.3321 0.0074  65  ARG A NH1 
938   N NH2 . ARG A 65  ? 1.9115 1.1693 1.8959 0.1123  -0.3447 -0.0153 65  ARG A NH2 
952   N N   . ARG A 66  ? 1.3949 0.7577 1.3535 0.1029  -0.3347 0.1102  66  ARG A N   
953   C CA  . ARG A 66  ? 1.3772 0.7811 1.3486 0.1246  -0.3308 0.1010  66  ARG A CA  
954   C C   . ARG A 66  ? 1.2391 0.6965 1.2109 0.1101  -0.3122 0.1080  66  ARG A C   
955   O O   . ARG A 66  ? 1.1837 0.6408 1.1411 0.0869  -0.3071 0.1284  66  ARG A O   
956   C CB  . ARG A 66  ? 1.5346 0.9131 1.4990 0.1416  -0.3490 0.1140  66  ARG A CB  
957   C CG  . ARG A 66  ? 1.6439 1.0645 1.6233 0.1649  -0.3475 0.1040  66  ARG A CG  
958   C CD  . ARG A 66  ? 1.8027 1.1970 1.7739 0.1811  -0.3673 0.1185  66  ARG A CD  
959   N NE  . ARG A 66  ? 1.9160 1.2991 1.8634 0.1607  -0.3694 0.1488  66  ARG A NE  
960   C CZ  . ARG A 66  ? 2.0256 1.3767 1.9575 0.1673  -0.3873 0.1684  66  ARG A CZ  
961   N NH1 . ARG A 66  ? 2.0694 1.3960 2.0087 0.1947  -0.4054 0.1605  66  ARG A NH1 
962   N NH2 . ARG A 66  ? 2.0695 1.4147 1.9781 0.1466  -0.3867 0.1958  66  ARG A NH2 
976   N N   . CYS A 67  ? 1.1992 0.7026 1.1878 0.1240  -0.3019 0.0906  67  CYS A N   
977   C CA  . CYS A 67  ? 1.1521 0.7058 1.1428 0.1142  -0.2854 0.0944  67  CYS A CA  
978   C C   . CYS A 67  ? 1.1522 0.7304 1.1493 0.1325  -0.2892 0.0942  67  CYS A C   
979   O O   . CYS A 67  ? 1.2298 0.8093 1.2411 0.1560  -0.2968 0.0788  67  CYS A O   
980   C CB  . CYS A 67  ? 1.1159 0.7053 1.1203 0.1110  -0.2685 0.0745  67  CYS A CB  
981   S SG  . CYS A 67  ? 1.1846 0.7536 1.1834 0.0894  -0.2632 0.0721  67  CYS A SG  
986   N N   . GLN A 68  ? 1.0815 0.6807 1.0686 0.1217  -0.2842 0.1106  68  GLN A N   
987   C CA  . GLN A 68  ? 1.0621 0.6892 1.0544 0.1358  -0.2869 0.1107  68  GLN A CA  
988   C C   . GLN A 68  ? 0.9923 0.6666 0.9861 0.1235  -0.2692 0.1105  68  GLN A C   
989   O O   . GLN A 68  ? 0.9837 0.6603 0.9652 0.1023  -0.2596 0.1221  68  GLN A O   
990   C CB  . GLN A 68  ? 1.1598 0.7585 1.1339 0.1378  -0.3033 0.1329  68  GLN A CB  
991   C CG  . GLN A 68  ? 1.3194 0.8742 1.2946 0.1570  -0.3239 0.1314  68  GLN A CG  
992   C CD  . GLN A 68  ? 1.4917 1.0139 1.4453 0.1569  -0.3408 0.1563  68  GLN A CD  
993   O OE1 . GLN A 68  ? 1.5577 1.0921 1.4946 0.1420  -0.3365 0.1746  68  GLN A OE1 
994   N NE2 . GLN A 68  ? 1.5734 1.0531 1.5262 0.1742  -0.3605 0.1570  68  GLN A NE2 
1003  N N   . PRO A 69  ? 0.9415 0.6541 0.9510 0.1361  -0.2648 0.0973  69  PRO A N   
1004  C CA  . PRO A 69  ? 0.8863 0.6403 0.8969 0.1246  -0.2488 0.0965  69  PRO A CA  
1005  C C   . PRO A 69  ? 0.8971 0.6523 0.8877 0.1131  -0.2503 0.1172  69  PRO A C   
1006  O O   . PRO A 69  ? 0.9930 0.7304 0.9733 0.1202  -0.2647 0.1294  69  PRO A O   
1007  C CB  . PRO A 69  ? 0.8708 0.6597 0.9025 0.1419  -0.2476 0.0787  69  PRO A CB  
1008  C CG  . PRO A 69  ? 0.9009 0.6713 0.9459 0.1616  -0.2584 0.0657  69  PRO A CG  
1009  C CD  . PRO A 69  ? 0.9325 0.6536 0.9609 0.1611  -0.2736 0.0813  69  PRO A CD  
1017  N N   . ILE A 70  ? 0.8886 0.6651 0.8730 0.0958  -0.2353 0.1210  70  ILE A N   
1018  C CA  . ILE A 70  ? 0.9083 0.6944 0.8746 0.0849  -0.2334 0.1373  70  ILE A CA  
1019  C C   . ILE A 70  ? 0.9592 0.7827 0.9342 0.0931  -0.2302 0.1282  70  ILE A C   
1020  O O   . ILE A 70  ? 0.9869 0.8378 0.9773 0.0937  -0.2188 0.1126  70  ILE A O   
1021  C CB  . ILE A 70  ? 0.8598 0.6515 0.8162 0.0633  -0.2189 0.1447  70  ILE A CB  
1022  C CG1 . ILE A 70  ? 0.8815 0.6372 0.8307 0.0532  -0.2228 0.1538  70  ILE A CG1 
1023  C CG2 . ILE A 70  ? 0.8467 0.6523 0.7845 0.0533  -0.2156 0.1595  70  ILE A CG2 
1024  C CD1 . ILE A 70  ? 0.8832 0.6473 0.8263 0.0321  -0.2089 0.1598  70  ILE A CD1 
1036  N N   . GLU A 71  ? 0.9947 0.8185 0.9587 0.0986  -0.2409 0.1382  71  GLU A N   
1037  C CA  . GLU A 71  ? 0.9639 0.8219 0.9352 0.1058  -0.2402 0.1300  71  GLU A CA  
1038  C C   . GLU A 71  ? 0.9032 0.7838 0.8629 0.0899  -0.2263 0.1338  71  GLU A C   
1039  O O   . GLU A 71  ? 0.9064 0.7859 0.8453 0.0836  -0.2291 0.1478  71  GLU A O   
1040  C CB  . GLU A 71  ? 1.0425 0.8924 1.0062 0.1186  -0.2586 0.1386  71  GLU A CB  
1041  C CG  . GLU A 71  ? 1.1153 1.0013 1.0867 0.1254  -0.2597 0.1300  71  GLU A CG  
1042  C CD  . GLU A 71  ? 1.2583 1.1374 1.2199 0.1373  -0.2790 0.1400  71  GLU A CD  
1043  O OE1 . GLU A 71  ? 1.3418 1.1907 1.3015 0.1481  -0.2936 0.1469  71  GLU A OE1 
1044  O OE2 . GLU A 71  ? 1.2943 1.1970 1.2492 0.1360  -0.2804 0.1407  71  GLU A OE2 
1051  N N   . PHE A 72  ? 0.8531 0.7540 0.8252 0.0838  -0.2112 0.1210  72  PHE A N   
1052  C CA  . PHE A 72  ? 0.8561 0.7808 0.8207 0.0721  -0.1985 0.1210  72  PHE A CA  
1053  C C   . PHE A 72  ? 0.8988 0.8508 0.8694 0.0791  -0.2009 0.1122  72  PHE A C   
1054  O O   . PHE A 72  ? 0.9436 0.9065 0.8990 0.0736  -0.1998 0.1180  72  PHE A O   
1055  C CB  . PHE A 72  ? 0.8533 0.7876 0.8284 0.0638  -0.1829 0.1112  72  PHE A CB  
1056  C CG  . PHE A 72  ? 0.8435 0.7582 0.8095 0.0519  -0.1780 0.1209  72  PHE A CG  
1057  C CD1 . PHE A 72  ? 0.8224 0.7423 0.7728 0.0381  -0.1697 0.1313  72  PHE A CD1 
1058  C CD2 . PHE A 72  ? 0.8833 0.7761 0.8571 0.0543  -0.1817 0.1187  72  PHE A CD2 
1059  C CE1 . PHE A 72  ? 0.8677 0.7732 0.8121 0.0261  -0.1651 0.1400  72  PHE A CE1 
1060  C CE2 . PHE A 72  ? 0.9047 0.7802 0.8711 0.0418  -0.1779 0.1272  72  PHE A CE2 
1061  C CZ  . PHE A 72  ? 0.9064 0.7894 0.8589 0.0272  -0.1696 0.1383  72  PHE A CZ  
1071  N N   . ASP A 73  ? 0.8838 0.8484 0.8764 0.0908  -0.2039 0.0976  73  ASP A N   
1072  C CA  . ASP A 73  ? 0.8235 0.8167 0.8260 0.0963  -0.2060 0.0875  73  ASP A CA  
1073  C C   . ASP A 73  ? 0.8480 0.8466 0.8727 0.1127  -0.2160 0.0770  73  ASP A C   
1074  O O   . ASP A 73  ? 0.8798 0.8805 0.9219 0.1162  -0.2102 0.0659  73  ASP A O   
1075  C CB  . ASP A 73  ? 0.7484 0.7646 0.7584 0.0868  -0.1903 0.0764  73  ASP A CB  
1076  C CG  . ASP A 73  ? 0.7289 0.7735 0.7577 0.0926  -0.1916 0.0620  73  ASP A CG  
1077  O OD1 . ASP A 73  ? 0.7368 0.7909 0.7634 0.0984  -0.2027 0.0632  73  ASP A OD1 
1078  O OD2 . ASP A 73  ? 0.7103 0.7684 0.7555 0.0905  -0.1816 0.0499  73  ASP A OD2 
1083  N N   . ALA A 74  ? 0.8478 0.8503 0.8715 0.1232  -0.2310 0.0800  74  ALA A N   
1084  C CA  . ALA A 74  ? 0.8702 0.8802 0.9157 0.1410  -0.2425 0.0704  74  ALA A CA  
1085  C C   . ALA A 74  ? 0.8063 0.8555 0.8728 0.1441  -0.2407 0.0551  74  ALA A C   
1086  O O   . ALA A 74  ? 0.7886 0.8515 0.8763 0.1589  -0.2496 0.0457  74  ALA A O   
1087  C CB  . ALA A 74  ? 0.9200 0.9100 0.9536 0.1526  -0.2624 0.0833  74  ALA A CB  
1093  N N   . THR A 75  ? 0.7447 0.8124 0.8067 0.1304  -0.2297 0.0520  75  THR A N   
1094  C CA  . THR A 75  ? 0.7002 0.8031 0.7795 0.1302  -0.2287 0.0390  75  THR A CA  
1095  C C   . THR A 75  ? 0.6933 0.8135 0.7934 0.1252  -0.2135 0.0246  75  THR A C   
1096  O O   . THR A 75  ? 0.6830 0.7886 0.7795 0.1193  -0.2021 0.0254  75  THR A O   
1097  C CB  . THR A 75  ? 0.6789 0.7901 0.7399 0.1183  -0.2270 0.0431  75  THR A CB  
1098  O OG1 . THR A 75  ? 0.6732 0.7777 0.7235 0.1036  -0.2104 0.0441  75  THR A OG1 
1099  C CG2 . THR A 75  ? 0.6588 0.7519 0.6942 0.1213  -0.2402 0.0590  75  THR A CG2 
1107  N N   . GLY A 76  ? 0.6598 0.8123 0.7814 0.1270  -0.2138 0.0118  76  GLY A N   
1108  C CA  . GLY A 76  ? 0.6518 0.8248 0.7921 0.1202  -0.1995 -0.0011 76  GLY A CA  
1109  C C   . GLY A 76  ? 0.6554 0.8344 0.7857 0.1026  -0.1882 -0.0016 76  GLY A C   
1110  O O   . GLY A 76  ? 0.6582 0.8186 0.7648 0.0949  -0.1863 0.0082  76  GLY A O   
1114  N N   . ASN A 77  ? 0.6531 0.8589 0.8020 0.0963  -0.1807 -0.0135 77  ASN A N   
1115  C CA  . ASN A 77  ? 0.6133 0.8234 0.7546 0.0799  -0.1707 -0.0153 77  ASN A CA  
1116  C C   . ASN A 77  ? 0.6160 0.8380 0.7521 0.0768  -0.1806 -0.0158 77  ASN A C   
1117  O O   . ASN A 77  ? 0.6344 0.8800 0.7877 0.0829  -0.1907 -0.0222 77  ASN A O   
1118  C CB  . ASN A 77  ? 0.5686 0.7999 0.7302 0.0725  -0.1587 -0.0265 77  ASN A CB  
1119  C CG  . ASN A 77  ? 0.5975 0.8168 0.7600 0.0733  -0.1475 -0.0264 77  ASN A CG  
1120  O OD1 . ASN A 77  ? 0.6118 0.8043 0.7565 0.0741  -0.1457 -0.0176 77  ASN A OD1 
1121  N ND2 . ASN A 77  ? 0.5858 0.8266 0.7688 0.0724  -0.1399 -0.0364 77  ASN A ND2 
1128  N N   . ARG A 78  ? 0.6106 0.8175 0.7233 0.0677  -0.1779 -0.0099 78  ARG A N   
1129  C CA  . ARG A 78  ? 0.6149 0.8328 0.7208 0.0624  -0.1853 -0.0127 78  ARG A CA  
1130  C C   . ARG A 78  ? 0.6360 0.8772 0.7607 0.0517  -0.1798 -0.0253 78  ARG A C   
1131  O O   . ARG A 78  ? 0.6702 0.9125 0.8045 0.0448  -0.1671 -0.0292 78  ARG A O   
1132  C CB  . ARG A 78  ? 0.6240 0.8209 0.7002 0.0554  -0.1816 -0.0052 78  ARG A CB  
1133  C CG  . ARG A 78  ? 0.6195 0.7984 0.6745 0.0636  -0.1900 0.0080  78  ARG A CG  
1134  C CD  . ARG A 78  ? 0.6310 0.7925 0.6584 0.0560  -0.1831 0.0148  78  ARG A CD  
1135  N NE  . ARG A 78  ? 0.6739 0.8202 0.6995 0.0516  -0.1690 0.0180  78  ARG A NE  
1136  C CZ  . ARG A 78  ? 0.7093 0.8411 0.7146 0.0463  -0.1613 0.0245  78  ARG A CZ  
1137  N NH1 . ARG A 78  ? 0.7411 0.8713 0.7248 0.0448  -0.1654 0.0282  78  ARG A NH1 
1138  N NH2 . ARG A 78  ? 0.6826 0.8033 0.6893 0.0428  -0.1497 0.0267  78  ARG A NH2 
1152  N N   . ASP A 79  ? 0.6313 0.8913 0.7606 0.0496  -0.1902 -0.0313 79  ASP A N   
1153  C CA  . ASP A 79  ? 0.6497 0.9327 0.7971 0.0377  -0.1872 -0.0431 79  ASP A CA  
1154  C C   . ASP A 79  ? 0.6600 0.9321 0.7879 0.0249  -0.1853 -0.0451 79  ASP A C   
1155  O O   . ASP A 79  ? 0.6714 0.9366 0.7797 0.0276  -0.1948 -0.0421 79  ASP A O   
1156  C CB  . ASP A 79  ? 0.6267 0.9423 0.7972 0.0435  -0.2010 -0.0506 79  ASP A CB  
1157  C CG  . ASP A 79  ? 0.6492 0.9838 0.8475 0.0535  -0.1995 -0.0542 79  ASP A CG  
1158  O OD1 . ASP A 79  ? 0.6673 0.9877 0.8648 0.0559  -0.1883 -0.0506 79  ASP A OD1 
1159  O OD2 . ASP A 79  ? 0.6638 1.0290 0.8852 0.0593  -0.2099 -0.0613 79  ASP A OD2 
1164  N N   . TYR A 80  ? 0.6669 0.9365 0.7989 0.0113  -0.1734 -0.0502 80  TYR A N   
1165  C CA  . TYR A 80  ? 0.6935 0.9571 0.8134 -0.0012 -0.1737 -0.0559 80  TYR A CA  
1166  C C   . TYR A 80  ? 0.6628 0.9543 0.7996 -0.0069 -0.1850 -0.0664 80  TYR A C   
1167  O O   . TYR A 80  ? 0.6732 0.9623 0.7967 -0.0119 -0.1928 -0.0710 80  TYR A O   
1168  C CB  . TYR A 80  ? 0.7268 0.9765 0.8459 -0.0138 -0.1588 -0.0575 80  TYR A CB  
1169  C CG  . TYR A 80  ? 0.7734 1.0163 0.8838 -0.0273 -0.1596 -0.0652 80  TYR A CG  
1170  C CD1 . TYR A 80  ? 0.7840 1.0018 0.8671 -0.0273 -0.1584 -0.0636 80  TYR A CD1 
1171  C CD2 . TYR A 80  ? 0.7966 1.0582 0.9262 -0.0403 -0.1617 -0.0747 80  TYR A CD2 
1172  C CE1 . TYR A 80  ? 0.8302 1.0393 0.9047 -0.0384 -0.1598 -0.0721 80  TYR A CE1 
1173  C CE2 . TYR A 80  ? 0.8308 1.0827 0.9518 -0.0534 -0.1635 -0.0823 80  TYR A CE2 
1174  C CZ  . TYR A 80  ? 0.8582 1.0825 0.9512 -0.0517 -0.1628 -0.0814 80  TYR A CZ  
1175  O OH  . TYR A 80  ? 0.9355 1.1477 1.0193 -0.0635 -0.1652 -0.0904 80  TYR A OH  
1185  N N   . ALA A 81  ? 0.6587 0.9782 0.8251 -0.0062 -0.1859 -0.0710 81  ALA A N   
1186  C CA  . ALA A 81  ? 0.6697 1.0220 0.8575 -0.0106 -0.1973 -0.0809 81  ALA A CA  
1187  C C   . ALA A 81  ? 0.7255 1.1073 0.9436 -0.0007 -0.1986 -0.0826 81  ALA A C   
1188  O O   . ALA A 81  ? 0.7520 1.1255 0.9721 0.0081  -0.1903 -0.0769 81  ALA A O   
1189  C CB  . ALA A 81  ? 0.6355 0.9924 0.8304 -0.0315 -0.1921 -0.0900 81  ALA A CB  
1195  N N   . LYS A 82  ? 0.7272 1.1445 0.9694 -0.0019 -0.2095 -0.0914 82  LYS A N   
1196  C CA  . LYS A 82  ? 0.7528 1.2028 1.0266 0.0088  -0.2113 -0.0950 82  LYS A CA  
1197  C C   . LYS A 82  ? 0.7796 1.2358 1.0692 0.0003  -0.1928 -0.0970 82  LYS A C   
1198  O O   . LYS A 82  ? 0.8314 1.2918 1.1260 -0.0192 -0.1838 -0.1014 82  LYS A O   
1199  C CB  . LYS A 82  ? 0.7717 1.2633 1.0715 0.0064  -0.2254 -0.1056 82  LYS A CB  
1200  C CG  . LYS A 82  ? 0.8355 1.3600 1.1640 0.0251  -0.2336 -0.1086 82  LYS A CG  
1201  C CD  . LYS A 82  ? 0.9064 1.4791 1.2670 0.0199  -0.2449 -0.1207 82  LYS A CD  
1202  C CE  . LYS A 82  ? 0.9659 1.5681 1.3501 0.0432  -0.2589 -0.1231 82  LYS A CE  
1203  N NZ  . LYS A 82  ? 1.0258 1.6069 1.3856 0.0600  -0.2773 -0.1148 82  LYS A NZ  
1217  N N   . ASP A 83  ? 0.7402 1.1952 1.0361 0.0148  -0.1874 -0.0934 83  ASP A N   
1218  C CA  . ASP A 83  ? 0.7421 1.2019 1.0495 0.0092  -0.1698 -0.0948 83  ASP A CA  
1219  C C   . ASP A 83  ? 0.7158 1.1411 0.9986 -0.0053 -0.1560 -0.0885 83  ASP A C   
1220  O O   . ASP A 83  ? 0.7255 1.1558 1.0158 -0.0169 -0.1417 -0.0900 83  ASP A O   
1221  C CB  . ASP A 83  ? 0.8238 1.3296 1.1660 -0.0016 -0.1662 -0.1060 83  ASP A CB  
1222  C CG  . ASP A 83  ? 0.9054 1.4501 1.2764 0.0147  -0.1790 -0.1134 83  ASP A CG  
1223  O OD1 . ASP A 83  ? 0.9311 1.4739 1.3056 0.0349  -0.1806 -0.1118 83  ASP A OD1 
1224  O OD2 . ASP A 83  ? 0.9333 1.5098 1.3233 0.0077  -0.1884 -0.1211 83  ASP A OD2 
1229  N N   . ASP A 84  ? 0.6798 1.0709 0.9328 -0.0045 -0.1603 -0.0814 84  ASP A N   
1230  C CA  . ASP A 84  ? 0.6415 0.9989 0.8704 -0.0154 -0.1490 -0.0756 84  ASP A CA  
1231  C C   . ASP A 84  ? 0.6039 0.9293 0.8072 -0.0022 -0.1505 -0.0656 84  ASP A C   
1232  O O   . ASP A 84  ? 0.6151 0.9236 0.7977 -0.0006 -0.1583 -0.0622 84  ASP A O   
1233  C CB  . ASP A 84  ? 0.6632 1.0142 0.8828 -0.0317 -0.1521 -0.0795 84  ASP A CB  
1234  C CG  . ASP A 84  ? 0.6904 1.0126 0.8929 -0.0447 -0.1392 -0.0758 84  ASP A CG  
1235  O OD1 . ASP A 84  ? 0.6825 0.9830 0.8718 -0.0386 -0.1306 -0.0682 84  ASP A OD1 
1236  O OD2 . ASP A 84  ? 0.7316 1.0520 0.9338 -0.0611 -0.1386 -0.0807 84  ASP A OD2 
1241  N N   . PRO A 85  ? 0.5726 0.8898 0.7762 0.0069  -0.1432 -0.0609 85  PRO A N   
1242  C CA  . PRO A 85  ? 0.5673 0.8562 0.7490 0.0187  -0.1456 -0.0511 85  PRO A CA  
1243  C C   . PRO A 85  ? 0.6234 0.8820 0.7786 0.0105  -0.1391 -0.0450 85  PRO A C   
1244  O O   . PRO A 85  ? 0.6439 0.8966 0.7973 -0.0020 -0.1287 -0.0466 85  PRO A O   
1245  C CB  . PRO A 85  ? 0.5388 0.8279 0.7301 0.0273  -0.1381 -0.0499 85  PRO A CB  
1246  C CG  . PRO A 85  ? 0.5368 0.8609 0.7574 0.0244  -0.1350 -0.0601 85  PRO A CG  
1247  C CD  . PRO A 85  ? 0.5907 0.9258 0.8148 0.0066  -0.1329 -0.0648 85  PRO A CD  
1255  N N   . LEU A 86  ? 0.6136 0.8533 0.7479 0.0180  -0.1455 -0.0376 86  LEU A N   
1256  C CA  . LEU A 86  ? 0.5820 0.7952 0.6916 0.0129  -0.1393 -0.0319 86  LEU A CA  
1257  C C   . LEU A 86  ? 0.5925 0.7880 0.6962 0.0159  -0.1291 -0.0248 86  LEU A C   
1258  O O   . LEU A 86  ? 0.6010 0.7798 0.6919 0.0094  -0.1203 -0.0224 86  LEU A O   
1259  C CB  . LEU A 86  ? 0.5896 0.7934 0.6788 0.0186  -0.1493 -0.0269 86  LEU A CB  
1260  C CG  . LEU A 86  ? 0.5947 0.7751 0.6583 0.0150  -0.1433 -0.0218 86  LEU A CG  
1261  C CD1 . LEU A 86  ? 0.6117 0.7908 0.6715 0.0033  -0.1400 -0.0301 86  LEU A CD1 
1262  C CD2 . LEU A 86  ? 0.6323 0.8059 0.6761 0.0225  -0.1522 -0.0146 86  LEU A CD2 
1274  N N   . GLU A 87  ? 0.6029 0.8012 0.7155 0.0261  -0.1309 -0.0222 87  GLU A N   
1275  C CA  . GLU A 87  ? 0.5667 0.7479 0.6732 0.0295  -0.1233 -0.0160 87  GLU A CA  
1276  C C   . GLU A 87  ? 0.5276 0.7218 0.6541 0.0360  -0.1218 -0.0205 87  GLU A C   
1277  O O   . GLU A 87  ? 0.5202 0.7368 0.6651 0.0405  -0.1279 -0.0272 87  GLU A O   
1278  C CB  . GLU A 87  ? 0.5986 0.7603 0.6864 0.0366  -0.1289 -0.0057 87  GLU A CB  
1279  C CG  . GLU A 87  ? 0.6026 0.7700 0.6927 0.0473  -0.1431 -0.0036 87  GLU A CG  
1280  C CD  . GLU A 87  ? 0.6267 0.7751 0.6937 0.0505  -0.1485 0.0078  87  GLU A CD  
1281  O OE1 . GLU A 87  ? 0.6632 0.7978 0.7139 0.0440  -0.1409 0.0126  87  GLU A OE1 
1282  O OE2 . GLU A 87  ? 0.6552 0.8032 0.7204 0.0595  -0.1605 0.0123  87  GLU A OE2 
1289  N N   . PHE A 88  ? 0.5539 0.7355 0.6771 0.0370  -0.1138 -0.0176 88  PHE A N   
1290  C CA  . PHE A 88  ? 0.5592 0.7509 0.6984 0.0434  -0.1107 -0.0230 88  PHE A CA  
1291  C C   . PHE A 88  ? 0.5942 0.7634 0.7233 0.0514  -0.1119 -0.0165 88  PHE A C   
1292  O O   . PHE A 88  ? 0.5878 0.7412 0.7051 0.0461  -0.1041 -0.0122 88  PHE A O   
1293  C CB  . PHE A 88  ? 0.5482 0.7503 0.6945 0.0331  -0.0979 -0.0283 88  PHE A CB  
1294  C CG  . PHE A 88  ? 0.5331 0.7531 0.6875 0.0219  -0.0963 -0.0334 88  PHE A CG  
1295  C CD1 . PHE A 88  ? 0.5454 0.7524 0.6854 0.0107  -0.0933 -0.0299 88  PHE A CD1 
1296  C CD2 . PHE A 88  ? 0.5110 0.7611 0.6881 0.0226  -0.0984 -0.0423 88  PHE A CD2 
1297  C CE1 . PHE A 88  ? 0.5103 0.7302 0.6570 -0.0005 -0.0928 -0.0349 88  PHE A CE1 
1298  C CE2 . PHE A 88  ? 0.5023 0.7689 0.6875 0.0103  -0.0974 -0.0469 88  PHE A CE2 
1299  C CZ  . PHE A 88  ? 0.5028 0.7525 0.6721 -0.0017 -0.0949 -0.0431 88  PHE A CZ  
1309  N N   . LYS A 89  ? 0.6181 0.7853 0.7520 0.0642  -0.1224 -0.0157 89  LYS A N   
1310  C CA  . LYS A 89  ? 0.6001 0.7429 0.7238 0.0712  -0.1258 -0.0090 89  LYS A CA  
1311  C C   . LYS A 89  ? 0.6075 0.7517 0.7429 0.0785  -0.1224 -0.0163 89  LYS A C   
1312  O O   . LYS A 89  ? 0.6534 0.7756 0.7799 0.0815  -0.1230 -0.0120 89  LYS A O   
1313  C CB  . LYS A 89  ? 0.5675 0.7012 0.6862 0.0809  -0.1405 -0.0024 89  LYS A CB  
1314  C CG  . LYS A 89  ? 0.5878 0.7165 0.6896 0.0742  -0.1440 0.0060  89  LYS A CG  
1315  C CD  . LYS A 89  ? 0.6171 0.7390 0.7129 0.0838  -0.1592 0.0129  89  LYS A CD  
1316  C CE  . LYS A 89  ? 0.6494 0.7680 0.7259 0.0769  -0.1620 0.0205  89  LYS A CE  
1317  N NZ  . LYS A 89  ? 0.7091 0.8209 0.7766 0.0856  -0.1772 0.0287  89  LYS A NZ  
1331  N N   . SER A 90  ? 0.5725 0.7429 0.7277 0.0810  -0.1187 -0.0278 90  SER A N   
1332  C CA  . SER A 90  ? 0.5665 0.7411 0.7323 0.0887  -0.1146 -0.0367 90  SER A CA  
1333  C C   . SER A 90  ? 0.5738 0.7356 0.7275 0.0795  -0.1029 -0.0350 90  SER A C   
1334  O O   . SER A 90  ? 0.5234 0.6903 0.6714 0.0665  -0.0938 -0.0330 90  SER A O   
1335  C CB  . SER A 90  ? 0.5017 0.7124 0.6913 0.0914  -0.1110 -0.0495 90  SER A CB  
1336  O OG  . SER A 90  ? 0.5436 0.7679 0.7469 0.1024  -0.1234 -0.0522 90  SER A OG  
1342  N N   . HIS A 91  ? 0.6330 0.7770 0.7823 0.0864  -0.1042 -0.0360 91  HIS A N   
1343  C CA  . HIS A 91  ? 0.6494 0.7809 0.7870 0.0789  -0.0951 -0.0349 91  HIS A CA  
1344  C C   . HIS A 91  ? 0.6362 0.7510 0.7558 0.0670  -0.0930 -0.0225 91  HIS A C   
1345  O O   . HIS A 91  ? 0.6147 0.7269 0.7260 0.0579  -0.0840 -0.0212 91  HIS A O   
1346  C CB  . HIS A 91  ? 0.6396 0.7949 0.7853 0.0737  -0.0827 -0.0444 91  HIS A CB  
1347  C CG  . HIS A 91  ? 0.6966 0.8751 0.8620 0.0851  -0.0828 -0.0579 91  HIS A CG  
1348  N ND1 . HIS A 91  ? 0.7359 0.9078 0.9043 0.0970  -0.0847 -0.0663 91  HIS A ND1 
1349  C CD2 . HIS A 91  ? 0.7091 0.9191 0.8933 0.0867  -0.0813 -0.0653 91  HIS A CD2 
1350  C CE1 . HIS A 91  ? 0.7292 0.9282 0.9175 0.1068  -0.0839 -0.0788 91  HIS A CE1 
1351  N NE2 . HIS A 91  ? 0.6989 0.9228 0.8979 0.1004  -0.0817 -0.0781 91  HIS A NE2 
1359  N N   . GLN A 92  ? 0.6496 0.7538 0.7624 0.0675  -0.1013 -0.0136 92  GLN A N   
1360  C CA  . GLN A 92  ? 0.6463 0.7373 0.7428 0.0576  -0.0991 -0.0029 92  GLN A CA  
1361  C C   . GLN A 92  ? 0.6767 0.7449 0.7614 0.0557  -0.0991 0.0033  92  GLN A C   
1362  O O   . GLN A 92  ? 0.6547 0.7147 0.7273 0.0475  -0.0958 0.0113  92  GLN A O   
1363  C CB  . GLN A 92  ? 0.6383 0.7271 0.7297 0.0588  -0.1077 0.0042  92  GLN A CB  
1364  C CG  . GLN A 92  ? 0.6405 0.7128 0.7290 0.0681  -0.1194 0.0096  92  GLN A CG  
1365  C CD  . GLN A 92  ? 0.6232 0.6967 0.7065 0.0701  -0.1286 0.0161  92  GLN A CD  
1366  O OE1 . GLN A 92  ? 0.6039 0.6861 0.6813 0.0629  -0.1255 0.0180  92  GLN A OE1 
1367  N NE2 . GLN A 92  ? 0.6496 0.7133 0.7339 0.0805  -0.1406 0.0192  92  GLN A NE2 
1376  N N   . TRP A 93  ? 0.7121 0.7704 0.8007 0.0633  -0.1030 -0.0010 93  TRP A N   
1377  C CA  . TRP A 93  ? 0.6712 0.7075 0.7498 0.0605  -0.1038 0.0037  93  TRP A CA  
1378  C C   . TRP A 93  ? 0.6305 0.6488 0.6973 0.0571  -0.1106 0.0171  93  TRP A C   
1379  O O   . TRP A 93  ? 0.6436 0.6513 0.7005 0.0487  -0.1079 0.0243  93  TRP A O   
1380  C CB  . TRP A 93  ? 0.6627 0.7028 0.7357 0.0509  -0.0934 0.0029  93  TRP A CB  
1381  C CG  . TRP A 93  ? 0.6746 0.7234 0.7539 0.0538  -0.0879 -0.0089 93  TRP A CG  
1382  C CD1 . TRP A 93  ? 0.6567 0.7273 0.7468 0.0568  -0.0827 -0.0184 93  TRP A CD1 
1383  C CD2 . TRP A 93  ? 0.6565 0.6942 0.7310 0.0530  -0.0867 -0.0125 93  TRP A CD2 
1384  N NE1 . TRP A 93  ? 0.6845 0.7588 0.7756 0.0584  -0.0776 -0.0276 93  TRP A NE1 
1385  C CE2 . TRP A 93  ? 0.6634 0.7169 0.7444 0.0565  -0.0805 -0.0246 93  TRP A CE2 
1386  C CE3 . TRP A 93  ? 0.6055 0.6226 0.6707 0.0490  -0.0905 -0.0070 93  TRP A CE3 
1387  C CZ2 . TRP A 93  ? 0.6328 0.6812 0.7096 0.0570  -0.0781 -0.0319 93  TRP A CZ2 
1388  C CZ3 . TRP A 93  ? 0.5953 0.6069 0.6578 0.0489  -0.0890 -0.0144 93  TRP A CZ3 
1389  C CH2 . TRP A 93  ? 0.6045 0.6311 0.6718 0.0534  -0.0830 -0.0270 93  TRP A CH2 
1400  N N   . PHE A 94  ? 0.6412 0.6576 0.7091 0.0635  -0.1195 0.0208  94  PHE A N   
1401  C CA  . PHE A 94  ? 0.7104 0.7094 0.7652 0.0601  -0.1262 0.0345  94  PHE A CA  
1402  C C   . PHE A 94  ? 0.7315 0.7048 0.7815 0.0599  -0.1312 0.0384  94  PHE A C   
1403  O O   . PHE A 94  ? 0.7528 0.7168 0.8104 0.0694  -0.1371 0.0312  94  PHE A O   
1404  C CB  . PHE A 94  ? 0.7212 0.7218 0.7765 0.0679  -0.1364 0.0380  94  PHE A CB  
1405  C CG  . PHE A 94  ? 0.7065 0.6893 0.7458 0.0639  -0.1431 0.0532  94  PHE A CG  
1406  C CD1 . PHE A 94  ? 0.6869 0.6753 0.7138 0.0536  -0.1374 0.0615  94  PHE A CD1 
1407  C CD2 . PHE A 94  ? 0.7264 0.6862 0.7621 0.0704  -0.1550 0.0594  94  PHE A CD2 
1408  C CE1 . PHE A 94  ? 0.6990 0.6739 0.7101 0.0489  -0.1422 0.0757  94  PHE A CE1 
1409  C CE2 . PHE A 94  ? 0.7328 0.6758 0.7519 0.0649  -0.1608 0.0751  94  PHE A CE2 
1410  C CZ  . PHE A 94  ? 0.7154 0.6676 0.7221 0.0537  -0.1538 0.0833  94  PHE A CZ  
1420  N N   . GLY A 95  ? 0.7044 0.6668 0.7425 0.0491  -0.1292 0.0492  95  GLY A N   
1421  C CA  . GLY A 95  ? 0.7053 0.6442 0.7387 0.0452  -0.1331 0.0533  95  GLY A CA  
1422  C C   . GLY A 95  ? 0.7478 0.6896 0.7833 0.0387  -0.1251 0.0471  95  GLY A C   
1423  O O   . GLY A 95  ? 0.8127 0.7358 0.8453 0.0345  -0.1286 0.0489  95  GLY A O   
1427  N N   . ALA A 96  ? 0.7469 0.7106 0.7867 0.0372  -0.1154 0.0402  96  ALA A N   
1428  C CA  . ALA A 96  ? 0.7319 0.6992 0.7714 0.0306  -0.1083 0.0361  96  ALA A CA  
1429  C C   . ALA A 96  ? 0.7694 0.7307 0.8006 0.0189  -0.1070 0.0472  96  ALA A C   
1430  O O   . ALA A 96  ? 0.7841 0.7430 0.8148 0.0132  -0.1047 0.0452  96  ALA A O   
1431  C CB  . ALA A 96  ? 0.6398 0.6299 0.6830 0.0304  -0.0987 0.0295  96  ALA A CB  
1437  N N   . SER A 97  ? 0.7810 0.7422 0.8058 0.0151  -0.1082 0.0585  97  SER A N   
1438  C CA  . SER A 97  ? 0.7695 0.7282 0.7873 0.0037  -0.1065 0.0695  97  SER A CA  
1439  C C   . SER A 97  ? 0.7364 0.6828 0.7460 0.0020  -0.1132 0.0816  97  SER A C   
1440  O O   . SER A 97  ? 0.7204 0.6720 0.7273 0.0078  -0.1150 0.0831  97  SER A O   
1441  C CB  . SER A 97  ? 0.7662 0.7463 0.7827 -0.0006 -0.0968 0.0705  97  SER A CB  
1442  O OG  . SER A 97  ? 0.8194 0.8101 0.8336 0.0042  -0.0952 0.0706  97  SER A OG  
1448  N N   . VAL A 98  ? 0.7345 0.6646 0.7395 -0.0067 -0.1173 0.0905  98  VAL A N   
1449  C CA  . VAL A 98  ? 0.7689 0.6838 0.7639 -0.0103 -0.1242 0.1041  98  VAL A CA  
1450  C C   . VAL A 98  ? 0.7699 0.6850 0.7594 -0.0260 -0.1208 0.1157  98  VAL A C   
1451  O O   . VAL A 98  ? 0.7587 0.6696 0.7535 -0.0330 -0.1201 0.1132  98  VAL A O   
1452  C CB  . VAL A 98  ? 0.7978 0.6838 0.7930 -0.0035 -0.1366 0.1034  98  VAL A CB  
1453  C CG1 . VAL A 98  ? 0.8122 0.6790 0.7945 -0.0086 -0.1445 0.1200  98  VAL A CG1 
1454  C CG2 . VAL A 98  ? 0.8354 0.7264 0.8383 0.0127  -0.1395 0.0914  98  VAL A CG2 
1464  N N   . ARG A 99  ? 0.7867 0.7088 0.7659 -0.0318 -0.1185 0.1280  99  ARG A N   
1465  C CA  A ARG A 99  ? 0.8303 0.7579 0.8046 -0.0473 -0.1139 0.1399  99  ARG A CA  
1466  C CA  B ARG A 99  ? 0.8311 0.7579 0.8055 -0.0474 -0.1142 0.1399  99  ARG A CA  
1467  C C   . ARG A 99  ? 0.8643 0.7809 0.8233 -0.0527 -0.1185 0.1560  99  ARG A C   
1468  O O   . ARG A 99  ? 0.8878 0.8077 0.8390 -0.0443 -0.1203 0.1573  99  ARG A O   
1469  C CB  A ARG A 99  ? 0.7907 0.7506 0.7684 -0.0497 -0.1015 0.1365  99  ARG A CB  
1470  C CB  B ARG A 99  ? 0.7917 0.7506 0.7700 -0.0505 -0.1017 0.1366  99  ARG A CB  
1471  C CG  A ARG A 99  ? 0.8157 0.7851 0.8063 -0.0511 -0.0972 0.1264  99  ARG A CG  
1472  C CG  B ARG A 99  ? 0.8149 0.7821 0.8062 -0.0507 -0.0980 0.1255  99  ARG A CG  
1473  C CD  A ARG A 99  ? 0.7853 0.7516 0.7789 -0.0661 -0.0977 0.1336  99  ARG A CD  
1474  C CD  B ARG A 99  ? 0.7898 0.7463 0.7851 -0.0638 -0.1012 0.1302  99  ARG A CD  
1475  N NE  A ARG A 99  ? 0.7930 0.7703 0.7982 -0.0671 -0.0946 0.1240  99  ARG A NE  
1476  N NE  B ARG A 99  ? 0.8083 0.7838 0.8033 -0.0772 -0.0943 0.1400  99  ARG A NE  
1477  C CZ  A ARG A 99  ? 0.7818 0.7453 0.7926 -0.0623 -0.0999 0.1137  99  ARG A CZ  
1478  C CZ  B ARG A 99  ? 0.7871 0.7541 0.7762 -0.0912 -0.0965 0.1539  99  ARG A CZ  
1479  N NH1 A ARG A 99  ? 0.8008 0.7397 0.8084 -0.0552 -0.1081 0.1107  99  ARG A NH1 
1480  N NH1 B ARG A 99  ? 0.7452 0.7361 0.7363 -0.1030 -0.0885 0.1612  99  ARG A NH1 
1481  N NH2 A ARG A 99  ? 0.7590 0.7344 0.7782 -0.0638 -0.0972 0.1059  99  ARG A NH2 
1482  N NH2 B ARG A 99  ? 0.7748 0.7101 0.7566 -0.0937 -0.1067 0.1607  99  ARG A NH2 
1509  N N   . SER A 100 ? 0.8969 0.8011 0.8510 -0.0674 -0.1205 0.1686  100 SER A N   
1510  C CA  . SER A 100 ? 0.9182 0.8067 0.8557 -0.0746 -0.1259 0.1863  100 SER A CA  
1511  C C   . SER A 100 ? 0.9347 0.8389 0.8674 -0.0934 -0.1174 0.1991  100 SER A C   
1512  O O   . SER A 100 ? 1.0061 0.9063 0.9464 -0.1061 -0.1167 0.2011  100 SER A O   
1513  C CB  . SER A 100 ? 0.9347 0.7826 0.8697 -0.0738 -0.1404 0.1906  100 SER A CB  
1514  O OG  . SER A 100 ? 1.0402 0.8697 0.9571 -0.0788 -0.1473 0.2085  100 SER A OG  
1520  N N   . LYS A 101 ? 0.9044 0.8289 0.8249 -0.0953 -0.1105 0.2068  101 LYS A N   
1521  C CA  . LYS A 101 ? 0.9293 0.8665 0.8402 -0.1131 -0.1035 0.2226  101 LYS A CA  
1522  C C   . LYS A 101 ? 0.9506 0.8665 0.8392 -0.1158 -0.1115 0.2396  101 LYS A C   
1523  O O   . LYS A 101 ? 1.0266 0.9288 0.9082 -0.1015 -0.1199 0.2369  101 LYS A O   
1524  C CB  . LYS A 101 ? 0.9503 0.9298 0.8637 -0.1125 -0.0886 0.2170  101 LYS A CB  
1525  C CG  . LYS A 101 ? 0.9849 0.9869 0.8935 -0.1309 -0.0784 0.2300  101 LYS A CG  
1526  C CD  . LYS A 101 ? 1.0131 1.0562 0.9233 -0.1255 -0.0645 0.2219  101 LYS A CD  
1527  C CE  . LYS A 101 ? 1.0693 1.1411 0.9767 -0.1424 -0.0527 0.2330  101 LYS A CE  
1528  N NZ  . LYS A 101 ? 1.1439 1.2128 1.0650 -0.1595 -0.0533 0.2391  101 LYS A NZ  
1542  N N   . GLN A 102 ? 0.9677 0.8841 0.8448 -0.1346 -0.1083 0.2575  102 GLN A N   
1543  C CA  . GLN A 102 ? 0.9999 0.8801 0.8600 -0.1438 -0.1198 0.2766  102 GLN A CA  
1544  C C   . GLN A 102 ? 1.0436 0.8958 0.8912 -0.1274 -0.1339 0.2779  102 GLN A C   
1545  O O   . GLN A 102 ? 1.0929 0.9095 0.9449 -0.1215 -0.1473 0.2761  102 GLN A O   
1546  C CB  . GLN A 102 ? 1.0954 0.9932 0.9376 -0.1622 -0.1108 0.2958  102 GLN A CB  
1547  C CG  . GLN A 102 ? 1.2326 1.1626 1.0883 -0.1793 -0.0966 0.2957  102 GLN A CG  
1548  C CD  . GLN A 102 ? 1.3563 1.3295 1.2025 -0.1841 -0.0809 0.2996  102 GLN A CD  
1549  O OE1 . GLN A 102 ? 1.3245 1.3155 1.1648 -0.1686 -0.0771 0.2903  102 GLN A OE1 
1550  N NE2 . GLN A 102 ? 1.4664 1.4576 1.3115 -0.2059 -0.0717 0.3126  102 GLN A NE2 
1559  N N   . ASP A 103 ? 1.0609 0.9292 0.8941 -0.1188 -0.1319 0.2795  103 ASP A N   
1560  C CA  . ASP A 103 ? 1.0831 0.9303 0.9082 -0.1013 -0.1457 0.2778  103 ASP A CA  
1561  C C   . ASP A 103 ? 1.0257 0.8892 0.8684 -0.0816 -0.1445 0.2547  103 ASP A C   
1562  O O   . ASP A 103 ? 1.0684 0.9125 0.9163 -0.0663 -0.1565 0.2476  103 ASP A O   
1563  C CB  . ASP A 103 ? 1.1670 1.0206 0.9651 -0.1023 -0.1468 0.2923  103 ASP A CB  
1564  C CG  . ASP A 103 ? 1.3432 1.1684 1.1194 -0.1183 -0.1540 0.3180  103 ASP A CG  
1565  O OD1 . ASP A 103 ? 1.4145 1.1999 1.1930 -0.1186 -0.1674 0.3237  103 ASP A OD1 
1566  O OD2 . ASP A 103 ? 1.4183 1.2602 1.1739 -0.1305 -0.1463 0.3323  103 ASP A OD2 
1571  N N   . LYS A 104 ? 0.9150 0.8140 0.7672 -0.0820 -0.1301 0.2431  104 LYS A N   
1572  C CA  . LYS A 104 ? 0.8831 0.7997 0.7492 -0.0657 -0.1275 0.2228  104 LYS A CA  
1573  C C   . LYS A 104 ? 0.8183 0.7202 0.7057 -0.0581 -0.1323 0.2092  104 LYS A C   
1574  O O   . LYS A 104 ? 0.7664 0.6582 0.6625 -0.0676 -0.1314 0.2106  104 LYS A O   
1575  C CB  . LYS A 104 ? 0.9231 0.8774 0.7931 -0.0693 -0.1113 0.2152  104 LYS A CB  
1576  C CG  . LYS A 104 ? 0.9956 0.9683 0.8439 -0.0762 -0.1049 0.2265  104 LYS A CG  
1577  C CD  . LYS A 104 ? 0.9949 1.0025 0.8484 -0.0828 -0.0884 0.2212  104 LYS A CD  
1578  C CE  . LYS A 104 ? 1.0088 1.0188 0.8642 -0.1016 -0.0824 0.2338  104 LYS A CE  
1579  N NZ  . LYS A 104 ? 1.0330 1.0466 0.8646 -0.1146 -0.0799 0.2531  104 LYS A NZ  
1593  N N   . ILE A 105 ? 0.8405 0.7426 0.7362 -0.0415 -0.1375 0.1958  105 ILE A N   
1594  C CA  . ILE A 105 ? 0.8395 0.7343 0.7550 -0.0325 -0.1401 0.1803  105 ILE A CA  
1595  C C   . ILE A 105 ? 0.8419 0.7633 0.7676 -0.0221 -0.1331 0.1639  105 ILE A C   
1596  O O   . ILE A 105 ? 0.8673 0.7973 0.7872 -0.0137 -0.1359 0.1619  105 ILE A O   
1597  C CB  . ILE A 105 ? 0.8812 0.7449 0.7979 -0.0220 -0.1557 0.1806  105 ILE A CB  
1598  C CG1 . ILE A 105 ? 0.9616 0.7936 0.8659 -0.0328 -0.1642 0.1984  105 ILE A CG1 
1599  C CG2 . ILE A 105 ? 0.8285 0.6888 0.7655 -0.0126 -0.1565 0.1630  105 ILE A CG2 
1600  C CD1 . ILE A 105 ? 1.0008 0.7981 0.9057 -0.0212 -0.1808 0.1989  105 ILE A CD1 
1612  N N   . LEU A 106 ? 0.7950 0.7284 0.7352 -0.0231 -0.1248 0.1524  106 LEU A N   
1613  C CA  . LEU A 106 ? 0.7149 0.6708 0.6646 -0.0151 -0.1178 0.1376  106 LEU A CA  
1614  C C   . LEU A 106 ? 0.7784 0.7276 0.7443 -0.0069 -0.1205 0.1242  106 LEU A C   
1615  O O   . LEU A 106 ? 0.8368 0.7790 0.8099 -0.0118 -0.1189 0.1219  106 LEU A O   
1616  C CB  . LEU A 106 ? 0.7011 0.6800 0.6517 -0.0230 -0.1048 0.1363  106 LEU A CB  
1617  C CG  . LEU A 106 ? 0.6486 0.6474 0.6071 -0.0155 -0.0979 0.1222  106 LEU A CG  
1618  C CD1 . LEU A 106 ? 0.6519 0.6572 0.6026 -0.0080 -0.1009 0.1200  106 LEU A CD1 
1619  C CD2 . LEU A 106 ? 0.6301 0.6487 0.5900 -0.0218 -0.0865 0.1212  106 LEU A CD2 
1631  N N   . ALA A 107 ? 0.7858 0.7389 0.7573 0.0050  -0.1244 0.1149  107 ALA A N   
1632  C CA  . ALA A 107 ? 0.7562 0.7087 0.7428 0.0133  -0.1253 0.1010  107 ALA A CA  
1633  C C   . ALA A 107 ? 0.7133 0.6886 0.7062 0.0185  -0.1191 0.0900  107 ALA A C   
1634  O O   . ALA A 107 ? 0.7237 0.7093 0.7101 0.0201  -0.1195 0.0920  107 ALA A O   
1635  C CB  . ALA A 107 ? 0.7694 0.7028 0.7594 0.0235  -0.1378 0.0999  107 ALA A CB  
1641  N N   . CYS A 108 ? 0.7122 0.6946 0.7167 0.0203  -0.1136 0.0787  108 CYS A N   
1642  C CA  . CYS A 108 ? 0.7497 0.7517 0.7596 0.0223  -0.1066 0.0695  108 CYS A CA  
1643  C C   . CYS A 108 ? 0.7150 0.7209 0.7385 0.0296  -0.1072 0.0571  108 CYS A C   
1644  O O   . CYS A 108 ? 0.7049 0.7001 0.7339 0.0326  -0.1102 0.0537  108 CYS A O   
1645  C CB  . CYS A 108 ? 0.7552 0.7663 0.7632 0.0146  -0.0965 0.0694  108 CYS A CB  
1646  S SG  . CYS A 108 ? 0.7533 0.7682 0.7474 0.0064  -0.0929 0.0815  108 CYS A SG  
1651  N N   . ALA A 109 ? 0.6836 0.7059 0.7121 0.0320  -0.1040 0.0500  109 ALA A N   
1652  C CA  . ALA A 109 ? 0.6674 0.6997 0.7091 0.0371  -0.1023 0.0382  109 ALA A CA  
1653  C C   . ALA A 109 ? 0.6500 0.6941 0.6925 0.0311  -0.0921 0.0337  109 ALA A C   
1654  O O   . ALA A 109 ? 0.5921 0.6472 0.6344 0.0295  -0.0900 0.0316  109 ALA A O   
1655  C CB  . ALA A 109 ? 0.6570 0.6988 0.7057 0.0445  -0.1090 0.0343  109 ALA A CB  
1661  N N   . PRO A 110 ? 0.6751 0.7159 0.7176 0.0276  -0.0865 0.0321  110 PRO A N   
1662  C CA  . PRO A 110 ? 0.6661 0.7150 0.7069 0.0220  -0.0779 0.0299  110 PRO A CA  
1663  C C   . PRO A 110 ? 0.6755 0.7372 0.7245 0.0226  -0.0741 0.0213  110 PRO A C   
1664  O O   . PRO A 110 ? 0.7308 0.7968 0.7772 0.0176  -0.0679 0.0204  110 PRO A O   
1665  C CB  . PRO A 110 ? 0.6412 0.6828 0.6797 0.0191  -0.0751 0.0309  110 PRO A CB  
1666  C CG  . PRO A 110 ? 0.6637 0.6919 0.7010 0.0209  -0.0820 0.0352  110 PRO A CG  
1667  C CD  . PRO A 110 ? 0.6650 0.6929 0.7075 0.0281  -0.0888 0.0328  110 PRO A CD  
1675  N N   . LEU A 111 ? 0.6075 0.6758 0.6667 0.0284  -0.0777 0.0150  111 LEU A N   
1676  C CA  . LEU A 111 ? 0.5860 0.6707 0.6550 0.0277  -0.0736 0.0068  111 LEU A CA  
1677  C C   . LEU A 111 ? 0.5847 0.6802 0.6610 0.0309  -0.0793 0.0045  111 LEU A C   
1678  O O   . LEU A 111 ? 0.5804 0.6920 0.6696 0.0331  -0.0788 -0.0033 111 LEU A O   
1679  C CB  . LEU A 111 ? 0.5838 0.6736 0.6609 0.0316  -0.0712 -0.0009 111 LEU A CB  
1680  C CG  . LEU A 111 ? 0.6115 0.6983 0.6820 0.0260  -0.0635 -0.0013 111 LEU A CG  
1681  C CD1 . LEU A 111 ? 0.6289 0.7194 0.7049 0.0311  -0.0621 -0.0096 111 LEU A CD1 
1682  C CD2 . LEU A 111 ? 0.6326 0.7288 0.7015 0.0178  -0.0560 -0.0015 111 LEU A CD2 
1694  N N   . TYR A 112 ? 0.5519 0.6410 0.6202 0.0311  -0.0847 0.0109  112 TYR A N   
1695  C CA  . TYR A 112 ? 0.6119 0.7113 0.6838 0.0326  -0.0904 0.0092  112 TYR A CA  
1696  C C   . TYR A 112 ? 0.6711 0.7788 0.7423 0.0241  -0.0846 0.0059  112 TYR A C   
1697  O O   . TYR A 112 ? 0.7199 0.8185 0.7796 0.0188  -0.0801 0.0099  112 TYR A O   
1698  C CB  . TYR A 112 ? 0.6411 0.7296 0.7011 0.0351  -0.0979 0.0178  112 TYR A CB  
1699  C CG  . TYR A 112 ? 0.6029 0.6997 0.6595 0.0342  -0.1028 0.0174  112 TYR A CG  
1700  C CD1 . TYR A 112 ? 0.5653 0.6707 0.6290 0.0410  -0.1127 0.0154  112 TYR A CD1 
1701  C CD2 . TYR A 112 ? 0.5843 0.6801 0.6303 0.0274  -0.0983 0.0184  112 TYR A CD2 
1702  C CE1 . TYR A 112 ? 0.5572 0.6708 0.6167 0.0398  -0.1181 0.0145  112 TYR A CE1 
1703  C CE2 . TYR A 112 ? 0.5859 0.6884 0.6273 0.0264  -0.1032 0.0166  112 TYR A CE2 
1704  C CZ  . TYR A 112 ? 0.5975 0.7093 0.6453 0.0321  -0.1132 0.0148  112 TYR A CZ  
1705  O OH  . TYR A 112 ? 0.5911 0.7105 0.6334 0.0309  -0.1191 0.0125  112 TYR A OH  
1715  N N   . HIS A 113 ? 0.6534 0.7783 0.7375 0.0228  -0.0849 -0.0016 113 HIS A N   
1716  C CA  . HIS A 113 ? 0.6479 0.7795 0.7324 0.0135  -0.0806 -0.0050 113 HIS A CA  
1717  C C   . HIS A 113 ? 0.6350 0.7737 0.7198 0.0137  -0.0887 -0.0069 113 HIS A C   
1718  O O   . HIS A 113 ? 0.6844 0.8312 0.7758 0.0212  -0.0972 -0.0078 113 HIS A O   
1719  C CB  . HIS A 113 ? 0.6826 0.8304 0.7814 0.0086  -0.0744 -0.0120 113 HIS A CB  
1720  C CG  . HIS A 113 ? 0.6905 0.8348 0.7893 0.0096  -0.0673 -0.0117 113 HIS A CG  
1721  N ND1 . HIS A 113 ? 0.7158 0.8583 0.8180 0.0192  -0.0701 -0.0122 113 HIS A ND1 
1722  C CD2 . HIS A 113 ? 0.6794 0.8207 0.7738 0.0022  -0.0583 -0.0110 113 HIS A CD2 
1723  C CE1 . HIS A 113 ? 0.7136 0.8533 0.8136 0.0175  -0.0629 -0.0130 113 HIS A CE1 
1724  N NE2 . HIS A 113 ? 0.6884 0.8281 0.7833 0.0073  -0.0556 -0.0118 113 HIS A NE2 
1732  N N   . TRP A 114 ? 0.6272 0.7619 0.7040 0.0060  -0.0869 -0.0078 114 TRP A N   
1733  C CA  . TRP A 114 ? 0.6586 0.7990 0.7331 0.0051  -0.0946 -0.0107 114 TRP A CA  
1734  C C   . TRP A 114 ? 0.6526 0.7987 0.7319 -0.0059 -0.0916 -0.0174 114 TRP A C   
1735  O O   . TRP A 114 ? 0.6422 0.7791 0.7182 -0.0129 -0.0835 -0.0168 114 TRP A O   
1736  C CB  . TRP A 114 ? 0.7243 0.8501 0.7791 0.0080  -0.0973 -0.0048 114 TRP A CB  
1737  C CG  . TRP A 114 ? 0.7303 0.8460 0.7725 0.0017  -0.0935 -0.0066 114 TRP A CG  
1738  C CD1 . TRP A 114 ? 0.7652 0.8695 0.8032 -0.0031 -0.0850 -0.0060 114 TRP A CD1 
1739  C CD2 . TRP A 114 ? 0.7203 0.8353 0.7514 0.0008  -0.0989 -0.0097 114 TRP A CD2 
1740  N NE1 . TRP A 114 ? 0.8088 0.9042 0.8349 -0.0061 -0.0849 -0.0091 114 TRP A NE1 
1741  C CE2 . TRP A 114 ? 0.7966 0.8988 0.8180 -0.0040 -0.0930 -0.0120 114 TRP A CE2 
1742  C CE3 . TRP A 114 ? 0.6880 0.8117 0.7155 0.0042  -0.1088 -0.0112 114 TRP A CE3 
1743  C CZ2 . TRP A 114 ? 0.8640 0.9617 0.8724 -0.0053 -0.0961 -0.0171 114 TRP A CZ2 
1744  C CZ3 . TRP A 114 ? 0.7684 0.8888 0.7819 0.0019  -0.1119 -0.0156 114 TRP A CZ3 
1745  C CH2 . TRP A 114 ? 0.8586 0.9661 0.8630 -0.0026 -0.1053 -0.0192 114 TRP A CH2 
1756  N N   . ARG A 115 ? 0.6805 0.8413 0.7676 -0.0079 -0.0992 -0.0234 115 ARG A N   
1757  C CA  . ARG A 115 ? 0.7085 0.8782 0.8048 -0.0200 -0.0971 -0.0304 115 ARG A CA  
1758  C C   . ARG A 115 ? 0.7480 0.8980 0.8280 -0.0272 -0.0951 -0.0310 115 ARG A C   
1759  O O   . ARG A 115 ? 0.8105 0.9472 0.8861 -0.0334 -0.0869 -0.0291 115 ARG A O   
1760  C CB  . ARG A 115 ? 0.7054 0.8986 0.8161 -0.0197 -0.1073 -0.0373 115 ARG A CB  
1761  C CG  . ARG A 115 ? 0.7112 0.9160 0.8322 -0.0337 -0.1079 -0.0454 115 ARG A CG  
1762  C CD  . ARG A 115 ? 0.7190 0.9385 0.8435 -0.0323 -0.1211 -0.0513 115 ARG A CD  
1763  N NE  . ARG A 115 ? 0.7379 0.9743 0.8774 -0.0461 -0.1232 -0.0600 115 ARG A NE  
1764  C CZ  . ARG A 115 ? 0.7574 0.9830 0.8877 -0.0570 -0.1260 -0.0650 115 ARG A CZ  
1765  N NH1 . ARG A 115 ? 0.7759 0.9750 0.8818 -0.0543 -0.1265 -0.0630 115 ARG A NH1 
1766  N NH2 . ARG A 115 ? 0.7465 0.9886 0.8927 -0.0709 -0.1283 -0.0728 115 ARG A NH2 
1780  N N   . THR A 116 ? 0.7743 0.9226 0.8451 -0.0262 -0.1031 -0.0343 116 THR A N   
1781  C CA  . THR A 116 ? 0.7660 0.8945 0.8166 -0.0271 -0.1031 -0.0351 116 THR A CA  
1782  C C   . THR A 116 ? 0.8299 0.9697 0.8817 -0.0303 -0.1135 -0.0433 116 THR A C   
1783  O O   . THR A 116 ? 0.8775 1.0388 0.9457 -0.0307 -0.1194 -0.0461 116 THR A O   
1784  C CB  . THR A 116 ? 0.7603 0.8700 0.8055 -0.0348 -0.0948 -0.0353 116 THR A CB  
1785  O OG1 . THR A 116 ? 0.7955 0.9128 0.8555 -0.0467 -0.0927 -0.0391 116 THR A OG1 
1786  C CG2 . THR A 116 ? 0.7480 0.8463 0.7877 -0.0288 -0.0864 -0.0265 116 THR A CG2 
1794  N N   . GLU A 117 ? 0.8730 1.0003 0.9084 -0.0319 -0.1166 -0.0481 117 GLU A N   
1795  C CA  . GLU A 117 ? 0.9005 1.0388 0.9381 -0.0373 -0.1269 -0.0577 117 GLU A CA  
1796  C C   . GLU A 117 ? 0.9000 1.0329 0.9448 -0.0521 -0.1259 -0.0659 117 GLU A C   
1797  O O   . GLU A 117 ? 0.9286 1.0773 0.9844 -0.0597 -0.1339 -0.0736 117 GLU A O   
1798  C CB  . GLU A 117 ? 0.9464 1.0772 0.9613 -0.0310 -0.1329 -0.0602 117 GLU A CB  
1799  C CG  . GLU A 117 ? 0.9487 1.0848 0.9553 -0.0186 -0.1346 -0.0508 117 GLU A CG  
1800  C CD  . GLU A 117 ? 0.9920 1.1308 0.9795 -0.0138 -0.1436 -0.0535 117 GLU A CD  
1801  O OE1 . GLU A 117 ? 1.0173 1.1427 0.9842 -0.0107 -0.1396 -0.0536 117 GLU A OE1 
1802  O OE2 . GLU A 117 ? 0.9962 1.1522 0.9891 -0.0129 -0.1548 -0.0558 117 GLU A OE2 
1809  N N   . MET A 118 ? 0.9198 1.0312 0.9593 -0.0570 -0.1170 -0.0641 118 MET A N   
1810  C CA  . MET A 118 ? 0.9471 1.0483 0.9905 -0.0719 -0.1169 -0.0709 118 MET A CA  
1811  C C   . MET A 118 ? 0.9164 1.0348 0.9830 -0.0835 -0.1134 -0.0694 118 MET A C   
1812  O O   . MET A 118 ? 0.9813 1.1083 1.0588 -0.0970 -0.1180 -0.0766 118 MET A O   
1813  C CB  . MET A 118 ? 0.9753 1.0442 1.0027 -0.0720 -0.1101 -0.0692 118 MET A CB  
1814  C CG  . MET A 118 ? 1.0256 1.0778 1.0307 -0.0629 -0.1134 -0.0744 118 MET A CG  
1815  S SD  . MET A 118 ? 1.0562 1.1177 1.0553 -0.0657 -0.1267 -0.0880 118 MET A SD  
1816  C CE  . MET A 118 ? 1.0641 1.1244 1.0402 -0.0481 -0.1271 -0.0865 118 MET A CE  
1826  N N   . LYS A 119 ? 0.8738 0.9989 0.9483 -0.0793 -0.1051 -0.0607 119 LYS A N   
1827  C CA  . LYS A 119 ? 0.8973 1.0391 0.9918 -0.0902 -0.0995 -0.0593 119 LYS A CA  
1828  C C   . LYS A 119 ? 0.8416 1.0051 0.9483 -0.0797 -0.0962 -0.0542 119 LYS A C   
1829  O O   . LYS A 119 ? 0.8628 1.0205 0.9600 -0.0655 -0.0962 -0.0492 119 LYS A O   
1830  C CB  . LYS A 119 ? 1.0042 1.1226 1.0921 -0.1003 -0.0902 -0.0545 119 LYS A CB  
1831  C CG  . LYS A 119 ? 1.1630 1.2666 1.2487 -0.1169 -0.0934 -0.0605 119 LYS A CG  
1832  C CD  . LYS A 119 ? 1.2599 1.3334 1.3343 -0.1247 -0.0857 -0.0541 119 LYS A CD  
1833  C CE  . LYS A 119 ? 1.3043 1.3509 1.3688 -0.1362 -0.0913 -0.0605 119 LYS A CE  
1834  N NZ  . LYS A 119 ? 1.3120 1.3321 1.3701 -0.1486 -0.0852 -0.0538 119 LYS A NZ  
1848  N N   . GLN A 120 ? 0.7535 0.9425 0.8818 -0.0873 -0.0932 -0.0559 120 GLN A N   
1849  C CA  . GLN A 120 ? 0.6901 0.9001 0.8317 -0.0778 -0.0893 -0.0530 120 GLN A CA  
1850  C C   . GLN A 120 ? 0.7210 0.9139 0.8527 -0.0760 -0.0781 -0.0448 120 GLN A C   
1851  O O   . GLN A 120 ? 0.7909 0.9823 0.9254 -0.0882 -0.0697 -0.0429 120 GLN A O   
1852  C CB  . GLN A 120 ? 0.7085 0.9538 0.8769 -0.0865 -0.0886 -0.0588 120 GLN A CB  
1853  C CG  . GLN A 120 ? 0.7344 1.0076 0.9184 -0.0785 -0.1003 -0.0655 120 GLN A CG  
1854  C CD  . GLN A 120 ? 0.7652 1.0778 0.9788 -0.0859 -0.0987 -0.0719 120 GLN A CD  
1855  O OE1 . GLN A 120 ? 0.7452 1.0729 0.9703 -0.0834 -0.0897 -0.0705 120 GLN A OE1 
1856  N NE2 . GLN A 120 ? 0.8120 1.1433 1.0385 -0.0953 -0.1073 -0.0796 120 GLN A NE2 
1865  N N   . GLU A 121 ? 0.7196 0.9001 0.8395 -0.0617 -0.0782 -0.0395 121 GLU A N   
1866  C CA  . GLU A 121 ? 0.7036 0.8694 0.8142 -0.0584 -0.0692 -0.0322 121 GLU A CA  
1867  C C   . GLU A 121 ? 0.6502 0.8258 0.7655 -0.0440 -0.0700 -0.0302 121 GLU A C   
1868  O O   . GLU A 121 ? 0.6456 0.8366 0.7700 -0.0361 -0.0778 -0.0336 121 GLU A O   
1869  C CB  . GLU A 121 ? 0.7188 0.8531 0.8072 -0.0570 -0.0685 -0.0276 121 GLU A CB  
1870  C CG  . GLU A 121 ? 0.7343 0.8532 0.8160 -0.0693 -0.0694 -0.0305 121 GLU A CG  
1871  C CD  . GLU A 121 ? 0.8002 0.9138 0.8839 -0.0827 -0.0613 -0.0274 121 GLU A CD  
1872  O OE1 . GLU A 121 ? 0.8388 0.9605 0.9267 -0.0817 -0.0541 -0.0229 121 GLU A OE1 
1873  O OE2 . GLU A 121 ? 0.8599 0.9599 0.9395 -0.0947 -0.0624 -0.0294 121 GLU A OE2 
1880  N N   . ARG A 122 ? 0.6078 0.7737 0.7166 -0.0406 -0.0627 -0.0248 122 ARG A N   
1881  C CA  . ARG A 122 ? 0.6062 0.7743 0.7160 -0.0274 -0.0637 -0.0226 122 ARG A CA  
1882  C C   . ARG A 122 ? 0.5506 0.6944 0.6426 -0.0250 -0.0593 -0.0152 122 ARG A C   
1883  O O   . ARG A 122 ? 0.5352 0.6761 0.6251 -0.0278 -0.0518 -0.0128 122 ARG A O   
1884  C CB  . ARG A 122 ? 0.6853 0.8759 0.8118 -0.0263 -0.0590 -0.0268 122 ARG A CB  
1885  C CG  . ARG A 122 ? 0.7495 0.9407 0.8779 -0.0122 -0.0610 -0.0263 122 ARG A CG  
1886  C CD  . ARG A 122 ? 0.7516 0.9672 0.8974 -0.0102 -0.0561 -0.0330 122 ARG A CD  
1887  N NE  . ARG A 122 ? 0.7871 1.0001 0.9341 0.0036  -0.0583 -0.0339 122 ARG A NE  
1888  C CZ  . ARG A 122 ? 0.9443 1.1436 1.0808 0.0057  -0.0530 -0.0309 122 ARG A CZ  
1889  N NH1 . ARG A 122 ? 1.0761 1.2639 1.1998 -0.0042 -0.0453 -0.0261 122 ARG A NH1 
1890  N NH2 . ARG A 122 ? 0.9710 1.1669 1.1094 0.0179  -0.0564 -0.0329 122 ARG A NH2 
1904  N N   . GLU A 123 ? 0.5724 0.7010 0.6515 -0.0199 -0.0641 -0.0117 123 GLU A N   
1905  C CA  . GLU A 123 ? 0.5971 0.7054 0.6608 -0.0182 -0.0604 -0.0054 123 GLU A CA  
1906  C C   . GLU A 123 ? 0.6114 0.7161 0.6714 -0.0080 -0.0630 -0.0010 123 GLU A C   
1907  O O   . GLU A 123 ? 0.6336 0.7396 0.6917 -0.0025 -0.0697 -0.0004 123 GLU A O   
1908  C CB  . GLU A 123 ? 0.6219 0.7164 0.6737 -0.0211 -0.0624 -0.0055 123 GLU A CB  
1909  C CG  . GLU A 123 ? 0.6976 0.7890 0.7508 -0.0325 -0.0601 -0.0091 123 GLU A CG  
1910  C CD  . GLU A 123 ? 0.7454 0.8168 0.7846 -0.0340 -0.0611 -0.0094 123 GLU A CD  
1911  O OE1 . GLU A 123 ? 0.7534 0.8185 0.7829 -0.0260 -0.0637 -0.0082 123 GLU A OE1 
1912  O OE2 . GLU A 123 ? 0.7410 0.8028 0.7785 -0.0433 -0.0590 -0.0108 123 GLU A OE2 
1919  N N   . PRO A 124 ? 0.5895 0.6889 0.6472 -0.0061 -0.0585 0.0026  124 PRO A N   
1920  C CA  . PRO A 124 ? 0.5487 0.6434 0.6038 0.0020  -0.0615 0.0066  124 PRO A CA  
1921  C C   . PRO A 124 ? 0.5207 0.6026 0.5626 0.0037  -0.0625 0.0127  124 PRO A C   
1922  O O   . PRO A 124 ? 0.4612 0.5348 0.4969 0.0039  -0.0591 0.0170  124 PRO A O   
1923  C CB  . PRO A 124 ? 0.5824 0.6771 0.6398 0.0016  -0.0561 0.0065  124 PRO A CB  
1924  C CG  . PRO A 124 ? 0.5748 0.6662 0.6275 -0.0064 -0.0496 0.0069  124 PRO A CG  
1925  C CD  . PRO A 124 ? 0.5992 0.6964 0.6560 -0.0119 -0.0509 0.0031  124 PRO A CD  
1933  N N   . VAL A 125 ? 0.5161 0.5987 0.5537 0.0049  -0.0672 0.0126  125 VAL A N   
1934  C CA  . VAL A 125 ? 0.5851 0.6596 0.6103 0.0070  -0.0675 0.0177  125 VAL A CA  
1935  C C   . VAL A 125 ? 0.5891 0.6609 0.6124 0.0113  -0.0702 0.0242  125 VAL A C   
1936  O O   . VAL A 125 ? 0.6074 0.6741 0.6221 0.0116  -0.0685 0.0296  125 VAL A O   
1937  C CB  . VAL A 125 ? 0.6716 0.7485 0.6905 0.0069  -0.0717 0.0150  125 VAL A CB  
1938  C CG1 . VAL A 125 ? 0.7424 0.8183 0.7624 0.0013  -0.0697 0.0083  125 VAL A CG1 
1939  C CG2 . VAL A 125 ? 0.6370 0.7226 0.6606 0.0103  -0.0797 0.0143  125 VAL A CG2 
1949  N N   . GLY A 126 ? 0.5824 0.6573 0.6139 0.0145  -0.0745 0.0236  126 GLY A N   
1950  C CA  . GLY A 126 ? 0.6295 0.6980 0.6587 0.0182  -0.0785 0.0299  126 GLY A CA  
1951  C C   . GLY A 126 ? 0.6760 0.7434 0.6962 0.0201  -0.0845 0.0351  126 GLY A C   
1952  O O   . GLY A 126 ? 0.7351 0.8062 0.7480 0.0184  -0.0838 0.0342  126 GLY A O   
1956  N N   . THR A 127 ? 0.6906 0.7519 0.7101 0.0237  -0.0909 0.0406  127 THR A N   
1957  C CA  . THR A 127 ? 0.6663 0.7250 0.6746 0.0250  -0.0971 0.0478  127 THR A CA  
1958  C C   . THR A 127 ? 0.6558 0.7012 0.6597 0.0251  -0.1005 0.0574  127 THR A C   
1959  O O   . THR A 127 ? 0.6384 0.6766 0.6502 0.0262  -0.1005 0.0562  127 THR A O   
1960  C CB  . THR A 127 ? 0.6678 0.7337 0.6802 0.0302  -0.1058 0.0442  127 THR A CB  
1961  O OG1 . THR A 127 ? 0.6916 0.7558 0.6893 0.0306  -0.1114 0.0515  127 THR A OG1 
1962  C CG2 . THR A 127 ? 0.6391 0.7017 0.6636 0.0371  -0.1124 0.0426  127 THR A CG2 
1970  N N   . CYS A 128 ? 0.6610 0.7027 0.6511 0.0232  -0.1034 0.0668  128 CYS A N   
1971  C CA  . CYS A 128 ? 0.6525 0.6801 0.6365 0.0212  -0.1073 0.0779  128 CYS A CA  
1972  C C   . CYS A 128 ? 0.6633 0.6864 0.6356 0.0239  -0.1167 0.0860  128 CYS A C   
1973  O O   . CYS A 128 ? 0.6778 0.7114 0.6443 0.0259  -0.1186 0.0836  128 CYS A O   
1974  C CB  . CYS A 128 ? 0.6459 0.6738 0.6226 0.0128  -0.0992 0.0844  128 CYS A CB  
1975  S SG  . CYS A 128 ? 0.7433 0.7763 0.7311 0.0099  -0.0893 0.0766  128 CYS A SG  
1980  N N   . PHE A 129 ? 0.6919 0.6980 0.6600 0.0236  -0.1234 0.0959  129 PHE A N   
1981  C CA  . PHE A 129 ? 0.6984 0.6961 0.6522 0.0251  -0.1331 0.1071  129 PHE A CA  
1982  C C   . PHE A 129 ? 0.7488 0.7336 0.6896 0.0154  -0.1315 0.1218  129 PHE A C   
1983  O O   . PHE A 129 ? 0.7538 0.7264 0.7011 0.0115  -0.1302 0.1235  129 PHE A O   
1984  C CB  . PHE A 129 ? 0.6834 0.6697 0.6452 0.0358  -0.1460 0.1055  129 PHE A CB  
1985  C CG  . PHE A 129 ? 0.6816 0.6848 0.6550 0.0444  -0.1490 0.0930  129 PHE A CG  
1986  C CD1 . PHE A 129 ? 0.7030 0.7155 0.6674 0.0475  -0.1557 0.0947  129 PHE A CD1 
1987  C CD2 . PHE A 129 ? 0.6698 0.6811 0.6626 0.0485  -0.1451 0.0795  129 PHE A CD2 
1988  C CE1 . PHE A 129 ? 0.7225 0.7522 0.6991 0.0540  -0.1589 0.0828  129 PHE A CE1 
1989  C CE2 . PHE A 129 ? 0.6501 0.6793 0.6549 0.0545  -0.1472 0.0685  129 PHE A CE2 
1990  C CZ  . PHE A 129 ? 0.6842 0.7227 0.6818 0.0570  -0.1544 0.0699  129 PHE A CZ  
2000  N N   . LEU A 130 ? 0.7819 0.7707 0.7040 0.0106  -0.1314 0.1320  130 LEU A N   
2001  C CA  . LEU A 130 ? 0.7956 0.7762 0.7038 -0.0005 -0.1289 0.1474  130 LEU A CA  
2002  C C   . LEU A 130 ? 0.8080 0.7727 0.6993 0.0006  -0.1411 0.1615  130 LEU A C   
2003  O O   . LEU A 130 ? 0.8231 0.7968 0.7021 0.0047  -0.1450 0.1625  130 LEU A O   
2004  C CB  . LEU A 130 ? 0.7948 0.7970 0.6939 -0.0082 -0.1163 0.1478  130 LEU A CB  
2005  C CG  . LEU A 130 ? 0.8229 0.8236 0.7075 -0.0211 -0.1117 0.1637  130 LEU A CG  
2006  C CD1 . LEU A 130 ? 0.8006 0.7899 0.6970 -0.0289 -0.1094 0.1670  130 LEU A CD1 
2007  C CD2 . LEU A 130 ? 0.8703 0.8970 0.7461 -0.0255 -0.0993 0.1616  130 LEU A CD2 
2019  N N   . GLN A 131 ? 0.7748 0.7143 0.6644 -0.0029 -0.1480 0.1724  131 GLN A N   
2020  C CA  . GLN A 131 ? 0.8606 0.7789 0.7332 -0.0023 -0.1609 0.1881  131 GLN A CA  
2021  C C   . GLN A 131 ? 0.9290 0.8381 0.7855 -0.0187 -0.1567 0.2062  131 GLN A C   
2022  O O   . GLN A 131 ? 0.9252 0.8230 0.7900 -0.0270 -0.1534 0.2082  131 GLN A O   
2023  C CB  . GLN A 131 ? 0.9050 0.7973 0.7891 0.0086  -0.1747 0.1857  131 GLN A CB  
2024  C CG  . GLN A 131 ? 1.0106 0.8747 0.8775 0.0098  -0.1898 0.2031  131 GLN A CG  
2025  C CD  . GLN A 131 ? 1.1053 0.9455 0.9853 0.0243  -0.2043 0.1978  131 GLN A CD  
2026  O OE1 . GLN A 131 ? 1.1412 0.9495 1.0180 0.0218  -0.2123 0.2072  131 GLN A OE1 
2027  N NE2 . GLN A 131 ? 1.1299 0.9856 1.0253 0.0395  -0.2078 0.1822  131 GLN A NE2 
2036  N N   . ASP A 132 ? 1.0287 0.9440 0.8619 -0.0243 -0.1565 0.2191  132 ASP A N   
2037  C CA  . ASP A 132 ? 1.1487 1.0573 0.9648 -0.0414 -0.1522 0.2380  132 ASP A CA  
2038  C C   . ASP A 132 ? 1.2528 1.1264 1.0533 -0.0427 -0.1677 0.2565  132 ASP A C   
2039  O O   . ASP A 132 ? 1.3636 1.2117 1.1672 -0.0510 -0.1713 0.2652  132 ASP A O   
2040  C CB  . ASP A 132 ? 1.2031 1.1408 1.0009 -0.0481 -0.1412 0.2418  132 ASP A CB  
2041  C CG  . ASP A 132 ? 1.3051 1.2453 1.0893 -0.0674 -0.1323 0.2589  132 ASP A CG  
2042  O OD1 . ASP A 132 ? 1.3682 1.2807 1.1417 -0.0760 -0.1406 0.2767  132 ASP A OD1 
2043  O OD2 . ASP A 132 ? 1.3248 1.2948 1.1094 -0.0741 -0.1170 0.2545  132 ASP A OD2 
2048  N N   . GLY A 133 ? 1.2331 1.1038 1.0164 -0.0345 -0.1781 0.2626  133 GLY A N   
2049  C CA  . GLY A 133 ? 1.3039 1.1399 1.0726 -0.0317 -0.1956 0.2791  133 GLY A CA  
2050  C C   . GLY A 133 ? 1.3665 1.1981 1.1434 -0.0105 -0.2104 0.2686  133 GLY A C   
2051  O O   . GLY A 133 ? 1.3555 1.1844 1.1575 0.0010  -0.2130 0.2523  133 GLY A O   
2055  N N   . THR A 134 ? 1.4369 1.2699 1.1925 -0.0053 -0.2201 0.2778  134 THR A N   
2056  C CA  . THR A 134 ? 1.4291 1.2718 1.1937 0.0140  -0.2312 0.2648  134 THR A CA  
2057  C C   . THR A 134 ? 1.3444 1.2254 1.1242 0.0170  -0.2182 0.2432  134 THR A C   
2058  O O   . THR A 134 ? 1.3328 1.2241 1.1322 0.0312  -0.2234 0.2267  134 THR A O   
2059  C CB  . THR A 134 ? 1.4598 1.2974 1.1959 0.0175  -0.2449 0.2802  134 THR A CB  
2060  O OG1 . THR A 134 ? 1.5131 1.3748 1.2260 0.0049  -0.2328 0.2861  134 THR A OG1 
2061  C CG2 . THR A 134 ? 1.4309 1.2262 1.1503 0.0148  -0.2593 0.3031  134 THR A CG2 
2069  N N   . LYS A 135 ? 1.2588 1.1610 1.0304 0.0037  -0.2014 0.2432  135 LYS A N   
2070  C CA  . LYS A 135 ? 1.1275 1.0628 0.9104 0.0061  -0.1893 0.2239  135 LYS A CA  
2071  C C   . LYS A 135 ? 1.0084 0.9465 0.8227 0.0102  -0.1829 0.2065  135 LYS A C   
2072  O O   . LYS A 135 ? 1.0119 0.9388 0.8348 0.0025  -0.1766 0.2093  135 LYS A O   
2073  C CB  . LYS A 135 ? 1.1126 1.0679 0.8786 -0.0081 -0.1732 0.2284  135 LYS A CB  
2074  C CG  . LYS A 135 ? 1.1320 1.1082 0.8756 -0.0065 -0.1733 0.2278  135 LYS A CG  
2075  C CD  . LYS A 135 ? 1.1007 1.1016 0.8596 0.0019  -0.1683 0.2046  135 LYS A CD  
2076  C CE  . LYS A 135 ? 1.1223 1.1457 0.8578 0.0005  -0.1645 0.2020  135 LYS A CE  
2077  N NZ  . LYS A 135 ? 1.1171 1.1625 0.8670 0.0058  -0.1573 0.1793  135 LYS A NZ  
2091  N N   . THR A 136 ? 0.9301 0.8840 0.7610 0.0216  -0.1847 0.1887  136 THR A N   
2092  C CA  . THR A 136 ? 0.8806 0.8424 0.7389 0.0250  -0.1771 0.1713  136 THR A CA  
2093  C C   . THR A 136 ? 0.8041 0.7940 0.6672 0.0272  -0.1698 0.1556  136 THR A C   
2094  O O   . THR A 136 ? 0.8267 0.8263 0.6841 0.0339  -0.1780 0.1522  136 THR A O   
2095  C CB  . THR A 136 ? 0.9081 0.8555 0.7859 0.0377  -0.1890 0.1651  136 THR A CB  
2096  O OG1 . THR A 136 ? 0.9530 0.8698 0.8250 0.0359  -0.1970 0.1792  136 THR A OG1 
2097  C CG2 . THR A 136 ? 0.8813 0.8387 0.7852 0.0401  -0.1800 0.1475  136 THR A CG2 
2105  N N   . VAL A 137 ? 0.7468 0.7488 0.6201 0.0216  -0.1554 0.1463  137 VAL A N   
2106  C CA  . VAL A 137 ? 0.7499 0.7747 0.6273 0.0228  -0.1479 0.1316  137 VAL A CA  
2107  C C   . VAL A 137 ? 0.7532 0.7819 0.6549 0.0241  -0.1403 0.1179  137 VAL A C   
2108  O O   . VAL A 137 ? 0.7896 0.8080 0.7002 0.0208  -0.1361 0.1205  137 VAL A O   
2109  C CB  . VAL A 137 ? 0.7381 0.7760 0.5968 0.0141  -0.1367 0.1349  137 VAL A CB  
2110  C CG1 . VAL A 137 ? 0.7536 0.7890 0.5853 0.0118  -0.1435 0.1492  137 VAL A CG1 
2111  C CG2 . VAL A 137 ? 0.7007 0.7368 0.5640 0.0053  -0.1245 0.1390  137 VAL A CG2 
2121  N N   . GLU A 138 ? 0.7223 0.7658 0.6336 0.0283  -0.1390 0.1035  138 GLU A N   
2122  C CA  . GLU A 138 ? 0.7254 0.7741 0.6566 0.0284  -0.1310 0.0910  138 GLU A CA  
2123  C C   . GLU A 138 ? 0.7015 0.7584 0.6276 0.0216  -0.1177 0.0882  138 GLU A C   
2124  O O   . GLU A 138 ? 0.7303 0.7963 0.6412 0.0195  -0.1150 0.0882  138 GLU A O   
2125  C CB  . GLU A 138 ? 0.7057 0.7662 0.6500 0.0342  -0.1356 0.0776  138 GLU A CB  
2126  C CG  . GLU A 138 ? 0.6733 0.7375 0.6380 0.0340  -0.1285 0.0664  138 GLU A CG  
2127  C CD  . GLU A 138 ? 0.6581 0.7359 0.6365 0.0375  -0.1324 0.0540  138 GLU A CD  
2128  O OE1 . GLU A 138 ? 0.6671 0.7532 0.6383 0.0390  -0.1393 0.0522  138 GLU A OE1 
2129  O OE2 . GLU A 138 ? 0.6386 0.7198 0.6346 0.0381  -0.1286 0.0462  138 GLU A OE2 
2136  N N   . TYR A 139 ? 0.6599 0.7141 0.5984 0.0190  -0.1099 0.0852  139 TYR A N   
2137  C CA  . TYR A 139 ? 0.6603 0.7220 0.5970 0.0141  -0.0980 0.0825  139 TYR A CA  
2138  C C   . TYR A 139 ? 0.6518 0.7152 0.6056 0.0156  -0.0933 0.0712  139 TYR A C   
2139  O O   . TYR A 139 ? 0.6028 0.6596 0.5673 0.0147  -0.0916 0.0720  139 TYR A O   
2140  C CB  . TYR A 139 ? 0.6751 0.7319 0.6069 0.0077  -0.0934 0.0939  139 TYR A CB  
2141  C CG  . TYR A 139 ? 0.7304 0.7973 0.6638 0.0040  -0.0817 0.0907  139 TYR A CG  
2142  C CD1 . TYR A 139 ? 0.7624 0.8426 0.6860 0.0046  -0.0758 0.0859  139 TYR A CD1 
2143  C CD2 . TYR A 139 ? 0.7635 0.8272 0.7084 0.0007  -0.0773 0.0916  139 TYR A CD2 
2144  C CE1 . TYR A 139 ? 0.7728 0.8628 0.6993 0.0033  -0.0659 0.0823  139 TYR A CE1 
2145  C CE2 . TYR A 139 ? 0.7712 0.8456 0.7189 -0.0014 -0.0679 0.0887  139 TYR A CE2 
2146  C CZ  . TYR A 139 ? 0.7505 0.8381 0.6896 0.0004  -0.0622 0.0841  139 TYR A CZ  
2147  O OH  . TYR A 139 ? 0.7171 0.8158 0.6602 0.0003  -0.0535 0.0806  139 TYR A OH  
2157  N N   . ALA A 140 ? 0.6838 0.7553 0.6389 0.0172  -0.0917 0.0608  140 ALA A N   
2158  C CA  . ALA A 140 ? 0.6543 0.7270 0.6228 0.0173  -0.0871 0.0509  140 ALA A CA  
2159  C C   . ALA A 140 ? 0.6308 0.7079 0.5929 0.0158  -0.0793 0.0460  140 ALA A C   
2160  O O   . ALA A 140 ? 0.6012 0.6816 0.5611 0.0164  -0.0799 0.0375  140 ALA A O   
2161  C CB  . ALA A 140 ? 0.6589 0.7354 0.6367 0.0199  -0.0933 0.0428  140 ALA A CB  
2167  N N   . PRO A 141 ? 0.6417 0.7190 0.6014 0.0140  -0.0724 0.0505  141 PRO A N   
2168  C CA  . PRO A 141 ? 0.6522 0.7346 0.6065 0.0148  -0.0654 0.0452  141 PRO A CA  
2169  C C   . PRO A 141 ? 0.6522 0.7302 0.6146 0.0158  -0.0633 0.0356  141 PRO A C   
2170  O O   . PRO A 141 ? 0.6697 0.7485 0.6264 0.0177  -0.0603 0.0287  141 PRO A O   
2171  C CB  . PRO A 141 ? 0.6282 0.7140 0.5830 0.0128  -0.0593 0.0526  141 PRO A CB  
2172  C CG  . PRO A 141 ? 0.6177 0.6960 0.5822 0.0102  -0.0626 0.0585  141 PRO A CG  
2173  C CD  . PRO A 141 ? 0.6427 0.7160 0.6062 0.0114  -0.0711 0.0595  141 PRO A CD  
2181  N N   . CYS A 142 ? 0.6476 0.7205 0.6221 0.0145  -0.0647 0.0348  142 CYS A N   
2182  C CA  . CYS A 142 ? 0.6343 0.7024 0.6154 0.0136  -0.0626 0.0275  142 CYS A CA  
2183  C C   . CYS A 142 ? 0.6363 0.7050 0.6200 0.0121  -0.0674 0.0204  142 CYS A C   
2184  O O   . CYS A 142 ? 0.6502 0.7143 0.6383 0.0095  -0.0658 0.0146  142 CYS A O   
2185  C CB  . CYS A 142 ? 0.6410 0.7055 0.6325 0.0121  -0.0606 0.0301  142 CYS A CB  
2186  S SG  . CYS A 142 ? 0.7070 0.7699 0.6978 0.0131  -0.0542 0.0336  142 CYS A SG  
2191  N N   . ARG A 143 ? 0.6455 0.7197 0.6265 0.0130  -0.0737 0.0212  143 ARG A N   
2192  C CA  . ARG A 143 ? 0.6560 0.7342 0.6397 0.0114  -0.0795 0.0138  143 ARG A CA  
2193  C C   . ARG A 143 ? 0.6911 0.7684 0.6619 0.0116  -0.0796 0.0076  143 ARG A C   
2194  O O   . ARG A 143 ? 0.6683 0.7510 0.6298 0.0130  -0.0850 0.0065  143 ARG A O   
2195  C CB  . ARG A 143 ? 0.6414 0.7265 0.6281 0.0138  -0.0876 0.0171  143 ARG A CB  
2196  C CG  . ARG A 143 ? 0.6316 0.7249 0.6257 0.0122  -0.0944 0.0093  143 ARG A CG  
2197  C CD  . ARG A 143 ? 0.5839 0.6844 0.5841 0.0167  -0.1031 0.0129  143 ARG A CD  
2198  N NE  . ARG A 143 ? 0.6271 0.7261 0.6116 0.0203  -0.1082 0.0200  143 ARG A NE  
2199  C CZ  . ARG A 143 ? 0.6439 0.7423 0.6285 0.0251  -0.1152 0.0276  143 ARG A CZ  
2200  N NH1 . ARG A 143 ? 0.6270 0.7266 0.6277 0.0283  -0.1179 0.0273  143 ARG A NH1 
2201  N NH2 . ARG A 143 ? 0.6755 0.7714 0.6431 0.0270  -0.1195 0.0354  143 ARG A NH2 
2215  N N   . SER A 144 ? 0.7345 0.8038 0.7038 0.0107  -0.0740 0.0032  144 SER A N   
2216  C CA  . SER A 144 ? 0.7673 0.8326 0.7248 0.0120  -0.0735 -0.0046 144 SER A CA  
2217  C C   . SER A 144 ? 0.7830 0.8420 0.7453 0.0066  -0.0768 -0.0141 144 SER A C   
2218  O O   . SER A 144 ? 0.8048 0.8668 0.7796 0.0015  -0.0793 -0.0141 144 SER A O   
2219  C CB  . SER A 144 ? 0.7213 0.7807 0.6742 0.0160  -0.0660 -0.0035 144 SER A CB  
2220  O OG  . SER A 144 ? 0.6840 0.7338 0.6463 0.0139  -0.0629 -0.0032 144 SER A OG  
2226  N N   . GLN A 145 ? 0.7712 0.8216 0.7235 0.0073  -0.0768 -0.0227 145 GLN A N   
2227  C CA  . GLN A 145 ? 0.7691 0.8088 0.7247 0.0009  -0.0795 -0.0317 145 GLN A CA  
2228  C C   . GLN A 145 ? 0.7460 0.7696 0.7057 -0.0005 -0.0741 -0.0304 145 GLN A C   
2229  O O   . GLN A 145 ? 0.7143 0.7244 0.6749 -0.0065 -0.0758 -0.0366 145 GLN A O   
2230  C CB  . GLN A 145 ? 0.7745 0.8098 0.7158 0.0025  -0.0836 -0.0428 145 GLN A CB  
2231  C CG  . GLN A 145 ? 0.7861 0.8366 0.7228 0.0019  -0.0912 -0.0449 145 GLN A CG  
2232  C CD  . GLN A 145 ? 0.7790 0.8321 0.6958 0.0085  -0.0919 -0.0504 145 GLN A CD  
2233  O OE1 . GLN A 145 ? 0.7564 0.7988 0.6637 0.0129  -0.0879 -0.0570 145 GLN A OE1 
2234  N NE2 . GLN A 145 ? 0.7685 0.8363 0.6782 0.0099  -0.0973 -0.0476 145 GLN A NE2 
2243  N N   . ASP A 146 ? 0.7534 0.7776 0.7151 0.0043  -0.0683 -0.0221 146 ASP A N   
2244  C CA  . ASP A 146 ? 0.7435 0.7538 0.7084 0.0038  -0.0639 -0.0192 146 ASP A CA  
2245  C C   . ASP A 146 ? 0.7378 0.7519 0.7153 -0.0038 -0.0631 -0.0135 146 ASP A C   
2246  O O   . ASP A 146 ? 0.7718 0.7929 0.7547 -0.0020 -0.0601 -0.0059 146 ASP A O   
2247  C CB  . ASP A 146 ? 0.7664 0.7786 0.7276 0.0129  -0.0589 -0.0142 146 ASP A CB  
2248  C CG  . ASP A 146 ? 0.8178 0.8130 0.7775 0.0159  -0.0565 -0.0144 146 ASP A CG  
2249  O OD1 . ASP A 146 ? 0.8469 0.8254 0.8060 0.0106  -0.0586 -0.0181 146 ASP A OD1 
2250  O OD2 . ASP A 146 ? 0.8258 0.8243 0.7850 0.0233  -0.0529 -0.0103 146 ASP A OD2 
2255  N N   . ILE A 147 ? 0.7339 0.7438 0.7162 -0.0130 -0.0658 -0.0180 147 ILE A N   
2256  C CA  . ILE A 147 ? 0.7956 0.8146 0.7908 -0.0211 -0.0651 -0.0148 147 ILE A CA  
2257  C C   . ILE A 147 ? 0.8290 0.8347 0.8248 -0.0259 -0.0603 -0.0102 147 ILE A C   
2258  O O   . ILE A 147 ? 0.9771 0.9642 0.9670 -0.0299 -0.0609 -0.0129 147 ILE A O   
2259  C CB  . ILE A 147 ? 0.8821 0.9078 0.8836 -0.0300 -0.0703 -0.0221 147 ILE A CB  
2260  C CG1 . ILE A 147 ? 0.9185 0.9236 0.9126 -0.0360 -0.0722 -0.0287 147 ILE A CG1 
2261  C CG2 . ILE A 147 ? 0.9165 0.9568 0.9168 -0.0252 -0.0762 -0.0257 147 ILE A CG2 
2262  C CD1 . ILE A 147 ? 0.9925 1.0011 0.9953 -0.0494 -0.0759 -0.0342 147 ILE A CD1 
2274  N N   . ASP A 148 ? 0.7892 0.8013 0.7895 -0.0242 -0.0561 -0.0030 148 ASP A N   
2275  C CA  . ASP A 148 ? 0.7818 0.7927 0.7873 -0.0327 -0.0522 0.0009  148 ASP A CA  
2276  C C   . ASP A 148 ? 0.7536 0.7624 0.7557 -0.0263 -0.0484 0.0082  148 ASP A C   
2277  O O   . ASP A 148 ? 0.7504 0.7627 0.7499 -0.0171 -0.0491 0.0096  148 ASP A O   
2278  C CB  . ASP A 148 ? 0.8064 0.7994 0.8077 -0.0426 -0.0523 -0.0006 148 ASP A CB  
2279  C CG  . ASP A 148 ? 0.8036 0.8047 0.8134 -0.0551 -0.0486 0.0018  148 ASP A CG  
2280  O OD1 . ASP A 148 ? 0.7934 0.8091 0.8090 -0.0538 -0.0446 0.0057  148 ASP A OD1 
2281  O OD2 . ASP A 148 ? 0.8317 0.8255 0.8426 -0.0668 -0.0496 -0.0008 148 ASP A OD2 
2286  N N   . ALA A 149 ? 0.7323 0.7371 0.7340 -0.0317 -0.0445 0.0132  149 ALA A N   
2287  C CA  . ALA A 149 ? 0.7398 0.7385 0.7354 -0.0256 -0.0424 0.0196  149 ALA A CA  
2288  C C   . ALA A 149 ? 0.7591 0.7423 0.7456 -0.0175 -0.0448 0.0197  149 ALA A C   
2289  O O   . ALA A 149 ? 0.8117 0.7991 0.7970 -0.0087 -0.0448 0.0219  149 ALA A O   
2290  C CB  . ALA A 149 ? 0.7305 0.7234 0.7228 -0.0333 -0.0386 0.0251  149 ALA A CB  
2296  N N   . ASP A 150 ? 0.7666 0.7321 0.7472 -0.0204 -0.0469 0.0167  150 ASP A N   
2297  C CA  . ASP A 150 ? 0.7904 0.7408 0.7627 -0.0108 -0.0492 0.0153  150 ASP A CA  
2298  C C   . ASP A 150 ? 0.7259 0.6890 0.6994 -0.0016 -0.0502 0.0103  150 ASP A C   
2299  O O   . ASP A 150 ? 0.6658 0.6281 0.6360 0.0085  -0.0500 0.0108  150 ASP A O   
2300  C CB  . ASP A 150 ? 0.9106 0.8368 0.8758 -0.0153 -0.0523 0.0114  150 ASP A CB  
2301  C CG  . ASP A 150 ? 1.0522 0.9821 1.0219 -0.0257 -0.0540 0.0047  150 ASP A CG  
2302  O OD1 . ASP A 150 ? 1.1118 1.0523 1.0887 -0.0365 -0.0517 0.0073  150 ASP A OD1 
2303  O OD2 . ASP A 150 ? 1.1298 1.0537 1.0961 -0.0231 -0.0576 -0.0037 150 ASP A OD2 
2308  N N   . GLY A 151 ? 0.7465 0.7224 0.7245 -0.0050 -0.0514 0.0057  151 GLY A N   
2309  C CA  . GLY A 151 ? 0.7412 0.7306 0.7187 0.0023  -0.0521 0.0030  151 GLY A CA  
2310  C C   . GLY A 151 ? 0.7115 0.7182 0.6955 0.0037  -0.0504 0.0090  151 GLY A C   
2311  O O   . GLY A 151 ? 0.7151 0.7220 0.7016 0.0037  -0.0481 0.0149  151 GLY A O   
2315  N N   . GLN A 152 ? 0.7025 0.7225 0.6882 0.0047  -0.0522 0.0077  152 GLN A N   
2316  C CA  . GLN A 152 ? 0.7197 0.7526 0.7109 0.0057  -0.0519 0.0132  152 GLN A CA  
2317  C C   . GLN A 152 ? 0.7036 0.7443 0.7034 0.0004  -0.0542 0.0122  152 GLN A C   
2318  O O   . GLN A 152 ? 0.6840 0.7340 0.6878 0.0022  -0.0559 0.0151  152 GLN A O   
2319  C CB  . GLN A 152 ? 0.7286 0.7702 0.7148 0.0110  -0.0528 0.0143  152 GLN A CB  
2320  C CG  . GLN A 152 ? 0.7831 0.8218 0.7610 0.0170  -0.0504 0.0122  152 GLN A CG  
2321  C CD  . GLN A 152 ? 0.7668 0.8169 0.7383 0.0204  -0.0506 0.0127  152 GLN A CD  
2322  O OE1 . GLN A 152 ? 0.7476 0.7984 0.7121 0.0207  -0.0532 0.0071  152 GLN A OE1 
2323  N NE2 . GLN A 152 ? 0.7254 0.7846 0.6984 0.0219  -0.0481 0.0198  152 GLN A NE2 
2332  N N   . GLY A 153 ? 0.6603 0.6975 0.6635 -0.0062 -0.0544 0.0082  153 GLY A N   
2333  C CA  . GLY A 153 ? 0.6320 0.6809 0.6457 -0.0108 -0.0563 0.0059  153 GLY A CA  
2334  C C   . GLY A 153 ? 0.6216 0.6782 0.6426 -0.0097 -0.0541 0.0099  153 GLY A C   
2335  O O   . GLY A 153 ? 0.6152 0.6838 0.6448 -0.0086 -0.0568 0.0084  153 GLY A O   
2339  N N   . PHE A 154 ? 0.5871 0.6367 0.6047 -0.0093 -0.0499 0.0143  154 PHE A N   
2340  C CA  . PHE A 154 ? 0.6049 0.6601 0.6274 -0.0084 -0.0479 0.0169  154 PHE A CA  
2341  C C   . PHE A 154 ? 0.6373 0.6901 0.6558 -0.0024 -0.0485 0.0218  154 PHE A C   
2342  O O   . PHE A 154 ? 0.6391 0.6916 0.6580 -0.0020 -0.0467 0.0243  154 PHE A O   
2343  C CB  . PHE A 154 ? 0.6174 0.6685 0.6385 -0.0142 -0.0430 0.0181  154 PHE A CB  
2344  C CG  . PHE A 154 ? 0.6444 0.7017 0.6718 -0.0223 -0.0414 0.0140  154 PHE A CG  
2345  C CD1 . PHE A 154 ? 0.6618 0.7133 0.6876 -0.0271 -0.0431 0.0113  154 PHE A CD1 
2346  C CD2 . PHE A 154 ? 0.6705 0.7409 0.7059 -0.0253 -0.0381 0.0120  154 PHE A CD2 
2347  C CE1 . PHE A 154 ? 0.7196 0.7783 0.7525 -0.0365 -0.0418 0.0076  154 PHE A CE1 
2348  C CE2 . PHE A 154 ? 0.6864 0.7668 0.7295 -0.0338 -0.0358 0.0082  154 PHE A CE2 
2349  C CZ  . PHE A 154 ? 0.7088 0.7834 0.7511 -0.0402 -0.0378 0.0065  154 PHE A CZ  
2359  N N   . CYS A 155 ? 0.6411 0.6936 0.6555 0.0014  -0.0512 0.0229  155 CYS A N   
2360  C CA  . CYS A 155 ? 0.6104 0.6621 0.6210 0.0052  -0.0511 0.0281  155 CYS A CA  
2361  C C   . CYS A 155 ? 0.5863 0.6415 0.6019 0.0061  -0.0531 0.0308  155 CYS A C   
2362  O O   . CYS A 155 ? 0.5701 0.6239 0.5849 0.0066  -0.0522 0.0346  155 CYS A O   
2363  C CB  . CYS A 155 ? 0.6313 0.6846 0.6357 0.0080  -0.0527 0.0283  155 CYS A CB  
2364  S SG  . CYS A 155 ? 0.6719 0.7302 0.6738 0.0103  -0.0537 0.0353  155 CYS A SG  
2369  N N   . GLN A 156 ? 0.5546 0.6141 0.5758 0.0066  -0.0565 0.0283  156 GLN A N   
2370  C CA  . GLN A 156 ? 0.5906 0.6502 0.6161 0.0089  -0.0598 0.0300  156 GLN A CA  
2371  C C   . GLN A 156 ? 0.6153 0.6712 0.6351 0.0099  -0.0620 0.0370  156 GLN A C   
2372  O O   . GLN A 156 ? 0.6004 0.6526 0.6207 0.0092  -0.0624 0.0404  156 GLN A O   
2373  C CB  . GLN A 156 ? 0.5969 0.6553 0.6258 0.0080  -0.0571 0.0283  156 GLN A CB  
2374  C CG  . GLN A 156 ? 0.6235 0.6882 0.6581 0.0060  -0.0541 0.0221  156 GLN A CG  
2375  C CD  . GLN A 156 ? 0.6747 0.7398 0.7106 0.0055  -0.0513 0.0199  156 GLN A CD  
2376  O OE1 . GLN A 156 ? 0.7037 0.7661 0.7340 0.0023  -0.0473 0.0214  156 GLN A OE1 
2377  N NE2 . GLN A 156 ? 0.7162 0.7839 0.7584 0.0095  -0.0540 0.0160  156 GLN A NE2 
2386  N N   . GLY A 157 ? 0.6242 0.6822 0.6382 0.0105  -0.0635 0.0389  157 GLY A N   
2387  C CA  . GLY A 157 ? 0.6375 0.6947 0.6449 0.0100  -0.0642 0.0462  157 GLY A CA  
2388  C C   . GLY A 157 ? 0.6872 0.7388 0.6963 0.0103  -0.0698 0.0511  157 GLY A C   
2389  O O   . GLY A 157 ? 0.6762 0.7261 0.6888 0.0134  -0.0751 0.0489  157 GLY A O   
2393  N N   . GLY A 158 ? 0.7311 0.7794 0.7381 0.0070  -0.0692 0.0576  158 GLY A N   
2394  C CA  . GLY A 158 ? 0.6955 0.7340 0.7036 0.0060  -0.0748 0.0624  158 GLY A CA  
2395  C C   . GLY A 158 ? 0.6189 0.6515 0.6341 0.0053  -0.0750 0.0590  158 GLY A C   
2396  O O   . GLY A 158 ? 0.6177 0.6393 0.6337 0.0043  -0.0802 0.0620  158 GLY A O   
2400  N N   . PHE A 159 ? 0.5872 0.6253 0.6060 0.0057  -0.0701 0.0529  159 PHE A N   
2401  C CA  . PHE A 159 ? 0.6228 0.6569 0.6457 0.0048  -0.0700 0.0492  159 PHE A CA  
2402  C C   . PHE A 159 ? 0.6798 0.7082 0.7017 -0.0005 -0.0723 0.0552  159 PHE A C   
2403  O O   . PHE A 159 ? 0.6972 0.7166 0.7217 -0.0011 -0.0760 0.0529  159 PHE A O   
2404  C CB  . PHE A 159 ? 0.6164 0.6578 0.6395 0.0044  -0.0641 0.0450  159 PHE A CB  
2405  C CG  . PHE A 159 ? 0.6244 0.6635 0.6497 0.0042  -0.0637 0.0400  159 PHE A CG  
2406  C CD1 . PHE A 159 ? 0.6348 0.6746 0.6635 0.0073  -0.0634 0.0327  159 PHE A CD1 
2407  C CD2 . PHE A 159 ? 0.6231 0.6620 0.6472 0.0007  -0.0636 0.0420  159 PHE A CD2 
2408  C CE1 . PHE A 159 ? 0.6208 0.6602 0.6496 0.0071  -0.0623 0.0274  159 PHE A CE1 
2409  C CE2 . PHE A 159 ? 0.6159 0.6530 0.6398 0.0004  -0.0638 0.0369  159 PHE A CE2 
2410  C CZ  . PHE A 159 ? 0.6382 0.6752 0.6634 0.0037  -0.0627 0.0295  159 PHE A CZ  
2420  N N   . SER A 160 ? 0.6730 0.7073 0.6915 -0.0046 -0.0701 0.0623  160 SER A N   
2421  C CA  . SER A 160 ? 0.6878 0.7195 0.7062 -0.0117 -0.0720 0.0694  160 SER A CA  
2422  C C   . SER A 160 ? 0.6883 0.7261 0.7010 -0.0149 -0.0704 0.0779  160 SER A C   
2423  O O   . SER A 160 ? 0.6794 0.7281 0.6891 -0.0117 -0.0658 0.0769  160 SER A O   
2424  C CB  . SER A 160 ? 0.6975 0.7377 0.7197 -0.0151 -0.0690 0.0680  160 SER A CB  
2425  O OG  . SER A 160 ? 0.7114 0.7659 0.7331 -0.0128 -0.0631 0.0678  160 SER A OG  
2431  N N   . ILE A 161 ? 0.6766 0.7067 0.6869 -0.0215 -0.0742 0.0863  161 ILE A N   
2432  C CA  . ILE A 161 ? 0.6812 0.7169 0.6839 -0.0259 -0.0726 0.0959  161 ILE A CA  
2433  C C   . ILE A 161 ? 0.6875 0.7220 0.6909 -0.0375 -0.0734 0.1052  161 ILE A C   
2434  O O   . ILE A 161 ? 0.7249 0.7480 0.7336 -0.0418 -0.0779 0.1044  161 ILE A O   
2435  C CB  . ILE A 161 ? 0.7073 0.7313 0.7021 -0.0219 -0.0783 0.0989  161 ILE A CB  
2436  C CG1 . ILE A 161 ? 0.7470 0.7494 0.7449 -0.0199 -0.0871 0.0975  161 ILE A CG1 
2437  C CG2 . ILE A 161 ? 0.6925 0.7248 0.6858 -0.0130 -0.0760 0.0913  161 ILE A CG2 
2438  C CD1 . ILE A 161 ? 0.7537 0.7421 0.7438 -0.0171 -0.0949 0.1038  161 ILE A CD1 
2450  N N   . ASP A 162 ? 0.6372 0.6844 0.6349 -0.0432 -0.0689 0.1137  162 ASP A N   
2451  C CA  . ASP A 162 ? 0.6489 0.6971 0.6463 -0.0565 -0.0690 0.1247  162 ASP A CA  
2452  C C   . ASP A 162 ? 0.6431 0.7033 0.6292 -0.0605 -0.0641 0.1342  162 ASP A C   
2453  O O   . ASP A 162 ? 0.6061 0.6773 0.5864 -0.0525 -0.0599 0.1302  162 ASP A O   
2454  C CB  . ASP A 162 ? 0.6759 0.7407 0.6853 -0.0622 -0.0648 0.1221  162 ASP A CB  
2455  C CG  . ASP A 162 ? 0.7820 0.8391 0.7949 -0.0768 -0.0688 0.1304  162 ASP A CG  
2456  O OD1 . ASP A 162 ? 0.8301 0.8732 0.8342 -0.0843 -0.0724 0.1411  162 ASP A OD1 
2457  O OD2 . ASP A 162 ? 0.8334 0.8978 0.8573 -0.0812 -0.0691 0.1266  162 ASP A OD2 
2462  N N   . PHE A 163 ? 0.6720 0.7296 0.6543 -0.0738 -0.0648 0.1468  163 PHE A N   
2463  C CA  . PHE A 163 ? 0.7007 0.7720 0.6712 -0.0806 -0.0593 0.1577  163 PHE A CA  
2464  C C   . PHE A 163 ? 0.7300 0.8292 0.7090 -0.0912 -0.0502 0.1610  163 PHE A C   
2465  O O   . PHE A 163 ? 0.7908 0.8883 0.7812 -0.1005 -0.0523 0.1625  163 PHE A O   
2466  C CB  . PHE A 163 ? 0.7733 0.8204 0.7307 -0.0893 -0.0670 0.1720  163 PHE A CB  
2467  C CG  . PHE A 163 ? 0.8217 0.8509 0.7667 -0.0784 -0.0741 0.1715  163 PHE A CG  
2468  C CD1 . PHE A 163 ? 0.8485 0.8913 0.7800 -0.0738 -0.0700 0.1731  163 PHE A CD1 
2469  C CD2 . PHE A 163 ? 0.8719 0.8720 0.8189 -0.0725 -0.0855 0.1688  163 PHE A CD2 
2470  C CE1 . PHE A 163 ? 0.8772 0.9056 0.7982 -0.0641 -0.0777 0.1725  163 PHE A CE1 
2471  C CE2 . PHE A 163 ? 0.9019 0.8889 0.8400 -0.0619 -0.0926 0.1681  163 PHE A CE2 
2472  C CZ  . PHE A 163 ? 0.8941 0.8955 0.8193 -0.0581 -0.0891 0.1703  163 PHE A CZ  
2482  N N   . THR A 164 ? 0.7198 0.8461 0.6940 -0.0896 -0.0405 0.1613  164 THR A N   
2483  C CA  . THR A 164 ? 0.7544 0.9112 0.7365 -0.1000 -0.0311 0.1656  164 THR A CA  
2484  C C   . THR A 164 ? 0.7744 0.9299 0.7449 -0.1171 -0.0301 0.1831  164 THR A C   
2485  O O   . THR A 164 ? 0.7613 0.8946 0.7148 -0.1182 -0.0358 0.1915  164 THR A O   
2486  C CB  . THR A 164 ? 0.7974 0.9858 0.7800 -0.0897 -0.0204 0.1569  164 THR A CB  
2487  O OG1 . THR A 164 ? 0.8468 1.0401 0.8101 -0.0898 -0.0164 0.1628  164 THR A OG1 
2488  C CG2 . THR A 164 ? 0.7773 0.9593 0.7652 -0.0723 -0.0228 0.1413  164 THR A CG2 
2496  N N   . LYS A 165 ? 0.7817 0.9623 0.7621 -0.1309 -0.0232 0.1891  165 LYS A N   
2497  C CA  . LYS A 165 ? 0.7931 0.9737 0.7629 -0.1501 -0.0213 0.2071  165 LYS A CA  
2498  C C   . LYS A 165 ? 0.8353 1.0294 0.7842 -0.1484 -0.0139 0.2133  165 LYS A C   
2499  O O   . LYS A 165 ? 0.8697 1.0545 0.8025 -0.1622 -0.0147 0.2298  165 LYS A O   
2500  C CB  . LYS A 165 ? 0.7968 1.0067 0.7840 -0.1664 -0.0145 0.2113  165 LYS A CB  
2501  C CG  . LYS A 165 ? 0.8335 1.0917 0.8239 -0.1673 0.0009  0.2104  165 LYS A CG  
2502  C CD  . LYS A 165 ? 0.9216 1.2091 0.9305 -0.1861 0.0066  0.2166  165 LYS A CD  
2503  C CE  . LYS A 165 ? 1.0030 1.3399 1.0131 -0.1892 0.0227  0.2181  165 LYS A CE  
2504  N NZ  . LYS A 165 ? 1.0270 1.3963 1.0564 -0.2095 0.0287  0.2252  165 LYS A NZ  
2518  N N   . ALA A 166 ? 0.8470 1.0609 0.7943 -0.1321 -0.0073 0.2004  166 ALA A N   
2519  C CA  . ALA A 166 ? 0.8860 1.1155 0.8131 -0.1290 0.0001  0.2032  166 ALA A CA  
2520  C C   . ALA A 166 ? 0.9120 1.1153 0.8224 -0.1149 -0.0083 0.1986  166 ALA A C   
2521  O O   . ALA A 166 ? 0.9121 1.1296 0.8103 -0.1050 -0.0030 0.1920  166 ALA A O   
2522  C CB  . ALA A 166 ? 0.8639 1.1360 0.8001 -0.1208 0.0136  0.1911  166 ALA A CB  
2528  N N   . ASP A 167 ? 0.9516 1.1177 0.8616 -0.1136 -0.0215 0.2010  167 ASP A N   
2529  C CA  . ASP A 167 ? 0.9955 1.1376 0.8917 -0.1015 -0.0307 0.1979  167 ASP A CA  
2530  C C   . ASP A 167 ? 0.9047 1.0578 0.8062 -0.0835 -0.0280 0.1790  167 ASP A C   
2531  O O   . ASP A 167 ? 0.8741 1.0284 0.7606 -0.0750 -0.0285 0.1751  167 ASP A O   
2532  C CB  . ASP A 167 ? 1.1589 1.2985 1.0284 -0.1074 -0.0312 0.2120  167 ASP A CB  
2533  C CG  . ASP A 167 ? 1.3103 1.4246 1.1716 -0.1230 -0.0389 0.2316  167 ASP A CG  
2534  O OD1 . ASP A 167 ? 1.3447 1.4289 1.2152 -0.1220 -0.0501 0.2315  167 ASP A OD1 
2535  O OD2 . ASP A 167 ? 1.3788 1.5027 1.2236 -0.1365 -0.0338 0.2470  167 ASP A OD2 
2540  N N   . ARG A 168 ? 0.8635 1.0237 0.7856 -0.0783 -0.0257 0.1673  168 ARG A N   
2541  C CA  . ARG A 168 ? 0.7879 0.9489 0.7167 -0.0623 -0.0260 0.1504  168 ARG A CA  
2542  C C   . ARG A 168 ? 0.7853 0.9205 0.7260 -0.0582 -0.0358 0.1456  168 ARG A C   
2543  O O   . ARG A 168 ? 0.7968 0.9224 0.7472 -0.0665 -0.0393 0.1509  168 ARG A O   
2544  C CB  . ARG A 168 ? 0.7437 0.9340 0.6852 -0.0577 -0.0155 0.1404  168 ARG A CB  
2545  C CG  . ARG A 168 ? 0.7268 0.9335 0.6586 -0.0465 -0.0091 0.1301  168 ARG A CG  
2546  C CD  . ARG A 168 ? 0.7174 0.9511 0.6629 -0.0400 0.0002  0.1196  168 ARG A CD  
2547  N NE  . ARG A 168 ? 0.7282 0.9784 0.6625 -0.0301 0.0070  0.1101  168 ARG A NE  
2548  C CZ  . ARG A 168 ? 0.7172 0.9564 0.6474 -0.0171 0.0040  0.0971  168 ARG A CZ  
2549  N NH1 . ARG A 168 ? 0.6979 0.9120 0.6349 -0.0128 -0.0049 0.0929  168 ARG A NH1 
2550  N NH2 . ARG A 168 ? 0.7332 0.9870 0.6524 -0.0089 0.0100  0.0879  168 ARG A NH2 
2564  N N   . VAL A 169 ? 0.7822 0.9068 0.7219 -0.0459 -0.0401 0.1351  169 VAL A N   
2565  C CA  . VAL A 169 ? 0.7397 0.8437 0.6901 -0.0408 -0.0480 0.1288  169 VAL A CA  
2566  C C   . VAL A 169 ? 0.7049 0.8194 0.6693 -0.0340 -0.0434 0.1165  169 VAL A C   
2567  O O   . VAL A 169 ? 0.7460 0.8735 0.7084 -0.0264 -0.0381 0.1082  169 VAL A O   
2568  C CB  . VAL A 169 ? 0.7106 0.7984 0.6528 -0.0325 -0.0559 0.1253  169 VAL A CB  
2569  C CG1 . VAL A 169 ? 0.6302 0.7055 0.5854 -0.0252 -0.0607 0.1149  169 VAL A CG1 
2570  C CG2 . VAL A 169 ? 0.7602 0.8312 0.6908 -0.0382 -0.0638 0.1383  169 VAL A CG2 
2580  N N   . LEU A 170 ? 0.6765 0.7842 0.6539 -0.0366 -0.0460 0.1152  170 LEU A N   
2581  C CA  . LEU A 170 ? 0.6669 0.7800 0.6561 -0.0301 -0.0438 0.1047  170 LEU A CA  
2582  C C   . LEU A 170 ? 0.6943 0.7871 0.6861 -0.0242 -0.0506 0.0983  170 LEU A C   
2583  O O   . LEU A 170 ? 0.7216 0.7986 0.7157 -0.0281 -0.0569 0.1015  170 LEU A O   
2584  C CB  . LEU A 170 ? 0.6293 0.7527 0.6308 -0.0371 -0.0419 0.1072  170 LEU A CB  
2585  C CG  . LEU A 170 ? 0.6155 0.7420 0.6280 -0.0304 -0.0416 0.0976  170 LEU A CG  
2586  C CD1 . LEU A 170 ? 0.6002 0.7393 0.6112 -0.0199 -0.0359 0.0897  170 LEU A CD1 
2587  C CD2 . LEU A 170 ? 0.6606 0.7990 0.6850 -0.0378 -0.0411 0.1004  170 LEU A CD2 
2599  N N   . LEU A 171 ? 0.6620 0.7556 0.6536 -0.0152 -0.0493 0.0889  171 LEU A N   
2600  C CA  . LEU A 171 ? 0.6325 0.7114 0.6268 -0.0102 -0.0543 0.0824  171 LEU A CA  
2601  C C   . LEU A 171 ? 0.6585 0.7409 0.6590 -0.0050 -0.0511 0.0738  171 LEU A C   
2602  O O   . LEU A 171 ? 0.6990 0.7926 0.6987 -0.0017 -0.0461 0.0709  171 LEU A O   
2603  C CB  . LEU A 171 ? 0.6245 0.6985 0.6103 -0.0059 -0.0573 0.0807  171 LEU A CB  
2604  C CG  . LEU A 171 ? 0.6211 0.6855 0.6112 -0.0006 -0.0614 0.0728  171 LEU A CG  
2605  C CD1 . LEU A 171 ? 0.6267 0.6853 0.6108 0.0014  -0.0677 0.0747  171 LEU A CD1 
2606  C CD2 . LEU A 171 ? 0.5886 0.6584 0.5801 0.0039  -0.0572 0.0639  171 LEU A CD2 
2618  N N   . GLY A 172 ? 0.6352 0.7075 0.6411 -0.0040 -0.0544 0.0698  172 GLY A N   
2619  C CA  . GLY A 172 ? 0.6298 0.7030 0.6398 -0.0003 -0.0521 0.0634  172 GLY A CA  
2620  C C   . GLY A 172 ? 0.6677 0.7316 0.6782 0.0027  -0.0542 0.0573  172 GLY A C   
2621  O O   . GLY A 172 ? 0.6911 0.7475 0.7034 0.0019  -0.0583 0.0571  172 GLY A O   
2625  N N   . GLY A 173 ? 0.6582 0.7226 0.6674 0.0061  -0.0514 0.0522  173 GLY A N   
2626  C CA  . GLY A 173 ? 0.6612 0.7195 0.6717 0.0071  -0.0522 0.0467  173 GLY A CA  
2627  C C   . GLY A 173 ? 0.6406 0.6969 0.6514 0.0077  -0.0496 0.0443  173 GLY A C   
2628  O O   . GLY A 173 ? 0.6472 0.7038 0.6549 0.0102  -0.0473 0.0434  173 GLY A O   
2632  N N   . PRO A 174 ? 0.6273 0.6807 0.6407 0.0059  -0.0502 0.0431  174 PRO A N   
2633  C CA  . PRO A 174 ? 0.6330 0.6843 0.6442 0.0060  -0.0484 0.0427  174 PRO A CA  
2634  C C   . PRO A 174 ? 0.6345 0.6805 0.6423 0.0057  -0.0461 0.0398  174 PRO A C   
2635  O O   . PRO A 174 ? 0.6775 0.7195 0.6815 0.0054  -0.0451 0.0408  174 PRO A O   
2636  C CB  . PRO A 174 ? 0.6389 0.6895 0.6521 0.0037  -0.0500 0.0417  174 PRO A CB  
2637  C CG  . PRO A 174 ? 0.6577 0.7076 0.6747 0.0035  -0.0517 0.0389  174 PRO A CG  
2638  C CD  . PRO A 174 ? 0.6428 0.6943 0.6600 0.0046  -0.0531 0.0418  174 PRO A CD  
2646  N N   . GLY A 175 ? 0.6267 0.6722 0.6353 0.0051  -0.0460 0.0367  175 GLY A N   
2647  C CA  . GLY A 175 ? 0.6488 0.6894 0.6554 0.0023  -0.0442 0.0338  175 GLY A CA  
2648  C C   . GLY A 175 ? 0.6466 0.6808 0.6486 0.0037  -0.0440 0.0325  175 GLY A C   
2649  O O   . GLY A 175 ? 0.6973 0.7241 0.6968 0.0003  -0.0430 0.0307  175 GLY A O   
2653  N N   . SER A 176 ? 0.5907 0.6275 0.5911 0.0084  -0.0449 0.0331  176 SER A N   
2654  C CA  . SER A 176 ? 0.6518 0.6829 0.6472 0.0111  -0.0449 0.0299  176 SER A CA  
2655  C C   . SER A 176 ? 0.6644 0.6836 0.6552 0.0131  -0.0442 0.0306  176 SER A C   
2656  O O   . SER A 176 ? 0.6540 0.6737 0.6449 0.0153  -0.0440 0.0348  176 SER A O   
2657  C CB  . SER A 176 ? 0.6708 0.7103 0.6647 0.0163  -0.0448 0.0303  176 SER A CB  
2658  O OG  . SER A 176 ? 0.6474 0.6945 0.6426 0.0144  -0.0464 0.0306  176 SER A OG  
2664  N N   . PHE A 177 ? 0.6763 0.6836 0.6625 0.0120  -0.0448 0.0265  177 PHE A N   
2665  C CA  . PHE A 177 ? 0.7133 0.7046 0.6934 0.0151  -0.0455 0.0270  177 PHE A CA  
2666  C C   . PHE A 177 ? 0.7313 0.7165 0.7098 0.0110  -0.0450 0.0331  177 PHE A C   
2667  O O   . PHE A 177 ? 0.7275 0.7108 0.7040 0.0162  -0.0459 0.0373  177 PHE A O   
2668  C CB  . PHE A 177 ? 0.7141 0.7087 0.6931 0.0258  -0.0457 0.0263  177 PHE A CB  
2669  C CG  . PHE A 177 ? 0.7146 0.7213 0.6944 0.0293  -0.0448 0.0216  177 PHE A CG  
2670  C CD1 . PHE A 177 ? 0.7204 0.7233 0.6969 0.0262  -0.0458 0.0155  177 PHE A CD1 
2671  C CD2 . PHE A 177 ? 0.6970 0.7200 0.6803 0.0345  -0.0430 0.0237  177 PHE A CD2 
2672  C CE1 . PHE A 177 ? 0.7178 0.7320 0.6922 0.0293  -0.0453 0.0117  177 PHE A CE1 
2673  C CE2 . PHE A 177 ? 0.6757 0.7104 0.6575 0.0366  -0.0416 0.0206  177 PHE A CE2 
2674  C CZ  . PHE A 177 ? 0.7003 0.7303 0.6766 0.0345  -0.0428 0.0147  177 PHE A CZ  
2684  N N   . TYR A 178 ? 0.6878 0.6717 0.6671 0.0016  -0.0437 0.0333  178 TYR A N   
2685  C CA  . TYR A 178 ? 0.7025 0.6831 0.6787 -0.0039 -0.0422 0.0388  178 TYR A CA  
2686  C C   . TYR A 178 ? 0.6413 0.6335 0.6195 0.0002  -0.0421 0.0423  178 TYR A C   
2687  O O   . TYR A 178 ? 0.6278 0.6148 0.6004 0.0020  -0.0431 0.0474  178 TYR A O   
2688  C CB  . TYR A 178 ? 0.7436 0.7026 0.7098 -0.0045 -0.0437 0.0426  178 TYR A CB  
2689  C CG  . TYR A 178 ? 0.8319 0.7791 0.7955 -0.0149 -0.0429 0.0411  178 TYR A CG  
2690  C CD1 . TYR A 178 ? 0.8844 0.8386 0.8496 -0.0262 -0.0391 0.0430  178 TYR A CD1 
2691  C CD2 . TYR A 178 ? 0.8826 0.8132 0.8428 -0.0140 -0.0458 0.0370  178 TYR A CD2 
2692  C CE1 . TYR A 178 ? 0.9365 0.8830 0.9012 -0.0376 -0.0379 0.0419  178 TYR A CE1 
2693  C CE2 . TYR A 178 ? 0.9281 0.8476 0.8867 -0.0254 -0.0457 0.0354  178 TYR A CE2 
2694  C CZ  . TYR A 178 ? 0.9679 0.8964 0.9294 -0.0378 -0.0416 0.0384  178 TYR A CZ  
2695  O OH  . TYR A 178 ? 1.0268 0.9472 0.9884 -0.0509 -0.0411 0.0371  178 TYR A OH  
2705  N N   . TRP A 179 ? 0.6185 0.6255 0.6045 0.0013  -0.0418 0.0398  179 TRP A N   
2706  C CA  . TRP A 179 ? 0.6393 0.6570 0.6285 0.0032  -0.0422 0.0419  179 TRP A CA  
2707  C C   . TRP A 179 ? 0.6438 0.6618 0.6315 0.0100  -0.0445 0.0453  179 TRP A C   
2708  O O   . TRP A 179 ? 0.6025 0.6262 0.5907 0.0104  -0.0457 0.0479  179 TRP A O   
2709  C CB  . TRP A 179 ? 0.6285 0.6475 0.6152 -0.0024 -0.0404 0.0432  179 TRP A CB  
2710  C CG  . TRP A 179 ? 0.6137 0.6394 0.6059 -0.0078 -0.0379 0.0387  179 TRP A CG  
2711  C CD1 . TRP A 179 ? 0.6161 0.6527 0.6158 -0.0072 -0.0382 0.0351  179 TRP A CD1 
2712  C CD2 . TRP A 179 ? 0.6313 0.6538 0.6231 -0.0144 -0.0354 0.0369  179 TRP A CD2 
2713  N NE1 . TRP A 179 ? 0.6292 0.6716 0.6341 -0.0114 -0.0360 0.0308  179 TRP A NE1 
2714  C CE2 . TRP A 179 ? 0.6278 0.6633 0.6286 -0.0168 -0.0339 0.0318  179 TRP A CE2 
2715  C CE3 . TRP A 179 ? 0.6516 0.6608 0.6366 -0.0188 -0.0346 0.0392  179 TRP A CE3 
2716  C CZ2 . TRP A 179 ? 0.6612 0.7011 0.6663 -0.0238 -0.0314 0.0287  179 TRP A CZ2 
2717  C CZ3 . TRP A 179 ? 0.6977 0.7084 0.6856 -0.0274 -0.0321 0.0366  179 TRP A CZ3 
2718  C CH2 . TRP A 179 ? 0.6880 0.7161 0.6867 -0.0300 -0.0302 0.0312  179 TRP A CH2 
2729  N N   . GLN A 180 ? 0.6688 0.6823 0.6554 0.0158  -0.0453 0.0443  180 GLN A N   
2730  C CA  . GLN A 180 ? 0.6605 0.6818 0.6501 0.0233  -0.0469 0.0458  180 GLN A CA  
2731  C C   . GLN A 180 ? 0.6438 0.6814 0.6410 0.0222  -0.0462 0.0457  180 GLN A C   
2732  O O   . GLN A 180 ? 0.6880 0.7360 0.6896 0.0244  -0.0474 0.0483  180 GLN A O   
2733  C CB  . GLN A 180 ? 0.6836 0.6989 0.6712 0.0308  -0.0471 0.0426  180 GLN A CB  
2734  C CG  . GLN A 180 ? 0.7143 0.7101 0.6940 0.0337  -0.0494 0.0438  180 GLN A CG  
2735  C CD  . GLN A 180 ? 0.7199 0.7081 0.6979 0.0427  -0.0503 0.0387  180 GLN A CD  
2736  O OE1 . GLN A 180 ? 0.7280 0.7297 0.7107 0.0480  -0.0486 0.0346  180 GLN A OE1 
2737  N NE2 . GLN A 180 ? 0.7595 0.7250 0.7294 0.0441  -0.0529 0.0388  180 GLN A NE2 
2746  N N   . GLY A 181 ? 0.6693 0.7089 0.6680 0.0184  -0.0450 0.0433  181 GLY A N   
2747  C CA  . GLY A 181 ? 0.6942 0.7455 0.6980 0.0170  -0.0450 0.0443  181 GLY A CA  
2748  C C   . GLY A 181 ? 0.6933 0.7518 0.6970 0.0214  -0.0435 0.0433  181 GLY A C   
2749  O O   . GLY A 181 ? 0.7431 0.7991 0.7441 0.0273  -0.0426 0.0408  181 GLY A O   
2753  N N   . GLN A 182 ? 0.6511 0.7181 0.6567 0.0188  -0.0433 0.0451  182 GLN A N   
2754  C CA  . GLN A 182 ? 0.6337 0.7095 0.6370 0.0217  -0.0411 0.0444  182 GLN A CA  
2755  C C   . GLN A 182 ? 0.6536 0.7400 0.6595 0.0170  -0.0410 0.0499  182 GLN A C   
2756  O O   . GLN A 182 ? 0.6558 0.7375 0.6633 0.0119  -0.0439 0.0527  182 GLN A O   
2757  C CB  . GLN A 182 ? 0.5933 0.6620 0.5901 0.0225  -0.0413 0.0393  182 GLN A CB  
2758  C CG  . GLN A 182 ? 0.6024 0.6797 0.5938 0.0263  -0.0390 0.0369  182 GLN A CG  
2759  C CD  . GLN A 182 ? 0.6215 0.6909 0.6057 0.0267  -0.0405 0.0307  182 GLN A CD  
2760  O OE1 . GLN A 182 ? 0.5915 0.6536 0.5765 0.0224  -0.0437 0.0300  182 GLN A OE1 
2761  N NE2 . GLN A 182 ? 0.6673 0.7396 0.6448 0.0321  -0.0385 0.0252  182 GLN A NE2 
2770  N N   . LEU A 183 ? 0.6317 0.7321 0.6377 0.0188  -0.0377 0.0515  183 LEU A N   
2771  C CA  . LEU A 183 ? 0.6171 0.7277 0.6229 0.0131  -0.0368 0.0578  183 LEU A CA  
2772  C C   . LEU A 183 ? 0.6320 0.7477 0.6286 0.0151  -0.0342 0.0561  183 LEU A C   
2773  O O   . LEU A 183 ? 0.6523 0.7725 0.6458 0.0221  -0.0311 0.0500  183 LEU A O   
2774  C CB  . LEU A 183 ? 0.6212 0.7489 0.6352 0.0112  -0.0343 0.0618  183 LEU A CB  
2775  C CG  . LEU A 183 ? 0.6267 0.7522 0.6493 0.0085  -0.0377 0.0634  183 LEU A CG  
2776  C CD1 . LEU A 183 ? 0.6420 0.7881 0.6739 0.0052  -0.0357 0.0675  183 LEU A CD1 
2777  C CD2 . LEU A 183 ? 0.6002 0.7108 0.6218 0.0019  -0.0426 0.0660  183 LEU A CD2 
2789  N N   . ILE A 184 ? 0.6091 0.7228 0.6002 0.0097  -0.0363 0.0613  184 ILE A N   
2790  C CA  . ILE A 184 ? 0.5914 0.7106 0.5712 0.0106  -0.0346 0.0611  184 ILE A CA  
2791  C C   . ILE A 184 ? 0.5998 0.7268 0.5762 0.0027  -0.0340 0.0716  184 ILE A C   
2792  O O   . ILE A 184 ? 0.6657 0.7833 0.6453 -0.0033 -0.0386 0.0782  184 ILE A O   
2793  C CB  . ILE A 184 ? 0.5901 0.6958 0.5634 0.0123  -0.0397 0.0568  184 ILE A CB  
2794  C CG1 . ILE A 184 ? 0.5886 0.6857 0.5650 0.0178  -0.0400 0.0472  184 ILE A CG1 
2795  C CG2 . ILE A 184 ? 0.5839 0.6960 0.5436 0.0130  -0.0391 0.0567  184 ILE A CG2 
2796  C CD1 . ILE A 184 ? 0.5703 0.6566 0.5438 0.0177  -0.0450 0.0425  184 ILE A CD1 
2808  N N   . SER A 185 ? 0.6001 0.7438 0.5693 0.0026  -0.0283 0.0731  185 SER A N   
2809  C CA  . SER A 185 ? 0.6431 0.7956 0.6066 -0.0064 -0.0267 0.0844  185 SER A CA  
2810  C C   . SER A 185 ? 0.6795 0.8369 0.6257 -0.0052 -0.0253 0.0847  185 SER A C   
2811  O O   . SER A 185 ? 0.7039 0.8726 0.6448 0.0018  -0.0203 0.0761  185 SER A O   
2812  C CB  . SER A 185 ? 0.6383 0.8130 0.6106 -0.0102 -0.0194 0.0878  185 SER A CB  
2813  O OG  . SER A 185 ? 0.6593 0.8431 0.6251 -0.0210 -0.0171 0.0997  185 SER A OG  
2819  N N   . ASP A 186 ? 0.6810 0.8288 0.6173 -0.0115 -0.0306 0.0943  186 ASP A N   
2820  C CA  . ASP A 186 ? 0.7346 0.8858 0.6521 -0.0112 -0.0310 0.0964  186 ASP A CA  
2821  C C   . ASP A 186 ? 0.7464 0.9006 0.6542 -0.0223 -0.0308 0.1122  186 ASP A C   
2822  O O   . ASP A 186 ? 0.7927 0.9350 0.7072 -0.0296 -0.0351 0.1215  186 ASP A O   
2823  C CB  . ASP A 186 ? 0.7758 0.9090 0.6883 -0.0061 -0.0405 0.0918  186 ASP A CB  
2824  C CG  . ASP A 186 ? 0.7678 0.9020 0.6815 0.0032  -0.0395 0.0765  186 ASP A CG  
2825  O OD1 . ASP A 186 ? 0.7790 0.9267 0.6829 0.0069  -0.0338 0.0704  186 ASP A OD1 
2826  O OD2 . ASP A 186 ? 0.7241 0.8453 0.6479 0.0066  -0.0444 0.0702  186 ASP A OD2 
2831  N N   . GLN A 187 ? 0.6958 0.8650 0.5864 -0.0238 -0.0258 0.1152  187 GLN A N   
2832  C CA  . GLN A 187 ? 0.6878 0.8593 0.5650 -0.0354 -0.0255 0.1318  187 GLN A CA  
2833  C C   . GLN A 187 ? 0.7152 0.8621 0.5812 -0.0360 -0.0380 0.1394  187 GLN A C   
2834  O O   . GLN A 187 ? 0.7488 0.8902 0.6063 -0.0277 -0.0435 0.1320  187 GLN A O   
2835  C CB  . GLN A 187 ? 0.7195 0.9167 0.5797 -0.0364 -0.0156 0.1320  187 GLN A CB  
2836  C CG  . GLN A 187 ? 0.7864 1.0111 0.6581 -0.0330 -0.0032 0.1225  187 GLN A CG  
2837  C CD  . GLN A 187 ? 0.8372 1.0875 0.6913 -0.0302 0.0064  0.1180  187 GLN A CD  
2838  O OE1 . GLN A 187 ? 0.8181 1.0631 0.6525 -0.0261 0.0027  0.1153  187 GLN A OE1 
2839  N NE2 . GLN A 187 ? 0.9090 1.1889 0.7705 -0.0320 0.0187  0.1165  187 GLN A NE2 
2848  N N   . VAL A 188 ? 0.7004 0.8320 0.5669 -0.0456 -0.0434 0.1539  188 VAL A N   
2849  C CA  . VAL A 188 ? 0.7466 0.8536 0.6032 -0.0447 -0.0564 0.1617  188 VAL A CA  
2850  C C   . VAL A 188 ? 0.7680 0.8813 0.5996 -0.0432 -0.0580 0.1656  188 VAL A C   
2851  O O   . VAL A 188 ? 0.8169 0.9166 0.6414 -0.0363 -0.0688 0.1643  188 VAL A O   
2852  C CB  . VAL A 188 ? 0.8271 0.9154 0.6850 -0.0562 -0.0617 0.1780  188 VAL A CB  
2853  C CG1 . VAL A 188 ? 0.8187 0.9002 0.7005 -0.0571 -0.0614 0.1723  188 VAL A CG1 
2854  C CG2 . VAL A 188 ? 0.9145 1.0166 0.7583 -0.0704 -0.0538 0.1932  188 VAL A CG2 
2864  N N   . ALA A 189 ? 0.7885 0.9245 0.6065 -0.0493 -0.0473 0.1699  189 ALA A N   
2865  C CA  . ALA A 189 ? 0.8271 0.9717 0.6188 -0.0477 -0.0479 0.1723  189 ALA A CA  
2866  C C   . ALA A 189 ? 0.8684 1.0162 0.6600 -0.0340 -0.0510 0.1537  189 ALA A C   
2867  O O   . ALA A 189 ? 0.9327 1.0730 0.7087 -0.0296 -0.0604 0.1542  189 ALA A O   
2868  C CB  . ALA A 189 ? 0.7808 0.9540 0.5597 -0.0561 -0.0336 0.1774  189 ALA A CB  
2874  N N   . GLU A 190 ? 0.8486 1.0067 0.6573 -0.0274 -0.0439 0.1376  190 GLU A N   
2875  C CA  . GLU A 190 ? 0.8086 0.9658 0.6192 -0.0158 -0.0474 0.1199  190 GLU A CA  
2876  C C   . GLU A 190 ? 0.7869 0.9212 0.6071 -0.0114 -0.0611 0.1185  190 GLU A C   
2877  O O   . GLU A 190 ? 0.7794 0.9101 0.5910 -0.0057 -0.0694 0.1127  190 GLU A O   
2878  C CB  . GLU A 190 ? 0.7956 0.9639 0.6234 -0.0102 -0.0380 0.1049  190 GLU A CB  
2879  C CG  . GLU A 190 ? 0.8440 1.0381 0.6619 -0.0090 -0.0253 0.0991  190 GLU A CG  
2880  C CD  . GLU A 190 ? 0.8929 1.0929 0.6905 -0.0023 -0.0268 0.0885  190 GLU A CD  
2881  O OE1 . GLU A 190 ? 0.9425 1.1497 0.7168 -0.0067 -0.0272 0.0971  190 GLU A OE1 
2882  O OE2 . GLU A 190 ? 0.8850 1.0812 0.6887 0.0068  -0.0281 0.0717  190 GLU A OE2 
2889  N N   . ILE A 191 ? 0.7422 0.8629 0.5811 -0.0138 -0.0638 0.1231  191 ILE A N   
2890  C CA  . ILE A 191 ? 0.7208 0.8231 0.5721 -0.0084 -0.0751 0.1194  191 ILE A CA  
2891  C C   . ILE A 191 ? 0.7805 0.8729 0.6167 -0.0069 -0.0875 0.1273  191 ILE A C   
2892  O O   . ILE A 191 ? 0.8123 0.8993 0.6535 0.0003  -0.0966 0.1194  191 ILE A O   
2893  C CB  . ILE A 191 ? 0.6823 0.7717 0.5523 -0.0120 -0.0756 0.1243  191 ILE A CB  
2894  C CG1 . ILE A 191 ? 0.6734 0.7734 0.5587 -0.0121 -0.0650 0.1153  191 ILE A CG1 
2895  C CG2 . ILE A 191 ? 0.6827 0.7551 0.5648 -0.0058 -0.0869 0.1203  191 ILE A CG2 
2896  C CD1 . ILE A 191 ? 0.6778 0.7679 0.5799 -0.0163 -0.0650 0.1193  191 ILE A CD1 
2908  N N   . VAL A 192 ? 0.7915 0.8823 0.6092 -0.0139 -0.0885 0.1433  192 VAL A N   
2909  C CA  . VAL A 192 ? 0.8698 0.9488 0.6715 -0.0122 -0.1017 0.1532  192 VAL A CA  
2910  C C   . VAL A 192 ? 0.8891 0.9830 0.6680 -0.0095 -0.1024 0.1494  192 VAL A C   
2911  O O   . VAL A 192 ? 0.9385 1.0278 0.7113 -0.0030 -0.1145 0.1469  192 VAL A O   
2912  C CB  . VAL A 192 ? 0.9279 0.9925 0.7193 -0.0217 -0.1045 0.1744  192 VAL A CB  
2913  C CG1 . VAL A 192 ? 0.8563 0.9063 0.6701 -0.0248 -0.1038 0.1761  192 VAL A CG1 
2914  C CG2 . VAL A 192 ? 1.0057 1.0871 0.7770 -0.0323 -0.0931 0.1842  192 VAL A CG2 
2924  N N   . SER A 193 ? 0.8729 0.9861 0.6390 -0.0140 -0.0898 0.1480  193 SER A N   
2925  C CA  . SER A 193 ? 0.9003 1.0276 0.6414 -0.0118 -0.0901 0.1442  193 SER A CA  
2926  C C   . SER A 193 ? 0.8505 0.9829 0.5992 -0.0021 -0.0932 0.1231  193 SER A C   
2927  O O   . SER A 193 ? 0.9233 1.0579 0.6566 0.0020  -0.1023 0.1193  193 SER A O   
2928  C CB  . SER A 193 ? 0.9168 1.0657 0.6431 -0.0185 -0.0746 0.1466  193 SER A CB  
2929  O OG  . SER A 193 ? 0.9433 1.1052 0.6863 -0.0148 -0.0630 0.1304  193 SER A OG  
2935  N N   . LYS A 194 ? 0.7945 0.9284 0.5662 0.0009  -0.0865 0.1096  194 LYS A N   
2936  C CA  . LYS A 194 ? 0.8078 0.9444 0.5875 0.0083  -0.0887 0.0902  194 LYS A CA  
2937  C C   . LYS A 194 ? 0.8102 0.9336 0.6062 0.0125  -0.1018 0.0867  194 LYS A C   
2938  O O   . LYS A 194 ? 0.8079 0.9330 0.6120 0.0168  -0.1045 0.0714  194 LYS A O   
2939  C CB  . LYS A 194 ? 0.8182 0.9602 0.6144 0.0098  -0.0765 0.0782  194 LYS A CB  
2940  C CG  . LYS A 194 ? 0.9052 1.0642 0.6905 0.0072  -0.0626 0.0794  194 LYS A CG  
2941  C CD  . LYS A 194 ? 0.9851 1.1581 0.7462 0.0104  -0.0607 0.0703  194 LYS A CD  
2942  C CE  . LYS A 194 ? 1.0672 1.2605 0.8208 0.0095  -0.0453 0.0686  194 LYS A CE  
2943  N NZ  . LYS A 194 ? 1.1585 1.3666 0.8871 0.0135  -0.0424 0.0582  194 LYS A NZ  
2957  N N   . TYR A 195 ? 0.7981 0.9086 0.5997 0.0114  -0.1098 0.0998  195 TYR A N   
2958  C CA  . TYR A 195 ? 0.8039 0.9050 0.6234 0.0167  -0.1213 0.0954  195 TYR A CA  
2959  C C   . TYR A 195 ? 0.8012 0.9081 0.6097 0.0212  -0.1333 0.0897  195 TYR A C   
2960  O O   . TYR A 195 ? 0.7994 0.9085 0.5843 0.0206  -0.1391 0.0988  195 TYR A O   
2961  C CB  . TYR A 195 ? 0.8128 0.8979 0.6392 0.0162  -0.1280 0.1100  195 TYR A CB  
2962  C CG  . TYR A 195 ? 0.7905 0.8691 0.6369 0.0232  -0.1393 0.1040  195 TYR A CG  
2963  C CD1 . TYR A 195 ? 0.8009 0.8813 0.6714 0.0251  -0.1348 0.0911  195 TYR A CD1 
2964  C CD2 . TYR A 195 ? 0.8231 0.8951 0.6641 0.0284  -0.1543 0.1114  195 TYR A CD2 
2965  C CE1 . TYR A 195 ? 0.7913 0.8698 0.6807 0.0311  -0.1437 0.0851  195 TYR A CE1 
2966  C CE2 . TYR A 195 ? 0.8131 0.8831 0.6747 0.0360  -0.1641 0.1048  195 TYR A CE2 
2967  C CZ  . TYR A 195 ? 0.8126 0.8872 0.6986 0.0369  -0.1581 0.0913  195 TYR A CZ  
2968  O OH  . TYR A 195 ? 0.7823 0.8587 0.6894 0.0440  -0.1665 0.0842  195 TYR A OH  
2978  N N   . ASP A 196 ? 0.8043 0.9145 0.6297 0.0250  -0.1372 0.0748  196 ASP A N   
2979  C CA  . ASP A 196 ? 0.8345 0.9514 0.6559 0.0290  -0.1502 0.0677  196 ASP A CA  
2980  C C   . ASP A 196 ? 0.8295 0.9452 0.6797 0.0324  -0.1562 0.0594  196 ASP A C   
2981  O O   . ASP A 196 ? 0.8104 0.9276 0.6771 0.0304  -0.1485 0.0479  196 ASP A O   
2982  C CB  . ASP A 196 ? 0.8379 0.9660 0.6453 0.0277  -0.1467 0.0538  196 ASP A CB  
2983  C CG  . ASP A 196 ? 0.8303 0.9664 0.6295 0.0306  -0.1613 0.0473  196 ASP A CG  
2984  O OD1 . ASP A 196 ? 0.8051 0.9406 0.6181 0.0342  -0.1734 0.0496  196 ASP A OD1 
2985  O OD2 . ASP A 196 ? 0.8236 0.9679 0.6029 0.0297  -0.1609 0.0390  196 ASP A OD2 
2990  N N   . PRO A 197 ? 0.8104 0.9242 0.6676 0.0376  -0.1695 0.0650  197 PRO A N   
2991  C CA  . PRO A 197 ? 0.7867 0.9034 0.6732 0.0412  -0.1738 0.0564  197 PRO A CA  
2992  C C   . PRO A 197 ? 0.8080 0.9387 0.7044 0.0393  -0.1754 0.0392  197 PRO A C   
2993  O O   . PRO A 197 ? 0.8326 0.9675 0.7538 0.0391  -0.1739 0.0307  197 PRO A O   
2994  C CB  . PRO A 197 ? 0.7481 0.8618 0.6362 0.0491  -0.1894 0.0658  197 PRO A CB  
2995  C CG  . PRO A 197 ? 0.7590 0.8723 0.6166 0.0490  -0.1964 0.0754  197 PRO A CG  
2996  C CD  . PRO A 197 ? 0.7584 0.8680 0.5971 0.0412  -0.1817 0.0792  197 PRO A CD  
3004  N N   . ASN A 198 ? 0.7925 0.9304 0.6696 0.0372  -0.1782 0.0337  198 ASN A N   
3005  C CA  . ASN A 198 ? 0.7536 0.9023 0.6385 0.0338  -0.1800 0.0167  198 ASN A CA  
3006  C C   . ASN A 198 ? 0.7657 0.9089 0.6555 0.0279  -0.1655 0.0074  198 ASN A C   
3007  O O   . ASN A 198 ? 0.7974 0.9453 0.6971 0.0238  -0.1661 -0.0064 198 ASN A O   
3008  C CB  . ASN A 198 ? 0.7298 0.8867 0.5903 0.0339  -0.1892 0.0129  198 ASN A CB  
3009  C CG  . ASN A 198 ? 0.7129 0.8762 0.5684 0.0402  -0.2061 0.0214  198 ASN A CG  
3010  O OD1 . ASN A 198 ? 0.7462 0.9077 0.5748 0.0422  -0.2108 0.0312  198 ASN A OD1 
3011  N ND2 . ASN A 198 ? 0.6994 0.8710 0.5806 0.0438  -0.2153 0.0178  198 ASN A ND2 
3018  N N   . VAL A 199 ? 0.7172 0.8503 0.6007 0.0272  -0.1534 0.0147  199 VAL A N   
3019  C CA  . VAL A 199 ? 0.6921 0.8194 0.5787 0.0234  -0.1403 0.0070  199 VAL A CA  
3020  C C   . VAL A 199 ? 0.7127 0.8326 0.6192 0.0230  -0.1329 0.0125  199 VAL A C   
3021  O O   . VAL A 199 ? 0.7332 0.8482 0.6377 0.0249  -0.1307 0.0250  199 VAL A O   
3022  C CB  . VAL A 199 ? 0.7027 0.8284 0.5650 0.0235  -0.1321 0.0092  199 VAL A CB  
3023  C CG1 . VAL A 199 ? 0.7030 0.8228 0.5697 0.0217  -0.1203 -0.0003 199 VAL A CG1 
3024  C CG2 . VAL A 199 ? 0.7381 0.8720 0.5774 0.0244  -0.1401 0.0045  199 VAL A CG2 
3034  N N   . TYR A 200 ? 0.7080 0.8266 0.6326 0.0197  -0.1292 0.0032  200 TYR A N   
3035  C CA  . TYR A 200 ? 0.6697 0.7828 0.6128 0.0191  -0.1226 0.0068  200 TYR A CA  
3036  C C   . TYR A 200 ? 0.6924 0.7963 0.6310 0.0178  -0.1103 0.0087  200 TYR A C   
3037  O O   . TYR A 200 ? 0.6966 0.7956 0.6442 0.0182  -0.1051 0.0154  200 TYR A O   
3038  C CB  . TYR A 200 ? 0.6562 0.7740 0.6200 0.0152  -0.1242 -0.0029 200 TYR A CB  
3039  C CG  . TYR A 200 ? 0.6555 0.7868 0.6270 0.0163  -0.1366 -0.0069 200 TYR A CG  
3040  C CD1 . TYR A 200 ? 0.6468 0.7827 0.6141 0.0229  -0.1459 0.0012  200 TYR A CD1 
3041  C CD2 . TYR A 200 ? 0.6645 0.8040 0.6477 0.0104  -0.1398 -0.0186 200 TYR A CD2 
3042  C CE1 . TYR A 200 ? 0.6698 0.8198 0.6452 0.0253  -0.1585 -0.0026 200 TYR A CE1 
3043  C CE2 . TYR A 200 ? 0.6391 0.7948 0.6316 0.0112  -0.1517 -0.0228 200 TYR A CE2 
3044  C CZ  . TYR A 200 ? 0.6606 0.8221 0.6494 0.0195  -0.1613 -0.0150 200 TYR A CZ  
3045  O OH  . TYR A 200 ? 0.6664 0.8454 0.6655 0.0218  -0.1743 -0.0193 200 TYR A OH  
3055  N N   . SER A 201 ? 0.6935 0.7955 0.6187 0.0171  -0.1060 0.0022  201 SER A N   
3056  C CA  . SER A 201 ? 0.6873 0.7831 0.6083 0.0176  -0.0950 0.0029  201 SER A CA  
3057  C C   . SER A 201 ? 0.7544 0.8554 0.6538 0.0203  -0.0928 0.0059  201 SER A C   
3058  O O   . SER A 201 ? 0.7914 0.8945 0.6774 0.0213  -0.0939 -0.0033 201 SER A O   
3059  C CB  . SER A 201 ? 0.7234 0.8115 0.6491 0.0154  -0.0914 -0.0089 201 SER A CB  
3060  O OG  . SER A 201 ? 0.7869 0.8726 0.7309 0.0112  -0.0936 -0.0112 201 SER A OG  
3066  N N   . ILE A 202 ? 0.7845 0.8877 0.6799 0.0209  -0.0897 0.0185  202 ILE A N   
3067  C CA  . ILE A 202 ? 0.7831 0.8939 0.6577 0.0217  -0.0876 0.0243  202 ILE A CA  
3068  C C   . ILE A 202 ? 0.7727 0.8868 0.6429 0.0232  -0.0758 0.0210  202 ILE A C   
3069  O O   . ILE A 202 ? 0.7609 0.8718 0.6440 0.0228  -0.0694 0.0239  202 ILE A O   
3070  C CB  . ILE A 202 ? 0.7576 0.8682 0.6300 0.0200  -0.0906 0.0406  202 ILE A CB  
3071  C CG1 . ILE A 202 ? 0.7926 0.9005 0.6692 0.0211  -0.1036 0.0428  202 ILE A CG1 
3072  C CG2 . ILE A 202 ? 0.7650 0.8842 0.6149 0.0188  -0.0868 0.0485  202 ILE A CG2 
3073  C CD1 . ILE A 202 ? 0.8718 0.9738 0.7490 0.0207  -0.1084 0.0581  202 ILE A CD1 
3085  N N   . LYS A 203 ? 0.7499 0.8718 0.6019 0.0256  -0.0734 0.0142  203 LYS A N   
3086  C CA  . LYS A 203 ? 0.7093 0.8377 0.5566 0.0291  -0.0624 0.0091  203 LYS A CA  
3087  C C   . LYS A 203 ? 0.7262 0.8672 0.5655 0.0267  -0.0556 0.0227  203 LYS A C   
3088  O O   . LYS A 203 ? 0.8075 0.9602 0.6268 0.0264  -0.0542 0.0249  203 LYS A O   
3089  C CB  . LYS A 203 ? 0.7032 0.8347 0.5341 0.0335  -0.0626 -0.0060 203 LYS A CB  
3090  C CG  . LYS A 203 ? 0.7554 0.8727 0.5949 0.0349  -0.0671 -0.0208 203 LYS A CG  
3091  C CD  . LYS A 203 ? 0.7926 0.9110 0.6144 0.0395  -0.0674 -0.0370 203 LYS A CD  
3092  C CE  . LYS A 203 ? 0.8530 0.9537 0.6833 0.0396  -0.0720 -0.0514 203 LYS A CE  
3093  N NZ  . LYS A 203 ? 0.8692 0.9638 0.7089 0.0326  -0.0829 -0.0505 203 LYS A NZ  
3107  N N   . TYR A 204 ? 0.6767 0.8161 0.5313 0.0240  -0.0514 0.0319  204 TYR A N   
3108  C CA  . TYR A 204 ? 0.7217 0.8733 0.5718 0.0199  -0.0444 0.0446  204 TYR A CA  
3109  C C   . TYR A 204 ? 0.7823 0.9497 0.6299 0.0242  -0.0328 0.0373  204 TYR A C   
3110  O O   . TYR A 204 ? 0.8295 0.9936 0.6901 0.0296  -0.0294 0.0278  204 TYR A O   
3111  C CB  . TYR A 204 ? 0.7017 0.8455 0.5695 0.0150  -0.0450 0.0556  204 TYR A CB  
3112  C CG  . TYR A 204 ? 0.7215 0.8498 0.5948 0.0128  -0.0561 0.0610  204 TYR A CG  
3113  C CD1 . TYR A 204 ? 0.7261 0.8524 0.5867 0.0095  -0.0630 0.0719  204 TYR A CD1 
3114  C CD2 . TYR A 204 ? 0.7768 0.8933 0.6680 0.0147  -0.0598 0.0553  204 TYR A CD2 
3115  C CE1 . TYR A 204 ? 0.7555 0.8685 0.6227 0.0096  -0.0738 0.0758  204 TYR A CE1 
3116  C CE2 . TYR A 204 ? 0.8543 0.9600 0.7521 0.0139  -0.0692 0.0588  204 TYR A CE2 
3117  C CZ  . TYR A 204 ? 0.8400 0.9442 0.7267 0.0121  -0.0764 0.0685  204 TYR A CZ  
3118  O OH  . TYR A 204 ? 0.8645 0.9588 0.7592 0.0133  -0.0864 0.0711  204 TYR A OH  
3128  N N   . ASN A 205 ? 0.8240 1.0093 0.6548 0.0222  -0.0266 0.0420  205 ASN A N   
3129  C CA  . ASN A 205 ? 0.8809 1.0865 0.7111 0.0265  -0.0145 0.0359  205 ASN A CA  
3130  C C   . ASN A 205 ? 0.9093 1.1240 0.7561 0.0212  -0.0079 0.0469  205 ASN A C   
3131  O O   . ASN A 205 ? 0.9537 1.1603 0.8062 0.0125  -0.0121 0.0611  205 ASN A O   
3132  C CB  . ASN A 205 ? 0.9473 1.1722 0.7522 0.0259  -0.0093 0.0361  205 ASN A CB  
3133  C CG  . ASN A 205 ? 1.0385 1.2860 0.8421 0.0335  0.0032  0.0245  205 ASN A CG  
3134  O OD1 . ASN A 205 ? 1.0338 1.2798 0.8548 0.0409  0.0064  0.0149  205 ASN A OD1 
3135  N ND2 . ASN A 205 ? 1.1198 1.3889 0.9020 0.0323  0.0102  0.0252  205 ASN A ND2 
3142  N N   . ASN A 206 ? 0.8719 1.1034 0.7271 0.0270  0.0018  0.0394  206 ASN A N   
3143  C CA  . ASN A 206 ? 0.8379 1.0828 0.7102 0.0225  0.0083  0.0479  206 ASN A CA  
3144  C C   . ASN A 206 ? 0.7486 0.9730 0.6402 0.0195  0.0010  0.0528  206 ASN A C   
3145  O O   . ASN A 206 ? 0.6966 0.9261 0.5998 0.0117  0.0026  0.0637  206 ASN A O   
3146  C CB  . ASN A 206 ? 0.8726 1.1351 0.7353 0.0103  0.0135  0.0639  206 ASN A CB  
3147  C CG  . ASN A 206 ? 0.9633 1.2515 0.8068 0.0125  0.0229  0.0596  206 ASN A CG  
3148  O OD1 . ASN A 206 ? 1.0489 1.3520 0.8942 0.0236  0.0299  0.0446  206 ASN A OD1 
3149  N ND2 . ASN A 206 ? 0.9826 1.2757 0.8063 0.0026  0.0230  0.0725  206 ASN A ND2 
3156  N N   . GLN A 207 ? 0.7286 0.9303 0.6234 0.0249  -0.0069 0.0446  207 GLN A N   
3157  C CA  . GLN A 207 ? 0.7027 0.8869 0.6145 0.0229  -0.0128 0.0476  207 GLN A CA  
3158  C C   . GLN A 207 ? 0.6970 0.8877 0.6252 0.0287  -0.0080 0.0422  207 GLN A C   
3159  O O   . GLN A 207 ? 0.7222 0.9198 0.6497 0.0385  -0.0038 0.0306  207 GLN A O   
3160  C CB  . GLN A 207 ? 0.7036 0.8649 0.6140 0.0258  -0.0218 0.0407  207 GLN A CB  
3161  C CG  . GLN A 207 ? 0.6678 0.8127 0.5942 0.0234  -0.0271 0.0436  207 GLN A CG  
3162  C CD  . GLN A 207 ? 0.6780 0.8044 0.6045 0.0252  -0.0347 0.0367  207 GLN A CD  
3163  O OE1 . GLN A 207 ? 0.7361 0.8564 0.6623 0.0309  -0.0347 0.0256  207 GLN A OE1 
3164  N NE2 . GLN A 207 ? 0.6618 0.7792 0.5894 0.0201  -0.0415 0.0432  207 GLN A NE2 
3173  N N   . LEU A 208 ? 0.6807 0.8687 0.6234 0.0233  -0.0096 0.0502  208 LEU A N   
3174  C CA  . LEU A 208 ? 0.6579 0.8503 0.6168 0.0282  -0.0074 0.0466  208 LEU A CA  
3175  C C   . LEU A 208 ? 0.6344 0.8028 0.6011 0.0284  -0.0150 0.0456  208 LEU A C   
3176  O O   . LEU A 208 ? 0.6377 0.7943 0.6050 0.0207  -0.0202 0.0529  208 LEU A O   
3177  C CB  . LEU A 208 ? 0.6385 0.8510 0.6080 0.0209  -0.0029 0.0562  208 LEU A CB  
3178  C CG  . LEU A 208 ? 0.6462 0.8873 0.6097 0.0183  0.0062  0.0591  208 LEU A CG  
3179  C CD1 . LEU A 208 ? 0.6564 0.9155 0.6325 0.0078  0.0095  0.0699  208 LEU A CD1 
3180  C CD2 . LEU A 208 ? 0.6369 0.8941 0.6000 0.0318  0.0128  0.0456  208 LEU A CD2 
3192  N N   . ALA A 209 ? 0.6251 0.7861 0.5970 0.0372  -0.0157 0.0366  209 ALA A N   
3193  C CA  . ALA A 209 ? 0.6252 0.7647 0.6026 0.0368  -0.0219 0.0357  209 ALA A CA  
3194  C C   . ALA A 209 ? 0.6906 0.8279 0.6762 0.0452  -0.0214 0.0303  209 ALA A C   
3195  O O   . ALA A 209 ? 0.7033 0.8460 0.6867 0.0547  -0.0183 0.0223  209 ALA A O   
3196  C CB  . ALA A 209 ? 0.6470 0.7685 0.6150 0.0369  -0.0264 0.0302  209 ALA A CB  
3202  N N   . THR A 210 ? 0.7197 0.8486 0.7139 0.0424  -0.0250 0.0345  210 THR A N   
3203  C CA  . THR A 210 ? 0.6895 0.8113 0.6890 0.0501  -0.0266 0.0306  210 THR A CA  
3204  C C   . THR A 210 ? 0.7004 0.8004 0.6916 0.0547  -0.0292 0.0229  210 THR A C   
3205  O O   . THR A 210 ? 0.6832 0.7726 0.6676 0.0495  -0.0311 0.0216  210 THR A O   
3206  C CB  . THR A 210 ? 0.6297 0.7462 0.6369 0.0449  -0.0303 0.0370  210 THR A CB  
3207  O OG1 . THR A 210 ? 0.6002 0.7011 0.6034 0.0373  -0.0336 0.0391  210 THR A OG1 
3208  C CG2 . THR A 210 ? 0.6286 0.7658 0.6450 0.0398  -0.0286 0.0438  210 THR A CG2 
3216  N N   . ARG A 211 ? 0.7029 0.7962 0.6954 0.0643  -0.0300 0.0178  211 ARG A N   
3217  C CA  . ARG A 211 ? 0.7143 0.7853 0.6986 0.0689  -0.0327 0.0099  211 ARG A CA  
3218  C C   . ARG A 211 ? 0.7228 0.7725 0.7080 0.0670  -0.0375 0.0132  211 ARG A C   
3219  O O   . ARG A 211 ? 0.7138 0.7677 0.7057 0.0663  -0.0387 0.0197  211 ARG A O   
3220  C CB  . ARG A 211 ? 0.7974 0.8723 0.7799 0.0826  -0.0307 0.0007  211 ARG A CB  
3221  C CG  . ARG A 211 ? 0.8703 0.9679 0.8495 0.0849  -0.0248 -0.0037 211 ARG A CG  
3222  C CD  . ARG A 211 ? 1.0392 1.1450 1.0189 0.1002  -0.0219 -0.0138 211 ARG A CD  
3223  N NE  . ARG A 211 ? 1.2141 1.3119 1.1808 0.1047  -0.0212 -0.0255 211 ARG A NE  
3224  C CZ  . ARG A 211 ? 1.3259 1.4442 1.2859 0.1055  -0.0154 -0.0299 211 ARG A CZ  
3225  N NH1 . ARG A 211 ? 1.3911 1.5389 1.3566 0.1011  -0.0093 -0.0225 211 ARG A NH1 
3226  N NH2 . ARG A 211 ? 1.3508 1.4595 1.2975 0.1099  -0.0159 -0.0417 211 ARG A NH2 
3240  N N   . THR A 212 ? 0.7466 0.7737 0.7241 0.0651  -0.0404 0.0087  212 THR A N   
3241  C CA  . THR A 212 ? 0.7464 0.7519 0.7223 0.0624  -0.0443 0.0120  212 THR A CA  
3242  C C   . THR A 212 ? 0.7444 0.7442 0.7219 0.0738  -0.0465 0.0122  212 THR A C   
3243  O O   . THR A 212 ? 0.7783 0.7799 0.7552 0.0854  -0.0461 0.0051  212 THR A O   
3244  C CB  . THR A 212 ? 0.7537 0.7368 0.7214 0.0575  -0.0468 0.0065  212 THR A CB  
3245  O OG1 . THR A 212 ? 0.7870 0.7791 0.7542 0.0493  -0.0456 0.0048  212 THR A OG1 
3246  C CG2 . THR A 212 ? 0.7375 0.7008 0.7032 0.0505  -0.0497 0.0123  212 THR A CG2 
3254  N N   . ALA A 213 ? 0.7138 0.7072 0.6928 0.0714  -0.0493 0.0200  213 ALA A N   
3255  C CA  . ALA A 213 ? 0.7399 0.7283 0.7205 0.0823  -0.0530 0.0221  213 ALA A CA  
3256  C C   . ALA A 213 ? 0.7130 0.6714 0.6843 0.0790  -0.0580 0.0265  213 ALA A C   
3257  O O   . ALA A 213 ? 0.7036 0.6471 0.6686 0.0680  -0.0576 0.0270  213 ALA A O   
3258  C CB  . ALA A 213 ? 0.7428 0.7551 0.7333 0.0828  -0.0527 0.0284  213 ALA A CB  
3264  N N   . GLN A 214 ? 0.7299 0.6806 0.7007 0.0884  -0.0628 0.0302  214 GLN A N   
3265  C CA  . GLN A 214 ? 0.7660 0.6866 0.7259 0.0859  -0.0682 0.0363  214 GLN A CA  
3266  C C   . GLN A 214 ? 0.7702 0.6909 0.7263 0.0700  -0.0665 0.0446  214 GLN A C   
3267  O O   . GLN A 214 ? 0.7391 0.6830 0.7021 0.0648  -0.0633 0.0466  214 GLN A O   
3268  C CB  . GLN A 214 ? 0.7373 0.6530 0.6975 0.0998  -0.0747 0.0402  214 GLN A CB  
3269  C CG  . GLN A 214 ? 0.8690 0.7826 0.8331 0.1179  -0.0770 0.0309  214 GLN A CG  
3270  C CD  . GLN A 214 ? 0.9072 0.8587 0.8863 0.1259  -0.0724 0.0252  214 GLN A CD  
3271  O OE1 . GLN A 214 ? 0.8831 0.8598 0.8692 0.1167  -0.0677 0.0283  214 GLN A OE1 
3272  N NE2 . GLN A 214 ? 0.9550 0.9104 0.9391 0.1431  -0.0735 0.0166  214 GLN A NE2 
3281  N N   . ALA A 215 ? 0.7815 0.6753 0.7261 0.0622  -0.0686 0.0491  215 ALA A N   
3282  C CA  . ALA A 215 ? 0.7961 0.6910 0.7366 0.0469  -0.0659 0.0557  215 ALA A CA  
3283  C C   . ALA A 215 ? 0.7702 0.6774 0.7103 0.0475  -0.0675 0.0637  215 ALA A C   
3284  O O   . ALA A 215 ? 0.7495 0.6663 0.6887 0.0366  -0.0641 0.0669  215 ALA A O   
3285  C CB  . ALA A 215 ? 0.8452 0.7096 0.7730 0.0377  -0.0676 0.0598  215 ALA A CB  
3291  N N   . ILE A 216 ? 0.7586 0.6670 0.6998 0.0604  -0.0730 0.0660  216 ILE A N   
3292  C CA  . ILE A 216 ? 0.7636 0.6850 0.7044 0.0611  -0.0759 0.0729  216 ILE A CA  
3293  C C   . ILE A 216 ? 0.7063 0.6576 0.6584 0.0558  -0.0712 0.0697  216 ILE A C   
3294  O O   . ILE A 216 ? 0.6551 0.6160 0.6051 0.0509  -0.0720 0.0742  216 ILE A O   
3295  C CB  . ILE A 216 ? 0.8148 0.7363 0.7581 0.0776  -0.0836 0.0745  216 ILE A CB  
3296  C CG1 . ILE A 216 ? 0.9360 0.8686 0.8767 0.0773  -0.0883 0.0822  216 ILE A CG1 
3297  C CG2 . ILE A 216 ? 0.7720 0.7158 0.7316 0.0884  -0.0817 0.0654  216 ILE A CG2 
3298  C CD1 . ILE A 216 ? 1.0285 0.9630 0.9723 0.0937  -0.0973 0.0846  216 ILE A CD1 
3310  N N   . PHE A 217 ? 0.6990 0.6638 0.6616 0.0565  -0.0667 0.0622  217 PHE A N   
3311  C CA  . PHE A 217 ? 0.7344 0.7240 0.7071 0.0515  -0.0629 0.0599  217 PHE A CA  
3312  C C   . PHE A 217 ? 0.7503 0.7390 0.7208 0.0388  -0.0581 0.0588  217 PHE A C   
3313  O O   . PHE A 217 ? 0.7208 0.7261 0.6989 0.0347  -0.0555 0.0566  217 PHE A O   
3314  C CB  . PHE A 217 ? 0.7165 0.7223 0.7004 0.0587  -0.0606 0.0536  217 PHE A CB  
3315  C CG  . PHE A 217 ? 0.6920 0.7049 0.6815 0.0724  -0.0646 0.0531  217 PHE A CG  
3316  C CD1 . PHE A 217 ? 0.6649 0.6989 0.6632 0.0750  -0.0672 0.0558  217 PHE A CD1 
3317  C CD2 . PHE A 217 ? 0.6990 0.6980 0.6857 0.0831  -0.0661 0.0489  217 PHE A CD2 
3318  C CE1 . PHE A 217 ? 0.6645 0.7090 0.6704 0.0883  -0.0711 0.0548  217 PHE A CE1 
3319  C CE2 . PHE A 217 ? 0.7049 0.7121 0.6983 0.0978  -0.0700 0.0474  217 PHE A CE2 
3320  C CZ  . PHE A 217 ? 0.6840 0.7157 0.6878 0.1006  -0.0723 0.0505  217 PHE A CZ  
3330  N N   . ASP A 218 ? 0.7529 0.7229 0.7140 0.0323  -0.0571 0.0603  218 ASP A N   
3331  C CA  . ASP A 218 ? 0.7599 0.7325 0.7211 0.0210  -0.0525 0.0585  218 ASP A CA  
3332  C C   . ASP A 218 ? 0.7082 0.6946 0.6705 0.0160  -0.0515 0.0605  218 ASP A C   
3333  O O   . ASP A 218 ? 0.6454 0.6338 0.6037 0.0185  -0.0548 0.0649  218 ASP A O   
3334  C CB  . ASP A 218 ? 0.7895 0.7421 0.7408 0.0134  -0.0515 0.0609  218 ASP A CB  
3335  C CG  . ASP A 218 ? 0.7797 0.7161 0.7297 0.0164  -0.0528 0.0569  218 ASP A CG  
3336  O OD1 . ASP A 218 ? 0.7694 0.7138 0.7265 0.0234  -0.0528 0.0508  218 ASP A OD1 
3337  O OD2 . ASP A 218 ? 0.7985 0.7140 0.7394 0.0110  -0.0537 0.0599  218 ASP A OD2 
3342  N N   . ASP A 219 ? 0.7204 0.7164 0.6881 0.0096  -0.0477 0.0565  219 ASP A N   
3343  C CA  . ASP A 219 ? 0.6898 0.6963 0.6580 0.0048  -0.0465 0.0563  219 ASP A CA  
3344  C C   . ASP A 219 ? 0.6995 0.7173 0.6721 0.0094  -0.0501 0.0571  219 ASP A C   
3345  O O   . ASP A 219 ? 0.6889 0.7102 0.6570 0.0077  -0.0517 0.0587  219 ASP A O   
3346  C CB  . ASP A 219 ? 0.6912 0.6899 0.6475 -0.0012 -0.0452 0.0605  219 ASP A CB  
3347  C CG  . ASP A 219 ? 0.7614 0.7491 0.7138 -0.0080 -0.0416 0.0607  219 ASP A CG  
3348  O OD1 . ASP A 219 ? 0.7563 0.7503 0.7169 -0.0115 -0.0385 0.0552  219 ASP A OD1 
3349  O OD2 . ASP A 219 ? 0.7974 0.7696 0.7387 -0.0101 -0.0426 0.0667  219 ASP A OD2 
3354  N N   . SER A 220 ? 0.6835 0.7084 0.6647 0.0146  -0.0512 0.0556  220 SER A N   
3355  C CA  . SER A 220 ? 0.6871 0.7252 0.6750 0.0174  -0.0543 0.0563  220 SER A CA  
3356  C C   . SER A 220 ? 0.6467 0.6944 0.6423 0.0131  -0.0533 0.0534  220 SER A C   
3357  O O   . SER A 220 ? 0.6188 0.6749 0.6181 0.0116  -0.0561 0.0538  220 SER A O   
3358  C CB  . SER A 220 ? 0.6482 0.6911 0.6414 0.0255  -0.0558 0.0571  220 SER A CB  
3359  O OG  . SER A 220 ? 0.7117 0.7441 0.6980 0.0313  -0.0586 0.0601  220 SER A OG  
3365  N N   . TYR A 221 ? 0.6106 0.6562 0.6084 0.0110  -0.0502 0.0505  221 TYR A N   
3366  C CA  . TYR A 221 ? 0.6284 0.6795 0.6322 0.0077  -0.0502 0.0484  221 TYR A CA  
3367  C C   . TYR A 221 ? 0.6261 0.6869 0.6366 0.0089  -0.0515 0.0506  221 TYR A C   
3368  O O   . TYR A 221 ? 0.5906 0.6556 0.6052 0.0053  -0.0536 0.0513  221 TYR A O   
3369  C CB  . TYR A 221 ? 0.6600 0.7110 0.6626 0.0038  -0.0517 0.0465  221 TYR A CB  
3370  C CG  . TYR A 221 ? 0.7143 0.7601 0.7116 0.0014  -0.0488 0.0434  221 TYR A CG  
3371  C CD1 . TYR A 221 ? 0.7581 0.7989 0.7527 0.0011  -0.0457 0.0433  221 TYR A CD1 
3372  C CD2 . TYR A 221 ? 0.7033 0.7504 0.6983 -0.0010 -0.0491 0.0400  221 TYR A CD2 
3373  C CE1 . TYR A 221 ? 0.7688 0.8080 0.7599 -0.0029 -0.0424 0.0410  221 TYR A CE1 
3374  C CE2 . TYR A 221 ? 0.7184 0.7649 0.7092 -0.0035 -0.0453 0.0368  221 TYR A CE2 
3375  C CZ  . TYR A 221 ? 0.7484 0.7920 0.7378 -0.0050 -0.0416 0.0378  221 TYR A CZ  
3376  O OH  . TYR A 221 ? 0.7313 0.7772 0.7178 -0.0091 -0.0371 0.0351  221 TYR A OH  
3386  N N   . LEU A 222 ? 0.6424 0.7068 0.6538 0.0135  -0.0501 0.0516  222 LEU A N   
3387  C CA  . LEU A 222 ? 0.6447 0.7213 0.6621 0.0136  -0.0494 0.0535  222 LEU A CA  
3388  C C   . LEU A 222 ? 0.6224 0.6974 0.6402 0.0093  -0.0490 0.0535  222 LEU A C   
3389  O O   . LEU A 222 ? 0.6205 0.6878 0.6346 0.0096  -0.0481 0.0508  222 LEU A O   
3390  C CB  . LEU A 222 ? 0.6521 0.7334 0.6692 0.0206  -0.0470 0.0525  222 LEU A CB  
3391  C CG  . LEU A 222 ? 0.6282 0.7243 0.6497 0.0206  -0.0443 0.0538  222 LEU A CG  
3392  C CD1 . LEU A 222 ? 0.6444 0.7561 0.6746 0.0169  -0.0455 0.0578  222 LEU A CD1 
3393  C CD2 . LEU A 222 ? 0.5692 0.6692 0.5888 0.0290  -0.0413 0.0503  222 LEU A CD2 
3405  N N   . GLY A 223 ? 0.6133 0.6952 0.6356 0.0048  -0.0503 0.0570  223 GLY A N   
3406  C CA  . GLY A 223 ? 0.6317 0.7092 0.6532 0.0007  -0.0515 0.0585  223 GLY A CA  
3407  C C   . GLY A 223 ? 0.6097 0.6768 0.6316 -0.0022 -0.0552 0.0565  223 GLY A C   
3408  O O   . GLY A 223 ? 0.6081 0.6689 0.6295 -0.0038 -0.0573 0.0571  223 GLY A O   
3412  N N   . TYR A 224 ? 0.5984 0.6633 0.6204 -0.0022 -0.0563 0.0538  224 TYR A N   
3413  C CA  . TYR A 224 ? 0.6368 0.6936 0.6589 -0.0045 -0.0596 0.0504  224 TYR A CA  
3414  C C   . TYR A 224 ? 0.6565 0.7106 0.6821 -0.0098 -0.0637 0.0535  224 TYR A C   
3415  O O   . TYR A 224 ? 0.6603 0.7041 0.6859 -0.0103 -0.0670 0.0511  224 TYR A O   
3416  C CB  . TYR A 224 ? 0.6608 0.7184 0.6804 -0.0044 -0.0603 0.0477  224 TYR A CB  
3417  C CG  . TYR A 224 ? 0.6604 0.7109 0.6773 -0.0050 -0.0618 0.0417  224 TYR A CG  
3418  C CD1 . TYR A 224 ? 0.6571 0.7029 0.6759 -0.0082 -0.0664 0.0395  224 TYR A CD1 
3419  C CD2 . TYR A 224 ? 0.6247 0.6737 0.6371 -0.0026 -0.0584 0.0378  224 TYR A CD2 
3420  C CE1 . TYR A 224 ? 0.6657 0.7056 0.6816 -0.0072 -0.0676 0.0322  224 TYR A CE1 
3421  C CE2 . TYR A 224 ? 0.6465 0.6926 0.6565 -0.0026 -0.0586 0.0314  224 TYR A CE2 
3422  C CZ  . TYR A 224 ? 0.6493 0.6910 0.6610 -0.0040 -0.0631 0.0279  224 TYR A CZ  
3423  O OH  . TYR A 224 ? 0.6220 0.6613 0.6309 -0.0027 -0.0631 0.0198  224 TYR A OH  
3433  N N   . SER A 225 ? 0.6364 0.6998 0.6655 -0.0137 -0.0638 0.0588  225 SER A N   
3434  C CA  . SER A 225 ? 0.6152 0.6766 0.6476 -0.0212 -0.0673 0.0635  225 SER A CA  
3435  C C   . SER A 225 ? 0.5919 0.6684 0.6273 -0.0240 -0.0638 0.0702  225 SER A C   
3436  O O   . SER A 225 ? 0.5897 0.6796 0.6268 -0.0198 -0.0600 0.0696  225 SER A O   
3437  C CB  . SER A 225 ? 0.6101 0.6694 0.6454 -0.0262 -0.0722 0.0610  225 SER A CB  
3438  O OG  . SER A 225 ? 0.6473 0.7206 0.6852 -0.0250 -0.0710 0.0604  225 SER A OG  
3444  N N   . VAL A 226 ? 0.5918 0.6660 0.6273 -0.0308 -0.0650 0.0767  226 VAL A N   
3445  C CA  . VAL A 226 ? 0.6001 0.6910 0.6374 -0.0346 -0.0605 0.0835  226 VAL A CA  
3446  C C   . VAL A 226 ? 0.6260 0.7164 0.6667 -0.0471 -0.0635 0.0910  226 VAL A C   
3447  O O   . VAL A 226 ? 0.6744 0.7451 0.7125 -0.0516 -0.0695 0.0923  226 VAL A O   
3448  C CB  . VAL A 226 ? 0.6337 0.7245 0.6632 -0.0300 -0.0568 0.0854  226 VAL A CB  
3449  C CG1 . VAL A 226 ? 0.6430 0.7343 0.6698 -0.0194 -0.0540 0.0779  226 VAL A CG1 
3450  C CG2 . VAL A 226 ? 0.6536 0.7254 0.6768 -0.0324 -0.0617 0.0888  226 VAL A CG2 
3460  N N   . ALA A 227 ? 0.6360 0.7482 0.6830 -0.0527 -0.0593 0.0958  227 ALA A N   
3461  C CA  . ALA A 227 ? 0.6499 0.7661 0.7003 -0.0668 -0.0604 0.1048  227 ALA A CA  
3462  C C   . ALA A 227 ? 0.6279 0.7714 0.6807 -0.0687 -0.0519 0.1101  227 ALA A C   
3463  O O   . ALA A 227 ? 0.5926 0.7515 0.6462 -0.0583 -0.0464 0.1050  227 ALA A O   
3464  C CB  . ALA A 227 ? 0.6746 0.7930 0.7352 -0.0752 -0.0657 0.1031  227 ALA A CB  
3470  N N   . VAL A 228 ? 0.6057 0.7548 0.6589 -0.0824 -0.0508 0.1202  228 VAL A N   
3471  C CA  . VAL A 228 ? 0.5944 0.7713 0.6484 -0.0857 -0.0416 0.1258  228 VAL A CA  
3472  C C   . VAL A 228 ? 0.6593 0.8571 0.7261 -0.1014 -0.0403 0.1323  228 VAL A C   
3473  O O   . VAL A 228 ? 0.7420 0.9247 0.8117 -0.1138 -0.0473 0.1366  228 VAL A O   
3474  C CB  . VAL A 228 ? 0.6284 0.7949 0.6661 -0.0877 -0.0394 0.1338  228 VAL A CB  
3475  C CG1 . VAL A 228 ? 0.5608 0.7160 0.5885 -0.0718 -0.0394 0.1261  228 VAL A CG1 
3476  C CG2 . VAL A 228 ? 0.6978 0.8359 0.7290 -0.0997 -0.0475 0.1430  228 VAL A CG2 
3486  N N   . GLY A 229 ? 0.6433 0.8770 0.7186 -0.1006 -0.0314 0.1323  229 GLY A N   
3487  C CA  . GLY A 229 ? 0.6477 0.9098 0.7380 -0.1152 -0.0285 0.1379  229 GLY A CA  
3488  C C   . GLY A 229 ? 0.6392 0.9430 0.7394 -0.1075 -0.0181 0.1338  229 GLY A C   
3489  O O   . GLY A 229 ? 0.6693 0.9760 0.7679 -0.0894 -0.0161 0.1240  229 GLY A O   
3493  N N   . ASP A 230 ? 0.5921 0.9282 0.7026 -0.1209 -0.0114 0.1408  230 ASP A N   
3494  C CA  . ASP A 230 ? 0.6073 0.9875 0.7288 -0.1133 -0.0006 0.1362  230 ASP A CA  
3495  C C   . ASP A 230 ? 0.6238 1.0281 0.7685 -0.1080 -0.0039 0.1279  230 ASP A C   
3496  O O   . ASP A 230 ? 0.6518 1.0588 0.8090 -0.1220 -0.0102 0.1313  230 ASP A O   
3497  C CB  . ASP A 230 ? 0.5743 0.9832 0.6970 -0.1305 0.0094  0.1475  230 ASP A CB  
3498  C CG  . ASP A 230 ? 0.5758 1.0279 0.7040 -0.1197 0.0225  0.1417  230 ASP A CG  
3499  O OD1 . ASP A 230 ? 0.5639 1.0142 0.6889 -0.0981 0.0234  0.1298  230 ASP A OD1 
3500  O OD2 . ASP A 230 ? 0.5959 1.0839 0.7318 -0.1330 0.0320  0.1486  230 ASP A OD2 
3505  N N   . PHE A 231 ? 0.6175 1.0380 0.7672 -0.0877 -0.0007 0.1170  231 PHE A N   
3506  C CA  . PHE A 231 ? 0.6438 1.0858 0.8140 -0.0793 -0.0051 0.1090  231 PHE A CA  
3507  C C   . PHE A 231 ? 0.6426 1.1283 0.8267 -0.0657 0.0039  0.1019  231 PHE A C   
3508  O O   . PHE A 231 ? 0.6684 1.1730 0.8696 -0.0555 -0.0003 0.0948  231 PHE A O   
3509  C CB  . PHE A 231 ? 0.6293 1.0372 0.7917 -0.0648 -0.0152 0.1014  231 PHE A CB  
3510  C CG  . PHE A 231 ? 0.6000 0.9699 0.7526 -0.0763 -0.0248 0.1058  231 PHE A CG  
3511  C CD1 . PHE A 231 ? 0.5938 0.9661 0.7586 -0.0877 -0.0332 0.1069  231 PHE A CD1 
3512  C CD2 . PHE A 231 ? 0.5783 0.9114 0.7101 -0.0754 -0.0258 0.1079  231 PHE A CD2 
3513  C CE1 . PHE A 231 ? 0.6075 0.9445 0.7628 -0.0971 -0.0420 0.1093  231 PHE A CE1 
3514  C CE2 . PHE A 231 ? 0.5859 0.8855 0.7099 -0.0841 -0.0345 0.1107  231 PHE A CE2 
3515  C CZ  . PHE A 231 ? 0.5902 0.8908 0.7254 -0.0947 -0.0424 0.1110  231 PHE A CZ  
3525  N N   . ASN A 232 ? 0.6146 1.1172 0.7914 -0.0645 0.0158  0.1032  232 ASN A N   
3526  C CA  . ASN A 232 ? 0.5958 1.1465 0.7878 -0.0547 0.0261  0.0968  232 ASN A CA  
3527  C C   . ASN A 232 ? 0.6106 1.1959 0.8066 -0.0735 0.0378  0.1061  232 ASN A C   
3528  O O   . ASN A 232 ? 0.6078 1.2326 0.8105 -0.0662 0.0496  0.1013  232 ASN A O   
3529  C CB  . ASN A 232 ? 0.6261 1.1692 0.8054 -0.0312 0.0305  0.0859  232 ASN A CB  
3530  C CG  . ASN A 232 ? 0.7163 1.2267 0.8675 -0.0340 0.0332  0.0899  232 ASN A CG  
3531  O OD1 . ASN A 232 ? 0.7836 1.2775 0.9245 -0.0526 0.0320  0.1015  232 ASN A OD1 
3532  N ND2 . ASN A 232 ? 0.7390 1.2392 0.8777 -0.0153 0.0358  0.0800  232 ASN A ND2 
3539  N N   . GLY A 233 ? 0.6164 1.1867 0.8074 -0.0975 0.0350  0.1193  233 GLY A N   
3540  C CA  . GLY A 233 ? 0.5892 1.1926 0.7865 -0.1194 0.0447  0.1304  233 GLY A CA  
3541  C C   . GLY A 233 ? 0.6202 1.2375 0.8004 -0.1191 0.0586  0.1335  233 GLY A C   
3542  O O   . GLY A 233 ? 0.6868 1.3461 0.8759 -0.1325 0.0700  0.1395  233 GLY A O   
3546  N N   . ASP A 234 ? 0.5781 1.1632 0.7338 -0.1050 0.0581  0.1295  234 ASP A N   
3547  C CA  . ASP A 234 ? 0.5888 1.1840 0.7245 -0.1044 0.0701  0.1320  234 ASP A CA  
3548  C C   . ASP A 234 ? 0.6239 1.1818 0.7334 -0.1213 0.0670  0.1471  234 ASP A C   
3549  O O   . ASP A 234 ? 0.6900 1.2457 0.7773 -0.1190 0.0739  0.1493  234 ASP A O   
3550  C CB  . ASP A 234 ? 0.6110 1.1995 0.7365 -0.0770 0.0719  0.1162  234 ASP A CB  
3551  C CG  . ASP A 234 ? 0.6213 1.1544 0.7300 -0.0674 0.0593  0.1133  234 ASP A CG  
3552  O OD1 . ASP A 234 ? 0.6460 1.1473 0.7530 -0.0792 0.0489  0.1217  234 ASP A OD1 
3553  O OD2 . ASP A 234 ? 0.6508 1.1728 0.7483 -0.0480 0.0599  0.1019  234 ASP A OD2 
3558  N N   . GLY A 235 ? 0.6027 1.1309 0.7139 -0.1372 0.0562  0.1571  235 GLY A N   
3559  C CA  . GLY A 235 ? 0.6243 1.1148 0.7124 -0.1524 0.0515  0.1717  235 GLY A CA  
3560  C C   . GLY A 235 ? 0.6734 1.1178 0.7392 -0.1378 0.0433  0.1675  235 GLY A C   
3561  O O   . GLY A 235 ? 0.7359 1.1450 0.7840 -0.1481 0.0367  0.1788  235 GLY A O   
3565  N N   . ILE A 236 ? 0.6127 1.0562 0.6792 -0.1145 0.0430  0.1519  236 ILE A N   
3566  C CA  . ILE A 236 ? 0.6149 1.0181 0.6626 -0.1010 0.0354  0.1468  236 ILE A CA  
3567  C C   . ILE A 236 ? 0.6498 1.0226 0.7072 -0.0967 0.0226  0.1420  236 ILE A C   
3568  O O   . ILE A 236 ? 0.6542 1.0406 0.7299 -0.0877 0.0212  0.1324  236 ILE A O   
3569  C CB  . ILE A 236 ? 0.5940 1.0102 0.6354 -0.0798 0.0419  0.1326  236 ILE A CB  
3570  C CG1 . ILE A 236 ? 0.6175 1.0649 0.6468 -0.0841 0.0552  0.1365  236 ILE A CG1 
3571  C CG2 . ILE A 236 ? 0.5545 0.9300 0.5790 -0.0673 0.0333  0.1269  236 ILE A CG2 
3572  C CD1 . ILE A 236 ? 0.6072 1.0735 0.6325 -0.0635 0.0627  0.1207  236 ILE A CD1 
3584  N N   . ASP A 237 ? 0.6962 1.0288 0.7410 -0.1024 0.0129  0.1486  237 ASP A N   
3585  C CA  . ASP A 237 ? 0.6945 0.9979 0.7460 -0.0979 0.0014  0.1433  237 ASP A CA  
3586  C C   . ASP A 237 ? 0.6580 0.9586 0.7114 -0.0765 0.0005  0.1283  237 ASP A C   
3587  O O   . ASP A 237 ? 0.6123 0.9099 0.6529 -0.0652 0.0039  0.1233  237 ASP A O   
3588  C CB  . ASP A 237 ? 0.7133 0.9750 0.7491 -0.1038 -0.0079 0.1508  237 ASP A CB  
3589  C CG  . ASP A 237 ? 0.7935 1.0469 0.8311 -0.1251 -0.0118 0.1645  237 ASP A CG  
3590  O OD1 . ASP A 237 ? 0.8295 1.1111 0.8818 -0.1369 -0.0070 0.1681  237 ASP A OD1 
3591  O OD2 . ASP A 237 ? 0.8099 1.0286 0.8351 -0.1301 -0.0200 0.1714  237 ASP A OD2 
3596  N N   . ASP A 238 ? 0.6485 0.9491 0.7172 -0.0718 -0.0047 0.1216  238 ASP A N   
3597  C CA  . ASP A 238 ? 0.6012 0.8973 0.6724 -0.0532 -0.0066 0.1089  238 ASP A CA  
3598  C C   . ASP A 238 ? 0.6213 0.8807 0.6874 -0.0506 -0.0169 0.1065  238 ASP A C   
3599  O O   . ASP A 238 ? 0.5915 0.8330 0.6568 -0.0622 -0.0232 0.1127  238 ASP A O   
3600  C CB  . ASP A 238 ? 0.5634 0.8902 0.6550 -0.0480 -0.0047 0.1031  238 ASP A CB  
3601  C CG  . ASP A 238 ? 0.5914 0.9596 0.6904 -0.0490 0.0065  0.1038  238 ASP A CG  
3602  O OD1 . ASP A 238 ? 0.5988 0.9719 0.6858 -0.0415 0.0136  0.1009  238 ASP A OD1 
3603  O OD2 . ASP A 238 ? 0.5781 0.9755 0.6950 -0.0577 0.0084  0.1067  238 ASP A OD2 
3608  N N   . PHE A 239 ? 0.6228 0.8710 0.6853 -0.0354 -0.0185 0.0970  239 PHE A N   
3609  C CA  . PHE A 239 ? 0.6159 0.8315 0.6710 -0.0318 -0.0262 0.0940  239 PHE A CA  
3610  C C   . PHE A 239 ? 0.6264 0.8391 0.6917 -0.0286 -0.0319 0.0892  239 PHE A C   
3611  O O   . PHE A 239 ? 0.6657 0.8897 0.7367 -0.0178 -0.0306 0.0830  239 PHE A O   
3612  C CB  . PHE A 239 ? 0.5785 0.7823 0.6217 -0.0195 -0.0244 0.0874  239 PHE A CB  
3613  C CG  . PHE A 239 ? 0.6017 0.8113 0.6332 -0.0209 -0.0190 0.0907  239 PHE A CG  
3614  C CD1 . PHE A 239 ? 0.6173 0.8260 0.6435 -0.0338 -0.0189 0.1012  239 PHE A CD1 
3615  C CD2 . PHE A 239 ? 0.5832 0.7977 0.6076 -0.0096 -0.0145 0.0832  239 PHE A CD2 
3616  C CE1 . PHE A 239 ? 0.6240 0.8383 0.6370 -0.0354 -0.0142 0.1051  239 PHE A CE1 
3617  C CE2 . PHE A 239 ? 0.5991 0.8198 0.6108 -0.0109 -0.0098 0.0854  239 PHE A CE2 
3618  C CZ  . PHE A 239 ? 0.6122 0.8337 0.6177 -0.0238 -0.0095 0.0968  239 PHE A CZ  
3628  N N   . VAL A 240 ? 0.6035 0.7999 0.6697 -0.0373 -0.0387 0.0920  240 VAL A N   
3629  C CA  . VAL A 240 ? 0.5747 0.7641 0.6464 -0.0348 -0.0451 0.0872  240 VAL A CA  
3630  C C   . VAL A 240 ? 0.6072 0.7680 0.6677 -0.0292 -0.0489 0.0830  240 VAL A C   
3631  O O   . VAL A 240 ? 0.6404 0.7843 0.6929 -0.0329 -0.0500 0.0855  240 VAL A O   
3632  C CB  . VAL A 240 ? 0.6011 0.7931 0.6814 -0.0485 -0.0504 0.0913  240 VAL A CB  
3633  C CG1 . VAL A 240 ? 0.6150 0.8026 0.6995 -0.0454 -0.0573 0.0855  240 VAL A CG1 
3634  C CG2 . VAL A 240 ? 0.5827 0.8056 0.6752 -0.0569 -0.0458 0.0966  240 VAL A CG2 
3644  N N   . SER A 241 ? 0.5968 0.7530 0.6569 -0.0204 -0.0510 0.0769  241 SER A N   
3645  C CA  . SER A 241 ? 0.6327 0.7656 0.6831 -0.0159 -0.0534 0.0728  241 SER A CA  
3646  C C   . SER A 241 ? 0.6191 0.7480 0.6699 -0.0121 -0.0575 0.0685  241 SER A C   
3647  O O   . SER A 241 ? 0.5742 0.7154 0.6293 -0.0064 -0.0574 0.0674  241 SER A O   
3648  C CB  . SER A 241 ? 0.6660 0.7947 0.7090 -0.0074 -0.0489 0.0702  241 SER A CB  
3649  O OG  . SER A 241 ? 0.6760 0.7855 0.7116 -0.0044 -0.0509 0.0662  241 SER A OG  
3655  N N   . GLY A 242 ? 0.6314 0.7432 0.6770 -0.0147 -0.0614 0.0659  242 GLY A N   
3656  C CA  . GLY A 242 ? 0.6023 0.7092 0.6447 -0.0117 -0.0648 0.0619  242 GLY A CA  
3657  C C   . GLY A 242 ? 0.6236 0.7221 0.6581 -0.0034 -0.0619 0.0592  242 GLY A C   
3658  O O   . GLY A 242 ? 0.6523 0.7421 0.6824 -0.0016 -0.0588 0.0582  242 GLY A O   
3662  N N   . VAL A 243 ? 0.6424 0.7431 0.6746 0.0012  -0.0638 0.0585  243 VAL A N   
3663  C CA  . VAL A 243 ? 0.6032 0.6939 0.6269 0.0077  -0.0618 0.0572  243 VAL A CA  
3664  C C   . VAL A 243 ? 0.6209 0.7057 0.6372 0.0068  -0.0655 0.0560  243 VAL A C   
3665  O O   . VAL A 243 ? 0.6325 0.7214 0.6472 0.0110  -0.0687 0.0579  243 VAL A O   
3666  C CB  . VAL A 243 ? 0.5806 0.6785 0.6069 0.0159  -0.0605 0.0586  243 VAL A CB  
3667  C CG1 . VAL A 243 ? 0.5901 0.6731 0.6072 0.0209  -0.0582 0.0574  243 VAL A CG1 
3668  C CG2 . VAL A 243 ? 0.5916 0.7027 0.6262 0.0157  -0.0571 0.0595  243 VAL A CG2 
3678  N N   . PRO A 244 ? 0.6036 0.6795 0.6148 0.0023  -0.0655 0.0527  244 PRO A N   
3679  C CA  . PRO A 244 ? 0.6272 0.7015 0.6315 0.0001  -0.0693 0.0507  244 PRO A CA  
3680  C C   . PRO A 244 ? 0.6209 0.6890 0.6133 0.0034  -0.0687 0.0522  244 PRO A C   
3681  O O   . PRO A 244 ? 0.6755 0.7446 0.6605 0.0024  -0.0727 0.0518  244 PRO A O   
3682  C CB  . PRO A 244 ? 0.6548 0.7218 0.6578 -0.0044 -0.0685 0.0453  244 PRO A CB  
3683  C CG  . PRO A 244 ? 0.6344 0.6966 0.6402 -0.0030 -0.0635 0.0453  244 PRO A CG  
3684  C CD  . PRO A 244 ? 0.5948 0.6638 0.6070 -0.0005 -0.0626 0.0501  244 PRO A CD  
3692  N N   . ARG A 245 ? 0.6482 0.7088 0.6371 0.0066  -0.0645 0.0541  245 ARG A N   
3693  C CA  . ARG A 245 ? 0.6512 0.7030 0.6276 0.0082  -0.0641 0.0571  245 ARG A CA  
3694  C C   . ARG A 245 ? 0.6157 0.6665 0.5919 0.0154  -0.0672 0.0623  245 ARG A C   
3695  O O   . ARG A 245 ? 0.6391 0.6799 0.6040 0.0173  -0.0685 0.0664  245 ARG A O   
3696  C CB  . ARG A 245 ? 0.6971 0.7392 0.6689 0.0055  -0.0579 0.0557  245 ARG A CB  
3697  C CG  . ARG A 245 ? 0.6999 0.7433 0.6689 0.0000  -0.0550 0.0504  245 ARG A CG  
3698  C CD  . ARG A 245 ? 0.6857 0.7234 0.6510 -0.0032 -0.0489 0.0494  245 ARG A CD  
3699  N NE  . ARG A 245 ? 0.7173 0.7460 0.6704 -0.0043 -0.0481 0.0553  245 ARG A NE  
3700  C CZ  . ARG A 245 ? 0.7304 0.7580 0.6704 -0.0079 -0.0473 0.0574  245 ARG A CZ  
3701  N NH1 . ARG A 245 ? 0.7353 0.7714 0.6727 -0.0100 -0.0469 0.0522  245 ARG A NH1 
3702  N NH2 . ARG A 245 ? 0.7716 0.7882 0.6996 -0.0095 -0.0471 0.0646  245 ARG A NH2 
3716  N N   . ALA A 246 ? 0.6182 0.6793 0.6064 0.0198  -0.0686 0.0623  246 ALA A N   
3717  C CA  . ALA A 246 ? 0.6372 0.6994 0.6274 0.0288  -0.0715 0.0655  246 ALA A CA  
3718  C C   . ALA A 246 ? 0.6709 0.7372 0.6567 0.0320  -0.0790 0.0691  246 ALA A C   
3719  O O   . ALA A 246 ? 0.6873 0.7584 0.6695 0.0265  -0.0819 0.0684  246 ALA A O   
3720  C CB  . ALA A 246 ? 0.6294 0.7069 0.6345 0.0323  -0.0702 0.0636  246 ALA A CB  
3726  N N   . ALA A 247 ? 0.6966 0.7606 0.6821 0.0419  -0.0828 0.0724  247 ALA A N   
3727  C CA  . ALA A 247 ? 0.6656 0.7336 0.6471 0.0472  -0.0915 0.0766  247 ALA A CA  
3728  C C   . ALA A 247 ? 0.6743 0.7294 0.6369 0.0411  -0.0933 0.0801  247 ALA A C   
3729  O O   . ALA A 247 ? 0.6867 0.7504 0.6454 0.0394  -0.0995 0.0811  247 ALA A O   
3730  C CB  . ALA A 247 ? 0.6653 0.7591 0.6618 0.0469  -0.0960 0.0744  247 ALA A CB  
3736  N N   . ARG A 248 ? 0.7104 0.7463 0.6610 0.0371  -0.0878 0.0816  248 ARG A N   
3737  C CA  . ARG A 248 ? 0.7592 0.7842 0.6911 0.0299  -0.0872 0.0849  248 ARG A CA  
3738  C C   . ARG A 248 ? 0.6967 0.7352 0.6285 0.0225  -0.0871 0.0799  248 ARG A C   
3739  O O   . ARG A 248 ? 0.7255 0.7666 0.6458 0.0210  -0.0922 0.0819  248 ARG A O   
3740  C CB  . ARG A 248 ? 0.8883 0.9021 0.8052 0.0356  -0.0949 0.0938  248 ARG A CB  
3741  C CG  . ARG A 248 ? 1.0551 1.0493 0.9694 0.0432  -0.0959 0.0987  248 ARG A CG  
3742  C CD  . ARG A 248 ? 1.1737 1.1502 1.0815 0.0353  -0.0873 0.0986  248 ARG A CD  
3743  N NE  . ARG A 248 ? 1.2708 1.2311 1.1571 0.0276  -0.0866 0.1063  248 ARG A NE  
3744  C CZ  . ARG A 248 ? 1.2660 1.2150 1.1454 0.0174  -0.0788 0.1068  248 ARG A CZ  
3745  N NH1 . ARG A 248 ? 1.2917 1.2434 1.1841 0.0146  -0.0721 0.0996  248 ARG A NH1 
3746  N NH2 . ARG A 248 ? 1.2039 1.1407 1.0632 0.0094  -0.0777 0.1148  248 ARG A NH2 
3760  N N   . THR A 249 ? 0.6745 0.7205 0.6184 0.0180  -0.0818 0.0730  249 THR A N   
3761  C CA  . THR A 249 ? 0.7298 0.7839 0.6747 0.0110  -0.0806 0.0665  249 THR A CA  
3762  C C   . THR A 249 ? 0.6875 0.7566 0.6405 0.0114  -0.0882 0.0643  249 THR A C   
3763  O O   . THR A 249 ? 0.7257 0.7995 0.6788 0.0056  -0.0889 0.0583  249 THR A O   
3764  C CB  . THR A 249 ? 0.8467 0.8945 0.7732 0.0055  -0.0783 0.0661  249 THR A CB  
3765  O OG1 . THR A 249 ? 0.8895 0.9377 0.8026 0.0075  -0.0856 0.0712  249 THR A OG1 
3766  C CG2 . THR A 249 ? 0.9088 0.9437 0.8280 0.0031  -0.0708 0.0690  249 THR A CG2 
3774  N N   . LEU A 250 ? 0.6939 0.7714 0.6545 0.0180  -0.0943 0.0682  250 LEU A N   
3775  C CA  . LEU A 250 ? 0.6966 0.7923 0.6698 0.0167  -0.1007 0.0655  250 LEU A CA  
3776  C C   . LEU A 250 ? 0.6923 0.7948 0.6818 0.0120  -0.0962 0.0611  250 LEU A C   
3777  O O   . LEU A 250 ? 0.6508 0.7636 0.6482 0.0060  -0.0999 0.0574  250 LEU A O   
3778  C CB  . LEU A 250 ? 0.6788 0.7859 0.6596 0.0259  -0.1078 0.0702  250 LEU A CB  
3779  C CG  . LEU A 250 ? 0.6907 0.7958 0.6572 0.0305  -0.1166 0.0750  250 LEU A CG  
3780  C CD1 . LEU A 250 ? 0.6400 0.7562 0.6172 0.0422  -0.1234 0.0792  250 LEU A CD1 
3781  C CD2 . LEU A 250 ? 0.7328 0.8470 0.6941 0.0233  -0.1231 0.0710  250 LEU A CD2 
3793  N N   . GLY A 251 ? 0.6932 0.7888 0.6865 0.0138  -0.0889 0.0616  251 GLY A N   
3794  C CA  . GLY A 251 ? 0.6569 0.7581 0.6633 0.0099  -0.0849 0.0591  251 GLY A CA  
3795  C C   . GLY A 251 ? 0.6274 0.7460 0.6492 0.0137  -0.0860 0.0613  251 GLY A C   
3796  O O   . GLY A 251 ? 0.6074 0.7393 0.6341 0.0176  -0.0920 0.0631  251 GLY A O   
3800  N N   . MET A 252 ? 0.5963 0.7168 0.6257 0.0130  -0.0801 0.0611  252 MET A N   
3801  C CA  . MET A 252 ? 0.5775 0.7174 0.6216 0.0155  -0.0791 0.0625  252 MET A CA  
3802  C C   . MET A 252 ? 0.5610 0.7034 0.6113 0.0078  -0.0743 0.0622  252 MET A C   
3803  O O   . MET A 252 ? 0.5307 0.6576 0.5739 0.0034  -0.0717 0.0609  252 MET A O   
3804  C CB  . MET A 252 ? 0.5649 0.7045 0.6088 0.0274  -0.0765 0.0633  252 MET A CB  
3805  C CG  . MET A 252 ? 0.6627 0.7994 0.7012 0.0364  -0.0826 0.0652  252 MET A CG  
3806  S SD  . MET A 252 ? 0.6273 0.7609 0.6666 0.0516  -0.0808 0.0652  252 MET A SD  
3807  C CE  . MET A 252 ? 0.6161 0.7842 0.6776 0.0554  -0.0796 0.0633  252 MET A CE  
3817  N N   . VAL A 253 ? 0.5714 0.7349 0.6353 0.0060  -0.0732 0.0639  253 VAL A N   
3818  C CA  . VAL A 253 ? 0.5731 0.7409 0.6420 -0.0011 -0.0682 0.0657  253 VAL A CA  
3819  C C   . VAL A 253 ? 0.5633 0.7499 0.6401 0.0058  -0.0628 0.0665  253 VAL A C   
3820  O O   . VAL A 253 ? 0.6154 0.8249 0.7042 0.0087  -0.0644 0.0667  253 VAL A O   
3821  C CB  . VAL A 253 ? 0.6194 0.7954 0.6964 -0.0140 -0.0719 0.0675  253 VAL A CB  
3822  C CG1 . VAL A 253 ? 0.5948 0.7792 0.6776 -0.0215 -0.0666 0.0716  253 VAL A CG1 
3823  C CG2 . VAL A 253 ? 0.6092 0.7634 0.6767 -0.0199 -0.0764 0.0648  253 VAL A CG2 
3833  N N   . TYR A 254 ? 0.5986 0.7770 0.6690 0.0089  -0.0568 0.0659  254 TYR A N   
3834  C CA  . TYR A 254 ? 0.6225 0.8175 0.6980 0.0160  -0.0509 0.0651  254 TYR A CA  
3835  C C   . TYR A 254 ? 0.6116 0.8224 0.6930 0.0061  -0.0461 0.0690  254 TYR A C   
3836  O O   . TYR A 254 ? 0.5774 0.7756 0.6533 -0.0039 -0.0464 0.0722  254 TYR A O   
3837  C CB  . TYR A 254 ? 0.7112 0.8887 0.7750 0.0244  -0.0474 0.0616  254 TYR A CB  
3838  C CG  . TYR A 254 ? 0.7277 0.8875 0.7840 0.0332  -0.0512 0.0589  254 TYR A CG  
3839  C CD1 . TYR A 254 ? 0.7161 0.8800 0.7763 0.0370  -0.0572 0.0596  254 TYR A CD1 
3840  C CD2 . TYR A 254 ? 0.7128 0.8515 0.7575 0.0368  -0.0494 0.0562  254 TYR A CD2 
3841  C CE1 . TYR A 254 ? 0.7301 0.8759 0.7811 0.0441  -0.0609 0.0589  254 TYR A CE1 
3842  C CE2 . TYR A 254 ? 0.7052 0.8264 0.7423 0.0427  -0.0527 0.0551  254 TYR A CE2 
3843  C CZ  . TYR A 254 ? 0.7424 0.8663 0.7817 0.0464  -0.0582 0.0570  254 TYR A CZ  
3844  O OH  . TYR A 254 ? 0.7895 0.8943 0.8188 0.0515  -0.0617 0.0576  254 TYR A OH  
3854  N N   . ILE A 255 ? 0.6140 0.8528 0.7064 0.0092  -0.0418 0.0689  255 ILE A N   
3855  C CA  . ILE A 255 ? 0.6041 0.8608 0.7002 0.0004  -0.0352 0.0730  255 ILE A CA  
3856  C C   . ILE A 255 ? 0.6031 0.8707 0.6963 0.0117  -0.0277 0.0687  255 ILE A C   
3857  O O   . ILE A 255 ? 0.5968 0.8799 0.6978 0.0240  -0.0268 0.0634  255 ILE A O   
3858  C CB  . ILE A 255 ? 0.5972 0.8831 0.7105 -0.0091 -0.0358 0.0768  255 ILE A CB  
3859  C CG1 . ILE A 255 ? 0.6012 0.8729 0.7155 -0.0208 -0.0443 0.0798  255 ILE A CG1 
3860  C CG2 . ILE A 255 ? 0.5809 0.8868 0.6969 -0.0191 -0.0277 0.0822  255 ILE A CG2 
3861  C CD1 . ILE A 255 ? 0.6050 0.9021 0.7357 -0.0340 -0.0460 0.0839  255 ILE A CD1 
3873  N N   . TYR A 256 ? 0.6197 0.8787 0.7011 0.0083  -0.0229 0.0703  256 TYR A N   
3874  C CA  . TYR A 256 ? 0.6212 0.8897 0.6970 0.0175  -0.0157 0.0655  256 TYR A CA  
3875  C C   . TYR A 256 ? 0.6175 0.9111 0.6951 0.0078  -0.0079 0.0710  256 TYR A C   
3876  O O   . TYR A 256 ? 0.6205 0.9112 0.6970 -0.0072 -0.0090 0.0798  256 TYR A O   
3877  C CB  . TYR A 256 ? 0.6481 0.8876 0.7066 0.0216  -0.0167 0.0623  256 TYR A CB  
3878  C CG  . TYR A 256 ? 0.6667 0.8821 0.7216 0.0306  -0.0226 0.0570  256 TYR A CG  
3879  C CD1 . TYR A 256 ? 0.6459 0.8399 0.6982 0.0245  -0.0290 0.0599  256 TYR A CD1 
3880  C CD2 . TYR A 256 ? 0.6962 0.9094 0.7494 0.0449  -0.0218 0.0489  256 TYR A CD2 
3881  C CE1 . TYR A 256 ? 0.6383 0.8120 0.6861 0.0312  -0.0335 0.0561  256 TYR A CE1 
3882  C CE2 . TYR A 256 ? 0.7310 0.9203 0.7794 0.0514  -0.0273 0.0457  256 TYR A CE2 
3883  C CZ  . TYR A 256 ? 0.7090 0.8798 0.7545 0.0438  -0.0327 0.0498  256 TYR A CZ  
3884  O OH  . TYR A 256 ? 0.7107 0.8595 0.7505 0.0489  -0.0372 0.0475  256 TYR A OH  
3894  N N   . ASP A 257 ? 0.6218 0.9394 0.7013 0.0166  -0.0001 0.0657  257 ASP A N   
3895  C CA  . ASP A 257 ? 0.6249 0.9690 0.7037 0.0078  0.0088  0.0706  257 ASP A CA  
3896  C C   . ASP A 257 ? 0.6791 1.0024 0.7375 0.0005  0.0096  0.0757  257 ASP A C   
3897  O O   . ASP A 257 ? 0.7037 1.0066 0.7486 0.0096  0.0082  0.0695  257 ASP A O   
3898  C CB  . ASP A 257 ? 0.6816 1.0564 0.7658 0.0214  0.0174  0.0614  257 ASP A CB  
3899  C CG  . ASP A 257 ? 0.7846 1.1946 0.8705 0.0116  0.0282  0.0665  257 ASP A CG  
3900  O OD1 . ASP A 257 ? 0.8412 1.2426 0.9133 -0.0020 0.0301  0.0757  257 ASP A OD1 
3901  O OD2 . ASP A 257 ? 0.8433 1.2905 0.9444 0.0178  0.0348  0.0616  257 ASP A OD2 
3906  N N   . GLY A 258 ? 0.7060 1.0341 0.7622 -0.0163 0.0111  0.0872  258 GLY A N   
3907  C CA  . GLY A 258 ? 0.6894 0.9971 0.7262 -0.0236 0.0102  0.0938  258 GLY A CA  
3908  C C   . GLY A 258 ? 0.6590 0.9804 0.6813 -0.0192 0.0186  0.0913  258 GLY A C   
3909  O O   . GLY A 258 ? 0.6666 0.9735 0.6715 -0.0252 0.0175  0.0975  258 GLY A O   
3913  N N   . LYS A 259 ? 0.6573 1.0062 0.6855 -0.0080 0.0264  0.0818  259 LYS A N   
3914  C CA  . LYS A 259 ? 0.7088 1.0730 0.7226 -0.0020 0.0349  0.0768  259 LYS A CA  
3915  C C   . LYS A 259 ? 0.6839 1.0332 0.6902 0.0166  0.0330  0.0616  259 LYS A C   
3916  O O   . LYS A 259 ? 0.7122 1.0549 0.6996 0.0197  0.0347  0.0581  259 LYS A O   
3917  C CB  . LYS A 259 ? 0.8067 1.2170 0.8318 -0.0029 0.0468  0.0759  259 LYS A CB  
3918  C CG  . LYS A 259 ? 0.8892 1.3199 0.9020 0.0083  0.0566  0.0657  259 LYS A CG  
3919  C CD  . LYS A 259 ? 0.9504 1.4308 0.9734 0.0040  0.0698  0.0671  259 LYS A CD  
3920  C CE  . LYS A 259 ? 1.0302 1.5214 1.0365 -0.0146 0.0764  0.0814  259 LYS A CE  
3921  N NZ  . LYS A 259 ? 1.0759 1.6185 1.0926 -0.0211 0.0905  0.0838  259 LYS A NZ  
3935  N N   . ASN A 260 ? 0.6836 1.0262 0.7033 0.0285  0.0286  0.0529  260 ASN A N   
3936  C CA  . ASN A 260 ? 0.7052 1.0312 0.7183 0.0453  0.0262  0.0390  260 ASN A CA  
3937  C C   . ASN A 260 ? 0.6467 0.9412 0.6651 0.0495  0.0158  0.0371  260 ASN A C   
3938  O O   . ASN A 260 ? 0.6312 0.9098 0.6460 0.0626  0.0130  0.0264  260 ASN A O   
3939  C CB  . ASN A 260 ? 0.8301 1.1849 0.8521 0.0604  0.0336  0.0271  260 ASN A CB  
3940  C CG  . ASN A 260 ? 1.0033 1.3881 1.0487 0.0589  0.0361  0.0307  260 ASN A CG  
3941  O OD1 . ASN A 260 ? 0.9869 1.3646 1.0426 0.0489  0.0302  0.0399  260 ASN A OD1 
3942  N ND2 . ASN A 260 ? 1.2159 1.6361 1.2705 0.0691  0.0448  0.0225  260 ASN A ND2 
3948  N N   . MET A 261 ? 0.6532 0.9375 0.6789 0.0386  0.0101  0.0470  261 MET A N   
3949  C CA  . MET A 261 ? 0.6739 0.9311 0.7035 0.0412  0.0011  0.0460  261 MET A CA  
3950  C C   . MET A 261 ? 0.6712 0.9342 0.7130 0.0547  -0.0003 0.0384  261 MET A C   
3951  O O   . MET A 261 ? 0.6896 0.9284 0.7302 0.0605  -0.0069 0.0353  261 MET A O   
3952  C CB  . MET A 261 ? 0.6745 0.9004 0.6887 0.0433  -0.0035 0.0421  261 MET A CB  
3953  C CG  . MET A 261 ? 0.6750 0.8740 0.6911 0.0402  -0.0118 0.0446  261 MET A CG  
3954  S SD  . MET A 261 ? 0.6739 0.8682 0.6929 0.0238  -0.0156 0.0571  261 MET A SD  
3955  C CE  . MET A 261 ? 0.6535 0.8328 0.6558 0.0187  -0.0168 0.0592  261 MET A CE  
3965  N N   . SER A 262 ? 0.6618 0.9575 0.7155 0.0601  0.0057  0.0358  262 SER A N   
3966  C CA  . SER A 262 ? 0.6432 0.9473 0.7111 0.0732  0.0030  0.0299  262 SER A CA  
3967  C C   . SER A 262 ? 0.6533 0.9574 0.7339 0.0651  -0.0036 0.0379  262 SER A C   
3968  O O   . SER A 262 ? 0.6729 0.9860 0.7573 0.0497  -0.0030 0.0470  262 SER A O   
3969  C CB  . SER A 262 ? 0.6345 0.9782 0.7135 0.0820  0.0115  0.0238  262 SER A CB  
3970  O OG  . SER A 262 ? 0.6936 1.0479 0.7886 0.0957  0.0078  0.0186  262 SER A OG  
3976  N N   . SER A 263 ? 0.6501 0.9423 0.7358 0.0755  -0.0107 0.0346  263 SER A N   
3977  C CA  . SER A 263 ? 0.6291 0.9186 0.7239 0.0690  -0.0182 0.0410  263 SER A CA  
3978  C C   . SER A 263 ? 0.6231 0.9521 0.7384 0.0671  -0.0163 0.0429  263 SER A C   
3979  O O   . SER A 263 ? 0.5766 0.9303 0.7028 0.0803  -0.0132 0.0364  263 SER A O   
3980  C CB  . SER A 263 ? 0.6512 0.9157 0.7425 0.0806  -0.0265 0.0377  263 SER A CB  
3981  O OG  . SER A 263 ? 0.6720 0.9320 0.7683 0.0736  -0.0339 0.0438  263 SER A OG  
3987  N N   . LEU A 264 ? 0.6225 0.9580 0.7440 0.0509  -0.0186 0.0512  264 LEU A N   
3988  C CA  . LEU A 264 ? 0.6362 1.0100 0.7780 0.0446  -0.0170 0.0540  264 LEU A CA  
3989  C C   . LEU A 264 ? 0.5930 0.9679 0.7460 0.0433  -0.0272 0.0560  264 LEU A C   
3990  O O   . LEU A 264 ? 0.5950 0.9978 0.7653 0.0521  -0.0292 0.0527  264 LEU A O   
3991  C CB  . LEU A 264 ? 0.6750 1.0584 0.8158 0.0243  -0.0116 0.0625  264 LEU A CB  
3992  C CG  . LEU A 264 ? 0.7415 1.1423 0.8767 0.0228  0.0001  0.0622  264 LEU A CG  
3993  C CD1 . LEU A 264 ? 0.7685 1.1747 0.9020 0.0008  0.0032  0.0733  264 LEU A CD1 
3994  C CD2 . LEU A 264 ? 0.7401 1.1826 0.8912 0.0348  0.0072  0.0552  264 LEU A CD2 
4006  N N   A TYR A 265 ? 0.6240 0.9706 0.7675 0.0334  -0.0341 0.0606  265 TYR A N   
4007  N N   B TYR A 265 ? 0.6244 0.9710 0.7679 0.0333  -0.0341 0.0607  265 TYR A N   
4008  C CA  A TYR A 265 ? 0.5679 0.9153 0.7194 0.0311  -0.0441 0.0621  265 TYR A CA  
4009  C CA  B TYR A 265 ? 0.5679 0.9146 0.7190 0.0301  -0.0440 0.0624  265 TYR A CA  
4010  C C   A TYR A 265 ? 0.6450 0.9522 0.7789 0.0305  -0.0508 0.0629  265 TYR A C   
4011  C C   B TYR A 265 ? 0.6451 0.9517 0.7785 0.0313  -0.0507 0.0626  265 TYR A C   
4012  O O   A TYR A 265 ? 0.5998 0.8817 0.7185 0.0266  -0.0478 0.0638  265 TYR A O   
4013  O O   B TYR A 265 ? 0.6016 0.8822 0.7194 0.0292  -0.0477 0.0630  265 TYR A O   
4014  C CB  A TYR A 265 ? 0.5830 0.9523 0.7478 0.0127  -0.0450 0.0676  265 TYR A CB  
4015  C CB  B TYR A 265 ? 0.5812 0.9446 0.7430 0.0104  -0.0450 0.0684  265 TYR A CB  
4016  C CG  A TYR A 265 ? 0.4911 0.8693 0.6671 0.0111  -0.0556 0.0675  265 TYR A CG  
4017  C CG  B TYR A 265 ? 0.4906 0.8980 0.6719 0.0061  -0.0381 0.0693  265 TYR A CG  
4018  C CD1 A TYR A 265 ? 0.4580 0.8695 0.6528 0.0212  -0.0583 0.0642  265 TYR A CD1 
4019  C CD1 B TYR A 265 ? 0.4489 0.8909 0.6509 0.0142  -0.0409 0.0657  265 TYR A CD1 
4020  C CD2 A TYR A 265 ? 0.4754 0.8299 0.6429 0.0001  -0.0634 0.0700  265 TYR A CD2 
4021  C CD2 B TYR A 265 ? 0.4822 0.8984 0.6613 -0.0063 -0.0288 0.0741  265 TYR A CD2 
4022  C CE1 A TYR A 265 ? 0.4380 0.8587 0.6423 0.0198  -0.0693 0.0641  265 TYR A CE1 
4023  C CE1 B TYR A 265 ? 0.4252 0.9119 0.6470 0.0099  -0.0338 0.0660  265 TYR A CE1 
4024  C CE2 A TYR A 265 ? 0.4536 0.8164 0.6291 -0.0017 -0.0736 0.0692  265 TYR A CE2 
4025  C CE2 B TYR A 265 ? 0.4514 0.9104 0.6478 -0.0118 -0.0213 0.0755  265 TYR A CE2 
4026  C CZ  A TYR A 265 ? 0.4259 0.8218 0.6196 0.0078  -0.0769 0.0667  265 TYR A CZ  
4027  C CZ  B TYR A 265 ? 0.4315 0.9271 0.6502 -0.0038 -0.0233 0.0710  265 TYR A CZ  
4028  O OH  A TYR A 265 ? 0.4415 0.8467 0.6427 0.0061  -0.0884 0.0659  265 TYR A OH  
4029  O OH  B TYR A 265 ? 0.4174 0.9600 0.6555 -0.0096 -0.0150 0.0718  265 TYR A OH  
4048  N N   . ASN A 266 ? 0.6173 0.9211 0.7533 0.0343  -0.0600 0.0625  266 ASN A N   
4049  C CA  . ASN A 266 ? 0.6012 0.8716 0.7209 0.0348  -0.0662 0.0629  266 ASN A CA  
4050  C C   . ASN A 266 ? 0.6349 0.9085 0.7584 0.0253  -0.0749 0.0649  266 ASN A C   
4051  O O   . ASN A 266 ? 0.7144 1.0151 0.8535 0.0260  -0.0795 0.0647  266 ASN A O   
4052  C CB  . ASN A 266 ? 0.5975 0.8550 0.7103 0.0522  -0.0695 0.0601  266 ASN A CB  
4053  C CG  . ASN A 266 ? 0.6224 0.8598 0.7230 0.0591  -0.0630 0.0574  266 ASN A CG  
4054  O OD1 . ASN A 266 ? 0.5950 0.8185 0.6867 0.0505  -0.0581 0.0582  266 ASN A OD1 
4055  N ND2 . ASN A 266 ? 0.7647 0.9995 0.8647 0.0752  -0.0640 0.0538  266 ASN A ND2 
4062  N N   . PHE A 267 ? 0.6227 0.8702 0.7325 0.0168  -0.0775 0.0658  267 PHE A N   
4063  C CA  . PHE A 267 ? 0.6197 0.8638 0.7277 0.0101  -0.0864 0.0658  267 PHE A CA  
4064  C C   . PHE A 267 ? 0.6529 0.8694 0.7422 0.0166  -0.0899 0.0649  267 PHE A C   
4065  O O   . PHE A 267 ? 0.6760 0.8718 0.7534 0.0204  -0.0847 0.0646  267 PHE A O   
4066  C CB  . PHE A 267 ? 0.6074 0.8459 0.7156 -0.0069 -0.0867 0.0666  267 PHE A CB  
4067  C CG  . PHE A 267 ? 0.5765 0.8400 0.7014 -0.0170 -0.0832 0.0693  267 PHE A CG  
4068  C CD1 . PHE A 267 ? 0.5923 0.8565 0.7172 -0.0190 -0.0740 0.0719  267 PHE A CD1 
4069  C CD2 . PHE A 267 ? 0.5286 0.8155 0.6686 -0.0255 -0.0893 0.0696  267 PHE A CD2 
4070  C CE1 . PHE A 267 ? 0.6006 0.8884 0.7392 -0.0297 -0.0701 0.0756  267 PHE A CE1 
4071  C CE2 . PHE A 267 ? 0.5372 0.8484 0.6930 -0.0369 -0.0855 0.0729  267 PHE A CE2 
4072  C CZ  . PHE A 267 ? 0.5901 0.9016 0.7446 -0.0392 -0.0755 0.0764  267 PHE A CZ  
4082  N N   . THR A 268 ? 0.6542 0.8719 0.7406 0.0171  -0.0989 0.0646  268 THR A N   
4083  C CA  . THR A 268 ? 0.6586 0.8528 0.7260 0.0222  -0.1023 0.0648  268 THR A CA  
4084  C C   . THR A 268 ? 0.6617 0.8523 0.7221 0.0132  -0.1096 0.0630  268 THR A C   
4085  O O   . THR A 268 ? 0.6512 0.8615 0.7226 0.0085  -0.1164 0.0621  268 THR A O   
4086  C CB  . THR A 268 ? 0.6610 0.8582 0.7270 0.0371  -0.1068 0.0670  268 THR A CB  
4087  O OG1 . THR A 268 ? 0.6997 0.9005 0.7727 0.0463  -0.1003 0.0668  268 THR A OG1 
4088  C CG2 . THR A 268 ? 0.6378 0.8083 0.6817 0.0405  -0.1093 0.0691  268 THR A CG2 
4096  N N   . GLY A 269 ? 0.6600 0.8269 0.7024 0.0106  -0.1081 0.0617  269 GLY A N   
4097  C CA  . GLY A 269 ? 0.6813 0.8430 0.7141 0.0033  -0.1142 0.0583  269 GLY A CA  
4098  C C   . GLY A 269 ? 0.7386 0.9065 0.7641 0.0091  -0.1237 0.0601  269 GLY A C   
4099  O O   . GLY A 269 ? 0.8036 0.9751 0.8293 0.0200  -0.1257 0.0646  269 GLY A O   
4103  N N   . GLU A 270 ? 0.7693 0.9370 0.7871 0.0020  -0.1305 0.0560  270 GLU A N   
4104  C CA  . GLU A 270 ? 0.8297 1.0050 0.8392 0.0058  -0.1412 0.0572  270 GLU A CA  
4105  C C   . GLU A 270 ? 0.7858 0.9418 0.7686 0.0061  -0.1416 0.0568  270 GLU A C   
4106  O O   . GLU A 270 ? 0.8093 0.9683 0.7805 0.0108  -0.1500 0.0599  270 GLU A O   
4107  C CB  . GLU A 270 ? 0.9582 1.1525 0.9790 -0.0032 -0.1506 0.0522  270 GLU A CB  
4108  C CG  . GLU A 270 ? 1.1109 1.3307 1.1590 -0.0049 -0.1514 0.0534  270 GLU A CG  
4109  C CD  . GLU A 270 ? 1.2510 1.4924 1.3087 0.0066  -0.1585 0.0579  270 GLU A CD  
4110  O OE1 . GLU A 270 ? 1.3005 1.5335 1.3517 0.0194  -0.1556 0.0629  270 GLU A OE1 
4111  O OE2 . GLU A 270 ? 1.2989 1.5656 1.3714 0.0030  -0.1678 0.0561  270 GLU A OE2 
4118  N N   . GLN A 271 ? 0.7466 0.8850 0.7195 0.0013  -0.1330 0.0532  271 GLN A N   
4119  C CA  . GLN A 271 ? 0.7694 0.8936 0.7181 0.0000  -0.1320 0.0515  271 GLN A CA  
4120  C C   . GLN A 271 ? 0.7903 0.8973 0.7315 0.0014  -0.1203 0.0534  271 GLN A C   
4121  O O   . GLN A 271 ? 0.7946 0.8984 0.7479 -0.0005 -0.1132 0.0511  271 GLN A O   
4122  C CB  . GLN A 271 ? 0.7699 0.8939 0.7137 -0.0091 -0.1349 0.0411  271 GLN A CB  
4123  C CG  . GLN A 271 ? 0.8199 0.9325 0.7384 -0.0103 -0.1325 0.0375  271 GLN A CG  
4124  C CD  . GLN A 271 ? 0.8474 0.9596 0.7612 -0.0177 -0.1362 0.0252  271 GLN A CD  
4125  O OE1 . GLN A 271 ? 0.9077 1.0098 0.8203 -0.0206 -0.1292 0.0178  271 GLN A OE1 
4126  N NE2 . GLN A 271 ? 0.7828 0.9059 0.6941 -0.0203 -0.1479 0.0222  271 GLN A NE2 
4135  N N   . MET A 272 ? 0.8039 0.9006 0.7249 0.0041  -0.1188 0.0580  272 MET A N   
4136  C CA  . MET A 272 ? 0.8356 0.9174 0.7492 0.0040  -0.1081 0.0602  272 MET A CA  
4137  C C   . MET A 272 ? 0.8065 0.8852 0.7208 -0.0026 -0.1008 0.0507  272 MET A C   
4138  O O   . MET A 272 ? 0.8210 0.9023 0.7269 -0.0068 -0.1032 0.0433  272 MET A O   
4139  C CB  . MET A 272 ? 0.9483 1.0204 0.8380 0.0054  -0.1084 0.0674  272 MET A CB  
4140  C CG  . MET A 272 ? 1.0421 1.1113 0.9303 0.0139  -0.1151 0.0780  272 MET A CG  
4141  S SD  . MET A 272 ? 1.1418 1.1915 1.0281 0.0171  -0.1068 0.0858  272 MET A SD  
4142  C CE  . MET A 272 ? 1.1878 1.2389 1.0836 0.0302  -0.1168 0.0934  272 MET A CE  
4152  N N   . ALA A 273 ? 0.7800 0.8527 0.7042 -0.0026 -0.0926 0.0503  273 ALA A N   
4153  C CA  . ALA A 273 ? 0.7928 0.8614 0.7177 -0.0067 -0.0853 0.0422  273 ALA A CA  
4154  C C   . ALA A 273 ? 0.7597 0.8327 0.6931 -0.0103 -0.0895 0.0330  273 ALA A C   
4155  O O   . ALA A 273 ? 0.7659 0.8355 0.6952 -0.0127 -0.0864 0.0244  273 ALA A O   
4156  C CB  . ALA A 273 ? 0.8006 0.8651 0.7057 -0.0091 -0.0802 0.0409  273 ALA A CB  
4162  N N   . ALA A 274 ? 0.7303 0.8108 0.6761 -0.0108 -0.0966 0.0344  274 ALA A N   
4163  C CA  . ALA A 274 ? 0.7477 0.8296 0.7035 -0.0159 -0.1007 0.0270  274 ALA A CA  
4164  C C   . ALA A 274 ? 0.6951 0.7712 0.6647 -0.0168 -0.0953 0.0263  274 ALA A C   
4165  O O   . ALA A 274 ? 0.7095 0.7830 0.6871 -0.0215 -0.0985 0.0215  274 ALA A O   
4166  C CB  . ALA A 274 ? 0.7530 0.8476 0.7184 -0.0181 -0.1101 0.0294  274 ALA A CB  
4172  N N   . TYR A 275 ? 0.6110 0.6838 0.5822 -0.0129 -0.0880 0.0313  275 TYR A N   
4173  C CA  . TYR A 275 ? 0.6128 0.6818 0.5961 -0.0130 -0.0837 0.0320  275 TYR A CA  
4174  C C   . TYR A 275 ? 0.6176 0.6938 0.6151 -0.0163 -0.0879 0.0353  275 TYR A C   
4175  O O   . TYR A 275 ? 0.5628 0.6347 0.5682 -0.0202 -0.0882 0.0337  275 TYR A O   
4176  C CB  . TYR A 275 ? 0.6362 0.6955 0.6179 -0.0142 -0.0811 0.0239  275 TYR A CB  
4177  C CG  . TYR A 275 ? 0.6516 0.7069 0.6347 -0.0109 -0.0735 0.0250  275 TYR A CG  
4178  C CD1 . TYR A 275 ? 0.6270 0.6808 0.6209 -0.0104 -0.0719 0.0286  275 TYR A CD1 
4179  C CD2 . TYR A 275 ? 0.6566 0.7111 0.6299 -0.0091 -0.0679 0.0230  275 TYR A CD2 
4180  C CE1 . TYR A 275 ? 0.6395 0.6907 0.6348 -0.0076 -0.0662 0.0291  275 TYR A CE1 
4181  C CE2 . TYR A 275 ? 0.6573 0.7100 0.6335 -0.0072 -0.0616 0.0237  275 TYR A CE2 
4182  C CZ  . TYR A 275 ? 0.6577 0.7087 0.6452 -0.0062 -0.0612 0.0264  275 TYR A CZ  
4183  O OH  . TYR A 275 ? 0.6945 0.7447 0.6849 -0.0046 -0.0561 0.0265  275 TYR A OH  
4193  N N   . PHE A 276 ? 0.6127 0.6913 0.6527 -0.0070 -0.0946 0.1104  276 PHE A N   
4194  C CA  . PHE A 276 ? 0.6205 0.7099 0.6657 -0.0111 -0.1005 0.1116  276 PHE A CA  
4195  C C   . PHE A 276 ? 0.6152 0.7142 0.6728 -0.0115 -0.0978 0.1077  276 PHE A C   
4196  O O   . PHE A 276 ? 0.5750 0.6809 0.6459 -0.0085 -0.0925 0.1056  276 PHE A O   
4197  C CB  . PHE A 276 ? 0.6643 0.7603 0.7154 -0.0107 -0.1023 0.1157  276 PHE A CB  
4198  C CG  . PHE A 276 ? 0.6577 0.7662 0.7180 -0.0150 -0.1067 0.1162  276 PHE A CG  
4199  C CD1 . PHE A 276 ? 0.6676 0.7888 0.7444 -0.0150 -0.1026 0.1138  276 PHE A CD1 
4200  C CD2 . PHE A 276 ? 0.6222 0.7299 0.6760 -0.0192 -0.1143 0.1183  276 PHE A CD2 
4201  C CE1 . PHE A 276 ? 0.6682 0.8008 0.7537 -0.0193 -0.1049 0.1136  276 PHE A CE1 
4202  C CE2 . PHE A 276 ? 0.6263 0.7455 0.6908 -0.0236 -0.1169 0.1183  276 PHE A CE2 
4203  C CZ  . PHE A 276 ? 0.6453 0.7769 0.7252 -0.0238 -0.1117 0.1161  276 PHE A CZ  
4213  N N   . GLY A 277 ? 0.6301 0.7291 0.6830 -0.0150 -0.1018 0.1067  277 GLY A N   
4214  C CA  . GLY A 277 ? 0.6311 0.7372 0.6908 -0.0153 -0.1005 0.1032  277 GLY A CA  
4215  C C   . GLY A 277 ? 0.6547 0.7528 0.7105 -0.0132 -0.1009 0.0997  277 GLY A C   
4216  O O   . GLY A 277 ? 0.6137 0.7169 0.6739 -0.0127 -0.1011 0.0965  277 GLY A O   
4220  N N   . PHE A 278 ? 0.6524 0.7381 0.7005 -0.0118 -0.1013 0.0996  278 PHE A N   
4221  C CA  . PHE A 278 ? 0.6549 0.7326 0.7015 -0.0099 -0.1024 0.0958  278 PHE A CA  
4222  C C   . PHE A 278 ? 0.6203 0.6984 0.6617 -0.0132 -0.1089 0.0973  278 PHE A C   
4223  O O   . PHE A 278 ? 0.5738 0.6503 0.6178 -0.0110 -0.1108 0.0941  278 PHE A O   
4224  C CB  . PHE A 278 ? 0.6829 0.7472 0.7207 -0.0092 -0.1020 0.0956  278 PHE A CB  
4225  C CG  . PHE A 278 ? 0.6847 0.7404 0.7240 -0.0068 -0.1028 0.0909  278 PHE A CG  
4226  C CD1 . PHE A 278 ? 0.6703 0.7248 0.7207 -0.0020 -0.0967 0.0853  278 PHE A CD1 
4227  C CD2 . PHE A 278 ? 0.6767 0.7253 0.7086 -0.0094 -0.1095 0.0919  278 PHE A CD2 
4228  C CE1 . PHE A 278 ? 0.6631 0.7104 0.7181 0.0004  -0.0978 0.0802  278 PHE A CE1 
4229  C CE2 . PHE A 278 ? 0.6795 0.7200 0.7150 -0.0068 -0.1110 0.0875  278 PHE A CE2 
4230  C CZ  . PHE A 278 ? 0.6711 0.7114 0.7186 -0.0018 -0.1054 0.0813  278 PHE A CZ  
4240  N N   . SER A 279 ? 0.6333 0.7132 0.6677 -0.0185 -0.1125 0.1022  279 SER A N   
4241  C CA  . SER A 279 ? 0.6678 0.7470 0.6960 -0.0225 -0.1173 0.1050  279 SER A CA  
4242  C C   . SER A 279 ? 0.6450 0.7340 0.6736 -0.0278 -0.1169 0.1088  279 SER A C   
4243  O O   . SER A 279 ? 0.6059 0.6982 0.6373 -0.0290 -0.1159 0.1101  279 SER A O   
4244  C CB  . SER A 279 ? 0.7310 0.7966 0.7502 -0.0244 -0.1224 0.1068  279 SER A CB  
4245  O OG  . SER A 279 ? 0.8028 0.8646 0.8184 -0.0265 -0.1228 0.1080  279 SER A OG  
4251  N N   . VAL A 280 ? 0.6613 0.7548 0.6872 -0.0307 -0.1177 0.1105  280 VAL A N   
4252  C CA  . VAL A 280 ? 0.6956 0.7982 0.7226 -0.0365 -0.1159 0.1135  280 VAL A CA  
4253  C C   . VAL A 280 ? 0.7097 0.8073 0.7261 -0.0413 -0.1185 0.1180  280 VAL A C   
4254  O O   . VAL A 280 ? 0.6943 0.7850 0.7035 -0.0391 -0.1215 0.1181  280 VAL A O   
4255  C CB  . VAL A 280 ? 0.7143 0.8317 0.7513 -0.0351 -0.1103 0.1100  280 VAL A CB  
4256  C CG1 . VAL A 280 ? 0.7403 0.8615 0.7886 -0.0305 -0.1075 0.1069  280 VAL A CG1 
4257  C CG2 . VAL A 280 ? 0.7001 0.8192 0.7340 -0.0322 -0.1101 0.1067  280 VAL A CG2 
4267  N N   . ALA A 281 ? 0.6888 0.7894 0.7052 -0.0480 -0.1174 0.1218  281 ALA A N   
4268  C CA  . ALA A 281 ? 0.6847 0.7803 0.6912 -0.0537 -0.1181 0.1272  281 ALA A CA  
4269  C C   . ALA A 281 ? 0.6495 0.7562 0.6616 -0.0603 -0.1125 0.1288  281 ALA A C   
4270  O O   . ALA A 281 ? 0.6162 0.7317 0.6408 -0.0610 -0.1107 0.1264  281 ALA A O   
4271  C CB  . ALA A 281 ? 0.7066 0.7873 0.7075 -0.0560 -0.1237 0.1309  281 ALA A CB  
4277  N N   . ALA A 282 ? 0.6464 0.7523 0.6492 -0.0651 -0.1097 0.1328  282 ALA A N   
4278  C CA  . ALA A 282 ? 0.6396 0.7555 0.6473 -0.0722 -0.1025 0.1341  282 ALA A CA  
4279  C C   . ALA A 282 ? 0.6935 0.7990 0.6908 -0.0795 -0.1020 0.1417  282 ALA A C   
4280  O O   . ALA A 282 ? 0.7156 0.8119 0.6964 -0.0791 -0.1034 0.1459  282 ALA A O   
4281  C CB  . ALA A 282 ? 0.5991 0.7273 0.6059 -0.0711 -0.0960 0.1302  282 ALA A CB  
4287  N N   . THR A 283 ? 0.6858 0.7925 0.6933 -0.0859 -0.1003 0.1434  283 THR A N   
4288  C CA  . THR A 283 ? 0.7116 0.8090 0.7130 -0.0939 -0.0983 0.1505  283 THR A CA  
4289  C C   . THR A 283 ? 0.7645 0.8700 0.7845 -0.1009 -0.0944 0.1493  283 THR A C   
4290  O O   . THR A 283 ? 0.7648 0.8763 0.7994 -0.0985 -0.0986 0.1442  283 THR A O   
4291  C CB  . THR A 283 ? 0.7216 0.8005 0.7141 -0.0923 -0.1067 0.1548  283 THR A CB  
4292  O OG1 . THR A 283 ? 0.7469 0.8161 0.7347 -0.1003 -0.1040 0.1623  283 THR A OG1 
4293  C CG2 . THR A 283 ? 0.6942 0.7716 0.6987 -0.0894 -0.1134 0.1501  283 THR A CG2 
4301  N N   . ASP A 284 ? 0.8215 0.9269 0.8407 -0.1095 -0.0866 0.1538  284 ASP A N   
4302  C CA  . ASP A 284 ? 0.7998 0.9131 0.8394 -0.1170 -0.0822 0.1523  284 ASP A CA  
4303  C C   . ASP A 284 ? 0.7878 0.8892 0.8329 -0.1195 -0.0898 0.1543  284 ASP A C   
4304  O O   . ASP A 284 ? 0.8349 0.9222 0.8703 -0.1239 -0.0893 0.1611  284 ASP A O   
4305  C CB  . ASP A 284 ? 0.8043 0.9208 0.8415 -0.1259 -0.0695 0.1563  284 ASP A CB  
4306  C CG  . ASP A 284 ? 0.8129 0.9381 0.8748 -0.1343 -0.0641 0.1541  284 ASP A CG  
4307  O OD1 . ASP A 284 ? 0.8025 0.9352 0.8843 -0.1321 -0.0707 0.1480  284 ASP A OD1 
4308  O OD2 . ASP A 284 ? 0.8263 0.9505 0.8876 -0.1432 -0.0534 0.1584  284 ASP A OD2 
4313  N N   . ILE A 285 ? 0.7590 0.8655 0.8193 -0.1165 -0.0971 0.1482  285 ILE A N   
4314  C CA  . ILE A 285 ? 0.7805 0.8758 0.8446 -0.1176 -0.1057 0.1482  285 ILE A CA  
4315  C C   . ILE A 285 ? 0.7998 0.8989 0.8841 -0.1266 -0.1036 0.1472  285 ILE A C   
4316  O O   . ILE A 285 ? 0.7956 0.8840 0.8832 -0.1296 -0.1092 0.1477  285 ILE A O   
4317  C CB  . ILE A 285 ? 0.7994 0.8959 0.8653 -0.1093 -0.1155 0.1421  285 ILE A CB  
4318  C CG1 . ILE A 285 ? 0.8585 0.9391 0.9185 -0.1083 -0.1242 0.1422  285 ILE A CG1 
4319  C CG2 . ILE A 285 ? 0.8042 0.9155 0.8908 -0.1098 -0.1174 0.1360  285 ILE A CG2 
4320  C CD1 . ILE A 285 ? 0.8921 0.9583 0.9328 -0.1042 -0.1254 0.1465  285 ILE A CD1 
4332  N N   . ASN A 286 ? 0.8006 0.9149 0.9007 -0.1312 -0.0956 0.1449  286 ASN A N   
4333  C CA  . ASN A 286 ? 0.7974 0.9178 0.9218 -0.1394 -0.0939 0.1422  286 ASN A CA  
4334  C C   . ASN A 286 ? 0.8013 0.9241 0.9302 -0.1493 -0.0796 0.1467  286 ASN A C   
4335  O O   . ASN A 286 ? 0.8689 1.0000 1.0221 -0.1566 -0.0755 0.1435  286 ASN A O   
4336  C CB  . ASN A 286 ? 0.7824 0.9201 0.9286 -0.1362 -0.0983 0.1339  286 ASN A CB  
4337  C CG  . ASN A 286 ? 0.7556 0.9077 0.9036 -0.1334 -0.0903 0.1320  286 ASN A CG  
4338  O OD1 . ASN A 286 ? 0.7315 0.8802 0.8596 -0.1299 -0.0857 0.1354  286 ASN A OD1 
4339  N ND2 . ASN A 286 ? 0.7628 0.9313 0.9362 -0.1347 -0.0892 0.1259  286 ASN A ND2 
4346  N N   . GLY A 287 ? 0.7780 0.8936 0.8844 -0.1497 -0.0717 0.1537  287 GLY A N   
4347  C CA  . GLY A 287 ? 0.7708 0.8838 0.8754 -0.1596 -0.0579 0.1598  287 GLY A CA  
4348  C C   . GLY A 287 ? 0.7786 0.9096 0.8974 -0.1643 -0.0448 0.1558  287 GLY A C   
4349  O O   . GLY A 287 ? 0.8070 0.9377 0.9321 -0.1742 -0.0324 0.1591  287 GLY A O   
4353  N N   . ASP A 288 ? 0.7669 0.9131 0.8919 -0.1577 -0.0464 0.1486  288 ASP A N   
4354  C CA  . ASP A 288 ? 0.7906 0.9544 0.9302 -0.1614 -0.0338 0.1436  288 ASP A CA  
4355  C C   . ASP A 288 ? 0.8646 1.0295 0.9798 -0.1587 -0.0254 0.1456  288 ASP A C   
4356  O O   . ASP A 288 ? 0.9014 1.0819 1.0270 -0.1597 -0.0158 0.1397  288 ASP A O   
4357  C CB  . ASP A 288 ? 0.7830 0.9640 0.9502 -0.1563 -0.0406 0.1336  288 ASP A CB  
4358  C CG  . ASP A 288 ? 0.8044 0.9850 0.9595 -0.1444 -0.0521 0.1314  288 ASP A CG  
4359  O OD1 . ASP A 288 ? 0.8124 0.9802 0.9400 -0.1399 -0.0551 0.1366  288 ASP A OD1 
4360  O OD2 . ASP A 288 ? 0.7884 0.9811 0.9626 -0.1393 -0.0581 0.1246  288 ASP A OD2 
4365  N N   . ASP A 289 ? 0.8883 1.0374 0.9727 -0.1551 -0.0292 0.1529  289 ASP A N   
4366  C CA  . ASP A 289 ? 0.8916 1.0397 0.9498 -0.1520 -0.0235 0.1550  289 ASP A CA  
4367  C C   . ASP A 289 ? 0.8293 0.9914 0.8922 -0.1430 -0.0271 0.1462  289 ASP A C   
4368  O O   . ASP A 289 ? 0.8523 1.0174 0.8984 -0.1405 -0.0218 0.1452  289 ASP A O   
4369  C CB  . ASP A 289 ? 0.9633 1.1147 1.0160 -0.1617 -0.0057 0.1576  289 ASP A CB  
4370  C CG  . ASP A 289 ? 1.0196 1.1532 1.0595 -0.1702 -0.0009 0.1688  289 ASP A CG  
4371  O OD1 . ASP A 289 ? 1.0295 1.1454 1.0494 -0.1667 -0.0106 0.1764  289 ASP A OD1 
4372  O OD2 . ASP A 289 ? 1.0294 1.1666 1.0808 -0.1805 0.0130  0.1698  289 ASP A OD2 
4377  N N   . TYR A 290 ? 0.7933 0.9633 0.8782 -0.1379 -0.0362 0.1399  290 TYR A N   
4378  C CA  . TYR A 290 ? 0.7735 0.9541 0.8634 -0.1287 -0.0407 0.1328  290 TYR A CA  
4379  C C   . TYR A 290 ? 0.7737 0.9424 0.8507 -0.1200 -0.0547 0.1348  290 TYR A C   
4380  O O   . TYR A 290 ? 0.7839 0.9458 0.8678 -0.1194 -0.0637 0.1361  290 TYR A O   
4381  C CB  . TYR A 290 ? 0.7554 0.9527 0.8785 -0.1286 -0.0409 0.1249  290 TYR A CB  
4382  C CG  . TYR A 290 ? 0.7766 0.9894 0.9157 -0.1351 -0.0263 0.1199  290 TYR A CG  
4383  C CD1 . TYR A 290 ? 0.7419 0.9657 0.8793 -0.1318 -0.0194 0.1141  290 TYR A CD1 
4384  C CD2 . TYR A 290 ? 0.8175 1.0343 0.9751 -0.1448 -0.0189 0.1200  290 TYR A CD2 
4385  C CE1 . TYR A 290 ? 0.7625 1.0007 0.9151 -0.1378 -0.0051 0.1084  290 TYR A CE1 
4386  C CE2 . TYR A 290 ? 0.8186 1.0498 0.9925 -0.1510 -0.0042 0.1146  290 TYR A CE2 
4387  C CZ  . TYR A 290 ? 0.7980 1.0399 0.9688 -0.1474 0.0028  0.1087  290 TYR A CZ  
4388  O OH  . TYR A 290 ? 0.7638 1.0205 0.9514 -0.1537 0.0184  0.1023  290 TYR A OH  
4398  N N   . ALA A 291 ? 0.7731 0.9395 0.8323 -0.1134 -0.0561 0.1343  291 ALA A N   
4399  C CA  . ALA A 291 ? 0.7572 0.9125 0.8051 -0.1052 -0.0677 0.1355  291 ALA A CA  
4400  C C   . ALA A 291 ? 0.6972 0.8581 0.7636 -0.0997 -0.0754 0.1305  291 ALA A C   
4401  O O   . ALA A 291 ? 0.6669 0.8423 0.7512 -0.0982 -0.0724 0.1246  291 ALA A O   
4402  C CB  . ALA A 291 ? 0.7708 0.9258 0.8014 -0.0991 -0.0673 0.1339  291 ALA A CB  
4408  N N   . ASP A 292 ? 0.6935 0.8422 0.7550 -0.0966 -0.0852 0.1329  292 ASP A N   
4409  C CA  . ASP A 292 ? 0.7168 0.8675 0.7904 -0.0914 -0.0931 0.1292  292 ASP A CA  
4410  C C   . ASP A 292 ? 0.7386 0.8819 0.8001 -0.0826 -0.0988 0.1283  292 ASP A C   
4411  O O   . ASP A 292 ? 0.7888 0.9207 0.8334 -0.0811 -0.1005 0.1314  292 ASP A O   
4412  C CB  . ASP A 292 ? 0.7410 0.8841 0.8201 -0.0956 -0.0994 0.1312  292 ASP A CB  
4413  C CG  . ASP A 292 ? 0.7601 0.9094 0.8529 -0.1052 -0.0931 0.1321  292 ASP A CG  
4414  O OD1 . ASP A 292 ? 0.7725 0.9367 0.8800 -0.1073 -0.0860 0.1286  292 ASP A OD1 
4415  O OD2 . ASP A 292 ? 0.7713 0.9108 0.8620 -0.1109 -0.0946 0.1358  292 ASP A OD2 
4420  N N   . VAL A 293 ? 0.6988 0.8482 0.7702 -0.0766 -0.1017 0.1242  293 VAL A N   
4421  C CA  . VAL A 293 ? 0.6500 0.7946 0.7138 -0.0683 -0.1047 0.1224  293 VAL A CA  
4422  C C   . VAL A 293 ? 0.6184 0.7517 0.6779 -0.0654 -0.1129 0.1232  293 VAL A C   
4423  O O   . VAL A 293 ? 0.6469 0.7822 0.7153 -0.0666 -0.1169 0.1227  293 VAL A O   
4424  C CB  . VAL A 293 ? 0.6402 0.7978 0.7172 -0.0635 -0.1012 0.1176  293 VAL A CB  
4425  C CG1 . VAL A 293 ? 0.6495 0.8014 0.7206 -0.0554 -0.1033 0.1158  293 VAL A CG1 
4426  C CG2 . VAL A 293 ? 0.6378 0.8069 0.7187 -0.0665 -0.0925 0.1153  293 VAL A CG2 
4436  N N   . PHE A 294 ? 0.6214 0.7428 0.6675 -0.0614 -0.1156 0.1239  294 PHE A N   
4437  C CA  . PHE A 294 ? 0.6416 0.7518 0.6821 -0.0578 -0.1217 0.1234  294 PHE A CA  
4438  C C   . PHE A 294 ? 0.6167 0.7257 0.6550 -0.0500 -0.1204 0.1204  294 PHE A C   
4439  O O   . PHE A 294 ? 0.6010 0.7107 0.6363 -0.0476 -0.1174 0.1194  294 PHE A O   
4440  C CB  . PHE A 294 ? 0.6666 0.7626 0.6959 -0.0606 -0.1255 0.1261  294 PHE A CB  
4441  C CG  . PHE A 294 ? 0.6685 0.7640 0.7010 -0.0688 -0.1261 0.1292  294 PHE A CG  
4442  C CD1 . PHE A 294 ? 0.6568 0.7580 0.6906 -0.0741 -0.1205 0.1322  294 PHE A CD1 
4443  C CD2 . PHE A 294 ? 0.7061 0.7953 0.7406 -0.0714 -0.1319 0.1287  294 PHE A CD2 
4444  C CE1 . PHE A 294 ? 0.6778 0.7782 0.7161 -0.0821 -0.1195 0.1352  294 PHE A CE1 
4445  C CE2 . PHE A 294 ? 0.7190 0.8079 0.7595 -0.0792 -0.1321 0.1309  294 PHE A CE2 
4446  C CZ  . PHE A 294 ? 0.7017 0.7960 0.7449 -0.0848 -0.1254 0.1345  294 PHE A CZ  
4456  N N   . ILE A 295 ? 0.6280 0.7349 0.6678 -0.0461 -0.1227 0.1190  295 ILE A N   
4457  C CA  . ILE A 295 ? 0.6356 0.7412 0.6754 -0.0391 -0.1200 0.1164  295 ILE A CA  
4458  C C   . ILE A 295 ? 0.6644 0.7570 0.6944 -0.0364 -0.1235 0.1159  295 ILE A C   
4459  O O   . ILE A 295 ? 0.7193 0.8093 0.7468 -0.0381 -0.1281 0.1169  295 ILE A O   
4460  C CB  . ILE A 295 ? 0.6349 0.7522 0.6872 -0.0365 -0.1169 0.1156  295 ILE A CB  
4461  C CG1 . ILE A 295 ? 0.6691 0.7999 0.7320 -0.0398 -0.1127 0.1148  295 ILE A CG1 
4462  C CG2 . ILE A 295 ? 0.5820 0.6969 0.6355 -0.0297 -0.1129 0.1133  295 ILE A CG2 
4463  C CD1 . ILE A 295 ? 0.6700 0.8131 0.7488 -0.0382 -0.1102 0.1137  295 ILE A CD1 
4475  N N   . GLY A 296 ? 0.6821 0.7671 0.7074 -0.0321 -0.1213 0.1136  296 GLY A N   
4476  C CA  . GLY A 296 ? 0.6805 0.7528 0.6965 -0.0295 -0.1227 0.1120  296 GLY A CA  
4477  C C   . GLY A 296 ? 0.7173 0.7889 0.7345 -0.0239 -0.1177 0.1105  296 GLY A C   
4478  O O   . GLY A 296 ? 0.7252 0.8025 0.7510 -0.0206 -0.1124 0.1090  296 GLY A O   
4482  N N   . ALA A 297 ? 0.7091 0.7730 0.7169 -0.0229 -0.1194 0.1109  297 ALA A N   
4483  C CA  . ALA A 297 ? 0.6583 0.7181 0.6630 -0.0179 -0.1141 0.1106  297 ALA A CA  
4484  C C   . ALA A 297 ? 0.7029 0.7482 0.6934 -0.0171 -0.1139 0.1079  297 ALA A C   
4485  O O   . ALA A 297 ? 0.7671 0.8065 0.7453 -0.0175 -0.1173 0.1089  297 ALA A O   
4486  C CB  . ALA A 297 ? 0.6486 0.7139 0.6541 -0.0173 -0.1163 0.1146  297 ALA A CB  
4492  N N   . PRO A 298 ? 0.7004 0.7396 0.6924 -0.0157 -0.1103 0.1037  298 PRO A N   
4493  C CA  . PRO A 298 ? 0.7018 0.7276 0.6824 -0.0158 -0.1105 0.0999  298 PRO A CA  
4494  C C   . PRO A 298 ? 0.7031 0.7204 0.6720 -0.0127 -0.1047 0.0990  298 PRO A C   
4495  O O   . PRO A 298 ? 0.7030 0.7092 0.6601 -0.0132 -0.1047 0.0953  298 PRO A O   
4496  C CB  . PRO A 298 ? 0.7216 0.7449 0.7116 -0.0141 -0.1077 0.0956  298 PRO A CB  
4497  C CG  . PRO A 298 ? 0.7124 0.7477 0.7152 -0.0144 -0.1087 0.0978  298 PRO A CG  
4498  C CD  . PRO A 298 ? 0.6825 0.7270 0.6878 -0.0138 -0.1066 0.1015  298 PRO A CD  
4506  N N   . LEU A 299 ? 0.7094 0.7306 0.6804 -0.0097 -0.0995 0.1023  299 LEU A N   
4507  C CA  . LEU A 299 ? 0.7309 0.7426 0.6887 -0.0068 -0.0929 0.1029  299 LEU A CA  
4508  C C   . LEU A 299 ? 0.7262 0.7387 0.6720 -0.0071 -0.0985 0.1088  299 LEU A C   
4509  O O   . LEU A 299 ? 0.7328 0.7375 0.6654 -0.0044 -0.0937 0.1113  299 LEU A O   
4510  C CB  . LEU A 299 ? 0.7549 0.7676 0.7243 -0.0028 -0.0815 0.1024  299 LEU A CB  
4511  C CG  . LEU A 299 ? 0.7651 0.7795 0.7509 -0.0018 -0.0773 0.0962  299 LEU A CG  
4512  C CD1 . LEU A 299 ? 0.7527 0.7680 0.7514 0.0021  -0.0658 0.0949  299 LEU A CD1 
4513  C CD2 . LEU A 299 ? 0.7717 0.7754 0.7503 -0.0028 -0.0771 0.0901  299 LEU A CD2 
4525  N N   . PHE A 300 ? 0.7208 0.7422 0.6709 -0.0101 -0.1086 0.1112  300 PHE A N   
4526  C CA  . PHE A 300 ? 0.7664 0.7894 0.7081 -0.0101 -0.1160 0.1161  300 PHE A CA  
4527  C C   . PHE A 300 ? 0.7757 0.7858 0.6932 -0.0102 -0.1193 0.1144  300 PHE A C   
4528  O O   . PHE A 300 ? 0.7929 0.7971 0.7040 -0.0130 -0.1217 0.1089  300 PHE A O   
4529  C CB  . PHE A 300 ? 0.7217 0.7568 0.6756 -0.0142 -0.1257 0.1170  300 PHE A CB  
4530  C CG  . PHE A 300 ? 0.6915 0.7298 0.6409 -0.0143 -0.1350 0.1209  300 PHE A CG  
4531  C CD1 . PHE A 300 ? 0.7410 0.7733 0.6761 -0.0165 -0.1442 0.1189  300 PHE A CD1 
4532  C CD2 . PHE A 300 ? 0.7184 0.7659 0.6796 -0.0119 -0.1353 0.1259  300 PHE A CD2 
4533  C CE1 . PHE A 300 ? 0.7453 0.7810 0.6775 -0.0162 -0.1545 0.1218  300 PHE A CE1 
4534  C CE2 . PHE A 300 ? 0.7120 0.7626 0.6712 -0.0114 -0.1451 0.1293  300 PHE A CE2 
4535  C CZ  . PHE A 300 ? 0.7319 0.7766 0.6763 -0.0135 -0.1552 0.1273  300 PHE A CZ  
4545  N N   . MET A 301 ? 0.7710 0.7761 0.6743 -0.0071 -0.1197 0.1192  301 MET A N   
4546  C CA  . MET A 301 ? 0.8321 0.8242 0.7085 -0.0066 -0.1224 0.1179  301 MET A CA  
4547  C C   . MET A 301 ? 0.8875 0.8834 0.7574 -0.0079 -0.1375 0.1200  301 MET A C   
4548  O O   . MET A 301 ? 0.8693 0.8726 0.7466 -0.0060 -0.1424 0.1263  301 MET A O   
4549  C CB  . MET A 301 ? 0.8759 0.8573 0.7367 -0.0021 -0.1122 0.1222  301 MET A CB  
4550  C CG  . MET A 301 ? 0.8618 0.8374 0.7277 -0.0010 -0.0967 0.1183  301 MET A CG  
4551  S SD  . MET A 301 ? 0.8580 0.8199 0.7058 0.0035  -0.0826 0.1237  301 MET A SD  
4552  C CE  . MET A 301 ? 0.8470 0.8193 0.7126 0.0067  -0.0842 0.1338  301 MET A CE  
4562  N N   . ASP A 302 ? 0.9647 0.9559 0.8233 -0.0111 -0.1451 0.1141  302 ASP A N   
4563  C CA  . ASP A 302 ? 0.9794 0.9733 0.8317 -0.0125 -0.1603 0.1142  302 ASP A CA  
4564  C C   . ASP A 302 ? 0.9294 0.9104 0.7503 -0.0091 -0.1632 0.1154  302 ASP A C   
4565  O O   . ASP A 302 ? 0.9286 0.8973 0.7310 -0.0070 -0.1525 0.1146  302 ASP A O   
4566  C CB  . ASP A 302 ? 1.1092 1.1048 0.9676 -0.0181 -0.1674 0.1064  302 ASP A CB  
4567  C CG  . ASP A 302 ? 1.2631 1.2647 1.1230 -0.0203 -0.1835 0.1055  302 ASP A CG  
4568  O OD1 . ASP A 302 ? 1.3249 1.3308 1.1835 -0.0172 -0.1900 0.1112  302 ASP A OD1 
4569  O OD2 . ASP A 302 ? 1.3196 1.3215 1.1838 -0.0250 -0.1899 0.0989  302 ASP A OD2 
4574  N N   . ARG A 303 ? 0.9650 0.9490 0.7799 -0.0086 -0.1779 0.1172  303 ARG A N   
4575  C CA  . ARG A 303 ? 1.0480 1.0198 0.8305 -0.0055 -0.1841 0.1182  303 ARG A CA  
4576  C C   . ARG A 303 ? 1.0867 1.0546 0.8574 -0.0093 -0.1943 0.1082  303 ARG A C   
4577  O O   . ARG A 303 ? 1.0705 1.0487 0.8612 -0.0134 -0.2041 0.1037  303 ARG A O   
4578  C CB  . ARG A 303 ? 1.1297 1.1065 0.9125 -0.0015 -0.1957 0.1267  303 ARG A CB  
4579  C CG  . ARG A 303 ? 1.2676 1.2298 1.0139 0.0034  -0.1995 0.1313  303 ARG A CG  
4580  C CD  . ARG A 303 ? 1.3331 1.2842 1.0659 0.0072  -0.1823 0.1386  303 ARG A CD  
4581  N NE  . ARG A 303 ? 1.3074 1.2671 1.0639 0.0101  -0.1782 0.1478  303 ARG A NE  
4582  C CZ  . ARG A 303 ? 1.2489 1.2004 0.9983 0.0141  -0.1657 0.1561  303 ARG A CZ  
4583  N NH1 . ARG A 303 ? 1.2577 1.1919 0.9757 0.0156  -0.1554 0.1570  303 ARG A NH1 
4584  N NH2 . ARG A 303 ? 1.1989 1.1591 0.9732 0.0164  -0.1629 0.1632  303 ARG A NH2 
4598  N N   . GLY A 304 ? 1.1671 1.1199 0.9060 -0.0081 -0.1911 0.1041  304 GLY A N   
4599  C CA  . GLY A 304 ? 1.1958 1.1434 0.9223 -0.0115 -0.1990 0.0930  304 GLY A CA  
4600  C C   . GLY A 304 ? 1.2044 1.1480 0.9064 -0.0094 -0.2157 0.0923  304 GLY A C   
4601  O O   . GLY A 304 ? 1.1774 1.1200 0.8681 -0.0047 -0.2209 0.1014  304 GLY A O   
4605  N N   . SER A 305 ? 1.2197 1.1604 0.9140 -0.0129 -0.2249 0.0810  305 SER A N   
4606  C CA  . SER A 305 ? 1.2119 1.1486 0.8820 -0.0111 -0.2424 0.0779  305 SER A CA  
4607  C C   . SER A 305 ? 1.2119 1.1336 0.8408 -0.0053 -0.2382 0.0840  305 SER A C   
4608  O O   . SER A 305 ? 1.2104 1.1307 0.8224 -0.0012 -0.2520 0.0894  305 SER A O   
4609  C CB  . SER A 305 ? 1.2554 1.1887 0.9209 -0.0158 -0.2492 0.0629  305 SER A CB  
4610  O OG  . SER A 305 ? 1.3316 1.2587 0.9677 -0.0137 -0.2650 0.0584  305 SER A OG  
4616  N N   . ASP A 306 ? 1.2197 1.1294 0.8321 -0.0049 -0.2191 0.0834  306 ASP A N   
4617  C CA  . ASP A 306 ? 1.2147 1.1089 0.7884 -0.0001 -0.2111 0.0902  306 ASP A CA  
4618  C C   . ASP A 306 ? 1.1503 1.0469 0.7317 0.0045  -0.2055 0.1059  306 ASP A C   
4619  O O   . ASP A 306 ? 1.1262 1.0096 0.6769 0.0087  -0.1989 0.1138  306 ASP A O   
4620  C CB  . ASP A 306 ? 1.2656 1.1470 0.8237 -0.0017 -0.1907 0.0832  306 ASP A CB  
4621  C CG  . ASP A 306 ? 1.2730 1.1617 0.8667 -0.0044 -0.1752 0.0826  306 ASP A CG  
4622  O OD1 . ASP A 306 ? 1.2539 1.1566 0.8804 -0.0046 -0.1788 0.0889  306 ASP A OD1 
4623  O OD2 . ASP A 306 ? 1.3044 1.1848 0.8933 -0.0061 -0.1596 0.0754  306 ASP A OD2 
4628  N N   . GLY A 307 ? 1.1087 1.0211 0.7296 0.0036  -0.2074 0.1103  307 GLY A N   
4629  C CA  . GLY A 307 ? 1.1106 1.0264 0.7434 0.0076  -0.2015 0.1238  307 GLY A CA  
4630  C C   . GLY A 307 ? 1.1274 1.0391 0.7680 0.0076  -0.1784 0.1266  307 GLY A C   
4631  O O   . GLY A 307 ? 1.1359 1.0471 0.7814 0.0112  -0.1713 0.1376  307 GLY A O   
4635  N N   . LYS A 308 ? 1.1409 1.0497 0.7848 0.0037  -0.1669 0.1167  308 LYS A N   
4636  C CA  . LYS A 308 ? 1.1670 1.0725 0.8210 0.0037  -0.1456 0.1177  308 LYS A CA  
4637  C C   . LYS A 308 ? 1.1183 1.0399 0.8151 0.0013  -0.1434 0.1170  308 LYS A C   
4638  O O   . LYS A 308 ? 1.1000 1.0314 0.8151 -0.0025 -0.1530 0.1105  308 LYS A O   
4639  C CB  . LYS A 308 ? 1.2819 1.1754 0.9183 0.0012  -0.1339 0.1067  308 LYS A CB  
4640  C CG  . LYS A 308 ? 1.4204 1.2955 1.0180 0.0040  -0.1223 0.1098  308 LYS A CG  
4641  C CD  . LYS A 308 ? 1.5023 1.3674 1.0904 0.0014  -0.1069 0.0982  308 LYS A CD  
4642  C CE  . LYS A 308 ? 1.5847 1.4306 1.1302 0.0034  -0.0951 0.1001  308 LYS A CE  
4643  N NZ  . LYS A 308 ? 1.6095 1.4504 1.1506 0.0073  -0.0845 0.1146  308 LYS A NZ  
4657  N N   . LEU A 309 ? 1.1022 1.0258 0.8142 0.0034  -0.1305 0.1237  309 LEU A N   
4658  C CA  . LEU A 309 ? 1.0250 0.9621 0.7741 0.0014  -0.1260 0.1220  309 LEU A CA  
4659  C C   . LEU A 309 ? 0.9402 0.8743 0.6951 -0.0020 -0.1175 0.1112  309 LEU A C   
4660  O O   . LEU A 309 ? 0.9425 0.8640 0.6800 -0.0015 -0.1056 0.1072  309 LEU A O   
4661  C CB  . LEU A 309 ? 1.0063 0.9453 0.7694 0.0047  -0.1138 0.1302  309 LEU A CB  
4662  C CG  . LEU A 309 ? 0.9911 0.9379 0.7636 0.0078  -0.1220 0.1406  309 LEU A CG  
4663  C CD1 . LEU A 309 ? 0.9693 0.9146 0.7529 0.0110  -0.1073 0.1475  309 LEU A CD1 
4664  C CD2 . LEU A 309 ? 0.9609 0.9256 0.7624 0.0051  -0.1339 0.1387  309 LEU A CD2 
4676  N N   . GLN A 310 ? 0.8946 0.8401 0.6746 -0.0055 -0.1235 0.1066  310 GLN A N   
4677  C CA  . GLN A 310 ? 0.9135 0.8570 0.7034 -0.0084 -0.1172 0.0972  310 GLN A CA  
4678  C C   . GLN A 310 ? 0.8382 0.7950 0.6611 -0.0098 -0.1166 0.0984  310 GLN A C   
4679  O O   . GLN A 310 ? 0.8029 0.7709 0.6396 -0.0118 -0.1274 0.1009  310 GLN A O   
4680  C CB  . GLN A 310 ? 1.0260 0.9658 0.8054 -0.0121 -0.1276 0.0887  310 GLN A CB  
4681  C CG  . GLN A 310 ? 1.1446 1.0931 0.9270 -0.0140 -0.1453 0.0907  310 GLN A CG  
4682  C CD  . GLN A 310 ? 1.2608 1.2039 1.0307 -0.0173 -0.1551 0.0813  310 GLN A CD  
4683  O OE1 . GLN A 310 ? 1.3019 1.2332 1.0549 -0.0176 -0.1488 0.0737  310 GLN A OE1 
4684  N NE2 . GLN A 310 ? 1.3024 1.2543 1.0821 -0.0201 -0.1701 0.0809  310 GLN A NE2 
4693  N N   . GLU A 311 ? 0.8068 0.7622 0.6420 -0.0087 -0.1038 0.0961  311 GLU A N   
4694  C CA  . GLU A 311 ? 0.7820 0.7489 0.6459 -0.0095 -0.1029 0.0965  311 GLU A CA  
4695  C C   . GLU A 311 ? 0.7801 0.7491 0.6527 -0.0137 -0.1109 0.0906  311 GLU A C   
4696  O O   . GLU A 311 ? 0.7697 0.7300 0.6388 -0.0146 -0.1073 0.0832  311 GLU A O   
4697  C CB  . GLU A 311 ? 0.8077 0.7719 0.6822 -0.0069 -0.0882 0.0945  311 GLU A CB  
4698  C CG  . GLU A 311 ? 0.8395 0.8151 0.7418 -0.0070 -0.0877 0.0945  311 GLU A CG  
4699  C CD  . GLU A 311 ? 0.9002 0.8733 0.8148 -0.0041 -0.0743 0.0911  311 GLU A CD  
4700  O OE1 . GLU A 311 ? 0.9490 0.9188 0.8599 -0.0013 -0.0647 0.0943  311 GLU A OE1 
4701  O OE2 . GLU A 311 ? 0.9158 0.8897 0.8445 -0.0047 -0.0735 0.0852  311 GLU A OE2 
4708  N N   . VAL A 312 ? 0.7671 0.7472 0.6524 -0.0164 -0.1209 0.0939  312 VAL A N   
4709  C CA  . VAL A 312 ? 0.7732 0.7551 0.6677 -0.0209 -0.1284 0.0899  312 VAL A CA  
4710  C C   . VAL A 312 ? 0.7713 0.7651 0.6884 -0.0226 -0.1298 0.0934  312 VAL A C   
4711  O O   . VAL A 312 ? 0.7762 0.7699 0.7019 -0.0259 -0.1335 0.0910  312 VAL A O   
4712  C CB  . VAL A 312 ? 0.8269 0.8084 0.7111 -0.0241 -0.1406 0.0887  312 VAL A CB  
4713  C CG1 . VAL A 312 ? 0.8560 0.8246 0.7152 -0.0227 -0.1398 0.0837  312 VAL A CG1 
4714  C CG2 . VAL A 312 ? 0.8221 0.8148 0.7109 -0.0239 -0.1474 0.0957  312 VAL A CG2 
4724  N N   . GLY A 313 ? 0.7582 0.7614 0.6844 -0.0204 -0.1268 0.0990  313 GLY A N   
4725  C CA  . GLY A 313 ? 0.7352 0.7501 0.6804 -0.0221 -0.1280 0.1018  313 GLY A CA  
4726  C C   . GLY A 313 ? 0.7301 0.7544 0.6806 -0.0260 -0.1372 0.1051  313 GLY A C   
4727  O O   . GLY A 313 ? 0.7538 0.7751 0.6954 -0.0282 -0.1448 0.1040  313 GLY A O   
4731  N N   . GLN A 314 ? 0.7358 0.7720 0.7018 -0.0270 -0.1363 0.1084  314 GLN A N   
4732  C CA  . GLN A 314 ? 0.7246 0.7713 0.6996 -0.0309 -0.1432 0.1111  314 GLN A CA  
4733  C C   . GLN A 314 ? 0.7724 0.8292 0.7628 -0.0333 -0.1402 0.1128  314 GLN A C   
4734  O O   . GLN A 314 ? 0.8276 0.8874 0.8234 -0.0302 -0.1334 0.1131  314 GLN A O   
4735  C CB  . GLN A 314 ? 0.7173 0.7695 0.6921 -0.0279 -0.1451 0.1145  314 GLN A CB  
4736  C CG  . GLN A 314 ? 0.7439 0.8086 0.7324 -0.0313 -0.1518 0.1165  314 GLN A CG  
4737  C CD  . GLN A 314 ? 0.7683 0.8373 0.7574 -0.0276 -0.1553 0.1199  314 GLN A CD  
4738  O OE1 . GLN A 314 ? 0.7584 0.8356 0.7592 -0.0249 -0.1507 0.1227  314 GLN A OE1 
4739  N NE2 . GLN A 314 ? 0.8047 0.8679 0.7814 -0.0271 -0.1640 0.1194  314 GLN A NE2 
4748  N N   . VAL A 315 ? 0.7543 0.8158 0.7516 -0.0390 -0.1451 0.1135  315 VAL A N   
4749  C CA  . VAL A 315 ? 0.7075 0.7784 0.7171 -0.0422 -0.1421 0.1155  315 VAL A CA  
4750  C C   . VAL A 315 ? 0.7123 0.7958 0.7340 -0.0454 -0.1450 0.1172  315 VAL A C   
4751  O O   . VAL A 315 ? 0.7086 0.7916 0.7307 -0.0481 -0.1521 0.1164  315 VAL A O   
4752  C CB  . VAL A 315 ? 0.7254 0.7896 0.7331 -0.0469 -0.1435 0.1154  315 VAL A CB  
4753  C CG1 . VAL A 315 ? 0.7139 0.7872 0.7311 -0.0510 -0.1404 0.1184  315 VAL A CG1 
4754  C CG2 . VAL A 315 ? 0.7354 0.7880 0.7346 -0.0432 -0.1409 0.1132  315 VAL A CG2 
4764  N N   . SER A 316 ? 0.6987 0.7938 0.7318 -0.0448 -0.1399 0.1185  316 SER A N   
4765  C CA  . SER A 316 ? 0.6485 0.7569 0.6969 -0.0479 -0.1411 0.1193  316 SER A CA  
4766  C C   . SER A 316 ? 0.6387 0.7524 0.6942 -0.0545 -0.1378 0.1201  316 SER A C   
4767  O O   . SER A 316 ? 0.6431 0.7550 0.6942 -0.0546 -0.1325 0.1207  316 SER A O   
4768  C CB  . SER A 316 ? 0.6434 0.7615 0.7015 -0.0432 -0.1368 0.1197  316 SER A CB  
4769  O OG  . SER A 316 ? 0.6896 0.8166 0.7564 -0.0447 -0.1295 0.1191  316 SER A OG  
4775  N N   . VAL A 317 ? 0.6577 0.7778 0.7243 -0.0601 -0.1411 0.1200  317 VAL A N   
4776  C CA  . VAL A 317 ? 0.6795 0.8040 0.7531 -0.0674 -0.1369 0.1211  317 VAL A CA  
4777  C C   . VAL A 317 ? 0.6530 0.7939 0.7464 -0.0696 -0.1338 0.1200  317 VAL A C   
4778  O O   . VAL A 317 ? 0.6767 0.8232 0.7824 -0.0704 -0.1396 0.1184  317 VAL A O   
4779  C CB  . VAL A 317 ? 0.6749 0.7913 0.7470 -0.0734 -0.1423 0.1213  317 VAL A CB  
4780  C CG1 . VAL A 317 ? 0.7035 0.8232 0.7824 -0.0813 -0.1364 0.1236  317 VAL A CG1 
4781  C CG2 . VAL A 317 ? 0.6849 0.7850 0.7394 -0.0707 -0.1456 0.1213  317 VAL A CG2 
4791  N N   . SER A 318 ? 0.6550 0.8037 0.7521 -0.0704 -0.1250 0.1202  318 SER A N   
4792  C CA  . SER A 318 ? 0.7028 0.8677 0.8196 -0.0719 -0.1201 0.1179  318 SER A CA  
4793  C C   . SER A 318 ? 0.6933 0.8632 0.8150 -0.0803 -0.1124 0.1186  318 SER A C   
4794  O O   . SER A 318 ? 0.6424 0.8111 0.7538 -0.0812 -0.1052 0.1197  318 SER A O   
4795  C CB  . SER A 318 ? 0.7654 0.9361 0.8834 -0.0655 -0.1152 0.1163  318 SER A CB  
4796  O OG  . SER A 318 ? 0.8548 1.0190 0.9668 -0.0582 -0.1208 0.1166  318 SER A OG  
4802  N N   . LEU A 319 ? 0.7242 0.8994 0.8613 -0.0864 -0.1139 0.1177  319 LEU A N   
4803  C CA  . LEU A 319 ? 0.7564 0.9365 0.9005 -0.0953 -0.1050 0.1183  319 LEU A CA  
4804  C C   . LEU A 319 ? 0.7650 0.9611 0.9238 -0.0958 -0.0954 0.1148  319 LEU A C   
4805  O O   . LEU A 319 ? 0.7337 0.9414 0.9131 -0.0934 -0.0977 0.1107  319 LEU A O   
4806  C CB  . LEU A 319 ? 0.7428 0.9238 0.9024 -0.1018 -0.1094 0.1174  319 LEU A CB  
4807  C CG  . LEU A 319 ? 0.7849 0.9501 0.9314 -0.1054 -0.1141 0.1209  319 LEU A CG  
4808  C CD1 . LEU A 319 ? 0.8168 0.9687 0.9426 -0.0980 -0.1223 0.1222  319 LEU A CD1 
4809  C CD2 . LEU A 319 ? 0.7912 0.9593 0.9573 -0.1107 -0.1203 0.1179  319 LEU A CD2 
4821  N N   . GLN A 320 ? 0.7910 0.9874 0.9391 -0.0989 -0.0851 0.1160  320 GLN A N   
4822  C CA  . GLN A 320 ? 0.8004 1.0120 0.9614 -0.1005 -0.0745 0.1116  320 GLN A CA  
4823  C C   . GLN A 320 ? 0.8878 1.1095 1.0713 -0.1091 -0.0684 0.1094  320 GLN A C   
4824  O O   . GLN A 320 ? 0.9432 1.1581 1.1252 -0.1160 -0.0681 0.1128  320 GLN A O   
4825  C CB  . GLN A 320 ? 0.7142 0.9223 0.8538 -0.1013 -0.0658 0.1132  320 GLN A CB  
4826  C CG  . GLN A 320 ? 0.6634 0.8869 0.8136 -0.1029 -0.0540 0.1074  320 GLN A CG  
4827  C CD  . GLN A 320 ? 0.6909 0.9106 0.8171 -0.1041 -0.0461 0.1086  320 GLN A CD  
4828  O OE1 . GLN A 320 ? 0.7027 0.9336 0.8332 -0.1059 -0.0358 0.1035  320 GLN A OE1 
4829  N NE2 . GLN A 320 ? 0.7289 0.9327 0.8297 -0.1028 -0.0513 0.1150  320 GLN A NE2 
4838  N N   . ARG A 321 ? 0.8662 1.1044 1.0733 -0.1088 -0.0631 0.1031  321 ARG A N   
4839  C CA  . ARG A 321 ? 0.8520 1.1022 1.0854 -0.1167 -0.0560 0.0993  321 ARG A CA  
4840  C C   . ARG A 321 ? 0.8228 1.0860 1.0631 -0.1194 -0.0409 0.0942  321 ARG A C   
4841  O O   . ARG A 321 ? 0.8172 1.0838 1.0513 -0.1132 -0.0392 0.0915  321 ARG A O   
4842  C CB  . ARG A 321 ? 0.8535 1.1125 1.1163 -0.1138 -0.0663 0.0952  321 ARG A CB  
4843  C CG  . ARG A 321 ? 0.9242 1.1706 1.1774 -0.1096 -0.0822 0.0991  321 ARG A CG  
4844  C CD  . ARG A 321 ? 0.9820 1.2363 1.2637 -0.1094 -0.0922 0.0953  321 ARG A CD  
4845  N NE  . ARG A 321 ? 1.0096 1.2782 1.3144 -0.1039 -0.0931 0.0902  321 ARG A NE  
4846  C CZ  . ARG A 321 ? 1.0006 1.2789 1.3343 -0.1026 -0.1016 0.0861  321 ARG A CZ  
4847  N NH1 . ARG A 321 ? 1.0087 1.2988 1.3631 -0.0971 -0.1022 0.0821  321 ARG A NH1 
4848  N NH2 . ARG A 321 ? 0.9853 1.2614 1.3286 -0.1067 -0.1102 0.0855  321 ARG A NH2 
4862  N N   . ALA A 322 ? 0.8374 1.1077 1.0914 -0.1290 -0.0293 0.0922  322 ALA A N   
4863  C CA  . ALA A 322 ? 0.8846 1.1667 1.1433 -0.1328 -0.0131 0.0868  322 ALA A CA  
4864  C C   . ALA A 322 ? 0.8945 1.1925 1.1783 -0.1264 -0.0135 0.0781  322 ALA A C   
4865  O O   . ALA A 322 ? 0.8790 1.1839 1.1585 -0.1251 -0.0038 0.0732  322 ALA A O   
4866  C CB  . ALA A 322 ? 0.9032 1.1911 1.1778 -0.1445 -0.0001 0.0855  322 ALA A CB  
4872  N N   . SER A 323 ? 0.9066 1.2100 1.2166 -0.1220 -0.0251 0.0759  323 SER A N   
4873  C CA  . SER A 323 ? 0.9233 1.2403 1.2592 -0.1153 -0.0271 0.0687  323 SER A CA  
4874  C C   . SER A 323 ? 0.9508 1.2625 1.2684 -0.1056 -0.0321 0.0698  323 SER A C   
4875  O O   . SER A 323 ? 0.9233 1.2447 1.2611 -0.0996 -0.0333 0.0644  323 SER A O   
4876  C CB  . SER A 323 ? 0.9477 1.2692 1.3124 -0.1125 -0.0408 0.0677  323 SER A CB  
4877  O OG  . SER A 323 ? 0.9568 1.2632 1.3021 -0.1076 -0.0563 0.0750  323 SER A OG  
4883  N N   . GLY A 324 ? 1.0245 1.3210 1.3072 -0.1039 -0.0349 0.0762  324 GLY A N   
4884  C CA  . GLY A 324 ? 1.0480 1.3392 1.3148 -0.0952 -0.0390 0.0767  324 GLY A CA  
4885  C C   . GLY A 324 ? 1.0562 1.3379 1.3201 -0.0872 -0.0544 0.0814  324 GLY A C   
4886  O O   . GLY A 324 ? 1.0560 1.3301 1.3032 -0.0806 -0.0578 0.0831  324 GLY A O   
4890  N N   . ASP A 325 ? 1.0666 1.3485 1.3460 -0.0876 -0.0636 0.0831  325 ASP A N   
4891  C CA  . ASP A 325 ? 1.0780 1.3501 1.3516 -0.0805 -0.0782 0.0878  325 ASP A CA  
4892  C C   . ASP A 325 ? 1.0684 1.3230 1.3111 -0.0816 -0.0831 0.0944  325 ASP A C   
4893  O O   . ASP A 325 ? 1.1364 1.3863 1.3629 -0.0873 -0.0761 0.0961  325 ASP A O   
4894  C CB  . ASP A 325 ? 1.1098 1.3882 1.4096 -0.0805 -0.0875 0.0866  325 ASP A CB  
4895  C CG  . ASP A 325 ? 1.1796 1.4744 1.5126 -0.0779 -0.0847 0.0803  325 ASP A CG  
4896  O OD1 . ASP A 325 ? 1.2175 1.5177 1.5521 -0.0751 -0.0761 0.0768  325 ASP A OD1 
4897  O OD2 . ASP A 325 ? 1.2127 1.5150 1.5716 -0.0783 -0.0916 0.0782  325 ASP A OD2 
4902  N N   . PHE A 326 ? 0.9545 1.1990 1.1886 -0.0759 -0.0953 0.0982  326 PHE A N   
4903  C CA  . PHE A 326 ? 0.8411 1.0692 1.0496 -0.0764 -0.1012 0.1034  326 PHE A CA  
4904  C C   . PHE A 326 ? 0.7313 0.9551 0.9451 -0.0754 -0.1142 0.1049  326 PHE A C   
4905  O O   . PHE A 326 ? 0.6475 0.8763 0.8755 -0.0703 -0.1212 0.1038  326 PHE A O   
4906  C CB  . PHE A 326 ? 0.8207 1.0383 1.0070 -0.0696 -0.1019 0.1058  326 PHE A CB  
4907  C CG  . PHE A 326 ? 0.7748 0.9925 0.9487 -0.0712 -0.0917 0.1048  326 PHE A CG  
4908  C CD1 . PHE A 326 ? 0.7466 0.9746 0.9297 -0.0684 -0.0843 0.1002  326 PHE A CD1 
4909  C CD2 . PHE A 326 ? 0.7030 0.9100 0.8560 -0.0753 -0.0903 0.1083  326 PHE A CD2 
4910  C CE1 . PHE A 326 ? 0.7134 0.9416 0.8835 -0.0696 -0.0761 0.0985  326 PHE A CE1 
4911  C CE2 . PHE A 326 ? 0.6383 0.8449 0.7781 -0.0763 -0.0826 0.1078  326 PHE A CE2 
4912  C CZ  . PHE A 326 ? 0.6649 0.8823 0.8124 -0.0734 -0.0757 0.1026  326 PHE A CZ  
4922  N N   . GLN A 327 ? 0.6853 0.8994 0.8875 -0.0802 -0.1178 0.1073  327 GLN A N   
4923  C CA  . GLN A 327 ? 0.6819 0.8903 0.8857 -0.0799 -0.1306 0.1077  327 GLN A CA  
4924  C C   . GLN A 327 ? 0.7041 0.8952 0.8795 -0.0759 -0.1361 0.1113  327 GLN A C   
4925  O O   . GLN A 327 ? 0.7208 0.9023 0.8810 -0.0799 -0.1331 0.1133  327 GLN A O   
4926  C CB  . GLN A 327 ? 0.7641 0.9757 0.9813 -0.0892 -0.1300 0.1060  327 GLN A CB  
4927  C CG  . GLN A 327 ? 0.8839 1.0934 1.1095 -0.0893 -0.1438 0.1042  327 GLN A CG  
4928  C CD  . GLN A 327 ? 0.9787 1.1962 1.2281 -0.0985 -0.1422 0.1007  327 GLN A CD  
4929  O OE1 . GLN A 327 ? 1.0266 1.2379 1.2700 -0.1058 -0.1362 0.1023  327 GLN A OE1 
4930  N NE2 . GLN A 327 ? 0.9927 1.2238 1.2710 -0.0982 -0.1473 0.0960  327 GLN A NE2 
4939  N N   . THR A 328 ? 0.6806 0.8672 0.8491 -0.0680 -0.1437 0.1122  328 THR A N   
4940  C CA  . THR A 328 ? 0.6538 0.8250 0.7963 -0.0633 -0.1462 0.1149  328 THR A CA  
4941  C C   . THR A 328 ? 0.6003 0.7616 0.7332 -0.0628 -0.1581 0.1148  328 THR A C   
4942  O O   . THR A 328 ? 0.6080 0.7743 0.7528 -0.0622 -0.1672 0.1132  328 THR A O   
4943  C CB  . THR A 328 ? 0.7188 0.8900 0.8574 -0.0550 -0.1443 0.1161  328 THR A CB  
4944  O OG1 . THR A 328 ? 0.7230 0.9047 0.8727 -0.0555 -0.1339 0.1147  328 THR A OG1 
4945  C CG2 . THR A 328 ? 0.7322 0.8880 0.8458 -0.0509 -0.1442 0.1182  328 THR A CG2 
4953  N N   . THR A 329 ? 0.6762 0.8234 0.7880 -0.0629 -0.1584 0.1159  329 THR A N   
4954  C CA  . THR A 329 ? 0.8116 0.9475 0.9104 -0.0620 -0.1686 0.1148  329 THR A CA  
4955  C C   . THR A 329 ? 0.7768 0.8984 0.8518 -0.0576 -0.1660 0.1161  329 THR A C   
4956  O O   . THR A 329 ? 0.7828 0.9016 0.8525 -0.0580 -0.1576 0.1174  329 THR A O   
4957  C CB  . THR A 329 ? 1.0058 1.1399 1.1106 -0.0699 -0.1720 0.1124  329 THR A CB  
4958  O OG1 . THR A 329 ? 1.0835 1.2317 1.2137 -0.0743 -0.1737 0.1104  329 THR A OG1 
4959  C CG2 . THR A 329 ? 1.0841 1.2066 1.1754 -0.0688 -0.1828 0.1098  329 THR A CG2 
4967  N N   . LYS A 330 ? 0.7906 0.9029 0.8511 -0.0532 -0.1733 0.1154  330 LYS A N   
4968  C CA  . LYS A 330 ? 0.7943 0.8931 0.8335 -0.0488 -0.1703 0.1158  330 LYS A CA  
4969  C C   . LYS A 330 ? 0.8087 0.8956 0.8364 -0.0523 -0.1742 0.1126  330 LYS A C   
4970  O O   . LYS A 330 ? 0.8542 0.9421 0.8879 -0.0569 -0.1817 0.1100  330 LYS A O   
4971  C CB  . LYS A 330 ? 0.8000 0.8947 0.8280 -0.0418 -0.1738 0.1172  330 LYS A CB  
4972  C CG  . LYS A 330 ? 0.7934 0.8994 0.8355 -0.0381 -0.1719 0.1203  330 LYS A CG  
4973  C CD  . LYS A 330 ? 0.8021 0.9113 0.8487 -0.0362 -0.1600 0.1217  330 LYS A CD  
4974  C CE  . LYS A 330 ? 0.8239 0.9453 0.8881 -0.0332 -0.1579 0.1237  330 LYS A CE  
4975  N NZ  . LYS A 330 ? 0.8963 1.0140 0.9550 -0.0273 -0.1643 0.1268  330 LYS A NZ  
4989  N N   . LEU A 331 ? 0.7827 0.8583 0.7959 -0.0500 -0.1691 0.1123  331 LEU A N   
4990  C CA  . LEU A 331 ? 0.7322 0.7957 0.7358 -0.0528 -0.1717 0.1089  331 LEU A CA  
4991  C C   . LEU A 331 ? 0.7493 0.8006 0.7346 -0.0472 -0.1682 0.1073  331 LEU A C   
4992  O O   . LEU A 331 ? 0.8189 0.8687 0.8033 -0.0444 -0.1601 0.1087  331 LEU A O   
4993  C CB  . LEU A 331 ? 0.7157 0.7790 0.7274 -0.0580 -0.1672 0.1102  331 LEU A CB  
4994  C CG  . LEU A 331 ? 0.7697 0.8249 0.7820 -0.0638 -0.1720 0.1074  331 LEU A CG  
4995  C CD1 . LEU A 331 ? 0.8335 0.8960 0.8580 -0.0687 -0.1797 0.1054  331 LEU A CD1 
4996  C CD2 . LEU A 331 ? 0.7607 0.8133 0.7776 -0.0677 -0.1663 0.1106  331 LEU A CD2 
5008  N N   . ASN A 332 ? 0.7221 0.7650 0.6934 -0.0457 -0.1740 0.1037  332 ASN A N   
5009  C CA  . ASN A 332 ? 0.7462 0.7779 0.6993 -0.0404 -0.1696 0.1019  332 ASN A CA  
5010  C C   . ASN A 332 ? 0.7433 0.7629 0.6901 -0.0420 -0.1673 0.0970  332 ASN A C   
5011  O O   . ASN A 332 ? 0.7487 0.7663 0.7012 -0.0470 -0.1721 0.0943  332 ASN A O   
5012  C CB  . ASN A 332 ? 0.7526 0.7804 0.6901 -0.0375 -0.1763 0.1007  332 ASN A CB  
5013  C CG  . ASN A 332 ? 0.8020 0.8388 0.7435 -0.0338 -0.1771 0.1064  332 ASN A CG  
5014  O OD1 . ASN A 332 ? 0.7920 0.8398 0.7510 -0.0343 -0.1736 0.1101  332 ASN A OD1 
5015  N ND2 . ASN A 332 ? 0.8756 0.9070 0.8003 -0.0299 -0.1818 0.1071  332 ASN A ND2 
5022  N N   . GLY A 333 ? 0.7345 0.7459 0.6713 -0.0375 -0.1596 0.0955  333 GLY A N   
5023  C CA  . GLY A 333 ? 0.7455 0.7450 0.6774 -0.0380 -0.1570 0.0900  333 GLY A CA  
5024  C C   . GLY A 333 ? 0.8088 0.7987 0.7258 -0.0391 -0.1627 0.0834  333 GLY A C   
5025  O O   . GLY A 333 ? 0.8561 0.8477 0.7635 -0.0388 -0.1691 0.0833  333 GLY A O   
5029  N N   . PHE A 334 ? 0.8300 0.8093 0.7452 -0.0402 -0.1610 0.0773  334 PHE A N   
5030  C CA  . PHE A 334 ? 0.8503 0.8200 0.7531 -0.0419 -0.1661 0.0692  334 PHE A CA  
5031  C C   . PHE A 334 ? 0.8173 0.7753 0.7034 -0.0379 -0.1584 0.0631  334 PHE A C   
5032  O O   . PHE A 334 ? 0.8239 0.7751 0.6924 -0.0378 -0.1617 0.0571  334 PHE A O   
5033  C CB  . PHE A 334 ? 0.8953 0.8613 0.8111 -0.0472 -0.1708 0.0655  334 PHE A CB  
5034  C CG  . PHE A 334 ? 0.9193 0.8957 0.8526 -0.0519 -0.1762 0.0715  334 PHE A CG  
5035  C CD1 . PHE A 334 ? 0.8988 0.8807 0.8346 -0.0558 -0.1856 0.0704  334 PHE A CD1 
5036  C CD2 . PHE A 334 ? 0.9182 0.8987 0.8652 -0.0525 -0.1716 0.0778  334 PHE A CD2 
5037  C CE1 . PHE A 334 ? 0.8988 0.8903 0.8524 -0.0606 -0.1889 0.0754  334 PHE A CE1 
5038  C CE2 . PHE A 334 ? 0.9193 0.9088 0.8807 -0.0573 -0.1748 0.0833  334 PHE A CE2 
5039  C CZ  . PHE A 334 ? 0.9191 0.9141 0.8845 -0.0616 -0.1827 0.0821  334 PHE A CZ  
5049  N N   . GLU A 335 ? 0.7821 0.7376 0.6733 -0.0347 -0.1481 0.0638  335 GLU A N   
5050  C CA  . GLU A 335 ? 0.8437 0.7883 0.7227 -0.0312 -0.1386 0.0574  335 GLU A CA  
5051  C C   . GLU A 335 ? 0.8636 0.8111 0.7385 -0.0264 -0.1288 0.0626  335 GLU A C   
5052  O O   . GLU A 335 ? 0.8854 0.8421 0.7745 -0.0253 -0.1272 0.0693  335 GLU A O   
5053  C CB  . GLU A 335 ? 0.8830 0.8209 0.7757 -0.0315 -0.1345 0.0518  335 GLU A CB  
5054  C CG  . GLU A 335 ? 0.9560 0.8878 0.8525 -0.0359 -0.1423 0.0453  335 GLU A CG  
5055  C CD  . GLU A 335 ? 1.0373 0.9638 0.9519 -0.0360 -0.1401 0.0426  335 GLU A CD  
5056  O OE1 . GLU A 335 ? 1.0467 0.9793 0.9762 -0.0353 -0.1398 0.0496  335 GLU A OE1 
5057  O OE2 . GLU A 335 ? 1.0975 1.0134 1.0115 -0.0364 -0.1388 0.0332  335 GLU A OE2 
5064  N N   . VAL A 336 ? 0.8458 0.7846 0.7009 -0.0238 -0.1217 0.0591  336 VAL A N   
5065  C CA  . VAL A 336 ? 0.8726 0.8121 0.7234 -0.0195 -0.1111 0.0639  336 VAL A CA  
5066  C C   . VAL A 336 ? 0.8599 0.7994 0.7299 -0.0174 -0.1008 0.0619  336 VAL A C   
5067  O O   . VAL A 336 ? 0.8769 0.8099 0.7535 -0.0180 -0.0981 0.0540  336 VAL A O   
5068  C CB  . VAL A 336 ? 0.9284 0.8566 0.7509 -0.0176 -0.1051 0.0609  336 VAL A CB  
5069  C CG1 . VAL A 336 ? 0.9266 0.8547 0.7447 -0.0136 -0.0939 0.0676  336 VAL A CG1 
5070  C CG2 . VAL A 336 ? 0.9969 0.9245 0.7999 -0.0194 -0.1178 0.0615  336 VAL A CG2 
5080  N N   . PHE A 337 ? 0.8145 0.7617 0.6953 -0.0148 -0.0957 0.0684  337 PHE A N   
5081  C CA  . PHE A 337 ? 0.8054 0.7541 0.7054 -0.0122 -0.0864 0.0665  337 PHE A CA  
5082  C C   . PHE A 337 ? 0.8224 0.7748 0.7426 -0.0138 -0.0926 0.0642  337 PHE A C   
5083  O O   . PHE A 337 ? 0.8168 0.7698 0.7536 -0.0114 -0.0871 0.0614  337 PHE A O   
5084  C CB  . PHE A 337 ? 0.8008 0.7381 0.6943 -0.0100 -0.0730 0.0591  337 PHE A CB  
5085  C CG  . PHE A 337 ? 0.8594 0.7919 0.7339 -0.0079 -0.0639 0.0627  337 PHE A CG  
5086  C CD1 . PHE A 337 ? 0.8600 0.8000 0.7396 -0.0058 -0.0614 0.0713  337 PHE A CD1 
5087  C CD2 . PHE A 337 ? 0.9031 0.8231 0.7540 -0.0082 -0.0575 0.0577  337 PHE A CD2 
5088  C CE1 . PHE A 337 ? 0.8765 0.8106 0.7388 -0.0038 -0.0530 0.0759  337 PHE A CE1 
5089  C CE2 . PHE A 337 ? 0.9074 0.8214 0.7379 -0.0063 -0.0488 0.0624  337 PHE A CE2 
5090  C CZ  . PHE A 337 ? 0.8929 0.8136 0.7295 -0.0040 -0.0467 0.0720  337 PHE A CZ  
5100  N N   . ALA A 338 ? 0.8437 0.7981 0.7632 -0.0177 -0.1042 0.0655  338 ALA A N   
5101  C CA  . ALA A 338 ? 0.8398 0.7962 0.7764 -0.0194 -0.1101 0.0651  338 ALA A CA  
5102  C C   . ALA A 338 ? 0.7860 0.7545 0.7369 -0.0186 -0.1117 0.0721  338 ALA A C   
5103  O O   . ALA A 338 ? 0.7471 0.7168 0.7115 -0.0188 -0.1147 0.0723  338 ALA A O   
5104  C CB  . ALA A 338 ? 0.8386 0.7927 0.7708 -0.0243 -0.1208 0.0646  338 ALA A CB  
5110  N N   . ARG A 339 ? 0.7616 0.7383 0.7092 -0.0176 -0.1099 0.0777  339 ARG A N   
5111  C CA  . ARG A 339 ? 0.7818 0.7706 0.7426 -0.0168 -0.1104 0.0833  339 ARG A CA  
5112  C C   . ARG A 339 ? 0.7961 0.7907 0.7623 -0.0212 -0.1198 0.0873  339 ARG A C   
5113  O O   . ARG A 339 ? 0.7626 0.7623 0.7403 -0.0212 -0.1210 0.0891  339 ARG A O   
5114  C CB  . ARG A 339 ? 0.7216 0.7109 0.6967 -0.0128 -0.1037 0.0801  339 ARG A CB  
5115  C CG  . ARG A 339 ? 0.7302 0.7147 0.7026 -0.0090 -0.0924 0.0766  339 ARG A CG  
5116  C CD  . ARG A 339 ? 0.7693 0.7582 0.7598 -0.0050 -0.0857 0.0742  339 ARG A CD  
5117  N NE  . ARG A 339 ? 0.8136 0.7978 0.8026 -0.0020 -0.0734 0.0714  339 ARG A NE  
5118  C CZ  . ARG A 339 ? 0.7968 0.7826 0.8023 0.0015  -0.0652 0.0673  339 ARG A CZ  
5119  N NH1 . ARG A 339 ? 0.7717 0.7642 0.7958 0.0030  -0.0694 0.0651  339 ARG A NH1 
5120  N NH2 . ARG A 339 ? 0.8221 0.8026 0.8256 0.0035  -0.0527 0.0654  339 ARG A NH2 
5134  N N   . PHE A 340 ? 0.8148 0.8083 0.7724 -0.0252 -0.1265 0.0883  340 PHE A N   
5135  C CA  . PHE A 340 ? 0.7950 0.7949 0.7583 -0.0301 -0.1340 0.0927  340 PHE A CA  
5136  C C   . PHE A 340 ? 0.7606 0.7739 0.7333 -0.0296 -0.1324 0.0982  340 PHE A C   
5137  O O   . PHE A 340 ? 0.7483 0.7678 0.7198 -0.0274 -0.1296 0.1001  340 PHE A O   
5138  C CB  . PHE A 340 ? 0.8063 0.8054 0.7608 -0.0337 -0.1407 0.0924  340 PHE A CB  
5139  C CG  . PHE A 340 ? 0.8025 0.8090 0.7652 -0.0393 -0.1474 0.0963  340 PHE A CG  
5140  C CD1 . PHE A 340 ? 0.7997 0.8000 0.7658 -0.0438 -0.1521 0.0950  340 PHE A CD1 
5141  C CD2 . PHE A 340 ? 0.7854 0.8044 0.7535 -0.0402 -0.1484 0.1011  340 PHE A CD2 
5142  C CE1 . PHE A 340 ? 0.7844 0.7909 0.7589 -0.0495 -0.1568 0.0988  340 PHE A CE1 
5143  C CE2 . PHE A 340 ? 0.7666 0.7926 0.7439 -0.0457 -0.1532 0.1040  340 PHE A CE2 
5144  C CZ  . PHE A 340 ? 0.7542 0.7738 0.7343 -0.0506 -0.1569 0.1031  340 PHE A CZ  
5154  N N   . GLY A 341 ? 0.7386 0.7556 0.7199 -0.0317 -0.1342 0.1008  341 GLY A N   
5155  C CA  . GLY A 341 ? 0.7080 0.7375 0.6975 -0.0317 -0.1324 0.1049  341 GLY A CA  
5156  C C   . GLY A 341 ? 0.7510 0.7825 0.7472 -0.0274 -0.1278 0.1036  341 GLY A C   
5157  O O   . GLY A 341 ? 0.7310 0.7732 0.7337 -0.0270 -0.1258 0.1057  341 GLY A O   
5161  N N   . SER A 342 ? 0.7387 0.7608 0.7349 -0.0240 -0.1260 0.0991  342 SER A N   
5162  C CA  . SER A 342 ? 0.6502 0.6745 0.6553 -0.0195 -0.1227 0.0967  342 SER A CA  
5163  C C   . SER A 342 ? 0.6430 0.6712 0.6514 -0.0213 -0.1274 0.1001  342 SER A C   
5164  O O   . SER A 342 ? 0.6640 0.6992 0.6791 -0.0184 -0.1257 0.0992  342 SER A O   
5165  C CB  . SER A 342 ? 0.6494 0.6626 0.6564 -0.0158 -0.1204 0.0906  342 SER A CB  
5166  O OG  . SER A 342 ? 0.6783 0.6876 0.6803 -0.0141 -0.1143 0.0875  342 SER A OG  
5172  N N   . ALA A 343 ? 0.7048 0.7279 0.7081 -0.0260 -0.1330 0.1037  343 ALA A N   
5173  C CA  . ALA A 343 ? 0.7093 0.7339 0.7123 -0.0283 -0.1371 0.1083  343 ALA A CA  
5174  C C   . ALA A 343 ? 0.7096 0.7358 0.7080 -0.0354 -0.1394 0.1139  343 ALA A C   
5175  O O   . ALA A 343 ? 0.7332 0.7530 0.7290 -0.0384 -0.1415 0.1135  343 ALA A O   
5176  C CB  . ALA A 343 ? 0.6670 0.6796 0.6708 -0.0261 -0.1418 0.1073  343 ALA A CB  
5182  N N   . ILE A 344 ? 0.6991 0.7340 0.6972 -0.0383 -0.1387 0.1183  344 ILE A N   
5183  C CA  . ILE A 344 ? 0.6988 0.7370 0.6952 -0.0455 -0.1392 0.1234  344 ILE A CA  
5184  C C   . ILE A 344 ? 0.7442 0.7802 0.7355 -0.0481 -0.1405 0.1290  344 ILE A C   
5185  O O   . ILE A 344 ? 0.7902 0.8338 0.7802 -0.0462 -0.1382 0.1293  344 ILE A O   
5186  C CB  . ILE A 344 ? 0.7545 0.8072 0.7562 -0.0469 -0.1349 0.1230  344 ILE A CB  
5187  C CG1 . ILE A 344 ? 0.7551 0.8086 0.7593 -0.0432 -0.1341 0.1185  344 ILE A CG1 
5188  C CG2 . ILE A 344 ? 0.7852 0.8413 0.7886 -0.0546 -0.1353 0.1271  344 ILE A CG2 
5189  C CD1 . ILE A 344 ? 0.7308 0.7977 0.7417 -0.0429 -0.1306 0.1181  344 ILE A CD1 
5201  N N   . ALA A 345 ? 0.7562 0.7812 0.7439 -0.0526 -0.1441 0.1334  345 ALA A N   
5202  C CA  . ALA A 345 ? 0.7350 0.7540 0.7150 -0.0548 -0.1458 0.1402  345 ALA A CA  
5203  C C   . ALA A 345 ? 0.7764 0.7963 0.7550 -0.0636 -0.1433 0.1465  345 ALA A C   
5204  O O   . ALA A 345 ? 0.7778 0.7897 0.7599 -0.0680 -0.1454 0.1476  345 ALA A O   
5205  C CB  . ALA A 345 ? 0.7178 0.7202 0.6958 -0.0520 -0.1523 0.1409  345 ALA A CB  
5211  N N   . PRO A 346 ? 0.7950 0.8244 0.7698 -0.0668 -0.1382 0.1499  346 PRO A N   
5212  C CA  . PRO A 346 ? 0.7993 0.8275 0.7724 -0.0756 -0.1346 0.1567  346 PRO A CA  
5213  C C   . PRO A 346 ? 0.8241 0.8342 0.7893 -0.0778 -0.1390 0.1639  346 PRO A C   
5214  O O   . PRO A 346 ? 0.8374 0.8391 0.7933 -0.0728 -0.1435 0.1662  346 PRO A O   
5215  C CB  . PRO A 346 ? 0.7838 0.8236 0.7509 -0.0770 -0.1281 0.1584  346 PRO A CB  
5216  C CG  . PRO A 346 ? 0.7715 0.8234 0.7441 -0.0700 -0.1275 0.1505  346 PRO A CG  
5217  C CD  . PRO A 346 ? 0.7443 0.7867 0.7178 -0.0629 -0.1345 0.1468  346 PRO A CD  
5225  N N   . LEU A 347 ? 0.8286 0.8326 0.7992 -0.0850 -0.1382 0.1673  347 LEU A N   
5226  C CA  . LEU A 347 ? 0.8232 0.8088 0.7898 -0.0875 -0.1423 0.1739  347 LEU A CA  
5227  C C   . LEU A 347 ? 0.8013 0.7823 0.7607 -0.0958 -0.1367 0.1842  347 LEU A C   
5228  O O   . LEU A 347 ? 0.7922 0.7566 0.7477 -0.0984 -0.1394 0.1914  347 LEU A O   
5229  C CB  . LEU A 347 ? 0.8105 0.7895 0.7899 -0.0895 -0.1461 0.1693  347 LEU A CB  
5230  C CG  . LEU A 347 ? 0.8167 0.7962 0.8011 -0.0820 -0.1513 0.1596  347 LEU A CG  
5231  C CD1 . LEU A 347 ? 0.8169 0.7906 0.8118 -0.0854 -0.1543 0.1549  347 LEU A CD1 
5232  C CD2 . LEU A 347 ? 0.8313 0.8001 0.8092 -0.0746 -0.1566 0.1600  347 LEU A CD2 
5244  N N   . GLY A 348 ? 0.7937 0.7882 0.7518 -0.1000 -0.1282 0.1850  348 GLY A N   
5245  C CA  . GLY A 348 ? 0.7909 0.7817 0.7459 -0.1095 -0.1207 0.1936  348 GLY A CA  
5246  C C   . GLY A 348 ? 0.8335 0.8223 0.8070 -0.1165 -0.1199 0.1917  348 GLY A C   
5247  O O   . GLY A 348 ? 0.8446 0.8406 0.8324 -0.1145 -0.1236 0.1828  348 GLY A O   
5251  N N   . ASP A 349 ? 0.8881 0.8663 0.8609 -0.1249 -0.1152 0.2004  349 ASP A N   
5252  C CA  . ASP A 349 ? 0.8892 0.8640 0.8811 -0.1322 -0.1146 0.1989  349 ASP A CA  
5253  C C   . ASP A 349 ? 0.8847 0.8395 0.8764 -0.1300 -0.1235 0.2012  349 ASP A C   
5254  O O   . ASP A 349 ? 0.9401 0.8784 0.9246 -0.1337 -0.1224 0.2115  349 ASP A O   
5255  C CB  . ASP A 349 ? 0.9449 0.9200 0.9400 -0.1433 -0.1029 0.2061  349 ASP A CB  
5256  C CG  . ASP A 349 ? 0.9735 0.9513 0.9941 -0.1511 -0.1015 0.2014  349 ASP A CG  
5257  O OD1 . ASP A 349 ? 0.9688 0.9473 1.0019 -0.1476 -0.1106 0.1926  349 ASP A OD1 
5258  O OD2 . ASP A 349 ? 1.0007 0.9799 1.0288 -0.1608 -0.0912 0.2059  349 ASP A OD2 
5263  N N   . LEU A 350 ? 0.8477 0.8037 0.8477 -0.1239 -0.1320 0.1915  350 LEU A N   
5264  C CA  . LEU A 350 ? 0.8741 0.8123 0.8748 -0.1205 -0.1405 0.1915  350 LEU A CA  
5265  C C   . LEU A 350 ? 0.9290 0.8547 0.9424 -0.1292 -0.1395 0.1951  350 LEU A C   
5266  O O   . LEU A 350 ? 0.9292 0.8363 0.9381 -0.1299 -0.1418 0.2032  350 LEU A O   
5267  C CB  . LEU A 350 ? 0.8441 0.7877 0.8513 -0.1132 -0.1477 0.1790  350 LEU A CB  
5268  C CG  . LEU A 350 ? 0.8737 0.8008 0.8847 -0.1095 -0.1558 0.1760  350 LEU A CG  
5269  C CD1 . LEU A 350 ? 0.8790 0.7921 0.8773 -0.1042 -0.1592 0.1838  350 LEU A CD1 
5270  C CD2 . LEU A 350 ? 0.8556 0.7895 0.8710 -0.1031 -0.1605 0.1631  350 LEU A CD2 
5282  N N   . ASP A 351 ? 0.9840 0.9193 1.0148 -0.1357 -0.1366 0.1891  351 ASP A N   
5283  C CA  . ASP A 351 ? 1.0221 0.9471 1.0690 -0.1444 -0.1356 0.1906  351 ASP A CA  
5284  C C   . ASP A 351 ? 1.0484 0.9728 1.0970 -0.1545 -0.1242 0.2008  351 ASP A C   
5285  O O   . ASP A 351 ? 1.0857 1.0020 1.1499 -0.1629 -0.1216 0.2027  351 ASP A O   
5286  C CB  . ASP A 351 ? 1.0163 0.9513 1.0833 -0.1461 -0.1400 0.1772  351 ASP A CB  
5287  C CG  . ASP A 351 ? 0.9771 0.9344 1.0494 -0.1469 -0.1361 0.1717  351 ASP A CG  
5288  O OD1 . ASP A 351 ? 0.9584 0.9248 1.0170 -0.1422 -0.1328 0.1742  351 ASP A OD1 
5289  O OD2 . ASP A 351 ? 0.9712 0.9368 1.0628 -0.1521 -0.1369 0.1645  351 ASP A OD2 
5294  N N   . GLN A 352 ? 1.0291 0.9617 1.0627 -0.1543 -0.1167 0.2070  352 GLN A N   
5295  C CA  . GLN A 352 ? 1.0458 0.9776 1.0776 -0.1639 -0.1040 0.2169  352 GLN A CA  
5296  C C   . GLN A 352 ? 1.0587 1.0008 1.1175 -0.1735 -0.0981 0.2109  352 GLN A C   
5297  O O   . GLN A 352 ? 1.0810 1.0139 1.1497 -0.1831 -0.0908 0.2173  352 GLN A O   
5298  C CB  . GLN A 352 ? 1.0827 0.9904 1.1026 -0.1669 -0.1027 0.2311  352 GLN A CB  
5299  C CG  . GLN A 352 ? 1.1043 1.0025 1.0961 -0.1583 -0.1074 0.2390  352 GLN A CG  
5300  C CD  . GLN A 352 ? 1.0804 0.9891 1.0523 -0.1585 -0.0986 0.2439  352 GLN A CD  
5301  O OE1 . GLN A 352 ? 1.0701 0.9733 1.0329 -0.1663 -0.0877 0.2545  352 GLN A OE1 
5302  N NE2 . GLN A 352 ? 1.0443 0.9679 1.0093 -0.1501 -0.1026 0.2360  352 GLN A NE2 
5311  N N   . ASP A 353 ? 1.0397 1.0009 1.1117 -0.1707 -0.1016 0.1984  353 ASP A N   
5312  C CA  . ASP A 353 ? 1.0116 0.9857 1.1107 -0.1785 -0.0977 0.1911  353 ASP A CA  
5313  C C   . ASP A 353 ? 0.9715 0.9642 1.0732 -0.1819 -0.0866 0.1909  353 ASP A C   
5314  O O   . ASP A 353 ? 0.9957 1.0003 1.1220 -0.1889 -0.0820 0.1852  353 ASP A O   
5315  C CB  . ASP A 353 ? 1.0177 1.0002 1.1317 -0.1735 -0.1101 0.1770  353 ASP A CB  
5316  C CG  . ASP A 353 ? 1.0205 1.0180 1.1245 -0.1639 -0.1147 0.1706  353 ASP A CG  
5317  O OD1 . ASP A 353 ? 1.0365 1.0350 1.1205 -0.1593 -0.1107 0.1764  353 ASP A OD1 
5318  O OD2 . ASP A 353 ? 1.0167 1.0243 1.1327 -0.1607 -0.1226 0.1597  353 ASP A OD2 
5323  N N   . GLY A 354 ? 0.9157 0.9116 0.9944 -0.1770 -0.0823 0.1960  354 GLY A N   
5324  C CA  . GLY A 354 ? 0.9126 0.9255 0.9921 -0.1798 -0.0711 0.1954  354 GLY A CA  
5325  C C   . GLY A 354 ? 0.8941 0.9242 0.9709 -0.1706 -0.0761 0.1867  354 GLY A C   
5326  O O   . GLY A 354 ? 0.8679 0.9121 0.9438 -0.1717 -0.0671 0.1857  354 GLY A O   
5330  N N   . PHE A 355 ? 0.9043 0.9334 0.9800 -0.1619 -0.0893 0.1803  355 PHE A N   
5331  C CA  . PHE A 355 ? 0.9052 0.9486 0.9786 -0.1529 -0.0943 0.1726  355 PHE A CA  
5332  C C   . PHE A 355 ? 0.8955 0.9285 0.9470 -0.1431 -0.1024 0.1743  355 PHE A C   
5333  O O   . PHE A 355 ? 0.8829 0.9008 0.9310 -0.1414 -0.1099 0.1754  355 PHE A O   
5334  C CB  . PHE A 355 ? 0.9266 0.9810 1.0224 -0.1517 -0.1023 0.1617  355 PHE A CB  
5335  C CG  . PHE A 355 ? 0.9467 1.0128 1.0685 -0.1608 -0.0960 0.1584  355 PHE A CG  
5336  C CD1 . PHE A 355 ? 0.9278 1.0119 1.0589 -0.1620 -0.0880 0.1556  355 PHE A CD1 
5337  C CD2 . PHE A 355 ? 0.9538 1.0134 1.0934 -0.1681 -0.0979 0.1571  355 PHE A CD2 
5338  C CE1 . PHE A 355 ? 0.9329 1.0285 1.0912 -0.1703 -0.0820 0.1517  355 PHE A CE1 
5339  C CE2 . PHE A 355 ? 0.9297 1.0008 1.0966 -0.1766 -0.0922 0.1531  355 PHE A CE2 
5340  C CZ  . PHE A 355 ? 0.9312 1.0205 1.1079 -0.1776 -0.0841 0.1504  355 PHE A CZ  
5350  N N   . ASN A 356 ? 0.9121 0.9534 0.9511 -0.1368 -0.1006 0.1736  356 ASN A N   
5351  C CA  . ASN A 356 ? 0.8879 0.9214 0.9094 -0.1273 -0.1080 0.1739  356 ASN A CA  
5352  C C   . ASN A 356 ? 0.8388 0.8724 0.8681 -0.1211 -0.1184 0.1654  356 ASN A C   
5353  O O   . ASN A 356 ? 0.7972 0.8412 0.8426 -0.1222 -0.1203 0.1586  356 ASN A O   
5354  C CB  . ASN A 356 ? 0.8475 0.8918 0.8575 -0.1221 -0.1039 0.1732  356 ASN A CB  
5355  C CG  . ASN A 356 ? 0.8290 0.8693 0.8231 -0.1265 -0.0951 0.1819  356 ASN A CG  
5356  O OD1 . ASN A 356 ? 0.8312 0.8552 0.8148 -0.1299 -0.0951 0.1905  356 ASN A OD1 
5357  N ND2 . ASN A 356 ? 0.8401 0.8946 0.8316 -0.1264 -0.0874 0.1797  356 ASN A ND2 
5364  N N   . ASP A 357 ? 0.8329 0.8545 0.8503 -0.1143 -0.1252 0.1658  357 ASP A N   
5365  C CA  . ASP A 357 ? 0.8263 0.8447 0.8475 -0.1086 -0.1339 0.1584  357 ASP A CA  
5366  C C   . ASP A 357 ? 0.7618 0.7819 0.7717 -0.0988 -0.1362 0.1558  357 ASP A C   
5367  O O   . ASP A 357 ? 0.7346 0.7587 0.7352 -0.0967 -0.1322 0.1592  357 ASP A O   
5368  C CB  . ASP A 357 ? 0.9291 0.9295 0.9513 -0.1108 -0.1393 0.1600  357 ASP A CB  
5369  C CG  . ASP A 357 ? 1.0286 1.0259 1.0627 -0.1211 -0.1357 0.1637  357 ASP A CG  
5370  O OD1 . ASP A 357 ? 1.0540 1.0638 1.1026 -0.1256 -0.1335 0.1593  357 ASP A OD1 
5371  O OD2 . ASP A 357 ? 1.0821 1.0642 1.1124 -0.1248 -0.1349 0.1710  357 ASP A OD2 
5376  N N   . ILE A 358 ? 0.7487 0.7659 0.7597 -0.0931 -0.1424 0.1491  358 ILE A N   
5377  C CA  . ILE A 358 ? 0.7541 0.7743 0.7581 -0.0842 -0.1435 0.1454  358 ILE A CA  
5378  C C   . ILE A 358 ? 0.7357 0.7452 0.7388 -0.0794 -0.1496 0.1399  358 ILE A C   
5379  O O   . ILE A 358 ? 0.7216 0.7269 0.7304 -0.0823 -0.1531 0.1363  358 ILE A O   
5380  C CB  . ILE A 358 ? 0.7772 0.8148 0.7866 -0.0821 -0.1401 0.1413  358 ILE A CB  
5381  C CG1 . ILE A 358 ? 0.8274 0.8694 0.8302 -0.0745 -0.1382 0.1398  358 ILE A CG1 
5382  C CG2 . ILE A 358 ? 0.7613 0.8014 0.7776 -0.0809 -0.1444 0.1348  358 ILE A CG2 
5383  C CD1 . ILE A 358 ? 0.8567 0.9157 0.8652 -0.0738 -0.1330 0.1381  358 ILE A CD1 
5395  N N   . ALA A 359 ? 0.7369 0.7421 0.7335 -0.0722 -0.1506 0.1384  359 ALA A N   
5396  C CA  . ALA A 359 ? 0.7454 0.7415 0.7413 -0.0670 -0.1545 0.1321  359 ALA A CA  
5397  C C   . ALA A 359 ? 0.7724 0.7774 0.7672 -0.0604 -0.1521 0.1266  359 ALA A C   
5398  O O   . ALA A 359 ? 0.7878 0.8010 0.7814 -0.0573 -0.1487 0.1280  359 ALA A O   
5399  C CB  . ALA A 359 ? 0.7059 0.6880 0.6985 -0.0640 -0.1577 0.1343  359 ALA A CB  
5405  N N   . ILE A 360 ? 0.7529 0.7556 0.7478 -0.0584 -0.1535 0.1201  360 ILE A N   
5406  C CA  . ILE A 360 ? 0.7292 0.7373 0.7221 -0.0522 -0.1505 0.1153  360 ILE A CA  
5407  C C   . ILE A 360 ? 0.7349 0.7310 0.7251 -0.0478 -0.1514 0.1093  360 ILE A C   
5408  O O   . ILE A 360 ? 0.7889 0.7755 0.7782 -0.0502 -0.1548 0.1063  360 ILE A O   
5409  C CB  . ILE A 360 ? 0.7457 0.7629 0.7391 -0.0537 -0.1506 0.1135  360 ILE A CB  
5410  C CG1 . ILE A 360 ? 0.7480 0.7776 0.7478 -0.0584 -0.1492 0.1185  360 ILE A CG1 
5411  C CG2 . ILE A 360 ? 0.7448 0.7656 0.7348 -0.0472 -0.1468 0.1100  360 ILE A CG2 
5412  C CD1 . ILE A 360 ? 0.7337 0.7723 0.7375 -0.0602 -0.1510 0.1170  360 ILE A CD1 
5424  N N   . ALA A 361 ? 0.7617 0.7583 0.7521 -0.0416 -0.1477 0.1068  361 ALA A N   
5425  C CA  . ALA A 361 ? 0.8150 0.8007 0.8057 -0.0372 -0.1471 0.1007  361 ALA A CA  
5426  C C   . ALA A 361 ? 0.8376 0.8243 0.8238 -0.0337 -0.1422 0.0948  361 ALA A C   
5427  O O   . ALA A 361 ? 0.7614 0.7578 0.7471 -0.0316 -0.1381 0.0960  361 ALA A O   
5428  C CB  . ALA A 361 ? 0.8278 0.8124 0.8243 -0.0325 -0.1465 0.1010  361 ALA A CB  
5434  N N   . ALA A 362 ? 0.9137 0.8897 0.8963 -0.0332 -0.1423 0.0886  362 ALA A N   
5435  C CA  . ALA A 362 ? 0.9044 0.8778 0.8808 -0.0294 -0.1363 0.0825  362 ALA A CA  
5436  C C   . ALA A 362 ? 0.8579 0.8223 0.8409 -0.0252 -0.1327 0.0764  362 ALA A C   
5437  O O   . ALA A 362 ? 0.8620 0.8157 0.8437 -0.0257 -0.1333 0.0703  362 ALA A O   
5438  C CB  . ALA A 362 ? 0.9226 0.8911 0.8876 -0.0324 -0.1388 0.0790  362 ALA A CB  
5444  N N   . PRO A 363 ? 0.8282 0.7971 0.8206 -0.0209 -0.1291 0.0768  363 PRO A N   
5445  C CA  . PRO A 363 ? 0.7919 0.7531 0.7956 -0.0171 -0.1282 0.0714  363 PRO A CA  
5446  C C   . PRO A 363 ? 0.7803 0.7324 0.7830 -0.0147 -0.1214 0.0620  363 PRO A C   
5447  O O   . PRO A 363 ? 0.8213 0.7656 0.8349 -0.0124 -0.1216 0.0563  363 PRO A O   
5448  C CB  . PRO A 363 ? 0.7331 0.7034 0.7467 -0.0128 -0.1257 0.0730  363 PRO A CB  
5449  C CG  . PRO A 363 ? 0.7405 0.7224 0.7482 -0.0156 -0.1273 0.0806  363 PRO A CG  
5450  C CD  . PRO A 363 ? 0.7856 0.7669 0.7806 -0.0193 -0.1265 0.0815  363 PRO A CD  
5458  N N   . TYR A 364 ? 0.7822 0.7347 0.7723 -0.0152 -0.1152 0.0601  364 TYR A N   
5459  C CA  . TYR A 364 ? 0.8244 0.7680 0.8105 -0.0132 -0.1067 0.0511  364 TYR A CA  
5460  C C   . TYR A 364 ? 0.8279 0.7644 0.7971 -0.0170 -0.1087 0.0481  364 TYR A C   
5461  O O   . TYR A 364 ? 0.8425 0.7727 0.8012 -0.0160 -0.1009 0.0417  364 TYR A O   
5462  C CB  . TYR A 364 ? 0.8581 0.8061 0.8423 -0.0098 -0.0957 0.0508  364 TYR A CB  
5463  C CG  . TYR A 364 ? 0.8354 0.7920 0.8371 -0.0063 -0.0944 0.0530  364 TYR A CG  
5464  C CD1 . TYR A 364 ? 0.8156 0.7692 0.8358 -0.0027 -0.0921 0.0466  364 TYR A CD1 
5465  C CD2 . TYR A 364 ? 0.8124 0.7804 0.8136 -0.0065 -0.0961 0.0606  364 TYR A CD2 
5466  C CE1 . TYR A 364 ? 0.7910 0.7528 0.8274 0.0008  -0.0923 0.0476  364 TYR A CE1 
5467  C CE2 . TYR A 364 ? 0.7793 0.7554 0.7962 -0.0034 -0.0953 0.0613  364 TYR A CE2 
5468  C CZ  . TYR A 364 ? 0.7746 0.7475 0.8084 0.0003  -0.0938 0.0548  364 TYR A CZ  
5469  O OH  . TYR A 364 ? 0.7558 0.7371 0.8054 0.0036  -0.0942 0.0547  364 TYR A OH  
5479  N N   . GLY A 365 ? 0.8862 0.8233 0.8526 -0.0214 -0.1188 0.0521  365 GLY A N   
5480  C CA  . GLY A 365 ? 0.9150 0.8456 0.8685 -0.0252 -0.1225 0.0479  365 GLY A CA  
5481  C C   . GLY A 365 ? 0.9217 0.8409 0.8834 -0.0261 -0.1248 0.0402  365 GLY A C   
5482  O O   . GLY A 365 ? 0.9206 0.8363 0.8981 -0.0234 -0.1234 0.0380  365 GLY A O   
5486  N N   . GLY A 366 ? 0.9421 0.8556 0.8941 -0.0298 -0.1291 0.0354  366 GLY A N   
5487  C CA  . GLY A 366 ? 0.9473 0.8496 0.9074 -0.0312 -0.1314 0.0271  366 GLY A CA  
5488  C C   . GLY A 366 ? 1.0295 0.9231 0.9871 -0.0279 -0.1214 0.0155  366 GLY A C   
5489  O O   . GLY A 366 ? 1.0651 0.9605 1.0117 -0.0251 -0.1120 0.0139  366 GLY A O   
5493  N N   . GLU A 367 ? 1.1005 0.9841 1.0696 -0.0284 -0.1227 0.0071  367 GLU A N   
5494  C CA  . GLU A 367 ? 1.1931 1.0678 1.1624 -0.0258 -0.1128 -0.0059 367 GLU A CA  
5495  C C   . GLU A 367 ? 1.1682 1.0439 1.1554 -0.0205 -0.1053 -0.0065 367 GLU A C   
5496  O O   . GLU A 367 ? 1.1654 1.0422 1.1725 -0.0189 -0.1112 -0.0016 367 GLU A O   
5497  C CB  . GLU A 367 ? 1.3112 1.1749 1.2892 -0.0283 -0.1174 -0.0155 367 GLU A CB  
5498  C CG  . GLU A 367 ? 1.4120 1.2748 1.3763 -0.0339 -0.1261 -0.0162 367 GLU A CG  
5499  C CD  . GLU A 367 ? 1.4735 1.3255 1.4502 -0.0366 -0.1311 -0.0257 367 GLU A CD  
5500  O OE1 . GLU A 367 ? 1.4869 1.3334 1.4865 -0.0347 -0.1320 -0.0263 367 GLU A OE1 
5501  O OE2 . GLU A 367 ? 1.4975 1.3462 1.4616 -0.0404 -0.1346 -0.0327 367 GLU A OE2 
5508  N N   . ASP A 368 ? 1.1802 1.0553 1.1602 -0.0177 -0.0922 -0.0124 368 ASP A N   
5509  C CA  . ASP A 368 ? 1.2366 1.1132 1.2353 -0.0127 -0.0836 -0.0148 368 ASP A CA  
5510  C C   . ASP A 368 ? 1.1727 1.0603 1.1813 -0.0107 -0.0889 -0.0026 368 ASP A C   
5511  O O   . ASP A 368 ? 1.1609 1.0498 1.1921 -0.0072 -0.0906 -0.0027 368 ASP A O   
5512  C CB  . ASP A 368 ? 1.3617 1.2298 1.3848 -0.0107 -0.0837 -0.0249 368 ASP A CB  
5513  C CG  . ASP A 368 ? 1.4759 1.3337 1.4919 -0.0118 -0.0743 -0.0396 368 ASP A CG  
5514  O OD1 . ASP A 368 ? 1.5165 1.3700 1.5140 -0.0160 -0.0782 -0.0420 368 ASP A OD1 
5515  O OD2 . ASP A 368 ? 1.5094 1.3636 1.5390 -0.0086 -0.0628 -0.0495 368 ASP A OD2 
5520  N N   . LYS A 369 ? 1.1556 1.0512 1.1473 -0.0128 -0.0919 0.0072  369 LYS A N   
5521  C CA  . LYS A 369 ? 1.1574 1.0641 1.1557 -0.0114 -0.0958 0.0180  369 LYS A CA  
5522  C C   . LYS A 369 ? 1.1347 1.0419 1.1524 -0.0107 -0.1064 0.0219  369 LYS A C   
5523  O O   . LYS A 369 ? 1.1837 1.0968 1.2155 -0.0072 -0.1071 0.0252  369 LYS A O   
5524  C CB  . LYS A 369 ? 1.1763 1.0877 1.1807 -0.0071 -0.0841 0.0165  369 LYS A CB  
5525  C CG  . LYS A 369 ? 1.1835 1.0932 1.1674 -0.0075 -0.0725 0.0143  369 LYS A CG  
5526  C CD  . LYS A 369 ? 1.1272 1.0433 1.1181 -0.0040 -0.0623 0.0165  369 LYS A CD  
5527  C CE  . LYS A 369 ? 1.1337 1.0426 1.1165 -0.0029 -0.0458 0.0088  369 LYS A CE  
5528  N NZ  . LYS A 369 ? 1.1713 1.0721 1.1709 -0.0013 -0.0399 -0.0037 369 LYS A NZ  
5542  N N   . LYS A 370 ? 1.0446 0.9450 1.0627 -0.0140 -0.1150 0.0217  370 LYS A N   
5543  C CA  . LYS A 370 ? 0.9730 0.8715 1.0067 -0.0137 -0.1254 0.0269  370 LYS A CA  
5544  C C   . LYS A 370 ? 0.9684 0.8756 0.9957 -0.0167 -0.1332 0.0399  370 LYS A C   
5545  O O   . LYS A 370 ? 1.0200 0.9255 1.0566 -0.0167 -0.1415 0.0460  370 LYS A O   
5546  C CB  . LYS A 370 ? 0.9744 0.8606 1.0134 -0.0162 -0.1306 0.0215  370 LYS A CB  
5547  C CG  . LYS A 370 ? 0.9982 0.8752 1.0524 -0.0125 -0.1248 0.0087  370 LYS A CG  
5548  C CD  . LYS A 370 ? 1.0499 0.9147 1.1121 -0.0149 -0.1311 0.0038  370 LYS A CD  
5549  C CE  . LYS A 370 ? 1.1110 0.9669 1.1886 -0.0115 -0.1241 -0.0108 370 LYS A CE  
5550  N NZ  . LYS A 370 ? 1.1668 1.0105 1.2537 -0.0139 -0.1301 -0.0164 370 LYS A NZ  
5564  N N   . GLY A 371 ? 0.9131 0.8287 0.9248 -0.0190 -0.1308 0.0442  371 GLY A N   
5565  C CA  . GLY A 371 ? 0.8613 0.7866 0.8690 -0.0215 -0.1363 0.0554  371 GLY A CA  
5566  C C   . GLY A 371 ? 0.8409 0.7638 0.8434 -0.0277 -0.1442 0.0598  371 GLY A C   
5567  O O   . GLY A 371 ? 0.8482 0.7607 0.8554 -0.0297 -0.1482 0.0561  371 GLY A O   
5571  N N   . ILE A 372 ? 0.8336 0.7664 0.8285 -0.0310 -0.1462 0.0675  372 ILE A N   
5572  C CA  . ILE A 372 ? 0.8686 0.8013 0.8606 -0.0374 -0.1529 0.0720  372 ILE A CA  
5573  C C   . ILE A 372 ? 0.8737 0.8173 0.8663 -0.0395 -0.1549 0.0824  372 ILE A C   
5574  O O   . ILE A 372 ? 0.8836 0.8372 0.8741 -0.0366 -0.1508 0.0849  372 ILE A O   
5575  C CB  . ILE A 372 ? 0.8751 0.8086 0.8552 -0.0403 -0.1528 0.0670  372 ILE A CB  
5576  C CG1 . ILE A 372 ? 0.9573 0.8788 0.9355 -0.0391 -0.1509 0.0558  372 ILE A CG1 
5577  C CG2 . ILE A 372 ? 0.8420 0.7785 0.8225 -0.0470 -0.1597 0.0717  372 ILE A CG2 
5578  C CD1 . ILE A 372 ? 1.0420 0.9629 1.0059 -0.0415 -0.1517 0.0498  372 ILE A CD1 
5590  N N   . VAL A 373 ? 0.8549 0.7961 0.8511 -0.0447 -0.1604 0.0882  373 VAL A N   
5591  C CA  . VAL A 373 ? 0.8224 0.7731 0.8185 -0.0480 -0.1615 0.0978  373 VAL A CA  
5592  C C   . VAL A 373 ? 0.8135 0.7652 0.8094 -0.0553 -0.1648 0.0994  373 VAL A C   
5593  O O   . VAL A 373 ? 0.8353 0.7766 0.8355 -0.0588 -0.1687 0.0975  373 VAL A O   
5594  C CB  . VAL A 373 ? 0.8065 0.7524 0.8073 -0.0474 -0.1641 0.1048  373 VAL A CB  
5595  C CG1 . VAL A 373 ? 0.7969 0.7514 0.7953 -0.0522 -0.1641 0.1143  373 VAL A CG1 
5596  C CG2 . VAL A 373 ? 0.8185 0.7655 0.8217 -0.0399 -0.1619 0.1024  373 VAL A CG2 
5606  N N   . TYR A 374 ? 0.8038 0.7682 0.7971 -0.0576 -0.1635 0.1022  374 TYR A N   
5607  C CA  . TYR A 374 ? 0.8283 0.7962 0.8245 -0.0644 -0.1668 0.1031  374 TYR A CA  
5608  C C   . TYR A 374 ? 0.8062 0.7796 0.8078 -0.0694 -0.1660 0.1123  374 TYR A C   
5609  O O   . TYR A 374 ? 0.7680 0.7485 0.7676 -0.0672 -0.1623 0.1173  374 TYR A O   
5610  C CB  . TYR A 374 ? 0.8703 0.8485 0.8615 -0.0634 -0.1667 0.0994  374 TYR A CB  
5611  C CG  . TYR A 374 ? 0.9021 0.8743 0.8844 -0.0590 -0.1667 0.0908  374 TYR A CG  
5612  C CD1 . TYR A 374 ? 0.9105 0.8754 0.8906 -0.0617 -0.1716 0.0838  374 TYR A CD1 
5613  C CD2 . TYR A 374 ? 0.9116 0.8851 0.8873 -0.0525 -0.1612 0.0892  374 TYR A CD2 
5614  C CE1 . TYR A 374 ? 0.9141 0.8729 0.8832 -0.0579 -0.1707 0.0755  374 TYR A CE1 
5615  C CE2 . TYR A 374 ? 0.8884 0.8555 0.8545 -0.0489 -0.1595 0.0816  374 TYR A CE2 
5616  C CZ  . TYR A 374 ? 0.8842 0.8438 0.8456 -0.0516 -0.1641 0.0749  374 TYR A CZ  
5617  O OH  . TYR A 374 ? 0.8866 0.8394 0.8357 -0.0483 -0.1616 0.0669  374 TYR A OH  
5627  N N   . ILE A 375 ? 0.8442 0.8138 0.8525 -0.0764 -0.1689 0.1140  375 ILE A N   
5628  C CA  . ILE A 375 ? 0.8390 0.8123 0.8526 -0.0825 -0.1667 0.1226  375 ILE A CA  
5629  C C   . ILE A 375 ? 0.8236 0.8089 0.8444 -0.0878 -0.1670 0.1211  375 ILE A C   
5630  O O   . ILE A 375 ? 0.8705 0.8536 0.8965 -0.0906 -0.1717 0.1150  375 ILE A O   
5631  C CB  . ILE A 375 ? 0.8669 0.8253 0.8853 -0.0871 -0.1688 0.1267  375 ILE A CB  
5632  C CG1 . ILE A 375 ? 0.9149 0.8610 0.9283 -0.0810 -0.1701 0.1276  375 ILE A CG1 
5633  C CG2 . ILE A 375 ? 0.8698 0.8311 0.8914 -0.0939 -0.1648 0.1366  375 ILE A CG2 
5634  C CD1 . ILE A 375 ? 0.9315 0.8827 0.9372 -0.0765 -0.1670 0.1337  375 ILE A CD1 
5646  N N   . PHE A 376 ? 0.8046 0.8029 0.8267 -0.0890 -0.1624 0.1259  376 PHE A N   
5647  C CA  . PHE A 376 ? 0.8518 0.8632 0.8838 -0.0935 -0.1623 0.1246  376 PHE A CA  
5648  C C   . PHE A 376 ? 0.8521 0.8669 0.8918 -0.1010 -0.1569 0.1320  376 PHE A C   
5649  O O   . PHE A 376 ? 0.8335 0.8509 0.8670 -0.1000 -0.1511 0.1381  376 PHE A O   
5650  C CB  . PHE A 376 ? 0.8499 0.8750 0.8791 -0.0881 -0.1608 0.1224  376 PHE A CB  
5651  C CG  . PHE A 376 ? 0.8657 0.8876 0.8867 -0.0816 -0.1651 0.1156  376 PHE A CG  
5652  C CD1 . PHE A 376 ? 0.8536 0.8688 0.8639 -0.0749 -0.1631 0.1149  376 PHE A CD1 
5653  C CD2 . PHE A 376 ? 0.8694 0.8946 0.8931 -0.0822 -0.1711 0.1099  376 PHE A CD2 
5654  C CE1 . PHE A 376 ? 0.8536 0.8653 0.8556 -0.0694 -0.1652 0.1087  376 PHE A CE1 
5655  C CE2 . PHE A 376 ? 0.8703 0.8914 0.8829 -0.0764 -0.1744 0.1042  376 PHE A CE2 
5656  C CZ  . PHE A 376 ? 0.8650 0.8791 0.8665 -0.0703 -0.1705 0.1038  376 PHE A CZ  
5666  N N   . ASN A 377 ? 0.8400 0.8544 0.8928 -0.1086 -0.1583 0.1310  377 ASN A N   
5667  C CA  . ASN A 377 ? 0.8393 0.8561 0.9009 -0.1168 -0.1517 0.1377  377 ASN A CA  
5668  C C   . ASN A 377 ? 0.8229 0.8584 0.8954 -0.1190 -0.1479 0.1363  377 ASN A C   
5669  O O   . ASN A 377 ? 0.8310 0.8757 0.9109 -0.1169 -0.1532 0.1292  377 ASN A O   
5670  C CB  . ASN A 377 ? 0.8672 0.8743 0.9414 -0.1245 -0.1542 0.1370  377 ASN A CB  
5671  C CG  . ASN A 377 ? 0.8718 0.8595 0.9380 -0.1228 -0.1575 0.1387  377 ASN A CG  
5672  O OD1 . ASN A 377 ? 0.8355 0.8171 0.8999 -0.1187 -0.1646 0.1312  377 ASN A OD1 
5673  N ND2 . ASN A 377 ? 0.9121 0.8897 0.9732 -0.1257 -0.1524 0.1485  377 ASN A ND2 
5680  N N   . GLY A 378 ? 0.7891 0.8299 0.8621 -0.1231 -0.1386 0.1430  378 GLY A N   
5681  C CA  . GLY A 378 ? 0.7661 0.8247 0.8518 -0.1259 -0.1335 0.1414  378 GLY A CA  
5682  C C   . GLY A 378 ? 0.8016 0.8640 0.9088 -0.1357 -0.1311 0.1403  378 GLY A C   
5683  O O   . GLY A 378 ? 0.8196 0.8700 0.9302 -0.1417 -0.1307 0.1432  378 GLY A O   
5687  N N   . ARG A 379 ? 0.8258 0.9053 0.9500 -0.1373 -0.1294 0.1359  379 ARG A N   
5688  C CA  . ARG A 379 ? 0.8599 0.9462 1.0089 -0.1467 -0.1262 0.1337  379 ARG A CA  
5689  C C   . ARG A 379 ? 0.8257 0.9314 0.9887 -0.1477 -0.1194 0.1316  379 ARG A C   
5690  O O   . ARG A 379 ? 0.7899 0.9029 0.9431 -0.1409 -0.1182 0.1316  379 ARG A O   
5691  C CB  . ARG A 379 ? 0.9376 1.0226 1.1010 -0.1473 -0.1384 0.1254  379 ARG A CB  
5692  C CG  . ARG A 379 ? 0.9991 1.0903 1.1581 -0.1380 -0.1499 0.1184  379 ARG A CG  
5693  C CD  . ARG A 379 ? 1.0921 1.1800 1.2615 -0.1389 -0.1624 0.1102  379 ARG A CD  
5694  N NE  . ARG A 379 ? 1.1681 1.2613 1.3312 -0.1304 -0.1734 0.1041  379 ARG A NE  
5695  C CZ  . ARG A 379 ? 1.2134 1.3053 1.3815 -0.1294 -0.1860 0.0960  379 ARG A CZ  
5696  N NH1 . ARG A 379 ? 1.2335 1.3199 1.4157 -0.1364 -0.1894 0.0919  379 ARG A NH1 
5697  N NH2 . ARG A 379 ? 1.2055 1.3011 1.3639 -0.1213 -0.1952 0.0919  379 ARG A NH2 
5711  N N   . SER A 380 ? 0.8436 0.9578 1.0319 -0.1564 -0.1144 0.1293  380 SER A N   
5712  C CA  . SER A 380 ? 0.8453 0.9776 1.0497 -0.1587 -0.1053 0.1273  380 SER A CA  
5713  C C   . SER A 380 ? 0.7748 0.9208 0.9854 -0.1501 -0.1139 0.1206  380 SER A C   
5714  O O   . SER A 380 ? 0.7139 0.8717 0.9261 -0.1477 -0.1071 0.1204  380 SER A O   
5715  C CB  . SER A 380 ? 0.8542 0.9933 1.0893 -0.1696 -0.0997 0.1243  380 SER A CB  
5716  O OG  . SER A 380 ? 0.8837 1.0235 1.1371 -0.1697 -0.1131 0.1167  380 SER A OG  
5722  N N   . THR A 381 ? 0.7865 0.9306 1.0000 -0.1453 -0.1287 0.1151  381 THR A N   
5723  C CA  . THR A 381 ? 0.8457 1.0012 1.0642 -0.1371 -0.1374 0.1098  381 THR A CA  
5724  C C   . THR A 381 ? 0.8333 0.9843 1.0254 -0.1277 -0.1374 0.1134  381 THR A C   
5725  O O   . THR A 381 ? 0.8112 0.9729 1.0069 -0.1218 -0.1385 0.1114  381 THR A O   
5726  C CB  . THR A 381 ? 0.9229 1.0765 1.1492 -0.1349 -0.1536 0.1031  381 THR A CB  
5727  O OG1 . THR A 381 ? 0.9993 1.1355 1.2014 -0.1317 -0.1597 0.1048  381 THR A OG1 
5728  C CG2 . THR A 381 ? 0.9397 1.0984 1.1956 -0.1443 -0.1544 0.0983  381 THR A CG2 
5736  N N   . GLY A 382 ? 0.8521 0.9874 1.0199 -0.1262 -0.1364 0.1183  382 GLY A N   
5737  C CA  . GLY A 382 ? 0.8519 0.9823 0.9967 -0.1176 -0.1365 0.1209  382 GLY A CA  
5738  C C   . GLY A 382 ? 0.9080 1.0198 1.0318 -0.1159 -0.1399 0.1238  382 GLY A C   
5739  O O   . GLY A 382 ? 0.9954 1.0978 1.1163 -0.1220 -0.1354 0.1280  382 GLY A O   
5743  N N   . LEU A 383 ? 0.8891 0.9950 0.9987 -0.1078 -0.1472 0.1218  383 LEU A N   
5744  C CA  . LEU A 383 ? 0.8953 0.9841 0.9877 -0.1056 -0.1511 0.1227  383 LEU A CA  
5745  C C   . LEU A 383 ? 0.8860 0.9697 0.9823 -0.1059 -0.1620 0.1167  383 LEU A C   
5746  O O   . LEU A 383 ? 0.8877 0.9789 0.9891 -0.1026 -0.1689 0.1119  383 LEU A O   
5747  C CB  . LEU A 383 ? 0.8810 0.9658 0.9550 -0.0967 -0.1507 0.1236  383 LEU A CB  
5748  C CG  . LEU A 383 ? 0.8909 0.9586 0.9489 -0.0940 -0.1534 0.1242  383 LEU A CG  
5749  C CD1 . LEU A 383 ? 0.9158 0.9748 0.9704 -0.0990 -0.1480 0.1303  383 LEU A CD1 
5750  C CD2 . LEU A 383 ? 0.8780 0.9436 0.9223 -0.0850 -0.1530 0.1233  383 LEU A CD2 
5762  N N   . ASN A 384 ? 0.8842 0.9546 0.9779 -0.1099 -0.1640 0.1167  384 ASN A N   
5763  C CA  . ASN A 384 ? 0.9020 0.9659 0.9971 -0.1100 -0.1744 0.1098  384 ASN A CA  
5764  C C   . ASN A 384 ? 0.9181 0.9763 0.9940 -0.1009 -0.1795 0.1066  384 ASN A C   
5765  O O   . ASN A 384 ? 0.9374 0.9857 0.9984 -0.0971 -0.1760 0.1091  384 ASN A O   
5766  C CB  . ASN A 384 ? 0.9428 0.9928 1.0403 -0.1161 -0.1743 0.1105  384 ASN A CB  
5767  C CG  . ASN A 384 ? 0.9786 1.0238 1.0824 -0.1178 -0.1849 0.1017  384 ASN A CG  
5768  O OD1 . ASN A 384 ? 0.9773 1.0264 1.0764 -0.1128 -0.1931 0.0954  384 ASN A OD1 
5769  N ND2 . ASN A 384 ? 1.0269 1.0629 1.1407 -0.1248 -0.1848 0.1013  384 ASN A ND2 
5776  N N   . ALA A 385 ? 0.9238 0.9879 1.0003 -0.0975 -0.1877 0.1010  385 ALA A N   
5777  C CA  . ALA A 385 ? 0.9024 0.9619 0.9597 -0.0890 -0.1908 0.0990  385 ALA A CA  
5778  C C   . ALA A 385 ? 0.8503 0.8935 0.8931 -0.0875 -0.1938 0.0948  385 ALA A C   
5779  O O   . ALA A 385 ? 0.8443 0.8814 0.8699 -0.0809 -0.1927 0.0938  385 ALA A O   
5780  C CB  . ALA A 385 ? 0.9501 1.0183 1.0099 -0.0858 -0.1997 0.0949  385 ALA A CB  
5786  N N   . VAL A 386 ? 0.8346 0.8707 0.8854 -0.0936 -0.1966 0.0918  386 VAL A N   
5787  C CA  . VAL A 386 ? 0.8657 0.8865 0.9061 -0.0928 -0.1997 0.0864  386 VAL A CA  
5788  C C   . VAL A 386 ? 0.8954 0.9062 0.9348 -0.0942 -0.1921 0.0920  386 VAL A C   
5789  O O   . VAL A 386 ? 0.9097 0.9220 0.9620 -0.1004 -0.1883 0.0973  386 VAL A O   
5790  C CB  . VAL A 386 ? 0.8940 0.9123 0.9453 -0.0985 -0.2087 0.0785  386 VAL A CB  
5791  C CG1 . VAL A 386 ? 0.9179 0.9207 0.9581 -0.0971 -0.2118 0.0714  386 VAL A CG1 
5792  C CG2 . VAL A 386 ? 0.8915 0.9210 0.9456 -0.0971 -0.2179 0.0735  386 VAL A CG2 
5802  N N   . PRO A 387 ? 0.9027 0.9031 0.9278 -0.0887 -0.1897 0.0910  387 PRO A N   
5803  C CA  . PRO A 387 ? 0.9029 0.8933 0.9283 -0.0894 -0.1844 0.0961  387 PRO A CA  
5804  C C   . PRO A 387 ? 0.8897 0.8686 0.9246 -0.0955 -0.1877 0.0936  387 PRO A C   
5805  O O   . PRO A 387 ? 0.9198 0.8930 0.9544 -0.0960 -0.1938 0.0846  387 PRO A O   
5806  C CB  . PRO A 387 ? 0.8996 0.8829 0.9100 -0.0815 -0.1821 0.0934  387 PRO A CB  
5807  C CG  . PRO A 387 ? 0.8947 0.8784 0.8962 -0.0787 -0.1871 0.0848  387 PRO A CG  
5808  C CD  . PRO A 387 ? 0.8987 0.8957 0.9070 -0.0816 -0.1913 0.0854  387 PRO A CD  
5816  N N   . SER A 388 ? 0.8558 0.8308 0.8987 -0.1001 -0.1836 0.1015  388 SER A N   
5817  C CA  . SER A 388 ? 0.8477 0.8108 0.9018 -0.1064 -0.1856 0.1011  388 SER A CA  
5818  C C   . SER A 388 ? 0.8649 0.8114 0.9135 -0.1029 -0.1856 0.1007  388 SER A C   
5819  O O   . SER A 388 ? 0.8462 0.7807 0.9044 -0.1073 -0.1875 0.1001  388 SER A O   
5820  C CB  . SER A 388 ? 0.8359 0.8017 0.9012 -0.1138 -0.1804 0.1108  388 SER A CB  
5821  O OG  . SER A 388 ? 0.8462 0.8106 0.9022 -0.1110 -0.1742 0.1206  388 SER A OG  
5827  N N   . GLN A 389 ? 0.8902 0.8357 0.9260 -0.0950 -0.1835 0.1007  389 GLN A N   
5828  C CA  . GLN A 389 ? 0.9067 0.8374 0.9400 -0.0910 -0.1837 0.0994  389 GLN A CA  
5829  C C   . GLN A 389 ? 0.8886 0.8220 0.9095 -0.0824 -0.1815 0.0953  389 GLN A C   
5830  O O   . GLN A 389 ? 0.8609 0.8063 0.8751 -0.0795 -0.1784 0.0980  389 GLN A O   
5831  C CB  . GLN A 389 ? 0.9276 0.8504 0.9642 -0.0928 -0.1812 0.1107  389 GLN A CB  
5832  C CG  . GLN A 389 ? 0.9631 0.8684 1.0030 -0.0902 -0.1836 0.1093  389 GLN A CG  
5833  C CD  . GLN A 389 ? 0.9705 0.8660 1.0139 -0.0930 -0.1829 0.1216  389 GLN A CD  
5834  O OE1 . GLN A 389 ? 0.9781 0.8802 1.0189 -0.0966 -0.1793 0.1312  389 GLN A OE1 
5835  N NE2 . GLN A 389 ? 0.9563 0.8353 1.0055 -0.0914 -0.1861 0.1212  389 GLN A NE2 
5844  N N   . ILE A 390 ? 0.9112 0.8330 0.9308 -0.0784 -0.1825 0.0884  390 ILE A N   
5845  C CA  . ILE A 390 ? 0.8848 0.8071 0.8950 -0.0706 -0.1792 0.0833  390 ILE A CA  
5846  C C   . ILE A 390 ? 0.9114 0.8213 0.9268 -0.0668 -0.1787 0.0838  390 ILE A C   
5847  O O   . ILE A 390 ? 0.9612 0.8585 0.9842 -0.0683 -0.1816 0.0790  390 ILE A O   
5848  C CB  . ILE A 390 ? 0.9024 0.8239 0.9049 -0.0692 -0.1803 0.0713  390 ILE A CB  
5849  C CG1 . ILE A 390 ? 0.9088 0.8429 0.9060 -0.0719 -0.1825 0.0713  390 ILE A CG1 
5850  C CG2 . ILE A 390 ? 0.9187 0.8384 0.9123 -0.0617 -0.1750 0.0661  390 ILE A CG2 
5851  C CD1 . ILE A 390 ? 0.9305 0.8630 0.9180 -0.0713 -0.1857 0.0601  390 ILE A CD1 
5863  N N   . LEU A 391 ? 0.9052 0.8185 0.9181 -0.0617 -0.1756 0.0891  391 LEU A N   
5864  C CA  . LEU A 391 ? 0.8834 0.7864 0.9022 -0.0569 -0.1761 0.0895  391 LEU A CA  
5865  C C   . LEU A 391 ? 0.9396 0.8428 0.9559 -0.0500 -0.1718 0.0798  391 LEU A C   
5866  O O   . LEU A 391 ? 0.9716 0.8855 0.9799 -0.0473 -0.1673 0.0790  391 LEU A O   
5867  C CB  . LEU A 391 ? 0.8633 0.7697 0.8816 -0.0556 -0.1764 0.1009  391 LEU A CB  
5868  C CG  . LEU A 391 ? 0.9311 0.8333 0.9520 -0.0619 -0.1795 0.1118  391 LEU A CG  
5869  C CD1 . LEU A 391 ? 0.9822 0.8939 1.0009 -0.0692 -0.1779 0.1138  391 LEU A CD1 
5870  C CD2 . LEU A 391 ? 0.9532 0.8570 0.9700 -0.0592 -0.1798 0.1218  391 LEU A CD2 
5882  N N   . GLU A 392 ? 0.9503 0.8412 0.9745 -0.0475 -0.1726 0.0724  392 GLU A N   
5883  C CA  . GLU A 392 ? 0.9463 0.8357 0.9702 -0.0416 -0.1671 0.0620  392 GLU A CA  
5884  C C   . GLU A 392 ? 0.9379 0.8206 0.9746 -0.0358 -0.1680 0.0621  392 GLU A C   
5885  O O   . GLU A 392 ? 0.9620 0.8354 1.0085 -0.0366 -0.1741 0.0670  392 GLU A O   
5886  C CB  . GLU A 392 ? 1.0028 0.8841 1.0256 -0.0434 -0.1662 0.0497  392 GLU A CB  
5887  C CG  . GLU A 392 ? 1.0855 0.9724 1.0964 -0.0488 -0.1676 0.0483  392 GLU A CG  
5888  C CD  . GLU A 392 ? 1.1870 1.0646 1.1977 -0.0512 -0.1689 0.0361  392 GLU A CD  
5889  O OE1 . GLU A 392 ? 1.2280 1.0957 1.2514 -0.0543 -0.1738 0.0351  392 GLU A OE1 
5890  O OE2 . GLU A 392 ? 1.2332 1.1127 1.2307 -0.0500 -0.1650 0.0275  392 GLU A OE2 
5897  N N   . GLY A 393 ? 0.9046 0.7915 0.9420 -0.0299 -0.1620 0.0568  393 GLY A N   
5898  C CA  . GLY A 393 ? 0.9079 0.7895 0.9603 -0.0237 -0.1628 0.0546  393 GLY A CA  
5899  C C   . GLY A 393 ? 0.9479 0.8180 1.0112 -0.0218 -0.1604 0.0419  393 GLY A C   
5900  O O   . GLY A 393 ? 0.9559 0.8257 1.0118 -0.0230 -0.1538 0.0324  393 GLY A O   
5904  N N   . GLN A 394 ? 0.9811 0.8413 1.0617 -0.0187 -0.1661 0.0417  394 GLN A N   
5905  C CA  . GLN A 394 ? 1.0292 0.8777 1.1244 -0.0168 -0.1646 0.0295  394 GLN A CA  
5906  C C   . GLN A 394 ? 1.0215 0.8706 1.1316 -0.0095 -0.1591 0.0204  394 GLN A C   
5907  O O   . GLN A 394 ? 1.0554 0.8953 1.1802 -0.0074 -0.1566 0.0090  394 GLN A O   
5908  C CB  . GLN A 394 ? 1.0745 0.9097 1.1830 -0.0180 -0.1748 0.0345  394 GLN A CB  
5909  C CG  . GLN A 394 ? 1.1028 0.9377 1.2005 -0.0248 -0.1810 0.0470  394 GLN A CG  
5910  C CD  . GLN A 394 ? 1.1609 0.9979 1.2462 -0.0314 -0.1773 0.0419  394 GLN A CD  
5911  O OE1 . GLN A 394 ? 1.1817 1.0162 1.2672 -0.0312 -0.1718 0.0286  394 GLN A OE1 
5912  N NE2 . GLN A 394 ? 1.1929 1.0348 1.2675 -0.0374 -0.1804 0.0520  394 GLN A NE2 
5921  N N   . TRP A 395 ? 0.9727 0.8324 1.0814 -0.0058 -0.1568 0.0243  395 TRP A N   
5922  C CA  . TRP A 395 ? 0.9659 0.8268 1.0931 0.0013  -0.1532 0.0167  395 TRP A CA  
5923  C C   . TRP A 395 ? 0.9728 0.8429 1.0926 0.0022  -0.1395 0.0095  395 TRP A C   
5924  O O   . TRP A 395 ? 0.9948 0.8745 1.0963 -0.0004 -0.1364 0.0158  395 TRP A O   
5925  C CB  . TRP A 395 ? 1.0064 0.8712 1.1416 0.0056  -0.1627 0.0264  395 TRP A CB  
5926  C CG  . TRP A 395 ? 1.1065 0.9612 1.2451 0.0045  -0.1759 0.0359  395 TRP A CG  
5927  C CD1 . TRP A 395 ? 1.2019 1.0448 1.3611 0.0085  -0.1838 0.0337  395 TRP A CD1 
5928  C CD2 . TRP A 395 ? 1.1119 0.9666 1.2333 -0.0013 -0.1821 0.0495  395 TRP A CD2 
5929  N NE1 . TRP A 395 ? 1.2423 1.0766 1.3965 0.0057  -0.1946 0.0461  395 TRP A NE1 
5930  C CE2 . TRP A 395 ? 1.1806 1.0221 1.3117 -0.0006 -0.1931 0.0558  395 TRP A CE2 
5931  C CE3 . TRP A 395 ? 1.0785 0.9427 1.1787 -0.0069 -0.1791 0.0570  395 TRP A CE3 
5932  C CZ2 . TRP A 395 ? 1.1770 1.0143 1.2961 -0.0058 -0.1999 0.0695  395 TRP A CZ2 
5933  C CZ3 . TRP A 395 ? 1.1064 0.9676 1.1967 -0.0120 -0.1859 0.0695  395 TRP A CZ3 
5934  C CH2 . TRP A 395 ? 1.1444 0.9920 1.2435 -0.0117 -0.1956 0.0758  395 TRP A CH2 
5945  N N   . ALA A 396 ? 0.9739 0.8405 1.1091 0.0059  -0.1310 -0.0038 396 ALA A N   
5946  C CA  . ALA A 396 ? 1.0328 0.9060 1.1641 0.0072  -0.1164 -0.0113 396 ALA A CA  
5947  C C   . ALA A 396 ? 1.0927 0.9694 1.2499 0.0140  -0.1142 -0.0167 396 ALA A C   
5948  O O   . ALA A 396 ? 1.1220 0.9929 1.3024 0.0180  -0.1220 -0.0198 396 ALA A O   
5949  C CB  . ALA A 396 ? 1.0269 0.8925 1.1518 0.0048  -0.1052 -0.0239 396 ALA A CB  
5955  N N   . ALA A 397 ? 1.1414 1.0275 1.2959 0.0154  -0.1040 -0.0179 397 ALA A N   
5956  C CA  . ALA A 397 ? 1.2443 1.1359 1.4241 0.0214  -0.1012 -0.0234 397 ALA A CA  
5957  C C   . ALA A 397 ? 1.3163 1.2083 1.5004 0.0218  -0.0821 -0.0354 397 ALA A C   
5958  O O   . ALA A 397 ? 1.3157 1.2033 1.4802 0.0177  -0.0718 -0.0387 397 ALA A O   
5959  C CB  . ALA A 397 ? 1.2753 1.1787 1.4514 0.0228  -0.1075 -0.0128 397 ALA A CB  
5965  N N   . ARG A 398 ? 1.3777 1.2749 1.5878 0.0269  -0.0772 -0.0421 398 ARG A N   
5966  C CA  . ARG A 398 ? 1.3980 1.2952 1.6169 0.0274  -0.0578 -0.0540 398 ARG A CA  
5967  C C   . ARG A 398 ? 1.3537 1.2620 1.5799 0.0294  -0.0501 -0.0527 398 ARG A C   
5968  O O   . ARG A 398 ? 1.3902 1.2983 1.6230 0.0294  -0.0323 -0.0614 398 ARG A O   
5969  C CB  . ARG A 398 ? 1.4522 1.3430 1.7045 0.0314  -0.0549 -0.0687 398 ARG A CB  
5970  C CG  . ARG A 398 ? 1.5496 1.4282 1.7943 0.0283  -0.0508 -0.0763 398 ARG A CG  
5971  C CD  . ARG A 398 ? 1.6386 1.5113 1.9198 0.0325  -0.0482 -0.0914 398 ARG A CD  
5972  N NE  . ARG A 398 ? 1.6774 1.5520 1.9869 0.0384  -0.0663 -0.0888 398 ARG A NE  
5973  C CZ  . ARG A 398 ? 1.6846 1.5542 1.9899 0.0386  -0.0849 -0.0797 398 ARG A CZ  
5974  N NH1 . ARG A 398 ? 1.6918 1.5552 1.9685 0.0331  -0.0877 -0.0732 398 ARG A NH1 
5975  N NH2 . ARG A 398 ? 1.6739 1.5443 2.0035 0.0444  -0.1009 -0.0771 398 ARG A NH2 
5989  N N   . SER A 399 ? 1.2855 1.2029 1.5110 0.0310  -0.0621 -0.0426 399 SER A N   
5990  C CA  . SER A 399 ? 1.2643 1.1926 1.4988 0.0330  -0.0557 -0.0420 399 SER A CA  
5991  C C   . SER A 399 ? 1.1523 1.0869 1.3574 0.0292  -0.0559 -0.0293 399 SER A C   
5992  O O   . SER A 399 ? 1.1005 1.0373 1.2967 0.0274  -0.0414 -0.0293 399 SER A O   
5993  C CB  . SER A 399 ? 1.3922 1.3272 1.6559 0.0390  -0.0691 -0.0437 399 SER A CB  
5994  O OG  . SER A 399 ? 1.4791 1.4157 1.7293 0.0388  -0.0878 -0.0320 399 SER A OG  
6000  N N   . CYS A 400 ? 1.1100 1.0469 1.3005 0.0279  -0.0716 -0.0182 400 CYS A N   
6001  C CA  . CYS A 400 ? 0.9830 0.9263 1.1480 0.0244  -0.0735 -0.0064 400 CYS A CA  
6002  C C   . CYS A 400 ? 0.9711 0.9083 1.1130 0.0200  -0.0830 0.0013  400 CYS A C   
6003  O O   . CYS A 400 ? 1.0018 0.9333 1.1509 0.0209  -0.0943 0.0012  400 CYS A O   
6004  C CB  . CYS A 400 ? 0.9481 0.9030 1.1227 0.0272  -0.0829 -0.0013 400 CYS A CB  
6005  S SG  . CYS A 400 ? 0.9760 0.9413 1.1264 0.0236  -0.0833 0.0113  400 CYS A SG  
6010  N N   . PRO A 401 ? 0.9555 0.8932 1.0712 0.0154  -0.0792 0.0078  401 PRO A N   
6011  C CA  . PRO A 401 ? 0.9098 0.8410 1.0064 0.0109  -0.0866 0.0126  401 PRO A CA  
6012  C C   . PRO A 401 ? 0.8702 0.8031 0.9689 0.0107  -0.1028 0.0207  401 PRO A C   
6013  O O   . PRO A 401 ? 0.8726 0.8146 0.9758 0.0124  -0.1081 0.0262  401 PRO A O   
6014  C CB  . PRO A 401 ? 0.9047 0.8395 0.9758 0.0070  -0.0812 0.0190  401 PRO A CB  
6015  C CG  . PRO A 401 ? 0.9400 0.8842 1.0173 0.0095  -0.0736 0.0204  401 PRO A CG  
6016  C CD  . PRO A 401 ? 0.9662 0.9094 1.0700 0.0142  -0.0676 0.0104  401 PRO A CD  
6024  N N   . PRO A 402 ? 0.8725 0.7963 0.9674 0.0083  -0.1106 0.0214  402 PRO A N   
6025  C CA  . PRO A 402 ? 0.8719 0.7952 0.9686 0.0078  -0.1252 0.0299  402 PRO A CA  
6026  C C   . PRO A 402 ? 0.8348 0.7683 0.9176 0.0053  -0.1297 0.0413  402 PRO A C   
6027  O O   . PRO A 402 ? 0.8362 0.7729 0.9237 0.0070  -0.1389 0.0472  402 PRO A O   
6028  C CB  . PRO A 402 ? 0.8958 0.8076 0.9852 0.0037  -0.1294 0.0296  402 PRO A CB  
6029  C CG  . PRO A 402 ? 0.8895 0.7946 0.9824 0.0043  -0.1186 0.0173  402 PRO A CG  
6030  C CD  . PRO A 402 ? 0.8866 0.7994 0.9766 0.0060  -0.1058 0.0138  402 PRO A CD  
6038  N N   . SER A 403 ? 0.7946 0.7333 0.8602 0.0015  -0.1237 0.0443  403 SER A N   
6039  C CA  . SER A 403 ? 0.8199 0.7690 0.8743 -0.0010 -0.1268 0.0541  403 SER A CA  
6040  C C   . SER A 403 ? 0.7658 0.7126 0.8154 -0.0043 -0.1383 0.0628  403 SER A C   
6041  O O   . SER A 403 ? 0.7085 0.6627 0.7569 -0.0043 -0.1432 0.0696  403 SER A O   
6042  C CB  . SER A 403 ? 0.9284 0.8881 0.9927 0.0032  -0.1240 0.0538  403 SER A CB  
6043  O OG  . SER A 403 ? 1.0499 1.0083 1.1298 0.0075  -0.1315 0.0523  403 SER A OG  
6049  N N   . PHE A 404 ? 0.7836 0.7198 0.8305 -0.0074 -0.1421 0.0621  404 PHE A N   
6050  C CA  . PHE A 404 ? 0.7727 0.7051 0.8144 -0.0117 -0.1513 0.0707  404 PHE A CA  
6051  C C   . PHE A 404 ? 0.7860 0.7283 0.8137 -0.0167 -0.1509 0.0787  404 PHE A C   
6052  O O   . PHE A 404 ? 0.7550 0.6994 0.7735 -0.0199 -0.1468 0.0771  404 PHE A O   
6053  C CB  . PHE A 404 ? 0.7928 0.7122 0.8353 -0.0146 -0.1536 0.0668  404 PHE A CB  
6054  C CG  . PHE A 404 ? 0.7822 0.6970 0.8191 -0.0204 -0.1612 0.0755  404 PHE A CG  
6055  C CD1 . PHE A 404 ? 0.7725 0.6913 0.7977 -0.0265 -0.1602 0.0784  404 PHE A CD1 
6056  C CD2 . PHE A 404 ? 0.7984 0.7043 0.8431 -0.0196 -0.1694 0.0806  404 PHE A CD2 
6057  C CE1 . PHE A 404 ? 0.8117 0.7262 0.8345 -0.0323 -0.1661 0.0857  404 PHE A CE1 
6058  C CE2 . PHE A 404 ? 0.8048 0.7052 0.8446 -0.0254 -0.1751 0.0891  404 PHE A CE2 
6059  C CZ  . PHE A 404 ? 0.8027 0.7078 0.8326 -0.0321 -0.1728 0.0913  404 PHE A CZ  
6069  N N   . GLY A 405 ? 0.7744 0.7228 0.8005 -0.0172 -0.1553 0.0868  405 GLY A N   
6070  C CA  . GLY A 405 ? 0.7565 0.7154 0.7724 -0.0217 -0.1543 0.0938  405 GLY A CA  
6071  C C   . GLY A 405 ? 0.7695 0.7418 0.7862 -0.0185 -0.1497 0.0937  405 GLY A C   
6072  O O   . GLY A 405 ? 0.7593 0.7412 0.7697 -0.0218 -0.1489 0.0992  405 GLY A O   
6076  N N   . TYR A 406 ? 0.7748 0.7481 0.8010 -0.0125 -0.1464 0.0870  406 TYR A N   
6077  C CA  . TYR A 406 ? 0.7546 0.7402 0.7843 -0.0094 -0.1419 0.0860  406 TYR A CA  
6078  C C   . TYR A 406 ? 0.7635 0.7565 0.7895 -0.0106 -0.1469 0.0929  406 TYR A C   
6079  O O   . TYR A 406 ? 0.7935 0.7984 0.8187 -0.0105 -0.1431 0.0938  406 TYR A O   
6080  C CB  . TYR A 406 ? 0.7430 0.7271 0.7875 -0.0027 -0.1390 0.0776  406 TYR A CB  
6081  C CG  . TYR A 406 ? 0.7320 0.7277 0.7830 0.0004  -0.1323 0.0745  406 TYR A CG  
6082  C CD1 . TYR A 406 ? 0.6910 0.6951 0.7478 0.0031  -0.1361 0.0753  406 TYR A CD1 
6083  C CD2 . TYR A 406 ? 0.7863 0.7838 0.8372 0.0008  -0.1222 0.0707  406 TYR A CD2 
6084  C CE1 . TYR A 406 ? 0.7136 0.7282 0.7787 0.0058  -0.1298 0.0715  406 TYR A CE1 
6085  C CE2 . TYR A 406 ? 0.7911 0.7981 0.8497 0.0035  -0.1156 0.0683  406 TYR A CE2 
6086  C CZ  . TYR A 406 ? 0.7942 0.8101 0.8613 0.0060  -0.1194 0.0683  406 TYR A CZ  
6087  O OH  . TYR A 406 ? 0.8534 0.8788 0.9304 0.0086  -0.1127 0.0650  406 TYR A OH  
6097  N N   . SER A 407 ? 0.7686 0.7542 0.7919 -0.0116 -0.1550 0.0978  407 SER A N   
6098  C CA  . SER A 407 ? 0.7535 0.7439 0.7692 -0.0134 -0.1595 0.1052  407 SER A CA  
6099  C C   . SER A 407 ? 0.7570 0.7375 0.7638 -0.0190 -0.1646 0.1134  407 SER A C   
6100  O O   . SER A 407 ? 0.7501 0.7180 0.7603 -0.0190 -0.1681 0.1125  407 SER A O   
6101  C CB  . SER A 407 ? 0.7322 0.7232 0.7539 -0.0072 -0.1651 0.1030  407 SER A CB  
6102  O OG  . SER A 407 ? 0.8032 0.7810 0.8320 -0.0038 -0.1718 0.1013  407 SER A OG  
6108  N N   . MET A 408 ? 0.7559 0.7420 0.7523 -0.0240 -0.1642 0.1209  408 MET A N   
6109  C CA  . MET A 408 ? 0.7119 0.6891 0.7004 -0.0303 -0.1674 0.1294  408 MET A CA  
6110  C C   . MET A 408 ? 0.7154 0.6977 0.6924 -0.0331 -0.1679 0.1373  408 MET A C   
6111  O O   . MET A 408 ? 0.7254 0.7206 0.7008 -0.0316 -0.1644 0.1354  408 MET A O   
6112  C CB  . MET A 408 ? 0.7087 0.6870 0.6974 -0.0366 -0.1630 0.1293  408 MET A CB  
6113  C CG  . MET A 408 ? 0.7183 0.6899 0.7142 -0.0348 -0.1626 0.1218  408 MET A CG  
6114  S SD  . MET A 408 ? 0.7315 0.7043 0.7259 -0.0420 -0.1599 0.1213  408 MET A SD  
6115  C CE  . MET A 408 ? 0.6904 0.6820 0.6829 -0.0427 -0.1535 0.1212  408 MET A CE  
6125  N N   . LYS A 409 ? 0.7544 0.7258 0.7233 -0.0374 -0.1717 0.1462  409 LYS A N   
6126  C CA  . LYS A 409 ? 0.7658 0.7399 0.7209 -0.0415 -0.1707 0.1549  409 LYS A CA  
6127  C C   . LYS A 409 ? 0.8286 0.7898 0.7783 -0.0487 -0.1716 0.1644  409 LYS A C   
6128  O O   . LYS A 409 ? 0.9076 0.8534 0.8595 -0.0471 -0.1781 0.1670  409 LYS A O   
6129  C CB  . LYS A 409 ? 0.8010 0.7733 0.7483 -0.0354 -0.1772 0.1564  409 LYS A CB  
6130  C CG  . LYS A 409 ? 0.8409 0.8178 0.7708 -0.0392 -0.1750 0.1640  409 LYS A CG  
6131  C CD  . LYS A 409 ? 0.8830 0.8792 0.8147 -0.0403 -0.1665 0.1582  409 LYS A CD  
6132  C CE  . LYS A 409 ? 1.0050 1.0061 0.9194 -0.0448 -0.1628 0.1646  409 LYS A CE  
6133  N NZ  . LYS A 409 ? 1.0861 1.1062 1.0047 -0.0458 -0.1542 0.1580  409 LYS A NZ  
6147  N N   . GLY A 410 ? 0.8053 0.7729 0.7502 -0.0565 -0.1646 0.1690  410 GLY A N   
6148  C CA  . GLY A 410 ? 0.8042 0.7608 0.7455 -0.0643 -0.1636 0.1780  410 GLY A CA  
6149  C C   . GLY A 410 ? 0.8748 0.8343 0.8010 -0.0697 -0.1585 0.1870  410 GLY A C   
6150  O O   . GLY A 410 ? 0.8825 0.8474 0.7972 -0.0659 -0.1591 0.1877  410 GLY A O   
6154  N N   . ALA A 411 ? 0.8904 0.8460 0.8168 -0.0787 -0.1531 0.1935  411 ALA A N   
6155  C CA  . ALA A 411 ? 0.8414 0.7998 0.7550 -0.0858 -0.1453 0.2018  411 ALA A CA  
6156  C C   . ALA A 411 ? 0.8512 0.7949 0.7440 -0.0846 -0.1493 0.2130  411 ALA A C   
6157  O O   . ALA A 411 ? 0.8716 0.8191 0.7479 -0.0877 -0.1435 0.2185  411 ALA A O   
6158  C CB  . ALA A 411 ? 0.8120 0.7911 0.7248 -0.0853 -0.1382 0.1955  411 ALA A CB  
6164  N N   . THR A 412 ? 0.8507 0.7772 0.7431 -0.0800 -0.1593 0.2164  412 THR A N   
6165  C CA  . THR A 412 ? 0.8865 0.7965 0.7594 -0.0786 -0.1650 0.2284  412 THR A CA  
6166  C C   . THR A 412 ? 0.9100 0.7991 0.7890 -0.0816 -0.1692 0.2361  412 THR A C   
6167  O O   . THR A 412 ? 0.9078 0.7922 0.8043 -0.0778 -0.1753 0.2295  412 THR A O   
6168  C CB  . THR A 412 ? 0.8835 0.7933 0.7500 -0.0675 -0.1759 0.2245  412 THR A CB  
6169  O OG1 . THR A 412 ? 0.9176 0.8468 0.7794 -0.0651 -0.1715 0.2170  412 THR A OG1 
6170  C CG2 . THR A 412 ? 0.8882 0.7796 0.7334 -0.0653 -0.1839 0.2375  412 THR A CG2 
6178  N N   . ASP A 413 ? 0.9396 0.8158 0.8044 -0.0885 -0.1652 0.2499  413 ASP A N   
6179  C CA  . ASP A 413 ? 0.9901 0.8446 0.8602 -0.0922 -0.1683 0.2590  413 ASP A CA  
6180  C C   . ASP A 413 ? 1.0404 0.8769 0.8969 -0.0842 -0.1811 0.2673  413 ASP A C   
6181  O O   . ASP A 413 ? 1.1198 0.9448 0.9529 -0.0859 -0.1812 0.2810  413 ASP A O   
6182  C CB  . ASP A 413 ? 0.9916 0.8409 0.8551 -0.1042 -0.1562 0.2700  413 ASP A CB  
6183  C CG  . ASP A 413 ? 1.0326 0.8601 0.9056 -0.1090 -0.1581 0.2787  413 ASP A CG  
6184  O OD1 . ASP A 413 ? 1.0294 0.8489 0.9187 -0.1037 -0.1677 0.2733  413 ASP A OD1 
6185  O OD2 . ASP A 413 ? 1.0652 0.8831 0.9302 -0.1182 -0.1492 0.2906  413 ASP A OD2 
6190  N N   . ILE A 414 ? 1.0044 0.8381 0.8758 -0.0754 -0.1921 0.2590  414 ILE A N   
6191  C CA  . ILE A 414 ? 1.0295 0.8495 0.8913 -0.0661 -0.2059 0.2642  414 ILE A CA  
6192  C C   . ILE A 414 ? 1.0840 0.8777 0.9443 -0.0683 -0.2112 0.2781  414 ILE A C   
6193  O O   . ILE A 414 ? 1.1517 0.9307 0.9958 -0.0631 -0.2211 0.2886  414 ILE A O   
6194  C CB  . ILE A 414 ? 0.9815 0.8088 0.8623 -0.0558 -0.2147 0.2494  414 ILE A CB  
6195  C CG1 . ILE A 414 ? 1.0380 0.8551 0.9094 -0.0456 -0.2294 0.2533  414 ILE A CG1 
6196  C CG2 . ILE A 414 ? 0.9319 0.7519 0.8386 -0.0567 -0.2157 0.2428  414 ILE A CG2 
6197  C CD1 . ILE A 414 ? 1.0347 0.8614 0.9244 -0.0354 -0.2368 0.2381  414 ILE A CD1 
6209  N N   . ASP A 415 ? 1.0954 0.8823 0.9730 -0.0756 -0.2056 0.2783  415 ASP A N   
6210  C CA  . ASP A 415 ? 1.1149 0.8764 0.9940 -0.0786 -0.2093 0.2914  415 ASP A CA  
6211  C C   . ASP A 415 ? 1.1341 0.8878 0.9969 -0.0900 -0.1978 0.3065  415 ASP A C   
6212  O O   . ASP A 415 ? 1.2096 0.9419 1.0744 -0.0943 -0.1984 0.3184  415 ASP A O   
6213  C CB  . ASP A 415 ? 1.1403 0.8970 1.0503 -0.0797 -0.2106 0.2819  415 ASP A CB  
6214  C CG  . ASP A 415 ? 1.2047 0.9753 1.1282 -0.0893 -0.1979 0.2738  415 ASP A CG  
6215  O OD1 . ASP A 415 ? 1.2086 0.9966 1.1216 -0.0933 -0.1887 0.2722  415 ASP A OD1 
6216  O OD2 . ASP A 415 ? 1.2314 0.9958 1.1770 -0.0925 -0.1976 0.2684  415 ASP A OD2 
6221  N N   . LYS A 416 ? 1.1244 0.8947 0.9725 -0.0951 -0.1867 0.3060  416 LYS A N   
6222  C CA  . LYS A 416 ? 1.2033 0.9679 1.0347 -0.1061 -0.1739 0.3197  416 LYS A CA  
6223  C C   . LYS A 416 ? 1.2010 0.9571 1.0541 -0.1164 -0.1657 0.3218  416 LYS A C   
6224  O O   . LYS A 416 ? 1.2555 0.9955 1.0990 -0.1245 -0.1587 0.3368  416 LYS A O   
6225  C CB  . LYS A 416 ? 1.3571 1.1007 1.1574 -0.1039 -0.1794 0.3383  416 LYS A CB  
6226  C CG  . LYS A 416 ? 1.4885 1.2422 1.2614 -0.0968 -0.1839 0.3378  416 LYS A CG  
6227  C CD  . LYS A 416 ? 1.5800 1.3507 1.3374 -0.1049 -0.1676 0.3372  416 LYS A CD  
6228  C CE  . LYS A 416 ? 1.6172 1.3949 1.3439 -0.0986 -0.1717 0.3381  416 LYS A CE  
6229  N NZ  . LYS A 416 ? 1.6102 1.4037 1.3220 -0.1069 -0.1548 0.3371  416 LYS A NZ  
6243  N N   . ASN A 417 ? 1.1604 0.9269 1.0427 -0.1164 -0.1663 0.3067  417 ASN A N   
6244  C CA  . ASN A 417 ? 1.1269 0.8873 1.0326 -0.1257 -0.1599 0.3058  417 ASN A CA  
6245  C C   . ASN A 417 ? 1.0688 0.8482 0.9821 -0.1357 -0.1453 0.3001  417 ASN A C   
6246  O O   . ASN A 417 ? 1.0598 0.8369 0.9945 -0.1440 -0.1396 0.2978  417 ASN A O   
6247  C CB  . ASN A 417 ? 1.0936 0.8532 1.0265 -0.1204 -0.1693 0.2919  417 ASN A CB  
6248  C CG  . ASN A 417 ? 1.0721 0.8568 1.0192 -0.1192 -0.1669 0.2733  417 ASN A CG  
6249  O OD1 . ASN A 417 ? 1.0949 0.8974 1.0302 -0.1158 -0.1648 0.2687  417 ASN A OD1 
6250  N ND2 . ASN A 417 ? 1.0561 0.8417 1.0283 -0.1218 -0.1676 0.2625  417 ASN A ND2 
6257  N N   . GLY A 418 ? 1.0116 0.8099 0.9101 -0.1349 -0.1396 0.2969  418 GLY A N   
6258  C CA  . GLY A 418 ? 0.9812 0.7980 0.8875 -0.1437 -0.1259 0.2916  418 GLY A CA  
6259  C C   . GLY A 418 ? 0.9794 0.8193 0.9056 -0.1408 -0.1274 0.2731  418 GLY A C   
6260  O O   . GLY A 418 ? 0.9526 0.8086 0.8890 -0.1476 -0.1174 0.2677  418 GLY A O   
6264  N N   . TYR A 419 ? 1.0300 0.8715 0.9623 -0.1308 -0.1393 0.2635  419 TYR A N   
6265  C CA  . TYR A 419 ? 1.0380 0.8989 0.9870 -0.1275 -0.1410 0.2468  419 TYR A CA  
6266  C C   . TYR A 419 ? 1.0330 0.9016 0.9718 -0.1158 -0.1489 0.2405  419 TYR A C   
6267  O O   . TYR A 419 ? 1.0569 0.9119 0.9890 -0.1086 -0.1584 0.2439  419 TYR A O   
6268  C CB  . TYR A 419 ? 1.0477 0.9017 1.0207 -0.1286 -0.1462 0.2389  419 TYR A CB  
6269  C CG  . TYR A 419 ? 1.0343 0.8834 1.0225 -0.1404 -0.1385 0.2423  419 TYR A CG  
6270  C CD1 . TYR A 419 ? 1.0626 0.8908 1.0473 -0.1462 -0.1360 0.2563  419 TYR A CD1 
6271  C CD2 . TYR A 419 ? 0.9807 0.8458 0.9878 -0.1458 -0.1341 0.2315  419 TYR A CD2 
6272  C CE1 . TYR A 419 ? 1.0535 0.8771 1.0547 -0.1574 -0.1280 0.2591  419 TYR A CE1 
6273  C CE2 . TYR A 419 ? 0.9842 0.8459 1.0085 -0.1566 -0.1275 0.2334  419 TYR A CE2 
6274  C CZ  . TYR A 419 ? 1.0077 0.8488 1.0297 -0.1627 -0.1238 0.2470  419 TYR A CZ  
6275  O OH  . TYR A 419 ? 0.9857 0.8232 1.0273 -0.1739 -0.1163 0.2484  419 TYR A OH  
6285  N N   . PRO A 420 ? 1.0069 0.8968 0.9461 -0.1135 -0.1455 0.2312  420 PRO A N   
6286  C CA  . PRO A 420 ? 0.9378 0.8351 0.8690 -0.1028 -0.1521 0.2251  420 PRO A CA  
6287  C C   . PRO A 420 ? 0.9280 0.8205 0.8725 -0.0955 -0.1616 0.2157  420 PRO A C   
6288  O O   . PRO A 420 ? 0.9746 0.8658 0.9359 -0.0983 -0.1619 0.2093  420 PRO A O   
6289  C CB  . PRO A 420 ? 0.9079 0.8287 0.8413 -0.1037 -0.1447 0.2169  420 PRO A CB  
6290  C CG  . PRO A 420 ? 0.9543 0.8791 0.8916 -0.1148 -0.1339 0.2215  420 PRO A CG  
6291  C CD  . PRO A 420 ? 0.9865 0.8945 0.9348 -0.1204 -0.1355 0.2260  420 PRO A CD  
6299  N N   . ASP A 421 ? 0.9121 0.8024 0.8495 -0.0860 -0.1691 0.2140  421 ASP A N   
6300  C CA  . ASP A 421 ? 0.8999 0.7845 0.8493 -0.0784 -0.1776 0.2054  421 ASP A CA  
6301  C C   . ASP A 421 ? 0.8556 0.7566 0.8068 -0.0709 -0.1779 0.1941  421 ASP A C   
6302  O O   . ASP A 421 ? 0.8530 0.7678 0.7950 -0.0705 -0.1735 0.1940  421 ASP A O   
6303  C CB  . ASP A 421 ? 0.9220 0.7868 0.8659 -0.0734 -0.1870 0.2134  421 ASP A CB  
6304  C CG  . ASP A 421 ? 0.9657 0.8128 0.9059 -0.0810 -0.1859 0.2267  421 ASP A CG  
6305  O OD1 . ASP A 421 ? 0.9818 0.8259 0.9354 -0.0880 -0.1818 0.2249  421 ASP A OD1 
6306  O OD2 . ASP A 421 ? 1.0157 0.8515 0.9391 -0.0801 -0.1890 0.2391  421 ASP A OD2 
6311  N N   . LEU A 422 ? 0.8621 0.7609 0.8259 -0.0651 -0.1825 0.1841  422 LEU A N   
6312  C CA  . LEU A 422 ? 0.8763 0.7896 0.8449 -0.0591 -0.1811 0.1726  422 LEU A CA  
6313  C C   . LEU A 422 ? 0.9255 0.8321 0.8994 -0.0496 -0.1886 0.1675  422 LEU A C   
6314  O O   . LEU A 422 ? 0.9678 0.8599 0.9502 -0.0480 -0.1939 0.1668  422 LEU A O   
6315  C CB  . LEU A 422 ? 0.8703 0.7901 0.8502 -0.0621 -0.1770 0.1633  422 LEU A CB  
6316  C CG  . LEU A 422 ? 0.8643 0.7955 0.8492 -0.0560 -0.1753 0.1517  422 LEU A CG  
6317  C CD1 . LEU A 422 ? 0.8493 0.7970 0.8275 -0.0544 -0.1707 0.1520  422 LEU A CD1 
6318  C CD2 . LEU A 422 ? 0.8824 0.8164 0.8750 -0.0591 -0.1726 0.1439  422 LEU A CD2 
6330  N N   . ILE A 423 ? 0.9260 0.8437 0.8973 -0.0434 -0.1886 0.1631  423 ILE A N   
6331  C CA  . ILE A 423 ? 0.8987 0.8138 0.8791 -0.0342 -0.1942 0.1555  423 ILE A CA  
6332  C C   . ILE A 423 ? 0.9040 0.8307 0.8944 -0.0320 -0.1880 0.1432  423 ILE A C   
6333  O O   . ILE A 423 ? 0.9172 0.8585 0.9037 -0.0339 -0.1815 0.1413  423 ILE A O   
6334  C CB  . ILE A 423 ? 0.8868 0.8055 0.8590 -0.0285 -0.1993 0.1584  423 ILE A CB  
6335  C CG1 . ILE A 423 ? 1.0050 0.9118 0.9620 -0.0312 -0.2049 0.1722  423 ILE A CG1 
6336  C CG2 . ILE A 423 ? 0.8148 0.7304 0.8007 -0.0191 -0.2059 0.1498  423 ILE A CG2 
6337  C CD1 . ILE A 423 ? 1.0649 0.9760 1.0089 -0.0264 -0.2100 0.1755  423 ILE A CD1 
6349  N N   . VAL A 424 ? 0.8869 0.8066 0.8901 -0.0279 -0.1897 0.1348  424 VAL A N   
6350  C CA  . VAL A 424 ? 0.8151 0.7430 0.8263 -0.0253 -0.1835 0.1234  424 VAL A CA  
6351  C C   . VAL A 424 ? 0.8319 0.7578 0.8552 -0.0166 -0.1865 0.1158  424 VAL A C   
6352  O O   . VAL A 424 ? 0.8458 0.7588 0.8777 -0.0136 -0.1929 0.1150  424 VAL A O   
6353  C CB  . VAL A 424 ? 0.7851 0.7070 0.8004 -0.0294 -0.1806 0.1185  424 VAL A CB  
6354  C CG1 . VAL A 424 ? 0.8022 0.7314 0.8220 -0.0264 -0.1738 0.1074  424 VAL A CG1 
6355  C CG2 . VAL A 424 ? 0.7908 0.7154 0.7977 -0.0380 -0.1784 0.1252  424 VAL A CG2 
6365  N N   . GLY A 425 ? 0.8193 0.7576 0.8452 -0.0127 -0.1818 0.1099  425 GLY A N   
6366  C CA  . GLY A 425 ? 0.7790 0.7175 0.8193 -0.0048 -0.1831 0.1013  425 GLY A CA  
6367  C C   . GLY A 425 ? 0.7402 0.6788 0.7905 -0.0034 -0.1749 0.0903  425 GLY A C   
6368  O O   . GLY A 425 ? 0.7384 0.6824 0.7818 -0.0074 -0.1673 0.0889  425 GLY A O   
6372  N N   . ALA A 426 ? 0.7394 0.6715 0.8060 0.0023  -0.1767 0.0823  426 ALA A N   
6373  C CA  . ALA A 426 ? 0.7593 0.6910 0.8363 0.0043  -0.1676 0.0708  426 ALA A CA  
6374  C C   . ALA A 426 ? 0.7853 0.7196 0.8816 0.0120  -0.1683 0.0628  426 ALA A C   
6375  O O   . ALA A 426 ? 0.8356 0.7608 0.9472 0.0161  -0.1738 0.0584  426 ALA A O   
6376  C CB  . ALA A 426 ? 0.7678 0.6862 0.8477 0.0021  -0.1677 0.0672  426 ALA A CB  
6382  N N   . PHE A 427 ? 0.7351 0.6820 0.8329 0.0140  -0.1627 0.0604  427 PHE A N   
6383  C CA  . PHE A 427 ? 0.7498 0.7008 0.8677 0.0211  -0.1641 0.0527  427 PHE A CA  
6384  C C   . PHE A 427 ? 0.8050 0.7524 0.9414 0.0240  -0.1548 0.0402  427 PHE A C   
6385  O O   . PHE A 427 ? 0.8413 0.7884 0.9998 0.0300  -0.1576 0.0326  427 PHE A O   
6386  C CB  . PHE A 427 ? 0.7524 0.7182 0.8679 0.0220  -0.1610 0.0536  427 PHE A CB  
6387  C CG  . PHE A 427 ? 0.7300 0.7029 0.8442 0.0201  -0.1465 0.0492  427 PHE A CG  
6388  C CD1 . PHE A 427 ? 0.7082 0.6835 0.8414 0.0242  -0.1378 0.0386  427 PHE A CD1 
6389  C CD2 . PHE A 427 ? 0.6997 0.6767 0.7946 0.0144  -0.1418 0.0560  427 PHE A CD2 
6390  C CE1 . PHE A 427 ? 0.6847 0.6649 0.8150 0.0225  -0.1241 0.0360  427 PHE A CE1 
6391  C CE2 . PHE A 427 ? 0.6802 0.6626 0.7730 0.0132  -0.1297 0.0532  427 PHE A CE2 
6392  C CZ  . PHE A 427 ? 0.6926 0.6759 0.8018 0.0172  -0.1206 0.0437  427 PHE A CZ  
6402  N N   . GLY A 428 ? 0.7965 0.7410 0.9244 0.0200  -0.1439 0.0376  428 GLY A N   
6403  C CA  . GLY A 428 ? 0.8075 0.7475 0.9503 0.0222  -0.1335 0.0256  428 GLY A CA  
6404  C C   . GLY A 428 ? 0.7672 0.6953 0.9262 0.0250  -0.1396 0.0199  428 GLY A C   
6405  O O   . GLY A 428 ? 0.7493 0.6749 0.9293 0.0288  -0.1334 0.0085  428 GLY A O   
6409  N N   . VAL A 429 ? 0.7887 0.7090 0.9401 0.0230  -0.1512 0.0276  429 VAL A N   
6410  C CA  . VAL A 429 ? 0.8363 0.7443 1.0037 0.0258  -0.1591 0.0239  429 VAL A CA  
6411  C C   . VAL A 429 ? 0.8918 0.7982 1.0651 0.0298  -0.1753 0.0314  429 VAL A C   
6412  O O   . VAL A 429 ? 0.9305 0.8253 1.1136 0.0317  -0.1848 0.0322  429 VAL A O   
6413  C CB  . VAL A 429 ? 0.8160 0.7129 0.9715 0.0202  -0.1587 0.0257  429 VAL A CB  
6414  C CG1 . VAL A 429 ? 0.8224 0.7188 0.9737 0.0175  -0.1436 0.0158  429 VAL A CG1 
6415  C CG2 . VAL A 429 ? 0.8234 0.7220 0.9546 0.0143  -0.1645 0.0395  429 VAL A CG2 
6425  N N   . ASP A 430 ? 0.8792 0.7965 1.0462 0.0311  -0.1790 0.0370  430 ASP A N   
6426  C CA  . ASP A 430 ? 0.8247 0.7411 0.9946 0.0355  -0.1944 0.0435  430 ASP A CA  
6427  C C   . ASP A 430 ? 0.8618 0.7660 1.0177 0.0322  -0.2049 0.0554  430 ASP A C   
6428  O O   . ASP A 430 ? 0.8523 0.7464 1.0181 0.0364  -0.2173 0.0577  430 ASP A O   
6429  C CB  . ASP A 430 ? 0.7890 0.7037 0.9896 0.0438  -0.1999 0.0330  430 ASP A CB  
6430  C CG  . ASP A 430 ? 0.8669 0.7932 1.0844 0.0466  -0.1882 0.0207  430 ASP A CG  
6431  O OD1 . ASP A 430 ? 0.8882 0.8267 1.0988 0.0466  -0.1865 0.0227  430 ASP A OD1 
6432  O OD2 . ASP A 430 ? 0.8998 0.8229 1.1381 0.0485  -0.1797 0.0088  430 ASP A OD2 
6437  N N   . ARG A 431 ? 0.8961 0.8008 1.0294 0.0246  -0.1999 0.0632  431 ARG A N   
6438  C CA  . ARG A 431 ? 0.9613 0.8543 1.0819 0.0199  -0.2068 0.0739  431 ARG A CA  
6439  C C   . ARG A 431 ? 0.9104 0.8102 1.0060 0.0139  -0.2064 0.0859  431 ARG A C   
6440  O O   . ARG A 431 ? 0.8712 0.7842 0.9587 0.0119  -0.1980 0.0844  431 ARG A O   
6441  C CB  . ARG A 431 ? 1.0505 0.9347 1.1735 0.0155  -0.1999 0.0688  431 ARG A CB  
6442  C CG  . ARG A 431 ? 1.1567 1.0243 1.2829 0.0141  -0.2090 0.0744  431 ARG A CG  
6443  C CD  . ARG A 431 ? 1.2117 1.0698 1.3643 0.0213  -0.2144 0.0657  431 ARG A CD  
6444  N NE  . ARG A 431 ? 1.2455 1.1047 1.4120 0.0219  -0.2029 0.0503  431 ARG A NE  
6445  C CZ  . ARG A 431 ? 1.2904 1.1446 1.4830 0.0279  -0.2033 0.0389  431 ARG A CZ  
6446  N NH1 . ARG A 431 ? 1.3030 1.1506 1.5121 0.0344  -0.2164 0.0411  431 ARG A NH1 
6447  N NH2 . ARG A 431 ? 1.3065 1.1618 1.5084 0.0275  -0.1906 0.0251  431 ARG A NH2 
6461  N N   . ALA A 432 ? 0.8850 0.7752 0.9697 0.0112  -0.2151 0.0978  432 ALA A N   
6462  C CA  . ALA A 432 ? 0.8294 0.7238 0.8914 0.0044  -0.2138 0.1095  432 ALA A CA  
6463  C C   . ALA A 432 ? 0.8705 0.7499 0.9270 -0.0010 -0.2179 0.1185  432 ALA A C   
6464  O O   . ALA A 432 ? 0.9105 0.7759 0.9751 0.0023  -0.2273 0.1215  432 ALA A O   
6465  C CB  . ALA A 432 ? 0.7935 0.6941 0.8448 0.0072  -0.2205 0.1165  432 ALA A CB  
6471  N N   . ILE A 433 ? 0.8816 0.7637 0.9261 -0.0092 -0.2111 0.1225  433 ILE A N   
6472  C CA  . ILE A 433 ? 0.8973 0.7662 0.9402 -0.0153 -0.2127 0.1285  433 ILE A CA  
6473  C C   . ILE A 433 ? 0.8900 0.7613 0.9143 -0.0225 -0.2115 0.1415  433 ILE A C   
6474  O O   . ILE A 433 ? 0.8890 0.7748 0.9036 -0.0256 -0.2047 0.1415  433 ILE A O   
6475  C CB  . ILE A 433 ? 0.9538 0.8226 1.0040 -0.0189 -0.2052 0.1185  433 ILE A CB  
6476  C CG1 . ILE A 433 ? 1.0268 0.8943 1.0943 -0.0121 -0.2038 0.1047  433 ILE A CG1 
6477  C CG2 . ILE A 433 ? 0.9715 0.8261 1.0236 -0.0249 -0.2077 0.1232  433 ILE A CG2 
6478  C CD1 . ILE A 433 ? 1.0953 0.9782 1.1620 -0.0094 -0.1952 0.0960  433 ILE A CD1 
6490  N N   . LEU A 434 ? 0.9260 0.7826 0.9463 -0.0252 -0.2176 0.1525  434 LEU A N   
6491  C CA  . LEU A 434 ? 0.9175 0.7736 0.9216 -0.0331 -0.2153 0.1653  434 LEU A CA  
6492  C C   . LEU A 434 ? 0.8819 0.7296 0.8918 -0.0410 -0.2118 0.1661  434 LEU A C   
6493  O O   . LEU A 434 ? 0.8608 0.6927 0.8821 -0.0402 -0.2169 0.1659  434 LEU A O   
6494  C CB  . LEU A 434 ? 0.9871 0.8316 0.9799 -0.0311 -0.2239 0.1788  434 LEU A CB  
6495  C CG  . LEU A 434 ? 1.0661 0.9060 1.0420 -0.0399 -0.2205 0.1932  434 LEU A CG  
6496  C CD1 . LEU A 434 ? 1.0457 0.9045 1.0080 -0.0438 -0.2117 0.1933  434 LEU A CD1 
6497  C CD2 . LEU A 434 ? 1.1555 0.9791 1.1197 -0.0375 -0.2298 0.2072  434 LEU A CD2 
6509  N N   . TYR A 435 ? 0.8774 0.7358 0.8814 -0.0483 -0.2037 0.1662  435 TYR A N   
6510  C CA  . TYR A 435 ? 0.8815 0.7341 0.8911 -0.0567 -0.2005 0.1669  435 TYR A CA  
6511  C C   . TYR A 435 ? 0.8880 0.7373 0.8862 -0.0643 -0.1982 0.1812  435 TYR A C   
6512  O O   . TYR A 435 ? 0.8768 0.7388 0.8626 -0.0664 -0.1932 0.1852  435 TYR A O   
6513  C CB  . TYR A 435 ? 0.9085 0.7755 0.9217 -0.0595 -0.1938 0.1559  435 TYR A CB  
6514  C CG  . TYR A 435 ? 0.9315 0.8003 0.9541 -0.0532 -0.1941 0.1418  435 TYR A CG  
6515  C CD1 . TYR A 435 ? 0.9210 0.8014 0.9409 -0.0466 -0.1921 0.1360  435 TYR A CD1 
6516  C CD2 . TYR A 435 ? 0.9623 0.8209 0.9970 -0.0542 -0.1956 0.1338  435 TYR A CD2 
6517  C CE1 . TYR A 435 ? 0.9108 0.7922 0.9391 -0.0414 -0.1906 0.1234  435 TYR A CE1 
6518  C CE2 . TYR A 435 ? 0.9660 0.8259 1.0078 -0.0489 -0.1944 0.1206  435 TYR A CE2 
6519  C CZ  . TYR A 435 ? 0.9135 0.7846 0.9518 -0.0426 -0.1914 0.1158  435 TYR A CZ  
6520  O OH  . TYR A 435 ? 0.8715 0.7431 0.9166 -0.0379 -0.1886 0.1029  435 TYR A OH  
6530  N N   . ARG A 436 ? 0.9145 0.7464 0.9174 -0.0685 -0.2009 0.1887  436 ARG A N   
6531  C CA  . ARG A 436 ? 0.9460 0.7720 0.9389 -0.0766 -0.1974 0.2030  436 ARG A CA  
6532  C C   . ARG A 436 ? 0.9355 0.7665 0.9373 -0.0864 -0.1901 0.2000  436 ARG A C   
6533  O O   . ARG A 436 ? 0.9136 0.7427 0.9309 -0.0873 -0.1911 0.1897  436 ARG A O   
6534  C CB  . ARG A 436 ? 1.0070 0.8097 1.0000 -0.0758 -0.2043 0.2146  436 ARG A CB  
6535  C CG  . ARG A 436 ? 1.0687 0.8657 1.0536 -0.0657 -0.2136 0.2181  436 ARG A CG  
6536  C CD  . ARG A 436 ? 1.1411 0.9150 1.1206 -0.0658 -0.2203 0.2335  436 ARG A CD  
6537  N NE  . ARG A 436 ? 1.1951 0.9523 1.1952 -0.0671 -0.2238 0.2313  436 ARG A NE  
6538  C CZ  . ARG A 436 ? 1.3101 1.0451 1.3106 -0.0693 -0.2281 0.2445  436 ARG A CZ  
6539  N NH1 . ARG A 436 ? 1.3693 1.0958 1.3482 -0.0704 -0.2293 0.2615  436 ARG A NH1 
6540  N NH2 . ARG A 436 ? 1.3512 1.0722 1.3733 -0.0703 -0.2310 0.2405  436 ARG A NH2 
6554  N N   . ALA A 437 ? 0.9239 0.7614 0.9164 -0.0937 -0.1827 0.2083  437 ALA A N   
6555  C CA  . ALA A 437 ? 0.9385 0.7830 0.9410 -0.1033 -0.1756 0.2053  437 ALA A CA  
6556  C C   . ALA A 437 ? 0.9710 0.7972 0.9820 -0.1110 -0.1749 0.2141  437 ALA A C   
6557  O O   . ALA A 437 ? 0.9046 0.7181 0.9043 -0.1131 -0.1739 0.2286  437 ALA A O   
6558  C CB  . ALA A 437 ? 0.9292 0.7909 0.9213 -0.1076 -0.1669 0.2087  437 ALA A CB  
6564  N N   . ARG A 438 ? 1.0242 0.8483 1.0543 -0.1152 -0.1754 0.2052  438 ARG A N   
6565  C CA  . ARG A 438 ? 1.0591 0.8667 1.1018 -0.1232 -0.1742 0.2114  438 ARG A CA  
6566  C C   . ARG A 438 ? 1.0552 0.8698 1.0993 -0.1342 -0.1640 0.2177  438 ARG A C   
6567  O O   . ARG A 438 ? 1.0578 0.8923 1.1022 -0.1361 -0.1594 0.2109  438 ARG A O   
6568  C CB  . ARG A 438 ? 1.0988 0.9024 1.1627 -0.1236 -0.1789 0.1975  438 ARG A CB  
6569  C CG  . ARG A 438 ? 1.1397 0.9360 1.2057 -0.1135 -0.1875 0.1896  438 ARG A CG  
6570  C CD  . ARG A 438 ? 1.1469 0.9462 1.2294 -0.1134 -0.1903 0.1721  438 ARG A CD  
6571  N NE  . ARG A 438 ? 1.1429 0.9301 1.2442 -0.1214 -0.1902 0.1711  438 ARG A NE  
6572  C CZ  . ARG A 438 ? 1.1277 0.9151 1.2446 -0.1228 -0.1930 0.1560  438 ARG A CZ  
6573  N NH1 . ARG A 438 ? 1.1280 0.9264 1.2416 -0.1167 -0.1954 0.1416  438 ARG A NH1 
6574  N NH2 . ARG A 438 ? 1.1371 0.9133 1.2726 -0.1305 -0.1929 0.1553  438 ARG A NH2 
6588  N N   . PRO A 439 ? 1.0507 0.8492 1.0969 -0.1416 -0.1599 0.2305  439 PRO A N   
6589  C CA  . PRO A 439 ? 1.0449 0.8497 1.0958 -0.1529 -0.1487 0.2357  439 PRO A CA  
6590  C C   . PRO A 439 ? 1.0096 0.8237 1.0863 -0.1590 -0.1479 0.2219  439 PRO A C   
6591  O O   . PRO A 439 ? 0.9994 0.8069 1.0916 -0.1571 -0.1552 0.2121  439 PRO A O   
6592  C CB  . PRO A 439 ? 1.0972 0.8783 1.1444 -0.1585 -0.1451 0.2531  439 PRO A CB  
6593  C CG  . PRO A 439 ? 1.1032 0.8653 1.1556 -0.1517 -0.1562 0.2527  439 PRO A CG  
6594  C CD  . PRO A 439 ? 1.0605 0.8338 1.1047 -0.1398 -0.1648 0.2420  439 PRO A CD  
6602  N N   . VAL A 440 ? 1.0007 0.8308 1.0826 -0.1663 -0.1391 0.2206  440 VAL A N   
6603  C CA  . VAL A 440 ? 0.9933 0.8367 1.0987 -0.1713 -0.1393 0.2064  440 VAL A CA  
6604  C C   . VAL A 440 ? 1.0194 0.8555 1.1443 -0.1839 -0.1311 0.2119  440 VAL A C   
6605  O O   . VAL A 440 ? 1.0478 0.8834 1.1660 -0.1904 -0.1200 0.2240  440 VAL A O   
6606  C CB  . VAL A 440 ? 0.9741 0.8430 1.0754 -0.1694 -0.1369 0.1988  440 VAL A CB  
6607  C CG1 . VAL A 440 ? 0.9559 0.8380 1.0817 -0.1742 -0.1388 0.1846  440 VAL A CG1 
6608  C CG2 . VAL A 440 ? 0.9642 0.8393 1.0477 -0.1573 -0.1441 0.1937  440 VAL A CG2 
6618  N N   . ILE A 441 ? 1.0182 0.8487 1.1673 -0.1876 -0.1359 0.2023  441 ILE A N   
6619  C CA  . ILE A 441 ? 1.0494 0.8736 1.2228 -0.1999 -0.1289 0.2046  441 ILE A CA  
6620  C C   . ILE A 441 ? 1.0728 0.9190 1.2671 -0.2045 -0.1286 0.1899  441 ILE A C   
6621  O O   . ILE A 441 ? 1.0505 0.9036 1.2555 -0.2007 -0.1389 0.1741  441 ILE A O   
6622  C CB  . ILE A 441 ? 1.0535 0.8558 1.2430 -0.2014 -0.1348 0.2031  441 ILE A CB  
6623  C CG1 . ILE A 441 ? 1.0511 0.8315 1.2207 -0.1954 -0.1370 0.2174  441 ILE A CG1 
6624  C CG2 . ILE A 441 ? 1.0919 0.8875 1.3087 -0.2146 -0.1265 0.2058  441 ILE A CG2 
6625  C CD1 . ILE A 441 ? 1.0581 0.8175 1.2436 -0.1944 -0.1447 0.2143  441 ILE A CD1 
6637  N N   . THR A 442 ? 1.1172 0.9744 1.3172 -0.2124 -0.1172 0.1948  442 THR A N   
6638  C CA  . THR A 442 ? 1.1348 1.0113 1.3607 -0.2182 -0.1166 0.1817  442 THR A CA  
6639  C C   . THR A 442 ? 1.1344 1.0005 1.3922 -0.2285 -0.1152 0.1783  442 THR A C   
6640  O O   . THR A 442 ? 1.1136 0.9634 1.3752 -0.2363 -0.1051 0.1914  442 THR A O   
6641  C CB  . THR A 442 ? 1.1740 1.0668 1.3972 -0.2229 -0.1042 0.1873  442 THR A CB  
6642  O OG1 . THR A 442 ? 1.1596 1.0627 1.3552 -0.2131 -0.1062 0.1889  442 THR A OG1 
6643  C CG2 . THR A 442 ? 1.1829 1.0957 1.4369 -0.2289 -0.1043 0.1735  442 THR A CG2 
6651  N N   . VAL A 443 ? 1.1311 1.0060 1.4112 -0.2286 -0.1253 0.1608  443 VAL A N   
6652  C CA  . VAL A 443 ? 1.1299 0.9956 1.4424 -0.2373 -0.1266 0.1541  443 VAL A CA  
6653  C C   . VAL A 443 ? 1.0986 0.9849 1.4410 -0.2445 -0.1259 0.1417  443 VAL A C   
6654  O O   . VAL A 443 ? 1.0676 0.9735 1.4082 -0.2388 -0.1343 0.1298  443 VAL A O   
6655  C CB  . VAL A 443 ? 1.1267 0.9821 1.4412 -0.2310 -0.1411 0.1422  443 VAL A CB  
6656  C CG1 . VAL A 443 ? 1.1269 0.9735 1.4771 -0.2402 -0.1427 0.1337  443 VAL A CG1 
6657  C CG2 . VAL A 443 ? 1.1410 0.9763 1.4295 -0.2237 -0.1421 0.1540  443 VAL A CG2 
6667  N N   . ASN A 444 ? 1.1090 0.9904 1.4797 -0.2568 -0.1158 0.1449  444 ASN A N   
6668  C CA  . ASN A 444 ? 1.1123 1.0116 1.5185 -0.2650 -0.1148 0.1327  444 ASN A CA  
6669  C C   . ASN A 444 ? 1.0831 0.9732 1.5216 -0.2705 -0.1225 0.1203  444 ASN A C   
6670  O O   . ASN A 444 ? 1.1184 0.9891 1.5701 -0.2784 -0.1143 0.1286  444 ASN A O   
6671  C CB  . ASN A 444 ? 1.1825 1.0848 1.5994 -0.2758 -0.0953 0.1447  444 ASN A CB  
6672  C CG  . ASN A 444 ? 1.2390 1.1593 1.6350 -0.2714 -0.0893 0.1495  444 ASN A CG  
6673  O OD1 . ASN A 444 ? 1.2740 1.1904 1.6337 -0.2625 -0.0903 0.1583  444 ASN A OD1 
6674  N ND2 . ASN A 444 ? 1.2353 1.1756 1.6563 -0.2778 -0.0831 0.1430  444 ASN A ND2 
6681  N N   . ALA A 445 ? 1.0119 0.9153 1.4625 -0.2663 -0.1382 0.1006  445 ALA A N   
6682  C CA  . ALA A 445 ? 0.9545 0.8518 1.4354 -0.2707 -0.1477 0.0855  445 ALA A CA  
6683  C C   . ALA A 445 ? 0.9118 0.8281 1.4325 -0.2790 -0.1489 0.0720  445 ALA A C   
6684  O O   . ALA A 445 ? 0.8948 0.8318 1.4167 -0.2783 -0.1471 0.0705  445 ALA A O   
6685  C CB  . ALA A 445 ? 0.9426 0.8391 1.4069 -0.2596 -0.1659 0.0715  445 ALA A CB  
6691  N N   . GLY A 446 ? 0.9075 0.8167 1.4631 -0.2868 -0.1523 0.0614  446 GLY A N   
6692  C CA  . GLY A 446 ? 0.9332 0.8594 1.5316 -0.2950 -0.1551 0.0465  446 GLY A CA  
6693  C C   . GLY A 446 ? 1.0131 0.9334 1.6384 -0.2972 -0.1690 0.0277  446 GLY A C   
6694  O O   . GLY A 446 ? 1.0798 0.9782 1.7033 -0.2981 -0.1686 0.0304  446 GLY A O   
6698  N N   . LEU A 447 ? 0.9938 0.9340 1.6450 -0.2980 -0.1820 0.0079  447 LEU A N   
6699  C CA  . LEU A 447 ? 0.9659 0.9040 1.6432 -0.2997 -0.1975 -0.0132 447 LEU A CA  
6700  C C   . LEU A 447 ? 0.9899 0.9475 1.7144 -0.3081 -0.2013 -0.0282 447 LEU A C   
6701  O O   . LEU A 447 ? 1.0152 0.9951 1.7391 -0.3042 -0.2076 -0.0335 447 LEU A O   
6702  C CB  . LEU A 447 ? 0.9236 0.8649 1.5693 -0.2865 -0.2175 -0.0262 447 LEU A CB  
6703  C CG  . LEU A 447 ? 0.9415 0.8800 1.6075 -0.2869 -0.2347 -0.0494 447 LEU A CG  
6704  C CD1 . LEU A 447 ? 0.9625 0.8753 1.6406 -0.2926 -0.2280 -0.0465 447 LEU A CD1 
6705  C CD2 . LEU A 447 ? 0.9535 0.8979 1.5836 -0.2737 -0.2529 -0.0614 447 LEU A CD2 
6717  N N   . GLU A 448 ? 1.0023 0.9517 1.7697 -0.3194 -0.1978 -0.0352 448 GLU A N   
6718  C CA  . GLU A 448 ? 1.0224 0.9890 1.8414 -0.3287 -0.2006 -0.0502 448 GLU A CA  
6719  C C   . GLU A 448 ? 0.9753 0.9381 1.8234 -0.3310 -0.2172 -0.0732 448 GLU A C   
6720  O O   . GLU A 448 ? 0.9796 0.9203 1.8282 -0.3334 -0.2147 -0.0718 448 GLU A O   
6721  C CB  . GLU A 448 ? 1.1523 1.1139 2.0032 -0.3429 -0.1761 -0.0361 448 GLU A CB  
6722  C CG  . GLU A 448 ? 1.2502 1.2132 2.0715 -0.3417 -0.1575 -0.0129 448 GLU A CG  
6723  C CD  . GLU A 448 ? 1.3338 1.2885 2.1823 -0.3562 -0.1318 0.0018  448 GLU A CD  
6724  O OE1 . GLU A 448 ? 1.3677 1.3200 2.2645 -0.3676 -0.1287 -0.0076 448 GLU A OE1 
6725  O OE2 . GLU A 448 ? 1.3508 1.3009 2.1721 -0.3563 -0.1145 0.0226  448 GLU A OE2 
6732  N N   . VAL A 449 ? 0.9385 0.9228 1.8113 -0.3301 -0.2347 -0.0947 449 VAL A N   
6733  C CA  . VAL A 449 ? 0.9364 0.9209 1.8376 -0.3317 -0.2528 -0.1195 449 VAL A CA  
6734  C C   . VAL A 449 ? 0.9656 0.9675 1.9087 -0.3365 -0.2485 -0.1303 449 VAL A C   
6735  O O   . VAL A 449 ? 0.9848 1.0100 1.9328 -0.3326 -0.2562 -0.1367 449 VAL A O   
6736  C CB  . VAL A 449 ? 0.8827 0.8763 1.7518 -0.3184 -0.2784 -0.1360 449 VAL A CB  
6737  C CG1 . VAL A 449 ? 0.8908 0.8848 1.7788 -0.3170 -0.2939 -0.1611 449 VAL A CG1 
6738  C CG2 . VAL A 449 ? 0.8862 0.8634 1.6979 -0.3077 -0.2763 -0.1230 449 VAL A CG2 
6748  N N   . TYR A 450 ? 0.9653 0.9559 1.9394 -0.3446 -0.2363 -0.1321 450 TYR A N   
6749  C CA  . TYR A 450 ? 0.9918 0.9967 2.0087 -0.3498 -0.2309 -0.1424 450 TYR A CA  
6750  C C   . TYR A 450 ? 1.0347 1.0307 2.0754 -0.3512 -0.2372 -0.1597 450 TYR A C   
6751  O O   . TYR A 450 ? 1.1040 1.0764 2.1426 -0.3552 -0.2282 -0.1527 450 TYR A O   
6752  C CB  . TYR A 450 ? 1.0077 1.0087 2.0434 -0.3609 -0.2023 -0.1224 450 TYR A CB  
6753  C CG  . TYR A 450 ? 1.0590 1.0308 2.0864 -0.3679 -0.1835 -0.1034 450 TYR A CG  
6754  C CD1 . TYR A 450 ? 1.0525 1.0102 2.0426 -0.3665 -0.1778 -0.0832 450 TYR A CD1 
6755  C CD2 . TYR A 450 ? 1.1160 1.0738 2.1727 -0.3755 -0.1718 -0.1050 450 TYR A CD2 
6756  C CE1 . TYR A 450 ? 1.1007 1.0306 2.0816 -0.3719 -0.1616 -0.0647 450 TYR A CE1 
6757  C CE2 . TYR A 450 ? 1.1592 1.0892 2.2070 -0.3812 -0.1552 -0.0865 450 TYR A CE2 
6758  C CZ  . TYR A 450 ? 1.1602 1.0761 2.1693 -0.3791 -0.1505 -0.0663 450 TYR A CZ  
6759  O OH  . TYR A 450 ? 1.2156 1.1029 2.2143 -0.3836 -0.1350 -0.0470 450 TYR A OH  
6769  N N   . PRO A 451 ? 1.0089 1.0226 2.0726 -0.3475 -0.2528 -0.1823 451 PRO A N   
6770  C CA  . PRO A 451 ? 0.9843 1.0251 2.0521 -0.3416 -0.2657 -0.1921 451 PRO A CA  
6771  C C   . PRO A 451 ? 0.9514 0.9994 1.9765 -0.3296 -0.2878 -0.1970 451 PRO A C   
6772  O O   . PRO A 451 ? 0.9291 0.9633 1.9268 -0.3250 -0.2980 -0.2009 451 PRO A O   
6773  C CB  . PRO A 451 ? 1.0171 1.0679 2.1226 -0.3415 -0.2760 -0.2150 451 PRO A CB  
6774  C CG  . PRO A 451 ? 1.0329 1.0638 2.1365 -0.3422 -0.2798 -0.2230 451 PRO A CG  
6775  C CD  . PRO A 451 ? 1.0338 1.0407 2.1236 -0.3491 -0.2587 -0.2001 451 PRO A CD  
6783  N N   . SER A 452 ? 1.0067 1.0758 2.0264 -0.3244 -0.2947 -0.1968 452 SER A N   
6784  C CA  . SER A 452 ? 1.0214 1.0975 1.9993 -0.3127 -0.3148 -0.1997 452 SER A CA  
6785  C C   . SER A 452 ? 1.0560 1.1426 2.0315 -0.3035 -0.3410 -0.2240 452 SER A C   
6786  O O   . SER A 452 ? 1.1014 1.1813 2.0418 -0.2957 -0.3572 -0.2313 452 SER A O   
6787  C CB  . SER A 452 ? 0.9718 1.0649 1.9434 -0.3106 -0.3106 -0.1877 452 SER A CB  
6788  O OG  . SER A 452 ? 0.9702 1.0691 1.9006 -0.2992 -0.3293 -0.1890 452 SER A OG  
6794  N N   . ILE A 453 ? 0.9939 1.0966 2.0054 -0.3041 -0.3453 -0.2368 453 ILE A N   
6795  C CA  . ILE A 453 ? 0.9613 1.0736 1.9740 -0.2959 -0.3698 -0.2599 453 ILE A CA  
6796  C C   . ILE A 453 ? 0.9723 1.0708 2.0055 -0.3009 -0.3689 -0.2726 453 ILE A C   
6797  O O   . ILE A 453 ? 0.9371 1.0287 2.0067 -0.3113 -0.3500 -0.2680 453 ILE A O   
6798  C CB  . ILE A 453 ? 0.9331 1.0688 1.9769 -0.2936 -0.3759 -0.2680 453 ILE A CB  
6799  C CG1 . ILE A 453 ? 0.8993 1.0486 1.9220 -0.2878 -0.3775 -0.2558 453 ILE A CG1 
6800  C CG2 . ILE A 453 ? 0.9332 1.0775 1.9792 -0.2853 -0.4016 -0.2917 453 ILE A CG2 
6801  C CD1 . ILE A 453 ? 0.8800 1.0319 1.9241 -0.2969 -0.3515 -0.2371 453 ILE A CD1 
6813  N N   . LEU A 454 ? 0.9772 1.0711 1.9862 -0.2934 -0.3888 -0.2885 454 LEU A N   
6814  C CA  . LEU A 454 ? 0.9755 1.0548 1.9975 -0.2969 -0.3893 -0.3013 454 LEU A CA  
6815  C C   . LEU A 454 ? 0.9921 1.0835 2.0272 -0.2910 -0.4110 -0.3262 454 LEU A C   
6816  O O   . LEU A 454 ? 0.9975 1.0997 2.0034 -0.2805 -0.4318 -0.3348 454 LEU A O   
6817  C CB  . LEU A 454 ? 0.9660 1.0257 1.9457 -0.2938 -0.3916 -0.2983 454 LEU A CB  
6818  C CG  . LEU A 454 ? 0.9534 1.0011 1.9114 -0.2972 -0.3745 -0.2738 454 LEU A CG  
6819  C CD1 . LEU A 454 ? 0.9435 0.9751 1.8563 -0.2914 -0.3817 -0.2741 454 LEU A CD1 
6820  C CD2 . LEU A 454 ? 0.9558 0.9907 1.9484 -0.3097 -0.3487 -0.2597 454 LEU A CD2 
6832  N N   . ASN A 455 ? 1.0081 1.0971 2.0861 -0.2975 -0.4060 -0.3372 455 ASN A N   
6833  C CA  . ASN A 455 ? 1.0410 1.1395 2.1357 -0.2929 -0.4256 -0.3619 455 ASN A CA  
6834  C C   . ASN A 455 ? 1.0704 1.1517 2.1593 -0.2937 -0.4290 -0.3744 455 ASN A C   
6835  O O   . ASN A 455 ? 1.0595 1.1268 2.1757 -0.3028 -0.4116 -0.3703 455 ASN A O   
6836  C CB  . ASN A 455 ? 1.0408 1.1518 2.1934 -0.2991 -0.4186 -0.3672 455 ASN A CB  
6837  C CG  . ASN A 455 ? 1.0722 1.1946 2.2435 -0.2936 -0.4405 -0.3929 455 ASN A CG  
6838  O OD1 . ASN A 455 ? 1.1076 1.2265 2.2495 -0.2863 -0.4594 -0.4072 455 ASN A OD1 
6839  N ND2 . ASN A 455 ? 1.0740 1.2099 2.2945 -0.2972 -0.4378 -0.3992 455 ASN A ND2 
6846  N N   . GLN A 456 ? 1.0913 1.1731 2.1439 -0.2841 -0.4507 -0.3895 456 GLN A N   
6847  C CA  . GLN A 456 ? 1.1338 1.1999 2.1780 -0.2841 -0.4547 -0.4032 456 GLN A CA  
6848  C C   . GLN A 456 ? 1.1786 1.2452 2.2750 -0.2902 -0.4526 -0.4186 456 GLN A C   
6849  O O   . GLN A 456 ? 1.1989 1.2488 2.3099 -0.2960 -0.4418 -0.4204 456 GLN A O   
6850  C CB  . GLN A 456 ? 1.1885 1.2578 2.1849 -0.2725 -0.4790 -0.4183 456 GLN A CB  
6851  C CG  . GLN A 456 ? 1.2594 1.3269 2.2019 -0.2660 -0.4814 -0.4039 456 GLN A CG  
6852  C CD  . GLN A 456 ? 1.3606 1.4405 2.2643 -0.2540 -0.5061 -0.4152 456 GLN A CD  
6853  O OE1 . GLN A 456 ? 1.4321 1.5041 2.2873 -0.2473 -0.5149 -0.4186 456 GLN A OE1 
6854  N NE2 . GLN A 456 ? 1.3569 1.4558 2.2813 -0.2512 -0.5170 -0.4206 456 GLN A NE2 
6863  N N   . ASP A 457 ? 1.1816 1.2668 2.3078 -0.2885 -0.4631 -0.4300 457 ASP A N   
6864  C CA  . ASP A 457 ? 1.1708 1.2577 2.3501 -0.2942 -0.4610 -0.4449 457 ASP A CA  
6865  C C   . ASP A 457 ? 1.1648 1.2404 2.3837 -0.3066 -0.4329 -0.4295 457 ASP A C   
6866  O O   . ASP A 457 ? 1.1624 1.2299 2.4168 -0.3124 -0.4264 -0.4387 457 ASP A O   
6867  C CB  . ASP A 457 ? 1.1553 1.2650 2.3617 -0.2904 -0.4756 -0.4572 457 ASP A CB  
6868  C CG  . ASP A 457 ? 1.1725 1.2905 2.3527 -0.2795 -0.5047 -0.4792 457 ASP A CG  
6869  O OD1 . ASP A 457 ? 1.1801 1.2869 2.3172 -0.2749 -0.5128 -0.4842 457 ASP A OD1 
6870  O OD2 . ASP A 457 ? 1.1888 1.3241 2.3912 -0.2755 -0.5192 -0.4915 457 ASP A OD2 
6875  N N   . ASN A 458 ? 1.1789 1.2534 2.3916 -0.3106 -0.4158 -0.4060 458 ASN A N   
6876  C CA  . ASN A 458 ? 1.1866 1.2485 2.4303 -0.3223 -0.3880 -0.3889 458 ASN A CA  
6877  C C   . ASN A 458 ? 1.2316 1.2685 2.4566 -0.3252 -0.3786 -0.3827 458 ASN A C   
6878  O O   . ASN A 458 ? 1.1833 1.2122 2.3615 -0.3199 -0.3836 -0.3767 458 ASN A O   
6879  C CB  . ASN A 458 ? 1.1087 1.1761 2.3463 -0.3254 -0.3728 -0.3655 458 ASN A CB  
6880  C CG  . ASN A 458 ? 1.0759 1.1320 2.3473 -0.3378 -0.3438 -0.3481 458 ASN A CG  
6881  O OD1 . ASN A 458 ? 1.0975 1.1519 2.4135 -0.3442 -0.3363 -0.3560 458 ASN A OD1 
6882  N ND2 . ASN A 458 ? 1.0508 1.0984 2.2999 -0.3413 -0.3271 -0.3241 458 ASN A ND2 
6889  N N   . LYS A 459 ? 1.3102 1.3345 2.5730 -0.3335 -0.3645 -0.3839 459 LYS A N   
6890  C CA  . LYS A 459 ? 1.3153 1.3150 2.5669 -0.3362 -0.3555 -0.3793 459 LYS A CA  
6891  C C   . LYS A 459 ? 1.3681 1.3547 2.6612 -0.3480 -0.3296 -0.3652 459 LYS A C   
6892  O O   . LYS A 459 ? 1.4065 1.3949 2.7438 -0.3523 -0.3276 -0.3778 459 LYS A O   
6893  C CB  . LYS A 459 ? 1.2716 1.2687 2.5208 -0.3307 -0.3739 -0.4050 459 LYS A CB  
6894  C CG  . LYS A 459 ? 1.2116 1.2121 2.4070 -0.3196 -0.3950 -0.4145 459 LYS A CG  
6895  C CD  . LYS A 459 ? 1.2052 1.2139 2.4039 -0.3134 -0.4175 -0.4440 459 LYS A CD  
6896  C CE  . LYS A 459 ? 1.2045 1.2151 2.3462 -0.3026 -0.4372 -0.4530 459 LYS A CE  
6897  N NZ  . LYS A 459 ? 1.2258 1.2154 2.3426 -0.3016 -0.4339 -0.4549 459 LYS A NZ  
6911  N N   . THR A 460 ? 1.3673 1.3404 2.6452 -0.3530 -0.3098 -0.3390 460 THR A N   
6912  C CA  . THR A 460 ? 1.3713 1.3293 2.6808 -0.3642 -0.2837 -0.3219 460 THR A CA  
6913  C C   . THR A 460 ? 1.3676 1.2987 2.6509 -0.3662 -0.2709 -0.3033 460 THR A C   
6914  O O   . THR A 460 ? 1.3847 1.3021 2.6762 -0.3743 -0.2480 -0.2806 460 THR A O   
6915  C CB  . THR A 460 ? 1.3514 1.3209 2.6754 -0.3700 -0.2683 -0.3055 460 THR A CB  
6916  O OG1 . THR A 460 ? 1.3232 1.2987 2.6045 -0.3652 -0.2715 -0.2926 460 THR A OG1 
6917  C CG2 . THR A 460 ? 1.3550 1.3484 2.7179 -0.3697 -0.2772 -0.3239 460 THR A CG2 
6925  N N   . CYS A 461 ? 1.6189 1.1025 2.3586 -0.2653 -0.3718 -0.3566 461 CYS A N   
6926  C CA  . CYS A 461 ? 1.6703 1.0915 2.3860 -0.2407 -0.3795 -0.3440 461 CYS A CA  
6927  C C   . CYS A 461 ? 1.7349 1.0928 2.4541 -0.2079 -0.4178 -0.3909 461 CYS A C   
6928  O O   . CYS A 461 ? 1.7711 1.1485 2.4960 -0.1946 -0.4311 -0.4345 461 CYS A O   
6929  C CB  . CYS A 461 ? 1.6513 1.1219 2.3288 -0.2026 -0.3487 -0.3333 461 CYS A CB  
6930  S SG  . CYS A 461 ? 1.6471 1.1549 2.3102 -0.2353 -0.3100 -0.2719 461 CYS A SG  
6935  N N   . SER A 462 ? 1.7433 1.0307 2.4532 -0.1916 -0.4335 -0.3796 462 SER A N   
6936  C CA  . SER A 462 ? 1.7639 1.0003 2.4663 -0.1523 -0.4617 -0.4156 462 SER A CA  
6937  C C   . SER A 462 ? 1.7090 0.9335 2.3940 -0.1023 -0.4595 -0.4238 462 SER A C   
6938  O O   . SER A 462 ? 1.6674 0.8778 2.3476 -0.1099 -0.4496 -0.3832 462 SER A O   
6939  C CB  . SER A 462 ? 1.8515 1.0106 2.5643 -0.1811 -0.4873 -0.3922 462 SER A CB  
6940  O OG  . SER A 462 ? 1.8788 0.9988 2.5866 -0.2035 -0.4834 -0.3378 462 SER A OG  
6946  N N   . LEU A 463 ? 1.7086 0.9441 2.3827 -0.0515 -0.4675 -0.4755 463 LEU A N   
6947  C CA  . LEU A 463 ? 1.6794 0.9163 2.3407 -0.0008 -0.4628 -0.4885 463 LEU A CA  
6948  C C   . LEU A 463 ? 1.7522 0.9124 2.4216 0.0114  -0.4879 -0.4726 463 LEU A C   
6949  O O   . LEU A 463 ? 1.7718 0.8761 2.4521 -0.0109 -0.5122 -0.4652 463 LEU A O   
6950  C CB  . LEU A 463 ? 1.6538 0.9372 2.2983 0.0485  -0.4595 -0.5490 463 LEU A CB  
6951  C CG  . LEU A 463 ? 1.5492 0.9314 2.1665 0.0590  -0.4239 -0.5550 463 LEU A CG  
6952  C CD1 . LEU A 463 ? 1.5683 0.9824 2.1662 0.1061  -0.4269 -0.6173 463 LEU A CD1 
6953  C CD2 . LEU A 463 ? 1.4409 0.8687 2.0409 0.0668  -0.3909 -0.5119 463 LEU A CD2 
6965  N N   . PRO A 464 ? 1.7618 0.9192 2.4275 0.0471  -0.4839 -0.4667 464 PRO A N   
6966  C CA  . PRO A 464 ? 1.8348 0.9245 2.5105 0.0660  -0.5109 -0.4561 464 PRO A CA  
6967  C C   . PRO A 464 ? 1.9172 0.9781 2.5995 0.0903  -0.5363 -0.5024 464 PRO A C   
6968  O O   . PRO A 464 ? 1.9270 1.0340 2.6004 0.1191  -0.5289 -0.5536 464 PRO A O   
6969  C CB  . PRO A 464 ? 1.7906 0.9108 2.4636 0.1127  -0.4982 -0.4605 464 PRO A CB  
6970  C CG  . PRO A 464 ? 1.6780 0.8723 2.3336 0.0981  -0.4610 -0.4436 464 PRO A CG  
6971  C CD  . PRO A 464 ? 1.6600 0.8898 2.3086 0.0712  -0.4511 -0.4633 464 PRO A CD  
6979  N N   . GLY A 465 ? 1.9801 0.9637 2.6751 0.0775  -0.5669 -0.4835 465 GLY A N   
6980  C CA  . GLY A 465 ? 2.0326 0.9782 2.7359 0.0925  -0.5943 -0.5233 465 GLY A CA  
6981  C C   . GLY A 465 ? 2.0513 0.9871 2.7560 0.0443  -0.5998 -0.5222 465 GLY A C   
6982  O O   . GLY A 465 ? 1.9845 0.9243 2.6895 -0.0076 -0.5884 -0.4793 465 GLY A O   
6986  N N   . THR A 466 ? 2.1441 1.0715 2.8507 0.0619  -0.6171 -0.5713 466 THR A N   
6987  C CA  . THR A 466 ? 2.1566 1.0744 2.8677 0.0201  -0.6267 -0.5762 466 THR A CA  
6988  C C   . THR A 466 ? 2.0509 1.0510 2.7492 0.0141  -0.6020 -0.6003 466 THR A C   
6989  O O   . THR A 466 ? 2.0450 1.0487 2.7496 -0.0221 -0.6083 -0.6032 466 THR A O   
6990  C CB  . THR A 466 ? 2.2275 1.0911 2.9465 0.0389  -0.6612 -0.6171 466 THR A CB  
6991  O OG1 . THR A 466 ? 2.2106 1.1091 2.9178 0.1001  -0.6582 -0.6737 466 THR A OG1 
6992  C CG2 . THR A 466 ? 2.3070 1.0791 3.0424 0.0306  -0.6912 -0.5857 466 THR A CG2 
7000  N N   . ALA A 467 ? 1.9734 1.0404 2.6548 0.0479  -0.5756 -0.6168 467 ALA A N   
7001  C CA  . ALA A 467 ? 1.9654 1.1105 2.6321 0.0425  -0.5533 -0.6362 467 ALA A CA  
7002  C C   . ALA A 467 ? 2.0621 1.2254 2.7405 -0.0145 -0.5387 -0.5892 467 ALA A C   
7003  O O   . ALA A 467 ? 2.1283 1.2685 2.8153 -0.0380 -0.5313 -0.5404 467 ALA A O   
7004  C CB  . ALA A 467 ? 1.8368 1.0464 2.4813 0.0888  -0.5271 -0.6578 467 ALA A CB  
7010  N N   . LEU A 468 ? 2.0433 1.2528 2.7220 -0.0364 -0.5343 -0.6039 468 LEU A N   
7011  C CA  . LEU A 468 ? 1.9623 1.1935 2.6597 -0.0927 -0.5229 -0.5644 468 LEU A CA  
7012  C C   . LEU A 468 ? 1.8906 1.2090 2.5804 -0.0922 -0.5023 -0.5811 468 LEU A C   
7013  O O   . LEU A 468 ? 1.9049 1.2623 2.5703 -0.0516 -0.4994 -0.6231 468 LEU A O   
7014  C CB  . LEU A 468 ? 1.9513 1.1379 2.6707 -0.1342 -0.5473 -0.5576 468 LEU A CB  
7015  C CG  . LEU A 468 ? 1.9645 1.0591 2.6920 -0.1406 -0.5722 -0.5390 468 LEU A CG  
7016  C CD1 . LEU A 468 ? 2.0054 1.0618 2.7532 -0.1823 -0.5960 -0.5376 468 LEU A CD1 
7017  C CD2 . LEU A 468 ? 1.9178 0.9880 2.6473 -0.1615 -0.5587 -0.4814 468 LEU A CD2 
7029  N N   . LYS A 469 ? 1.7921 1.1439 2.5027 -0.1386 -0.4877 -0.5468 469 LYS A N   
7030  C CA  . LYS A 469 ? 1.6694 1.1019 2.3837 -0.1479 -0.4739 -0.5584 469 LYS A CA  
7031  C C   . LYS A 469 ? 1.6156 1.1037 2.3035 -0.1101 -0.4519 -0.5731 469 LYS A C   
7032  O O   . LYS A 469 ? 1.5925 1.1153 2.2547 -0.0756 -0.4551 -0.6143 469 LYS A O   
7033  C CB  . LYS A 469 ? 1.6438 1.0876 2.3579 -0.1444 -0.4969 -0.5994 469 LYS A CB  
7034  C CG  . LYS A 469 ? 1.6852 1.0713 2.4230 -0.1785 -0.5220 -0.5923 469 LYS A CG  
7035  C CD  . LYS A 469 ? 1.7612 1.1124 2.4811 -0.1469 -0.5507 -0.6412 469 LYS A CD  
7036  C CE  . LYS A 469 ? 1.8043 1.1624 2.5435 -0.1768 -0.5721 -0.6568 469 LYS A CE  
7037  N NZ  . LYS A 469 ? 1.8609 1.2110 2.5736 -0.1393 -0.5948 -0.7121 469 LYS A NZ  
7051  N N   . VAL A 470 ? 1.5979 1.1002 2.2821 -0.1167 -0.4244 -0.5306 470 VAL A N   
7052  C CA  . VAL A 470 ? 1.5176 1.0894 2.1653 -0.0854 -0.3906 -0.5215 470 VAL A CA  
7053  C C   . VAL A 470 ? 1.4609 1.0857 2.1161 -0.1168 -0.3592 -0.4742 470 VAL A C   
7054  O O   . VAL A 470 ? 1.4793 1.0786 2.1579 -0.1558 -0.3556 -0.4377 470 VAL A O   
7055  C CB  . VAL A 470 ? 1.4711 1.0151 2.0944 -0.0474 -0.3837 -0.5181 470 VAL A CB  
7056  C CG1 . VAL A 470 ? 1.3679 0.9805 1.9589 -0.0254 -0.3477 -0.4984 470 VAL A CG1 
7057  C CG2 . VAL A 470 ? 1.5397 1.0511 2.1527 -0.0071 -0.4092 -0.5738 470 VAL A CG2 
7067  N N   . SER A 471 ? 1.4118 1.1105 2.0448 -0.0992 -0.3368 -0.4756 471 SER A N   
7068  C CA  . SER A 471 ? 1.3917 1.1437 2.0270 -0.1191 -0.3055 -0.4362 471 SER A CA  
7069  C C   . SER A 471 ? 1.3882 1.1313 1.9990 -0.1081 -0.2818 -0.4016 471 SER A C   
7070  O O   . SER A 471 ? 1.4468 1.1854 2.0283 -0.0708 -0.2796 -0.4130 471 SER A O   
7071  C CB  . SER A 471 ? 1.3421 1.1674 1.9614 -0.1009 -0.2952 -0.4507 471 SER A CB  
7072  O OG  . SER A 471 ? 1.2889 1.1627 1.9260 -0.1255 -0.2733 -0.4215 471 SER A OG  
7078  N N   . CYS A 472 ? 1.3193 1.0644 1.9420 -0.1414 -0.2637 -0.3601 472 CYS A N   
7079  C CA  . CYS A 472 ? 1.3184 1.0457 1.9191 -0.1372 -0.2466 -0.3256 472 CYS A CA  
7080  C C   . CYS A 472 ? 1.3033 1.0782 1.8998 -0.1592 -0.2147 -0.2900 472 CYS A C   
7081  O O   . CYS A 472 ? 1.2268 1.0414 1.8462 -0.1834 -0.2063 -0.2888 472 CYS A O   
7082  C CB  . CYS A 472 ? 1.4082 1.0571 2.0219 -0.1572 -0.2660 -0.3088 472 CYS A CB  
7083  S SG  . CYS A 472 ? 1.4899 1.1195 2.1435 -0.2208 -0.2716 -0.2855 472 CYS A SG  
7088  N N   . PHE A 473 ? 1.3732 1.1446 1.9420 -0.1492 -0.1979 -0.2632 473 PHE A N   
7089  C CA  . PHE A 473 ? 1.3878 1.1952 1.9458 -0.1678 -0.1684 -0.2299 473 PHE A CA  
7090  C C   . PHE A 473 ? 1.3854 1.1579 1.9173 -0.1649 -0.1636 -0.1994 473 PHE A C   
7091  O O   . PHE A 473 ? 1.3864 1.1204 1.9099 -0.1399 -0.1807 -0.2074 473 PHE A O   
7092  C CB  . PHE A 473 ? 1.3475 1.2203 1.8914 -0.1457 -0.1498 -0.2403 473 PHE A CB  
7093  C CG  . PHE A 473 ? 1.3352 1.2137 1.8486 -0.1041 -0.1508 -0.2526 473 PHE A CG  
7094  C CD1 . PHE A 473 ? 1.3674 1.2424 1.8798 -0.0771 -0.1696 -0.2880 473 PHE A CD1 
7095  C CD2 . PHE A 473 ? 1.3024 1.1931 1.7876 -0.0936 -0.1325 -0.2297 473 PHE A CD2 
7096  C CE1 . PHE A 473 ? 1.3629 1.2512 1.8473 -0.0410 -0.1670 -0.2990 473 PHE A CE1 
7097  C CE2 . PHE A 473 ? 1.3038 1.2060 1.7650 -0.0589 -0.1320 -0.2395 473 PHE A CE2 
7098  C CZ  . PHE A 473 ? 1.3307 1.2342 1.7918 -0.0329 -0.1478 -0.2736 473 PHE A CZ  
7108  N N   . ASN A 474 ? 1.3616 1.1503 1.8817 -0.1895 -0.1411 -0.1663 474 ASN A N   
7109  C CA  . ASN A 474 ? 1.3599 1.1164 1.8535 -0.1936 -0.1380 -0.1333 474 ASN A CA  
7110  C C   . ASN A 474 ? 1.2825 1.0775 1.7456 -0.1693 -0.1185 -0.1271 474 ASN A C   
7111  O O   . ASN A 474 ? 1.2014 1.0490 1.6622 -0.1620 -0.1009 -0.1380 474 ASN A O   
7112  C CB  . ASN A 474 ? 1.4102 1.1549 1.9038 -0.2413 -0.1271 -0.0985 474 ASN A CB  
7113  C CG  . ASN A 474 ? 1.5332 1.2353 2.0574 -0.2722 -0.1474 -0.0983 474 ASN A CG  
7114  O OD1 . ASN A 474 ? 1.5995 1.2853 2.1482 -0.2583 -0.1693 -0.1291 474 ASN A OD1 
7115  N ND2 . ASN A 474 ? 1.5761 1.2597 2.0969 -0.3165 -0.1407 -0.0635 474 ASN A ND2 
7122  N N   . VAL A 475 ? 1.3074 1.0736 1.7490 -0.1573 -0.1245 -0.1088 475 VAL A N   
7123  C CA  . VAL A 475 ? 1.2214 1.0174 1.6346 -0.1396 -0.1090 -0.0979 475 VAL A CA  
7124  C C   . VAL A 475 ? 1.2281 0.9931 1.6185 -0.1594 -0.1090 -0.0600 475 VAL A C   
7125  O O   . VAL A 475 ? 1.2332 0.9451 1.6277 -0.1622 -0.1312 -0.0480 475 VAL A O   
7126  C CB  . VAL A 475 ? 1.1715 0.9753 1.5831 -0.0968 -0.1188 -0.1197 475 VAL A CB  
7127  C CG1 . VAL A 475 ? 1.1450 0.9781 1.5302 -0.0840 -0.1043 -0.1045 475 VAL A CG1 
7128  C CG2 . VAL A 475 ? 1.1229 0.9586 1.5482 -0.0788 -0.1191 -0.1558 475 VAL A CG2 
7138  N N   . ARG A 476 ? 1.2318 1.0271 1.5967 -0.1723 -0.0865 -0.0419 476 ARG A N   
7139  C CA  . ARG A 476 ? 1.2910 1.0630 1.6264 -0.1951 -0.0845 -0.0056 476 ARG A CA  
7140  C C   . ARG A 476 ? 1.2424 1.0433 1.5494 -0.1794 -0.0728 0.0010  476 ARG A C   
7141  O O   . ARG A 476 ? 1.2082 1.0457 1.4995 -0.1893 -0.0498 0.0016  476 ARG A O   
7142  C CB  . ARG A 476 ? 1.3688 1.1472 1.6988 -0.2382 -0.0670 0.0108  476 ARG A CB  
7143  C CG  . ARG A 476 ? 1.4484 1.2066 1.7393 -0.2655 -0.0626 0.0487  476 ARG A CG  
7144  C CD  . ARG A 476 ? 1.5298 1.3044 1.8152 -0.3092 -0.0406 0.0622  476 ARG A CD  
7145  N NE  . ARG A 476 ? 1.6480 1.3992 1.8897 -0.3391 -0.0380 0.1005  476 ARG A NE  
7146  C CZ  . ARG A 476 ? 1.7180 1.5035 1.9260 -0.3591 -0.0108 0.1107  476 ARG A CZ  
7147  N NH1 . ARG A 476 ? 1.6796 1.5231 1.8970 -0.3513 0.0162  0.0850  476 ARG A NH1 
7148  N NH2 . ARG A 476 ? 1.8132 1.5730 1.9762 -0.3867 -0.0122 0.1463  476 ARG A NH2 
7162  N N   . PHE A 477 ? 1.2403 1.0252 1.5439 -0.1546 -0.0899 0.0047  477 PHE A N   
7163  C CA  . PHE A 477 ? 1.2242 1.0327 1.5039 -0.1426 -0.0834 0.0141  477 PHE A CA  
7164  C C   . PHE A 477 ? 1.2403 1.0220 1.4874 -0.1668 -0.0878 0.0495  477 PHE A C   
7165  O O   . PHE A 477 ? 1.2569 0.9922 1.5041 -0.1792 -0.1068 0.0685  477 PHE A O   
7166  C CB  . PHE A 477 ? 1.2394 1.0538 1.5358 -0.1050 -0.0985 0.0001  477 PHE A CB  
7167  C CG  . PHE A 477 ? 1.3236 1.0922 1.6314 -0.0960 -0.1265 0.0118  477 PHE A CG  
7168  C CD1 . PHE A 477 ? 1.3900 1.1165 1.7206 -0.0973 -0.1441 0.0042  477 PHE A CD1 
7169  C CD2 . PHE A 477 ? 1.3331 1.0997 1.6317 -0.0852 -0.1383 0.0295  477 PHE A CD2 
7170  C CE1 . PHE A 477 ? 1.4406 1.1189 1.7837 -0.0864 -0.1733 0.0142  477 PHE A CE1 
7171  C CE2 . PHE A 477 ? 1.3844 1.1089 1.6978 -0.0733 -0.1673 0.0397  477 PHE A CE2 
7172  C CZ  . PHE A 477 ? 1.4339 1.1119 1.7692 -0.0728 -0.1851 0.0320  477 PHE A CZ  
7182  N N   . CYS A 478 ? 1.2631 1.0712 1.4801 -0.1740 -0.0723 0.0585  478 CYS A N   
7183  C CA  . CYS A 478 ? 1.3555 1.1447 1.5329 -0.1986 -0.0743 0.0900  478 CYS A CA  
7184  C C   . CYS A 478 ? 1.3506 1.1585 1.5097 -0.1837 -0.0776 0.0948  478 CYS A C   
7185  O O   . CYS A 478 ? 1.3081 1.1503 1.4804 -0.1619 -0.0699 0.0748  478 CYS A O   
7186  C CB  . CYS A 478 ? 1.4192 1.2232 1.5713 -0.2322 -0.0483 0.0951  478 CYS A CB  
7187  S SG  . CYS A 478 ? 1.5128 1.3070 1.6906 -0.2569 -0.0404 0.0904  478 CYS A SG  
7192  N N   . LEU A 479 ? 1.3719 1.1566 1.4990 -0.1983 -0.0906 0.1235  479 LEU A N   
7193  C CA  . LEU A 479 ? 1.3129 1.1126 1.4241 -0.1876 -0.0987 0.1306  479 LEU A CA  
7194  C C   . LEU A 479 ? 1.3092 1.0910 1.3681 -0.2173 -0.1015 0.1592  479 LEU A C   
7195  O O   . LEU A 479 ? 1.3069 1.0528 1.3474 -0.2396 -0.1103 0.1822  479 LEU A O   
7196  C CB  . LEU A 479 ? 1.2998 1.0910 1.4441 -0.1579 -0.1265 0.1317  479 LEU A CB  
7197  C CG  . LEU A 479 ? 1.2707 1.1016 1.4311 -0.1330 -0.1283 0.1203  479 LEU A CG  
7198  C CD1 . LEU A 479 ? 1.2306 1.1017 1.4056 -0.1215 -0.1041 0.0918  479 LEU A CD1 
7199  C CD2 . LEU A 479 ? 1.2889 1.1139 1.4891 -0.1034 -0.1543 0.1191  479 LEU A CD2 
7211  N N   . LYS A 480 ? 1.3073 1.1128 1.3397 -0.2193 -0.0948 0.1580  480 LYS A N   
7212  C CA  . LYS A 480 ? 1.3757 1.1693 1.3523 -0.2460 -0.0971 0.1803  480 LYS A CA  
7213  C C   . LYS A 480 ? 1.3934 1.2069 1.3612 -0.2349 -0.1072 0.1787  480 LYS A C   
7214  O O   . LYS A 480 ? 1.3902 1.2343 1.3828 -0.2166 -0.0973 0.1563  480 LYS A O   
7215  C CB  . LYS A 480 ? 1.3801 1.1864 1.3230 -0.2723 -0.0652 0.1721  480 LYS A CB  
7216  C CG  . LYS A 480 ? 1.4358 1.2343 1.3136 -0.3006 -0.0636 0.1906  480 LYS A CG  
7217  C CD  . LYS A 480 ? 1.4364 1.2577 1.2873 -0.3216 -0.0276 0.1747  480 LYS A CD  
7218  C CE  . LYS A 480 ? 1.4852 1.3008 1.2652 -0.3503 -0.0240 0.1901  480 LYS A CE  
7219  N NZ  . LYS A 480 ? 1.4631 1.3096 1.2194 -0.3651 0.0133  0.1670  480 LYS A NZ  
7233  N N   . ALA A 481 ? 1.4059 1.2011 1.3374 -0.2481 -0.1287 0.2041  481 ALA A N   
7234  C CA  . ALA A 481 ? 1.3679 1.1806 1.2956 -0.2396 -0.1445 0.2053  481 ALA A CA  
7235  C C   . ALA A 481 ? 1.4556 1.2540 1.3175 -0.2676 -0.1522 0.2242  481 ALA A C   
7236  O O   . ALA A 481 ? 1.5574 1.3276 1.3792 -0.2909 -0.1546 0.2453  481 ALA A O   
7237  C CB  . ALA A 481 ? 1.3368 1.1485 1.3097 -0.2142 -0.1762 0.2154  481 ALA A CB  
7243  N N   . ASP A 482 ? 1.4433 1.2615 1.2926 -0.2669 -0.1568 0.2167  482 ASP A N   
7244  C CA  . ASP A 482 ? 1.4980 1.3054 1.2842 -0.2912 -0.1679 0.2301  482 ASP A CA  
7245  C C   . ASP A 482 ? 1.4338 1.2635 1.2332 -0.2819 -0.1849 0.2234  482 ASP A C   
7246  O O   . ASP A 482 ? 1.3288 1.1844 1.1820 -0.2598 -0.1822 0.2085  482 ASP A O   
7247  C CB  . ASP A 482 ? 1.5677 1.3754 1.3012 -0.3143 -0.1355 0.2155  482 ASP A CB  
7248  C CG  . ASP A 482 ? 1.6971 1.4849 1.3542 -0.3443 -0.1454 0.2354  482 ASP A CG  
7249  O OD1 . ASP A 482 ? 1.7445 1.5128 1.3887 -0.3484 -0.1799 0.2650  482 ASP A OD1 
7250  O OD2 . ASP A 482 ? 1.7426 1.5359 1.3520 -0.3628 -0.1192 0.2206  482 ASP A OD2 
7255  N N   . GLY A 483 ? 1.4935 1.3142 1.2415 -0.3011 -0.2031 0.2352  483 GLY A N   
7256  C CA  . GLY A 483 ? 1.4852 1.3261 1.2455 -0.2969 -0.2228 0.2306  483 GLY A CA  
7257  C C   . GLY A 483 ? 1.5381 1.3658 1.2279 -0.3232 -0.2363 0.2359  483 GLY A C   
7258  O O   . GLY A 483 ? 1.6180 1.4231 1.2450 -0.3445 -0.2290 0.2436  483 GLY A O   
7262  N N   . LYS A 484 ? 1.4783 1.3228 1.1786 -0.3231 -0.2564 0.2312  484 LYS A N   
7263  C CA  . LYS A 484 ? 1.4949 1.3289 1.1331 -0.3467 -0.2749 0.2323  484 LYS A CA  
7264  C C   . LYS A 484 ? 1.4832 1.3295 1.1464 -0.3442 -0.3199 0.2542  484 LYS A C   
7265  O O   . LYS A 484 ? 1.4129 1.2899 1.1460 -0.3260 -0.3283 0.2519  484 LYS A O   
7266  C CB  . LYS A 484 ? 1.4738 1.3140 1.0993 -0.3523 -0.2556 0.1990  484 LYS A CB  
7267  C CG  . LYS A 484 ? 1.5005 1.3417 1.1016 -0.3678 -0.2847 0.1955  484 LYS A CG  
7268  C CD  . LYS A 484 ? 1.5519 1.3681 1.0654 -0.3934 -0.2997 0.2027  484 LYS A CD  
7269  C CE  . LYS A 484 ? 1.5528 1.3646 1.0325 -0.4100 -0.3180 0.1845  484 LYS A CE  
7270  N NZ  . LYS A 484 ? 1.4967 1.3323 1.0360 -0.4055 -0.3514 0.1942  484 LYS A NZ  
7284  N N   . GLY A 485 ? 1.5847 1.4110 1.1915 -0.3626 -0.3488 0.2756  485 GLY A N   
7285  C CA  . GLY A 485 ? 1.6676 1.5063 1.2923 -0.3626 -0.3958 0.2958  485 GLY A CA  
7286  C C   . GLY A 485 ? 1.7469 1.5772 1.3977 -0.3491 -0.4244 0.3292  485 GLY A C   
7287  O O   . GLY A 485 ? 1.7444 1.5462 1.3734 -0.3495 -0.4138 0.3431  485 GLY A O   
7291  N N   . VAL A 486 ? 1.8174 1.6738 1.5200 -0.3371 -0.4631 0.3421  486 VAL A N   
7292  C CA  . VAL A 486 ? 1.8706 1.7208 1.6074 -0.3196 -0.4983 0.3724  486 VAL A CA  
7293  C C   . VAL A 486 ? 1.8115 1.6729 1.6233 -0.2878 -0.4764 0.3649  486 VAL A C   
7294  O O   . VAL A 486 ? 1.7819 1.6881 1.6697 -0.2662 -0.4704 0.3488  486 VAL A O   
7295  C CB  . VAL A 486 ? 1.8665 1.7496 1.6434 -0.3142 -0.5466 0.3845  486 VAL A CB  
7296  C CG1 . VAL A 486 ? 1.8869 1.7705 1.7202 -0.2867 -0.5819 0.4101  486 VAL A CG1 
7297  C CG2 . VAL A 486 ? 1.9135 1.7779 1.6075 -0.3468 -0.5751 0.3949  486 VAL A CG2 
7307  N N   . LEU A 487 ? 1.7721 1.5939 1.5615 -0.2866 -0.4647 0.3764  487 LEU A N   
7308  C CA  . LEU A 487 ? 1.6675 1.4927 1.5200 -0.2585 -0.4447 0.3670  487 LEU A CA  
7309  C C   . LEU A 487 ? 1.7091 1.4856 1.5486 -0.2552 -0.4654 0.3961  487 LEU A C   
7310  O O   . LEU A 487 ? 1.7725 1.5085 1.5356 -0.2829 -0.4757 0.4199  487 LEU A O   
7311  C CB  . LEU A 487 ? 1.6088 1.4369 1.4511 -0.2636 -0.3920 0.3382  487 LEU A CB  
7312  C CG  . LEU A 487 ? 1.5617 1.4348 1.4347 -0.2595 -0.3700 0.3085  487 LEU A CG  
7313  C CD1 . LEU A 487 ? 1.6082 1.4699 1.4125 -0.2877 -0.3451 0.2930  487 LEU A CD1 
7314  C CD2 . LEU A 487 ? 1.4755 1.3719 1.4143 -0.2327 -0.3419 0.2874  487 LEU A CD2 
7326  N N   . PRO A 488 ? 1.6865 1.4639 1.5963 -0.2229 -0.4724 0.3950  488 PRO A N   
7327  C CA  . PRO A 488 ? 1.6986 1.4210 1.5990 -0.2198 -0.4930 0.4218  488 PRO A CA  
7328  C C   . PRO A 488 ? 1.6664 1.3549 1.5259 -0.2391 -0.4544 0.4175  488 PRO A C   
7329  O O   . PRO A 488 ? 1.5778 1.2909 1.4425 -0.2412 -0.4112 0.3877  488 PRO A O   
7330  C CB  . PRO A 488 ? 1.6649 1.4058 1.6619 -0.1750 -0.5094 0.4118  488 PRO A CB  
7331  C CG  . PRO A 488 ? 1.6028 1.4052 1.6495 -0.1599 -0.4735 0.3733  488 PRO A CG  
7332  C CD  . PRO A 488 ? 1.6207 1.4496 1.6213 -0.1879 -0.4635 0.3688  488 PRO A CD  
7340  N N   . ARG A 489 ? 1.7512 1.3825 1.5709 -0.2543 -0.4728 0.4499  489 ARG A N   
7341  C CA  . ARG A 489 ? 1.7558 1.3561 1.5365 -0.2778 -0.4387 0.4505  489 ARG A CA  
7342  C C   . ARG A 489 ? 1.7343 1.3317 1.5830 -0.2516 -0.4213 0.4295  489 ARG A C   
7343  O O   . ARG A 489 ? 1.7026 1.2981 1.5384 -0.2657 -0.3828 0.4148  489 ARG A O   
7344  C CB  . ARG A 489 ? 1.8148 1.3546 1.5279 -0.3080 -0.4643 0.4960  489 ARG A CB  
7345  C CG  . ARG A 489 ? 1.8620 1.4016 1.4874 -0.3421 -0.4734 0.5155  489 ARG A CG  
7346  C CD  . ARG A 489 ? 1.9746 1.4543 1.5283 -0.3745 -0.4968 0.5636  489 ARG A CD  
7347  N NE  . ARG A 489 ? 2.0440 1.5243 1.5079 -0.4065 -0.5089 0.5825  489 ARG A NE  
7348  C CZ  . ARG A 489 ? 2.1551 1.5892 1.5400 -0.4394 -0.5326 0.6274  489 ARG A CZ  
7349  N NH1 . ARG A 489 ? 2.2071 1.5868 1.5945 -0.4459 -0.5480 0.6607  489 ARG A NH1 
7350  N NH2 . ARG A 489 ? 2.2209 1.6610 1.5216 -0.4672 -0.5423 0.6394  489 ARG A NH2 
7364  N N   . LYS A 490 ? 1.7531 1.3521 1.6745 -0.2134 -0.4495 0.4258  490 LYS A N   
7365  C CA  . LYS A 490 ? 1.7626 1.3536 1.7464 -0.1863 -0.4389 0.4049  490 LYS A CA  
7366  C C   . LYS A 490 ? 1.6925 1.3481 1.7440 -0.1523 -0.4200 0.3644  490 LYS A C   
7367  O O   . LYS A 490 ? 1.7126 1.4085 1.7908 -0.1364 -0.4368 0.3612  490 LYS A O   
7368  C CB  . LYS A 490 ? 1.8660 1.4039 1.8808 -0.1663 -0.4860 0.4290  490 LYS A CB  
7369  C CG  . LYS A 490 ? 1.8841 1.3942 1.9484 -0.1456 -0.4793 0.4113  490 LYS A CG  
7370  C CD  . LYS A 490 ? 1.9890 1.4294 2.0690 -0.1336 -0.5297 0.4411  490 LYS A CD  
7371  C CE  . LYS A 490 ? 1.9777 1.4243 2.1481 -0.0806 -0.5460 0.4114  490 LYS A CE  
7372  N NZ  . LYS A 490 ? 1.9410 1.4551 2.1636 -0.0451 -0.5560 0.3922  490 LYS A NZ  
7386  N N   . LEU A 491 ? 1.6259 1.2933 1.7041 -0.1433 -0.3854 0.3347  491 LEU A N   
7387  C CA  . LEU A 491 ? 1.5559 1.2836 1.6899 -0.1150 -0.3631 0.2972  491 LEU A CA  
7388  C C   . LEU A 491 ? 1.5898 1.3067 1.7747 -0.0881 -0.3556 0.2740  491 LEU A C   
7389  O O   . LEU A 491 ? 1.6289 1.3077 1.7934 -0.1038 -0.3421 0.2746  491 LEU A O   
7390  C CB  . LEU A 491 ? 1.4855 1.2488 1.5861 -0.1366 -0.3219 0.2795  491 LEU A CB  
7391  C CG  . LEU A 491 ? 1.4794 1.2645 1.5396 -0.1572 -0.3271 0.2910  491 LEU A CG  
7392  C CD1 . LEU A 491 ? 1.4673 1.2470 1.4641 -0.1911 -0.2947 0.2868  491 LEU A CD1 
7393  C CD2 . LEU A 491 ? 1.4284 1.2747 1.5370 -0.1360 -0.3255 0.2717  491 LEU A CD2 
7405  N N   . ASN A 492 ? 1.5869 1.3409 1.8382 -0.0486 -0.3637 0.2519  492 ASN A N   
7406  C CA  . ASN A 492 ? 1.5965 1.3424 1.8989 -0.0174 -0.3613 0.2256  492 ASN A CA  
7407  C C   . ASN A 492 ? 1.5126 1.3172 1.8366 -0.0063 -0.3217 0.1885  492 ASN A C   
7408  O O   . ASN A 492 ? 1.4932 1.3580 1.8540 0.0148  -0.3172 0.1728  492 ASN A O   
7409  C CB  . ASN A 492 ? 1.6402 1.3865 2.0025 0.0227  -0.3992 0.2241  492 ASN A CB  
7410  C CG  . ASN A 492 ? 1.7142 1.4085 2.0548 0.0127  -0.4439 0.2650  492 ASN A CG  
7411  O OD1 . ASN A 492 ? 1.7846 1.4238 2.0660 -0.0228 -0.4482 0.2941  492 ASN A OD1 
7412  N ND2 . ASN A 492 ? 1.6998 1.4143 2.0885 0.0436  -0.4778 0.2679  492 ASN A ND2 
7419  N N   . PHE A 493 ? 1.4616 1.2503 1.7638 -0.0216 -0.2943 0.1759  493 PHE A N   
7420  C CA  . PHE A 493 ? 1.3705 1.2072 1.6879 -0.0123 -0.2597 0.1430  493 PHE A CA  
7421  C C   . PHE A 493 ? 1.3827 1.2180 1.7481 0.0214  -0.2610 0.1127  493 PHE A C   
7422  O O   . PHE A 493 ? 1.4270 1.2100 1.8055 0.0300  -0.2838 0.1159  493 PHE A O   
7423  C CB  . PHE A 493 ? 1.3292 1.1555 1.5995 -0.0455 -0.2301 0.1432  493 PHE A CB  
7424  C CG  . PHE A 493 ? 1.2995 1.1465 1.5273 -0.0720 -0.2185 0.1577  493 PHE A CG  
7425  C CD1 . PHE A 493 ? 1.3280 1.1427 1.5123 -0.0982 -0.2342 0.1886  493 PHE A CD1 
7426  C CD2 . PHE A 493 ? 1.2553 1.1511 1.4837 -0.0714 -0.1933 0.1401  493 PHE A CD2 
7427  C CE1 . PHE A 493 ? 1.3198 1.1518 1.4625 -0.1216 -0.2243 0.1974  493 PHE A CE1 
7428  C CE2 . PHE A 493 ? 1.2507 1.1593 1.4410 -0.0949 -0.1852 0.1506  493 PHE A CE2 
7429  C CZ  . PHE A 493 ? 1.2873 1.1646 1.4350 -0.1192 -0.2003 0.1770  493 PHE A CZ  
7439  N N   . GLN A 494 ? 1.3746 1.2661 1.7633 0.0394  -0.2372 0.0830  494 GLN A N   
7440  C CA  . GLN A 494 ? 1.4029 1.3028 1.8294 0.0704  -0.2324 0.0481  494 GLN A CA  
7441  C C   . GLN A 494 ? 1.3055 1.2240 1.7109 0.0579  -0.1994 0.0290  494 GLN A C   
7442  O O   . GLN A 494 ? 1.2531 1.2246 1.6521 0.0552  -0.1773 0.0227  494 GLN A O   
7443  C CB  . GLN A 494 ? 1.4640 1.4230 1.9407 0.1079  -0.2359 0.0284  494 GLN A CB  
7444  C CG  . GLN A 494 ? 1.5654 1.4991 2.0857 0.1393  -0.2712 0.0269  494 GLN A CG  
7445  C CD  . GLN A 494 ? 1.6270 1.5449 2.1426 0.1290  -0.3000 0.0634  494 GLN A CD  
7446  O OE1 . GLN A 494 ? 1.6179 1.5843 2.1298 0.1193  -0.2942 0.0760  494 GLN A OE1 
7447  N NE2 . GLN A 494 ? 1.6776 1.5251 2.1919 0.1296  -0.3336 0.0818  494 GLN A NE2 
7456  N N   . VAL A 495 ? 1.2781 1.1524 1.6742 0.0492  -0.1983 0.0212  495 VAL A N   
7457  C CA  . VAL A 495 ? 1.1975 1.0850 1.5760 0.0367  -0.1716 0.0041  495 VAL A CA  
7458  C C   . VAL A 495 ? 1.1885 1.0856 1.5976 0.0663  -0.1703 -0.0336 495 VAL A C   
7459  O O   . VAL A 495 ? 1.2014 1.0662 1.6383 0.0871  -0.1924 -0.0444 495 VAL A O   
7460  C CB  . VAL A 495 ? 1.1973 1.0368 1.5440 0.0013  -0.1692 0.0213  495 VAL A CB  
7461  C CG1 . VAL A 495 ? 1.1574 1.0157 1.4944 -0.0081 -0.1441 0.0012  495 VAL A CG1 
7462  C CG2 . VAL A 495 ? 1.2047 1.0372 1.5146 -0.0277 -0.1689 0.0555  495 VAL A CG2 
7472  N N   . GLU A 496 ? 1.2008 1.1401 1.6029 0.0685  -0.1462 -0.0541 496 GLU A N   
7473  C CA  . GLU A 496 ? 1.2584 1.2111 1.6794 0.0933  -0.1425 -0.0915 496 GLU A CA  
7474  C C   . GLU A 496 ? 1.2788 1.2355 1.6768 0.0750  -0.1245 -0.1009 496 GLU A C   
7475  O O   . GLU A 496 ? 1.2812 1.2609 1.6543 0.0552  -0.1074 -0.0865 496 GLU A O   
7476  C CB  . GLU A 496 ? 1.2298 1.2474 1.6701 0.1230  -0.1328 -0.1107 496 GLU A CB  
7477  C CG  . GLU A 496 ? 1.2610 1.2786 1.7414 0.1557  -0.1528 -0.1211 496 GLU A CG  
7478  C CD  . GLU A 496 ? 1.2341 1.3271 1.7363 0.1838  -0.1384 -0.1426 496 GLU A CD  
7479  O OE1 . GLU A 496 ? 1.1914 1.3314 1.6729 0.1759  -0.1139 -0.1478 496 GLU A OE1 
7480  O OE2 . GLU A 496 ? 1.2513 1.3580 1.7922 0.2136  -0.1521 -0.1538 496 GLU A OE2 
7487  N N   . LEU A 497 ? 1.2716 1.2046 1.6802 0.0827  -0.1310 -0.1265 497 LEU A N   
7488  C CA  . LEU A 497 ? 1.1963 1.1344 1.5904 0.0685  -0.1187 -0.1392 497 LEU A CA  
7489  C C   . LEU A 497 ? 1.1754 1.1443 1.5779 0.0961  -0.1154 -0.1778 497 LEU A C   
7490  O O   . LEU A 497 ? 1.1906 1.1502 1.6154 0.1230  -0.1289 -0.2011 497 LEU A O   
7491  C CB  . LEU A 497 ? 1.1912 1.0728 1.5882 0.0451  -0.1307 -0.1336 497 LEU A CB  
7492  C CG  . LEU A 497 ? 1.1846 1.0395 1.5641 0.0113  -0.1293 -0.0958 497 LEU A CG  
7493  C CD1 . LEU A 497 ? 1.2032 1.0023 1.5902 -0.0111 -0.1433 -0.0899 497 LEU A CD1 
7494  C CD2 . LEU A 497 ? 1.1499 1.0412 1.5045 -0.0081 -0.1052 -0.0856 497 LEU A CD2 
7506  N N   . LEU A 498 ? 1.1589 1.1636 1.5420 0.0905  -0.0988 -0.1853 498 LEU A N   
7507  C CA  . LEU A 498 ? 1.1756 1.2117 1.5567 0.1127  -0.0953 -0.2198 498 LEU A CA  
7508  C C   . LEU A 498 ? 1.1445 1.1787 1.5116 0.0963  -0.0922 -0.2276 498 LEU A C   
7509  O O   . LEU A 498 ? 1.1218 1.1700 1.4723 0.0767  -0.0803 -0.2072 498 LEU A O   
7510  C CB  . LEU A 498 ? 1.1554 1.2535 1.5246 0.1273  -0.0783 -0.2193 498 LEU A CB  
7511  C CG  . LEU A 498 ? 1.1514 1.2892 1.5066 0.1454  -0.0709 -0.2506 498 LEU A CG  
7512  C CD1 . LEU A 498 ? 1.1920 1.3132 1.5661 0.1720  -0.0851 -0.2900 498 LEU A CD1 
7513  C CD2 . LEU A 498 ? 1.1092 1.3098 1.4512 0.1538  -0.0523 -0.2434 498 LEU A CD2 
7525  N N   . LEU A 499 ? 1.1687 1.1857 1.5449 0.1056  -0.1048 -0.2588 499 LEU A N   
7526  C CA  . LEU A 499 ? 1.1633 1.1828 1.5317 0.0926  -0.1059 -0.2704 499 LEU A CA  
7527  C C   . LEU A 499 ? 1.1665 1.2350 1.5120 0.1108  -0.0982 -0.2916 499 LEU A C   
7528  O O   . LEU A 499 ? 1.1700 1.2603 1.5117 0.1366  -0.0970 -0.3125 499 LEU A O   
7529  C CB  . LEU A 499 ? 1.1977 1.1705 1.5883 0.0887  -0.1270 -0.2924 499 LEU A CB  
7530  C CG  . LEU A 499 ? 1.2472 1.1639 1.6597 0.0735  -0.1396 -0.2740 499 LEU A CG  
7531  C CD1 . LEU A 499 ? 1.3133 1.1828 1.7479 0.0779  -0.1642 -0.3025 499 LEU A CD1 
7532  C CD2 . LEU A 499 ? 1.2365 1.1443 1.6469 0.0372  -0.1307 -0.2407 499 LEU A CD2 
7544  N N   . ASP A 500 ? 1.1653 1.2524 1.4951 0.0974  -0.0934 -0.2863 500 ASP A N   
7545  C CA  . ASP A 500 ? 1.1990 1.3292 1.5006 0.1101  -0.0887 -0.3005 500 ASP A CA  
7546  C C   . ASP A 500 ? 1.2028 1.3731 1.4856 0.1236  -0.0724 -0.2898 500 ASP A C   
7547  O O   . ASP A 500 ? 1.2421 1.4445 1.5086 0.1439  -0.0691 -0.3116 500 ASP A O   
7548  C CB  . ASP A 500 ? 1.2698 1.3959 1.5710 0.1264  -0.1043 -0.3422 500 ASP A CB  
7549  C CG  . ASP A 500 ? 1.2861 1.4443 1.5586 0.1279  -0.1068 -0.3535 500 ASP A CG  
7550  O OD1 . ASP A 500 ? 1.2508 1.4329 1.5048 0.1182  -0.0968 -0.3280 500 ASP A OD1 
7551  O OD2 . ASP A 500 ? 1.3311 1.4874 1.5984 0.1390  -0.1213 -0.3883 500 ASP A OD2 
7556  N N   . LYS A 501 ? 1.1782 1.3493 1.4629 0.1105  -0.0616 -0.2563 501 LYS A N   
7557  C CA  . LYS A 501 ? 1.1798 1.3892 1.4533 0.1187  -0.0471 -0.2428 501 LYS A CA  
7558  C C   . LYS A 501 ? 1.1699 1.4230 1.4087 0.1197  -0.0377 -0.2402 501 LYS A C   
7559  O O   . LYS A 501 ? 1.1803 1.4756 1.4067 0.1325  -0.0268 -0.2447 501 LYS A O   
7560  C CB  . LYS A 501 ? 1.1726 1.3695 1.4537 0.1009  -0.0411 -0.2076 501 LYS A CB  
7561  C CG  . LYS A 501 ? 1.1679 1.4067 1.4332 0.0992  -0.0266 -0.1866 501 LYS A CG  
7562  C CD  . LYS A 501 ? 1.1433 1.3709 1.4223 0.0877  -0.0247 -0.1597 501 LYS A CD  
7563  C CE  . LYS A 501 ? 1.1180 1.3920 1.3895 0.0876  -0.0124 -0.1433 501 LYS A CE  
7564  N NZ  . LYS A 501 ? 1.1222 1.4369 1.4081 0.1121  -0.0077 -0.1642 501 LYS A NZ  
7578  N N   . LEU A 502 ? 1.1892 1.4344 1.4128 0.1062  -0.0422 -0.2320 502 LEU A N   
7579  C CA  . LEU A 502 ? 1.2778 1.5563 1.4664 0.1032  -0.0363 -0.2196 502 LEU A CA  
7580  C C   . LEU A 502 ? 1.3668 1.6816 1.5298 0.1213  -0.0353 -0.2451 502 LEU A C   
7581  O O   . LEU A 502 ? 1.4148 1.7671 1.5463 0.1201  -0.0254 -0.2322 502 LEU A O   
7582  C CB  . LEU A 502 ? 1.3299 1.5894 1.5130 0.0896  -0.0461 -0.2099 502 LEU A CB  
7583  C CG  . LEU A 502 ? 1.3500 1.5957 1.5355 0.0716  -0.0404 -0.1768 502 LEU A CG  
7584  C CD1 . LEU A 502 ? 1.3871 1.6144 1.5774 0.0629  -0.0508 -0.1745 502 LEU A CD1 
7585  C CD2 . LEU A 502 ? 1.3308 1.6048 1.4885 0.0680  -0.0303 -0.1530 502 LEU A CD2 
7597  N N   . LYS A 503 ? 1.3883 1.6924 1.5618 0.1364  -0.0456 -0.2810 503 LYS A N   
7598  C CA  . LYS A 503 ? 1.3957 1.7349 1.5412 0.1551  -0.0445 -0.3106 503 LYS A CA  
7599  C C   . LYS A 503 ? 1.4320 1.8153 1.5746 0.1680  -0.0245 -0.3113 503 LYS A C   
7600  O O   . LYS A 503 ? 1.4000 1.7744 1.5772 0.1762  -0.0210 -0.3147 503 LYS A O   
7601  C CB  . LYS A 503 ? 1.3502 1.6625 1.5114 0.1691  -0.0619 -0.3527 503 LYS A CB  
7602  C CG  . LYS A 503 ? 1.2674 1.5504 1.4302 0.1568  -0.0824 -0.3577 503 LYS A CG  
7603  C CD  . LYS A 503 ? 1.1983 1.5106 1.3180 0.1518  -0.0851 -0.3476 503 LYS A CD  
7604  C CE  . LYS A 503 ? 1.1795 1.4863 1.2872 0.1570  -0.1076 -0.3797 503 LYS A CE  
7605  N NZ  . LYS A 503 ? 1.1920 1.5333 1.2480 0.1569  -0.1109 -0.3720 503 LYS A NZ  
7619  N N   . GLN A 504 ? 1.4875 1.9208 1.5895 0.1690  -0.0122 -0.3068 504 GLN A N   
7620  C CA  . GLN A 504 ? 1.4768 1.9652 1.5757 0.1778  0.0103  -0.3053 504 GLN A CA  
7621  C C   . GLN A 504 ? 1.3821 1.8911 1.4907 0.2084  0.0129  -0.3540 504 GLN A C   
7622  O O   . GLN A 504 ? 1.3391 1.8205 1.4455 0.2211  -0.0036 -0.3889 504 GLN A O   
7623  C CB  . GLN A 504 ? 1.5535 2.0895 1.6022 0.1646  0.0231  -0.2820 504 GLN A CB  
7624  C CG  . GLN A 504 ? 1.5360 2.0519 1.5764 0.1362  0.0203  -0.2336 504 GLN A CG  
7625  C CD  . GLN A 504 ? 1.4867 2.0159 1.5545 0.1250  0.0347  -0.2047 504 GLN A CD  
7626  O OE1 . GLN A 504 ? 1.4395 1.9355 1.5482 0.1254  0.0297  -0.2026 504 GLN A OE1 
7627  N NE2 . GLN A 504 ? 1.4942 2.0726 1.5380 0.1126  0.0516  -0.1809 504 GLN A NE2 
7636  N N   . LYS A 505 ? 1.3343 1.8936 1.4566 0.2208  0.0332  -0.3579 505 LYS A N   
7637  C CA  . LYS A 505 ? 1.3224 1.9083 1.4571 0.2541  0.0380  -0.4070 505 LYS A CA  
7638  C C   . LYS A 505 ? 1.3427 1.9544 1.4251 0.2636  0.0383  -0.4394 505 LYS A C   
7639  O O   . LYS A 505 ? 1.3359 1.9863 1.3689 0.2478  0.0493  -0.4193 505 LYS A O   
7640  C CB  . LYS A 505 ? 1.2945 1.9467 1.4517 0.2644  0.0632  -0.4034 505 LYS A CB  
7641  C CG  . LYS A 505 ? 1.2394 1.8676 1.4514 0.2600  0.0590  -0.3783 505 LYS A CG  
7642  C CD  . LYS A 505 ? 1.2382 1.9402 1.4775 0.2710  0.0822  -0.3766 505 LYS A CD  
7643  C CE  . LYS A 505 ? 1.1899 1.8675 1.4836 0.2679  0.0736  -0.3530 505 LYS A CE  
7644  N NZ  . LYS A 505 ? 1.1587 1.9141 1.4859 0.2781  0.0942  -0.3511 505 LYS A NZ  
7658  N N   . GLY A 506 ? 1.3673 1.9544 1.4585 0.2889  0.0238  -0.4893 506 GLY A N   
7659  C CA  . GLY A 506 ? 1.4067 2.0076 1.4482 0.2982  0.0179  -0.5251 506 GLY A CA  
7660  C C   . GLY A 506 ? 1.3841 1.9280 1.4085 0.2814  -0.0106 -0.5208 506 GLY A C   
7661  O O   . GLY A 506 ? 1.3891 1.9415 1.3700 0.2870  -0.0202 -0.5490 506 GLY A O   
7665  N N   . ALA A 507 ? 1.3624 1.8527 1.4197 0.2611  -0.0243 -0.4878 507 ALA A N   
7666  C CA  . ALA A 507 ? 1.3593 1.8001 1.4123 0.2448  -0.0503 -0.4832 507 ALA A CA  
7667  C C   . ALA A 507 ? 1.3610 1.7378 1.4654 0.2496  -0.0711 -0.5038 507 ALA A C   
7668  O O   . ALA A 507 ? 1.3293 1.6867 1.4761 0.2535  -0.0665 -0.4953 507 ALA A O   
7669  C CB  . ALA A 507 ? 1.2849 1.7180 1.3336 0.2155  -0.0487 -0.4290 507 ALA A CB  
7675  N N   . ILE A 508 ? 1.3846 1.7281 1.4846 0.2474  -0.0962 -0.5290 508 ILE A N   
7676  C CA  . ILE A 508 ? 1.3671 1.6485 1.5132 0.2488  -0.1181 -0.5500 508 ILE A CA  
7677  C C   . ILE A 508 ? 1.3555 1.5997 1.5408 0.2239  -0.1190 -0.5065 508 ILE A C   
7678  O O   . ILE A 508 ? 1.3078 1.5622 1.4824 0.2027  -0.1141 -0.4699 508 ILE A O   
7679  C CB  . ILE A 508 ? 1.3348 1.5931 1.4684 0.2463  -0.1458 -0.5835 508 ILE A CB  
7680  C CG1 . ILE A 508 ? 1.3557 1.6566 1.4371 0.2683  -0.1445 -0.6247 508 ILE A CG1 
7681  C CG2 . ILE A 508 ? 1.3463 1.5401 1.5271 0.2479  -0.1689 -0.6093 508 ILE A CG2 
7682  C CD1 . ILE A 508 ? 1.3713 1.6653 1.4249 0.2598  -0.1707 -0.6449 508 ILE A CD1 
7694  N N   . ARG A 509 ? 1.4004 1.5998 1.6295 0.2270  -0.1263 -0.5108 509 ARG A N   
7695  C CA  . ARG A 509 ? 1.3858 1.5465 1.6494 0.2027  -0.1283 -0.4729 509 ARG A CA  
7696  C C   . ARG A 509 ? 1.3977 1.5027 1.6886 0.1886  -0.1541 -0.4875 509 ARG A C   
7697  O O   . ARG A 509 ? 1.4650 1.5343 1.7744 0.2021  -0.1709 -0.5207 509 ARG A O   
7698  C CB  . ARG A 509 ? 1.3865 1.5380 1.6770 0.2122  -0.1186 -0.4589 509 ARG A CB  
7699  C CG  . ARG A 509 ? 1.3749 1.5791 1.6477 0.2126  -0.0928 -0.4288 509 ARG A CG  
7700  C CD  . ARG A 509 ? 1.4348 1.6397 1.7361 0.2273  -0.0859 -0.4227 509 ARG A CD  
7701  N NE  . ARG A 509 ? 1.4790 1.7304 1.7694 0.2204  -0.0635 -0.3884 509 ARG A NE  
7702  C CZ  . ARG A 509 ? 1.5626 1.8399 1.8722 0.2349  -0.0530 -0.3835 509 ARG A CZ  
7703  N NH1 . ARG A 509 ? 1.6249 1.8855 1.9662 0.2610  -0.0632 -0.4117 509 ARG A NH1 
7704  N NH2 . ARG A 509 ? 1.5582 1.8778 1.8583 0.2237  -0.0344 -0.3511 509 ARG A NH2 
7718  N N   . ARG A 510 ? 1.3097 1.4081 1.6059 0.1610  -0.1576 -0.4630 510 ARG A N   
7719  C CA  . ARG A 510 ? 1.2562 1.3170 1.5768 0.1437  -0.1810 -0.4774 510 ARG A CA  
7720  C C   . ARG A 510 ? 1.2052 1.2103 1.5678 0.1270  -0.1886 -0.4634 510 ARG A C   
7721  O O   . ARG A 510 ? 1.2129 1.1762 1.5989 0.1202  -0.2112 -0.4858 510 ARG A O   
7722  C CB  . ARG A 510 ? 1.2090 1.2935 1.5236 0.1227  -0.1811 -0.4582 510 ARG A CB  
7723  C CG  . ARG A 510 ? 1.2352 1.3682 1.5050 0.1364  -0.1793 -0.4689 510 ARG A CG  
7724  C CD  . ARG A 510 ? 1.2318 1.3902 1.4948 0.1201  -0.1744 -0.4377 510 ARG A CD  
7725  N NE  . ARG A 510 ? 1.2302 1.4002 1.4882 0.1158  -0.1505 -0.3988 510 ARG A NE  
7726  C CZ  . ARG A 510 ? 1.2462 1.4408 1.4880 0.1087  -0.1426 -0.3711 510 ARG A CZ  
7727  N NH1 . ARG A 510 ? 1.2512 1.4632 1.4810 0.1067  -0.1570 -0.3760 510 ARG A NH1 
7728  N NH2 . ARG A 510 ? 1.2500 1.4495 1.4882 0.1041  -0.1229 -0.3388 510 ARG A NH2 
7742  N N   . ALA A 511 ? 1.1682 1.1702 1.5387 0.1184  -0.1722 -0.4260 511 ALA A N   
7743  C CA  . ALA A 511 ? 1.1743 1.1256 1.5772 0.0982  -0.1785 -0.4052 511 ALA A CA  
7744  C C   . ALA A 511 ? 1.1888 1.1121 1.6012 0.1195  -0.1824 -0.4103 511 ALA A C   
7745  O O   . ALA A 511 ? 1.1753 1.1323 1.5722 0.1430  -0.1684 -0.4105 511 ALA A O   
7746  C CB  . ALA A 511 ? 1.1414 1.1049 1.5448 0.0729  -0.1602 -0.3605 511 ALA A CB  
7752  N N   . LEU A 512 ? 1.2197 1.0820 1.6607 0.1104  -0.2029 -0.4136 512 LEU A N   
7753  C CA  . LEU A 512 ? 1.2486 1.0731 1.7055 0.1297  -0.2130 -0.4161 512 LEU A CA  
7754  C C   . LEU A 512 ? 1.2347 1.0006 1.7143 0.0991  -0.2241 -0.3819 512 LEU A C   
7755  O O   . LEU A 512 ? 1.2196 0.9664 1.7084 0.0656  -0.2295 -0.3711 512 LEU A O   
7756  C CB  . LEU A 512 ? 1.3405 1.1386 1.8064 0.1592  -0.2353 -0.4675 512 LEU A CB  
7757  C CG  . LEU A 512 ? 1.3427 1.1965 1.7812 0.1888  -0.2265 -0.5078 512 LEU A CG  
7758  C CD1 . LEU A 512 ? 1.3854 1.2032 1.8337 0.2138  -0.2519 -0.5620 512 LEU A CD1 
7759  C CD2 . LEU A 512 ? 1.3047 1.2160 1.7268 0.2137  -0.2013 -0.4993 512 LEU A CD2 
7771  N N   . PHE A 513 ? 1.2568 0.9976 1.7454 0.1096  -0.2279 -0.3639 513 PHE A N   
7772  C CA  . PHE A 513 ? 1.3054 0.9854 1.8098 0.0815  -0.2417 -0.3296 513 PHE A CA  
7773  C C   . PHE A 513 ? 1.3643 0.9719 1.8942 0.0812  -0.2753 -0.3529 513 PHE A C   
7774  O O   . PHE A 513 ? 1.3860 0.9825 1.9249 0.1155  -0.2904 -0.3956 513 PHE A O   
7775  C CB  . PHE A 513 ? 1.3428 1.0190 1.8467 0.0933  -0.2389 -0.3009 513 PHE A CB  
7776  C CG  . PHE A 513 ? 1.3257 1.0541 1.8061 0.0788  -0.2104 -0.2665 513 PHE A CG  
7777  C CD1 . PHE A 513 ? 1.3186 1.0411 1.7889 0.0379  -0.2005 -0.2320 513 PHE A CD1 
7778  C CD2 . PHE A 513 ? 1.3088 1.0931 1.7781 0.1052  -0.1935 -0.2701 513 PHE A CD2 
7779  C CE1 . PHE A 513 ? 1.2819 1.0481 1.7300 0.0264  -0.1760 -0.2047 513 PHE A CE1 
7780  C CE2 . PHE A 513 ? 1.2768 1.1026 1.7249 0.0904  -0.1705 -0.2394 513 PHE A CE2 
7781  C CZ  . PHE A 513 ? 1.2657 1.0798 1.7025 0.0524  -0.1627 -0.2082 513 PHE A CZ  
7791  N N   . LEU A 514 ? 1.3866 0.9447 1.9278 0.0406  -0.2867 -0.3248 514 LEU A N   
7792  C CA  . LEU A 514 ? 1.4860 0.9720 2.0519 0.0305  -0.3198 -0.3432 514 LEU A CA  
7793  C C   . LEU A 514 ? 1.5938 1.0202 2.1762 0.0637  -0.3477 -0.3568 514 LEU A C   
7794  O O   . LEU A 514 ? 1.6598 1.0625 2.2555 0.0931  -0.3683 -0.4041 514 LEU A O   
7795  C CB  . LEU A 514 ? 1.4989 0.9483 2.0728 -0.0245 -0.3234 -0.3024 514 LEU A CB  
7796  C CG  . LEU A 514 ? 1.5500 0.9325 2.1507 -0.0471 -0.3553 -0.3184 514 LEU A CG  
7797  C CD1 . LEU A 514 ? 1.5482 0.9688 2.1545 -0.0465 -0.3541 -0.3602 514 LEU A CD1 
7798  C CD2 . LEU A 514 ? 1.5361 0.8809 2.1437 -0.1032 -0.3576 -0.2695 514 LEU A CD2 
7810  N N   . TYR A 515 ? 1.6180 1.0197 2.1998 0.0610  -0.3506 -0.3172 515 TYR A N   
7811  C CA  . TYR A 515 ? 1.6782 1.0187 2.2810 0.0923  -0.3814 -0.3259 515 TYR A CA  
7812  C C   . TYR A 515 ? 1.6040 0.9897 2.2120 0.1506  -0.3761 -0.3725 515 TYR A C   
7813  O O   . TYR A 515 ? 1.6172 0.9661 2.2458 0.1831  -0.4005 -0.4171 515 TYR A O   
7814  C CB  . TYR A 515 ? 1.7576 1.0721 2.3546 0.0770  -0.3850 -0.2705 515 TYR A CB  
7815  C CG  . TYR A 515 ? 1.8954 1.1326 2.4945 0.0278  -0.4061 -0.2300 515 TYR A CG  
7816  C CD1 . TYR A 515 ? 1.8884 1.1463 2.4703 -0.0243 -0.3850 -0.1996 515 TYR A CD1 
7817  C CD2 . TYR A 515 ? 2.0320 1.1765 2.6513 0.0332  -0.4475 -0.2216 515 TYR A CD2 
7818  C CE1 . TYR A 515 ? 1.9738 1.1679 2.5566 -0.0728 -0.4012 -0.1611 515 TYR A CE1 
7819  C CE2 . TYR A 515 ? 2.1199 1.1920 2.7378 -0.0160 -0.4673 -0.1802 515 TYR A CE2 
7820  C CZ  . TYR A 515 ? 2.0979 1.1980 2.6965 -0.0705 -0.4424 -0.1495 515 TYR A CZ  
7821  O OH  . TYR A 515 ? 2.1848 1.2195 2.7811 -0.1229 -0.4590 -0.1069 515 TYR A OH  
7831  N N   . SER A 516 ? 1.5702 1.0371 2.1596 0.1637  -0.3436 -0.3640 516 SER A N   
7832  C CA  . SER A 516 ? 1.6014 1.1180 2.1974 0.2159  -0.3356 -0.4003 516 SER A CA  
7833  C C   . SER A 516 ? 1.5554 1.1110 2.1427 0.2375  -0.3272 -0.4559 516 SER A C   
7834  O O   . SER A 516 ? 1.5619 1.1385 2.1600 0.2831  -0.3294 -0.4991 516 SER A O   
7835  C CB  . SER A 516 ? 1.6142 1.2050 2.1931 0.2171  -0.3044 -0.3699 516 SER A CB  
7836  O OG  . SER A 516 ? 1.6584 1.3132 2.2420 0.2615  -0.2901 -0.4047 516 SER A OG  
7842  N N   . ARG A 517 ? 1.5014 1.0706 2.0696 0.2065  -0.3179 -0.4570 517 ARG A N   
7843  C CA  . ARG A 517 ? 1.4406 1.0578 1.9911 0.2225  -0.3075 -0.5031 517 ARG A CA  
7844  C C   . ARG A 517 ? 1.3415 1.0493 1.8700 0.2491  -0.2750 -0.5095 517 ARG A C   
7845  O O   . ARG A 517 ? 1.3230 1.0729 1.8361 0.2751  -0.2675 -0.5529 517 ARG A O   
7846  C CB  . ARG A 517 ? 1.5156 1.0847 2.0836 0.2519  -0.3372 -0.5601 517 ARG A CB  
7847  C CG  . ARG A 517 ? 1.5620 1.0729 2.1368 0.2196  -0.3620 -0.5703 517 ARG A CG  
7848  C CD  . ARG A 517 ? 1.6612 1.0720 2.2695 0.2251  -0.4035 -0.5851 517 ARG A CD  
7849  N NE  . ARG A 517 ? 1.7390 1.1373 2.3513 0.2661  -0.4214 -0.6504 517 ARG A NE  
7850  C CZ  . ARG A 517 ? 1.8469 1.1815 2.4751 0.2678  -0.4524 -0.6593 517 ARG A CZ  
7851  N NH1 . ARG A 517 ? 1.9087 1.2551 2.5302 0.3016  -0.4603 -0.7089 517 ARG A NH1 
7852  N NH2 . ARG A 517 ? 1.8992 1.1584 2.5475 0.2344  -0.4753 -0.6178 517 ARG A NH2 
7866  N N   . SER A 518 ? 1.2937 1.0321 1.8182 0.2406  -0.2561 -0.4661 518 SER A N   
7867  C CA  . SER A 518 ? 1.2676 1.0902 1.7725 0.2563  -0.2250 -0.4619 518 SER A CA  
7868  C C   . SER A 518 ? 1.2411 1.0943 1.7220 0.2185  -0.2031 -0.4161 518 SER A C   
7869  O O   . SER A 518 ? 1.2236 1.0347 1.7090 0.1851  -0.2103 -0.3819 518 SER A O   
7870  C CB  . SER A 518 ? 1.2776 1.1130 1.8058 0.2855  -0.2246 -0.4556 518 SER A CB  
7871  O OG  . SER A 518 ? 1.2719 1.0711 1.8106 0.2616  -0.2320 -0.4062 518 SER A OG  
7877  N N   . PRO A 519 ? 1.2583 1.1837 1.7126 0.2224  -0.1765 -0.4146 519 PRO A N   
7878  C CA  . PRO A 519 ? 1.2623 1.2131 1.6949 0.1897  -0.1578 -0.3741 519 PRO A CA  
7879  C C   . PRO A 519 ? 1.2852 1.2377 1.7236 0.1790  -0.1501 -0.3313 519 PRO A C   
7880  O O   . PRO A 519 ? 1.2320 1.1997 1.6530 0.1522  -0.1360 -0.2989 519 PRO A O   
7881  C CB  . PRO A 519 ? 1.2179 1.2395 1.6200 0.2013  -0.1366 -0.3891 519 PRO A CB  
7882  C CG  . PRO A 519 ? 1.2262 1.2765 1.6366 0.2402  -0.1345 -0.4214 519 PRO A CG  
7883  C CD  . PRO A 519 ? 1.2670 1.2541 1.7086 0.2563  -0.1622 -0.4494 519 PRO A CD  
7891  N N   . SER A 520 ? 1.3301 1.2670 1.7929 0.2001  -0.1609 -0.3319 520 SER A N   
7892  C CA  . SER A 520 ? 1.2939 1.2347 1.7626 0.1923  -0.1573 -0.2933 520 SER A CA  
7893  C C   . SER A 520 ? 1.2883 1.1556 1.7792 0.1850  -0.1844 -0.2765 520 SER A C   
7894  O O   . SER A 520 ? 1.3009 1.1218 1.8136 0.2015  -0.2073 -0.3022 520 SER A O   
7895  C CB  . SER A 520 ? 1.3237 1.3232 1.8040 0.2242  -0.1464 -0.3035 520 SER A CB  
7896  O OG  . SER A 520 ? 1.4274 1.4098 1.9394 0.2607  -0.1642 -0.3380 520 SER A OG  
7902  N N   . HIS A 521 ? 1.2698 1.1243 1.7525 0.1593  -0.1830 -0.2328 521 HIS A N   
7903  C CA  . HIS A 521 ? 1.3232 1.1110 1.8196 0.1488  -0.2085 -0.2080 521 HIS A CA  
7904  C C   . HIS A 521 ? 1.3482 1.1543 1.8371 0.1403  -0.2041 -0.1695 521 HIS A C   
7905  O O   . HIS A 521 ? 1.3133 1.1452 1.7746 0.1133  -0.1844 -0.1449 521 HIS A O   
7906  C CB  . HIS A 521 ? 1.2821 1.0165 1.7664 0.1098  -0.2151 -0.1916 521 HIS A CB  
7907  C CG  . HIS A 521 ? 1.2713 0.9448 1.7559 0.0873  -0.2351 -0.1529 521 HIS A CG  
7908  N ND1 . HIS A 521 ? 1.2349 0.9137 1.6928 0.0544  -0.2234 -0.1113 521 HIS A ND1 
7909  C CD2 . HIS A 521 ? 1.3207 0.9248 1.8258 0.0926  -0.2677 -0.1488 521 HIS A CD2 
7910  C CE1 . HIS A 521 ? 1.2775 0.8958 1.7357 0.0387  -0.2466 -0.0817 521 HIS A CE1 
7911  N NE2 . HIS A 521 ? 1.3358 0.9057 1.8233 0.0610  -0.2749 -0.1017 521 HIS A NE2 
7919  N N   . SER A 522 ? 1.3886 1.1810 1.9037 0.1645  -0.2244 -0.1663 522 SER A N   
7920  C CA  . SER A 522 ? 1.3586 1.1674 1.8710 0.1591  -0.2263 -0.1317 522 SER A CA  
7921  C C   . SER A 522 ? 1.4106 1.1467 1.9142 0.1338  -0.2517 -0.0938 522 SER A C   
7922  O O   . SER A 522 ? 1.4975 1.1685 2.0077 0.1278  -0.2721 -0.0966 522 SER A O   
7923  C CB  . SER A 522 ? 1.3634 1.2117 1.9139 0.2022  -0.2340 -0.1502 522 SER A CB  
7924  O OG  . SER A 522 ? 1.3622 1.2458 1.9102 0.1955  -0.2310 -0.1200 522 SER A OG  
7930  N N   . LYS A 523 ? 1.3665 1.1134 1.8527 0.1166  -0.2513 -0.0571 523 LYS A N   
7931  C CA  . LYS A 523 ? 1.4026 1.0861 1.8697 0.0880  -0.2731 -0.0165 523 LYS A CA  
7932  C C   . LYS A 523 ? 1.4197 1.1237 1.8737 0.0810  -0.2783 0.0168  523 LYS A C   
7933  O O   . LYS A 523 ? 1.3600 1.1189 1.7946 0.0704  -0.2538 0.0216  523 LYS A O   
7934  C CB  . LYS A 523 ? 1.3629 1.0230 1.7929 0.0438  -0.2567 -0.0019 523 LYS A CB  
7935  C CG  . LYS A 523 ? 1.3956 0.9940 1.7986 0.0080  -0.2745 0.0415  523 LYS A CG  
7936  C CD  . LYS A 523 ? 1.4921 1.0140 1.9184 0.0155  -0.3106 0.0431  523 LYS A CD  
7937  C CE  . LYS A 523 ? 1.5775 1.0380 1.9726 -0.0214 -0.3307 0.0923  523 LYS A CE  
7938  N NZ  . LYS A 523 ? 1.6815 1.0581 2.0948 -0.0232 -0.3655 0.0977  523 LYS A NZ  
7952  N N   . ASN A 524 ? 1.4883 1.1453 1.9524 0.0866  -0.3132 0.0402  524 ASN A N   
7953  C CA  . ASN A 524 ? 1.4871 1.1486 1.9303 0.0719  -0.3246 0.0782  524 ASN A CA  
7954  C C   . ASN A 524 ? 1.5406 1.1540 1.9295 0.0227  -0.3239 0.1165  524 ASN A C   
7955  O O   . ASN A 524 ? 1.6228 1.1796 2.0035 0.0055  -0.3311 0.1215  524 ASN A O   
7956  C CB  . ASN A 524 ? 1.5124 1.1483 1.9931 0.1030  -0.3661 0.0865  524 ASN A CB  
7957  C CG  . ASN A 524 ? 1.4581 1.1534 1.9962 0.1529  -0.3646 0.0478  524 ASN A CG  
7958  O OD1 . ASN A 524 ? 1.3622 1.1269 1.9042 0.1593  -0.3316 0.0233  524 ASN A OD1 
7959  N ND2 . ASN A 524 ? 1.5256 1.1948 2.1088 0.1886  -0.4008 0.0426  524 ASN A ND2 
7966  N N   . MET A 525 ? 1.5070 1.1452 1.8583 -0.0013 -0.3147 0.1425  525 MET A N   
7967  C CA  . MET A 525 ? 1.5269 1.1315 1.8213 -0.0483 -0.3089 0.1763  525 MET A CA  
7968  C C   . MET A 525 ? 1.5878 1.1872 1.8531 -0.0603 -0.3298 0.2127  525 MET A C   
7969  O O   . MET A 525 ? 1.6418 1.2680 1.9352 -0.0330 -0.3479 0.2109  525 MET A O   
7970  C CB  . MET A 525 ? 1.4374 1.0833 1.7036 -0.0719 -0.2661 0.1632  525 MET A CB  
7971  C CG  . MET A 525 ? 1.4150 1.0555 1.6985 -0.0716 -0.2486 0.1356  525 MET A CG  
7972  S SD  . MET A 525 ? 1.3560 1.0364 1.6054 -0.1027 -0.2042 0.1267  525 MET A SD  
7973  C CE  . MET A 525 ? 1.3904 1.0312 1.5832 -0.1522 -0.2054 0.1701  525 MET A CE  
7983  N N   . THR A 526 ? 1.5750 1.1434 1.7832 -0.1027 -0.3270 0.2453  526 THR A N   
7984  C CA  . THR A 526 ? 1.5683 1.1268 1.7359 -0.1203 -0.3473 0.2818  526 THR A CA  
7985  C C   . THR A 526 ? 1.5995 1.1564 1.6991 -0.1678 -0.3211 0.3001  526 THR A C   
7986  O O   . THR A 526 ? 1.6665 1.1850 1.7434 -0.1955 -0.3141 0.3126  526 THR A O   
7987  C CB  . THR A 526 ? 1.6012 1.0928 1.7744 -0.1152 -0.3954 0.3131  526 THR A CB  
7988  O OG1 . THR A 526 ? 1.5558 1.0502 1.7987 -0.0666 -0.4180 0.2892  526 THR A OG1 
7989  C CG2 . THR A 526 ? 1.6370 1.1226 1.7684 -0.1305 -0.4207 0.3506  526 THR A CG2 
7997  N N   . ILE A 527 ? 1.5646 1.1647 1.6337 -0.1776 -0.3064 0.3001  527 ILE A N   
7998  C CA  . ILE A 527 ? 1.5907 1.1980 1.5960 -0.2179 -0.2789 0.3100  527 ILE A CA  
7999  C C   . ILE A 527 ? 1.5389 1.1544 1.4997 -0.2303 -0.2950 0.3322  527 ILE A C   
8000  O O   . ILE A 527 ? 1.5095 1.1455 1.4976 -0.2059 -0.3174 0.3303  527 ILE A O   
8001  C CB  . ILE A 527 ? 1.6373 1.2947 1.6517 -0.2164 -0.2352 0.2735  527 ILE A CB  
8002  C CG1 . ILE A 527 ? 1.6542 1.3019 1.7072 -0.2082 -0.2217 0.2530  527 ILE A CG1 
8003  C CG2 . ILE A 527 ? 1.7019 1.3720 1.6538 -0.2529 -0.2078 0.2792  527 ILE A CG2 
8004  C CD1 . ILE A 527 ? 1.5936 1.2880 1.6606 -0.2033 -0.1842 0.2180  527 ILE A CD1 
8016  N N   . SER A 528 ? 1.5667 1.1694 1.4584 -0.2697 -0.2831 0.3523  528 SER A N   
8017  C CA  . SER A 528 ? 1.6697 1.2761 1.5067 -0.2869 -0.2980 0.3730  528 SER A CA  
8018  C C   . SER A 528 ? 1.6678 1.3149 1.4653 -0.3048 -0.2607 0.3515  528 SER A C   
8019  O O   . SER A 528 ? 1.6341 1.2962 1.4301 -0.3144 -0.2231 0.3309  528 SER A O   
8020  C CB  . SER A 528 ? 1.8428 1.3951 1.6205 -0.3190 -0.3220 0.4182  528 SER A CB  
8021  O OG  . SER A 528 ? 1.9156 1.4523 1.6608 -0.3513 -0.2924 0.4235  528 SER A OG  
8027  N N   . ARG A 529 ? 1.7372 1.4011 1.5050 -0.3083 -0.2741 0.3556  529 ARG A N   
8028  C CA  . ARG A 529 ? 1.7675 1.4650 1.4992 -0.3219 -0.2447 0.3328  529 ARG A CA  
8029  C C   . ARG A 529 ? 1.8845 1.5714 1.5517 -0.3578 -0.2150 0.3371  529 ARG A C   
8030  O O   . ARG A 529 ? 1.9706 1.6233 1.5912 -0.3831 -0.2276 0.3699  529 ARG A O   
8031  C CB  . ARG A 529 ? 1.7581 1.4657 1.4613 -0.3251 -0.2714 0.3411  529 ARG A CB  
8032  C CG  . ARG A 529 ? 1.6879 1.4182 1.4576 -0.2922 -0.2985 0.3359  529 ARG A CG  
8033  C CD  . ARG A 529 ? 1.7148 1.4582 1.4570 -0.2999 -0.3254 0.3439  529 ARG A CD  
8034  N NE  . ARG A 529 ? 1.8266 1.5336 1.5084 -0.3222 -0.3574 0.3804  529 ARG A NE  
8035  C CZ  . ARG A 529 ? 1.9086 1.6018 1.5054 -0.3559 -0.3504 0.3884  529 ARG A CZ  
8036  N NH1 . ARG A 529 ? 1.8958 1.6083 1.4610 -0.3693 -0.3123 0.3596  529 ARG A NH1 
8037  N NH2 . ARG A 529 ? 1.9971 1.6568 1.5387 -0.3754 -0.3828 0.4251  529 ARG A NH2 
8051  N N   . GLY A 530 ? 1.8784 1.5968 1.5441 -0.3600 -0.1756 0.3042  530 GLY A N   
8052  C CA  . GLY A 530 ? 1.9116 1.6333 1.5245 -0.3907 -0.1420 0.3008  530 GLY A CA  
8053  C C   . GLY A 530 ? 1.9232 1.6248 1.5464 -0.4048 -0.1313 0.3165  530 GLY A C   
8054  O O   . GLY A 530 ? 1.9599 1.6674 1.5421 -0.4342 -0.1030 0.3182  530 GLY A O   
8058  N N   . GLY A 531 ? 1.8818 1.5613 1.5612 -0.3848 -0.1534 0.3264  531 GLY A N   
8059  C CA  . GLY A 531 ? 1.8621 1.5144 1.5554 -0.3986 -0.1501 0.3426  531 GLY A CA  
8060  C C   . GLY A 531 ? 1.7716 1.4549 1.4978 -0.3984 -0.1095 0.3110  531 GLY A C   
8061  O O   . GLY A 531 ? 1.7212 1.4449 1.4621 -0.3841 -0.0850 0.2763  531 GLY A O   
8065  N N   . LEU A 532 ? 1.7701 1.4314 1.5097 -0.4154 -0.1052 0.3245  532 LEU A N   
8066  C CA  . LEU A 532 ? 1.7281 1.4190 1.5009 -0.4193 -0.0697 0.2979  532 LEU A CA  
8067  C C   . LEU A 532 ? 1.6865 1.3868 1.5343 -0.3796 -0.0752 0.2683  532 LEU A C   
8068  O O   . LEU A 532 ? 1.6853 1.3687 1.5605 -0.3507 -0.1049 0.2698  532 LEU A O   
8069  C CB  . LEU A 532 ? 1.7471 1.4128 1.5082 -0.4567 -0.0643 0.3247  532 LEU A CB  
8070  C CG  . LEU A 532 ? 1.8304 1.4704 1.5143 -0.4980 -0.0711 0.3674  532 LEU A CG  
8071  C CD1 . LEU A 532 ? 1.8708 1.4890 1.5498 -0.5379 -0.0629 0.3940  532 LEU A CD1 
8072  C CD2 . LEU A 532 ? 1.8470 1.5298 1.4713 -0.5128 -0.0417 0.3549  532 LEU A CD2 
8084  N N   . MET A 533 ? 1.6491 1.3807 1.5301 -0.3783 -0.0461 0.2403  533 MET A N   
8085  C CA  . MET A 533 ? 1.5966 1.3405 1.5424 -0.3438 -0.0485 0.2108  533 MET A CA  
8086  C C   . MET A 533 ? 1.6366 1.3358 1.6163 -0.3405 -0.0750 0.2249  533 MET A C   
8087  O O   . MET A 533 ? 1.7219 1.4090 1.7120 -0.3636 -0.0675 0.2308  533 MET A O   
8088  C CB  . MET A 533 ? 1.5533 1.3422 1.5219 -0.3455 -0.0133 0.1790  533 MET A CB  
8089  C CG  . MET A 533 ? 1.4921 1.3035 1.5133 -0.3078 -0.0136 0.1457  533 MET A CG  
8090  S SD  . MET A 533 ? 1.4524 1.3001 1.4598 -0.2852 -0.0034 0.1238  533 MET A SD  
8091  C CE  . MET A 533 ? 1.3984 1.2496 1.4580 -0.2432 -0.0226 0.1061  533 MET A CE  
8101  N N   . GLN A 534 ? 1.5695 1.2449 1.5696 -0.3117 -0.1069 0.2290  534 GLN A N   
8102  C CA  . GLN A 534 ? 1.5304 1.1592 1.5656 -0.3016 -0.1362 0.2377  534 GLN A CA  
8103  C C   . GLN A 534 ? 1.4665 1.1149 1.5594 -0.2734 -0.1293 0.1997  534 GLN A C   
8104  O O   . GLN A 534 ? 1.3942 1.0746 1.5098 -0.2403 -0.1274 0.1749  534 GLN A O   
8105  C CB  . GLN A 534 ? 1.5235 1.1227 1.5587 -0.2799 -0.1740 0.2559  534 GLN A CB  
8106  C CG  . GLN A 534 ? 1.5590 1.1028 1.6295 -0.2667 -0.2087 0.2651  534 GLN A CG  
8107  C CD  . GLN A 534 ? 1.5814 1.0985 1.6548 -0.2439 -0.2479 0.2839  534 GLN A CD  
8108  O OE1 . GLN A 534 ? 1.5647 1.0689 1.6866 -0.2078 -0.2709 0.2688  534 GLN A OE1 
8109  N NE2 . GLN A 534 ? 1.6203 1.1313 1.6424 -0.2641 -0.2565 0.3153  534 GLN A NE2 
8118  N N   . CYS A 535 ? 1.5032 1.1330 1.6180 -0.2887 -0.1266 0.1964  535 CYS A N   
8119  C CA  . CYS A 535 ? 1.4769 1.1260 1.6406 -0.2680 -0.1192 0.1599  535 CYS A CA  
8120  C C   . CYS A 535 ? 1.4591 1.0566 1.6590 -0.2536 -0.1512 0.1579  535 CYS A C   
8121  O O   . CYS A 535 ? 1.4872 1.0303 1.6768 -0.2616 -0.1793 0.1869  535 CYS A O   
8122  C CB  . CYS A 535 ? 1.5490 1.2269 1.7151 -0.2972 -0.0888 0.1503  535 CYS A CB  
8123  S SG  . CYS A 535 ? 1.5782 1.3212 1.7134 -0.3057 -0.0495 0.1395  535 CYS A SG  
8128  N N   . GLU A 536 ? 1.4155 1.0286 1.6571 -0.2310 -0.1487 0.1221  536 GLU A N   
8129  C CA  . GLU A 536 ? 1.4677 1.0337 1.7460 -0.2163 -0.1770 0.1112  536 GLU A CA  
8130  C C   . GLU A 536 ? 1.4218 1.0165 1.7347 -0.2053 -0.1648 0.0715  536 GLU A C   
8131  O O   . GLU A 536 ? 1.3481 0.9968 1.6655 -0.1837 -0.1460 0.0460  536 GLU A O   
8132  C CB  . GLU A 536 ? 1.5046 1.0530 1.7980 -0.1748 -0.2045 0.1057  536 GLU A CB  
8133  C CG  . GLU A 536 ? 1.6487 1.1234 1.9412 -0.1807 -0.2416 0.1353  536 GLU A CG  
8134  C CD  . GLU A 536 ? 1.7085 1.1699 2.0280 -0.1343 -0.2700 0.1233  536 GLU A CD  
8135  O OE1 . GLU A 536 ? 1.7766 1.1968 2.0854 -0.1343 -0.2978 0.1538  536 GLU A OE1 
8136  O OE2 . GLU A 536 ? 1.6830 1.1780 2.0344 -0.0978 -0.2648 0.0834  536 GLU A OE2 
8143  N N   . GLU A 537 ? 1.4541 1.0103 1.7901 -0.2217 -0.1781 0.0678  537 GLU A N   
8144  C CA  . GLU A 537 ? 1.3895 0.9680 1.7583 -0.2165 -0.1711 0.0317  537 GLU A CA  
8145  C C   . GLU A 537 ? 1.4066 0.9478 1.8082 -0.1830 -0.2010 0.0033  537 GLU A C   
8146  O O   . GLU A 537 ? 1.4482 0.9306 1.8539 -0.1751 -0.2304 0.0163  537 GLU A O   
8147  C CB  . GLU A 537 ? 1.4073 0.9770 1.7826 -0.2638 -0.1628 0.0441  537 GLU A CB  
8148  C CG  . GLU A 537 ? 1.4258 1.0392 1.7725 -0.2979 -0.1296 0.0661  537 GLU A CG  
8149  C CD  . GLU A 537 ? 1.5418 1.1611 1.9046 -0.3427 -0.1179 0.0725  537 GLU A CD  
8150  O OE1 . GLU A 537 ? 1.5683 1.1924 1.9703 -0.3395 -0.1244 0.0446  537 GLU A OE1 
8151  O OE2 . GLU A 537 ? 1.6095 1.2314 1.9455 -0.3825 -0.1024 0.1050  537 GLU A OE2 
8158  N N   . LEU A 538 ? 1.3785 0.9539 1.8025 -0.1625 -0.1945 -0.0369 538 LEU A N   
8159  C CA  . LEU A 538 ? 1.4083 0.9516 1.8627 -0.1358 -0.2203 -0.0710 538 LEU A CA  
8160  C C   . LEU A 538 ? 1.4163 1.0001 1.8877 -0.1362 -0.2084 -0.1057 538 LEU A C   
8161  O O   . LEU A 538 ? 1.4112 1.0483 1.8737 -0.1517 -0.1817 -0.1026 538 LEU A O   
8162  C CB  . LEU A 538 ? 1.3605 0.9086 1.8178 -0.0865 -0.2312 -0.0890 538 LEU A CB  
8163  C CG  . LEU A 538 ? 1.2931 0.9109 1.7474 -0.0533 -0.2109 -0.1200 538 LEU A CG  
8164  C CD1 . LEU A 538 ? 1.2575 0.8741 1.7222 -0.0079 -0.2251 -0.1380 538 LEU A CD1 
8165  C CD2 . LEU A 538 ? 1.2684 0.9410 1.6951 -0.0673 -0.1805 -0.0989 538 LEU A CD2 
8177  N N   . ILE A 539 ? 1.4081 0.9652 1.9046 -0.1177 -0.2308 -0.1402 539 ILE A N   
8178  C CA  . ILE A 539 ? 1.3329 0.9180 1.8471 -0.1210 -0.2278 -0.1734 539 ILE A CA  
8179  C C   . ILE A 539 ? 1.2899 0.9017 1.8050 -0.0736 -0.2319 -0.2172 539 ILE A C   
8180  O O   . ILE A 539 ? 1.2892 0.8720 1.8076 -0.0415 -0.2492 -0.2311 539 ILE A O   
8181  C CB  . ILE A 539 ? 1.3791 0.9071 1.9207 -0.1509 -0.2525 -0.1767 539 ILE A CB  
8182  C CG1 . ILE A 539 ? 1.4020 0.8942 1.9374 -0.1974 -0.2511 -0.1274 539 ILE A CG1 
8183  C CG2 . ILE A 539 ? 1.3478 0.9156 1.9087 -0.1634 -0.2466 -0.2043 539 ILE A CG2 
8184  C CD1 . ILE A 539 ? 1.4365 0.8843 1.9988 -0.2397 -0.2688 -0.1223 539 ILE A CD1 
8196  N N   . ALA A 540 ? 1.2792 0.9486 1.7914 -0.0690 -0.2162 -0.2386 540 ALA A N   
8197  C CA  . ALA A 540 ? 1.2995 1.0024 1.8056 -0.0295 -0.2171 -0.2786 540 ALA A CA  
8198  C C   . ALA A 540 ? 1.3554 1.0679 1.8767 -0.0375 -0.2272 -0.3104 540 ALA A C   
8199  O O   . ALA A 540 ? 1.3865 1.0951 1.9253 -0.0736 -0.2275 -0.2990 540 ALA A O   
8200  C CB  . ALA A 540 ? 1.2223 0.9902 1.7018 -0.0136 -0.1895 -0.2700 540 ALA A CB  
8206  N N   . TYR A 541 ? 1.3570 1.0867 1.8715 -0.0042 -0.2353 -0.3512 541 TYR A N   
8207  C CA  . TYR A 541 ? 1.3562 1.0892 1.8829 -0.0085 -0.2513 -0.3860 541 TYR A CA  
8208  C C   . TYR A 541 ? 1.2865 1.0757 1.7874 0.0229  -0.2438 -0.4165 541 TYR A C   
8209  O O   . TYR A 541 ? 1.2344 1.0489 1.7114 0.0528  -0.2308 -0.4186 541 TYR A O   
8210  C CB  . TYR A 541 ? 1.4485 1.1114 1.9975 -0.0063 -0.2847 -0.4121 541 TYR A CB  
8211  C CG  . TYR A 541 ? 1.5195 1.1699 2.0576 0.0400  -0.2977 -0.4530 541 TYR A CG  
8212  C CD1 . TYR A 541 ? 1.5622 1.1811 2.1013 0.0630  -0.3009 -0.4458 541 TYR A CD1 
8213  C CD2 . TYR A 541 ? 1.5455 1.2171 2.0735 0.0611  -0.3079 -0.5009 541 TYR A CD2 
8214  C CE1 . TYR A 541 ? 1.6035 1.2172 2.1385 0.1075  -0.3112 -0.4870 541 TYR A CE1 
8215  C CE2 . TYR A 541 ? 1.5943 1.2588 2.1112 0.1035  -0.3174 -0.5421 541 TYR A CE2 
8216  C CZ  . TYR A 541 ? 1.6031 1.2407 2.1258 0.1275  -0.3177 -0.5361 541 TYR A CZ  
8217  O OH  . TYR A 541 ? 1.6039 1.2419 2.1204 0.1724  -0.3251 -0.5808 541 TYR A OH  
8227  N N   . LEU A 542 ? 1.2988 1.1094 1.8048 0.0137  -0.2528 -0.4382 542 LEU A N   
8228  C CA  . LEU A 542 ? 1.2775 1.1378 1.7557 0.0387  -0.2509 -0.4669 542 LEU A CA  
8229  C C   . LEU A 542 ? 1.3292 1.1635 1.8042 0.0608  -0.2770 -0.5172 542 LEU A C   
8230  O O   . LEU A 542 ? 1.3490 1.1302 1.8520 0.0470  -0.3018 -0.5327 542 LEU A O   
8231  C CB  . LEU A 542 ? 1.2441 1.1467 1.7285 0.0178  -0.2486 -0.4613 542 LEU A CB  
8232  C CG  . LEU A 542 ? 1.2132 1.1650 1.6835 0.0133  -0.2213 -0.4270 542 LEU A CG  
8233  C CD1 . LEU A 542 ? 1.1653 1.1544 1.6501 -0.0031 -0.2259 -0.4291 542 LEU A CD1 
8234  C CD2 . LEU A 542 ? 1.2469 1.2318 1.6744 0.0455  -0.2067 -0.4287 542 LEU A CD2 
8246  N N   . ARG A 543 ? 1.3522 1.2246 1.7911 0.0940  -0.2712 -0.5429 543 ARG A N   
8247  C CA  . ARG A 543 ? 1.4585 1.3165 1.8859 0.1183  -0.2931 -0.5960 543 ARG A CA  
8248  C C   . ARG A 543 ? 1.5141 1.3828 1.9430 0.1026  -0.3143 -0.6195 543 ARG A C   
8249  O O   . ARG A 543 ? 1.5473 1.4461 1.9845 0.0783  -0.3091 -0.5951 543 ARG A O   
8250  C CB  . ARG A 543 ? 1.4831 1.3874 1.8676 0.1570  -0.2760 -0.6146 543 ARG A CB  
8251  C CG  . ARG A 543 ? 1.5365 1.4295 1.9258 0.1800  -0.2621 -0.6066 543 ARG A CG  
8252  C CD  . ARG A 543 ? 1.6489 1.4700 2.0705 0.1890  -0.2874 -0.6317 543 ARG A CD  
8253  N NE  . ARG A 543 ? 1.7009 1.4946 2.1219 0.1950  -0.3163 -0.6830 543 ARG A NE  
8254  C CZ  . ARG A 543 ? 1.7058 1.4295 2.1544 0.2008  -0.3449 -0.7115 543 ARG A CZ  
8255  N NH1 . ARG A 543 ? 1.7476 1.4483 2.1926 0.2050  -0.3722 -0.7602 543 ARG A NH1 
8256  N NH2 . ARG A 543 ? 1.6880 1.3613 2.1666 0.2023  -0.3493 -0.6913 543 ARG A NH2 
8270  N N   . ASP A 544 ? 1.5351 1.3796 1.9578 0.1182  -0.3400 -0.6698 544 ASP A N   
8271  C CA  . ASP A 544 ? 1.5539 1.4092 1.9752 0.1057  -0.3645 -0.6974 544 ASP A CA  
8272  C C   . ASP A 544 ? 1.6237 1.5509 1.9996 0.1178  -0.3519 -0.6962 544 ASP A C   
8273  O O   . ASP A 544 ? 1.6483 1.6103 1.9826 0.1454  -0.3308 -0.6967 544 ASP A O   
8274  C CB  . ASP A 544 ? 1.5422 1.3526 1.9609 0.1224  -0.3961 -0.7557 544 ASP A CB  
8275  C CG  . ASP A 544 ? 1.5542 1.2843 2.0232 0.1015  -0.4192 -0.7567 544 ASP A CG  
8276  O OD1 . ASP A 544 ? 1.5217 1.2347 2.0241 0.0727  -0.4088 -0.7102 544 ASP A OD1 
8277  O OD2 . ASP A 544 ? 1.6288 1.3156 2.0993 0.1127  -0.4450 -0.7963 544 ASP A OD2 
8282  N N   . GLU A 545 ? 1.6484 1.5989 2.0345 0.0956  -0.3663 -0.6930 545 GLU A N   
8283  C CA  . GLU A 545 ? 1.6265 1.6395 1.9716 0.1046  -0.3601 -0.6876 545 GLU A CA  
8284  C C   . GLU A 545 ? 1.6360 1.6689 1.9210 0.1381  -0.3643 -0.7282 545 GLU A C   
8285  O O   . GLU A 545 ? 1.6465 1.7294 1.8841 0.1520  -0.3486 -0.7163 545 GLU A O   
8286  C CB  . GLU A 545 ? 1.6543 1.6841 2.0258 0.0792  -0.3845 -0.6886 545 GLU A CB  
8287  C CG  . GLU A 545 ? 1.6450 1.6671 2.0776 0.0445  -0.3782 -0.6513 545 GLU A CG  
8288  C CD  . GLU A 545 ? 1.6881 1.7358 2.1537 0.0214  -0.4025 -0.6565 545 GLU A CD  
8289  O OE1 . GLU A 545 ? 1.7438 1.8009 2.1894 0.0296  -0.4313 -0.6932 545 GLU A OE1 
8290  O OE2 . GLU A 545 ? 1.6708 1.7327 2.1828 -0.0044 -0.3931 -0.6252 545 GLU A OE2 
8297  N N   . SER A 546 ? 1.6087 1.6023 1.8931 0.1506  -0.3856 -0.7768 546 SER A N   
8298  C CA  . SER A 546 ? 1.5464 1.5610 1.7723 0.1830  -0.3894 -0.8224 546 SER A CA  
8299  C C   . SER A 546 ? 1.4904 1.5365 1.6808 0.2112  -0.3531 -0.8114 546 SER A C   
8300  O O   . SER A 546 ? 1.5171 1.6037 1.6498 0.2351  -0.3464 -0.8368 546 SER A O   
8301  C CB  . SER A 546 ? 1.5547 1.5129 1.7938 0.1922  -0.4194 -0.8794 546 SER A CB  
8302  O OG  . SER A 546 ? 1.5061 1.4081 1.7904 0.1921  -0.4148 -0.8720 546 SER A OG  
8308  N N   . GLU A 547 ? 1.4220 1.4541 1.6445 0.2075  -0.3299 -0.7740 547 GLU A N   
8309  C CA  . GLU A 547 ? 1.4205 1.4809 1.6200 0.2333  -0.2978 -0.7656 547 GLU A CA  
8310  C C   . GLU A 547 ? 1.3633 1.4800 1.5365 0.2262  -0.2693 -0.7166 547 GLU A C   
8311  O O   . GLU A 547 ? 1.3088 1.4642 1.4523 0.2460  -0.2431 -0.7118 547 GLU A O   
8312  C CB  . GLU A 547 ? 1.4402 1.4511 1.6885 0.2359  -0.2925 -0.7551 547 GLU A CB  
8313  C CG  . GLU A 547 ? 1.5571 1.5016 1.8340 0.2434  -0.3233 -0.8013 547 GLU A CG  
8314  C CD  . GLU A 547 ? 1.6120 1.5060 1.9317 0.2506  -0.3207 -0.7907 547 GLU A CD  
8315  O OE1 . GLU A 547 ? 1.5727 1.4808 1.9046 0.2430  -0.2970 -0.7431 547 GLU A OE1 
8316  O OE2 . GLU A 547 ? 1.6995 1.5369 2.0400 0.2642  -0.3450 -0.8303 547 GLU A OE2 
8323  N N   . PHE A 548 ? 1.3927 1.5158 1.5787 0.1987  -0.2741 -0.6813 548 PHE A N   
8324  C CA  . PHE A 548 ? 1.3923 1.5616 1.5535 0.1919  -0.2522 -0.6366 548 PHE A CA  
8325  C C   . PHE A 548 ? 1.4158 1.6015 1.5701 0.1743  -0.2720 -0.6278 548 PHE A C   
8326  O O   . PHE A 548 ? 1.4140 1.5726 1.6129 0.1538  -0.2914 -0.6272 548 PHE A O   
8327  C CB  . PHE A 548 ? 1.3335 1.4892 1.5321 0.1780  -0.2307 -0.5901 548 PHE A CB  
8328  C CG  . PHE A 548 ? 1.3233 1.4400 1.5762 0.1502  -0.2441 -0.5743 548 PHE A CG  
8329  C CD1 . PHE A 548 ? 1.3729 1.4367 1.6661 0.1451  -0.2571 -0.5911 548 PHE A CD1 
8330  C CD2 . PHE A 548 ? 1.2726 1.4064 1.5371 0.1290  -0.2434 -0.5421 548 PHE A CD2 
8331  C CE1 . PHE A 548 ? 1.3700 1.4023 1.7111 0.1153  -0.2671 -0.5737 548 PHE A CE1 
8332  C CE2 . PHE A 548 ? 1.2709 1.3782 1.5867 0.1026  -0.2518 -0.5289 548 PHE A CE2 
8333  C CZ  . PHE A 548 ? 1.3280 1.3863 1.6806 0.0938  -0.2625 -0.5434 548 PHE A CZ  
8343  N N   . ARG A 549 ? 1.4356 1.6671 1.5352 0.1817  -0.2682 -0.6202 549 ARG A N   
8344  C CA  . ARG A 549 ? 1.4547 1.7054 1.5452 0.1684  -0.2879 -0.6062 549 ARG A CA  
8345  C C   . ARG A 549 ? 1.4156 1.6857 1.5084 0.1576  -0.2700 -0.5525 549 ARG A C   
8346  O O   . ARG A 549 ? 1.3805 1.6755 1.4477 0.1543  -0.2816 -0.5363 549 ARG A O   
8347  C CB  . ARG A 549 ? 1.5196 1.8020 1.5433 0.1825  -0.3037 -0.6342 549 ARG A CB  
8348  C CG  . ARG A 549 ? 1.5288 1.8520 1.4879 0.1981  -0.2772 -0.6223 549 ARG A CG  
8349  C CD  . ARG A 549 ? 1.5862 1.9430 1.4736 0.2068  -0.2948 -0.6437 549 ARG A CD  
8350  N NE  . ARG A 549 ? 1.6272 1.9686 1.5070 0.2178  -0.3181 -0.7031 549 ARG A NE  
8351  C CZ  . ARG A 549 ? 1.6824 2.0458 1.5026 0.2250  -0.3400 -0.7327 549 ARG A CZ  
8352  N NH1 . ARG A 549 ? 1.7135 2.0574 1.5305 0.2349  -0.3621 -0.7900 549 ARG A NH1 
8353  N NH2 . ARG A 549 ? 1.7035 2.1054 1.4648 0.2216  -0.3420 -0.7048 549 ARG A NH2 
8367  N N   . ASP A 550 ? 1.4350 1.6910 1.5572 0.1525  -0.2446 -0.5252 550 ASP A N   
8368  C CA  . ASP A 550 ? 1.4199 1.6866 1.5496 0.1414  -0.2280 -0.4773 550 ASP A CA  
8369  C C   . ASP A 550 ? 1.4123 1.6491 1.6070 0.1219  -0.2286 -0.4638 550 ASP A C   
8370  O O   . ASP A 550 ? 1.3894 1.6019 1.6109 0.1182  -0.2130 -0.4575 550 ASP A O   
8371  C CB  . ASP A 550 ? 1.3713 1.6524 1.4754 0.1498  -0.1971 -0.4556 550 ASP A CB  
8372  C CG  . ASP A 550 ? 1.2854 1.5723 1.3952 0.1375  -0.1823 -0.4081 550 ASP A CG  
8373  O OD1 . ASP A 550 ? 1.2466 1.5287 1.3776 0.1259  -0.1955 -0.3939 550 ASP A OD1 
8374  O OD2 . ASP A 550 ? 1.2473 1.5448 1.3430 0.1401  -0.1585 -0.3869 550 ASP A OD2 
8379  N N   . LYS A 551 ? 1.4214 1.6635 1.6414 0.1095  -0.2471 -0.4592 551 LYS A N   
8380  C CA  . LYS A 551 ? 1.3788 1.6041 1.6597 0.0889  -0.2455 -0.4459 551 LYS A CA  
8381  C C   . LYS A 551 ? 1.3109 1.5528 1.5999 0.0828  -0.2336 -0.4085 551 LYS A C   
8382  O O   . LYS A 551 ? 1.2562 1.4941 1.5939 0.0666  -0.2310 -0.3981 551 LYS A O   
8383  C CB  . LYS A 551 ? 1.3902 1.6132 1.7078 0.0777  -0.2750 -0.4731 551 LYS A CB  
8384  C CG  . LYS A 551 ? 1.4265 1.6259 1.7393 0.0824  -0.2918 -0.5142 551 LYS A CG  
8385  C CD  . LYS A 551 ? 1.4390 1.6383 1.7894 0.0680  -0.3240 -0.5395 551 LYS A CD  
8386  C CE  . LYS A 551 ? 1.4869 1.6578 1.8297 0.0729  -0.3450 -0.5841 551 LYS A CE  
8387  N NZ  . LYS A 551 ? 1.5152 1.6860 1.8972 0.0554  -0.3789 -0.6086 551 LYS A NZ  
8401  N N   . LEU A 552 ? 1.3125 1.5729 1.5550 0.0946  -0.2262 -0.3888 552 LEU A N   
8402  C CA  . LEU A 552 ? 1.2863 1.5573 1.5321 0.0914  -0.2203 -0.3559 552 LEU A CA  
8403  C C   . LEU A 552 ? 1.2508 1.5091 1.4965 0.0867  -0.1906 -0.3275 552 LEU A C   
8404  O O   . LEU A 552 ? 1.2052 1.4563 1.4863 0.0756  -0.1812 -0.3115 552 LEU A O   
8405  C CB  . LEU A 552 ? 1.3221 1.6150 1.5157 0.1039  -0.2346 -0.3470 552 LEU A CB  
8406  C CG  . LEU A 552 ? 1.3612 1.6699 1.5673 0.1058  -0.2668 -0.3549 552 LEU A CG  
8407  C CD1 . LEU A 552 ? 1.3881 1.6981 1.6161 0.1034  -0.2886 -0.3938 552 LEU A CD1 
8408  C CD2 . LEU A 552 ? 1.4156 1.7399 1.5599 0.1171  -0.2805 -0.3394 552 LEU A CD2 
8420  N N   . THR A 553 ? 1.2678 1.5271 1.4746 0.0948  -0.1756 -0.3225 553 THR A N   
8421  C CA  . THR A 553 ? 1.2271 1.4779 1.4323 0.0900  -0.1506 -0.2948 553 THR A CA  
8422  C C   . THR A 553 ? 1.1787 1.4041 1.4288 0.0779  -0.1403 -0.2969 553 THR A C   
8423  O O   . THR A 553 ? 1.2190 1.4308 1.4874 0.0775  -0.1472 -0.3214 553 THR A O   
8424  C CB  . THR A 553 ? 1.2504 1.5145 1.4131 0.1006  -0.1369 -0.2927 553 THR A CB  
8425  O OG1 . THR A 553 ? 1.2930 1.5481 1.4664 0.1075  -0.1351 -0.3208 553 THR A OG1 
8426  C CG2 . THR A 553 ? 1.2715 1.5629 1.3830 0.1101  -0.1477 -0.2933 553 THR A CG2 
8434  N N   . PRO A 554 ? 1.1075 1.3232 1.3735 0.0669  -0.1252 -0.2717 554 PRO A N   
8435  C CA  . PRO A 554 ? 1.0747 1.2667 1.3766 0.0526  -0.1155 -0.2702 554 PRO A CA  
8436  C C   . PRO A 554 ? 1.0744 1.2511 1.3680 0.0574  -0.1067 -0.2732 554 PRO A C   
8437  O O   . PRO A 554 ? 1.0831 1.2732 1.3457 0.0713  -0.1018 -0.2728 554 PRO A O   
8438  C CB  . PRO A 554 ? 1.0414 1.2316 1.3498 0.0424  -0.1012 -0.2428 554 PRO A CB  
8439  C CG  . PRO A 554 ? 1.0391 1.2437 1.3094 0.0529  -0.1000 -0.2265 554 PRO A CG  
8440  C CD  . PRO A 554 ? 1.0786 1.3015 1.3285 0.0658  -0.1185 -0.2437 554 PRO A CD  
8448  N N   . ILE A 555 ? 1.0606 1.2104 1.3844 0.0452  -0.1053 -0.2755 555 ILE A N   
8449  C CA  . ILE A 555 ? 1.0699 1.1979 1.3945 0.0500  -0.1013 -0.2777 555 ILE A CA  
8450  C C   . ILE A 555 ? 1.0769 1.1922 1.4054 0.0371  -0.0852 -0.2473 555 ILE A C   
8451  O O   . ILE A 555 ? 1.0988 1.1988 1.4488 0.0171  -0.0820 -0.2366 555 ILE A O   
8452  C CB  . ILE A 555 ? 1.0530 1.1510 1.4056 0.0449  -0.1166 -0.3008 555 ILE A CB  
8453  C CG1 . ILE A 555 ? 1.0481 1.1583 1.3950 0.0567  -0.1353 -0.3341 555 ILE A CG1 
8454  C CG2 . ILE A 555 ? 1.0609 1.1317 1.4162 0.0533  -0.1157 -0.3020 555 ILE A CG2 
8455  C CD1 . ILE A 555 ? 1.0578 1.1370 1.4367 0.0463  -0.1541 -0.3572 555 ILE A CD1 
8467  N N   . THR A 556 ? 1.0650 1.1899 1.3724 0.0471  -0.0749 -0.2340 556 THR A N   
8468  C CA  . THR A 556 ? 1.0854 1.2001 1.3920 0.0357  -0.0622 -0.2059 556 THR A CA  
8469  C C   . THR A 556 ? 1.1132 1.1988 1.4349 0.0355  -0.0656 -0.2050 556 THR A C   
8470  O O   . THR A 556 ? 1.1665 1.2530 1.4893 0.0541  -0.0717 -0.2215 556 THR A O   
8471  C CB  . THR A 556 ? 1.1008 1.2420 1.3805 0.0435  -0.0518 -0.1896 556 THR A CB  
8472  O OG1 . THR A 556 ? 1.1729 1.3359 1.4402 0.0637  -0.0535 -0.2054 556 THR A OG1 
8473  C CG2 . THR A 556 ? 1.0619 1.2190 1.3273 0.0387  -0.0500 -0.1807 556 THR A CG2 
8481  N N   . ILE A 557 ? 1.0940 1.1543 1.4264 0.0153  -0.0624 -0.1862 557 ILE A N   
8482  C CA  . ILE A 557 ? 1.0960 1.1254 1.4374 0.0124  -0.0670 -0.1758 557 ILE A CA  
8483  C C   . ILE A 557 ? 1.1003 1.1410 1.4247 0.0112  -0.0563 -0.1505 557 ILE A C   
8484  O O   . ILE A 557 ? 1.0901 1.1311 1.4041 -0.0066 -0.0466 -0.1314 557 ILE A O   
8485  C CB  . ILE A 557 ? 1.0883 1.0822 1.4464 -0.0130 -0.0713 -0.1674 557 ILE A CB  
8486  C CG1 . ILE A 557 ? 1.0872 1.0695 1.4669 -0.0141 -0.0847 -0.1932 557 ILE A CG1 
8487  C CG2 . ILE A 557 ? 1.1288 1.0861 1.4905 -0.0174 -0.0789 -0.1503 557 ILE A CG2 
8488  C CD1 . ILE A 557 ? 1.0449 1.0592 1.4264 -0.0158 -0.0812 -0.2070 557 ILE A CD1 
8500  N N   . PHE A 558 ? 1.1144 1.1671 1.4376 0.0304  -0.0585 -0.1525 558 PHE A N   
8501  C CA  . PHE A 558 ? 1.1162 1.1854 1.4277 0.0297  -0.0508 -0.1303 558 PHE A CA  
8502  C C   . PHE A 558 ? 1.1115 1.1505 1.4339 0.0256  -0.0601 -0.1149 558 PHE A C   
8503  O O   . PHE A 558 ? 1.1480 1.1640 1.4895 0.0372  -0.0738 -0.1270 558 PHE A O   
8504  C CB  . PHE A 558 ? 1.1559 1.2674 1.4626 0.0516  -0.0460 -0.1403 558 PHE A CB  
8505  C CG  . PHE A 558 ? 1.1850 1.3194 1.4834 0.0480  -0.0385 -0.1173 558 PHE A CG  
8506  C CD1 . PHE A 558 ? 1.1816 1.3264 1.4591 0.0319  -0.0293 -0.0993 558 PHE A CD1 
8507  C CD2 . PHE A 558 ? 1.2185 1.3642 1.5335 0.0612  -0.0427 -0.1150 558 PHE A CD2 
8508  C CE1 . PHE A 558 ? 1.1909 1.3541 1.4617 0.0258  -0.0248 -0.0787 558 PHE A CE1 
8509  C CE2 . PHE A 558 ? 1.2213 1.3921 1.5329 0.0557  -0.0375 -0.0940 558 PHE A CE2 
8510  C CZ  . PHE A 558 ? 1.2059 1.3843 1.4942 0.0364  -0.0287 -0.0755 558 PHE A CZ  
8520  N N   . MET A 559 ? 1.0930 1.1291 1.4017 0.0092  -0.0553 -0.0886 559 MET A N   
8521  C CA  . MET A 559 ? 1.1319 1.1410 1.4447 0.0032  -0.0662 -0.0693 559 MET A CA  
8522  C C   . MET A 559 ? 1.1799 1.2162 1.4851 0.0055  -0.0633 -0.0527 559 MET A C   
8523  O O   . MET A 559 ? 1.2154 1.2677 1.5002 -0.0077 -0.0519 -0.0420 559 MET A O   
8524  C CB  . MET A 559 ? 1.1217 1.0953 1.4210 -0.0258 -0.0656 -0.0516 559 MET A CB  
8525  C CG  . MET A 559 ? 1.1478 1.0909 1.4426 -0.0354 -0.0789 -0.0270 559 MET A CG  
8526  S SD  . MET A 559 ? 1.1617 1.0762 1.4274 -0.0737 -0.0717 -0.0030 559 MET A SD  
8527  C CE  . MET A 559 ? 1.1939 1.0839 1.4464 -0.0792 -0.0903 0.0274  559 MET A CE  
8537  N N   . GLU A 560 ? 1.1872 1.2280 1.5120 0.0225  -0.0753 -0.0515 560 GLU A N   
8538  C CA  . GLU A 560 ? 1.1700 1.2391 1.4962 0.0243  -0.0763 -0.0354 560 GLU A CA  
8539  C C   . GLU A 560 ? 1.1938 1.2310 1.5285 0.0218  -0.0965 -0.0172 560 GLU A C   
8540  O O   . GLU A 560 ? 1.2421 1.2543 1.5992 0.0374  -0.1120 -0.0260 560 GLU A O   
8541  C CB  . GLU A 560 ? 1.2210 1.3411 1.5694 0.0506  -0.0715 -0.0531 560 GLU A CB  
8542  C CG  . GLU A 560 ? 1.3426 1.5026 1.6991 0.0507  -0.0710 -0.0372 560 GLU A CG  
8543  C CD  . GLU A 560 ? 1.4644 1.6835 1.8443 0.0748  -0.0620 -0.0556 560 GLU A CD  
8544  O OE1 . GLU A 560 ? 1.5124 1.7380 1.8975 0.0930  -0.0569 -0.0822 560 GLU A OE1 
8545  O OE2 . GLU A 560 ? 1.5041 1.7660 1.8970 0.0744  -0.0598 -0.0441 560 GLU A OE2 
8552  N N   . TYR A 561 ? 1.1847 1.2189 1.5000 0.0022  -0.0989 0.0080  561 TYR A N   
8553  C CA  . TYR A 561 ? 1.2209 1.2248 1.5373 -0.0030 -0.1207 0.0295  561 TYR A CA  
8554  C C   . TYR A 561 ? 1.2308 1.2705 1.5557 0.0000  -0.1274 0.0429  561 TYR A C   
8555  O O   . TYR A 561 ? 1.1850 1.2487 1.4906 -0.0153 -0.1155 0.0499  561 TYR A O   
8556  C CB  . TYR A 561 ? 1.2244 1.1844 1.5029 -0.0346 -0.1207 0.0493  561 TYR A CB  
8557  C CG  . TYR A 561 ? 1.1824 1.1568 1.4264 -0.0575 -0.1052 0.0586  561 TYR A CG  
8558  C CD1 . TYR A 561 ? 1.1436 1.1275 1.3743 -0.0652 -0.0837 0.0449  561 TYR A CD1 
8559  C CD2 . TYR A 561 ? 1.1900 1.1662 1.4156 -0.0705 -0.1149 0.0796  561 TYR A CD2 
8560  C CE1 . TYR A 561 ? 1.1182 1.1104 1.3198 -0.0831 -0.0718 0.0505  561 TYR A CE1 
8561  C CE2 . TYR A 561 ? 1.1706 1.1549 1.3639 -0.0905 -0.1027 0.0845  561 TYR A CE2 
8562  C CZ  . TYR A 561 ? 1.1401 1.1308 1.3222 -0.0958 -0.0810 0.0693  561 TYR A CZ  
8563  O OH  . TYR A 561 ? 1.1490 1.1433 1.3014 -0.1127 -0.0710 0.0713  561 TYR A OH  
8573  N N   . ARG A 562 ? 1.3119 1.3543 1.6691 0.0200  -0.1485 0.0455  562 ARG A N   
8574  C CA  . ARG A 562 ? 1.3629 1.4439 1.7396 0.0255  -0.1593 0.0572  562 ARG A CA  
8575  C C   . ARG A 562 ? 1.4191 1.4612 1.7940 0.0211  -0.1899 0.0813  562 ARG A C   
8576  O O   . ARG A 562 ? 1.4781 1.4663 1.8459 0.0206  -0.2035 0.0861  562 ARG A O   
8577  C CB  . ARG A 562 ? 1.3841 1.5199 1.8108 0.0595  -0.1562 0.0342  562 ARG A CB  
8578  C CG  . ARG A 562 ? 1.4045 1.6029 1.8539 0.0605  -0.1558 0.0420  562 ARG A CG  
8579  C CD  . ARG A 562 ? 1.4170 1.6784 1.9146 0.0930  -0.1460 0.0161  562 ARG A CD  
8580  N NE  . ARG A 562 ? 1.4570 1.6983 1.9895 0.1265  -0.1628 -0.0024 562 ARG A NE  
8581  C CZ  . ARG A 562 ? 1.4948 1.7237 2.0591 0.1420  -0.1921 0.0066  562 ARG A CZ  
8582  N NH1 . ARG A 562 ? 1.5052 1.7431 2.0691 0.1258  -0.2080 0.0342  562 ARG A NH1 
8583  N NH2 . ARG A 562 ? 1.5134 1.7175 2.1098 0.1743  -0.2086 -0.0127 562 ARG A NH2 
8597  N N   . LEU A 563 ? 1.4011 1.4697 1.7818 0.0158  -0.2029 0.0984  563 LEU A N   
8598  C CA  . LEU A 563 ? 1.4260 1.4607 1.7984 0.0084  -0.2348 0.1252  563 LEU A CA  
8599  C C   . LEU A 563 ? 1.4089 1.4866 1.8364 0.0351  -0.2569 0.1251  563 LEU A C   
8600  O O   . LEU A 563 ? 1.3971 1.5365 1.8461 0.0362  -0.2477 0.1207  563 LEU A O   
8601  C CB  . LEU A 563 ? 1.4244 1.4458 1.7427 -0.0288 -0.2336 0.1479  563 LEU A CB  
8602  C CG  . LEU A 563 ? 1.4438 1.4438 1.7474 -0.0400 -0.2674 0.1771  563 LEU A CG  
8603  C CD1 . LEU A 563 ? 1.5158 1.4532 1.8092 -0.0375 -0.2908 0.1922  563 LEU A CD1 
8604  C CD2 . LEU A 563 ? 1.3971 1.3893 1.6428 -0.0763 -0.2611 0.1916  563 LEU A CD2 
8616  N N   . ASP A 564 ? 1.4238 1.4696 1.8772 0.0561  -0.2870 0.1303  564 ASP A N   
8617  C CA  . ASP A 564 ? 1.4415 1.5234 1.9487 0.0817  -0.3147 0.1337  564 ASP A CA  
8618  C C   . ASP A 564 ? 1.4840 1.5710 1.9652 0.0546  -0.3332 0.1644  564 ASP A C   
8619  O O   . ASP A 564 ? 1.5283 1.5571 1.9666 0.0346  -0.3556 0.1912  564 ASP A O   
8620  C CB  . ASP A 564 ? 1.4881 1.5215 2.0246 0.1101  -0.3474 0.1340  564 ASP A CB  
8621  C CG  . ASP A 564 ? 1.5292 1.6092 2.1369 0.1475  -0.3737 0.1275  564 ASP A CG  
8622  O OD1 . ASP A 564 ? 1.5157 1.6521 2.1390 0.1407  -0.3776 0.1375  564 ASP A OD1 
8623  O OD2 . ASP A 564 ? 1.5739 1.6351 2.2251 0.1840  -0.3914 0.1110  564 ASP A OD2 
8628  N N   . TYR A 565 ? 1.4692 1.6256 1.9733 0.0513  -0.3242 0.1610  565 TYR A N   
8629  C CA  . TYR A 565 ? 1.4870 1.6492 1.9610 0.0207  -0.3387 0.1862  565 TYR A CA  
8630  C C   . TYR A 565 ? 1.6035 1.7641 2.1052 0.0321  -0.3846 0.2069  565 TYR A C   
8631  O O   . TYR A 565 ? 1.6710 1.8002 2.1275 0.0054  -0.4069 0.2334  565 TYR A O   
8632  C CB  . TYR A 565 ? 1.3865 1.6205 1.8773 0.0095  -0.3156 0.1768  565 TYR A CB  
8633  C CG  . TYR A 565 ? 1.3429 1.5696 1.7903 -0.0119 -0.2771 0.1656  565 TYR A CG  
8634  C CD1 . TYR A 565 ? 1.4010 1.5625 1.7838 -0.0338 -0.2687 0.1716  565 TYR A CD1 
8635  C CD2 . TYR A 565 ? 1.2822 1.5698 1.7545 -0.0106 -0.2498 0.1499  565 TYR A CD2 
8636  C CE1 . TYR A 565 ? 1.3937 1.5508 1.7432 -0.0499 -0.2363 0.1600  565 TYR A CE1 
8637  C CE2 . TYR A 565 ? 1.2772 1.5545 1.7107 -0.0285 -0.2193 0.1415  565 TYR A CE2 
8638  C CZ  . TYR A 565 ? 1.3293 1.5413 1.7040 -0.0463 -0.2137 0.1455  565 TYR A CZ  
8639  O OH  . TYR A 565 ? 1.3005 1.5038 1.6423 -0.0609 -0.1858 0.1359  565 TYR A OH  
8649  N N   . ARG A 566 ? 1.6242 1.8188 2.1988 0.0723  -0.4005 0.1941  566 ARG A N   
8650  C CA  . ARG A 566 ? 1.6536 1.8585 2.2656 0.0865  -0.4464 0.2124  566 ARG A CA  
8651  C C   . ARG A 566 ? 1.7501 1.8662 2.3143 0.0766  -0.4831 0.2425  566 ARG A C   
8652  O O   . ARG A 566 ? 1.7658 1.8756 2.3233 0.0676  -0.5212 0.2690  566 ARG A O   
8653  C CB  . ARG A 566 ? 1.5800 1.8378 2.2842 0.1370  -0.4548 0.1879  566 ARG A CB  
8654  C CG  . ARG A 566 ? 1.4491 1.8096 2.2071 0.1459  -0.4232 0.1628  566 ARG A CG  
8655  C CD  . ARG A 566 ? 1.4043 1.8260 2.2571 0.1971  -0.4343 0.1383  566 ARG A CD  
8656  N NE  . ARG A 566 ? 1.4161 1.8613 2.3160 0.2095  -0.4805 0.1565  566 ARG A NE  
8657  C CZ  . ARG A 566 ? 1.4559 1.8432 2.3666 0.2317  -0.5265 0.1703  566 ARG A CZ  
8658  N NH1 . ARG A 566 ? 1.5054 1.8050 2.3832 0.2419  -0.5321 0.1689  566 ARG A NH1 
8659  N NH2 . ARG A 566 ? 1.4527 1.8691 2.4086 0.2425  -0.5696 0.1872  566 ARG A NH2 
8673  N N   . THR A 567 ? 1.7956 1.8434 2.3251 0.0757  -0.4737 0.2405  567 THR A N   
8674  C CA  . THR A 567 ? 1.8537 1.8171 2.3438 0.0675  -0.5098 0.2709  567 THR A CA  
8675  C C   . THR A 567 ? 1.8806 1.8097 2.2856 0.0195  -0.5147 0.3028  567 THR A C   
8676  O O   . THR A 567 ? 1.9809 1.8595 2.3545 0.0094  -0.5538 0.3355  567 THR A O   
8677  C CB  . THR A 567 ? 1.8224 1.7244 2.3007 0.0752  -0.4971 0.2602  567 THR A CB  
8678  O OG1 . THR A 567 ? 1.8861 1.7041 2.3255 0.0632  -0.5333 0.2941  567 THR A OG1 
8679  C CG2 . THR A 567 ? 1.7499 1.6496 2.1778 0.0457  -0.4482 0.2470  567 THR A CG2 
8687  N N   . ALA A 568 ? 1.7661 1.7202 2.1311 -0.0098 -0.4773 0.2935  568 ALA A N   
8688  C CA  . ALA A 568 ? 1.6980 1.6208 1.9791 -0.0541 -0.4759 0.3161  568 ALA A CA  
8689  C C   . ALA A 568 ? 1.6607 1.6283 1.9403 -0.0681 -0.4938 0.3254  568 ALA A C   
8690  O O   . ALA A 568 ? 1.6238 1.5898 1.8451 -0.1021 -0.4789 0.3283  568 ALA A O   
8691  C CB  . ALA A 568 ? 1.6079 1.5240 1.8447 -0.0770 -0.4270 0.2984  568 ALA A CB  
8697  N N   . ALA A 569 ? 1.6781 1.6862 2.0232 -0.0420 -0.5271 0.3287  569 ALA A N   
8698  C CA  . ALA A 569 ? 1.6784 1.7369 2.0338 -0.0547 -0.5462 0.3359  569 ALA A CA  
8699  C C   . ALA A 569 ? 1.7507 1.7602 2.0306 -0.0865 -0.5806 0.3692  569 ALA A C   
8700  O O   . ALA A 569 ? 1.8251 1.7647 2.0418 -0.1008 -0.5856 0.3878  569 ALA A O   
8701  C CB  . ALA A 569 ? 1.6618 1.7829 2.1153 -0.0165 -0.5731 0.3296  569 ALA A CB  
8707  N N   . ASP A 570 ? 1.7294 1.7784 2.0144 -0.0998 -0.6049 0.3772  570 ASP A N   
8708  C CA  . ASP A 570 ? 1.7820 1.7937 1.9938 -0.1310 -0.6397 0.4060  570 ASP A CA  
8709  C C   . ASP A 570 ? 1.7120 1.7664 1.9774 -0.1181 -0.6920 0.4203  570 ASP A C   
8710  O O   . ASP A 570 ? 1.6483 1.7674 2.0092 -0.0869 -0.6960 0.4056  570 ASP A O   
8711  C CB  . ASP A 570 ? 1.8460 1.8555 1.9857 -0.1722 -0.6121 0.3969  570 ASP A CB  
8712  C CG  . ASP A 570 ? 1.9082 1.8624 1.9752 -0.1905 -0.5725 0.3917  570 ASP A CG  
8713  O OD1 . ASP A 570 ? 1.9881 1.8831 2.0027 -0.1982 -0.5863 0.4145  570 ASP A OD1 
8714  O OD2 . ASP A 570 ? 1.8692 1.8402 1.9333 -0.1976 -0.5286 0.3659  570 ASP A OD2 
8719  N N   . THR A 571 ? 1.7249 1.7460 1.9276 -0.1427 -0.7325 0.4487  571 THR A N   
8720  C CA  . THR A 571 ? 1.7126 1.7734 1.9606 -0.1341 -0.7873 0.4642  571 THR A CA  
8721  C C   . THR A 571 ? 1.7180 1.8670 2.0314 -0.1363 -0.7759 0.4409  571 THR A C   
8722  O O   . THR A 571 ? 1.7183 1.9286 2.1181 -0.1130 -0.8074 0.4417  571 THR A O   
8723  C CB  . THR A 571 ? 1.6837 1.6954 1.8370 -0.1684 -0.8281 0.4959  571 THR A CB  
8724  O OG1 . THR A 571 ? 1.6596 1.7164 1.8589 -0.1623 -0.8826 0.5088  571 THR A OG1 
8725  C CG2 . THR A 571 ? 1.6424 1.6382 1.7043 -0.2134 -0.7946 0.4844  571 THR A CG2 
8733  N N   . THR A 572 ? 1.6911 1.8484 1.9672 -0.1645 -0.7323 0.4208  572 THR A N   
8734  C CA  . THR A 572 ? 1.5803 1.8160 1.9167 -0.1703 -0.7177 0.4004  572 THR A CA  
8735  C C   . THR A 572 ? 1.5091 1.8103 1.9528 -0.1314 -0.6955 0.3807  572 THR A C   
8736  O O   . THR A 572 ? 1.4293 1.8105 1.9456 -0.1294 -0.6959 0.3704  572 THR A O   
8737  C CB  . THR A 572 ? 1.4896 1.7076 1.7616 -0.2053 -0.6741 0.3827  572 THR A CB  
8738  O OG1 . THR A 572 ? 1.3946 1.5661 1.6312 -0.1978 -0.6309 0.3723  572 THR A OG1 
8739  C CG2 . THR A 572 ? 1.5591 1.7336 1.7363 -0.2452 -0.6982 0.3952  572 THR A CG2 
8747  N N   . GLY A 573 ? 1.5092 1.7804 1.9642 -0.1017 -0.6763 0.3746  573 GLY A N   
8748  C CA  . GLY A 573 ? 1.3806 1.7067 1.9185 -0.0683 -0.6436 0.3490  573 GLY A CA  
8749  C C   . GLY A 573 ? 1.2234 1.5513 1.7351 -0.0836 -0.5856 0.3263  573 GLY A C   
8750  O O   . GLY A 573 ? 1.1491 1.5336 1.7247 -0.0627 -0.5555 0.3043  573 GLY A O   
8754  N N   . LEU A 574 ? 1.1684 1.4373 1.5874 -0.1184 -0.5696 0.3304  574 LEU A N   
8755  C CA  . LEU A 574 ? 1.0952 1.3645 1.4854 -0.1369 -0.5205 0.3106  574 LEU A CA  
8756  C C   . LEU A 574 ? 1.1215 1.3350 1.4760 -0.1255 -0.4900 0.3022  574 LEU A C   
8757  O O   . LEU A 574 ? 1.1513 1.2967 1.4345 -0.1396 -0.4964 0.3151  574 LEU A O   
8758  C CB  . LEU A 574 ? 1.1121 1.3558 1.4290 -0.1806 -0.5240 0.3161  574 LEU A CB  
8759  C CG  . LEU A 574 ? 1.0699 1.3395 1.3840 -0.2021 -0.4892 0.2979  574 LEU A CG  
8760  C CD1 . LEU A 574 ? 1.0363 1.3934 1.4394 -0.1953 -0.4913 0.2929  574 LEU A CD1 
8761  C CD2 . LEU A 574 ? 1.1207 1.3503 1.3557 -0.2420 -0.4991 0.3015  574 LEU A CD2 
8773  N N   . GLN A 575 ? 1.1333 1.3786 1.5363 -0.1018 -0.4570 0.2807  575 GLN A N   
8774  C CA  . GLN A 575 ? 1.1744 1.3731 1.5517 -0.0905 -0.4288 0.2699  575 GLN A CA  
8775  C C   . GLN A 575 ? 1.1535 1.3237 1.4656 -0.1201 -0.3932 0.2607  575 GLN A C   
8776  O O   . GLN A 575 ? 1.1370 1.3400 1.4490 -0.1384 -0.3798 0.2535  575 GLN A O   
8777  C CB  . GLN A 575 ? 1.2050 1.4499 1.6559 -0.0535 -0.4083 0.2472  575 GLN A CB  
8778  C CG  . GLN A 575 ? 1.3002 1.5910 1.8312 -0.0192 -0.4394 0.2486  575 GLN A CG  
8779  C CD  . GLN A 575 ? 1.3340 1.6899 1.9385 0.0139  -0.4132 0.2206  575 GLN A CD  
8780  O OE1 . GLN A 575 ? 1.3192 1.6799 1.9097 0.0109  -0.3736 0.2024  575 GLN A OE1 
8781  N NE2 . GLN A 575 ? 1.3743 1.7833 2.0572 0.0465  -0.4359 0.2162  575 GLN A NE2 
8790  N N   . PRO A 576 ? 1.1681 1.2777 1.4270 -0.1256 -0.3788 0.2607  576 PRO A N   
8791  C CA  . PRO A 576 ? 1.1655 1.2535 1.3725 -0.1477 -0.3432 0.2477  576 PRO A CA  
8792  C C   . PRO A 576 ? 1.1241 1.2462 1.3713 -0.1307 -0.3080 0.2238  576 PRO A C   
8793  O O   . PRO A 576 ? 1.1290 1.2836 1.4355 -0.1011 -0.3071 0.2151  576 PRO A O   
8794  C CB  . PRO A 576 ? 1.2094 1.2310 1.3586 -0.1563 -0.3411 0.2567  576 PRO A CB  
8795  C CG  . PRO A 576 ? 1.2145 1.2253 1.4038 -0.1287 -0.3632 0.2660  576 PRO A CG  
8796  C CD  . PRO A 576 ? 1.2003 1.2579 1.4460 -0.1132 -0.3959 0.2738  576 PRO A CD  
8804  N N   . ILE A 577 ? 1.1012 1.2151 1.3132 -0.1489 -0.2798 0.2118  577 ILE A N   
8805  C CA  . ILE A 577 ? 1.0828 1.2246 1.3212 -0.1375 -0.2476 0.1916  577 ILE A CA  
8806  C C   . ILE A 577 ? 1.1078 1.2058 1.2968 -0.1476 -0.2214 0.1808  577 ILE A C   
8807  O O   . ILE A 577 ? 1.1412 1.2012 1.2745 -0.1705 -0.2227 0.1856  577 ILE A O   
8808  C CB  . ILE A 577 ? 1.1041 1.2948 1.3644 -0.1493 -0.2425 0.1891  577 ILE A CB  
8809  C CG1 . ILE A 577 ? 1.0683 1.2926 1.3585 -0.1353 -0.2121 0.1720  577 ILE A CG1 
8810  C CG2 . ILE A 577 ? 1.1663 1.3262 1.3700 -0.1821 -0.2430 0.1919  577 ILE A CG2 
8811  C CD1 . ILE A 577 ? 1.0495 1.3263 1.3669 -0.1477 -0.2071 0.1736  577 ILE A CD1 
8823  N N   . LEU A 578 ? 1.0979 1.2051 1.3085 -0.1298 -0.1977 0.1641  578 LEU A N   
8824  C CA  . LEU A 578 ? 1.1094 1.1834 1.2838 -0.1367 -0.1732 0.1519  578 LEU A CA  
8825  C C   . LEU A 578 ? 1.0742 1.1531 1.2247 -0.1548 -0.1585 0.1448  578 LEU A C   
8826  O O   . LEU A 578 ? 1.0228 1.1390 1.1989 -0.1548 -0.1571 0.1439  578 LEU A O   
8827  C CB  . LEU A 578 ? 1.0986 1.1828 1.3049 -0.1121 -0.1563 0.1354  578 LEU A CB  
8828  C CG  . LEU A 578 ? 1.1437 1.2092 1.3707 -0.0933 -0.1700 0.1380  578 LEU A CG  
8829  C CD1 . LEU A 578 ? 1.1212 1.2013 1.3816 -0.0683 -0.1543 0.1166  578 LEU A CD1 
8830  C CD2 . LEU A 578 ? 1.1961 1.2061 1.3774 -0.1110 -0.1748 0.1493  578 LEU A CD2 
8842  N N   . ASN A 579 ? 1.1111 1.1521 1.2134 -0.1707 -0.1479 0.1397  579 ASN A N   
8843  C CA  . ASN A 579 ? 1.1077 1.1441 1.1868 -0.1845 -0.1352 0.1295  579 ASN A CA  
8844  C C   . ASN A 579 ? 1.0675 1.1306 1.1782 -0.1705 -0.1179 0.1181  579 ASN A C   
8845  O O   . ASN A 579 ? 1.0521 1.1122 1.1713 -0.1562 -0.1021 0.1067  579 ASN A O   
8846  C CB  . ASN A 579 ? 1.1278 1.1247 1.1584 -0.1963 -0.1220 0.1199  579 ASN A CB  
8847  C CG  . ASN A 579 ? 1.1348 1.1203 1.1394 -0.2091 -0.1139 0.1073  579 ASN A CG  
8848  O OD1 . ASN A 579 ? 1.1020 1.1046 1.1269 -0.2077 -0.1140 0.1054  579 ASN A OD1 
8849  N ND2 . ASN A 579 ? 1.1695 1.1253 1.1284 -0.2219 -0.1070 0.0985  579 ASN A ND2 
8856  N N   . GLN A 580 ? 1.0888 1.1785 1.2153 -0.1771 -0.1221 0.1225  580 GLN A N   
8857  C CA  . GLN A 580 ? 1.0836 1.2029 1.2368 -0.1669 -0.1076 0.1167  580 GLN A CA  
8858  C C   . GLN A 580 ? 1.0637 1.1564 1.1918 -0.1693 -0.0915 0.1037  580 GLN A C   
8859  O O   . GLN A 580 ? 1.0343 1.1454 1.1781 -0.1588 -0.0794 0.0985  580 GLN A O   
8860  C CB  . GLN A 580 ? 1.1396 1.2967 1.3163 -0.1785 -0.1173 0.1293  580 GLN A CB  
8861  C CG  . GLN A 580 ? 1.1742 1.3726 1.3799 -0.1698 -0.1027 0.1281  580 GLN A CG  
8862  C CD  . GLN A 580 ? 1.2094 1.4665 1.4572 -0.1731 -0.1103 0.1409  580 GLN A CD  
8863  O OE1 . GLN A 580 ? 1.2264 1.5059 1.5008 -0.1637 -0.1225 0.1445  580 GLN A OE1 
8864  N NE2 . GLN A 580 ? 1.1941 1.4779 1.4503 -0.1870 -0.1042 0.1490  580 GLN A NE2 
8873  N N   . PHE A 581 ? 1.1381 1.1903 1.2276 -0.1815 -0.0917 0.0972  581 PHE A N   
8874  C CA  . PHE A 581 ? 1.2113 1.2392 1.2817 -0.1812 -0.0787 0.0825  581 PHE A CA  
8875  C C   . PHE A 581 ? 1.2737 1.2917 1.3427 -0.1667 -0.0628 0.0682  581 PHE A C   
8876  O O   . PHE A 581 ? 1.2938 1.3027 1.3600 -0.1603 -0.0518 0.0552  581 PHE A O   
8877  C CB  . PHE A 581 ? 1.2419 1.2347 1.2744 -0.1997 -0.0860 0.0775  581 PHE A CB  
8878  C CG  . PHE A 581 ? 1.2096 1.2064 1.2432 -0.2173 -0.1036 0.0895  581 PHE A CG  
8879  C CD1 . PHE A 581 ? 1.1183 1.1413 1.1801 -0.2177 -0.1049 0.1000  581 PHE A CD1 
8880  C CD2 . PHE A 581 ? 1.2285 1.2046 1.2333 -0.2360 -0.1194 0.0909  581 PHE A CD2 
8881  C CE1 . PHE A 581 ? 1.0935 1.1223 1.1596 -0.2382 -0.1212 0.1131  581 PHE A CE1 
8882  C CE2 . PHE A 581 ? 1.1935 1.1731 1.2021 -0.2547 -0.1381 0.1015  581 PHE A CE2 
8883  C CZ  . PHE A 581 ? 1.1470 1.1534 1.1887 -0.2567 -0.1388 0.1133  581 PHE A CZ  
8893  N N   . THR A 582 ? 1.3084 1.3269 1.3811 -0.1622 -0.0634 0.0711  582 THR A N   
8894  C CA  . THR A 582 ? 1.3068 1.3195 1.3854 -0.1508 -0.0499 0.0596  582 THR A CA  
8895  C C   . THR A 582 ? 1.2870 1.3270 1.4030 -0.1315 -0.0493 0.0594  582 THR A C   
8896  O O   . THR A 582 ? 1.3228 1.3769 1.4566 -0.1268 -0.0606 0.0699  582 THR A O   
8897  C CB  . THR A 582 ? 1.3128 1.3045 1.3708 -0.1604 -0.0518 0.0643  582 THR A CB  
8898  O OG1 . THR A 582 ? 1.3352 1.3348 1.4098 -0.1563 -0.0674 0.0799  582 THR A OG1 
8899  C CG2 . THR A 582 ? 1.3094 1.2794 1.3249 -0.1805 -0.0543 0.0648  582 THR A CG2 
8907  N N   . PRO A 583 ? 1.2137 1.2631 1.3426 -0.1187 -0.0380 0.0464  583 PRO A N   
8908  C CA  . PRO A 583 ? 1.1457 1.2231 1.3054 -0.0999 -0.0373 0.0428  583 PRO A CA  
8909  C C   . PRO A 583 ? 1.0953 1.1656 1.2694 -0.0919 -0.0426 0.0422  583 PRO A C   
8910  O O   . PRO A 583 ? 1.0822 1.1254 1.2443 -0.0988 -0.0404 0.0398  583 PRO A O   
8911  C CB  . PRO A 583 ? 1.1446 1.2241 1.3056 -0.0907 -0.0260 0.0274  583 PRO A CB  
8912  C CG  . PRO A 583 ? 1.1685 1.2287 1.3059 -0.1031 -0.0236 0.0269  583 PRO A CG  
8913  C CD  . PRO A 583 ? 1.1944 1.2313 1.3112 -0.1191 -0.0273 0.0328  583 PRO A CD  
8921  N N   . ALA A 584 ? 1.0839 1.1795 1.2854 -0.0774 -0.0498 0.0443  584 ALA A N   
8922  C CA  . ALA A 584 ? 1.1238 1.2095 1.3440 -0.0659 -0.0595 0.0432  584 ALA A CA  
8923  C C   . ALA A 584 ? 1.1035 1.1899 1.3410 -0.0482 -0.0530 0.0232  584 ALA A C   
8924  O O   . ALA A 584 ? 1.1090 1.1900 1.3687 -0.0336 -0.0625 0.0181  584 ALA A O   
8925  C CB  . ALA A 584 ? 1.1446 1.2585 1.3915 -0.0554 -0.0728 0.0520  584 ALA A CB  
8931  N N   . ASN A 585 ? 1.0840 1.1748 1.3126 -0.0485 -0.0400 0.0108  585 ASN A N   
8932  C CA  . ASN A 585 ? 1.0654 1.1565 1.3074 -0.0340 -0.0359 -0.0096 585 ASN A CA  
8933  C C   . ASN A 585 ? 1.0500 1.1241 1.2767 -0.0452 -0.0268 -0.0166 585 ASN A C   
8934  O O   . ASN A 585 ? 1.0376 1.1134 1.2461 -0.0557 -0.0205 -0.0115 585 ASN A O   
8935  C CB  . ASN A 585 ? 1.0568 1.1883 1.3110 -0.0155 -0.0311 -0.0214 585 ASN A CB  
8936  C CG  . ASN A 585 ? 1.0734 1.2253 1.3098 -0.0245 -0.0231 -0.0131 585 ASN A CG  
8937  O OD1 . ASN A 585 ? 1.1070 1.2451 1.3269 -0.0325 -0.0182 -0.0155 585 ASN A OD1 
8938  N ND2 . ASN A 585 ? 1.0536 1.2389 1.2962 -0.0233 -0.0228 -0.0031 585 ASN A ND2 
8945  N N   . ILE A 586 ? 1.0605 1.1181 1.2979 -0.0428 -0.0274 -0.0294 586 ILE A N   
8946  C CA  . ILE A 586 ? 1.0627 1.1123 1.2957 -0.0517 -0.0190 -0.0391 586 ILE A CA  
8947  C C   . ILE A 586 ? 1.0495 1.1046 1.3026 -0.0378 -0.0219 -0.0605 586 ILE A C   
8948  O O   . ILE A 586 ? 1.0646 1.1173 1.3330 -0.0247 -0.0307 -0.0679 586 ILE A O   
8949  C CB  . ILE A 586 ? 1.0864 1.1087 1.3099 -0.0734 -0.0161 -0.0298 586 ILE A CB  
8950  C CG1 . ILE A 586 ? 1.1139 1.1116 1.3483 -0.0753 -0.0278 -0.0233 586 ILE A CG1 
8951  C CG2 . ILE A 586 ? 1.1165 1.1350 1.3133 -0.0876 -0.0123 -0.0139 586 ILE A CG2 
8952  C CD1 . ILE A 586 ? 1.1468 1.1177 1.3673 -0.1006 -0.0249 -0.0100 586 ILE A CD1 
8964  N N   . SER A 587 ? 1.0321 1.0944 1.2864 -0.0395 -0.0162 -0.0725 587 SER A N   
8965  C CA  . SER A 587 ? 1.0484 1.1194 1.3189 -0.0269 -0.0211 -0.0941 587 SER A CA  
8966  C C   . SER A 587 ? 0.9870 1.0572 1.2673 -0.0370 -0.0170 -0.1040 587 SER A C   
8967  O O   . SER A 587 ? 0.9590 1.0366 1.2309 -0.0431 -0.0093 -0.0999 587 SER A O   
8968  C CB  . SER A 587 ? 1.1188 1.2187 1.3808 -0.0089 -0.0221 -0.1009 587 SER A CB  
8969  O OG  . SER A 587 ? 1.1869 1.2967 1.4324 -0.0137 -0.0165 -0.0914 587 SER A OG  
8975  N N   . ARG A 588 ? 0.9793 1.0411 1.2806 -0.0383 -0.0235 -0.1184 588 ARG A N   
8976  C CA  . ARG A 588 ? 0.9352 1.0053 1.2552 -0.0457 -0.0224 -0.1323 588 ARG A CA  
8977  C C   . ARG A 588 ? 0.9361 1.0162 1.2685 -0.0297 -0.0356 -0.1552 588 ARG A C   
8978  O O   . ARG A 588 ? 0.9759 1.0477 1.3064 -0.0172 -0.0443 -0.1622 588 ARG A O   
8979  C CB  . ARG A 588 ? 0.9791 1.0302 1.3146 -0.0696 -0.0186 -0.1271 588 ARG A CB  
8980  C CG  . ARG A 588 ? 1.0538 1.0950 1.3706 -0.0876 -0.0057 -0.1052 588 ARG A CG  
8981  C CD  . ARG A 588 ? 1.1237 1.1876 1.4387 -0.0933 0.0089  -0.1079 588 ARG A CD  
8982  N NE  . ARG A 588 ? 1.1959 1.2512 1.4941 -0.1145 0.0227  -0.0923 588 ARG A NE  
8983  C CZ  . ARG A 588 ? 1.2245 1.2713 1.4923 -0.1152 0.0265  -0.0780 588 ARG A CZ  
8984  N NH1 . ARG A 588 ? 1.2036 1.2511 1.4588 -0.0974 0.0184  -0.0753 588 ARG A NH1 
8985  N NH2 . ARG A 588 ? 1.2450 1.2848 1.4938 -0.1358 0.0383  -0.0663 588 ARG A NH2 
8999  N N   . GLN A 589 ? 0.9228 1.0220 1.2681 -0.0285 -0.0382 -0.1690 589 GLN A N   
9000  C CA  . GLN A 589 ? 0.9554 1.0664 1.3069 -0.0137 -0.0529 -0.1915 589 GLN A CA  
9001  C C   . GLN A 589 ? 0.9489 1.0630 1.3342 -0.0257 -0.0602 -0.2077 589 GLN A C   
9002  O O   . GLN A 589 ? 0.9332 1.0605 1.3361 -0.0383 -0.0524 -0.2044 589 GLN A O   
9003  C CB  . GLN A 589 ? 0.9594 1.0955 1.2900 0.0026  -0.0554 -0.1921 589 GLN A CB  
9004  C CG  . GLN A 589 ? 0.9513 1.1013 1.2905 -0.0020 -0.0519 -0.1878 589 GLN A CG  
9005  C CD  . GLN A 589 ? 0.9622 1.1280 1.2779 0.0137  -0.0589 -0.1842 589 GLN A CD  
9006  O OE1 . GLN A 589 ? 0.9607 1.1286 1.2474 0.0230  -0.0595 -0.1772 589 GLN A OE1 
9007  N NE2 . GLN A 589 ? 0.9769 1.1554 1.3065 0.0163  -0.0648 -0.1884 589 GLN A NE2 
9016  N N   . ALA A 590 ? 0.9626 1.0665 1.3590 -0.0216 -0.0753 -0.2272 590 ALA A N   
9017  C CA  . ALA A 590 ? 0.9684 1.0766 1.3983 -0.0328 -0.0871 -0.2458 590 ALA A CA  
9018  C C   . ALA A 590 ? 0.9643 1.0980 1.3898 -0.0147 -0.1031 -0.2673 590 ALA A C   
9019  O O   . ALA A 590 ? 0.9592 1.1023 1.3518 0.0057  -0.1051 -0.2683 590 ALA A O   
9020  C CB  . ALA A 590 ? 0.9758 1.0483 1.4212 -0.0428 -0.0979 -0.2541 590 ALA A CB  
9026  N N   . HIS A 591 ? 0.9555 1.1029 1.4141 -0.0243 -0.1151 -0.2836 591 HIS A N   
9027  C CA  . HIS A 591 ? 0.9715 1.1443 1.4280 -0.0094 -0.1341 -0.3036 591 HIS A CA  
9028  C C   . HIS A 591 ? 0.9880 1.1542 1.4723 -0.0178 -0.1557 -0.3305 591 HIS A C   
9029  O O   . HIS A 591 ? 0.9875 1.1376 1.5058 -0.0410 -0.1545 -0.3305 591 HIS A O   
9030  C CB  . HIS A 591 ? 1.0073 1.2138 1.4808 -0.0093 -0.1319 -0.2971 591 HIS A CB  
9031  C CG  . HIS A 591 ? 1.0315 1.2421 1.4728 0.0031  -0.1185 -0.2755 591 HIS A CG  
9032  N ND1 . HIS A 591 ? 1.0122 1.2098 1.4476 -0.0062 -0.0961 -0.2542 591 HIS A ND1 
9033  C CD2 . HIS A 591 ? 1.0417 1.2650 1.4530 0.0221  -0.1264 -0.2710 591 HIS A CD2 
9034  C CE1 . HIS A 591 ? 1.0093 1.2107 1.4156 0.0066  -0.0912 -0.2394 591 HIS A CE1 
9035  N NE2 . HIS A 591 ? 1.0231 1.2390 1.4146 0.0231  -0.1091 -0.2476 591 HIS A NE2 
9043  N N   . ILE A 592 ? 1.0019 1.1799 1.4689 -0.0005 -0.1765 -0.3525 592 ILE A N   
9044  C CA  . ILE A 592 ? 1.0428 1.2144 1.5307 -0.0059 -0.2015 -0.3827 592 ILE A CA  
9045  C C   . ILE A 592 ? 1.0099 1.2178 1.5351 -0.0143 -0.2160 -0.3908 592 ILE A C   
9046  O O   . ILE A 592 ? 0.9988 1.2369 1.5111 0.0001  -0.2194 -0.3852 592 ILE A O   
9047  C CB  . ILE A 592 ? 1.1010 1.2667 1.5450 0.0183  -0.2168 -0.4064 592 ILE A CB  
9048  C CG1 . ILE A 592 ? 1.1006 1.2330 1.5217 0.0267  -0.2039 -0.4036 592 ILE A CG1 
9049  C CG2 . ILE A 592 ? 1.1657 1.3284 1.6277 0.0142  -0.2472 -0.4416 592 ILE A CG2 
9050  C CD1 . ILE A 592 ? 1.1244 1.2568 1.5030 0.0525  -0.2134 -0.4294 592 ILE A CD1 
9062  N N   . LEU A 593 ? 1.0002 1.2051 1.5744 -0.0382 -0.2263 -0.4030 593 LEU A N   
9063  C CA  . LEU A 593 ? 0.9826 1.2276 1.6033 -0.0483 -0.2417 -0.4136 593 LEU A CA  
9064  C C   . LEU A 593 ? 1.0105 1.2708 1.6112 -0.0291 -0.2739 -0.4397 593 LEU A C   
9065  O O   . LEU A 593 ? 1.0803 1.3149 1.6456 -0.0183 -0.2879 -0.4592 593 LEU A O   
9066  C CB  . LEU A 593 ? 0.9858 1.2233 1.6634 -0.0829 -0.2451 -0.4200 593 LEU A CB  
9067  C CG  . LEU A 593 ? 0.9675 1.2536 1.7120 -0.1038 -0.2503 -0.4242 593 LEU A CG  
9068  C CD1 . LEU A 593 ? 0.9908 1.2998 1.7532 -0.0983 -0.2880 -0.4546 593 LEU A CD1 
9069  C CD2 . LEU A 593 ? 0.9454 1.2730 1.6999 -0.0947 -0.2282 -0.4048 593 LEU A CD2 
9081  N N   . LEU A 594 ? 0.9777 1.2815 1.6006 -0.0235 -0.2865 -0.4409 594 LEU A N   
9082  C CA  . LEU A 594 ? 1.0045 1.3272 1.6078 -0.0063 -0.3202 -0.4620 594 LEU A CA  
9083  C C   . LEU A 594 ? 1.0445 1.4041 1.7139 -0.0217 -0.3447 -0.4789 594 LEU A C   
9084  O O   . LEU A 594 ? 1.0402 1.4290 1.7667 -0.0360 -0.3316 -0.4676 594 LEU A O   
9085  C CB  . LEU A 594 ? 1.0156 1.3553 1.5742 0.0203  -0.3192 -0.4441 594 LEU A CB  
9086  C CG  . LEU A 594 ? 1.0371 1.3493 1.5353 0.0334  -0.2935 -0.4237 594 LEU A CG  
9087  C CD1 . LEU A 594 ? 1.0215 1.3500 1.4838 0.0536  -0.2942 -0.4022 594 LEU A CD1 
9088  C CD2 . LEU A 594 ? 1.1021 1.3876 1.5526 0.0412  -0.2999 -0.4435 594 LEU A CD2 
9100  N N   . ASP A 595 ? 1.1158 1.4780 1.7777 -0.0186 -0.3802 -0.5077 595 ASP A N   
9101  C CA  . ASP A 595 ? 1.1743 1.5735 1.8999 -0.0338 -0.4093 -0.5270 595 ASP A CA  
9102  C C   . ASP A 595 ? 1.1124 1.5287 1.8063 -0.0142 -0.4507 -0.5483 595 ASP A C   
9103  O O   . ASP A 595 ? 1.0437 1.4885 1.7829 -0.0249 -0.4829 -0.5695 595 ASP A O   
9104  C CB  . ASP A 595 ? 1.3370 1.7137 2.1058 -0.0665 -0.4142 -0.5448 595 ASP A CB  
9105  C CG  . ASP A 595 ? 1.4060 1.7712 2.2110 -0.0913 -0.3769 -0.5210 595 ASP A CG  
9106  O OD1 . ASP A 595 ? 1.3966 1.7973 2.2307 -0.0919 -0.3544 -0.4993 595 ASP A OD1 
9107  O OD2 . ASP A 595 ? 1.4573 1.7764 2.2600 -0.1097 -0.3714 -0.5244 595 ASP A OD2 
9112  N N   . GLY B 1   ? 1.1967 1.3541 3.0493 0.1180  -0.0239 0.0013  5   GLY B N   
9113  C CA  . GLY B 1   ? 1.2017 1.3349 3.0478 0.1199  0.0444  -0.0337 5   GLY B CA  
9114  C C   . GLY B 1   ? 1.2001 1.2836 2.8023 0.0893  0.0838  -0.0262 5   GLY B C   
9115  O O   . GLY B 1   ? 1.1911 1.2884 2.7606 0.0573  0.1682  -0.0800 5   GLY B O   
9118  N N   . CYS B 2   ? 1.2229 1.2508 2.6577 0.0957  0.0209  0.0376  6   CYS B N   
9119  C CA  . CYS B 2   ? 1.2578 1.2398 2.4768 0.0735  0.0435  0.0466  6   CYS B CA  
9120  C C   . CYS B 2   ? 1.2875 1.2731 2.3908 0.0414  0.0344  0.0558  6   CYS B C   
9121  O O   . CYS B 2   ? 1.2860 1.2253 2.2234 0.0353  0.0135  0.0836  6   CYS B O   
9122  C CB  . CYS B 2   ? 1.3155 1.2315 2.4310 0.0975  -0.0089 0.0976  6   CYS B CB  
9123  S SG  . CYS B 2   ? 1.3877 1.2586 2.2882 0.0786  0.0279  0.0903  6   CYS B SG  
9128  N N   . ALA B 3   ? 1.3351 1.3745 2.5328 0.0197  0.0513  0.0285  7   ALA B N   
9129  C CA  . ALA B 3   ? 1.3721 1.4114 2.4717 -0.0169 0.0501  0.0325  7   ALA B CA  
9130  C C   . ALA B 3   ? 1.3907 1.4534 2.4738 -0.0683 0.1339  -0.0222 7   ALA B C   
9131  O O   . ALA B 3   ? 1.4074 1.4955 2.4989 -0.1060 0.1496  -0.0394 7   ALA B O   
9132  C CB  . ALA B 3   ? 1.3802 1.4589 2.5809 -0.0122 -0.0037 0.0484  7   ALA B CB  
9138  N N   . LEU B 4   ? 1.3948 1.4474 2.4450 -0.0782 0.1901  -0.0512 8   LEU B N   
9139  C CA  . LEU B 4   ? 1.4576 1.5323 2.4845 -0.1383 0.2730  -0.1059 8   LEU B CA  
9140  C C   . LEU B 4   ? 1.5878 1.6050 2.4023 -0.1784 0.2701  -0.0805 8   LEU B C   
9141  O O   . LEU B 4   ? 1.5971 1.5611 2.2985 -0.1529 0.2096  -0.0287 8   LEU B O   
9142  C CB  . LEU B 4   ? 1.4270 1.5151 2.4990 -0.1400 0.3340  -0.1496 8   LEU B CB  
9143  C CG  . LEU B 4   ? 1.3882 1.5196 2.6810 -0.0961 0.3364  -0.1755 8   LEU B CG  
9144  C CD1 . LEU B 4   ? 1.3984 1.5457 2.7352 -0.1132 0.4156  -0.2342 8   LEU B CD1 
9145  C CD2 . LEU B 4   ? 1.3745 1.5752 2.8589 -0.1012 0.3398  -0.2090 8   LEU B CD2 
9157  N N   . GLY B 5   ? 1.7020 1.7279 2.4662 -0.2463 0.3365  -0.1203 9   GLY B N   
9158  C CA  . GLY B 5   ? 1.7938 1.7573 2.3613 -0.2928 0.3315  -0.0944 9   GLY B CA  
9159  C C   . GLY B 5   ? 1.7740 1.6720 2.2013 -0.2565 0.2788  -0.0454 9   GLY B C   
9160  O O   . GLY B 5   ? 1.7310 1.6346 2.1776 -0.2219 0.2809  -0.0503 9   GLY B O   
9164  N N   . GLY B 6   ? 1.7768 1.6124 2.0718 -0.2653 0.2328  -0.0028 10  GLY B N   
9165  C CA  . GLY B 6   ? 1.7018 1.4821 1.8938 -0.2245 0.1756  0.0377  10  GLY B CA  
9166  C C   . GLY B 6   ? 1.5836 1.3674 1.8381 -0.1651 0.1189  0.0631  10  GLY B C   
9167  O O   . GLY B 6   ? 1.5225 1.3241 1.8416 -0.1658 0.1028  0.0688  10  GLY B O   
9171  N N   . ALA B 7   ? 1.5695 1.3387 1.8008 -0.1210 0.0900  0.0754  11  ALA B N   
9172  C CA  . ALA B 7   ? 1.5466 1.3182 1.8235 -0.0759 0.0417  0.0959  11  ALA B CA  
9173  C C   . ALA B 7   ? 1.5390 1.2854 1.7853 -0.0810 -0.0022 0.1202  11  ALA B C   
9174  O O   . ALA B 7   ? 1.4716 1.2434 1.7915 -0.0721 -0.0258 0.1290  11  ALA B O   
9175  C CB  . ALA B 7   ? 1.5409 1.3651 1.9631 -0.0578 0.0542  0.0839  11  ALA B CB  
9181  N N   . GLU B 8   ? 1.5925 1.2859 1.7313 -0.0971 -0.0165 0.1314  12  GLU B N   
9182  C CA  . GLU B 8   ? 1.5814 1.2388 1.6846 -0.1016 -0.0565 0.1505  12  GLU B CA  
9183  C C   . GLU B 8   ? 1.4689 1.0932 1.5249 -0.0685 -0.1003 0.1581  12  GLU B C   
9184  O O   . GLU B 8   ? 1.4446 1.0375 1.4761 -0.0711 -0.1316 0.1665  12  GLU B O   
9185  C CB  . GLU B 8   ? 1.7170 1.3254 1.7416 -0.1450 -0.0473 0.1584  12  GLU B CB  
9186  C CG  . GLU B 8   ? 1.7781 1.4205 1.8477 -0.1927 0.0008  0.1424  12  GLU B CG  
9187  C CD  . GLU B 8   ? 1.8946 1.4759 1.8629 -0.2485 0.0106  0.1535  12  GLU B CD  
9188  O OE1 . GLU B 8   ? 1.9559 1.4645 1.8208 -0.2449 -0.0245 0.1784  12  GLU B OE1 
9189  O OE2 . GLU B 8   ? 1.9313 1.5352 1.9265 -0.2985 0.0516  0.1363  12  GLU B OE2 
9196  N N   . THR B 9   ? 1.4192 1.0523 1.4677 -0.0419 -0.0978 0.1479  13  THR B N   
9197  C CA  . THR B 9   ? 1.4330 1.0464 1.4491 -0.0158 -0.1296 0.1418  13  THR B CA  
9198  C C   . THR B 9   ? 1.3760 1.0243 1.4321 0.0028  -0.1233 0.1340  13  THR B C   
9199  O O   . THR B 9   ? 1.4087 1.0864 1.5101 0.0042  -0.0937 0.1316  13  THR B O   
9200  C CB  . THR B 9   ? 1.5203 1.0987 1.4711 -0.0068 -0.1374 0.1333  13  THR B CB  
9201  O OG1 . THR B 9   ? 1.6400 1.1802 1.5451 -0.0332 -0.1383 0.1498  13  THR B OG1 
9202  C CG2 . THR B 9   ? 1.5378 1.0915 1.4718 0.0140  -0.1737 0.1188  13  THR B CG2 
9210  N N   . CYS B 10  ? 1.3256 0.9662 1.3644 0.0118  -0.1493 0.1272  14  CYS B N   
9211  C CA  . CYS B 10  ? 1.3194 0.9782 1.3727 0.0201  -0.1466 0.1234  14  CYS B CA  
9212  C C   . CYS B 10  ? 1.3055 0.9702 1.3491 0.0339  -0.1160 0.1055  14  CYS B C   
9213  O O   . CYS B 10  ? 1.2479 0.9300 1.3308 0.0382  -0.0960 0.1093  14  CYS B O   
9214  C CB  . CYS B 10  ? 1.3619 1.0077 1.3756 0.0132  -0.1719 0.1096  14  CYS B CB  
9215  S SG  . CYS B 10  ? 1.4073 1.0616 1.4179 0.0033  -0.1779 0.1183  14  CYS B SG  
9220  N N   . GLU B 11  ? 1.3633 1.0127 1.3613 0.0409  -0.1152 0.0851  15  GLU B N   
9221  C CA  . GLU B 11  ? 1.3927 1.0535 1.3777 0.0494  -0.0877 0.0656  15  GLU B CA  
9222  C C   . GLU B 11  ? 1.3424 1.0202 1.3556 0.0379  -0.0526 0.0745  15  GLU B C   
9223  O O   . GLU B 11  ? 1.2976 0.9959 1.3348 0.0399  -0.0190 0.0613  15  GLU B O   
9224  C CB  . GLU B 11  ? 1.5051 1.1486 1.4450 0.0585  -0.1064 0.0457  15  GLU B CB  
9225  C CG  . GLU B 11  ? 1.5676 1.2256 1.4865 0.0607  -0.0846 0.0289  15  GLU B CG  
9226  C CD  . GLU B 11  ? 1.6318 1.2754 1.5193 0.0740  -0.1177 0.0108  15  GLU B CD  
9227  O OE1 . GLU B 11  ? 1.6429 1.2712 1.5410 0.0870  -0.1492 -0.0026 15  GLU B OE1 
9228  O OE2 . GLU B 11  ? 1.6639 1.3130 1.5222 0.0693  -0.1141 0.0074  15  GLU B OE2 
9235  N N   . ASP B 12  ? 1.3650 1.0339 1.3771 0.0200  -0.0544 0.0910  16  ASP B N   
9236  C CA  . ASP B 12  ? 1.3707 1.0617 1.4140 -0.0025 -0.0123 0.0887  16  ASP B CA  
9237  C C   . ASP B 12  ? 1.3228 1.0477 1.4657 0.0035  0.0076  0.0886  16  ASP B C   
9238  O O   . ASP B 12  ? 1.3338 1.0858 1.5281 -0.0041 0.0517  0.0701  16  ASP B O   
9239  C CB  . ASP B 12  ? 1.4155 1.0858 1.4299 -0.0328 -0.0168 0.1039  16  ASP B CB  
9240  C CG  . ASP B 12  ? 1.4696 1.0989 1.3870 -0.0458 -0.0344 0.1090  16  ASP B CG  
9241  O OD1 . ASP B 12  ? 1.4613 1.0863 1.3465 -0.0251 -0.0487 0.0976  16  ASP B OD1 
9242  O OD2 . ASP B 12  ? 1.5285 1.1280 1.4024 -0.0794 -0.0370 0.1250  16  ASP B OD2 
9247  N N   . CYS B 13  ? 1.2804 1.0034 1.4567 0.0149  -0.0273 0.1079  17  CYS B N   
9248  C CA  . CYS B 13  ? 1.2681 1.0173 1.5450 0.0235  -0.0261 0.1164  17  CYS B CA  
9249  C C   . CYS B 13  ? 1.3097 1.0564 1.6024 0.0413  -0.0138 0.1087  17  CYS B C   
9250  O O   . CYS B 13  ? 1.3195 1.0861 1.7015 0.0467  0.0135  0.1004  17  CYS B O   
9251  C CB  . CYS B 13  ? 1.2436 0.9881 1.5327 0.0245  -0.0766 0.1436  17  CYS B CB  
9252  S SG  . CYS B 13  ? 1.2508 1.0139 1.6483 0.0387  -0.1026 0.1670  17  CYS B SG  
9257  N N   . LEU B 14  ? 1.3117 1.0330 1.5258 0.0481  -0.0308 0.1063  18  LEU B N   
9258  C CA  . LEU B 14  ? 1.2617 0.9741 1.4761 0.0575  -0.0160 0.0968  18  LEU B CA  
9259  C C   . LEU B 14  ? 1.2250 0.9556 1.4658 0.0568  0.0388  0.0670  18  LEU B C   
9260  O O   . LEU B 14  ? 1.2322 0.9602 1.5200 0.0637  0.0609  0.0601  18  LEU B O   
9261  C CB  . LEU B 14  ? 1.2688 0.9596 1.3903 0.0557  -0.0323 0.0840  18  LEU B CB  
9262  C CG  . LEU B 14  ? 1.3164 0.9835 1.4103 0.0466  -0.0695 0.1032  18  LEU B CG  
9263  C CD1 . LEU B 14  ? 1.3693 1.0388 1.4895 0.0391  -0.1096 0.1354  18  LEU B CD1 
9264  C CD2 . LEU B 14  ? 1.2959 0.9528 1.3063 0.0371  -0.0729 0.0719  18  LEU B CD2 
9276  N N   . LEU B 15  ? 1.2259 0.9700 1.4319 0.0431  0.0605  0.0496  19  LEU B N   
9277  C CA  . LEU B 15  ? 1.2634 1.0264 1.4693 0.0310  0.1129  0.0167  19  LEU B CA  
9278  C C   . LEU B 15  ? 1.2563 1.0471 1.5727 0.0217  0.1572  0.0027  19  LEU B C   
9279  O O   . LEU B 15  ? 1.2906 1.0956 1.6398 0.0160  0.2051  -0.0284 19  LEU B O   
9280  C CB  . LEU B 15  ? 1.3450 1.1071 1.4653 0.0100  0.1129  0.0089  19  LEU B CB  
9281  C CG  . LEU B 15  ? 1.4087 1.1906 1.4982 -0.0134 0.1596  -0.0243 19  LEU B CG  
9282  C CD1 . LEU B 15  ? 1.3923 1.1759 1.4560 0.0027  0.1646  -0.0461 19  LEU B CD1 
9283  C CD2 . LEU B 15  ? 1.4770 1.2474 1.4755 -0.0419 0.1449  -0.0174 19  LEU B CD2 
9295  N N   . ILE B 16  ? 1.2313 1.0344 1.6171 0.0186  0.1451  0.0180  20  ILE B N   
9296  C CA  . ILE B 16  ? 1.2485 1.0888 1.7567 0.0057  0.1926  -0.0089 20  ILE B CA  
9297  C C   . ILE B 16  ? 1.2463 1.0861 1.8727 0.0339  0.1972  -0.0114 20  ILE B C   
9298  O O   . ILE B 16  ? 1.2609 1.1252 1.9792 0.0265  0.2530  -0.0512 20  ILE B O   
9299  C CB  . ILE B 16  ? 1.3086 1.1686 1.8679 -0.0074 0.1777  0.0020  20  ILE B CB  
9300  C CG1 . ILE B 16  ? 1.3847 1.2320 1.8227 -0.0426 0.1782  0.0048  20  ILE B CG1 
9301  C CG2 . ILE B 16  ? 1.3136 1.2223 2.0296 -0.0196 0.2282  -0.0367 20  ILE B CG2 
9302  C CD1 . ILE B 16  ? 1.4567 1.3168 1.8437 -0.0870 0.2391  -0.0328 20  ILE B CD1 
9314  N N   . GLY B 17  ? 1.2291 1.0365 1.8543 0.0616  0.1389  0.0297  21  GLY B N   
9315  C CA  . GLY B 17  ? 1.1845 0.9748 1.9138 0.0861  0.1283  0.0406  21  GLY B CA  
9316  C C   . GLY B 17  ? 1.1458 0.8821 1.7883 0.0975  0.0841  0.0755  21  GLY B C   
9317  O O   . GLY B 17  ? 1.1497 0.8692 1.6784 0.0903  0.0473  0.0963  21  GLY B O   
9321  N N   . PRO B 18  ? 1.1461 0.8509 1.8424 0.1103  0.0909  0.0779  22  PRO B N   
9322  C CA  . PRO B 18  ? 1.1415 0.7871 1.7474 0.1097  0.0512  0.1117  22  PRO B CA  
9323  C C   . PRO B 18  ? 1.1343 0.7481 1.7515 0.1142  -0.0288 0.1718  22  PRO B C   
9324  O O   . PRO B 18  ? 1.1126 0.6818 1.6163 0.0976  -0.0640 0.1987  22  PRO B O   
9325  C CB  . PRO B 18  ? 1.2073 0.8230 1.8716 0.1166  0.0901  0.0933  22  PRO B CB  
9326  C CG  . PRO B 18  ? 1.2523 0.9074 2.0880 0.1308  0.1260  0.0649  22  PRO B CG  
9327  C CD  . PRO B 18  ? 1.2097 0.9284 2.0335 0.1170  0.1480  0.0391  22  PRO B CD  
9335  N N   . GLN B 19  ? 1.1910 0.8299 1.9393 0.1301  -0.0583 0.1898  23  GLN B N   
9336  C CA  . GLN B 19  ? 1.3337 0.9455 2.1037 0.1330  -0.1430 0.2502  23  GLN B CA  
9337  C C   . GLN B 19  ? 1.3618 1.0145 2.1070 0.1220  -0.1771 0.2618  23  GLN B C   
9338  O O   . GLN B 19  ? 1.4575 1.1054 2.2445 0.1230  -0.2471 0.3066  23  GLN B O   
9339  C CB  . GLN B 19  ? 1.3734 0.9797 2.3347 0.1629  -0.1682 0.2672  23  GLN B CB  
9340  C CG  . GLN B 19  ? 1.2998 0.9829 2.4340 0.1799  -0.1351 0.2256  23  GLN B CG  
9341  C CD  . GLN B 19  ? 1.2171 0.9294 2.4094 0.1806  -0.0383 0.1559  23  GLN B CD  
9342  O OE1 . GLN B 19  ? 1.1179 0.8374 2.1831 0.1586  0.0159  0.1237  23  GLN B OE1 
9343  N NE2 . GLN B 19  ? 1.2551 0.9862 2.6470 0.2036  -0.0182 0.1293  23  GLN B NE2 
9352  N N   . CYS B 20  ? 1.3021 0.9907 1.9797 0.1094  -0.1341 0.2248  24  CYS B N   
9353  C CA  . CYS B 20  ? 1.3017 1.0251 1.9639 0.0975  -0.1572 0.2298  24  CYS B CA  
9354  C C   . CYS B 20  ? 1.2747 0.9692 1.7803 0.0737  -0.1893 0.2465  24  CYS B C   
9355  O O   . CYS B 20  ? 1.2631 0.9229 1.6659 0.0643  -0.1763 0.2381  24  CYS B O   
9356  C CB  . CYS B 20  ? 1.3302 1.0989 2.0120 0.0918  -0.0946 0.1826  24  CYS B CB  
9357  S SG  . CYS B 20  ? 1.3923 1.1904 2.2178 0.1045  -0.0248 0.1371  24  CYS B SG  
9362  N N   . ALA B 21  ? 1.2928 1.0064 1.7895 0.0604  -0.2274 0.2626  25  ALA B N   
9363  C CA  . ALA B 21  ? 1.3450 1.0359 1.7138 0.0326  -0.2595 0.2736  25  ALA B CA  
9364  C C   . ALA B 21  ? 1.3898 1.1099 1.7431 0.0218  -0.2533 0.2563  25  ALA B C   
9365  O O   . ALA B 21  ? 1.3703 1.1235 1.7972 0.0312  -0.2245 0.2395  25  ALA B O   
9366  C CB  . ALA B 21  ? 1.3801 1.0477 1.7392 0.0147  -0.3310 0.3236  25  ALA B CB  
9372  N N   . TRP B 22  ? 1.4553 1.1596 1.7106 -0.0042 -0.2770 0.2569  26  TRP B N   
9373  C CA  . TRP B 22  ? 1.4249 1.1429 1.6559 -0.0171 -0.2735 0.2402  26  TRP B CA  
9374  C C   . TRP B 22  ? 1.4634 1.1805 1.6535 -0.0500 -0.3239 0.2593  26  TRP B C   
9375  O O   . TRP B 22  ? 1.5279 1.2252 1.6706 -0.0700 -0.3569 0.2802  26  TRP B O   
9376  C CB  . TRP B 22  ? 1.4125 1.1091 1.5642 -0.0148 -0.2372 0.2027  26  TRP B CB  
9377  C CG  . TRP B 22  ? 1.3982 1.0965 1.5429 -0.0199 -0.2278 0.1880  26  TRP B CG  
9378  C CD1 . TRP B 22  ? 1.4185 1.0987 1.5069 -0.0371 -0.2408 0.1729  26  TRP B CD1 
9379  C CD2 . TRP B 22  ? 1.3578 1.0701 1.5511 -0.0139 -0.2011 0.1850  26  TRP B CD2 
9380  N NE1 . TRP B 22  ? 1.4204 1.0939 1.5186 -0.0380 -0.2296 0.1677  26  TRP B NE1 
9381  C CE2 . TRP B 22  ? 1.3684 1.0608 1.5211 -0.0282 -0.2047 0.1761  26  TRP B CE2 
9382  C CE3 . TRP B 22  ? 1.3288 1.0666 1.5960 -0.0040 -0.1706 0.1842  26  TRP B CE3 
9383  C CZ2 . TRP B 22  ? 1.3448 1.0346 1.5112 -0.0372 -0.1824 0.1739  26  TRP B CZ2 
9384  C CZ3 . TRP B 22  ? 1.3058 1.0513 1.5897 -0.0168 -0.1421 0.1736  26  TRP B CZ3 
9385  C CH2 . TRP B 22  ? 1.3153 1.0333 1.5404 -0.0353 -0.1498 0.1722  26  TRP B CH2 
9396  N N   . CYS B 23  ? 1.4729 1.2078 1.6724 -0.0632 -0.3284 0.2513  27  CYS B N   
9397  C CA  . CYS B 23  ? 1.5464 1.2898 1.7165 -0.0997 -0.3722 0.2639  27  CYS B CA  
9398  C C   . CYS B 23  ? 1.5715 1.2961 1.6677 -0.1201 -0.3536 0.2275  27  CYS B C   
9399  O O   . CYS B 23  ? 1.5514 1.2579 1.6373 -0.1009 -0.3159 0.2005  27  CYS B O   
9400  C CB  . CYS B 23  ? 1.5642 1.3532 1.8379 -0.0999 -0.3984 0.2846  27  CYS B CB  
9401  S SG  . CYS B 23  ? 1.6688 1.4805 1.9200 -0.1482 -0.4641 0.3073  27  CYS B SG  
9406  N N   . ALA B 24  ? 1.6197 1.3466 1.6668 -0.1622 -0.3836 0.2264  28  ALA B N   
9407  C CA  . ALA B 24  ? 1.5868 1.2951 1.5773 -0.1854 -0.3662 0.1846  28  ALA B CA  
9408  C C   . ALA B 24  ? 1.5996 1.3304 1.5934 -0.2259 -0.3944 0.1882  28  ALA B C   
9409  O O   . ALA B 24  ? 1.6045 1.3544 1.5743 -0.2623 -0.4356 0.2113  28  ALA B O   
9410  C CB  . ALA B 24  ? 1.5911 1.2753 1.4960 -0.2085 -0.3559 0.1531  28  ALA B CB  
9416  N N   . GLN B 25  ? 1.6249 1.3491 1.6424 -0.2237 -0.3747 0.1672  29  GLN B N   
9417  C CA  . GLN B 25  ? 1.7014 1.4348 1.7126 -0.2642 -0.3850 0.1518  29  GLN B CA  
9418  C C   . GLN B 25  ? 1.6819 1.4656 1.7579 -0.2779 -0.4171 0.1842  29  GLN B C   
9419  O O   . GLN B 25  ? 1.6976 1.4938 1.7767 -0.3119 -0.4224 0.1703  29  GLN B O   
9420  C CB  . GLN B 25  ? 1.7962 1.5256 1.7284 -0.3168 -0.3953 0.1228  29  GLN B CB  
9421  C CG  . GLN B 25  ? 1.8387 1.5684 1.7608 -0.3603 -0.3909 0.0888  29  GLN B CG  
9422  C CD  . GLN B 25  ? 1.7926 1.4782 1.7458 -0.3331 -0.3549 0.0587  29  GLN B CD  
9423  O OE1 . GLN B 25  ? 1.7672 1.4460 1.7690 -0.3018 -0.3481 0.0824  29  GLN B OE1 
9424  N NE2 . GLN B 25  ? 1.7890 1.4413 1.7158 -0.3494 -0.3325 0.0044  29  GLN B NE2 
9433  N N   . GLU B 26  ? 1.6127 1.4278 1.7530 -0.2525 -0.4375 0.2212  30  GLU B N   
9434  C CA  . GLU B 26  ? 1.5329 1.4039 1.7699 -0.2558 -0.4648 0.2433  30  GLU B CA  
9435  C C   . GLU B 26  ? 1.5824 1.4848 1.7987 -0.3097 -0.5055 0.2433  30  GLU B C   
9436  O O   . GLU B 26  ? 1.4913 1.4190 1.7481 -0.3287 -0.4989 0.2282  30  GLU B O   
9437  C CB  . GLU B 26  ? 1.4423 1.3151 1.7426 -0.2369 -0.4195 0.2256  30  GLU B CB  
9438  C CG  . GLU B 26  ? 1.3971 1.3367 1.8197 -0.2383 -0.4348 0.2353  30  GLU B CG  
9439  C CD  . GLU B 26  ? 1.3532 1.2950 1.8402 -0.2168 -0.3815 0.2189  30  GLU B CD  
9440  O OE1 . GLU B 26  ? 1.3508 1.2351 1.7695 -0.2098 -0.3377 0.2041  30  GLU B OE1 
9441  O OE2 . GLU B 26  ? 1.3312 1.3334 1.9398 -0.2106 -0.3847 0.2185  30  GLU B OE2 
9448  N N   . ASN B 27  ? 1.7423 1.6416 1.8856 -0.3422 -0.5465 0.2592  31  ASN B N   
9449  C CA  . ASN B 27  ? 1.8485 1.7800 1.9557 -0.4039 -0.5909 0.2616  31  ASN B CA  
9450  C C   . ASN B 27  ? 1.7366 1.7364 1.9581 -0.4015 -0.6415 0.2927  31  ASN B C   
9451  O O   . ASN B 27  ? 1.6902 1.7297 1.9167 -0.4460 -0.6653 0.2839  31  ASN B O   
9452  C CB  . ASN B 27  ? 2.0328 1.9456 2.0291 -0.4481 -0.6295 0.2795  31  ASN B CB  
9453  C CG  . ASN B 27  ? 2.1093 1.9715 1.9975 -0.4713 -0.5773 0.2289  31  ASN B CG  
9454  O OD1 . ASN B 27  ? 2.0840 1.9288 1.9774 -0.4661 -0.5262 0.1801  31  ASN B OD1 
9455  N ND2 . ASN B 27  ? 2.1914 2.0275 1.9863 -0.4997 -0.5911 0.2383  31  ASN B ND2 
9462  N N   . GLY B 35  ? 1.4172 1.2258 1.8286 -0.2020 -0.1279 0.1526  39  GLY B N   
9463  C CA  . GLY B 35  ? 1.3821 1.2694 1.9280 -0.1838 -0.1261 0.1429  39  GLY B CA  
9464  C C   . GLY B 35  ? 1.3692 1.2523 1.9189 -0.1493 -0.1122 0.1443  39  GLY B C   
9465  O O   . GLY B 35  ? 1.3664 1.1972 1.8195 -0.1486 -0.0899 0.1448  39  GLY B O   
9468  N N   . GLU B 36  ? 1.3562 1.2927 2.0220 -0.1211 -0.1297 0.1457  40  GLU B N   
9469  C CA  . GLU B 36  ? 1.3501 1.2837 2.0363 -0.0886 -0.1167 0.1454  40  GLU B CA  
9470  C C   . GLU B 36  ? 1.3154 1.2475 2.0165 -0.0569 -0.1787 0.1788  40  GLU B C   
9471  O O   . GLU B 36  ? 1.2561 1.2325 2.0827 -0.0402 -0.2070 0.1863  40  GLU B O   
9472  C CB  . GLU B 36  ? 1.4040 1.3952 2.2297 -0.0916 -0.0680 0.1087  40  GLU B CB  
9473  C CG  . GLU B 36  ? 1.5172 1.5036 2.3017 -0.1374 0.0021  0.0725  40  GLU B CG  
9474  C CD  . GLU B 36  ? 1.5806 1.6329 2.5123 -0.1504 0.0610  0.0215  40  GLU B CD  
9475  O OE1 . GLU B 36  ? 1.5745 1.6803 2.6670 -0.1175 0.0405  0.0144  40  GLU B OE1 
9476  O OE2 . GLU B 36  ? 1.6368 1.6854 2.5255 -0.1974 0.1268  -0.0132 40  GLU B OE2 
9483  N N   . ARG B 37  ? 1.3743 1.2529 1.9484 -0.0526 -0.2017 0.1974  41  ARG B N   
9484  C CA  . ARG B 37  ? 1.4105 1.2768 1.9669 -0.0362 -0.2521 0.2261  41  ARG B CA  
9485  C C   . ARG B 37  ? 1.4566 1.3156 2.0468 -0.0075 -0.2378 0.2278  41  ARG B C   
9486  O O   . ARG B 37  ? 1.5594 1.4122 2.1705 0.0043  -0.2809 0.2556  41  ARG B O   
9487  C CB  . ARG B 37  ? 1.3695 1.1864 1.7866 -0.0486 -0.2680 0.2300  41  ARG B CB  
9488  C CG  . ARG B 37  ? 1.3321 1.1442 1.7095 -0.0780 -0.2775 0.2235  41  ARG B CG  
9489  C CD  . ARG B 37  ? 1.3258 1.0839 1.5862 -0.0837 -0.2714 0.2097  41  ARG B CD  
9490  N NE  . ARG B 37  ? 1.3491 1.1011 1.5675 -0.1120 -0.3030 0.2087  41  ARG B NE  
9491  C CZ  . ARG B 37  ? 1.3796 1.1300 1.5992 -0.1360 -0.3019 0.2001  41  ARG B CZ  
9492  N NH1 . ARG B 37  ? 1.3770 1.1275 1.6297 -0.1383 -0.2719 0.1948  41  ARG B NH1 
9493  N NH2 . ARG B 37  ? 1.4296 1.1764 1.6116 -0.1652 -0.3272 0.1936  41  ARG B NH2 
9507  N N   . CYS B 38  ? 1.3740 1.2284 1.9616 -0.0018 -0.1797 0.1998  42  CYS B N   
9508  C CA  . CYS B 38  ? 1.3106 1.1586 1.9309 0.0215  -0.1566 0.1935  42  CYS B CA  
9509  C C   . CYS B 38  ? 1.2761 1.1648 2.0622 0.0393  -0.1687 0.1969  42  CYS B C   
9510  O O   . CYS B 38  ? 1.2626 1.1987 2.1601 0.0331  -0.1351 0.1673  42  CYS B O   
9511  C CB  . CYS B 38  ? 1.2874 1.1305 1.8708 0.0138  -0.0903 0.1581  42  CYS B CB  
9512  S SG  . CYS B 38  ? 1.2643 1.0853 1.8270 0.0349  -0.0599 0.1460  42  CYS B SG  
9517  N N   . ASP B 39  ? 1.2670 1.1351 2.0750 0.0582  -0.2172 0.2305  43  ASP B N   
9518  C CA  . ASP B 39  ? 1.2717 1.1673 2.2498 0.0818  -0.2438 0.2407  43  ASP B CA  
9519  C C   . ASP B 39  ? 1.2906 1.1315 2.2341 0.0959  -0.2954 0.2855  43  ASP B C   
9520  O O   . ASP B 39  ? 1.3220 1.1136 2.1120 0.0821  -0.2988 0.2986  43  ASP B O   
9521  C CB  . ASP B 39  ? 1.2690 1.2164 2.3495 0.0753  -0.2896 0.2507  43  ASP B CB  
9522  C CG  . ASP B 39  ? 1.2377 1.2462 2.5368 0.0949  -0.2723 0.2195  43  ASP B CG  
9523  O OD1 . ASP B 39  ? 1.2391 1.2359 2.6393 0.1248  -0.2761 0.2220  43  ASP B OD1 
9524  O OD2 . ASP B 39  ? 1.2181 1.2860 2.5946 0.0780  -0.2513 0.1870  43  ASP B OD2 
9529  N N   . THR B 40  ? 1.2676 1.1155 2.3603 0.1208  -0.3362 0.3066  44  THR B N   
9530  C CA  . THR B 40  ? 1.2916 1.0748 2.3538 0.1294  -0.3921 0.3571  44  THR B CA  
9531  C C   . THR B 40  ? 1.3800 1.1311 2.2994 0.0966  -0.4651 0.4083  44  THR B C   
9532  O O   . THR B 40  ? 1.4152 1.2068 2.3528 0.0822  -0.5035 0.4180  44  THR B O   
9533  C CB  . THR B 40  ? 1.2804 1.0737 2.5511 0.1648  -0.4359 0.3749  44  THR B CB  
9534  O OG1 . THR B 40  ? 1.1828 1.0220 2.6038 0.1870  -0.3573 0.3112  44  THR B OG1 
9535  C CG2 . THR B 40  ? 1.3760 1.0927 2.5893 0.1647  -0.4772 0.4187  44  THR B CG2 
9543  N N   . PRO B 41  ? 1.4351 1.1166 2.2078 0.0765  -0.4803 0.4354  45  PRO B N   
9544  C CA  . PRO B 41  ? 1.5171 1.1704 2.1438 0.0316  -0.5410 0.4747  45  PRO B CA  
9545  C C   . PRO B 41  ? 1.6175 1.2859 2.3194 0.0252  -0.6379 0.5286  45  PRO B C   
9546  O O   . PRO B 41  ? 1.6924 1.3813 2.3197 -0.0112 -0.6721 0.5386  45  PRO B O   
9547  C CB  . PRO B 41  ? 1.5372 1.1098 2.0335 0.0103  -0.5423 0.4951  45  PRO B CB  
9548  C CG  . PRO B 41  ? 1.4821 1.0428 2.0558 0.0483  -0.4797 0.4649  45  PRO B CG  
9549  C CD  . PRO B 41  ? 1.4044 1.0383 2.1171 0.0824  -0.4262 0.4162  45  PRO B CD  
9557  N N   . ALA B 42  ? 1.5946 1.2674 2.4306 0.0509  -0.6665 0.5428  46  ALA B N   
9558  C CA  . ALA B 42  ? 1.5918 1.2908 2.4926 0.0388  -0.7468 0.5759  46  ALA B CA  
9559  C C   . ALA B 42  ? 1.5452 1.3275 2.5495 0.0460  -0.7519 0.5545  46  ALA B C   
9560  O O   . ALA B 42  ? 1.6105 1.4136 2.5830 0.0143  -0.8130 0.5799  46  ALA B O   
9561  C CB  . ALA B 42  ? 1.5616 1.2513 2.6106 0.0705  -0.7693 0.5845  46  ALA B CB  
9567  N N   . ASN B 43  ? 1.4257 1.2571 2.5526 0.0821  -0.6858 0.5054  47  ASN B N   
9568  C CA  . ASN B 43  ? 1.3468 1.2611 2.5722 0.0831  -0.6798 0.4767  47  ASN B CA  
9569  C C   . ASN B 43  ? 1.3667 1.2795 2.4087 0.0339  -0.6716 0.4724  47  ASN B C   
9570  O O   . ASN B 43  ? 1.3503 1.3125 2.4181 0.0128  -0.7086 0.4752  47  ASN B O   
9571  C CB  . ASN B 43  ? 1.2240 1.1846 2.5603 0.1076  -0.5787 0.4043  47  ASN B CB  
9572  C CG  . ASN B 43  ? 1.2142 1.1764 2.7374 0.1529  -0.5711 0.3938  47  ASN B CG  
9573  O OD1 . ASN B 43  ? 1.2958 1.2039 2.7939 0.1554  -0.6134 0.4289  47  ASN B OD1 
9574  N ND2 . ASN B 43  ? 1.1510 1.1728 2.8130 0.1667  -0.4924 0.3254  47  ASN B ND2 
9581  N N   . LEU B 44  ? 1.4252 1.2843 2.2923 0.0148  -0.6226 0.4602  48  LEU B N   
9582  C CA  . LEU B 44  ? 1.5002 1.3541 2.2096 -0.0295 -0.6113 0.4477  48  LEU B CA  
9583  C C   . LEU B 44  ? 1.6341 1.4733 2.2625 -0.0729 -0.6995 0.4978  48  LEU B C   
9584  O O   . LEU B 44  ? 1.6664 1.5380 2.2563 -0.1072 -0.7152 0.4899  48  LEU B O   
9585  C CB  . LEU B 44  ? 1.4813 1.2837 2.0459 -0.0365 -0.5466 0.4199  48  LEU B CB  
9586  C CG  . LEU B 44  ? 1.4038 1.2114 2.0228 -0.0008 -0.4657 0.3767  48  LEU B CG  
9587  C CD1 . LEU B 44  ? 1.4035 1.1758 1.8783 -0.0135 -0.4109 0.3442  48  LEU B CD1 
9588  C CD2 . LEU B 44  ? 1.3291 1.1994 2.0756 0.0122  -0.4323 0.3439  48  LEU B CD2 
9600  N N   . LEU B 45  ? 1.6811 1.4672 2.2744 -0.0789 -0.7580 0.5501  49  LEU B N   
9601  C CA  . LEU B 45  ? 1.7111 1.4812 2.2248 -0.1292 -0.8497 0.6036  49  LEU B CA  
9602  C C   . LEU B 45  ? 1.6780 1.5162 2.3360 -0.1219 -0.9017 0.6123  49  LEU B C   
9603  O O   . LEU B 45  ? 1.6955 1.5542 2.2906 -0.1699 -0.9481 0.6264  49  LEU B O   
9604  C CB  . LEU B 45  ? 1.7632 1.4603 2.2071 -0.1440 -0.8735 0.6376  49  LEU B CB  
9605  C CG  . LEU B 45  ? 1.7553 1.3827 1.9848 -0.1987 -0.8570 0.6413  49  LEU B CG  
9606  C CD1 . LEU B 45  ? 1.8001 1.3581 1.9931 -0.2038 -0.8708 0.6701  49  LEU B CD1 
9607  C CD2 . LEU B 45  ? 1.8169 1.4480 1.9044 -0.2762 -0.8976 0.6519  49  LEU B CD2 
9619  N N   . ALA B 46  ? 1.6326 1.5087 2.4879 -0.0659 -0.8906 0.5977  50  ALA B N   
9620  C CA  . ALA B 46  ? 1.6752 1.6209 2.6873 -0.0561 -0.9348 0.5965  50  ALA B CA  
9621  C C   . ALA B 46  ? 1.6807 1.7019 2.7137 -0.0728 -0.9209 0.5652  50  ALA B C   
9622  O O   . ALA B 46  ? 1.6854 1.7564 2.7657 -0.0937 -0.9687 0.5704  50  ALA B O   
9623  C CB  . ALA B 46  ? 1.6139 1.5881 2.8426 0.0041  -0.9118 0.5713  50  ALA B CB  
9629  N N   . LYS B 47  ? 1.7478 1.5460 1.5854 -0.4895 -0.5637 0.0215  51  LYS B N   
9630  C CA  . LYS B 47  ? 1.8480 1.5997 1.6766 -0.5260 -0.5992 0.0323  51  LYS B CA  
9631  C C   . LYS B 47  ? 1.9792 1.6427 1.7783 -0.5160 -0.6258 0.0053  51  LYS B C   
9632  O O   . LYS B 47  ? 2.0492 1.6607 1.8412 -0.5311 -0.6466 0.0125  51  LYS B O   
9633  C CB  . LYS B 47  ? 1.7758 1.5337 1.6200 -0.5441 -0.5961 0.0576  51  LYS B CB  
9634  C CG  . LYS B 47  ? 1.6848 1.5317 1.5590 -0.5588 -0.5736 0.0845  51  LYS B CG  
9635  C CD  . LYS B 47  ? 1.7040 1.6022 1.5867 -0.5851 -0.5832 0.0953  51  LYS B CD  
9636  C CE  . LYS B 47  ? 1.8105 1.6651 1.6778 -0.6105 -0.6087 0.1034  51  LYS B CE  
9637  N NZ  . LYS B 47  ? 1.8604 1.6940 1.7285 -0.6326 -0.6149 0.1272  51  LYS B NZ  
9651  N N   . GLY B 48  ? 1.9983 1.6481 1.7814 -0.4837 -0.6182 -0.0250 52  GLY B N   
9652  C CA  . GLY B 48  ? 2.0378 1.6135 1.7928 -0.4737 -0.6443 -0.0549 52  GLY B CA  
9653  C C   . GLY B 48  ? 1.9963 1.5349 1.7419 -0.4332 -0.6311 -0.0821 52  GLY B C   
9654  O O   . GLY B 48  ? 2.0133 1.5173 1.7373 -0.4118 -0.6391 -0.1146 52  GLY B O   
9658  N N   . CYS B 49  ? 1.9453 1.4932 1.7066 -0.4224 -0.6112 -0.0707 53  CYS B N   
9659  C CA  . CYS B 49  ? 1.9733 1.4841 1.7274 -0.3863 -0.6014 -0.0953 53  CYS B CA  
9660  C C   . CYS B 49  ? 1.9503 1.4845 1.6940 -0.3515 -0.5784 -0.1231 53  CYS B C   
9661  O O   . CYS B 49  ? 1.9206 1.5160 1.6766 -0.3406 -0.5471 -0.1141 53  CYS B O   
9662  C CB  . CYS B 49  ? 1.9484 1.4797 1.7234 -0.3810 -0.5791 -0.0755 53  CYS B CB  
9663  S SG  . CYS B 49  ? 1.9938 1.5116 1.7809 -0.4267 -0.6030 -0.0377 53  CYS B SG  
9668  N N   . GLN B 50  ? 1.9499 1.4357 1.6703 -0.3343 -0.5950 -0.1573 54  GLN B N   
9669  C CA  . GLN B 50  ? 1.8928 1.4009 1.5991 -0.3054 -0.5766 -0.1848 54  GLN B CA  
9670  C C   . GLN B 50  ? 1.8484 1.3770 1.5625 -0.2716 -0.5430 -0.1930 54  GLN B C   
9671  O O   . GLN B 50  ? 1.7824 1.2984 1.5108 -0.2676 -0.5373 -0.1827 54  GLN B O   
9672  C CB  . GLN B 50  ? 1.9137 1.3658 1.5926 -0.2968 -0.6047 -0.2213 54  GLN B CB  
9673  C CG  . GLN B 50  ? 1.9374 1.3632 1.6065 -0.3309 -0.6410 -0.2147 54  GLN B CG  
9674  C CD  . GLN B 50  ? 1.9864 1.3510 1.6297 -0.3206 -0.6702 -0.2520 54  GLN B CD  
9675  O OE1 . GLN B 50  ? 2.0268 1.3760 1.6573 -0.2873 -0.6631 -0.2868 54  GLN B OE1 
9676  N NE2 . GLN B 50  ? 1.9726 1.3141 1.6142 -0.3435 -0.6924 -0.2415 54  GLN B NE2 
9685  N N   . LEU B 51  ? 1.8721 1.4341 1.5758 -0.2487 -0.5214 -0.2111 55  LEU B N   
9686  C CA  . LEU B 51  ? 1.8446 1.4318 1.5545 -0.2187 -0.4888 -0.2180 55  LEU B CA  
9687  C C   . LEU B 51  ? 1.7976 1.3347 1.5016 -0.1956 -0.4959 -0.2450 55  LEU B C   
9688  O O   . LEU B 51  ? 1.6948 1.2337 1.4137 -0.1830 -0.4801 -0.2383 55  LEU B O   
9689  C CB  . LEU B 51  ? 1.8671 1.4977 1.5633 -0.2028 -0.4682 -0.2315 55  LEU B CB  
9690  C CG  . LEU B 51  ? 1.8348 1.5220 1.5400 -0.2189 -0.4563 -0.2047 55  LEU B CG  
9691  C CD1 . LEU B 51  ? 1.8521 1.5699 1.5371 -0.2058 -0.4446 -0.2210 55  LEU B CD1 
9692  C CD2 . LEU B 51  ? 1.7492 1.4745 1.4815 -0.2172 -0.4308 -0.1765 55  LEU B CD2 
9704  N N   . ASN B 52  ? 1.8620 1.3546 1.5447 -0.1888 -0.5205 -0.2770 56  ASN B N   
9705  C CA  . ASN B 52  ? 1.8930 1.3400 1.5703 -0.1629 -0.5288 -0.3078 56  ASN B CA  
9706  C C   . ASN B 52  ? 1.8772 1.2761 1.5693 -0.1729 -0.5483 -0.2929 56  ASN B C   
9707  O O   . ASN B 52  ? 1.8921 1.2589 1.5862 -0.1498 -0.5512 -0.3128 56  ASN B O   
9708  C CB  . ASN B 52  ? 1.9911 1.4009 1.6426 -0.1540 -0.5543 -0.3471 56  ASN B CB  
9709  C CG  . ASN B 52  ? 2.0283 1.4838 1.6618 -0.1516 -0.5404 -0.3582 56  ASN B CG  
9710  O OD1 . ASN B 52  ? 2.0108 1.5050 1.6481 -0.1730 -0.5325 -0.3310 56  ASN B OD1 
9711  N ND2 . ASN B 52  ? 2.0725 1.5264 1.6864 -0.1253 -0.5377 -0.3985 56  ASN B ND2 
9718  N N   . PHE B 53  ? 1.8435 1.2394 1.5463 -0.2073 -0.5619 -0.2583 57  PHE B N   
9719  C CA  . PHE B 53  ? 1.8338 1.1846 1.5480 -0.2227 -0.5831 -0.2404 57  PHE B CA  
9720  C C   . PHE B 53  ? 1.8011 1.1917 1.5394 -0.2323 -0.5588 -0.2042 57  PHE B C   
9721  O O   . PHE B 53  ? 1.7855 1.1444 1.5333 -0.2346 -0.5678 -0.1943 57  PHE B O   
9722  C CB  . PHE B 53  ? 1.8304 1.1423 1.5368 -0.2591 -0.6223 -0.2275 57  PHE B CB  
9723  C CG  . PHE B 53  ? 1.8811 1.1349 1.5646 -0.2507 -0.6550 -0.2634 57  PHE B CG  
9724  C CD1 . PHE B 53  ? 1.9047 1.1778 1.5704 -0.2441 -0.6530 -0.2863 57  PHE B CD1 
9725  C CD2 . PHE B 53  ? 1.9215 1.1171 1.6072 -0.2428 -0.6752 -0.2678 57  PHE B CD2 
9726  C CE1 . PHE B 53  ? 1.9765 1.2131 1.6278 -0.2301 -0.6694 -0.3144 57  PHE B CE1 
9727  C CE2 . PHE B 53  ? 2.0043 1.1620 1.6764 -0.2278 -0.6931 -0.2955 57  PHE B CE2 
9728  C CZ  . PHE B 53  ? 2.0347 1.2135 1.6899 -0.2215 -0.6896 -0.3195 57  PHE B CZ  
9738  N N   . ILE B 54  ? 1.8074 1.2654 1.5554 -0.2376 -0.5297 -0.1851 58  ILE B N   
9739  C CA  . ILE B 54  ? 1.8279 1.3261 1.5990 -0.2455 -0.5067 -0.1533 58  ILE B CA  
9740  C C   . ILE B 54  ? 1.8005 1.2955 1.5788 -0.2146 -0.4859 -0.1646 58  ILE B C   
9741  O O   . ILE B 54  ? 1.8382 1.3317 1.6065 -0.1844 -0.4747 -0.1942 58  ILE B O   
9742  C CB  . ILE B 54  ? 1.8375 1.4076 1.6177 -0.2523 -0.4810 -0.1356 58  ILE B CB  
9743  C CG1 . ILE B 54  ? 1.8130 1.4230 1.6179 -0.2676 -0.4647 -0.1010 58  ILE B CG1 
9744  C CG2 . ILE B 54  ? 1.8175 1.4193 1.5914 -0.2200 -0.4525 -0.1564 58  ILE B CG2 
9745  C CD1 . ILE B 54  ? 1.7781 1.4499 1.5942 -0.2851 -0.4533 -0.0797 58  ILE B CD1 
9757  N N   . GLU B 55  ? 1.7328 1.2296 1.5282 -0.2235 -0.4810 -0.1406 59  GLU B N   
9758  C CA  . GLU B 55  ? 1.6957 1.1867 1.4997 -0.1981 -0.4643 -0.1475 59  GLU B CA  
9759  C C   . GLU B 55  ? 1.6483 1.1983 1.4723 -0.2005 -0.4320 -0.1210 59  GLU B C   
9760  O O   . GLU B 55  ? 1.6532 1.2186 1.4895 -0.2275 -0.4353 -0.0911 59  GLU B O   
9761  C CB  . GLU B 55  ? 1.7363 1.1640 1.5405 -0.2048 -0.4934 -0.1459 59  GLU B CB  
9762  C CG  . GLU B 55  ? 1.8317 1.1971 1.6190 -0.1865 -0.5205 -0.1819 59  GLU B CG  
9763  C CD  . GLU B 55  ? 1.8674 1.2328 1.6558 -0.1459 -0.5023 -0.2113 59  GLU B CD  
9764  O OE1 . GLU B 55  ? 1.8747 1.2259 1.6749 -0.1371 -0.4995 -0.2055 59  GLU B OE1 
9765  O OE2 . GLU B 55  ? 1.8919 1.2745 1.6693 -0.1239 -0.4906 -0.2397 59  GLU B OE2 
9772  N N   . ASN B 56  ? 1.5888 1.1730 1.4159 -0.1730 -0.4014 -0.1324 60  ASN B N   
9773  C CA  . ASN B 56  ? 1.5112 1.1476 1.3568 -0.1714 -0.3713 -0.1107 60  ASN B CA  
9774  C C   . ASN B 56  ? 1.4369 1.0877 1.2840 -0.1385 -0.3448 -0.1274 60  ASN B C   
9775  O O   . ASN B 56  ? 1.3947 1.0744 1.2344 -0.1238 -0.3282 -0.1399 60  ASN B O   
9776  C CB  . ASN B 56  ? 1.4926 1.1823 1.3429 -0.1852 -0.3598 -0.0950 60  ASN B CB  
9777  C CG  . ASN B 56  ? 1.3931 1.1359 1.2632 -0.1820 -0.3308 -0.0746 60  ASN B CG  
9778  O OD1 . ASN B 56  ? 1.3457 1.0857 1.2271 -0.1766 -0.3216 -0.0670 60  ASN B OD1 
9779  N ND2 . ASN B 56  ? 1.3448 1.1355 1.2195 -0.1847 -0.3177 -0.0664 60  ASN B ND2 
9786  N N   . PRO B 57  ? 1.4085 1.0418 1.2644 -0.1277 -0.3407 -0.1270 61  PRO B N   
9787  C CA  . PRO B 57  ? 1.3572 1.0124 1.2174 -0.0996 -0.3133 -0.1385 61  PRO B CA  
9788  C C   . PRO B 57  ? 1.2733 0.9825 1.1491 -0.1028 -0.2857 -0.1150 61  PRO B C   
9789  O O   . PRO B 57  ? 1.1894 0.9135 1.0778 -0.1237 -0.2873 -0.0893 61  PRO B O   
9790  C CB  . PRO B 57  ? 1.3854 0.9993 1.2508 -0.0899 -0.3236 -0.1448 61  PRO B CB  
9791  C CG  . PRO B 57  ? 1.4076 0.9987 1.2789 -0.1192 -0.3457 -0.1201 61  PRO B CG  
9792  C CD  . PRO B 57  ? 1.4417 1.0345 1.3036 -0.1422 -0.3620 -0.1146 61  PRO B CD  
9800  N N   . VAL B 58  ? 1.2994 1.0394 1.1739 -0.0821 -0.2610 -0.1245 62  VAL B N   
9801  C CA  . VAL B 58  ? 1.2938 1.0825 1.1817 -0.0818 -0.2360 -0.1055 62  VAL B CA  
9802  C C   . VAL B 58  ? 1.2349 1.0330 1.1269 -0.0582 -0.2141 -0.1139 62  VAL B C   
9803  O O   . VAL B 58  ? 1.2587 1.0391 1.1402 -0.0402 -0.2139 -0.1376 62  VAL B O   
9804  C CB  . VAL B 58  ? 1.3456 1.1691 1.2268 -0.0855 -0.2296 -0.1032 62  VAL B CB  
9805  C CG1 . VAL B 58  ? 1.3241 1.1533 1.1887 -0.0647 -0.2186 -0.1260 62  VAL B CG1 
9806  C CG2 . VAL B 58  ? 1.3556 1.2242 1.2545 -0.0911 -0.2123 -0.0793 62  VAL B CG2 
9816  N N   . SER B 59  ? 1.1786 1.0071 1.0865 -0.0586 -0.1958 -0.0951 63  SER B N   
9817  C CA  . SER B 59  ? 1.1456 0.9865 1.0582 -0.0386 -0.1744 -0.1001 63  SER B CA  
9818  C C   . SER B 59  ? 1.1252 0.9846 1.0239 -0.0238 -0.1618 -0.1156 63  SER B C   
9819  O O   . SER B 59  ? 1.0909 0.9701 0.9822 -0.0302 -0.1618 -0.1122 63  SER B O   
9820  C CB  . SER B 59  ? 1.1370 1.0094 1.0679 -0.0430 -0.1584 -0.0772 63  SER B CB  
9821  O OG  . SER B 59  ? 1.1783 1.0412 1.1204 -0.0606 -0.1699 -0.0611 63  SER B OG  
9827  N N   . GLN B 60  ? 1.1519 1.0069 1.0468 -0.0049 -0.1516 -0.1322 64  GLN B N   
9828  C CA  . GLN B 60  ? 1.1880 1.0625 1.0678 0.0076  -0.1397 -0.1479 64  GLN B CA  
9829  C C   . GLN B 60  ? 1.1879 1.0743 1.0730 0.0244  -0.1206 -0.1535 64  GLN B C   
9830  O O   . GLN B 60  ? 1.2309 1.1003 1.1279 0.0302  -0.1215 -0.1544 64  GLN B O   
9831  C CB  . GLN B 60  ? 1.2524 1.1053 1.1136 0.0120  -0.1551 -0.1744 64  GLN B CB  
9832  C CG  . GLN B 60  ? 1.3447 1.1592 1.2088 0.0216  -0.1691 -0.1927 64  GLN B CG  
9833  C CD  . GLN B 60  ? 1.4634 1.2533 1.3102 0.0255  -0.1883 -0.2198 64  GLN B CD  
9834  O OE1 . GLN B 60  ? 1.5320 1.3415 1.3619 0.0291  -0.1835 -0.2334 64  GLN B OE1 
9835  N NE2 . GLN B 60  ? 1.4743 1.2201 1.3241 0.0243  -0.2116 -0.2278 64  GLN B NE2 
9844  N N   . VAL B 61  ? 1.1445 1.0607 1.0199 0.0306  -0.1046 -0.1561 65  VAL B N   
9845  C CA  . VAL B 61  ? 1.0975 1.0305 0.9756 0.0442  -0.0859 -0.1608 65  VAL B CA  
9846  C C   . VAL B 61  ? 1.1157 1.0588 0.9750 0.0550  -0.0825 -0.1869 65  VAL B C   
9847  O O   . VAL B 61  ? 1.1818 1.1351 1.0235 0.0497  -0.0863 -0.1923 65  VAL B O   
9848  C CB  . VAL B 61  ? 1.0568 1.0192 0.9404 0.0402  -0.0695 -0.1385 65  VAL B CB  
9849  C CG1 . VAL B 61  ? 1.0401 1.0165 0.9280 0.0521  -0.0519 -0.1416 65  VAL B CG1 
9850  C CG2 . VAL B 61  ? 1.0470 1.0060 0.9485 0.0295  -0.0734 -0.1153 65  VAL B CG2 
9860  N N   . GLU B 62  ? 1.0770 1.0205 0.9400 0.0700  -0.0754 -0.2035 66  GLU B N   
9861  C CA  . GLU B 62  ? 1.0937 1.0568 0.9413 0.0817  -0.0684 -0.2295 66  GLU B CA  
9862  C C   . GLU B 62  ? 1.0813 1.0761 0.9329 0.0873  -0.0464 -0.2240 66  GLU B C   
9863  O O   . GLU B 62  ? 1.0539 1.0423 0.9230 0.0939  -0.0412 -0.2196 66  GLU B O   
9864  C CB  . GLU B 62  ? 1.1542 1.0920 1.0033 0.0965  -0.0820 -0.2595 66  GLU B CB  
9865  C CG  . GLU B 62  ? 1.2486 1.2119 1.0826 0.1102  -0.0751 -0.2908 66  GLU B CG  
9866  C CD  . GLU B 62  ? 1.3510 1.2890 1.1894 0.1283  -0.0902 -0.3232 66  GLU B CD  
9867  O OE1 . GLU B 62  ? 1.3797 1.2759 1.2318 0.1287  -0.1076 -0.3191 66  GLU B OE1 
9868  O OE2 . GLU B 62  ? 1.3895 1.3502 1.2176 0.1421  -0.0856 -0.3531 66  GLU B OE2 
9875  N N   . ILE B 63  ? 1.0707 1.0990 0.9051 0.0830  -0.0345 -0.2232 67  ILE B N   
9876  C CA  . ILE B 63  ? 1.0076 1.0678 0.8425 0.0846  -0.0148 -0.2163 67  ILE B CA  
9877  C C   . ILE B 63  ? 1.0307 1.1109 0.8603 0.0990  -0.0079 -0.2466 67  ILE B C   
9878  O O   . ILE B 63  ? 1.0651 1.1609 0.8757 0.1008  -0.0099 -0.2674 67  ILE B O   
9879  C CB  . ILE B 63  ? 0.9502 1.0359 0.7682 0.0704  -0.0076 -0.1977 67  ILE B CB  
9880  C CG1 . ILE B 63  ? 0.9206 0.9889 0.7476 0.0591  -0.0152 -0.1699 67  ILE B CG1 
9881  C CG2 . ILE B 63  ? 0.9166 1.0335 0.7328 0.0698  0.0108  -0.1903 67  ILE B CG2 
9882  C CD1 . ILE B 63  ? 0.9333 1.0211 0.7455 0.0463  -0.0128 -0.1510 67  ILE B CD1 
9894  N N   . LEU B 64  ? 1.0160 1.0986 0.8628 0.1097  0.0000  -0.2503 68  LEU B N   
9895  C CA  . LEU B 64  ? 1.0578 1.1636 0.9045 0.1253  0.0070  -0.2797 68  LEU B CA  
9896  C C   . LEU B 64  ? 1.0760 1.2291 0.9156 0.1206  0.0282  -0.2741 68  LEU B C   
9897  O O   . LEU B 64  ? 1.1530 1.3424 0.9781 0.1241  0.0357  -0.2953 68  LEU B O   
9898  C CB  . LEU B 64  ? 1.0514 1.1313 0.9222 0.1408  0.0004  -0.2894 68  LEU B CB  
9899  C CG  . LEU B 64  ? 1.0725 1.1027 0.9507 0.1446  -0.0230 -0.2950 68  LEU B CG  
9900  C CD1 . LEU B 64  ? 1.0422 1.0500 0.9424 0.1601  -0.0298 -0.3049 68  LEU B CD1 
9901  C CD2 . LEU B 64  ? 1.1275 1.1524 0.9885 0.1492  -0.0360 -0.3218 68  LEU B CD2 
9913  N N   . LYS B 65  ? 1.0021 1.1568 0.8513 0.1118  0.0372  -0.2461 69  LYS B N   
9914  C CA  . LYS B 65  ? 0.9504 1.1451 0.7931 0.1042  0.0551  -0.2364 69  LYS B CA  
9915  C C   . LYS B 65  ? 0.8822 1.0709 0.7196 0.0863  0.0565  -0.2015 69  LYS B C   
9916  O O   . LYS B 65  ? 0.8793 1.0414 0.7335 0.0854  0.0531  -0.1826 69  LYS B O   
9917  C CB  . LYS B 65  ? 0.9943 1.1978 0.8577 0.1151  0.0643  -0.2415 69  LYS B CB  
9918  C CG  . LYS B 65  ? 1.1259 1.3443 0.9950 0.1346  0.0639  -0.2783 69  LYS B CG  
9919  C CD  . LYS B 65  ? 1.2174 1.4540 1.1061 0.1440  0.0745  -0.2827 69  LYS B CD  
9920  C CE  . LYS B 65  ? 1.2858 1.4824 1.1990 0.1599  0.0621  -0.2893 69  LYS B CE  
9921  N NZ  . LYS B 65  ? 1.3075 1.5223 1.2403 0.1695  0.0714  -0.2936 69  LYS B NZ  
9935  N N   . ASN B 66  ? 0.8592 1.0730 0.6732 0.0725  0.0605  -0.1938 70  ASN B N   
9936  C CA  . ASN B 66  ? 0.8767 1.0850 0.6839 0.0563  0.0592  -0.1621 70  ASN B CA  
9937  C C   . ASN B 66  ? 0.8856 1.1321 0.6731 0.0424  0.0706  -0.1526 70  ASN B C   
9938  O O   . ASN B 66  ? 0.9112 1.1660 0.6778 0.0280  0.0669  -0.1389 70  ASN B O   
9939  C CB  . ASN B 66  ? 0.8948 1.0840 0.6914 0.0503  0.0449  -0.1568 70  ASN B CB  
9940  C CG  . ASN B 66  ? 0.9232 1.1012 0.7193 0.0378  0.0403  -0.1252 70  ASN B CG  
9941  O OD1 . ASN B 66  ? 0.9225 1.0934 0.7329 0.0372  0.0446  -0.1079 70  ASN B OD1 
9942  N ND2 . ASN B 66  ? 0.9569 1.1331 0.7369 0.0286  0.0304  -0.1186 70  ASN B ND2 
9949  N N   . LYS B 67  ? 0.8624 1.1339 0.6561 0.0455  0.0836  -0.1592 71  LYS B N   
9950  C CA  . LYS B 67  ? 0.9030 1.2128 0.6784 0.0293  0.0942  -0.1482 71  LYS B CA  
9951  C C   . LYS B 67  ? 0.9091 1.2009 0.6803 0.0134  0.0890  -0.1125 71  LYS B C   
9952  O O   . LYS B 67  ? 0.8796 1.1397 0.6711 0.0185  0.0847  -0.0986 71  LYS B O   
9953  C CB  . LYS B 67  ? 0.9127 1.2504 0.7005 0.0348  0.1083  -0.1586 71  LYS B CB  
9954  C CG  . LYS B 67  ? 1.0014 1.3871 0.7689 0.0164  0.1200  -0.1509 71  LYS B CG  
9955  C CD  . LYS B 67  ? 1.0742 1.4914 0.8566 0.0222  0.1339  -0.1629 71  LYS B CD  
9956  C CE  . LYS B 67  ? 1.1749 1.6432 0.9365 0.0002  0.1453  -0.1529 71  LYS B CE  
9957  N NZ  . LYS B 67  ? 1.2271 1.7284 1.0049 0.0039  0.1586  -0.1619 71  LYS B NZ  
9971  N N   . PRO B 68  ? 0.9173 1.2283 0.6621 -0.0056 0.0879  -0.0975 72  PRO B N   
9972  C CA  . PRO B 68  ? 0.8764 1.1657 0.6175 -0.0190 0.0792  -0.0642 72  PRO B CA  
9973  C C   . PRO B 68  ? 0.8320 1.1165 0.5877 -0.0215 0.0850  -0.0485 72  PRO B C   
9974  O O   . PRO B 68  ? 0.8258 1.1376 0.5850 -0.0213 0.0977  -0.0581 72  PRO B O   
9975  C CB  . PRO B 68  ? 0.9166 1.2333 0.6235 -0.0401 0.0772  -0.0540 72  PRO B CB  
9976  C CG  . PRO B 68  ? 0.9553 1.3006 0.6490 -0.0351 0.0821  -0.0835 72  PRO B CG  
9977  C CD  . PRO B 68  ? 0.9397 1.2922 0.6561 -0.0157 0.0927  -0.1102 72  PRO B CD  
9985  N N   . LEU B 69  ? 0.8402 1.0912 0.6054 -0.0232 0.0748  -0.0253 73  LEU B N   
9986  C CA  . LEU B 69  ? 0.8647 1.1067 0.6422 -0.0263 0.0775  -0.0090 73  LEU B CA  
9987  C C   . LEU B 69  ? 0.8924 1.1629 0.6472 -0.0481 0.0819  0.0052  73  LEU B C   
9988  O O   . LEU B 69  ? 0.9548 1.2345 0.6838 -0.0644 0.0750  0.0173  73  LEU B O   
9989  C CB  . LEU B 69  ? 0.8575 1.0598 0.6470 -0.0236 0.0636  0.0114  73  LEU B CB  
9990  C CG  . LEU B 69  ? 0.8466 1.0229 0.6613 -0.0047 0.0598  0.0012  73  LEU B CG  
9991  C CD1 . LEU B 69  ? 0.8534 1.0010 0.6749 -0.0040 0.0450  0.0198  73  LEU B CD1 
9992  C CD2 . LEU B 69  ? 0.8110 0.9837 0.6492 0.0070  0.0695  -0.0080 73  LEU B CD2 
10004 N N   . SER B 70  ? 0.8464 1.1315 0.6101 -0.0500 0.0925  0.0048  74  SER B N   
10005 C CA  . SER B 70  ? 0.9107 1.2271 0.6538 -0.0731 0.0973  0.0183  74  SER B CA  
10006 C C   . SER B 70  ? 1.0107 1.2979 0.7442 -0.0891 0.0822  0.0515  74  SER B C   
10007 O O   . SER B 70  ? 1.0519 1.3013 0.8046 -0.0798 0.0744  0.0614  74  SER B O   
10008 C CB  . SER B 70  ? 0.9080 1.2494 0.6656 -0.0706 0.1122  0.0084  74  SER B CB  
10009 O OG  . SER B 70  ? 0.9350 1.2441 0.7122 -0.0668 0.1080  0.0227  74  SER B OG  
10015 N N   . VAL B 71  ? 1.0532 1.3583 0.7563 -0.1131 0.0770  0.0681  75  VAL B N   
10016 C CA  . VAL B 71  ? 1.0233 1.2998 0.7131 -0.1305 0.0590  0.1006  75  VAL B CA  
10017 C C   . VAL B 71  ? 1.0186 1.3170 0.6960 -0.1543 0.0633  0.1168  75  VAL B C   
10018 O O   . VAL B 71  ? 1.0237 1.3719 0.6842 -0.1690 0.0763  0.1096  75  VAL B O   
10019 C CB  . VAL B 71  ? 1.0221 1.2973 0.6847 -0.1426 0.0456  0.1116  75  VAL B CB  
10020 C CG1 . VAL B 71  ? 1.0901 1.4198 0.7247 -0.1594 0.0573  0.1018  75  VAL B CG1 
10021 C CG2 . VAL B 71  ? 1.0181 1.2608 0.6670 -0.1602 0.0239  0.1459  75  VAL B CG2 
10031 N N   . GLY B 72  ? 0.9957 1.2588 0.6817 -0.1584 0.0518  0.1377  76  GLY B N   
10032 C CA  . GLY B 72  ? 1.0177 1.2939 0.6911 -0.1836 0.0517  0.1572  76  GLY B CA  
10033 C C   . GLY B 72  ? 0.9968 1.3022 0.6892 -0.1780 0.0714  0.1407  76  GLY B C   
10034 O O   . GLY B 72  ? 1.0066 1.3259 0.7198 -0.1550 0.0859  0.1128  76  GLY B O   
10038 N N   . ARG B 73  ? 0.9806 1.2941 0.6654 -0.2004 0.0700  0.1593  77  ARG B N   
10039 C CA  . ARG B 73  ? 1.0037 1.3485 0.7052 -0.1986 0.0875  0.1465  77  ARG B CA  
10040 C C   . ARG B 73  ? 1.0047 1.4163 0.6997 -0.2002 0.1087  0.1224  77  ARG B C   
10041 O O   . ARG B 73  ? 1.0366 1.4831 0.7030 -0.2212 0.1097  0.1281  77  ARG B O   
10042 C CB  . ARG B 73  ? 1.0800 1.4221 0.7709 -0.2271 0.0798  0.1739  77  ARG B CB  
10043 C CG  . ARG B 73  ? 1.1118 1.4830 0.8221 -0.2258 0.0957  0.1629  77  ARG B CG  
10044 C CD  . ARG B 73  ? 1.1941 1.5627 0.8919 -0.2572 0.0865  0.1917  77  ARG B CD  
10045 N NE  . ARG B 73  ? 1.2227 1.6227 0.9400 -0.2565 0.1019  0.1807  77  ARG B NE  
10046 C CZ  . ARG B 73  ? 1.2901 1.7595 1.0044 -0.2673 0.1214  0.1677  77  ARG B CZ  
10047 N NH1 . ARG B 73  ? 1.3159 1.8320 1.0073 -0.2801 0.1287  0.1632  77  ARG B NH1 
10048 N NH2 . ARG B 73  ? 1.3208 1.8157 1.0558 -0.2647 0.1334  0.1581  77  ARG B NH2 
10062 N N   . GLN B 74  ? 0.9922 1.4223 0.7140 -0.1773 0.1247  0.0946  78  GLN B N   
10063 C CA  . GLN B 74  ? 1.0257 1.5173 0.7477 -0.1719 0.1441  0.0659  78  GLN B CA  
10064 C C   . GLN B 74  ? 1.0568 1.5927 0.7880 -0.1823 0.1577  0.0628  78  GLN B C   
10065 O O   . GLN B 74  ? 1.0181 1.5328 0.7743 -0.1708 0.1584  0.0618  78  GLN B O   
10066 C CB  . GLN B 74  ? 1.0128 1.4914 0.7589 -0.1363 0.1495  0.0345  78  GLN B CB  
10067 C CG  . GLN B 74  ? 1.0135 1.4483 0.7540 -0.1254 0.1358  0.0370  78  GLN B CG  
10068 C CD  . GLN B 74  ? 1.0419 1.5019 0.7498 -0.1425 0.1332  0.0408  78  GLN B CD  
10069 O OE1 . GLN B 74  ? 1.0259 1.5394 0.7233 -0.1455 0.1461  0.0212  78  GLN B OE1 
10070 N NE2 . GLN B 74  ? 1.0830 1.5059 0.7746 -0.1532 0.1156  0.0652  78  GLN B NE2 
10079 N N   . LYS B 75  ? 1.1311 1.7315 0.8419 -0.2048 0.1685  0.0610  79  LYS B N   
10080 C CA  . LYS B 75  ? 1.1737 1.8276 0.8942 -0.2148 0.1831  0.0549  79  LYS B CA  
10081 C C   . LYS B 75  ? 1.2100 1.8929 0.9607 -0.1826 0.1991  0.0154  79  LYS B C   
10082 O O   . LYS B 75  ? 1.2204 1.9333 0.9898 -0.1820 0.2090  0.0083  79  LYS B O   
10083 C CB  . LYS B 75  ? 1.1873 1.9087 0.8764 -0.2499 0.1903  0.0641  79  LYS B CB  
10084 C CG  . LYS B 75  ? 1.2098 1.9058 0.8669 -0.2869 0.1726  0.1067  79  LYS B CG  
10085 C CD  . LYS B 75  ? 1.2189 1.9684 0.8567 -0.3158 0.1727  0.1116  79  LYS B CD  
10086 C CE  . LYS B 75  ? 1.2211 1.9397 0.8300 -0.3526 0.1511  0.1543  79  LYS B CE  
10087 N NZ  . LYS B 75  ? 1.2344 2.0034 0.8276 -0.3809 0.1488  0.1589  79  LYS B NZ  
10101 N N   . ASN B 76  ? 1.2232 1.8962 0.9795 -0.1563 0.2001  -0.0099 80  ASN B N   
10102 C CA  . ASN B 76  ? 1.2134 1.9094 0.9963 -0.1247 0.2117  -0.0486 80  ASN B CA  
10103 C C   . ASN B 76  ? 1.1558 1.7836 0.9621 -0.0951 0.2015  -0.0546 80  ASN B C   
10104 O O   . ASN B 76  ? 1.1393 1.7242 0.9357 -0.0904 0.1902  -0.0480 80  ASN B O   
10105 C CB  . ASN B 76  ? 1.2780 2.0243 1.0463 -0.1198 0.2204  -0.0761 80  ASN B CB  
10106 C CG  . ASN B 76  ? 1.2973 2.0574 1.0928 -0.0840 0.2279  -0.1176 80  ASN B CG  
10107 O OD1 . ASN B 76  ? 1.3332 2.0588 1.1328 -0.0619 0.2208  -0.1333 80  ASN B OD1 
10108 N ND2 . ASN B 76  ? 1.2769 2.0781 1.0944 -0.0776 0.2371  -0.1339 80  ASN B ND2 
10115 N N   . SER B 77  ? 1.1134 1.7337 0.9501 -0.0764 0.2053  -0.0664 81  SER B N   
10116 C CA  . SER B 77  ? 1.0796 1.6378 0.9380 -0.0516 0.1957  -0.0693 81  SER B CA  
10117 C C   . SER B 77  ? 1.0743 1.6200 0.9363 -0.0273 0.1930  -0.0952 81  SER B C   
10118 O O   . SER B 77  ? 1.0471 1.5387 0.9190 -0.0126 0.1825  -0.0926 81  SER B O   
10119 C CB  . SER B 77  ? 1.0780 1.6372 0.9666 -0.0382 0.2004  -0.0774 81  SER B CB  
10120 O OG  . SER B 77  ? 1.1269 1.6898 1.0129 -0.0607 0.2006  -0.0522 81  SER B OG  
10126 N N   . SER B 78  ? 1.0928 1.6881 0.9468 -0.0233 0.2017  -0.1206 82  SER B N   
10127 C CA  . SER B 78  ? 1.1126 1.6957 0.9699 0.0001  0.1977  -0.1477 82  SER B CA  
10128 C C   . SER B 78  ? 1.1107 1.6688 0.9426 -0.0091 0.1881  -0.1362 82  SER B C   
10129 O O   . SER B 78  ? 1.1339 1.6705 0.9680 0.0087  0.1817  -0.1543 82  SER B O   
10130 C CB  . SER B 78  ? 1.1680 1.8148 1.0278 0.0108  0.2096  -0.1835 82  SER B CB  
10131 O OG  . SER B 78  ? 1.1794 1.8560 1.0633 0.0186  0.2184  -0.1942 82  SER B OG  
10137 N N   . ASP B 79  ? 1.0886 1.6476 0.8966 -0.0367 0.1854  -0.1065 83  ASP B N   
10138 C CA  . ASP B 79  ? 1.0704 1.6050 0.8543 -0.0466 0.1746  -0.0927 83  ASP B CA  
10139 C C   . ASP B 79  ? 1.0113 1.4811 0.8008 -0.0474 0.1599  -0.0655 83  ASP B C   
10140 O O   . ASP B 79  ? 1.0178 1.4648 0.7893 -0.0562 0.1491  -0.0507 83  ASP B O   
10141 C CB  . ASP B 79  ? 1.1532 1.7316 0.9041 -0.0774 0.1785  -0.0775 83  ASP B CB  
10142 C CG  . ASP B 79  ? 1.2405 1.8878 0.9817 -0.0765 0.1925  -0.1073 83  ASP B CG  
10143 O OD1 . ASP B 79  ? 1.2640 1.9136 1.0164 -0.0513 0.1940  -0.1397 83  ASP B OD1 
10144 O OD2 . ASP B 79  ? 1.2813 1.9813 1.0033 -0.1014 0.2011  -0.0987 83  ASP B OD2 
10149 N N   . ILE B 80  ? 0.9647 1.4069 0.7788 -0.0379 0.1589  -0.0597 84  ILE B N   
10150 C CA  . ILE B 80  ? 0.9401 1.3248 0.7624 -0.0355 0.1457  -0.0383 84  ILE B CA  
10151 C C   . ILE B 80  ? 0.9192 1.2707 0.7542 -0.0130 0.1388  -0.0536 84  ILE B C   
10152 O O   . ILE B 80  ? 0.9221 1.2761 0.7761 0.0066  0.1433  -0.0769 84  ILE B O   
10153 C CB  . ILE B 80  ? 0.9145 1.2852 0.7570 -0.0345 0.1474  -0.0278 84  ILE B CB  
10154 C CG1 . ILE B 80  ? 0.9039 1.3001 0.7311 -0.0612 0.1504  -0.0069 84  ILE B CG1 
10155 C CG2 . ILE B 80  ? 0.8954 1.2092 0.7505 -0.0260 0.1347  -0.0131 84  ILE B CG2 
10156 C CD1 . ILE B 80  ? 0.8631 1.2488 0.7085 -0.0624 0.1519  0.0028  84  ILE B CD1 
10168 N N   . VAL B 81  ? 0.8974 1.2177 0.7224 -0.0163 0.1265  -0.0399 85  VAL B N   
10169 C CA  . VAL B 81  ? 0.8571 1.1452 0.6928 0.0009  0.1181  -0.0499 85  VAL B CA  
10170 C C   . VAL B 81  ? 0.8457 1.0914 0.6879 -0.0008 0.1060  -0.0264 85  VAL B C   
10171 O O   . VAL B 81  ? 0.8939 1.1317 0.7191 -0.0143 0.0973  -0.0073 85  VAL B O   
10172 C CB  . VAL B 81  ? 0.8515 1.1518 0.6674 -0.0006 0.1147  -0.0616 85  VAL B CB  
10173 C CG1 . VAL B 81  ? 0.8745 1.1413 0.7025 0.0156  0.1051  -0.0716 85  VAL B CG1 
10174 C CG2 . VAL B 81  ? 0.7934 1.1416 0.6012 0.0008  0.1269  -0.0866 85  VAL B CG2 
10184 N N   . GLN B 82  ? 0.8105 1.0304 0.6773 0.0132  0.1047  -0.0282 86  GLN B N   
10185 C CA  . GLN B 82  ? 0.7985 0.9832 0.6748 0.0141  0.0945  -0.0096 86  GLN B CA  
10186 C C   . GLN B 82  ? 0.7895 0.9494 0.6769 0.0268  0.0861  -0.0154 86  GLN B C   
10187 O O   . GLN B 82  ? 0.8064 0.9428 0.6998 0.0273  0.0767  -0.0013 86  GLN B O   
10188 C CB  . GLN B 82  ? 0.7921 0.9683 0.6869 0.0178  0.0987  -0.0045 86  GLN B CB  
10189 C CG  . GLN B 82  ? 0.8098 1.0125 0.6965 0.0046  0.1073  0.0006  86  GLN B CG  
10190 C CD  . GLN B 82  ? 0.7669 0.9550 0.6683 0.0044  0.1074  0.0116  86  GLN B CD  
10191 O OE1 . GLN B 82  ? 0.7447 0.9157 0.6400 -0.0059 0.0991  0.0316  86  GLN B OE1 
10192 N NE2 . GLN B 82  ? 0.7155 0.9089 0.6361 0.0160  0.1153  -0.0019 86  GLN B NE2 
10201 N N   . ILE B 83  ? 0.7610 0.9262 0.6518 0.0366  0.0882  -0.0359 87  ILE B N   
10202 C CA  . ILE B 83  ? 0.7714 0.9149 0.6704 0.0453  0.0791  -0.0409 87  ILE B CA  
10203 C C   . ILE B 83  ? 0.8293 0.9851 0.7131 0.0453  0.0772  -0.0569 87  ILE B C   
10204 O O   . ILE B 83  ? 0.8434 1.0214 0.7218 0.0482  0.0849  -0.0747 87  ILE B O   
10205 C CB  . ILE B 83  ? 0.7507 0.8786 0.6735 0.0584  0.0800  -0.0497 87  ILE B CB  
10206 C CG1 . ILE B 83  ? 0.7528 0.8583 0.6836 0.0628  0.0692  -0.0487 87  ILE B CG1 
10207 C CG2 . ILE B 83  ? 0.7093 0.8513 0.6348 0.0669  0.0865  -0.0723 87  ILE B CG2 
10208 C CD1 . ILE B 83  ? 0.7318 0.8207 0.6842 0.0717  0.0681  -0.0515 87  ILE B CD1 
10220 N N   . ALA B 84  ? 0.8591 1.0024 0.7364 0.0428  0.0666  -0.0520 88  ALA B N   
10221 C CA  . ALA B 84  ? 0.8926 1.0438 0.7549 0.0423  0.0625  -0.0666 88  ALA B CA  
10222 C C   . ALA B 84  ? 0.8930 1.0195 0.7645 0.0463  0.0503  -0.0653 88  ALA B C   
10223 O O   . ALA B 84  ? 0.9186 1.0321 0.7967 0.0431  0.0437  -0.0474 88  ALA B O   
10224 C CB  . ALA B 84  ? 0.9450 1.1159 0.7807 0.0280  0.0617  -0.0581 88  ALA B CB  
10230 N N   . PRO B 85  ? 0.8908 1.0107 0.7636 0.0532  0.0457  -0.0842 89  PRO B N   
10231 C CA  . PRO B 85  ? 0.9091 1.0409 0.7770 0.0608  0.0502  -0.1096 89  PRO B CA  
10232 C C   . PRO B 85  ? 0.8624 0.9935 0.7485 0.0713  0.0580  -0.1176 89  PRO B C   
10233 O O   . PRO B 85  ? 0.8574 0.9789 0.7583 0.0711  0.0606  -0.1025 89  PRO B O   
10234 C CB  . PRO B 85  ? 0.9418 1.0540 0.8101 0.0650  0.0373  -0.1225 89  PRO B CB  
10235 C CG  . PRO B 85  ? 0.9430 1.0437 0.8096 0.0557  0.0278  -0.1032 89  PRO B CG  
10236 C CD  . PRO B 85  ? 0.9298 1.0292 0.8085 0.0530  0.0328  -0.0814 89  PRO B CD  
10244 N N   . GLN B 86  ? 0.8681 1.0102 0.7535 0.0811  0.0609  -0.1424 90  GLN B N   
10245 C CA  . GLN B 86  ? 0.8470 0.9900 0.7502 0.0926  0.0667  -0.1526 90  GLN B CA  
10246 C C   . GLN B 86  ? 0.8230 0.9423 0.7380 0.1064  0.0559  -0.1725 90  GLN B C   
10247 O O   . GLN B 86  ? 0.7910 0.9032 0.7234 0.1162  0.0569  -0.1778 90  GLN B O   
10248 C CB  . GLN B 86  ? 0.8650 1.0480 0.7605 0.0936  0.0802  -0.1652 90  GLN B CB  
10249 C CG  . GLN B 86  ? 0.8822 1.0878 0.7657 0.0777  0.0899  -0.1439 90  GLN B CG  
10250 C CD  . GLN B 86  ? 0.9181 1.1411 0.7751 0.0651  0.0887  -0.1408 90  GLN B CD  
10251 O OE1 . GLN B 86  ? 0.9111 1.1455 0.7565 0.0692  0.0863  -0.1615 90  GLN B OE1 
10252 N NE2 . GLN B 86  ? 0.9474 1.1714 0.7943 0.0498  0.0889  -0.1151 90  GLN B NE2 
10261 N N   . SER B 87  ? 0.8549 0.9601 0.7606 0.1070  0.0438  -0.1830 91  SER B N   
10262 C CA  . SER B 87  ? 0.9312 1.0080 0.8468 0.1186  0.0299  -0.2006 91  SER B CA  
10263 C C   . SER B 87  ? 0.9356 0.9911 0.8408 0.1120  0.0150  -0.2003 91  SER B C   
10264 O O   . SER B 87  ? 0.9288 1.0005 0.8149 0.1073  0.0154  -0.2072 91  SER B O   
10265 C CB  . SER B 87  ? 1.0282 1.1217 0.9437 0.1345  0.0318  -0.2323 91  SER B CB  
10266 O OG  . SER B 87  ? 1.1050 1.1654 1.0311 0.1468  0.0152  -0.2490 91  SER B OG  
10272 N N   . LEU B 88  ? 0.9378 0.9591 0.8548 0.1101  0.0015  -0.1917 92  LEU B N   
10273 C CA  . LEU B 88  ? 0.9469 0.9470 0.8562 0.1019  -0.0141 -0.1895 92  LEU B CA  
10274 C C   . LEU B 88  ? 0.9588 0.9213 0.8791 0.1069  -0.0322 -0.1979 92  LEU B C   
10275 O O   . LEU B 88  ? 0.9417 0.8914 0.8781 0.1121  -0.0327 -0.1943 92  LEU B O   
10276 C CB  . LEU B 88  ? 0.9365 0.9370 0.8477 0.0868  -0.0133 -0.1608 92  LEU B CB  
10277 C CG  . LEU B 88  ? 0.9699 0.9995 0.8742 0.0804  0.0014  -0.1452 92  LEU B CG  
10278 C CD1 . LEU B 88  ? 0.9359 0.9602 0.8502 0.0704  -0.0004 -0.1193 92  LEU B CD1 
10279 C CD2 . LEU B 88  ? 1.0573 1.1062 0.9387 0.0760  0.0022  -0.1532 92  LEU B CD2 
10291 N N   . ILE B 89  ? 1.0050 0.9483 0.9153 0.1039  -0.0486 -0.2082 93  ILE B N   
10292 C CA  . ILE B 89  ? 1.0443 0.9469 0.9621 0.1023  -0.0701 -0.2101 93  ILE B CA  
10293 C C   . ILE B 89  ? 1.0034 0.8977 0.9202 0.0830  -0.0778 -0.1866 93  ILE B C   
10294 O O   . ILE B 89  ? 0.9813 0.8903 0.8848 0.0751  -0.0766 -0.1841 93  ILE B O   
10295 C CB  . ILE B 89  ? 1.1907 1.0740 1.0987 0.1131  -0.0865 -0.2409 93  ILE B CB  
10296 C CG1 . ILE B 89  ? 1.2474 1.1477 1.1572 0.1342  -0.0779 -0.2679 93  ILE B CG1 
10297 C CG2 . ILE B 89  ? 1.2382 1.0736 1.1534 0.1092  -0.1120 -0.2396 93  ILE B CG2 
10298 C CD1 . ILE B 89  ? 1.2639 1.1459 1.1934 0.1459  -0.0819 -0.2705 93  ILE B CD1 
10310 N N   . LEU B 90  ? 1.0006 0.8744 0.9313 0.0748  -0.0860 -0.1695 94  LEU B N   
10311 C CA  . LEU B 90  ? 0.9971 0.8674 0.9298 0.0558  -0.0938 -0.1476 94  LEU B CA  
10312 C C   . LEU B 90  ? 1.0194 0.8501 0.9537 0.0483  -0.1186 -0.1498 94  LEU B C   
10313 O O   . LEU B 90  ? 1.0256 0.8366 0.9714 0.0472  -0.1253 -0.1430 94  LEU B O   
10314 C CB  . LEU B 90  ? 1.0179 0.9065 0.9651 0.0495  -0.0805 -0.1231 94  LEU B CB  
10315 C CG  . LEU B 90  ? 1.0706 0.9630 1.0234 0.0309  -0.0871 -0.1013 94  LEU B CG  
10316 C CD1 . LEU B 90  ? 1.1070 1.0183 1.0489 0.0245  -0.0866 -0.0993 94  LEU B CD1 
10317 C CD2 . LEU B 90  ? 1.0361 0.9466 1.0046 0.0278  -0.0746 -0.0816 94  LEU B CD2 
10329 N N   . LYS B 91  ? 1.0643 0.8822 0.9857 0.0419  -0.1337 -0.1587 95  LYS B N   
10330 C CA  . LYS B 91  ? 1.1390 0.9181 1.0596 0.0303  -0.1601 -0.1580 95  LYS B CA  
10331 C C   . LYS B 91  ? 1.1395 0.9291 1.0660 0.0069  -0.1628 -0.1301 95  LYS B C   
10332 O O   . LYS B 91  ? 1.1666 0.9792 1.0870 -0.0010 -0.1585 -0.1244 95  LYS B O   
10333 C CB  . LYS B 91  ? 1.1987 0.9591 1.1024 0.0345  -0.1760 -0.1824 95  LYS B CB  
10334 C CG  . LYS B 91  ? 1.2496 0.9874 1.1506 0.0565  -0.1834 -0.2127 95  LYS B CG  
10335 C CD  . LYS B 91  ? 1.3227 1.0548 1.2054 0.0637  -0.1932 -0.2403 95  LYS B CD  
10336 C CE  . LYS B 91  ? 1.3529 1.0953 1.2327 0.0899  -0.1847 -0.2721 95  LYS B CE  
10337 N NZ  . LYS B 91  ? 1.4046 1.1559 1.2647 0.0965  -0.1882 -0.2988 95  LYS B NZ  
10351 N N   . LEU B 92  ? 1.1292 0.9051 1.0677 -0.0043 -0.1703 -0.1129 96  LEU B N   
10352 C CA  . LEU B 92  ? 1.1164 0.9108 1.0632 -0.0262 -0.1702 -0.0865 96  LEU B CA  
10353 C C   . LEU B 92  ? 1.1842 0.9464 1.1286 -0.0471 -0.1974 -0.0787 96  LEU B C   
10354 O O   . LEU B 92  ? 1.2212 0.9466 1.1664 -0.0475 -0.2133 -0.0811 96  LEU B O   
10355 C CB  . LEU B 92  ? 1.0624 0.8773 1.0248 -0.0258 -0.1541 -0.0697 96  LEU B CB  
10356 C CG  . LEU B 92  ? 1.0310 0.8890 0.9992 -0.0172 -0.1284 -0.0640 96  LEU B CG  
10357 C CD1 . LEU B 92  ? 0.9978 0.8692 0.9809 -0.0169 -0.1163 -0.0498 96  LEU B CD1 
10358 C CD2 . LEU B 92  ? 1.0438 0.9308 1.0117 -0.0290 -0.1264 -0.0534 96  LEU B CD2 
10370 N N   . ARG B 93  ? 1.1910 0.9668 1.1325 -0.0651 -0.2041 -0.0685 97  ARG B N   
10371 C CA  . ARG B 93  ? 1.2075 0.9635 1.1491 -0.0912 -0.2274 -0.0538 97  ARG B CA  
10372 C C   . ARG B 93  ? 1.2761 1.0552 1.2330 -0.1064 -0.2202 -0.0283 97  ARG B C   
10373 O O   . ARG B 93  ? 1.2684 1.0908 1.2358 -0.1016 -0.1975 -0.0198 97  ARG B O   
10374 C CB  . ARG B 93  ? 1.1403 0.9107 1.0752 -0.1062 -0.2353 -0.0510 97  ARG B CB  
10375 C CG  . ARG B 93  ? 1.1631 0.9081 1.0944 -0.1342 -0.2634 -0.0394 97  ARG B CG  
10376 C CD  . ARG B 93  ? 1.1719 0.9431 1.1003 -0.1498 -0.2671 -0.0337 97  ARG B CD  
10377 N NE  . ARG B 93  ? 1.2210 0.9861 1.1514 -0.1822 -0.2885 -0.0142 97  ARG B NE  
10378 C CZ  . ARG B 93  ? 1.3347 1.0758 1.2536 -0.1989 -0.3129 -0.0171 97  ARG B CZ  
10379 N NH1 . ARG B 93  ? 1.3872 1.1081 1.2911 -0.1851 -0.3193 -0.0403 97  ARG B NH1 
10380 N NH2 . ARG B 93  ? 1.4196 1.1592 1.3414 -0.2310 -0.3314 0.0036  97  ARG B NH2 
10394 N N   . PRO B 94  ? 1.3366 1.0879 1.2941 -0.1247 -0.2398 -0.0159 98  PRO B N   
10395 C CA  . PRO B 94  ? 1.3086 1.0862 1.2791 -0.1408 -0.2325 0.0083  98  PRO B CA  
10396 C C   . PRO B 94  ? 1.2943 1.1261 1.2738 -0.1561 -0.2210 0.0237  98  PRO B C   
10397 O O   . PRO B 94  ? 1.3067 1.1426 1.2817 -0.1716 -0.2332 0.0264  98  PRO B O   
10398 C CB  . PRO B 94  ? 1.3693 1.1036 1.3340 -0.1634 -0.2620 0.0196  98  PRO B CB  
10399 C CG  . PRO B 94  ? 1.4351 1.1262 1.3853 -0.1639 -0.2862 0.0037  98  PRO B CG  
10400 C CD  . PRO B 94  ? 1.4150 1.1088 1.3609 -0.1321 -0.2710 -0.0233 98  PRO B CD  
10408 N N   . GLY B 95  ? 1.2546 1.1290 1.2478 -0.1507 -0.1982 0.0327  99  GLY B N   
10409 C CA  . GLY B 95  ? 1.2188 1.1487 1.2239 -0.1604 -0.1860 0.0446  99  GLY B CA  
10410 C C   . GLY B 95  ? 1.1565 1.1094 1.1617 -0.1431 -0.1730 0.0327  99  GLY B C   
10411 O O   . GLY B 95  ? 1.1031 1.1029 1.1201 -0.1471 -0.1630 0.0407  99  GLY B O   
10415 N N   . GLY B 96  ? 1.1498 1.0734 1.1424 -0.1240 -0.1736 0.0137  100 GLY B N   
10416 C CA  . GLY B 96  ? 1.1348 1.0782 1.1244 -0.1086 -0.1622 0.0033  100 GLY B CA  
10417 C C   . GLY B 96  ? 1.1117 1.0661 1.1051 -0.0844 -0.1400 -0.0035 100 GLY B C   
10418 O O   . GLY B 96  ? 1.1906 1.1216 1.1822 -0.0740 -0.1370 -0.0098 100 GLY B O   
10422 N N   . ALA B 97  ? 0.9939 0.9835 0.9930 -0.0761 -0.1261 -0.0018 101 ALA B N   
10423 C CA  . ALA B 97  ? 0.9342 0.9361 0.9369 -0.0557 -0.1064 -0.0058 101 ALA B CA  
10424 C C   . ALA B 97  ? 0.8781 0.8766 0.8666 -0.0422 -0.1026 -0.0188 101 ALA B C   
10425 O O   . ALA B 97  ? 0.8745 0.8799 0.8564 -0.0482 -0.1108 -0.0198 101 ALA B O   
10426 C CB  . ALA B 97  ? 0.9289 0.9732 0.9498 -0.0559 -0.0943 0.0071  101 ALA B CB  
10432 N N   . GLN B 98  ? 0.8263 0.8163 0.8098 -0.0253 -0.0906 -0.0281 102 GLN B N   
10433 C CA  . GLN B 98  ? 0.8511 0.8435 0.8205 -0.0134 -0.0844 -0.0388 102 GLN B CA  
10434 C C   . GLN B 98  ? 0.8287 0.8408 0.8048 -0.0012 -0.0666 -0.0337 102 GLN B C   
10435 O O   . GLN B 98  ? 0.8068 0.8173 0.7930 0.0037  -0.0583 -0.0307 102 GLN B O   
10436 C CB  . GLN B 98  ? 0.9039 0.8672 0.8578 -0.0056 -0.0886 -0.0582 102 GLN B CB  
10437 C CG  . GLN B 98  ? 0.9300 0.8919 0.8647 -0.0046 -0.0944 -0.0706 102 GLN B CG  
10438 C CD  . GLN B 98  ? 0.9482 0.9057 0.8800 -0.0204 -0.1121 -0.0671 102 GLN B CD  
10439 O OE1 . GLN B 98  ? 0.9718 0.9292 0.9163 -0.0334 -0.1200 -0.0546 102 GLN B OE1 
10440 N NE2 . GLN B 98  ? 0.9689 0.9251 0.8833 -0.0209 -0.1186 -0.0779 102 GLN B NE2 
10449 N N   . THR B 99  ? 0.8227 0.8518 0.7925 0.0028  -0.0625 -0.0321 103 THR B N   
10450 C CA  . THR B 99  ? 0.7897 0.8350 0.7644 0.0127  -0.0492 -0.0257 103 THR B CA  
10451 C C   . THR B 99  ? 0.7940 0.8327 0.7508 0.0215  -0.0419 -0.0360 103 THR B C   
10452 O O   . THR B 99  ? 0.8068 0.8473 0.7471 0.0196  -0.0464 -0.0413 103 THR B O   
10453 C CB  . THR B 99  ? 0.7760 0.8455 0.7578 0.0104  -0.0521 -0.0143 103 THR B CB  
10454 O OG1 . THR B 99  ? 0.7809 0.8634 0.7803 0.0015  -0.0582 -0.0063 103 THR B OG1 
10455 C CG2 . THR B 99  ? 0.7391 0.8200 0.7265 0.0211  -0.0414 -0.0077 103 THR B CG2 
10463 N N   . LEU B 100 ? 0.8087 0.8430 0.7687 0.0299  -0.0307 -0.0389 104 LEU B N   
10464 C CA  . LEU B 100 ? 0.8436 0.8781 0.7887 0.0372  -0.0219 -0.0479 104 LEU B CA  
10465 C C   . LEU B 100 ? 0.8596 0.9098 0.8043 0.0398  -0.0140 -0.0361 104 LEU B C   
10466 O O   . LEU B 100 ? 0.8557 0.9116 0.8163 0.0417  -0.0110 -0.0247 104 LEU B O   
10467 C CB  . LEU B 100 ? 0.8510 0.8737 0.8003 0.0447  -0.0151 -0.0577 104 LEU B CB  
10468 C CG  . LEU B 100 ? 0.8931 0.8943 0.8464 0.0432  -0.0253 -0.0673 104 LEU B CG  
10469 C CD1 . LEU B 100 ? 0.8518 0.8433 0.8133 0.0517  -0.0188 -0.0734 104 LEU B CD1 
10470 C CD2 . LEU B 100 ? 0.9762 0.9678 0.9124 0.0424  -0.0349 -0.0837 104 LEU B CD2 
10482 N N   . GLN B 101 ? 0.8857 0.9428 0.8115 0.0395  -0.0117 -0.0391 105 GLN B N   
10483 C CA  . GLN B 101 ? 0.9276 0.9953 0.8491 0.0401  -0.0064 -0.0273 105 GLN B CA  
10484 C C   . GLN B 101 ? 0.8939 0.9634 0.8103 0.0445  0.0062  -0.0327 105 GLN B C   
10485 O O   . GLN B 101 ? 0.8985 0.9714 0.8003 0.0447  0.0097  -0.0465 105 GLN B O   
10486 C CB  . GLN B 101 ? 1.0405 1.1167 0.9428 0.0335  -0.0136 -0.0236 105 GLN B CB  
10487 C CG  . GLN B 101 ? 1.1284 1.2069 1.0378 0.0294  -0.0266 -0.0159 105 GLN B CG  
10488 C CD  . GLN B 101 ? 1.1999 1.2827 1.1305 0.0334  -0.0282 -0.0018 105 GLN B CD  
10489 O OE1 . GLN B 101 ? 1.2420 1.3277 1.1905 0.0333  -0.0331 0.0000  105 GLN B OE1 
10490 N NE2 . GLN B 101 ? 1.2159 1.3002 1.1443 0.0365  -0.0250 0.0078  105 GLN B NE2 
10499 N N   . VAL B 102 ? 0.8548 0.9243 0.7837 0.0482  0.0126  -0.0232 106 VAL B N   
10500 C CA  . VAL B 102 ? 0.8364 0.9089 0.7633 0.0514  0.0242  -0.0263 106 VAL B CA  
10501 C C   . VAL B 102 ? 0.8466 0.9246 0.7678 0.0479  0.0256  -0.0113 106 VAL B C   
10502 O O   . VAL B 102 ? 0.8730 0.9464 0.8054 0.0494  0.0203  0.0011  106 VAL B O   
10503 C CB  . VAL B 102 ? 0.8229 0.8869 0.7699 0.0583  0.0294  -0.0292 106 VAL B CB  
10504 C CG1 . VAL B 102 ? 0.8192 0.8885 0.7648 0.0615  0.0409  -0.0333 106 VAL B CG1 
10505 C CG2 . VAL B 102 ? 0.8567 0.9104 0.8089 0.0599  0.0239  -0.0413 106 VAL B CG2 
10515 N N   . HIS B 103 ? 0.8584 0.9470 0.7621 0.0431  0.0318  -0.0126 107 HIS B N   
10516 C CA  . HIS B 103 ? 0.8768 0.9689 0.7706 0.0362  0.0311  0.0031  107 HIS B CA  
10517 C C   . HIS B 103 ? 0.8725 0.9697 0.7687 0.0364  0.0425  0.0026  107 HIS B C   
10518 O O   . HIS B 103 ? 0.8432 0.9528 0.7354 0.0375  0.0519  -0.0115 107 HIS B O   
10519 C CB  . HIS B 103 ? 0.9051 1.0094 0.7725 0.0253  0.0269  0.0055  107 HIS B CB  
10520 C CG  . HIS B 103 ? 0.9367 1.0383 0.7999 0.0246  0.0160  0.0031  107 HIS B CG  
10521 N ND1 . HIS B 103 ? 0.9321 1.0266 0.7968 0.0225  0.0030  0.0176  107 HIS B ND1 
10522 C CD2 . HIS B 103 ? 0.9384 1.0433 0.7969 0.0259  0.0148  -0.0127 107 HIS B CD2 
10523 C CE1 . HIS B 103 ? 0.9486 1.0445 0.8097 0.0215  -0.0047 0.0117  107 HIS B CE1 
10524 N NE2 . HIS B 103 ? 0.9449 1.0457 0.8014 0.0230  0.0020  -0.0065 107 HIS B NE2 
10532 N N   . VAL B 104 ? 0.8846 0.9729 0.7883 0.0360  0.0408  0.0168  108 VAL B N   
10533 C CA  . VAL B 104 ? 0.8631 0.9547 0.7701 0.0349  0.0500  0.0186  108 VAL B CA  
10534 C C   . VAL B 104 ? 0.8714 0.9617 0.7638 0.0231  0.0447  0.0366  108 VAL B C   
10535 O O   . VAL B 104 ? 0.8570 0.9336 0.7479 0.0218  0.0319  0.0496  108 VAL B O   
10536 C CB  . VAL B 104 ? 0.8470 0.9256 0.7787 0.0455  0.0521  0.0177  108 VAL B CB  
10537 C CG1 . VAL B 104 ? 0.8367 0.9191 0.7714 0.0438  0.0612  0.0192  108 VAL B CG1 
10538 C CG2 . VAL B 104 ? 0.8274 0.9048 0.7718 0.0543  0.0545  0.0029  108 VAL B CG2 
10548 N N   . ARG B 105 ? 0.8788 0.9837 0.7607 0.0142  0.0534  0.0375  109 ARG B N   
10549 C CA  . ARG B 105 ? 0.8668 0.9704 0.7333 -0.0005 0.0480  0.0562  109 ARG B CA  
10550 C C   . ARG B 105 ? 0.8249 0.9411 0.6940 -0.0052 0.0596  0.0549  109 ARG B C   
10551 O O   . ARG B 105 ? 0.7867 0.9280 0.6541 -0.0049 0.0724  0.0400  109 ARG B O   
10552 C CB  . ARG B 105 ? 0.9257 1.0450 0.7641 -0.0156 0.0439  0.0620  109 ARG B CB  
10553 C CG  . ARG B 105 ? 1.0018 1.1186 0.8209 -0.0344 0.0358  0.0843  109 ARG B CG  
10554 C CD  . ARG B 105 ? 1.1111 1.2507 0.9000 -0.0518 0.0343  0.0888  109 ARG B CD  
10555 N NE  . ARG B 105 ? 1.2284 1.3662 0.9964 -0.0735 0.0254  0.1125  109 ARG B NE  
10556 C CZ  . ARG B 105 ? 1.2694 1.4270 1.0290 -0.0881 0.0342  0.1173  109 ARG B CZ  
10557 N NH1 . ARG B 105 ? 1.2749 1.4570 1.0468 -0.0812 0.0527  0.0986  109 ARG B NH1 
10558 N NH2 . ARG B 105 ? 1.2742 1.4270 1.0131 -0.1104 0.0232  0.1416  109 ARG B NH2 
10572 N N   . GLN B 106 ? 0.8642 0.9634 0.7381 -0.0089 0.0540  0.0692  110 GLN B N   
10573 C CA  . GLN B 106 ? 0.8670 0.9768 0.7441 -0.0148 0.0634  0.0699  110 GLN B CA  
10574 C C   . GLN B 106 ? 0.8545 0.9837 0.7062 -0.0378 0.0633  0.0829  110 GLN B C   
10575 O O   . GLN B 106 ? 0.8915 1.0066 0.7268 -0.0501 0.0492  0.1016  110 GLN B O   
10576 C CB  . GLN B 106 ? 0.8852 0.9671 0.7785 -0.0089 0.0566  0.0785  110 GLN B CB  
10577 C CG  . GLN B 106 ? 0.8881 0.9578 0.8064 0.0115  0.0589  0.0655  110 GLN B CG  
10578 C CD  . GLN B 106 ? 0.9034 0.9548 0.8376 0.0169  0.0566  0.0695  110 GLN B CD  
10579 O OE1 . GLN B 106 ? 0.8920 0.9218 0.8371 0.0265  0.0466  0.0724  110 GLN B OE1 
10580 N NE2 . GLN B 106 ? 0.8993 0.9619 0.8353 0.0112  0.0657  0.0683  110 GLN B NE2 
10589 N N   . THR B 107 ? 0.7979 0.9611 0.6464 -0.0438 0.0782  0.0731  111 THR B N   
10590 C CA  . THR B 107 ? 0.8370 1.0278 0.6614 -0.0678 0.0804  0.0844  111 THR B CA  
10591 C C   . THR B 107 ? 0.8439 1.0170 0.6650 -0.0829 0.0715  0.1068  111 THR B C   
10592 O O   . THR B 107 ? 0.8285 0.9781 0.6690 -0.0730 0.0694  0.1074  111 THR B O   
10593 C CB  . THR B 107 ? 0.8801 1.1177 0.7056 -0.0682 0.0993  0.0649  111 THR B CB  
10594 O OG1 . THR B 107 ? 0.9892 1.2611 0.7901 -0.0937 0.1023  0.0758  111 THR B OG1 
10595 C CG2 . THR B 107 ? 0.8497 1.0878 0.6998 -0.0576 0.1081  0.0560  111 THR B CG2 
10603 N N   . GLU B 108 ? 0.8840 1.0682 0.6789 -0.1085 0.0650  0.1259  112 GLU B N   
10604 C CA  . GLU B 108 ? 0.9241 1.0852 0.7121 -0.1258 0.0518  0.1503  112 GLU B CA  
10605 C C   . GLU B 108 ? 0.9135 1.0905 0.7144 -0.1293 0.0632  0.1466  112 GLU B C   
10606 O O   . GLU B 108 ? 0.9535 1.0990 0.7640 -0.1291 0.0536  0.1570  112 GLU B O   
10607 C CB  . GLU B 108 ? 0.9927 1.1651 0.7470 -0.1560 0.0418  0.1730  112 GLU B CB  
10608 C CG  . GLU B 108 ? 1.0983 1.2442 0.8387 -0.1552 0.0239  0.1836  112 GLU B CG  
10609 C CD  . GLU B 108 ? 1.1815 1.3515 0.9203 -0.1427 0.0342  0.1634  112 GLU B CD  
10610 O OE1 . GLU B 108 ? 1.2000 1.4053 0.9486 -0.1336 0.0544  0.1404  112 GLU B OE1 
10611 O OE2 . GLU B 108 ? 1.2308 1.3835 0.9591 -0.1416 0.0206  0.1702  112 GLU B OE2 
10618 N N   . ASP B 109 ? 0.8816 1.1080 0.6835 -0.1317 0.0827  0.1306  113 ASP B N   
10619 C CA  . ASP B 109 ? 0.8475 1.0968 0.6624 -0.1353 0.0943  0.1256  113 ASP B CA  
10620 C C   . ASP B 109 ? 0.7841 1.0498 0.6244 -0.1085 0.1103  0.0960  113 ASP B C   
10621 O O   . ASP B 109 ? 0.7837 1.0840 0.6214 -0.1024 0.1216  0.0776  113 ASP B O   
10622 C CB  . ASP B 109 ? 0.9164 1.2160 0.7103 -0.1646 0.1021  0.1341  113 ASP B CB  
10623 C CG  . ASP B 109 ? 0.9228 1.2395 0.7274 -0.1749 0.1085  0.1374  113 ASP B CG  
10624 O OD1 . ASP B 109 ? 0.8905 1.1924 0.7215 -0.1545 0.1128  0.1248  113 ASP B OD1 
10625 O OD2 . ASP B 109 ? 0.9759 1.3224 0.7620 -0.2047 0.1088  0.1535  113 ASP B OD2 
10630 N N   . TYR B 110 ? 0.7549 0.9950 0.6192 -0.0926 0.1096  0.0912  114 TYR B N   
10631 C CA  . TYR B 110 ? 0.7369 0.9856 0.6254 -0.0679 0.1212  0.0662  114 TYR B CA  
10632 C C   . TYR B 110 ? 0.7591 1.0099 0.6658 -0.0666 0.1259  0.0653  114 TYR B C   
10633 O O   . TYR B 110 ? 0.7993 1.0172 0.7083 -0.0715 0.1153  0.0809  114 TYR B O   
10634 C CB  . TYR B 110 ? 0.6844 0.8942 0.5843 -0.0461 0.1136  0.0599  114 TYR B CB  
10635 C CG  . TYR B 110 ? 0.6294 0.8503 0.5469 -0.0240 0.1234  0.0346  114 TYR B CG  
10636 C CD1 . TYR B 110 ? 0.6523 0.9055 0.5625 -0.0215 0.1316  0.0183  114 TYR B CD1 
10637 C CD2 . TYR B 110 ? 0.6260 0.8241 0.5662 -0.0061 0.1229  0.0271  114 TYR B CD2 
10638 C CE1 . TYR B 110 ? 0.6542 0.9124 0.5800 -0.0011 0.1372  -0.0050 114 TYR B CE1 
10639 C CE2 . TYR B 110 ? 0.6362 0.8405 0.5911 0.0122  0.1288  0.0061  114 TYR B CE2 
10640 C CZ  . TYR B 110 ? 0.6568 0.8890 0.6048 0.0150  0.1351  -0.0098 114 TYR B CZ  
10641 O OH  . TYR B 110 ? 0.6712 0.9046 0.6335 0.0336  0.1379  -0.0309 114 TYR B OH  
10651 N N   . PRO B 111 ? 0.7524 1.0403 0.6724 -0.0593 0.1402  0.0466  115 PRO B N   
10652 C CA  . PRO B 111 ? 0.7113 1.0038 0.6487 -0.0588 0.1441  0.0460  115 PRO B CA  
10653 C C   . PRO B 111 ? 0.6609 0.9083 0.6167 -0.0408 0.1368  0.0453  115 PRO B C   
10654 O O   . PRO B 111 ? 0.6629 0.8857 0.6240 -0.0239 0.1330  0.0380  115 PRO B O   
10655 C CB  . PRO B 111 ? 0.6795 1.0204 0.6297 -0.0487 0.1595  0.0217  115 PRO B CB  
10656 C CG  . PRO B 111 ? 0.7157 1.0619 0.6608 -0.0355 0.1615  0.0058  115 PRO B CG  
10657 C CD  . PRO B 111 ? 0.7559 1.0838 0.6762 -0.0503 0.1520  0.0239  115 PRO B CD  
10665 N N   . VAL B 112 ? 0.6757 0.9149 0.6407 -0.0461 0.1349  0.0530  116 VAL B N   
10666 C CA  . VAL B 112 ? 0.6898 0.8893 0.6700 -0.0322 0.1278  0.0536  116 VAL B CA  
10667 C C   . VAL B 112 ? 0.7086 0.9243 0.7071 -0.0288 0.1349  0.0461  116 VAL B C   
10668 O O   . VAL B 112 ? 0.7596 0.9948 0.7547 -0.0464 0.1366  0.0547  116 VAL B O   
10669 C CB  . VAL B 112 ? 0.7132 0.8731 0.6828 -0.0430 0.1121  0.0744  116 VAL B CB  
10670 C CG1 . VAL B 112 ? 0.7078 0.8323 0.6939 -0.0270 0.1058  0.0714  116 VAL B CG1 
10671 C CG2 . VAL B 112 ? 0.7251 0.8703 0.6768 -0.0470 0.1033  0.0829  116 VAL B CG2 
10681 N N   . ASP B 113 ? 0.6568 0.8649 0.6741 -0.0078 0.1379  0.0311  117 ASP B N   
10682 C CA  . ASP B 113 ? 0.6338 0.8480 0.6693 -0.0023 0.1414  0.0253  117 ASP B CA  
10683 C C   . ASP B 113 ? 0.6537 0.8263 0.6949 0.0031  0.1317  0.0326  117 ASP B C   
10684 O O   . ASP B 113 ? 0.6919 0.8371 0.7328 0.0141  0.1259  0.0318  117 ASP B O   
10685 C CB  . ASP B 113 ? 0.6648 0.8974 0.7172 0.0169  0.1489  0.0041  117 ASP B CB  
10686 C CG  . ASP B 113 ? 0.7292 1.0084 0.7796 0.0146  0.1588  -0.0079 117 ASP B CG  
10687 O OD1 . ASP B 113 ? 0.7658 1.0729 0.8055 -0.0046 0.1627  0.0003  117 ASP B OD1 
10688 O OD2 . ASP B 113 ? 0.7176 1.0061 0.7769 0.0315  0.1620  -0.0262 117 ASP B OD2 
10693 N N   . LEU B 114 ? 0.6672 0.8381 0.7139 -0.0048 0.1298  0.0389  118 LEU B N   
10694 C CA  . LEU B 114 ? 0.6325 0.7675 0.6846 0.0005  0.1208  0.0436  118 LEU B CA  
10695 C C   . LEU B 114 ? 0.5889 0.7348 0.6571 0.0038  0.1246  0.0375  118 LEU B C   
10696 O O   . LEU B 114 ? 0.5810 0.7469 0.6495 -0.0103 0.1268  0.0424  118 LEU B O   
10697 C CB  . LEU B 114 ? 0.6660 0.7757 0.7034 -0.0154 0.1086  0.0611  118 LEU B CB  
10698 C CG  . LEU B 114 ? 0.6894 0.7599 0.7311 -0.0074 0.0974  0.0633  118 LEU B CG  
10699 C CD1 . LEU B 114 ? 0.7408 0.7801 0.7675 -0.0137 0.0830  0.0758  118 LEU B CD1 
10700 C CD2 . LEU B 114 ? 0.7015 0.7705 0.7502 -0.0142 0.0954  0.0656  118 LEU B CD2 
10712 N N   . TYR B 115 ? 0.6102 0.7443 0.6914 0.0209  0.1248  0.0277  119 TYR B N   
10713 C CA  . TYR B 115 ? 0.6279 0.7680 0.7239 0.0251  0.1264  0.0226  119 TYR B CA  
10714 C C   . TYR B 115 ? 0.6657 0.7734 0.7611 0.0256  0.1172  0.0285  119 TYR B C   
10715 O O   . TYR B 115 ? 0.6887 0.7738 0.7833 0.0359  0.1129  0.0265  119 TYR B O   
10716 C CB  . TYR B 115 ? 0.5834 0.7329 0.6931 0.0424  0.1309  0.0084  119 TYR B CB  
10717 C CG  . TYR B 115 ? 0.5924 0.7548 0.7176 0.0460  0.1325  0.0029  119 TYR B CG  
10718 C CD1 . TYR B 115 ? 0.6444 0.8415 0.7768 0.0401  0.1383  -0.0007 119 TYR B CD1 
10719 C CD2 . TYR B 115 ? 0.6035 0.7466 0.7361 0.0548  0.1279  0.0011  119 TYR B CD2 
10720 C CE1 . TYR B 115 ? 0.6564 0.8663 0.8042 0.0439  0.1385  -0.0058 119 TYR B CE1 
10721 C CE2 . TYR B 115 ? 0.6522 0.8064 0.7980 0.0575  0.1279  -0.0030 119 TYR B CE2 
10722 C CZ  . TYR B 115 ? 0.6718 0.8583 0.8258 0.0527  0.1328  -0.0065 119 TYR B CZ  
10723 O OH  . TYR B 115 ? 0.6645 0.8631 0.8330 0.0560  0.1318  -0.0107 119 TYR B OH  
10733 N N   . TYR B 116 ? 0.6536 0.7613 0.7497 0.0141  0.1140  0.0347  120 TYR B N   
10734 C CA  . TYR B 116 ? 0.6848 0.7623 0.7794 0.0136  0.1041  0.0388  120 TYR B CA  
10735 C C   . TYR B 116 ? 0.7534 0.8345 0.8621 0.0240  0.1064  0.0298  120 TYR B C   
10736 O O   . TYR B 116 ? 0.8171 0.9163 0.9336 0.0183  0.1090  0.0292  120 TYR B O   
10737 C CB  . TYR B 116 ? 0.6700 0.7421 0.7557 -0.0062 0.0970  0.0512  120 TYR B CB  
10738 C CG  . TYR B 116 ? 0.6537 0.6877 0.7338 -0.0072 0.0830  0.0556  120 TYR B CG  
10739 C CD1 . TYR B 116 ? 0.6901 0.6952 0.7582 -0.0076 0.0723  0.0618  120 TYR B CD1 
10740 C CD2 . TYR B 116 ? 0.6616 0.6887 0.7487 -0.0071 0.0793  0.0525  120 TYR B CD2 
10741 C CE1 . TYR B 116 ? 0.7097 0.6796 0.7741 -0.0059 0.0577  0.0631  120 TYR B CE1 
10742 C CE2 . TYR B 116 ? 0.6849 0.6773 0.7668 -0.0065 0.0657  0.0538  120 TYR B CE2 
10743 C CZ  . TYR B 116 ? 0.7078 0.6716 0.7790 -0.0052 0.0546  0.0583  120 TYR B CZ  
10744 O OH  . TYR B 116 ? 0.7146 0.6432 0.7820 -0.0021 0.0393  0.0570  120 TYR B OH  
10754 N N   . LEU B 117 ? 0.7475 0.8137 0.8593 0.0381  0.1048  0.0235  121 LEU B N   
10755 C CA  . LEU B 117 ? 0.6938 0.7625 0.8165 0.0471  0.1058  0.0163  121 LEU B CA  
10756 C C   . LEU B 117 ? 0.6934 0.7391 0.8131 0.0477  0.0977  0.0166  121 LEU B C   
10757 O O   . LEU B 117 ? 0.6846 0.7124 0.7988 0.0538  0.0931  0.0154  121 LEU B O   
10758 C CB  . LEU B 117 ? 0.6459 0.7175 0.7730 0.0601  0.1094  0.0095  121 LEU B CB  
10759 C CG  . LEU B 117 ? 0.6832 0.7572 0.8195 0.0678  0.1090  0.0040  121 LEU B CG  
10760 C CD1 . LEU B 117 ? 0.6795 0.7717 0.8257 0.0646  0.1109  0.0026  121 LEU B CD1 
10761 C CD2 . LEU B 117 ? 0.6702 0.7454 0.8088 0.0773  0.1105  -0.0002 121 LEU B CD2 
10773 N N   . MET B 118 ? 0.6843 0.7324 0.8081 0.0421  0.0954  0.0168  122 MET B N   
10774 C CA  . MET B 118 ? 0.7134 0.7396 0.8328 0.0402  0.0863  0.0166  122 MET B CA  
10775 C C   . MET B 118 ? 0.7135 0.7438 0.8398 0.0461  0.0863  0.0096  122 MET B C   
10776 O O   . MET B 118 ? 0.7073 0.7564 0.8420 0.0439  0.0904  0.0092  122 MET B O   
10777 C CB  . MET B 118 ? 0.6771 0.6976 0.7911 0.0239  0.0802  0.0251  122 MET B CB  
10778 C CG  . MET B 118 ? 0.6421 0.6359 0.7511 0.0217  0.0681  0.0240  122 MET B CG  
10779 S SD  . MET B 118 ? 0.6909 0.6714 0.7907 -0.0006 0.0572  0.0368  122 MET B SD  
10780 C CE  . MET B 118 ? 0.7332 0.6801 0.8294 0.0030  0.0420  0.0298  122 MET B CE  
10790 N N   . ASP B 119 ? 0.6984 0.7132 0.8213 0.0537  0.0812  0.0036  123 ASP B N   
10791 C CA  . ASP B 119 ? 0.6899 0.7065 0.8156 0.0564  0.0791  -0.0027 123 ASP B CA  
10792 C C   . ASP B 119 ? 0.7188 0.7302 0.8438 0.0451  0.0731  0.0001  123 ASP B C   
10793 O O   . ASP B 119 ? 0.7286 0.7205 0.8467 0.0386  0.0649  0.0032  123 ASP B O   
10794 C CB  . ASP B 119 ? 0.6919 0.6959 0.8129 0.0664  0.0745  -0.0115 123 ASP B CB  
10795 C CG  . ASP B 119 ? 0.6834 0.6931 0.8053 0.0691  0.0729  -0.0194 123 ASP B CG  
10796 O OD1 . ASP B 119 ? 0.6749 0.6887 0.7989 0.0618  0.0715  -0.0176 123 ASP B OD1 
10797 O OD2 . ASP B 119 ? 0.6835 0.6961 0.8037 0.0781  0.0731  -0.0277 123 ASP B OD2 
10802 N N   . LEU B 120 ? 0.7190 0.7467 0.8510 0.0420  0.0756  -0.0003 124 LEU B N   
10803 C CA  . LEU B 120 ? 0.7398 0.7660 0.8724 0.0305  0.0698  0.0022  124 LEU B CA  
10804 C C   . LEU B 120 ? 0.7050 0.7299 0.8374 0.0336  0.0657  -0.0053 124 LEU B C   
10805 O O   . LEU B 120 ? 0.6669 0.6988 0.8029 0.0254  0.0628  -0.0038 124 LEU B O   
10806 C CB  . LEU B 120 ? 0.7649 0.8163 0.9070 0.0219  0.0753  0.0086  124 LEU B CB  
10807 C CG  . LEU B 120 ? 0.8191 0.8749 0.9591 0.0109  0.0769  0.0172  124 LEU B CG  
10808 C CD1 . LEU B 120 ? 0.8250 0.9122 0.9761 0.0017  0.0815  0.0207  124 LEU B CD1 
10809 C CD2 . LEU B 120 ? 0.8878 0.9161 1.0158 0.0001  0.0660  0.0224  124 LEU B CD2 
10821 N N   . SER B 121 ? 0.6590 0.6781 0.7871 0.0446  0.0654  -0.0136 125 SER B N   
10822 C CA  . SER B 121 ? 0.6751 0.6930 0.7999 0.0465  0.0607  -0.0220 125 SER B CA  
10823 C C   . SER B 121 ? 0.7045 0.6989 0.8227 0.0411  0.0493  -0.0257 125 SER B C   
10824 O O   . SER B 121 ? 0.6943 0.6714 0.8096 0.0355  0.0442  -0.0203 125 SER B O   
10825 C CB  . SER B 121 ? 0.7225 0.7450 0.8438 0.0583  0.0635  -0.0308 125 SER B CB  
10826 O OG  . SER B 121 ? 0.8453 0.8539 0.9629 0.0654  0.0620  -0.0343 125 SER B OG  
10831 N N   . ALA B 122 ? 0.7557 0.7481 0.8701 0.0420  0.0438  -0.0348 126 ALA B N   
10832 C CA  . ALA B 122 ? 0.8161 0.7858 0.9248 0.0351  0.0311  -0.0383 126 ALA B CA  
10833 C C   . ALA B 122 ? 0.7971 0.7369 0.8989 0.0410  0.0215  -0.0438 126 ALA B C   
10834 O O   . ALA B 122 ? 0.8126 0.7268 0.9097 0.0322  0.0090  -0.0412 126 ALA B O   
10835 C CB  . ALA B 122 ? 0.8325 0.8074 0.9374 0.0366  0.0271  -0.0494 126 ALA B CB  
10841 N N   . SER B 123 ? 0.7613 0.7030 0.8627 0.0552  0.0255  -0.0509 127 SER B N   
10842 C CA  . SER B 123 ? 0.7375 0.6516 0.8342 0.0635  0.0148  -0.0576 127 SER B CA  
10843 C C   . SER B 123 ? 0.7438 0.6415 0.8395 0.0554  0.0118  -0.0429 127 SER B C   
10844 O O   . SER B 123 ? 0.7271 0.5986 0.8186 0.0612  0.0006  -0.0460 127 SER B O   
10845 C CB  . SER B 123 ? 0.7515 0.6788 0.8498 0.0812  0.0204  -0.0703 127 SER B CB  
10846 O OG  . SER B 123 ? 0.7512 0.7003 0.8545 0.0816  0.0339  -0.0610 127 SER B OG  
10852 N N   . MET B 124 ? 0.7720 0.6857 0.8715 0.0425  0.0204  -0.0278 128 MET B N   
10853 C CA  . MET B 124 ? 0.8064 0.7120 0.9038 0.0331  0.0194  -0.0136 128 MET B CA  
10854 C C   . MET B 124 ? 0.8270 0.7238 0.9212 0.0124  0.0117  -0.0016 128 MET B C   
10855 O O   . MET B 124 ? 0.8142 0.7158 0.9072 0.0000  0.0138  0.0123  128 MET B O   
10856 C CB  . MET B 124 ? 0.7774 0.7126 0.8816 0.0349  0.0356  -0.0072 128 MET B CB  
10857 C CG  . MET B 124 ? 0.7606 0.7063 0.8676 0.0521  0.0429  -0.0170 128 MET B CG  
10858 S SD  . MET B 124 ? 0.7845 0.7058 0.8861 0.0636  0.0342  -0.0216 128 MET B SD  
10859 C CE  . MET B 124 ? 0.7385 0.6601 0.8376 0.0525  0.0375  -0.0045 128 MET B CE  
10869 N N   . ASP B 125 ? 0.8230 0.7095 0.9154 0.0072  0.0025  -0.0066 129 ASP B N   
10870 C CA  . ASP B 125 ? 0.8702 0.7473 0.9591 -0.0145 -0.0069 0.0052  129 ASP B CA  
10871 C C   . ASP B 125 ? 0.8867 0.7271 0.9648 -0.0231 -0.0232 0.0138  129 ASP B C   
10872 O O   . ASP B 125 ? 0.8849 0.7279 0.9596 -0.0427 -0.0249 0.0306  129 ASP B O   
10873 C CB  . ASP B 125 ? 0.9725 0.8427 1.0608 -0.0172 -0.0153 -0.0036 129 ASP B CB  
10874 C CG  . ASP B 125 ? 1.1526 1.0208 1.2393 -0.0417 -0.0233 0.0094  129 ASP B CG  
10875 O OD1 . ASP B 125 ? 1.1832 1.0866 1.2789 -0.0516 -0.0117 0.0176  129 ASP B OD1 
10876 O OD2 . ASP B 125 ? 1.2548 1.0868 1.3318 -0.0511 -0.0423 0.0109  129 ASP B OD2 
10881 N N   . ASP B 126 ? 0.8939 0.7009 0.9663 -0.0089 -0.0366 0.0022  130 ASP B N   
10882 C CA  . ASP B 126 ? 0.9238 0.6914 0.9859 -0.0147 -0.0552 0.0100  130 ASP B CA  
10883 C C   . ASP B 126 ? 0.9405 0.7202 1.0015 -0.0187 -0.0465 0.0239  130 ASP B C   
10884 O O   . ASP B 126 ? 1.0013 0.7630 1.0530 -0.0364 -0.0574 0.0404  130 ASP B O   
10885 C CB  . ASP B 126 ? 0.9347 0.6697 0.9944 0.0071  -0.0698 -0.0089 130 ASP B CB  
10886 C CG  . ASP B 126 ? 0.9300 0.6909 0.9983 0.0314  -0.0542 -0.0239 130 ASP B CG  
10887 O OD1 . ASP B 126 ? 0.9148 0.7139 0.9906 0.0332  -0.0352 -0.0261 130 ASP B OD1 
10888 O OD2 . ASP B 126 ? 0.9729 0.7167 1.0409 0.0480  -0.0620 -0.0330 130 ASP B OD2 
10893 N N   . ASP B 127 ? 0.8785 0.6888 0.9477 -0.0038 -0.0279 0.0180  131 ASP B N   
10894 C CA  . ASP B 127 ? 0.8698 0.6931 0.9378 -0.0062 -0.0193 0.0290  131 ASP B CA  
10895 C C   . ASP B 127 ? 0.8506 0.6960 0.9168 -0.0302 -0.0127 0.0469  131 ASP B C   
10896 O O   . ASP B 127 ? 0.8318 0.6708 0.8894 -0.0431 -0.0171 0.0612  131 ASP B O   
10897 C CB  . ASP B 127 ? 0.8666 0.7197 0.9443 0.0126  -0.0010 0.0188  131 ASP B CB  
10898 C CG  . ASP B 127 ? 0.8756 0.7145 0.9552 0.0351  -0.0063 0.0014  131 ASP B CG  
10899 O OD1 . ASP B 127 ? 0.8730 0.7059 0.9544 0.0418  -0.0113 -0.0114 131 ASP B OD1 
10900 O OD2 . ASP B 127 ? 0.8432 0.6799 0.9229 0.0460  -0.0055 -0.0002 131 ASP B OD2 
10905 N N   . LEU B 128 ? 0.8201 0.6945 0.8946 -0.0368 -0.0024 0.0461  132 LEU B N   
10906 C CA  . LEU B 128 ? 0.8246 0.7269 0.9000 -0.0588 0.0043  0.0606  132 LEU B CA  
10907 C C   . LEU B 128 ? 0.8537 0.7302 0.9161 -0.0834 -0.0136 0.0764  132 LEU B C   
10908 O O   . LEU B 128 ? 0.8235 0.7184 0.8813 -0.1030 -0.0105 0.0916  132 LEU B O   
10909 C CB  . LEU B 128 ? 0.7981 0.7319 0.8859 -0.0606 0.0140  0.0555  132 LEU B CB  
10910 C CG  . LEU B 128 ? 0.7715 0.7445 0.8729 -0.0466 0.0335  0.0478  132 LEU B CG  
10911 C CD1 . LEU B 128 ? 0.7684 0.7673 0.8811 -0.0511 0.0380  0.0449  132 LEU B CD1 
10912 C CD2 . LEU B 128 ? 0.7743 0.7740 0.8767 -0.0511 0.0448  0.0554  132 LEU B CD2 
10924 N N   . ASN B 129 ? 0.9402 0.7744 0.9957 -0.0834 -0.0335 0.0728  133 ASN B N   
10925 C CA  . ASN B 129 ? 1.0214 0.8267 1.0638 -0.1091 -0.0538 0.0888  133 ASN B CA  
10926 C C   . ASN B 129 ? 1.0318 0.8110 1.0605 -0.1160 -0.0656 0.1021  133 ASN B C   
10927 O O   . ASN B 129 ? 1.0856 0.8559 1.1024 -0.1436 -0.0771 0.1218  133 ASN B O   
10928 C CB  . ASN B 129 ? 1.1152 0.8792 1.1542 -0.1056 -0.0740 0.0790  133 ASN B CB  
10929 C CG  . ASN B 129 ? 1.1871 0.9720 1.2331 -0.1170 -0.0704 0.0774  133 ASN B CG  
10930 O OD1 . ASN B 129 ? 1.2145 1.0281 1.2618 -0.1407 -0.0649 0.0921  133 ASN B OD1 
10931 N ND2 . ASN B 129 ? 1.2349 1.0090 1.2856 -0.1005 -0.0734 0.0590  133 ASN B ND2 
10938 N N   . THR B 130 ? 0.9916 0.7597 1.0211 -0.0932 -0.0637 0.0929  134 THR B N   
10939 C CA  . THR B 130 ? 1.0678 0.8072 1.0843 -0.0974 -0.0775 0.1045  134 THR B CA  
10940 C C   . THR B 130 ? 1.0205 0.7966 1.0355 -0.1037 -0.0603 0.1151  134 THR B C   
10941 O O   . THR B 130 ? 1.0564 0.8130 1.0593 -0.1098 -0.0708 0.1268  134 THR B O   
10942 C CB  . THR B 130 ? 1.1186 0.8231 1.1369 -0.0688 -0.0887 0.0878  134 THR B CB  
10943 O OG1 . THR B 130 ? 1.1266 0.8644 1.1585 -0.0447 -0.0667 0.0716  134 THR B OG1 
10944 C CG2 . THR B 130 ? 1.1874 0.8536 1.2058 -0.0618 -0.1082 0.0752  134 THR B CG2 
10952 N N   . ILE B 131 ? 0.9125 0.7398 0.9390 -0.1020 -0.0357 0.1107  135 ILE B N   
10953 C CA  . ILE B 131 ? 0.8862 0.7504 0.9118 -0.1065 -0.0194 0.1177  135 ILE B CA  
10954 C C   . ILE B 131 ? 0.8690 0.7750 0.8950 -0.1323 -0.0095 0.1297  135 ILE B C   
10955 O O   . ILE B 131 ? 0.8075 0.7585 0.8394 -0.1319 0.0096  0.1283  135 ILE B O   
10956 C CB  . ILE B 131 ? 0.8609 0.7513 0.9006 -0.0796 0.0004  0.1003  135 ILE B CB  
10957 C CG1 . ILE B 131 ? 0.8172 0.7335 0.8726 -0.0716 0.0128  0.0878  135 ILE B CG1 
10958 C CG2 . ILE B 131 ? 0.8579 0.7147 0.8971 -0.0562 -0.0083 0.0896  135 ILE B CG2 
10959 C CD1 . ILE B 131 ? 0.7573 0.7072 0.8253 -0.0529 0.0327  0.0757  135 ILE B CD1 
10971 N N   . LYS B 132 ? 0.9579 0.8509 0.9781 -0.1548 -0.0230 0.1404  136 LYS B N   
10972 C CA  . LYS B 132 ? 1.0253 0.9630 1.0472 -0.1808 -0.0140 0.1516  136 LYS B CA  
10973 C C   . LYS B 132 ? 1.0080 0.9706 1.0175 -0.2010 -0.0096 0.1680  136 LYS B C   
10974 O O   . LYS B 132 ? 1.0396 1.0566 1.0543 -0.2151 0.0059  0.1715  136 LYS B O   
10975 C CB  . LYS B 132 ? 1.1490 1.0641 1.1653 -0.2039 -0.0324 0.1620  136 LYS B CB  
10976 C CG  . LYS B 132 ? 1.2018 1.1082 1.2315 -0.1888 -0.0329 0.1457  136 LYS B CG  
10977 C CD  . LYS B 132 ? 1.2759 1.1501 1.2970 -0.2117 -0.0553 0.1559  136 LYS B CD  
10978 C CE  . LYS B 132 ? 1.2736 1.1418 1.3069 -0.1979 -0.0560 0.1393  136 LYS B CE  
10979 N NZ  . LYS B 132 ? 1.3433 1.1696 1.3664 -0.2170 -0.0814 0.1467  136 LYS B NZ  
10993 N N   . GLU B 133 ? 0.9728 0.8989 0.9660 -0.2024 -0.0234 0.1774  137 GLU B N   
10994 C CA  . GLU B 133 ? 0.9807 0.9266 0.9585 -0.2226 -0.0215 0.1942  137 GLU B CA  
10995 C C   . GLU B 133 ? 0.8771 0.8164 0.8531 -0.1999 -0.0158 0.1865  137 GLU B C   
10996 O O   . GLU B 133 ? 0.8544 0.7877 0.8134 -0.2131 -0.0226 0.2009  137 GLU B O   
10997 C CB  . GLU B 133 ? 1.1173 1.0252 1.0727 -0.2545 -0.0481 0.2193  137 GLU B CB  
10998 C CG  . GLU B 133 ? 1.2503 1.1709 1.2053 -0.2837 -0.0539 0.2307  137 GLU B CG  
10999 C CD  . GLU B 133 ? 1.4484 1.3240 1.3797 -0.3165 -0.0838 0.2568  137 GLU B CD  
11000 O OE1 . GLU B 133 ? 1.5273 1.3604 1.4430 -0.3151 -0.1008 0.2658  137 GLU B OE1 
11001 O OE2 . GLU B 133 ? 1.5258 1.4076 1.4543 -0.3444 -0.0919 0.2690  137 GLU B OE2 
11008 N N   . LEU B 134 ? 0.8467 0.7878 0.8394 -0.1673 -0.0041 0.1646  138 LEU B N   
11009 C CA  . LEU B 134 ? 0.8717 0.8096 0.8642 -0.1462 0.0020  0.1566  138 LEU B CA  
11010 C C   . LEU B 134 ? 0.8306 0.8189 0.8201 -0.1544 0.0200  0.1595  138 LEU B C   
11011 O O   . LEU B 134 ? 0.8488 0.8317 0.8268 -0.1539 0.0179  0.1648  138 LEU B O   
11012 C CB  . LEU B 134 ? 0.8471 0.7824 0.8582 -0.1132 0.0114  0.1336  138 LEU B CB  
11013 C CG  . LEU B 134 ? 0.8234 0.7590 0.8368 -0.0908 0.0186  0.1238  138 LEU B CG  
11014 C CD1 . LEU B 134 ? 0.8890 0.7797 0.8888 -0.0894 -0.0014 0.1319  138 LEU B CD1 
11015 C CD2 . LEU B 134 ? 0.7992 0.7385 0.8305 -0.0633 0.0285  0.1032  138 LEU B CD2 
11027 N N   . GLY B 135 ? 0.7886 0.8276 0.7889 -0.1611 0.0371  0.1548  139 GLY B N   
11028 C CA  . GLY B 135 ? 0.7523 0.8435 0.7518 -0.1658 0.0549  0.1532  139 GLY B CA  
11029 C C   . GLY B 135 ? 0.7552 0.8497 0.7310 -0.1935 0.0470  0.1741  139 GLY B C   
11030 O O   . GLY B 135 ? 0.8018 0.9106 0.7697 -0.1901 0.0535  0.1733  139 GLY B O   
11034 N N   . SER B 136 ? 0.7346 0.8154 0.6977 -0.2228 0.0318  0.1940  140 SER B N   
11035 C CA  . SER B 136 ? 0.8048 0.8872 0.7428 -0.2535 0.0217  0.2174  140 SER B CA  
11036 C C   . SER B 136 ? 0.8534 0.8780 0.7761 -0.2462 0.0021  0.2255  140 SER B C   
11037 O O   . SER B 136 ? 0.9046 0.9380 0.8114 -0.2544 0.0020  0.2343  140 SER B O   
11038 C CB  . SER B 136 ? 0.8484 0.9307 0.7765 -0.2893 0.0088  0.2380  140 SER B CB  
11039 O OG  . SER B 136 ? 0.8971 0.9253 0.8301 -0.2831 -0.0094 0.2377  140 SER B OG  
11045 N N   . ARG B 137 ? 0.8807 0.8479 0.8082 -0.2302 -0.0152 0.2214  141 ARG B N   
11046 C CA  . ARG B 137 ? 0.9202 0.8330 0.8364 -0.2202 -0.0355 0.2267  141 ARG B CA  
11047 C C   . ARG B 137 ? 0.8521 0.7801 0.7735 -0.1952 -0.0213 0.2126  141 ARG B C   
11048 O O   . ARG B 137 ? 0.8224 0.7380 0.7281 -0.2002 -0.0301 0.2231  141 ARG B O   
11049 C CB  . ARG B 137 ? 0.9717 0.8285 0.8967 -0.2023 -0.0537 0.2183  141 ARG B CB  
11050 C CG  . ARG B 137 ? 1.0891 0.9133 1.0035 -0.2284 -0.0765 0.2355  141 ARG B CG  
11051 C CD  . ARG B 137 ? 1.2127 0.9905 1.1390 -0.2079 -0.0907 0.2214  141 ARG B CD  
11052 N NE  . ARG B 137 ? 1.3260 1.0550 1.2521 -0.1829 -0.1075 0.2136  141 ARG B NE  
11053 C CZ  . ARG B 137 ? 1.3362 1.0571 1.2800 -0.1481 -0.1015 0.1893  141 ARG B CZ  
11054 N NH1 . ARG B 137 ? 1.2702 1.0240 1.2321 -0.1341 -0.0801 0.1714  141 ARG B NH1 
11055 N NH2 . ARG B 137 ? 1.3765 1.0574 1.3199 -0.1276 -0.1180 0.1832  141 ARG B NH2 
11069 N N   . LEU B 138 ? 0.8365 0.7904 0.7793 -0.1694 -0.0009 0.1895  142 LEU B N   
11070 C CA  . LEU B 138 ? 0.8407 0.8071 0.7893 -0.1460 0.0114  0.1756  142 LEU B CA  
11071 C C   . LEU B 138 ? 0.8650 0.8760 0.8015 -0.1611 0.0241  0.1818  142 LEU B C   
11072 O O   . LEU B 138 ? 0.8832 0.8874 0.8093 -0.1571 0.0211  0.1845  142 LEU B O   
11073 C CB  . LEU B 138 ? 0.8131 0.7974 0.7858 -0.1189 0.0288  0.1517  142 LEU B CB  
11074 C CG  . LEU B 138 ? 0.8475 0.8461 0.8275 -0.0957 0.0416  0.1367  142 LEU B CG  
11075 C CD1 . LEU B 138 ? 0.8511 0.8087 0.8249 -0.0832 0.0265  0.1386  142 LEU B CD1 
11076 C CD2 . LEU B 138 ? 0.8360 0.8500 0.8381 -0.0734 0.0558  0.1164  142 LEU B CD2 
11088 N N   . SER B 139 ? 0.8584 0.9183 0.7966 -0.1782 0.0383  0.1829  143 SER B N   
11089 C CA  . SER B 139 ? 0.8575 0.9672 0.7851 -0.1917 0.0519  0.1854  143 SER B CA  
11090 C C   . SER B 139 ? 0.8169 0.9130 0.7160 -0.2203 0.0358  0.2109  143 SER B C   
11091 O O   . SER B 139 ? 0.7944 0.9148 0.6807 -0.2252 0.0420  0.2127  143 SER B O   
11092 C CB  . SER B 139 ? 0.9105 1.0794 0.8479 -0.2036 0.0695  0.1798  143 SER B CB  
11093 O OG  . SER B 139 ? 1.0280 1.1892 0.9614 -0.2281 0.0587  0.1957  143 SER B OG  
11099 N N   . LYS B 140 ? 0.8047 0.8608 0.6924 -0.2400 0.0136  0.2308  144 LYS B N   
11100 C CA  . LYS B 140 ? 0.8718 0.9082 0.7310 -0.2686 -0.0058 0.2576  144 LYS B CA  
11101 C C   . LYS B 140 ? 0.9230 0.9166 0.7751 -0.2505 -0.0191 0.2576  144 LYS B C   
11102 O O   . LYS B 140 ? 0.9445 0.9444 0.7757 -0.2655 -0.0241 0.2713  144 LYS B O   
11103 C CB  . LYS B 140 ? 0.9810 0.9794 0.8301 -0.2939 -0.0295 0.2789  144 LYS B CB  
11104 C CG  . LYS B 140 ? 1.1644 1.1361 0.9823 -0.3262 -0.0540 0.3097  144 LYS B CG  
11105 C CD  . LYS B 140 ? 1.3219 1.2867 1.1264 -0.3649 -0.0698 0.3339  144 LYS B CD  
11106 C CE  . LYS B 140 ? 1.4199 1.3023 1.2147 -0.3684 -0.1066 0.3494  144 LYS B CE  
11107 N NZ  . LYS B 140 ? 1.4579 1.3023 1.2293 -0.3758 -0.1292 0.3677  144 LYS B NZ  
11121 N N   . GLU B 141 ? 0.9387 0.8920 0.8081 -0.2189 -0.0249 0.2422  145 GLU B N   
11122 C CA  . GLU B 141 ? 0.9767 0.8947 0.8431 -0.1995 -0.0367 0.2398  145 GLU B CA  
11123 C C   . GLU B 141 ? 1.0067 0.9641 0.8777 -0.1836 -0.0153 0.2245  145 GLU B C   
11124 O O   . GLU B 141 ? 1.0473 0.9940 0.9060 -0.1821 -0.0230 0.2302  145 GLU B O   
11125 C CB  . GLU B 141 ? 0.9817 0.8526 0.8664 -0.1706 -0.0481 0.2259  145 GLU B CB  
11126 C CG  . GLU B 141 ? 1.0685 0.8842 0.9448 -0.1824 -0.0779 0.2412  145 GLU B CG  
11127 C CD  . GLU B 141 ? 1.1849 0.9652 1.0375 -0.1982 -0.1040 0.2638  145 GLU B CD  
11128 O OE1 . GLU B 141 ? 1.2119 0.9993 1.0601 -0.1888 -0.1013 0.2622  145 GLU B OE1 
11129 O OE2 . GLU B 141 ? 1.2620 1.0064 1.0999 -0.2210 -0.1285 0.2840  145 GLU B OE2 
11136 N N   . MET B 142 ? 0.9589 0.9600 0.8474 -0.1716 0.0097  0.2050  146 MET B N   
11137 C CA  . MET B 142 ? 0.8869 0.9246 0.7795 -0.1574 0.0286  0.1895  146 MET B CA  
11138 C C   . MET B 142 ? 0.9150 0.9951 0.7864 -0.1828 0.0356  0.2004  146 MET B C   
11139 O O   . MET B 142 ? 0.9266 1.0271 0.7939 -0.1745 0.0446  0.1919  146 MET B O   
11140 C CB  . MET B 142 ? 0.8095 0.8779 0.7268 -0.1374 0.0500  0.1657  146 MET B CB  
11141 C CG  . MET B 142 ? 0.7966 0.8303 0.7343 -0.1102 0.0461  0.1523  146 MET B CG  
11142 S SD  . MET B 142 ? 0.8156 0.8191 0.7556 -0.0851 0.0389  0.1444  146 MET B SD  
11143 C CE  . MET B 142 ? 0.7896 0.8412 0.7321 -0.0767 0.0609  0.1290  146 MET B CE  
11153 N N   . SER B 143 ? 0.9360 1.0316 0.7931 -0.2147 0.0313  0.2188  147 SER B N   
11154 C CA  . SER B 143 ? 1.0190 1.1597 0.8539 -0.2419 0.0377  0.2303  147 SER B CA  
11155 C C   . SER B 143 ? 1.0352 1.1484 0.8461 -0.2502 0.0207  0.2467  147 SER B C   
11156 O O   . SER B 143 ? 1.0740 1.2248 0.8684 -0.2622 0.0290  0.2488  147 SER B O   
11157 C CB  . SER B 143 ? 1.1752 1.3370 0.9990 -0.2776 0.0343  0.2495  147 SER B CB  
11158 O OG  . SER B 143 ? 1.2622 1.4578 1.1083 -0.2710 0.0513  0.2338  147 SER B OG  
11164 N N   . LYS B 144 ? 1.0130 1.0622 0.8219 -0.2434 -0.0038 0.2573  148 LYS B N   
11165 C CA  . LYS B 144 ? 1.0527 1.0718 0.8412 -0.2483 -0.0227 0.2722  148 LYS B CA  
11166 C C   . LYS B 144 ? 1.0222 1.0487 0.8199 -0.2195 -0.0121 0.2523  148 LYS B C   
11167 O O   . LYS B 144 ? 1.0523 1.0716 0.8320 -0.2251 -0.0218 0.2621  148 LYS B O   
11168 C CB  . LYS B 144 ? 1.1419 1.0900 0.9289 -0.2460 -0.0538 0.2866  148 LYS B CB  
11169 C CG  . LYS B 144 ? 1.2234 1.1542 1.0020 -0.2736 -0.0684 0.3063  148 LYS B CG  
11170 C CD  . LYS B 144 ? 1.2537 1.1106 1.0353 -0.2642 -0.0995 0.3139  148 LYS B CD  
11171 C CE  . LYS B 144 ? 1.2690 1.1054 1.0430 -0.2912 -0.1152 0.3320  148 LYS B CE  
11172 N NZ  . LYS B 144 ? 1.2988 1.0617 1.0777 -0.2787 -0.1463 0.3353  148 LYS B NZ  
11186 N N   . LEU B 145 ? 1.0015 1.0420 0.8256 -0.1907 0.0063  0.2258  149 LEU B N   
11187 C CA  . LEU B 145 ? 0.9772 1.0189 0.8123 -0.1628 0.0142  0.2068  149 LEU B CA  
11188 C C   . LEU B 145 ? 0.9781 1.0764 0.8172 -0.1579 0.0399  0.1879  149 LEU B C   
11189 O O   . LEU B 145 ? 0.9684 1.0753 0.8033 -0.1480 0.0436  0.1798  149 LEU B O   
11190 C CB  . LEU B 145 ? 0.9223 0.9318 0.7843 -0.1322 0.0125  0.1907  149 LEU B CB  
11191 C CG  . LEU B 145 ? 0.9954 0.9500 0.8582 -0.1320 -0.0123 0.2033  149 LEU B CG  
11192 C CD1 . LEU B 145 ? 0.9947 0.9305 0.8844 -0.1037 -0.0094 0.1845  149 LEU B CD1 
11193 C CD2 . LEU B 145 ? 1.0491 0.9691 0.8971 -0.1331 -0.0349 0.2170  149 LEU B CD2 
11205 N N   . THR B 146 ? 0.9870 1.1235 0.8348 -0.1636 0.0563  0.1797  150 THR B N   
11206 C CA  . THR B 146 ? 0.9543 1.1460 0.8074 -0.1579 0.0792  0.1597  150 THR B CA  
11207 C C   . THR B 146 ? 0.9708 1.2099 0.8184 -0.1823 0.0895  0.1647  150 THR B C   
11208 O O   . THR B 146 ? 0.9862 1.2143 0.8385 -0.1934 0.0840  0.1751  150 THR B O   
11209 C CB  . THR B 146 ? 0.8776 1.0683 0.7596 -0.1256 0.0911  0.1337  150 THR B CB  
11210 O OG1 . THR B 146 ? 0.8446 1.0864 0.7316 -0.1196 0.1105  0.1136  150 THR B OG1 
11211 C CG2 . THR B 146 ? 0.8430 1.0187 0.7432 -0.1217 0.0902  0.1333  150 THR B CG2 
11219 N N   . SER B 147 ? 0.9531 1.2473 0.7910 -0.1908 0.1042  0.1563  151 SER B N   
11220 C CA  . SER B 147 ? 0.9324 1.2835 0.7661 -0.2137 0.1163  0.1582  151 SER B CA  
11221 C C   . SER B 147 ? 0.8552 1.2410 0.7174 -0.1941 0.1346  0.1323  151 SER B C   
11222 O O   . SER B 147 ? 0.8293 1.2650 0.6935 -0.2102 0.1451  0.1313  151 SER B O   
11223 C CB  . SER B 147 ? 0.9697 1.3709 0.7788 -0.2328 0.1237  0.1599  151 SER B CB  
11224 O OG  . SER B 147 ? 0.9929 1.4106 0.8086 -0.2078 0.1351  0.1342  151 SER B OG  
11230 N N   . ASN B 148 ? 0.8343 1.1959 0.7186 -0.1609 0.1377  0.1120  152 ASN B N   
11231 C CA  . ASN B 148 ? 0.8036 1.1906 0.7156 -0.1399 0.1518  0.0877  152 ASN B CA  
11232 C C   . ASN B 148 ? 0.8075 1.1418 0.7389 -0.1205 0.1434  0.0868  152 ASN B C   
11233 O O   . ASN B 148 ? 0.8540 1.1621 0.7960 -0.0956 0.1423  0.0739  152 ASN B O   
11234 C CB  . ASN B 148 ? 0.7954 1.2118 0.7138 -0.1186 0.1642  0.0608  152 ASN B CB  
11235 C CG  . ASN B 148 ? 0.8274 1.3100 0.7321 -0.1348 0.1764  0.0546  152 ASN B CG  
11236 O OD1 . ASN B 148 ? 0.8638 1.3534 0.7429 -0.1520 0.1729  0.0661  152 ASN B OD1 
11237 N ND2 . ASN B 148 ? 0.8531 1.3873 0.7749 -0.1289 0.1906  0.0353  152 ASN B ND2 
11244 N N   . PHE B 149 ? 0.7961 1.1173 0.7315 -0.1330 0.1372  0.1003  153 PHE B N   
11245 C CA  . PHE B 149 ? 0.7605 1.0388 0.7140 -0.1164 0.1302  0.0982  153 PHE B CA  
11246 C C   . PHE B 149 ? 0.7660 1.0751 0.7401 -0.1133 0.1405  0.0873  153 PHE B C   
11247 O O   . PHE B 149 ? 0.7751 1.1186 0.7451 -0.1357 0.1439  0.0956  153 PHE B O   
11248 C CB  . PHE B 149 ? 0.7673 0.9963 0.7086 -0.1310 0.1108  0.1218  153 PHE B CB  
11249 C CG  . PHE B 149 ? 0.7307 0.9205 0.6896 -0.1154 0.1039  0.1184  153 PHE B CG  
11250 C CD1 . PHE B 149 ? 0.7328 0.8939 0.7041 -0.0882 0.1027  0.1055  153 PHE B CD1 
11251 C CD2 . PHE B 149 ? 0.7292 0.9132 0.6914 -0.1293 0.0983  0.1282  153 PHE B CD2 
11252 C CE1 . PHE B 149 ? 0.7309 0.8609 0.7170 -0.0750 0.0970  0.1018  153 PHE B CE1 
11253 C CE2 . PHE B 149 ? 0.7290 0.8786 0.7061 -0.1150 0.0919  0.1237  153 PHE B CE2 
11254 C CZ  . PHE B 149 ? 0.7158 0.8398 0.7045 -0.0877 0.0917  0.1102  153 PHE B CZ  
11264 N N   . ARG B 150 ? 0.7398 1.0380 0.7359 -0.0869 0.1445  0.0695  154 ARG B N   
11265 C CA  . ARG B 150 ? 0.7131 1.0333 0.7307 -0.0804 0.1517  0.0588  154 ARG B CA  
11266 C C   . ARG B 150 ? 0.7043 0.9778 0.7349 -0.0645 0.1433  0.0580  154 ARG B C   
11267 O O   . ARG B 150 ? 0.6985 0.9355 0.7281 -0.0495 0.1374  0.0558  154 ARG B O   
11268 C CB  . ARG B 150 ? 0.6833 1.0469 0.7162 -0.0625 0.1657  0.0340  154 ARG B CB  
11269 C CG  . ARG B 150 ? 0.7019 1.1196 0.7234 -0.0753 0.1757  0.0296  154 ARG B CG  
11270 C CD  . ARG B 150 ? 0.7258 1.1886 0.7671 -0.0557 0.1881  0.0021  154 ARG B CD  
11271 N NE  . ARG B 150 ? 0.8229 1.2543 0.8759 -0.0266 0.1853  -0.0139 154 ARG B NE  
11272 C CZ  . ARG B 150 ? 0.8852 1.3301 0.9608 -0.0042 0.1892  -0.0354 154 ARG B CZ  
11273 N NH1 . ARG B 150 ? 0.9187 1.4103 1.0100 -0.0048 0.1967  -0.0456 154 ARG B NH1 
11274 N NH2 . ARG B 150 ? 0.8837 1.2952 0.9665 0.0184  0.1842  -0.0462 154 ARG B NH2 
11288 N N   . LEU B 151 ? 0.6702 0.9479 0.7129 -0.0687 0.1429  0.0596  155 LEU B N   
11289 C CA  . LEU B 151 ? 0.6932 0.9306 0.7468 -0.0558 0.1351  0.0588  155 LEU B CA  
11290 C C   . LEU B 151 ? 0.6698 0.9308 0.7446 -0.0484 0.1415  0.0476  155 LEU B C   
11291 O O   . LEU B 151 ? 0.6823 0.9850 0.7616 -0.0611 0.1480  0.0474  155 LEU B O   
11292 C CB  . LEU B 151 ? 0.7346 0.9329 0.7753 -0.0719 0.1201  0.0782  155 LEU B CB  
11293 C CG  . LEU B 151 ? 0.8039 1.0141 0.8440 -0.0943 0.1167  0.0897  155 LEU B CG  
11294 C CD1 . LEU B 151 ? 0.8139 0.9733 0.8415 -0.1050 0.0982  0.1061  155 LEU B CD1 
11295 C CD2 . LEU B 151 ? 0.8807 1.1396 0.9115 -0.1176 0.1241  0.0966  155 LEU B CD2 
11307 N N   . GLY B 152 ? 0.6427 0.8791 0.7306 -0.0283 0.1391  0.0385  156 GLY B N   
11308 C CA  . GLY B 152 ? 0.6180 0.8692 0.7255 -0.0200 0.1422  0.0291  156 GLY B CA  
11309 C C   . GLY B 152 ? 0.6033 0.8139 0.7139 -0.0144 0.1328  0.0330  156 GLY B C   
11310 O O   . GLY B 152 ? 0.6070 0.7803 0.7065 -0.0143 0.1245  0.0402  156 GLY B O   
11314 N N   . PHE B 153 ? 0.6203 0.8414 0.7468 -0.0092 0.1339  0.0267  157 PHE B N   
11315 C CA  . PHE B 153 ? 0.6279 0.8170 0.7568 -0.0063 0.1255  0.0298  157 PHE B CA  
11316 C C   . PHE B 153 ? 0.6087 0.8028 0.7548 0.0112  0.1274  0.0176  157 PHE B C   
11317 O O   . PHE B 153 ? 0.6124 0.8397 0.7721 0.0161  0.1333  0.0088  157 PHE B O   
11318 C CB  . PHE B 153 ? 0.6554 0.8464 0.7815 -0.0264 0.1201  0.0407  157 PHE B CB  
11319 C CG  . PHE B 153 ? 0.6587 0.8156 0.7852 -0.0240 0.1104  0.0426  157 PHE B CG  
11320 C CD1 . PHE B 153 ? 0.6421 0.8072 0.7832 -0.0165 0.1110  0.0353  157 PHE B CD1 
11321 C CD2 . PHE B 153 ? 0.6952 0.8124 0.8075 -0.0285 0.0995  0.0506  157 PHE B CD2 
11322 C CE1 . PHE B 153 ? 0.6994 0.8358 0.8393 -0.0146 0.1023  0.0359  157 PHE B CE1 
11323 C CE2 . PHE B 153 ? 0.6835 0.7718 0.7963 -0.0247 0.0904  0.0493  157 PHE B CE2 
11324 C CZ  . PHE B 153 ? 0.6878 0.7868 0.8136 -0.0184 0.0925  0.0419  157 PHE B CZ  
11334 N N   . GLY B 154 ? 0.5864 0.7484 0.7315 0.0206  0.1213  0.0169  158 GLY B N   
11335 C CA  . GLY B 154 ? 0.6037 0.7658 0.7619 0.0336  0.1204  0.0088  158 GLY B CA  
11336 C C   . GLY B 154 ? 0.6312 0.7628 0.7846 0.0342  0.1128  0.0120  158 GLY B C   
11337 O O   . GLY B 154 ? 0.6406 0.7480 0.7818 0.0302  0.1081  0.0173  158 GLY B O   
11341 N N   . SER B 155 ? 0.6199 0.7538 0.7830 0.0400  0.1107  0.0077  159 SER B N   
11342 C CA  . SER B 155 ? 0.6175 0.7287 0.7764 0.0402  0.1040  0.0087  159 SER B CA  
11343 C C   . SER B 155 ? 0.6029 0.7127 0.7681 0.0523  0.1030  0.0030  159 SER B C   
11344 O O   . SER B 155 ? 0.6289 0.7548 0.8045 0.0589  0.1050  -0.0009 159 SER B O   
11345 C CB  . SER B 155 ? 0.6245 0.7399 0.7854 0.0279  0.0999  0.0125  159 SER B CB  
11346 O OG  . SER B 155 ? 0.6451 0.7893 0.8203 0.0278  0.1028  0.0097  159 SER B OG  
11352 N N   . PHE B 156 ? 0.5571 0.6477 0.7154 0.0549  0.0986  0.0024  160 PHE B N   
11353 C CA  . PHE B 156 ? 0.5395 0.6290 0.7005 0.0626  0.0966  -0.0009 160 PHE B CA  
11354 C C   . PHE B 156 ? 0.5371 0.6157 0.6921 0.0599  0.0916  -0.0021 160 PHE B C   
11355 O O   . PHE B 156 ? 0.5293 0.5940 0.6766 0.0565  0.0890  -0.0024 160 PHE B O   
11356 C CB  . PHE B 156 ? 0.5554 0.6381 0.7123 0.0705  0.0983  -0.0022 160 PHE B CB  
11357 C CG  . PHE B 156 ? 0.5853 0.6524 0.7318 0.0711  0.0973  -0.0028 160 PHE B CG  
11358 C CD1 . PHE B 156 ? 0.6441 0.7060 0.7864 0.0734  0.0943  -0.0059 160 PHE B CD1 
11359 C CD2 . PHE B 156 ? 0.5914 0.6512 0.7326 0.0698  0.0987  -0.0009 160 PHE B CD2 
11360 C CE1 . PHE B 156 ? 0.6782 0.7294 0.8134 0.0764  0.0928  -0.0091 160 PHE B CE1 
11361 C CE2 . PHE B 156 ? 0.6704 0.7154 0.8039 0.0723  0.0957  -0.0023 160 PHE B CE2 
11362 C CZ  . PHE B 156 ? 0.6951 0.7365 0.8267 0.0767  0.0928  -0.0074 160 PHE B CZ  
11372 N N   . VAL B 157 ? 0.6032 0.6877 0.7616 0.0616  0.0888  -0.0034 161 VAL B N   
11373 C CA  . VAL B 157 ? 0.6394 0.7168 0.7905 0.0603  0.0846  -0.0065 161 VAL B CA  
11374 C C   . VAL B 157 ? 0.5824 0.6636 0.7307 0.0649  0.0840  -0.0072 161 VAL B C   
11375 O O   . VAL B 157 ? 0.5701 0.6469 0.7107 0.0679  0.0850  -0.0105 161 VAL B O   
11376 C CB  . VAL B 157 ? 0.6763 0.7588 0.8307 0.0534  0.0802  -0.0063 161 VAL B CB  
11377 C CG1 . VAL B 157 ? 0.6758 0.7546 0.8221 0.0530  0.0758  -0.0110 161 VAL B CG1 
11378 C CG2 . VAL B 157 ? 0.7188 0.7955 0.8728 0.0455  0.0791  -0.0046 161 VAL B CG2 
11388 N N   . GLU B 158 ? 0.5719 0.6624 0.7265 0.0649  0.0815  -0.0038 162 GLU B N   
11389 C CA  . GLU B 158 ? 0.5777 0.6713 0.7274 0.0651  0.0782  -0.0019 162 GLU B CA  
11390 C C   . GLU B 158 ? 0.5783 0.6774 0.7366 0.0654  0.0723  0.0032  162 GLU B C   
11391 O O   . GLU B 158 ? 0.5484 0.6530 0.7167 0.0656  0.0705  0.0031  162 GLU B O   
11392 C CB  . GLU B 158 ? 0.6236 0.7198 0.7640 0.0608  0.0761  -0.0056 162 GLU B CB  
11393 C CG  . GLU B 158 ? 0.7195 0.8240 0.8519 0.0580  0.0736  -0.0033 162 GLU B CG  
11394 C CD  . GLU B 158 ? 0.7788 0.8836 0.9071 0.0608  0.0776  -0.0033 162 GLU B CD  
11395 O OE1 . GLU B 158 ? 0.7875 0.8886 0.9203 0.0624  0.0767  0.0026  162 GLU B OE1 
11396 O OE2 . GLU B 158 ? 0.7883 0.8977 0.9096 0.0622  0.0809  -0.0102 162 GLU B OE2 
11403 N N   . LYS B 159 ? 0.5821 0.6802 0.7366 0.0651  0.0680  0.0078  163 LYS B N   
11404 C CA  . LYS B 159 ? 0.6013 0.7003 0.7620 0.0650  0.0583  0.0135  163 LYS B CA  
11405 C C   . LYS B 159 ? 0.5896 0.6958 0.7501 0.0596  0.0534  0.0145  163 LYS B C   
11406 O O   . LYS B 159 ? 0.6099 0.7198 0.7584 0.0530  0.0534  0.0147  163 LYS B O   
11407 C CB  . LYS B 159 ? 0.6560 0.7502 0.8087 0.0615  0.0521  0.0206  163 LYS B CB  
11408 C CG  . LYS B 159 ? 0.6585 0.7440 0.8127 0.0664  0.0537  0.0207  163 LYS B CG  
11409 C CD  . LYS B 159 ? 0.6698 0.7500 0.8154 0.0597  0.0452  0.0298  163 LYS B CD  
11410 C CE  . LYS B 159 ? 0.6285 0.6985 0.7753 0.0636  0.0450  0.0299  163 LYS B CE  
11411 N NZ  . LYS B 159 ? 0.6152 0.6758 0.7755 0.0745  0.0404  0.0256  163 LYS B NZ  
11425 N N   . PRO B 160 ? 0.5765 0.6877 0.7500 0.0623  0.0490  0.0140  164 PRO B N   
11426 C CA  . PRO B 160 ? 0.5688 0.6879 0.7425 0.0566  0.0442  0.0146  164 PRO B CA  
11427 C C   . PRO B 160 ? 0.5952 0.7142 0.7645 0.0521  0.0321  0.0225  164 PRO B C   
11428 O O   . PRO B 160 ? 0.6479 0.7710 0.8274 0.0535  0.0226  0.0253  164 PRO B O   
11429 C CB  . PRO B 160 ? 0.5416 0.6701 0.7331 0.0612  0.0446  0.0111  164 PRO B CB  
11430 C CG  . PRO B 160 ? 0.5500 0.6761 0.7516 0.0709  0.0431  0.0105  164 PRO B CG  
11431 C CD  . PRO B 160 ? 0.5864 0.7000 0.7758 0.0711  0.0485  0.0114  164 PRO B CD  
11439 N N   . VAL B 161 ? 0.5604 0.6766 0.7140 0.0459  0.0317  0.0267  165 VAL B N   
11440 C CA  . VAL B 161 ? 0.5871 0.7039 0.7320 0.0379  0.0198  0.0365  165 VAL B CA  
11441 C C   . VAL B 161 ? 0.5953 0.7221 0.7211 0.0277  0.0242  0.0358  165 VAL B C   
11442 O O   . VAL B 161 ? 0.6079 0.7380 0.7281 0.0291  0.0354  0.0277  165 VAL B O   
11443 C CB  . VAL B 161 ? 0.6156 0.7203 0.7611 0.0390  0.0108  0.0453  165 VAL B CB  
11444 C CG1 . VAL B 161 ? 0.6155 0.7122 0.7807 0.0508  0.0032  0.0439  165 VAL B CG1 
11445 C CG2 . VAL B 161 ? 0.6385 0.7400 0.7773 0.0395  0.0204  0.0431  165 VAL B CG2 
11455 N N   . SER B 162 ? 0.5810 0.7141 0.6969 0.0176  0.0144  0.0438  166 SER B N   
11456 C CA  . SER B 162 ? 0.5798 0.7280 0.6763 0.0067  0.0178  0.0432  166 SER B CA  
11457 C C   . SER B 162 ? 0.6164 0.7665 0.7040 0.0024  0.0205  0.0482  166 SER B C   
11458 O O   . SER B 162 ? 0.6139 0.7509 0.7062 0.0027  0.0129  0.0580  166 SER B O   
11459 C CB  . SER B 162 ? 0.5742 0.7304 0.6608 -0.0050 0.0055  0.0523  166 SER B CB  
11460 O OG  . SER B 162 ? 0.6469 0.8233 0.7150 -0.0147 0.0105  0.0476  166 SER B OG  
11466 N N   . PRO B 163 ? 0.6419 0.8095 0.7174 -0.0015 0.0304  0.0408  167 PRO B N   
11467 C CA  . PRO B 163 ? 0.6527 0.8360 0.7209 -0.0012 0.0381  0.0268  167 PRO B CA  
11468 C C   . PRO B 163 ? 0.6300 0.8056 0.7072 0.0122  0.0487  0.0117  167 PRO B C   
11469 O O   . PRO B 163 ? 0.5959 0.7823 0.6666 0.0143  0.0546  -0.0017 167 PRO B O   
11470 C CB  . PRO B 163 ? 0.6737 0.8826 0.7247 -0.0121 0.0413  0.0274  167 PRO B CB  
11471 C CG  . PRO B 163 ? 0.6582 0.8610 0.7130 -0.0116 0.0428  0.0348  167 PRO B CG  
11472 C CD  . PRO B 163 ? 0.6311 0.8061 0.6988 -0.0074 0.0330  0.0459  167 PRO B CD  
11480 N N   . PHE B 164 ? 0.6300 0.7871 0.7214 0.0210  0.0499  0.0135  168 PHE B N   
11481 C CA  . PHE B 164 ? 0.6368 0.7851 0.7353 0.0315  0.0584  0.0021  168 PHE B CA  
11482 C C   . PHE B 164 ? 0.6000 0.7405 0.7046 0.0342  0.0572  -0.0042 168 PHE B C   
11483 O O   . PHE B 164 ? 0.5906 0.7229 0.6979 0.0403  0.0620  -0.0134 168 PHE B O   
11484 C CB  . PHE B 164 ? 0.6787 0.8137 0.7878 0.0380  0.0605  0.0068  168 PHE B CB  
11485 C CG  . PHE B 164 ? 0.6656 0.8055 0.7694 0.0343  0.0602  0.0137  168 PHE B CG  
11486 C CD1 . PHE B 164 ? 0.6778 0.8354 0.7704 0.0300  0.0648  0.0096  168 PHE B CD1 
11487 C CD2 . PHE B 164 ? 0.6592 0.7875 0.7695 0.0348  0.0545  0.0236  168 PHE B CD2 
11488 C CE1 . PHE B 164 ? 0.7074 0.8725 0.7951 0.0240  0.0643  0.0171  168 PHE B CE1 
11489 C CE2 . PHE B 164 ? 0.6851 0.8155 0.7896 0.0294  0.0524  0.0310  168 PHE B CE2 
11490 C CZ  . PHE B 164 ? 0.7075 0.8570 0.8005 0.0228  0.0575  0.0288  168 PHE B CZ  
11500 N N   . VAL B 165 ? 0.5979 0.7401 0.7047 0.0290  0.0495  0.0014  169 VAL B N   
11501 C CA  . VAL B 165 ? 0.6145 0.7525 0.7269 0.0290  0.0472  -0.0034 169 VAL B CA  
11502 C C   . VAL B 165 ? 0.6281 0.7770 0.7319 0.0204  0.0396  -0.0020 169 VAL B C   
11503 O O   . VAL B 165 ? 0.6527 0.8103 0.7498 0.0142  0.0341  0.0068  169 VAL B O   
11504 C CB  . VAL B 165 ? 0.6036 0.7344 0.7336 0.0328  0.0453  0.0020  169 VAL B CB  
11505 C CG1 . VAL B 165 ? 0.6005 0.7223 0.7371 0.0402  0.0530  -0.0001 169 VAL B CG1 
11506 C CG2 . VAL B 165 ? 0.6165 0.7508 0.7526 0.0316  0.0366  0.0130  169 VAL B CG2 
11516 N N   . LYS B 166 ? 0.6187 0.7662 0.7218 0.0187  0.0380  -0.0099 170 LYS B N   
11517 C CA  . LYS B 166 ? 0.6371 0.7937 0.7349 0.0105  0.0294  -0.0078 170 LYS B CA  
11518 C C   . LYS B 166 ? 0.6485 0.8048 0.7610 0.0096  0.0217  0.0041  170 LYS B C   
11519 O O   . LYS B 166 ? 0.6511 0.8010 0.7795 0.0151  0.0236  0.0053  170 LYS B O   
11520 C CB  . LYS B 166 ? 0.6870 0.8394 0.7815 0.0088  0.0283  -0.0198 170 LYS B CB  
11521 C CG  . LYS B 166 ? 0.7234 0.8783 0.8025 0.0108  0.0322  -0.0348 170 LYS B CG  
11522 C CD  . LYS B 166 ? 0.7758 0.9521 0.8385 0.0042  0.0305  -0.0351 170 LYS B CD  
11523 C CE  . LYS B 166 ? 0.8725 1.0570 0.9212 0.0074  0.0341  -0.0541 170 LYS B CE  
11524 N NZ  . LYS B 166 ? 0.9739 1.1469 1.0209 0.0078  0.0285  -0.0669 170 LYS B NZ  
11538 N N   . THR B 167 ? 0.6709 0.8359 0.7777 0.0026  0.0122  0.0127  171 THR B N   
11539 C CA  . THR B 167 ? 0.6767 0.8412 0.7978 0.0037  0.0020  0.0239  171 THR B CA  
11540 C C   . THR B 167 ? 0.7251 0.8978 0.8476 -0.0028 -0.0084 0.0257  171 THR B C   
11541 O O   . THR B 167 ? 0.7142 0.8890 0.8447 -0.0032 -0.0203 0.0356  171 THR B O   
11542 C CB  . THR B 167 ? 0.6369 0.7996 0.7524 0.0017  -0.0045 0.0359  171 THR B CB  
11543 O OG1 . THR B 167 ? 0.6967 0.8696 0.7897 -0.0091 -0.0049 0.0373  171 THR B OG1 
11544 C CG2 . THR B 167 ? 0.5949 0.7477 0.7168 0.0101  0.0031  0.0356  171 THR B CG2 
11552 N N   . THR B 168 ? 0.7431 0.9191 0.8583 -0.0074 -0.0058 0.0159  172 THR B N   
11553 C CA  . THR B 168 ? 0.7200 0.9034 0.8397 -0.0133 -0.0154 0.0168  172 THR B CA  
11554 C C   . THR B 168 ? 0.6996 0.8828 0.8431 -0.0080 -0.0151 0.0164  172 THR B C   
11555 O O   . THR B 168 ? 0.6768 0.8533 0.8281 -0.0021 -0.0055 0.0118  172 THR B O   
11556 C CB  . THR B 168 ? 0.7621 0.9478 0.8654 -0.0204 -0.0142 0.0054  172 THR B CB  
11557 O OG1 . THR B 168 ? 0.7729 0.9476 0.8801 -0.0162 -0.0056 -0.0056 172 THR B OG1 
11558 C CG2 . THR B 168 ? 0.7764 0.9692 0.8562 -0.0250 -0.0121 0.0026  172 THR B CG2 
11566 N N   . PRO B 169 ? 0.7354 0.9290 0.8912 -0.0105 -0.0257 0.0211  173 PRO B N   
11567 C CA  . PRO B 169 ? 0.6958 0.8969 0.8758 -0.0064 -0.0247 0.0199  173 PRO B CA  
11568 C C   . PRO B 169 ? 0.6644 0.8608 0.8437 -0.0101 -0.0153 0.0112  173 PRO B C   
11569 O O   . PRO B 169 ? 0.6350 0.8329 0.8281 -0.0055 -0.0081 0.0100  173 PRO B O   
11570 C CB  . PRO B 169 ? 0.6788 0.8947 0.8676 -0.0114 -0.0386 0.0244  173 PRO B CB  
11571 C CG  . PRO B 169 ? 0.7010 0.9139 0.8746 -0.0142 -0.0486 0.0323  173 PRO B CG  
11572 C CD  . PRO B 169 ? 0.7397 0.9416 0.8884 -0.0178 -0.0395 0.0280  173 PRO B CD  
11580 N N   . GLU B 170 ? 0.6999 0.8898 0.8623 -0.0188 -0.0163 0.0047  174 GLU B N   
11581 C CA  . GLU B 170 ? 0.7579 0.9377 0.9184 -0.0232 -0.0112 -0.0030 174 GLU B CA  
11582 C C   . GLU B 170 ? 0.7625 0.9277 0.9191 -0.0158 -0.0001 -0.0063 174 GLU B C   
11583 O O   . GLU B 170 ? 0.8032 0.9639 0.9681 -0.0165 0.0047  -0.0069 174 GLU B O   
11584 C CB  . GLU B 170 ? 0.8337 1.0057 0.9754 -0.0317 -0.0167 -0.0115 174 GLU B CB  
11585 C CG  . GLU B 170 ? 0.9717 1.1572 1.1159 -0.0409 -0.0285 -0.0088 174 GLU B CG  
11586 C CD  . GLU B 170 ? 1.1034 1.2998 1.2401 -0.0402 -0.0349 -0.0031 174 GLU B CD  
11587 O OE1 . GLU B 170 ? 1.1440 1.3384 1.2756 -0.0333 -0.0303 0.0004  174 GLU B OE1 
11588 O OE2 . GLU B 170 ? 1.1660 1.3727 1.3012 -0.0480 -0.0455 -0.0011 174 GLU B OE2 
11595 N N   . GLU B 171 ? 0.7391 0.8987 0.8826 -0.0101 0.0036  -0.0078 175 GLU B N   
11596 C CA  . GLU B 171 ? 0.7229 0.8699 0.8625 -0.0029 0.0134  -0.0114 175 GLU B CA  
11597 C C   . GLU B 171 ? 0.6568 0.8077 0.8127 0.0043  0.0186  -0.0042 175 GLU B C   
11598 O O   . GLU B 171 ? 0.6381 0.7801 0.7960 0.0081  0.0260  -0.0063 175 GLU B O   
11599 C CB  . GLU B 171 ? 0.7678 0.9135 0.8896 0.0001  0.0158  -0.0155 175 GLU B CB  
11600 C CG  . GLU B 171 ? 0.8109 0.9543 0.9152 -0.0045 0.0124  -0.0272 175 GLU B CG  
11601 C CD  . GLU B 171 ? 0.9134 1.0401 1.0114 0.0003  0.0169  -0.0397 175 GLU B CD  
11602 O OE1 . GLU B 171 ? 0.9582 1.0748 1.0644 0.0056  0.0226  -0.0373 175 GLU B OE1 
11603 O OE2 . GLU B 171 ? 0.9733 1.0965 1.0577 -0.0007 0.0135  -0.0525 175 GLU B OE2 
11610 N N   . ILE B 172 ? 0.6541 0.8176 0.8214 0.0068  0.0135  0.0034  176 ILE B N   
11611 C CA  . ILE B 172 ? 0.6592 0.8278 0.8436 0.0152  0.0169  0.0074  176 ILE B CA  
11612 C C   . ILE B 172 ? 0.6908 0.8680 0.8900 0.0127  0.0205  0.0055  176 ILE B C   
11613 O O   . ILE B 172 ? 0.7043 0.8800 0.9088 0.0167  0.0286  0.0045  176 ILE B O   
11614 C CB  . ILE B 172 ? 0.6799 0.8579 0.8741 0.0196  0.0071  0.0144  176 ILE B CB  
11615 C CG1 . ILE B 172 ? 0.7688 0.9375 0.9466 0.0197  0.0037  0.0190  176 ILE B CG1 
11616 C CG2 . ILE B 172 ? 0.6115 0.7973 0.8266 0.0301  0.0088  0.0149  176 ILE B CG2 
11617 C CD1 . ILE B 172 ? 0.8312 1.0037 1.0149 0.0215  -0.0101 0.0281  176 ILE B CD1 
11629 N N   . ALA B 173 ? 0.7169 0.9055 0.9222 0.0044  0.0142  0.0057  177 ALA B N   
11630 C CA  . ALA B 173 ? 0.6946 0.8965 0.9139 -0.0015 0.0169  0.0054  177 ALA B CA  
11631 C C   . ALA B 173 ? 0.6715 0.8557 0.8789 -0.0082 0.0229  0.0026  177 ALA B C   
11632 O O   . ALA B 173 ? 0.6414 0.8320 0.8568 -0.0106 0.0288  0.0040  177 ALA B O   
11633 C CB  . ALA B 173 ? 0.6646 0.8826 0.8918 -0.0108 0.0076  0.0066  177 ALA B CB  
11639 N N   . ASN B 174 ? 0.6855 0.8483 0.8736 -0.0112 0.0205  -0.0018 178 ASN B N   
11640 C CA  . ASN B 174 ? 0.7386 0.8798 0.9149 -0.0162 0.0225  -0.0056 178 ASN B CA  
11641 C C   . ASN B 174 ? 0.7284 0.8501 0.8863 -0.0095 0.0230  -0.0129 178 ASN B C   
11642 O O   . ASN B 174 ? 0.7394 0.8547 0.8856 -0.0128 0.0166  -0.0191 178 ASN B O   
11643 C CB  . ASN B 174 ? 0.7943 0.9324 0.9695 -0.0310 0.0145  -0.0059 178 ASN B CB  
11644 C CG  . ASN B 174 ? 0.8384 0.9484 1.0007 -0.0363 0.0127  -0.0093 178 ASN B CG  
11645 O OD1 . ASN B 174 ? 0.8599 0.9557 1.0163 -0.0285 0.0183  -0.0110 178 ASN B OD1 
11646 N ND2 . ASN B 174 ? 0.8856 0.9859 1.0435 -0.0498 0.0030  -0.0102 178 ASN B ND2 
11653 N N   . PRO B 175 ? 0.6960 0.8110 0.8510 0.0001  0.0306  -0.0135 179 PRO B N   
11654 C CA  . PRO B 175 ? 0.7038 0.8080 0.8434 0.0069  0.0319  -0.0210 179 PRO B CA  
11655 C C   . PRO B 175 ? 0.7347 0.8184 0.8612 0.0049  0.0274  -0.0315 179 PRO B C   
11656 O O   . PRO B 175 ? 0.7134 0.7923 0.8279 0.0113  0.0280  -0.0409 179 PRO B O   
11657 C CB  . PRO B 175 ? 0.6706 0.7732 0.8130 0.0160  0.0406  -0.0182 179 PRO B CB  
11658 C CG  . PRO B 175 ? 0.6565 0.7613 0.8114 0.0132  0.0435  -0.0122 179 PRO B CG  
11659 C CD  . PRO B 175 ? 0.6593 0.7800 0.8252 0.0050  0.0383  -0.0081 179 PRO B CD  
11667 N N   . CYS B 176 ? 0.7705 0.8428 0.8994 -0.0040 0.0219  -0.0305 180 CYS B N   
11668 C CA  . CYS B 176 ? 0.8320 0.8798 0.9489 -0.0065 0.0135  -0.0406 180 CYS B CA  
11669 C C   . CYS B 176 ? 0.8826 0.9302 0.9968 -0.0175 0.0030  -0.0432 180 CYS B C   
11670 O O   . CYS B 176 ? 0.9564 0.9808 1.0618 -0.0218 -0.0068 -0.0509 180 CYS B O   
11671 C CB  . CYS B 176 ? 0.8246 0.8517 0.9427 -0.0100 0.0119  -0.0367 180 CYS B CB  
11672 S SG  . CYS B 176 ? 0.8246 0.8491 0.9442 0.0023  0.0226  -0.0344 180 CYS B SG  
11677 N N   . SER B 177 ? 0.8569 0.9283 0.9785 -0.0220 0.0032  -0.0371 181 SER B N   
11678 C CA  . SER B 177 ? 0.8789 0.9528 0.9990 -0.0334 -0.0071 -0.0388 181 SER B CA  
11679 C C   . SER B 177 ? 0.8679 0.9264 0.9700 -0.0312 -0.0147 -0.0544 181 SER B C   
11680 O O   . SER B 177 ? 0.8692 0.9184 0.9667 -0.0410 -0.0257 -0.0587 181 SER B O   
11681 C CB  . SER B 177 ? 0.8903 0.9933 1.0206 -0.0353 -0.0064 -0.0309 181 SER B CB  
11682 O OG  . SER B 177 ? 0.9348 1.0471 1.0583 -0.0257 -0.0021 -0.0331 181 SER B OG  
11688 N N   . SER B 178 ? 0.8645 0.9221 0.9564 -0.0188 -0.0095 -0.0640 182 SER B N   
11689 C CA  . SER B 178 ? 0.9160 0.9662 0.9913 -0.0145 -0.0154 -0.0819 182 SER B CA  
11690 C C   . SER B 178 ? 0.9600 0.9771 1.0284 -0.0116 -0.0240 -0.0946 182 SER B C   
11691 O O   . SER B 178 ? 0.9785 0.9867 1.0342 -0.0079 -0.0318 -0.1123 182 SER B O   
11692 C CB  . SER B 178 ? 0.8993 0.9672 0.9673 -0.0031 -0.0061 -0.0878 182 SER B CB  
11693 O OG  . SER B 178 ? 0.9009 0.9608 0.9729 0.0068  0.0016  -0.0873 182 SER B OG  
11699 N N   . ILE B 179 ? 1.0065 1.0048 1.0824 -0.0131 -0.0242 -0.0866 183 ILE B N   
11700 C CA  . ILE B 179 ? 1.0709 1.0338 1.1399 -0.0089 -0.0342 -0.0971 183 ILE B CA  
11701 C C   . ILE B 179 ? 1.0898 1.0291 1.1535 -0.0219 -0.0513 -0.1006 183 ILE B C   
11702 O O   . ILE B 179 ? 1.1081 1.0272 1.1601 -0.0157 -0.0626 -0.1196 183 ILE B O   
11703 C CB  . ILE B 179 ? 1.1009 1.0517 1.1778 -0.0081 -0.0297 -0.0851 183 ILE B CB  
11704 C CG1 . ILE B 179 ? 1.0666 1.0390 1.1478 0.0049  -0.0141 -0.0832 183 ILE B CG1 
11705 C CG2 . ILE B 179 ? 1.1674 1.0777 1.2369 -0.0048 -0.0435 -0.0941 183 ILE B CG2 
11706 C CD1 . ILE B 179 ? 1.0849 1.0608 1.1568 0.0211  -0.0122 -0.1020 183 ILE B CD1 
11718 N N   . PRO B 180 ? 1.1069 1.0487 1.1789 -0.0399 -0.0547 -0.0843 184 PRO B N   
11719 C CA  . PRO B 180 ? 1.0533 1.0193 1.1407 -0.0482 -0.0440 -0.0640 184 PRO B CA  
11720 C C   . PRO B 180 ? 1.0036 0.9532 1.0954 -0.0524 -0.0435 -0.0530 184 PRO B C   
11721 O O   . PRO B 180 ? 1.0316 0.9461 1.1152 -0.0562 -0.0563 -0.0564 184 PRO B O   
11722 C CB  . PRO B 180 ? 1.0874 1.0650 1.1799 -0.0662 -0.0515 -0.0567 184 PRO B CB  
11723 C CG  . PRO B 180 ? 1.1595 1.1014 1.2392 -0.0733 -0.0698 -0.0670 184 PRO B CG  
11724 C CD  . PRO B 180 ? 1.1859 1.1091 1.2520 -0.0542 -0.0717 -0.0878 184 PRO B CD  
11732 N N   . TYR B 181 ? 0.9332 0.9076 1.0372 -0.0517 -0.0298 -0.0402 185 TYR B N   
11733 C CA  . TYR B 181 ? 0.9152 0.8818 1.0233 -0.0561 -0.0268 -0.0289 185 TYR B CA  
11734 C C   . TYR B 181 ? 0.8424 0.8472 0.9665 -0.0581 -0.0128 -0.0165 185 TYR B C   
11735 O O   . TYR B 181 ? 0.8208 0.8502 0.9511 -0.0492 -0.0048 -0.0187 185 TYR B O   
11736 C CB  . TYR B 181 ? 0.9238 0.8693 1.0243 -0.0399 -0.0247 -0.0367 185 TYR B CB  
11737 C CG  . TYR B 181 ? 0.9303 0.8556 1.0295 -0.0464 -0.0280 -0.0267 185 TYR B CG  
11738 C CD1 . TYR B 181 ? 0.9079 0.8534 1.0156 -0.0463 -0.0150 -0.0150 185 TYR B CD1 
11739 C CD2 . TYR B 181 ? 0.9619 0.8465 1.0501 -0.0526 -0.0456 -0.0291 185 TYR B CD2 
11740 C CE1 . TYR B 181 ? 0.9439 0.8729 1.0484 -0.0536 -0.0182 -0.0051 185 TYR B CE1 
11741 C CE2 . TYR B 181 ? 0.9802 0.8448 1.0654 -0.0602 -0.0506 -0.0178 185 TYR B CE2 
11742 C CZ  . TYR B 181 ? 0.9885 0.8771 1.0814 -0.0613 -0.0362 -0.0054 185 TYR B CZ  
11743 O OH  . TYR B 181 ? 1.0381 0.9088 1.1261 -0.0704 -0.0412 0.0065  185 TYR B OH  
11753 N N   . PHE B 182 ? 0.8423 0.8524 0.9726 -0.0700 -0.0109 -0.0037 186 PHE B N   
11754 C CA  . PHE B 182 ? 0.8321 0.8811 0.9789 -0.0713 0.0016  0.0055  186 PHE B CA  
11755 C C   . PHE B 182 ? 0.8295 0.8813 0.9773 -0.0557 0.0135  0.0049  186 PHE B C   
11756 O O   . PHE B 182 ? 0.8724 0.9085 1.0146 -0.0574 0.0139  0.0090  186 PHE B O   
11757 C CB  . PHE B 182 ? 0.8204 0.8828 0.9737 -0.0925 -0.0006 0.0186  186 PHE B CB  
11758 C CG  . PHE B 182 ? 0.7856 0.8935 0.9577 -0.0921 0.0120  0.0245  186 PHE B CG  
11759 C CD1 . PHE B 182 ? 0.7658 0.9050 0.9522 -0.0903 0.0137  0.0227  186 PHE B CD1 
11760 C CD2 . PHE B 182 ? 0.7622 0.8819 0.9376 -0.0920 0.0214  0.0306  186 PHE B CD2 
11761 C CE1 . PHE B 182 ? 0.7213 0.9023 0.9269 -0.0869 0.0236  0.0254  186 PHE B CE1 
11762 C CE2 . PHE B 182 ? 0.7130 0.8762 0.9063 -0.0893 0.0325  0.0328  186 PHE B CE2 
11763 C CZ  . PHE B 182 ? 0.7032 0.8968 0.9124 -0.0858 0.0333  0.0295  186 PHE B CZ  
11773 N N   . CYS B 183 ? 0.7819 0.8528 0.9364 -0.0415 0.0218  0.0006  187 CYS B N   
11774 C CA  . CYS B 183 ? 0.7584 0.8355 0.9156 -0.0276 0.0327  0.0004  187 CYS B CA  
11775 C C   . CYS B 183 ? 0.7560 0.8679 0.9301 -0.0239 0.0401  0.0041  187 CYS B C   
11776 O O   . CYS B 183 ? 0.8069 0.9348 0.9884 -0.0256 0.0366  0.0035  187 CYS B O   
11777 C CB  . CYS B 183 ? 0.7483 0.8106 0.8953 -0.0129 0.0333  -0.0093 187 CYS B CB  
11778 S SG  . CYS B 183 ? 0.7997 0.8229 0.9292 -0.0110 0.0240  -0.0183 187 CYS B SG  
11783 N N   . LEU B 184 ? 0.6972 0.8204 0.8777 -0.0183 0.0490  0.0071  188 LEU B N   
11784 C CA  . LEU B 184 ? 0.6503 0.8039 0.8475 -0.0111 0.0545  0.0076  188 LEU B CA  
11785 C C   . LEU B 184 ? 0.6191 0.7678 0.8144 0.0036  0.0549  0.0033  188 LEU B C   
11786 O O   . LEU B 184 ? 0.6692 0.7965 0.8512 0.0092  0.0553  0.0002  188 LEU B O   
11787 C CB  . LEU B 184 ? 0.6372 0.8060 0.8414 -0.0100 0.0631  0.0105  188 LEU B CB  
11788 C CG  . LEU B 184 ? 0.6740 0.8553 0.8803 -0.0276 0.0633  0.0169  188 LEU B CG  
11789 C CD1 . LEU B 184 ? 0.7283 0.9282 0.9395 -0.0260 0.0728  0.0186  188 LEU B CD1 
11790 C CD2 . LEU B 184 ? 0.6425 0.8520 0.8626 -0.0374 0.0594  0.0184  188 LEU B CD2 
11802 N N   . PRO B 185 ? 0.6089 0.7781 0.8175 0.0095  0.0536  0.0033  189 PRO B N   
11803 C CA  . PRO B 185 ? 0.6134 0.7768 0.8189 0.0207  0.0517  0.0019  189 PRO B CA  
11804 C C   . PRO B 185 ? 0.6269 0.7783 0.8263 0.0297  0.0583  0.0010  189 PRO B C   
11805 O O   . PRO B 185 ? 0.6356 0.7920 0.8400 0.0313  0.0646  0.0012  189 PRO B O   
11806 C CB  . PRO B 185 ? 0.6170 0.8043 0.8411 0.0259  0.0477  0.0029  189 PRO B CB  
11807 C CG  . PRO B 185 ? 0.6186 0.8297 0.8576 0.0200  0.0510  0.0029  189 PRO B CG  
11808 C CD  . PRO B 185 ? 0.6470 0.8464 0.8743 0.0056  0.0519  0.0048  189 PRO B CD  
11816 N N   . THR B 186 ? 0.6586 0.7967 0.8464 0.0343  0.0568  0.0000  190 THR B N   
11817 C CA  . THR B 186 ? 0.6715 0.7987 0.8527 0.0415  0.0622  -0.0007 190 THR B CA  
11818 C C   . THR B 186 ? 0.6696 0.8066 0.8634 0.0495  0.0645  0.0008  190 THR B C   
11819 O O   . THR B 186 ? 0.6859 0.8352 0.8916 0.0530  0.0594  0.0019  190 THR B O   
11820 C CB  . THR B 186 ? 0.6350 0.7545 0.8037 0.0434  0.0595  -0.0014 190 THR B CB  
11821 O OG1 . THR B 186 ? 0.6177 0.7325 0.7761 0.0372  0.0563  -0.0055 190 THR B OG1 
11822 C CG2 . THR B 186 ? 0.6319 0.7415 0.7929 0.0488  0.0653  -0.0028 190 THR B CG2 
11830 N N   . PHE B 187 ? 0.6679 0.7988 0.8590 0.0534  0.0711  -0.0002 191 PHE B N   
11831 C CA  . PHE B 187 ? 0.6349 0.7739 0.8362 0.0616  0.0735  -0.0011 191 PHE B CA  
11832 C C   . PHE B 187 ? 0.6298 0.7546 0.8216 0.0663  0.0776  -0.0013 191 PHE B C   
11833 O O   . PHE B 187 ? 0.6229 0.7358 0.8029 0.0630  0.0807  -0.0014 191 PHE B O   
11834 C CB  . PHE B 187 ? 0.5903 0.7474 0.8023 0.0590  0.0786  -0.0029 191 PHE B CB  
11835 C CG  . PHE B 187 ? 0.6032 0.7523 0.8049 0.0508  0.0842  -0.0013 191 PHE B CG  
11836 C CD1 . PHE B 187 ? 0.5877 0.7328 0.7843 0.0394  0.0818  0.0010  191 PHE B CD1 
11837 C CD2 . PHE B 187 ? 0.6399 0.7836 0.8366 0.0539  0.0900  -0.0017 191 PHE B CD2 
11838 C CE1 . PHE B 187 ? 0.6188 0.7519 0.8054 0.0313  0.0836  0.0036  191 PHE B CE1 
11839 C CE2 . PHE B 187 ? 0.6557 0.7898 0.8423 0.0459  0.0928  0.0011  191 PHE B CE2 
11840 C CZ  . PHE B 187 ? 0.6645 0.7921 0.8461 0.0346  0.0889  0.0041  191 PHE B CZ  
11850 N N   . GLY B 188 ? 0.6243 0.7500 0.8219 0.0746  0.0761  -0.0021 192 GLY B N   
11851 C CA  . GLY B 188 ? 0.6020 0.7155 0.7915 0.0785  0.0788  -0.0019 192 GLY B CA  
11852 C C   . GLY B 188 ? 0.5640 0.6786 0.7519 0.0789  0.0869  -0.0043 192 GLY B C   
11853 O O   . GLY B 188 ? 0.5350 0.6392 0.7120 0.0757  0.0905  -0.0033 192 GLY B O   
11857 N N   . PHE B 189 ? 0.5347 0.7189 0.6984 0.0330  -0.0104 0.0186  193 PHE B N   
11858 C CA  . PHE B 189 ? 0.5383 0.7230 0.6969 0.0305  0.0006  0.0166  193 PHE B CA  
11859 C C   . PHE B 189 ? 0.5993 0.8181 0.7796 0.0332  0.0084  0.0195  193 PHE B C   
11860 O O   . PHE B 189 ? 0.5688 0.8030 0.7629 0.0477  0.0105  0.0193  193 PHE B O   
11861 C CB  . PHE B 189 ? 0.5525 0.7148 0.6940 0.0401  0.0059  0.0107  193 PHE B CB  
11862 C CG  . PHE B 189 ? 0.5673 0.7332 0.7026 0.0406  0.0172  0.0084  193 PHE B CG  
11863 C CD1 . PHE B 189 ? 0.5629 0.7283 0.6913 0.0284  0.0198  0.0112  193 PHE B CD1 
11864 C CD2 . PHE B 189 ? 0.6030 0.7694 0.7360 0.0539  0.0252  0.0034  193 PHE B CD2 
11865 C CE1 . PHE B 189 ? 0.5949 0.7629 0.7146 0.0286  0.0300  0.0103  193 PHE B CE1 
11866 C CE2 . PHE B 189 ? 0.6013 0.7700 0.7244 0.0543  0.0360  0.0009  193 PHE B CE2 
11867 C CZ  . PHE B 189 ? 0.6110 0.7821 0.7279 0.0413  0.0382  0.0050  193 PHE B CZ  
11877 N N   . LYS B 190 ? 0.6590 0.8891 0.8417 0.0200  0.0133  0.0229  194 LYS B N   
11878 C CA  . LYS B 190 ? 0.6680 0.9344 0.8716 0.0193  0.0229  0.0271  194 LYS B CA  
11879 C C   . LYS B 190 ? 0.6757 0.9349 0.8640 0.0196  0.0364  0.0253  194 LYS B C   
11880 O O   . LYS B 190 ? 0.6750 0.9171 0.8471 0.0064  0.0366  0.0272  194 LYS B O   
11881 C CB  . LYS B 190 ? 0.6705 0.9584 0.8898 -0.0004 0.0170  0.0345  194 LYS B CB  
11882 C CG  . LYS B 190 ? 0.6959 1.0054 0.9363 -0.0002 0.0044  0.0377  194 LYS B CG  
11883 C CD  . LYS B 190 ? 0.7209 1.0470 0.9722 -0.0242 -0.0035 0.0441  194 LYS B CD  
11884 C CE  . LYS B 190 ? 0.8009 1.1521 1.0728 -0.0251 -0.0180 0.0476  194 LYS B CE  
11885 N NZ  . LYS B 190 ? 0.8447 1.2065 1.1223 -0.0517 -0.0286 0.0524  194 LYS B NZ  
11899 N N   . HIS B 191 ? 0.6819 0.9515 0.8724 0.0358  0.0476  0.0216  195 HIS B N   
11900 C CA  . HIS B 191 ? 0.6370 0.9071 0.8140 0.0364  0.0618  0.0204  195 HIS B CA  
11901 C C   . HIS B 191 ? 0.6051 0.9170 0.8052 0.0282  0.0715  0.0288  195 HIS B C   
11902 O O   . HIS B 191 ? 0.6125 0.9595 0.8386 0.0388  0.0767  0.0306  195 HIS B O   
11903 C CB  . HIS B 191 ? 0.6101 0.8691 0.7743 0.0571  0.0698  0.0113  195 HIS B CB  
11904 C CG  . HIS B 191 ? 0.6217 0.8841 0.7702 0.0594  0.0853  0.0095  195 HIS B CG  
11905 N ND1 . HIS B 191 ? 0.6235 0.8794 0.7566 0.0438  0.0880  0.0141  195 HIS B ND1 
11906 C CD2 . HIS B 191 ? 0.6532 0.9225 0.7958 0.0763  0.0992  0.0036  195 HIS B CD2 
11907 C CE1 . HIS B 191 ? 0.6668 0.9273 0.7850 0.0499  0.1026  0.0118  195 HIS B CE1 
11908 N NE2 . HIS B 191 ? 0.6683 0.9369 0.7914 0.0697  0.1101  0.0046  195 HIS B NE2 
11916 N N   . ILE B 192 ? 0.6150 0.9242 0.8064 0.0095  0.0742  0.0350  196 ILE B N   
11917 C CA  . ILE B 192 ? 0.6269 0.9733 0.8404 -0.0058 0.0806  0.0453  196 ILE B CA  
11918 C C   . ILE B 192 ? 0.5782 0.9386 0.7833 -0.0048 0.0996  0.0481  196 ILE B C   
11919 O O   . ILE B 192 ? 0.5453 0.9496 0.7747 -0.0024 0.1119  0.0531  196 ILE B O   
11920 C CB  . ILE B 192 ? 0.6990 1.0293 0.9078 -0.0308 0.0689  0.0517  196 ILE B CB  
11921 C CG1 . ILE B 192 ? 0.7121 1.0285 0.9256 -0.0306 0.0510  0.0481  196 ILE B CG1 
11922 C CG2 . ILE B 192 ? 0.7361 1.1042 0.9680 -0.0507 0.0742  0.0630  196 ILE B CG2 
11923 C CD1 . ILE B 192 ? 0.7732 1.0635 0.9740 -0.0519 0.0392  0.0513  196 ILE B CD1 
11935 N N   . LEU B 193 ? 0.6211 0.9473 0.7921 -0.0061 0.1026  0.0456  197 LEU B N   
11936 C CA  . LEU B 193 ? 0.6072 0.9416 0.7631 -0.0071 0.1198  0.0491  197 LEU B CA  
11937 C C   . LEU B 193 ? 0.5883 0.8946 0.7123 0.0106  0.1238  0.0383  197 LEU B C   
11938 O O   . LEU B 193 ? 0.5814 0.8496 0.6798 0.0082  0.1134  0.0350  197 LEU B O   
11939 C CB  . LEU B 193 ? 0.6160 0.9357 0.7570 -0.0306 0.1188  0.0599  197 LEU B CB  
11940 C CG  . LEU B 193 ? 0.6262 0.9469 0.7440 -0.0335 0.1352  0.0652  197 LEU B CG  
11941 C CD1 . LEU B 193 ? 0.5856 0.9569 0.7261 -0.0300 0.1546  0.0694  197 LEU B CD1 
11942 C CD2 . LEU B 193 ? 0.6735 0.9717 0.7740 -0.0566 0.1317  0.0770  197 LEU B CD2 
11954 N N   . PRO B 194 ? 0.5836 0.9070 0.7071 0.0284  0.1383  0.0323  198 PRO B N   
11955 C CA  . PRO B 194 ? 0.6117 0.9054 0.6985 0.0414  0.1424  0.0218  198 PRO B CA  
11956 C C   . PRO B 194 ? 0.6232 0.9024 0.6794 0.0286  0.1472  0.0279  198 PRO B C   
11957 O O   . PRO B 194 ? 0.6334 0.9294 0.6970 0.0121  0.1527  0.0406  198 PRO B O   
11958 C CB  . PRO B 194 ? 0.6106 0.9290 0.7039 0.0625  0.1598  0.0154  198 PRO B CB  
11959 C CG  . PRO B 194 ? 0.5349 0.8934 0.6732 0.0651  0.1596  0.0210  198 PRO B CG  
11960 C CD  . PRO B 194 ? 0.5390 0.9095 0.6945 0.0389  0.1512  0.0343  198 PRO B CD  
11968 N N   . LEU B 195 ? 0.6326 0.8793 0.6530 0.0354  0.1441  0.0195  199 LEU B N   
11969 C CA  . LEU B 195 ? 0.6415 0.8719 0.6292 0.0254  0.1462  0.0255  199 LEU B CA  
11970 C C   . LEU B 195 ? 0.6430 0.9014 0.6269 0.0227  0.1676  0.0331  199 LEU B C   
11971 O O   . LEU B 195 ? 0.6153 0.8935 0.6010 0.0374  0.1830  0.0264  199 LEU B O   
11972 C CB  . LEU B 195 ? 0.6941 0.8915 0.6451 0.0346  0.1394  0.0140  199 LEU B CB  
11973 C CG  . LEU B 195 ? 0.7581 0.9293 0.7109 0.0337  0.1185  0.0091  199 LEU B CG  
11974 C CD1 . LEU B 195 ? 0.8393 0.9851 0.7628 0.0433  0.1128  -0.0043 199 LEU B CD1 
11975 C CD2 . LEU B 195 ? 0.7297 0.8880 0.6777 0.0192  0.1074  0.0205  199 LEU B CD2 
11987 N N   . THR B 196 ? 0.6576 0.9166 0.6353 0.0044  0.1693  0.0476  200 THR B N   
11988 C CA  . THR B 196 ? 0.6707 0.9559 0.6435 -0.0022 0.1898  0.0578  200 THR B CA  
11989 C C   . THR B 196 ? 0.7119 0.9736 0.6551 -0.0191 0.1868  0.0709  200 THR B C   
11990 O O   . THR B 196 ? 0.7892 1.0217 0.7272 -0.0273 0.1693  0.0745  200 THR B O   
11991 C CB  . THR B 196 ? 0.7109 1.0412 0.7283 -0.0111 0.1988  0.0669  200 THR B CB  
11992 O OG1 . THR B 196 ? 0.7789 1.1371 0.7913 -0.0199 0.2199  0.0786  200 THR B OG1 
11993 C CG2 . THR B 196 ? 0.7100 1.0310 0.7476 -0.0309 0.1820  0.0759  200 THR B CG2 
12001 N N   . ASN B 197 ? 0.7363 1.0105 0.6585 -0.0226 0.2050  0.0786  201 ASN B N   
12002 C CA  . ASN B 197 ? 0.7548 1.0095 0.6487 -0.0395 0.2050  0.0944  201 ASN B CA  
12003 C C   . ASN B 197 ? 0.7732 1.0443 0.6924 -0.0630 0.2087  0.1118  201 ASN B C   
12004 O O   . ASN B 197 ? 0.8481 1.0951 0.7455 -0.0789 0.2055  0.1262  201 ASN B O   
12005 C CB  . ASN B 197 ? 0.8152 1.0744 0.6707 -0.0344 0.2233  0.0962  201 ASN B CB  
12006 C CG  . ASN B 197 ? 0.9445 1.2515 0.8197 -0.0290 0.2487  0.0956  201 ASN B CG  
12007 O OD1 . ASN B 197 ? 1.0556 1.3730 0.9288 -0.0081 0.2566  0.0800  201 ASN B OD1 
12008 N ND2 . ASN B 197 ? 0.9993 1.3354 0.8937 -0.0478 0.2617  0.1129  201 ASN B ND2 
12015 N N   . ASP B 198 ? 0.7689 1.0788 0.7322 -0.0661 0.2143  0.1114  202 ASP B N   
12016 C CA  . ASP B 198 ? 0.7870 1.1174 0.7767 -0.0915 0.2174  0.1275  202 ASP B CA  
12017 C C   . ASP B 198 ? 0.8049 1.0991 0.7992 -0.1034 0.1942  0.1292  202 ASP B C   
12018 O O   . ASP B 198 ? 0.8020 1.1027 0.8255 -0.0995 0.1822  0.1208  202 ASP B O   
12019 C CB  . ASP B 198 ? 0.7379 1.1269 0.7752 -0.0894 0.2293  0.1262  202 ASP B CB  
12020 C CG  . ASP B 198 ? 0.7734 1.1928 0.8370 -0.1187 0.2360  0.1445  202 ASP B CG  
12021 O OD1 . ASP B 198 ? 0.8048 1.1911 0.8501 -0.1413 0.2280  0.1567  202 ASP B OD1 
12022 O OD2 . ASP B 198 ? 0.7797 1.2560 0.8822 -0.1191 0.2489  0.1472  202 ASP B OD2 
12027 N N   . ALA B 199 ? 0.8213 1.0751 0.7838 -0.1166 0.1881  0.1404  203 ALA B N   
12028 C CA  . ALA B 199 ? 0.7875 1.0008 0.7476 -0.1245 0.1673  0.1413  203 ALA B CA  
12029 C C   . ALA B 199 ? 0.7276 0.9541 0.7186 -0.1485 0.1640  0.1492  203 ALA B C   
12030 O O   . ALA B 199 ? 0.7032 0.9115 0.7061 -0.1501 0.1474  0.1433  203 ALA B O   
12031 C CB  . ALA B 199 ? 0.8228 0.9878 0.7384 -0.1286 0.1623  0.1517  203 ALA B CB  
12037 N N   . GLU B 200 ? 0.7526 1.0111 0.7558 -0.1684 0.1795  0.1626  204 GLU B N   
12038 C CA  . GLU B 200 ? 0.8148 1.0921 0.8505 -0.1939 0.1753  0.1699  204 GLU B CA  
12039 C C   . GLU B 200 ? 0.7832 1.0985 0.8621 -0.1831 0.1688  0.1569  204 GLU B C   
12040 O O   . GLU B 200 ? 0.7972 1.1089 0.8956 -0.1972 0.1545  0.1563  204 GLU B O   
12041 C CB  . GLU B 200 ? 0.9088 1.2232 0.9538 -0.2175 0.1948  0.1875  204 GLU B CB  
12042 C CG  . GLU B 200 ? 1.0571 1.3269 1.0665 -0.2426 0.1950  0.2053  204 GLU B CG  
12043 C CD  . GLU B 200 ? 1.1156 1.3454 1.1254 -0.2648 0.1755  0.2082  204 GLU B CD  
12044 O OE1 . GLU B 200 ? 1.0811 1.3325 1.1259 -0.2684 0.1649  0.1998  204 GLU B OE1 
12045 O OE2 . GLU B 200 ? 1.1575 1.3316 1.1299 -0.2778 0.1705  0.2188  204 GLU B OE2 
12052 N N   . ARG B 201 ? 0.7257 1.0743 0.8167 -0.1578 0.1785  0.1463  205 ARG B N   
12053 C CA  . ARG B 201 ? 0.7021 1.0810 0.8299 -0.1436 0.1714  0.1341  205 ARG B CA  
12054 C C   . ARG B 201 ? 0.7060 1.0407 0.8243 -0.1356 0.1489  0.1229  205 ARG B C   
12055 O O   . ARG B 201 ? 0.7041 1.0493 0.8491 -0.1398 0.1363  0.1192  205 ARG B O   
12056 C CB  . ARG B 201 ? 0.7376 1.1479 0.8708 -0.1151 0.1864  0.1242  205 ARG B CB  
12057 C CG  . ARG B 201 ? 0.8172 1.2561 0.9857 -0.0968 0.1801  0.1126  205 ARG B CG  
12058 C CD  . ARG B 201 ? 0.9612 1.4498 1.1765 -0.1144 0.1787  0.1215  205 ARG B CD  
12059 N NE  . ARG B 201 ? 1.0674 1.5871 1.3164 -0.0944 0.1734  0.1121  205 ARG B NE  
12060 C CZ  . ARG B 201 ? 1.1436 1.7051 1.4349 -0.1051 0.1662  0.1173  205 ARG B CZ  
12061 N NH1 . ARG B 201 ? 1.1736 1.7503 1.4788 -0.1379 0.1631  0.1310  205 ARG B NH1 
12062 N NH2 . ARG B 201 ? 1.1606 1.7470 1.4787 -0.0836 0.1610  0.1094  205 ARG B NH2 
12076 N N   . PHE B 202 ? 0.7063 0.9940 0.7869 -0.1238 0.1436  0.1180  206 PHE B N   
12077 C CA  . PHE B 202 ? 0.6777 0.9239 0.7477 -0.1178 0.1238  0.1096  206 PHE B CA  
12078 C C   . PHE B 202 ? 0.6762 0.8999 0.7479 -0.1419 0.1120  0.1171  206 PHE B C   
12079 O O   . PHE B 202 ? 0.6258 0.8403 0.7092 -0.1415 0.0975  0.1100  206 PHE B O   
12080 C CB  . PHE B 202 ? 0.7082 0.9135 0.7386 -0.1041 0.1213  0.1066  206 PHE B CB  
12081 C CG  . PHE B 202 ? 0.6792 0.8484 0.7005 -0.0942 0.1034  0.0978  206 PHE B CG  
12082 C CD1 . PHE B 202 ? 0.6978 0.8278 0.7033 -0.1053 0.0926  0.1035  206 PHE B CD1 
12083 C CD2 . PHE B 202 ? 0.6265 0.7995 0.6531 -0.0734 0.0984  0.0842  206 PHE B CD2 
12084 C CE1 . PHE B 202 ? 0.6831 0.7835 0.6806 -0.0943 0.0784  0.0957  206 PHE B CE1 
12085 C CE2 . PHE B 202 ? 0.6212 0.7654 0.6408 -0.0654 0.0836  0.0775  206 PHE B CE2 
12086 C CZ  . PHE B 202 ? 0.6582 0.7685 0.6642 -0.0749 0.0743  0.0832  206 PHE B CZ  
12096 N N   . ASN B 203 ? 0.7273 0.9388 0.7839 -0.1637 0.1181  0.1314  207 ASN B N   
12097 C CA  . ASN B 203 ? 0.7541 0.9384 0.8078 -0.1891 0.1071  0.1385  207 ASN B CA  
12098 C C   . ASN B 203 ? 0.8002 1.0252 0.8948 -0.2039 0.1022  0.1374  207 ASN B C   
12099 O O   . ASN B 203 ? 0.8131 1.0166 0.9099 -0.2125 0.0861  0.1329  207 ASN B O   
12100 C CB  . ASN B 203 ? 0.7770 0.9426 0.8073 -0.2118 0.1162  0.1557  207 ASN B CB  
12101 C CG  . ASN B 203 ? 0.7929 0.9053 0.7778 -0.2002 0.1149  0.1587  207 ASN B CG  
12102 O OD1 . ASN B 203 ? 0.8460 0.9315 0.8178 -0.1789 0.1045  0.1482  207 ASN B OD1 
12103 N ND2 . ASN B 203 ? 0.8036 0.9026 0.7648 -0.2147 0.1253  0.1745  207 ASN B ND2 
12110 N N   . GLU B 204 ? 0.8307 1.1163 0.9575 -0.2062 0.1157  0.1416  208 GLU B N   
12111 C CA  . GLU B 204 ? 0.8461 1.1779 1.0151 -0.2215 0.1107  0.1433  208 GLU B CA  
12112 C C   . GLU B 204 ? 0.7456 1.0800 0.9307 -0.2035 0.0954  0.1288  208 GLU B C   
12113 O O   . GLU B 204 ? 0.7050 1.0399 0.9041 -0.2190 0.0803  0.1279  208 GLU B O   
12114 C CB  . GLU B 204 ? 0.9695 1.3713 1.1720 -0.2212 0.1302  0.1507  208 GLU B CB  
12115 C CG  . GLU B 204 ? 1.1193 1.5763 1.3680 -0.2426 0.1261  0.1573  208 GLU B CG  
12116 C CD  . GLU B 204 ? 1.2406 1.7739 1.5303 -0.2280 0.1432  0.1594  208 GLU B CD  
12117 O OE1 . GLU B 204 ? 1.2807 1.8658 1.6138 -0.2348 0.1372  0.1615  208 GLU B OE1 
12118 O OE2 . GLU B 204 ? 1.2877 1.8295 1.5652 -0.2085 0.1623  0.1587  208 GLU B OE2 
12125 N N   . ILE B 205 ? 0.7506 1.0854 0.9318 -0.1721 0.0987  0.1176  209 ILE B N   
12126 C CA  . ILE B 205 ? 0.7364 1.0741 0.9319 -0.1546 0.0855  0.1053  209 ILE B CA  
12127 C C   . ILE B 205 ? 0.7344 1.0172 0.9052 -0.1600 0.0673  0.0999  209 ILE B C   
12128 O O   . ILE B 205 ? 0.7810 1.0669 0.9656 -0.1641 0.0530  0.0954  209 ILE B O   
12129 C CB  . ILE B 205 ? 0.7338 1.0772 0.9255 -0.1221 0.0937  0.0951  209 ILE B CB  
12130 C CG1 . ILE B 205 ? 0.7421 1.1442 0.9625 -0.1141 0.1112  0.0987  209 ILE B CG1 
12131 C CG2 . ILE B 205 ? 0.7293 1.0609 0.9258 -0.1047 0.0792  0.0831  209 ILE B CG2 
12132 C CD1 . ILE B 205 ? 0.7676 1.1710 0.9792 -0.0835 0.1210  0.0885  209 ILE B CD1 
12144 N N   . VAL B 206 ? 0.7215 0.9542 0.8547 -0.1589 0.0677  0.1006  210 VAL B N   
12145 C CA  . VAL B 206 ? 0.7469 0.9268 0.8550 -0.1620 0.0526  0.0960  210 VAL B CA  
12146 C C   . VAL B 206 ? 0.7745 0.9481 0.8880 -0.1912 0.0425  0.1011  210 VAL B C   
12147 O O   . VAL B 206 ? 0.7625 0.9161 0.8724 -0.1931 0.0279  0.0939  210 VAL B O   
12148 C CB  . VAL B 206 ? 0.7898 0.9217 0.8586 -0.1562 0.0561  0.0990  210 VAL B CB  
12149 C CG1 . VAL B 206 ? 0.8080 0.8847 0.8500 -0.1635 0.0432  0.0976  210 VAL B CG1 
12150 C CG2 . VAL B 206 ? 0.7684 0.9000 0.8295 -0.1276 0.0597  0.0908  210 VAL B CG2 
12160 N N   . LYS B 207 ? 0.7708 0.9611 0.8912 -0.2158 0.0501  0.1136  211 LYS B N   
12161 C CA  . LYS B 207 ? 0.8045 0.9870 0.9281 -0.2482 0.0396  0.1191  211 LYS B CA  
12162 C C   . LYS B 207 ? 0.8352 1.0626 0.9958 -0.2529 0.0286  0.1143  211 LYS B C   
12163 O O   . LYS B 207 ? 0.8945 1.1045 1.0514 -0.2739 0.0133  0.1129  211 LYS B O   
12164 C CB  . LYS B 207 ? 0.8101 1.0080 0.9370 -0.2753 0.0513  0.1352  211 LYS B CB  
12165 C CG  . LYS B 207 ? 0.8885 1.0313 0.9725 -0.2781 0.0583  0.1427  211 LYS B CG  
12166 C CD  . LYS B 207 ? 0.9639 1.1285 1.0529 -0.3047 0.0721  0.1602  211 LYS B CD  
12167 C CE  . LYS B 207 ? 1.0384 1.1553 1.0851 -0.3017 0.0816  0.1691  211 LYS B CE  
12168 N NZ  . LYS B 207 ? 1.0952 1.2446 1.1489 -0.3213 0.0994  0.1863  211 LYS B NZ  
12182 N N   . ASN B 208 ? 0.7855 1.0681 0.9794 -0.2335 0.0355  0.1119  212 ASN B N   
12183 C CA  . ASN B 208 ? 0.7740 1.1045 1.0054 -0.2348 0.0254  0.1094  212 ASN B CA  
12184 C C   . ASN B 208 ? 0.7968 1.1077 1.0211 -0.2121 0.0125  0.0960  212 ASN B C   
12185 O O   . ASN B 208 ? 0.7985 1.1451 1.0503 -0.2099 0.0026  0.0938  212 ASN B O   
12186 C CB  . ASN B 208 ? 0.7658 1.1679 1.0382 -0.2236 0.0403  0.1149  212 ASN B CB  
12187 C CG  . ASN B 208 ? 0.8275 1.2624 1.1145 -0.2491 0.0534  0.1299  212 ASN B CG  
12188 O OD1 . ASN B 208 ? 0.8785 1.2981 1.1588 -0.2825 0.0460  0.1374  212 ASN B OD1 
12189 N ND2 . ASN B 208 ? 0.8096 1.2885 1.1149 -0.2342 0.0736  0.1343  212 ASN B ND2 
12196 N N   . GLN B 209 ? 0.8048 1.0626 0.9938 -0.1954 0.0122  0.0882  213 GLN B N   
12197 C CA  . GLN B 209 ? 0.7748 1.0154 0.9565 -0.1743 0.0020  0.0766  213 GLN B CA  
12198 C C   . GLN B 209 ? 0.8001 1.0106 0.9671 -0.1905 -0.0162 0.0724  213 GLN B C   
12199 O O   . GLN B 209 ? 0.8850 1.0588 1.0287 -0.2120 -0.0203 0.0751  213 GLN B O   
12200 C CB  . GLN B 209 ? 0.7610 0.9612 0.9128 -0.1519 0.0085  0.0707  213 GLN B CB  
12201 C CG  . GLN B 209 ? 0.7257 0.9519 0.8877 -0.1314 0.0236  0.0710  213 GLN B CG  
12202 C CD  . GLN B 209 ? 0.6526 0.9204 0.8444 -0.1142 0.0231  0.0666  213 GLN B CD  
12203 O OE1 . GLN B 209 ? 0.6989 0.9539 0.8865 -0.0991 0.0150  0.0587  213 GLN B OE1 
12204 N NE2 . GLN B 209 ? 0.5654 0.8833 0.7871 -0.1157 0.0326  0.0726  213 GLN B NE2 
12213 N N   . LYS B 210 ? 0.7389 0.9618 0.9162 -0.1796 -0.0273 0.0657  214 LYS B N   
12214 C CA  . LYS B 210 ? 0.7165 0.9103 0.8758 -0.1903 -0.0447 0.0597  214 LYS B CA  
12215 C C   . LYS B 210 ? 0.6868 0.8547 0.8281 -0.1643 -0.0474 0.0499  214 LYS B C   
12216 O O   . LYS B 210 ? 0.6408 0.8313 0.7972 -0.1414 -0.0411 0.0485  214 LYS B O   
12217 C CB  . LYS B 210 ? 0.7347 0.9743 0.9246 -0.2064 -0.0581 0.0630  214 LYS B CB  
12218 C CG  . LYS B 210 ? 0.7869 1.0636 1.0019 -0.2344 -0.0556 0.0743  214 LYS B CG  
12219 C CD  . LYS B 210 ? 0.8880 1.1175 1.0724 -0.2658 -0.0623 0.0756  214 LYS B CD  
12220 C CE  . LYS B 210 ? 0.9606 1.2303 1.1721 -0.2983 -0.0613 0.0881  214 LYS B CE  
12221 N NZ  . LYS B 210 ? 1.0392 1.2605 1.2200 -0.3333 -0.0718 0.0890  214 LYS B NZ  
12235 N N   . ILE B 211 ? 0.7022 0.8209 0.8094 -0.1683 -0.0562 0.0431  215 ILE B N   
12236 C CA  . ILE B 211 ? 0.6947 0.7886 0.7831 -0.1453 -0.0573 0.0348  215 ILE B CA  
12237 C C   . ILE B 211 ? 0.6485 0.7704 0.7531 -0.1392 -0.0683 0.0323  215 ILE B C   
12238 O O   . ILE B 211 ? 0.6796 0.8308 0.8028 -0.1550 -0.0791 0.0354  215 ILE B O   
12239 C CB  . ILE B 211 ? 0.8150 0.8484 0.8606 -0.1486 -0.0611 0.0285  215 ILE B CB  
12240 C CG1 . ILE B 211 ? 0.8605 0.8788 0.8935 -0.1744 -0.0761 0.0263  215 ILE B CG1 
12241 C CG2 . ILE B 211 ? 0.8769 0.8803 0.9050 -0.1479 -0.0496 0.0321  215 ILE B CG2 
12242 C CD1 . ILE B 211 ? 0.9248 0.8831 0.9128 -0.1731 -0.0813 0.0171  215 ILE B CD1 
12254 N N   . SER B 212 ? 0.6130 0.7267 0.7104 -0.1166 -0.0661 0.0275  216 SER B N   
12255 C CA  . SER B 212 ? 0.6251 0.7498 0.7254 -0.1088 -0.0767 0.0248  216 SER B CA  
12256 C C   . SER B 212 ? 0.6521 0.7305 0.7148 -0.1023 -0.0792 0.0170  216 SER B C   
12257 O O   . SER B 212 ? 0.6772 0.7175 0.7140 -0.1053 -0.0745 0.0138  216 SER B O   
12258 C CB  . SER B 212 ? 0.6201 0.7773 0.7458 -0.0877 -0.0708 0.0274  216 SER B CB  
12259 O OG  . SER B 212 ? 0.6480 0.8158 0.7765 -0.0811 -0.0819 0.0269  216 SER B OG  
12265 N N   . ALA B 213 ? 0.6757 0.7573 0.7343 -0.0923 -0.0861 0.0147  217 ALA B N   
12266 C CA  . ALA B 213 ? 0.6734 0.7163 0.6970 -0.0850 -0.0868 0.0079  217 ALA B CA  
12267 C C   . ALA B 213 ? 0.6313 0.6861 0.6585 -0.0680 -0.0876 0.0086  217 ALA B C   
12268 O O   . ALA B 213 ? 0.6150 0.7037 0.6690 -0.0628 -0.0904 0.0139  217 ALA B O   
12269 C CB  . ALA B 213 ? 0.7013 0.7184 0.6975 -0.1029 -0.0996 0.0026  217 ALA B CB  
12275 N N   . ASN B 214 ? 0.6697 0.6952 0.6688 -0.0586 -0.0842 0.0039  218 ASN B N   
12276 C CA  . ASN B 214 ? 0.6737 0.7030 0.6681 -0.0455 -0.0851 0.0049  218 ASN B CA  
12277 C C   . ASN B 214 ? 0.6981 0.6914 0.6543 -0.0423 -0.0828 -0.0015 218 ASN B C   
12278 O O   . ASN B 214 ? 0.7762 0.7416 0.7107 -0.0494 -0.0821 -0.0072 218 ASN B O   
12279 C CB  . ASN B 214 ? 0.6611 0.7063 0.6761 -0.0304 -0.0745 0.0092  218 ASN B CB  
12280 C CG  . ASN B 214 ? 0.7267 0.7530 0.7313 -0.0224 -0.0614 0.0068  218 ASN B CG  
12281 O OD1 . ASN B 214 ? 0.7512 0.7746 0.7515 -0.0113 -0.0553 0.0076  218 ASN B OD1 
12282 N ND2 . ASN B 214 ? 0.7401 0.7546 0.7410 -0.0286 -0.0576 0.0049  218 ASN B ND2 
12289 N N   . ILE B 215 ? 0.6599 0.6520 0.6061 -0.0310 -0.0808 -0.0004 219 ILE B N   
12290 C CA  . ILE B 215 ? 0.7011 0.6643 0.6098 -0.0281 -0.0797 -0.0061 219 ILE B CA  
12291 C C   . ILE B 215 ? 0.7324 0.6866 0.6330 -0.0126 -0.0643 -0.0060 219 ILE B C   
12292 O O   . ILE B 215 ? 0.8105 0.7403 0.6799 -0.0077 -0.0596 -0.0113 219 ILE B O   
12293 C CB  . ILE B 215 ? 0.7047 0.6729 0.6004 -0.0309 -0.0919 -0.0044 219 ILE B CB  
12294 C CG1 . ILE B 215 ? 0.8043 0.7959 0.7196 -0.0203 -0.0898 0.0045  219 ILE B CG1 
12295 C CG2 . ILE B 215 ? 0.6839 0.6636 0.5871 -0.0477 -0.1090 -0.0045 219 ILE B CG2 
12296 C CD1 . ILE B 215 ? 0.9075 0.9040 0.8099 -0.0217 -0.1023 0.0085  219 ILE B CD1 
12308 N N   . ASP B 216 ? 0.6805 0.6539 0.6068 -0.0047 -0.0562 -0.0005 220 ASP B N   
12309 C CA  . ASP B 216 ? 0.6755 0.6463 0.5981 0.0078  -0.0429 0.0007  220 ASP B CA  
12310 C C   . ASP B 216 ? 0.6533 0.6259 0.5905 0.0110  -0.0352 0.0006  220 ASP B C   
12311 O O   . ASP B 216 ? 0.5917 0.5774 0.5508 0.0058  -0.0380 0.0027  220 ASP B O   
12312 C CB  . ASP B 216 ? 0.6824 0.6718 0.6178 0.0128  -0.0410 0.0079  220 ASP B CB  
12313 C CG  . ASP B 216 ? 0.6787 0.6880 0.6452 0.0123  -0.0416 0.0123  220 ASP B CG  
12314 O OD1 . ASP B 216 ? 0.6835 0.6991 0.6636 0.0064  -0.0472 0.0112  220 ASP B OD1 
12315 O OD2 . ASP B 216 ? 0.6582 0.6764 0.6343 0.0171  -0.0362 0.0169  220 ASP B OD2 
12320 N N   . THR B 217 ? 0.6724 0.6333 0.5969 0.0209  -0.0250 -0.0011 221 THR B N   
12321 C CA  . THR B 217 ? 0.6996 0.6568 0.6312 0.0249  -0.0192 -0.0011 221 THR B CA  
12322 C C   . THR B 217 ? 0.6583 0.6410 0.6192 0.0256  -0.0171 0.0045  221 THR B C   
12323 O O   . THR B 217 ? 0.6534 0.6376 0.6249 0.0208  -0.0187 0.0051  221 THR B O   
12324 C CB  . THR B 217 ? 0.7348 0.6777 0.6478 0.0390  -0.0088 -0.0031 221 THR B CB  
12325 O OG1 . THR B 217 ? 0.7732 0.6824 0.6542 0.0383  -0.0106 -0.0104 221 THR B OG1 
12326 C CG2 . THR B 217 ? 0.7041 0.6513 0.6290 0.0467  -0.0027 0.0001  221 THR B CG2 
12334 N N   . PRO B 218 ? 0.6430 0.6439 0.6153 0.0301  -0.0136 0.0087  222 PRO B N   
12335 C CA  . PRO B 218 ? 0.6648 0.6845 0.6602 0.0291  -0.0129 0.0125  222 PRO B CA  
12336 C C   . PRO B 218 ? 0.7229 0.7487 0.7312 0.0211  -0.0200 0.0123  222 PRO B C   
12337 O O   . PRO B 218 ? 0.8707 0.8973 0.8778 0.0173  -0.0263 0.0124  222 PRO B O   
12338 C CB  . PRO B 218 ? 0.5992 0.6319 0.5994 0.0319  -0.0096 0.0167  222 PRO B CB  
12339 C CG  . PRO B 218 ? 0.5902 0.6148 0.5711 0.0377  -0.0046 0.0160  222 PRO B CG  
12340 C CD  . PRO B 218 ? 0.6228 0.6263 0.5850 0.0348  -0.0098 0.0104  222 PRO B CD  
12348 N N   . GLU B 219 ? 0.6586 0.6909 0.6792 0.0197  -0.0188 0.0126  223 GLU B N   
12349 C CA  . GLU B 219 ? 0.6395 0.6809 0.6736 0.0139  -0.0229 0.0126  223 GLU B CA  
12350 C C   . GLU B 219 ? 0.6261 0.6806 0.6746 0.0169  -0.0213 0.0140  223 GLU B C   
12351 O O   . GLU B 219 ? 0.6134 0.6691 0.6614 0.0204  -0.0179 0.0150  223 GLU B O   
12352 C CB  . GLU B 219 ? 0.6208 0.6578 0.6545 0.0091  -0.0214 0.0120  223 GLU B CB  
12353 C CG  . GLU B 219 ? 0.6445 0.6596 0.6587 0.0059  -0.0226 0.0099  223 GLU B CG  
12354 C CD  . GLU B 219 ? 0.7246 0.7354 0.7331 -0.0025 -0.0308 0.0079  223 GLU B CD  
12355 O OE1 . GLU B 219 ? 0.7371 0.7613 0.7538 -0.0020 -0.0353 0.0088  223 GLU B OE1 
12356 O OE2 . GLU B 219 ? 0.8183 0.8107 0.8124 -0.0103 -0.0336 0.0056  223 GLU B OE2 
12363 N N   . GLY B 220 ? 0.6157 0.6802 0.6766 0.0154  -0.0240 0.0140  224 GLY B N   
12364 C CA  . GLY B 220 ? 0.6390 0.7100 0.7094 0.0199  -0.0227 0.0141  224 GLY B CA  
12365 C C   . GLY B 220 ? 0.6291 0.7058 0.7051 0.0206  -0.0174 0.0122  224 GLY B C   
12366 O O   . GLY B 220 ? 0.6214 0.7050 0.7060 0.0242  -0.0161 0.0110  224 GLY B O   
12370 N N   . GLY B 221 ? 0.6059 0.6787 0.6748 0.0186  -0.0140 0.0122  225 GLY B N   
12371 C CA  . GLY B 221 ? 0.6227 0.6998 0.6926 0.0187  -0.0093 0.0112  225 GLY B CA  
12372 C C   . GLY B 221 ? 0.6572 0.7338 0.7257 0.0221  -0.0080 0.0087  225 GLY B C   
12373 O O   . GLY B 221 ? 0.6564 0.7366 0.7247 0.0234  -0.0041 0.0065  225 GLY B O   
12377 N N   . PHE B 222 ? 0.6241 0.6954 0.6898 0.0226  -0.0109 0.0090  226 PHE B N   
12378 C CA  . PHE B 222 ? 0.6176 0.6848 0.6800 0.0226  -0.0113 0.0062  226 PHE B CA  
12379 C C   . PHE B 222 ? 0.5879 0.6511 0.6530 0.0271  -0.0102 0.0025  226 PHE B C   
12380 O O   . PHE B 222 ? 0.5771 0.6345 0.6357 0.0284  -0.0084 -0.0020 226 PHE B O   
12381 C CB  . PHE B 222 ? 0.6406 0.7043 0.7009 0.0194  -0.0146 0.0088  226 PHE B CB  
12382 C CG  . PHE B 222 ? 0.6788 0.7505 0.7374 0.0174  -0.0145 0.0119  226 PHE B CG  
12383 C CD1 . PHE B 222 ? 0.6908 0.7668 0.7474 0.0199  -0.0123 0.0129  226 PHE B CD1 
12384 C CD2 . PHE B 222 ? 0.6839 0.7598 0.7434 0.0133  -0.0163 0.0150  226 PHE B CD2 
12385 C CE1 . PHE B 222 ? 0.7233 0.8069 0.7786 0.0215  -0.0123 0.0166  226 PHE B CE1 
12386 C CE2 . PHE B 222 ? 0.7006 0.7899 0.7621 0.0137  -0.0157 0.0188  226 PHE B CE2 
12387 C CZ  . PHE B 222 ? 0.7128 0.8055 0.7721 0.0194  -0.0139 0.0195  226 PHE B CZ  
12397 N N   . ASP B 223 ? 0.5997 0.6654 0.6728 0.0307  -0.0116 0.0043  227 ASP B N   
12398 C CA  . ASP B 223 ? 0.6418 0.7085 0.7206 0.0387  -0.0096 0.0018  227 ASP B CA  
12399 C C   . ASP B 223 ? 0.6616 0.7397 0.7430 0.0408  -0.0026 -0.0010 227 ASP B C   
12400 O O   . ASP B 223 ? 0.6570 0.7311 0.7346 0.0475  0.0020  -0.0059 227 ASP B O   
12401 C CB  . ASP B 223 ? 0.6423 0.7171 0.7323 0.0423  -0.0136 0.0060  227 ASP B CB  
12402 C CG  . ASP B 223 ? 0.6970 0.7568 0.7820 0.0451  -0.0191 0.0084  227 ASP B CG  
12403 O OD1 . ASP B 223 ? 0.7194 0.7614 0.7944 0.0458  -0.0186 0.0060  227 ASP B OD1 
12404 O OD2 . ASP B 223 ? 0.7028 0.7672 0.7919 0.0455  -0.0244 0.0132  227 ASP B OD2 
12409 N N   . ALA B 224 ? 0.6805 0.7704 0.7657 0.0349  -0.0011 0.0020  228 ALA B N   
12410 C CA  . ALA B 224 ? 0.6109 0.7125 0.6978 0.0349  0.0064  0.0014  228 ALA B CA  
12411 C C   . ALA B 224 ? 0.5959 0.6883 0.6667 0.0347  0.0099  -0.0025 228 ALA B C   
12412 O O   . ALA B 224 ? 0.6019 0.6985 0.6689 0.0391  0.0171  -0.0058 228 ALA B O   
12413 C CB  . ALA B 224 ? 0.5753 0.6858 0.6667 0.0261  0.0061  0.0066  228 ALA B CB  
12419 N N   . ILE B 225 ? 0.5950 0.6768 0.6557 0.0300  0.0049  -0.0019 229 ILE B N   
12420 C CA  . ILE B 225 ? 0.6242 0.6993 0.6695 0.0286  0.0054  -0.0051 229 ILE B CA  
12421 C C   . ILE B 225 ? 0.6782 0.7421 0.7153 0.0335  0.0067  -0.0127 229 ILE B C   
12422 O O   . ILE B 225 ? 0.7000 0.7612 0.7243 0.0357  0.0115  -0.0175 229 ILE B O   
12423 C CB  . ILE B 225 ? 0.5994 0.6709 0.6403 0.0234  -0.0014 -0.0021 229 ILE B CB  
12424 C CG1 . ILE B 225 ? 0.5681 0.6452 0.6117 0.0217  -0.0013 0.0045  229 ILE B CG1 
12425 C CG2 . ILE B 225 ? 0.5301 0.5973 0.5564 0.0207  -0.0040 -0.0053 229 ILE B CG2 
12426 C CD1 . ILE B 225 ? 0.5464 0.6238 0.5885 0.0205  -0.0063 0.0082  229 ILE B CD1 
12438 N N   . MET B 226 ? 0.6736 0.7273 0.7144 0.0354  0.0025  -0.0140 230 MET B N   
12439 C CA  . MET B 226 ? 0.6697 0.7048 0.6993 0.0405  0.0031  -0.0213 230 MET B CA  
12440 C C   . MET B 226 ? 0.6479 0.6875 0.6771 0.0520  0.0128  -0.0258 230 MET B C   
12441 O O   . MET B 226 ? 0.6279 0.6552 0.6392 0.0554  0.0169  -0.0335 230 MET B O   
12442 C CB  . MET B 226 ? 0.6659 0.6887 0.7007 0.0420  -0.0021 -0.0194 230 MET B CB  
12443 C CG  . MET B 226 ? 0.6544 0.6511 0.6760 0.0490  -0.0015 -0.0262 230 MET B CG  
12444 S SD  . MET B 226 ? 0.6675 0.6395 0.6625 0.0383  -0.0059 -0.0343 230 MET B SD  
12445 C CE  . MET B 226 ? 0.6637 0.6354 0.6644 0.0225  -0.0160 -0.0263 230 MET B CE  
12455 N N   . GLN B 227 ? 0.6448 0.7037 0.6935 0.0578  0.0166  -0.0211 231 GLN B N   
12456 C CA  . GLN B 227 ? 0.6750 0.7461 0.7289 0.0697  0.0270  -0.0238 231 GLN B CA  
12457 C C   . GLN B 227 ? 0.6763 0.7567 0.7197 0.0667  0.0354  -0.0255 231 GLN B C   
12458 O O   . GLN B 227 ? 0.6875 0.7658 0.7202 0.0762  0.0448  -0.0318 231 GLN B O   
12459 C CB  . GLN B 227 ? 0.6288 0.7258 0.7094 0.0731  0.0275  -0.0166 231 GLN B CB  
12460 C CG  . GLN B 227 ? 0.6264 0.7151 0.7152 0.0792  0.0199  -0.0145 231 GLN B CG  
12461 C CD  . GLN B 227 ? 0.6550 0.7238 0.7343 0.0950  0.0232  -0.0209 231 GLN B CD  
12462 O OE1 . GLN B 227 ? 0.6712 0.7531 0.7578 0.1093  0.0322  -0.0230 231 GLN B OE1 
12463 N NE2 . GLN B 227 ? 0.6727 0.7091 0.7348 0.0926  0.0165  -0.0238 231 GLN B NE2 
12472 N N   . ALA B 228 ? 0.6513 0.7399 0.6950 0.0548  0.0326  -0.0195 232 ALA B N   
12473 C CA  . ALA B 228 ? 0.6710 0.7670 0.7029 0.0514  0.0400  -0.0189 232 ALA B CA  
12474 C C   . ALA B 228 ? 0.6839 0.7597 0.6874 0.0519  0.0396  -0.0269 232 ALA B C   
12475 O O   . ALA B 228 ? 0.7609 0.8397 0.7493 0.0543  0.0483  -0.0295 232 ALA B O   
12476 C CB  . ALA B 228 ? 0.6568 0.7596 0.6924 0.0397  0.0359  -0.0100 232 ALA B CB  
12482 N N   . ALA B 229 ? 0.6682 0.7243 0.6630 0.0484  0.0293  -0.0307 233 ALA B N   
12483 C CA  . ALA B 229 ? 0.7365 0.7730 0.7037 0.0456  0.0260  -0.0387 233 ALA B CA  
12484 C C   . ALA B 229 ? 0.7639 0.7803 0.7158 0.0564  0.0317  -0.0501 233 ALA B C   
12485 O O   . ALA B 229 ? 0.7821 0.7841 0.7063 0.0569  0.0340  -0.0584 233 ALA B O   
12486 C CB  . ALA B 229 ? 0.7406 0.7673 0.7062 0.0348  0.0123  -0.0371 233 ALA B CB  
12492 N N   . VAL B 230 ? 0.7213 0.7343 0.6879 0.0659  0.0336  -0.0507 234 VAL B N   
12493 C CA  . VAL B 230 ? 0.7241 0.7112 0.6746 0.0785  0.0379  -0.0613 234 VAL B CA  
12494 C C   . VAL B 230 ? 0.7424 0.7443 0.6959 0.0957  0.0540  -0.0642 234 VAL B C   
12495 O O   . VAL B 230 ? 0.7897 0.7718 0.7180 0.1060  0.0616  -0.0751 234 VAL B O   
12496 C CB  . VAL B 230 ? 0.8042 0.7762 0.7663 0.0811  0.0305  -0.0593 234 VAL B CB  
12497 C CG1 . VAL B 230 ? 0.9904 0.9346 0.9381 0.0984  0.0363  -0.0686 234 VAL B CG1 
12498 C CG2 . VAL B 230 ? 0.7448 0.6997 0.6988 0.0637  0.0166  -0.0579 234 VAL B CG2 
12508 N N   . CYS B 231 ? 0.6935 0.7307 0.6769 0.0989  0.0598  -0.0546 235 CYS B N   
12509 C CA  . CYS B 231 ? 0.7160 0.7756 0.7094 0.1150  0.0755  -0.0552 235 CYS B CA  
12510 C C   . CYS B 231 ? 0.7953 0.8644 0.7701 0.1129  0.0870  -0.0576 235 CYS B C   
12511 O O   . CYS B 231 ? 0.8371 0.9392 0.8286 0.1080  0.0940  -0.0486 235 CYS B O   
12512 C CB  . CYS B 231 ? 0.6803 0.7780 0.7129 0.1148  0.0760  -0.0432 235 CYS B CB  
12513 S SG  . CYS B 231 ? 0.7111 0.8011 0.7641 0.1173  0.0621  -0.0385 235 CYS B SG  
12518 N N   . LYS B 232 ? 0.8071 0.8457 0.7448 0.1153  0.0885  -0.0694 236 LYS B N   
12519 C CA  . LYS B 232 ? 0.8082 0.8516 0.7214 0.1119  0.0975  -0.0716 236 LYS B CA  
12520 C C   . LYS B 232 ? 0.8221 0.8982 0.7471 0.1252  0.1180  -0.0688 236 LYS B C   
12521 O O   . LYS B 232 ? 0.8175 0.9178 0.7437 0.1169  0.1252  -0.0610 236 LYS B O   
12522 C CB  . LYS B 232 ? 0.8319 0.8340 0.6999 0.1135  0.0949  -0.0867 236 LYS B CB  
12523 C CG  . LYS B 232 ? 0.8644 0.8678 0.6999 0.1132  0.1055  -0.0910 236 LYS B CG  
12524 C CD  . LYS B 232 ? 0.8988 0.8579 0.6864 0.1121  0.0995  -0.1070 236 LYS B CD  
12525 C CE  . LYS B 232 ? 0.9559 0.9132 0.7058 0.1170  0.1131  -0.1138 236 LYS B CE  
12526 N NZ  . LYS B 232 ? 0.9667 0.9472 0.7142 0.1014  0.1102  -0.1019 236 LYS B NZ  
12540 N N   . GLU B 233 ? 0.8485 0.9269 0.7827 0.1463  0.1280  -0.0742 237 GLU B N   
12541 C CA  . GLU B 233 ? 0.8846 0.9986 0.8311 0.1611  0.1493  -0.0719 237 GLU B CA  
12542 C C   . GLU B 233 ? 0.7983 0.9622 0.7896 0.1515  0.1506  -0.0551 237 GLU B C   
12543 O O   . GLU B 233 ? 0.7496 0.9443 0.7457 0.1456  0.1630  -0.0478 237 GLU B O   
12544 C CB  . GLU B 233 ? 1.0314 1.1362 0.9784 0.1892  0.1591  -0.0813 237 GLU B CB  
12545 C CG  . GLU B 233 ? 1.1891 1.3326 1.1470 0.2084  0.1836  -0.0802 237 GLU B CG  
12546 C CD  . GLU B 233 ? 1.3599 1.4964 1.3222 0.2401  0.1932  -0.0883 237 GLU B CD  
12547 O OE1 . GLU B 233 ? 1.4045 1.5119 1.3699 0.2454  0.1794  -0.0910 237 GLU B OE1 
12548 O OE2 . GLU B 233 ? 1.4337 1.5937 1.3955 0.2607  0.2154  -0.0912 237 GLU B OE2 
12555 N N   . LYS B 234 ? 0.7823 0.9529 0.8043 0.1484  0.1376  -0.0487 238 LYS B N   
12556 C CA  . LYS B 234 ? 0.7278 0.9432 0.7907 0.1387  0.1373  -0.0340 238 LYS B CA  
12557 C C   . LYS B 234 ? 0.6818 0.8998 0.7406 0.1132  0.1306  -0.0252 238 LYS B C   
12558 O O   . LYS B 234 ? 0.6552 0.9074 0.7320 0.1034  0.1381  -0.0147 238 LYS B O   
12559 C CB  . LYS B 234 ? 0.7718 0.9896 0.8626 0.1423  0.1238  -0.0304 238 LYS B CB  
12560 C CG  . LYS B 234 ? 0.8436 1.0788 0.9535 0.1685  0.1326  -0.0325 238 LYS B CG  
12561 C CD  . LYS B 234 ? 0.8998 1.1209 1.0237 0.1741  0.1168  -0.0311 238 LYS B CD  
12562 C CE  . LYS B 234 ? 0.9631 1.2141 1.1161 0.1990  0.1235  -0.0280 238 LYS B CE  
12563 N NZ  . LYS B 234 ? 0.9770 1.2882 1.1737 0.1909  0.1244  -0.0141 238 LYS B NZ  
12577 N N   . ILE B 235 ? 0.6856 0.8680 0.7213 0.1023  0.1165  -0.0286 239 ILE B N   
12578 C CA  . ILE B 235 ? 0.6530 0.8343 0.6815 0.0820  0.1105  -0.0204 239 ILE B CA  
12579 C C   . ILE B 235 ? 0.7160 0.9021 0.7202 0.0800  0.1242  -0.0198 239 ILE B C   
12580 O O   . ILE B 235 ? 0.7079 0.9108 0.7167 0.0667  0.1279  -0.0088 239 ILE B O   
12581 C CB  . ILE B 235 ? 0.6581 0.8052 0.6698 0.0738  0.0929  -0.0238 239 ILE B CB  
12582 C CG1 . ILE B 235 ? 0.6867 0.8315 0.7220 0.0735  0.0804  -0.0219 239 ILE B CG1 
12583 C CG2 . ILE B 235 ? 0.6526 0.7966 0.6528 0.0574  0.0880  -0.0156 239 ILE B CG2 
12584 C CD1 . ILE B 235 ? 0.6904 0.8597 0.7540 0.0627  0.0772  -0.0103 239 ILE B CD1 
12596 N N   . GLY B 236 ? 0.7476 0.9160 0.7224 0.0927  0.1318  -0.0316 240 GLY B N   
12597 C CA  . GLY B 236 ? 0.7517 0.9240 0.6989 0.0930  0.1461  -0.0322 240 GLY B CA  
12598 C C   . GLY B 236 ? 0.7979 0.9383 0.7040 0.0844  0.1372  -0.0364 240 GLY B C   
12599 O O   . GLY B 236 ? 0.8258 0.9707 0.7084 0.0804  0.1467  -0.0330 240 GLY B O   
12603 N N   . TRP B 237 ? 0.8144 0.9256 0.7114 0.0807  0.1192  -0.0425 241 TRP B N   
12604 C CA  . TRP B 237 ? 0.8227 0.9082 0.6825 0.0726  0.1092  -0.0466 241 TRP B CA  
12605 C C   . TRP B 237 ? 0.8779 0.9497 0.6980 0.0826  0.1212  -0.0586 241 TRP B C   
12606 O O   . TRP B 237 ? 0.9422 1.0027 0.7564 0.0977  0.1288  -0.0710 241 TRP B O   
12607 C CB  . TRP B 237 ? 0.7927 0.8527 0.6516 0.0680  0.0895  -0.0525 241 TRP B CB  
12608 C CG  . TRP B 237 ? 0.7270 0.7968 0.6207 0.0603  0.0781  -0.0428 241 TRP B CG  
12609 C CD1 . TRP B 237 ? 0.7038 0.7714 0.6216 0.0647  0.0733  -0.0448 241 TRP B CD1 
12610 C CD2 . TRP B 237 ? 0.7067 0.7867 0.6108 0.0480  0.0705  -0.0298 241 TRP B CD2 
12611 N NE1 . TRP B 237 ? 0.6463 0.7234 0.5879 0.0552  0.0635  -0.0346 241 TRP B NE1 
12612 C CE2 . TRP B 237 ? 0.6667 0.7504 0.6004 0.0456  0.0620  -0.0259 241 TRP B CE2 
12613 C CE3 . TRP B 237 ? 0.7742 0.8579 0.6630 0.0400  0.0701  -0.0209 241 TRP B CE3 
12614 C CZ2 . TRP B 237 ? 0.6563 0.7460 0.6035 0.0363  0.0541  -0.0149 241 TRP B CZ2 
12615 C CZ3 . TRP B 237 ? 0.7294 0.8180 0.6331 0.0314  0.0618  -0.0091 241 TRP B CZ3 
12616 C CH2 . TRP B 237 ? 0.6889 0.7798 0.6210 0.0300  0.0543  -0.0070 241 TRP B CH2 
12627 N N   . ARG B 238 ? 0.8472 0.9173 0.6369 0.0753  0.1231  -0.0550 242 ARG B N   
12628 C CA  . ARG B 238 ? 0.9195 0.9745 0.6643 0.0831  0.1337  -0.0664 242 ARG B CA  
12629 C C   . ARG B 238 ? 0.9276 0.9489 0.6346 0.0749  0.1149  -0.0757 242 ARG B C   
12630 O O   . ARG B 238 ? 0.9002 0.9204 0.6135 0.0612  0.0968  -0.0675 242 ARG B O   
12631 C CB  . ARG B 238 ? 1.0184 1.0956 0.7502 0.0802  0.1497  -0.0555 242 ARG B CB  
12632 C CG  . ARG B 238 ? 1.1288 1.2112 0.8605 0.0628  0.1379  -0.0390 242 ARG B CG  
12633 C CD  . ARG B 238 ? 1.2723 1.3756 0.9935 0.0589  0.1551  -0.0259 242 ARG B CD  
12634 N NE  . ARG B 238 ? 1.3256 1.4339 1.0571 0.0437  0.1451  -0.0076 242 ARG B NE  
12635 C CZ  . ARG B 238 ? 1.3637 1.4855 1.0877 0.0359  0.1562  0.0078  242 ARG B CZ  
12636 N NH1 . ARG B 238 ? 1.3854 1.5225 1.0935 0.0409  0.1788  0.0078  242 ARG B NH1 
12637 N NH2 . ARG B 238 ? 1.3445 1.4632 1.0756 0.0234  0.1455  0.0236  242 ARG B NH2 
12651 N N   . ASN B 239 ? 1.0084 1.0024 0.6758 0.0837  0.1192  -0.0930 243 ASN B N   
12652 C CA  . ASN B 239 ? 1.1182 1.0807 0.7444 0.0735  0.1013  -0.1026 243 ASN B CA  
12653 C C   . ASN B 239 ? 1.0773 1.0522 0.6866 0.0605  0.0942  -0.0898 243 ASN B C   
12654 O O   . ASN B 239 ? 1.0646 1.0637 0.6795 0.0620  0.1084  -0.0773 243 ASN B O   
12655 C CB  . ASN B 239 ? 1.3533 1.2828 0.9287 0.0843  0.1100  -0.1231 243 ASN B CB  
12656 C CG  . ASN B 239 ? 1.5227 1.4303 1.1054 0.0998  0.1165  -0.1374 243 ASN B CG  
12657 O OD1 . ASN B 239 ? 1.3544 1.2757 0.9820 0.1043  0.1167  -0.1313 243 ASN B OD1 
12658 N ND2 . ASN B 239 ? 1.9107 1.7801 1.4439 0.1087  0.1215  -0.1570 243 ASN B ND2 
12664 N N   . ASP B 240 ? 1.0634 1.0223 0.6515 0.0475  0.0720  -0.0919 244 ASP B N   
12665 C CA  . ASP B 240 ? 1.0879 1.0521 0.6475 0.0378  0.0637  -0.0826 244 ASP B CA  
12666 C C   . ASP B 240 ? 0.9544 0.9488 0.5435 0.0352  0.0685  -0.0604 244 ASP B C   
12667 O O   . ASP B 240 ? 0.9034 0.9069 0.4722 0.0360  0.0799  -0.0515 244 ASP B O   
12668 C CB  . ASP B 240 ? 1.2278 1.1765 0.7315 0.0437  0.0763  -0.0933 244 ASP B CB  
12669 C CG  . ASP B 240 ? 1.4183 1.3291 0.8830 0.0439  0.0681  -0.1162 244 ASP B CG  
12670 O OD1 . ASP B 240 ? 1.4726 1.3706 0.9359 0.0305  0.0439  -0.1196 244 ASP B OD1 
12671 O OD2 . ASP B 240 ? 1.5042 1.3975 0.9391 0.0572  0.0863  -0.1308 244 ASP B OD2 
12676 N N   . SER B 241 ? 0.8985 0.9055 0.5332 0.0315  0.0598  -0.0513 245 SER B N   
12677 C CA  . SER B 241 ? 0.9348 0.9627 0.5947 0.0276  0.0606  -0.0312 245 SER B CA  
12678 C C   . SER B 241 ? 0.8415 0.8743 0.5393 0.0227  0.0441  -0.0258 245 SER B C   
12679 O O   . SER B 241 ? 0.8290 0.8545 0.5426 0.0234  0.0382  -0.0362 245 SER B O   
12680 C CB  . SER B 241 ? 0.9951 1.0406 0.6758 0.0335  0.0837  -0.0247 245 SER B CB  
12681 O OG  . SER B 241 ? 0.9901 1.0438 0.7142 0.0367  0.0852  -0.0266 245 SER B OG  
12687 N N   . LEU B 242 ? 0.8075 0.8507 0.5173 0.0183  0.0375  -0.0091 246 LEU B N   
12688 C CA  . LEU B 242 ? 0.7781 0.8276 0.5238 0.0160  0.0252  -0.0030 246 LEU B CA  
12689 C C   . LEU B 242 ? 0.7741 0.8302 0.5561 0.0195  0.0361  -0.0046 246 LEU B C   
12690 O O   . LEU B 242 ? 0.8284 0.8917 0.6151 0.0223  0.0530  -0.0023 246 LEU B O   
12691 C CB  . LEU B 242 ? 0.8100 0.8655 0.5578 0.0139  0.0184  0.0151  246 LEU B CB  
12692 C CG  . LEU B 242 ? 0.8909 0.9477 0.6284 0.0115  -0.0026 0.0196  246 LEU B CG  
12693 C CD1 . LEU B 242 ? 0.9399 1.0003 0.6824 0.0139  -0.0064 0.0386  246 LEU B CD1 
12694 C CD2 . LEU B 242 ? 0.9017 0.9627 0.6636 0.0092  -0.0156 0.0118  246 LEU B CD2 
12706 N N   . HIS B 243 ? 0.7600 0.8162 0.5681 0.0186  0.0261  -0.0077 247 HIS B N   
12707 C CA  . HIS B 243 ? 0.6991 0.7608 0.5407 0.0217  0.0329  -0.0093 247 HIS B CA  
12708 C C   . HIS B 243 ? 0.6855 0.7530 0.5528 0.0187  0.0233  0.0009  247 HIS B C   
12709 O O   . HIS B 243 ? 0.6994 0.7653 0.5767 0.0170  0.0113  -0.0018 247 HIS B O   
12710 C CB  . HIS B 243 ? 0.7187 0.7698 0.5620 0.0249  0.0315  -0.0241 247 HIS B CB  
12711 C CG  . HIS B 243 ? 0.7681 0.8080 0.5817 0.0302  0.0410  -0.0360 247 HIS B CG  
12712 N ND1 . HIS B 243 ? 0.8147 0.8337 0.6090 0.0304  0.0347  -0.0503 247 HIS B ND1 
12713 C CD2 . HIS B 243 ? 0.8210 0.8660 0.6186 0.0356  0.0572  -0.0361 247 HIS B CD2 
12714 C CE1 . HIS B 243 ? 0.8601 0.8691 0.6255 0.0374  0.0466  -0.0599 247 HIS B CE1 
12715 N NE2 . HIS B 243 ? 0.8462 0.8732 0.6140 0.0412  0.0612  -0.0512 247 HIS B NE2 
12724 N N   . LEU B 244 ? 0.7020 0.7749 0.5783 0.0177  0.0292  0.0125  248 LEU B N   
12725 C CA  . LEU B 244 ? 0.6739 0.7472 0.5687 0.0166  0.0218  0.0218  248 LEU B CA  
12726 C C   . LEU B 244 ? 0.6897 0.7674 0.6127 0.0164  0.0274  0.0204  248 LEU B C   
12727 O O   . LEU B 244 ? 0.7263 0.8092 0.6551 0.0141  0.0383  0.0235  248 LEU B O   
12728 C CB  . LEU B 244 ? 0.6835 0.7523 0.5646 0.0150  0.0230  0.0356  248 LEU B CB  
12729 C CG  . LEU B 244 ? 0.7125 0.7781 0.5633 0.0158  0.0166  0.0393  248 LEU B CG  
12730 C CD1 . LEU B 244 ? 0.7291 0.7865 0.5658 0.0153  0.0183  0.0550  248 LEU B CD1 
12731 C CD2 . LEU B 244 ? 0.7081 0.7775 0.5610 0.0179  0.0003  0.0363  248 LEU B CD2 
12743 N N   . LEU B 245 ? 0.6535 0.7309 0.5937 0.0177  0.0194  0.0164  249 LEU B N   
12744 C CA  . LEU B 245 ? 0.6144 0.6950 0.5791 0.0175  0.0217  0.0159  249 LEU B CA  
12745 C C   . LEU B 245 ? 0.6343 0.7099 0.6060 0.0167  0.0158  0.0241  249 LEU B C   
12746 O O   . LEU B 245 ? 0.6627 0.7374 0.6364 0.0193  0.0070  0.0244  249 LEU B O   
12747 C CB  . LEU B 245 ? 0.5990 0.6795 0.5741 0.0201  0.0179  0.0062  249 LEU B CB  
12748 C CG  . LEU B 245 ? 0.6272 0.7110 0.6254 0.0207  0.0185  0.0059  249 LEU B CG  
12749 C CD1 . LEU B 245 ? 0.6392 0.7331 0.6469 0.0207  0.0287  0.0068  249 LEU B CD1 
12750 C CD2 . LEU B 245 ? 0.6479 0.7271 0.6514 0.0232  0.0136  -0.0018 249 LEU B CD2 
12762 N N   . VAL B 246 ? 0.6435 0.7158 0.6181 0.0129  0.0210  0.0309  250 VAL B N   
12763 C CA  . VAL B 246 ? 0.6441 0.7040 0.6184 0.0129  0.0167  0.0383  250 VAL B CA  
12764 C C   . VAL B 246 ? 0.6380 0.6979 0.6310 0.0113  0.0154  0.0348  250 VAL B C   
12765 O O   . VAL B 246 ? 0.6595 0.7224 0.6612 0.0048  0.0200  0.0351  250 VAL B O   
12766 C CB  . VAL B 246 ? 0.7132 0.7619 0.6736 0.0076  0.0219  0.0482  250 VAL B CB  
12767 C CG1 . VAL B 246 ? 0.7537 0.7822 0.7082 0.0103  0.0169  0.0551  250 VAL B CG1 
12768 C CG2 . VAL B 246 ? 0.7445 0.7949 0.6841 0.0087  0.0241  0.0517  250 VAL B CG2 
12778 N N   . PHE B 247 ? 0.6353 0.6943 0.6341 0.0167  0.0087  0.0322  251 PHE B N   
12779 C CA  . PHE B 247 ? 0.6008 0.6582 0.6127 0.0162  0.0067  0.0292  251 PHE B CA  
12780 C C   . PHE B 247 ? 0.6185 0.6578 0.6228 0.0167  0.0055  0.0344  251 PHE B C   
12781 O O   . PHE B 247 ? 0.6399 0.6719 0.6358 0.0244  0.0027  0.0381  251 PHE B O   
12782 C CB  . PHE B 247 ? 0.6105 0.6752 0.6296 0.0211  0.0016  0.0246  251 PHE B CB  
12783 C CG  . PHE B 247 ? 0.6268 0.6895 0.6557 0.0213  -0.0004 0.0224  251 PHE B CG  
12784 C CD1 . PHE B 247 ? 0.6679 0.7223 0.6933 0.0258  -0.0023 0.0250  251 PHE B CD1 
12785 C CD2 . PHE B 247 ? 0.6474 0.7161 0.6872 0.0188  -0.0001 0.0178  251 PHE B CD2 
12786 C CE1 . PHE B 247 ? 0.6635 0.7152 0.6937 0.0260  -0.0036 0.0226  251 PHE B CE1 
12787 C CE2 . PHE B 247 ? 0.6622 0.7287 0.7080 0.0189  -0.0029 0.0166  251 PHE B CE2 
12788 C CZ  . PHE B 247 ? 0.6563 0.7141 0.6962 0.0217  -0.0045 0.0187  251 PHE B CZ  
12798 N N   . VAL B 248 ? 0.6260 0.6579 0.6327 0.0087  0.0072  0.0347  252 VAL B N   
12799 C CA  . VAL B 248 ? 0.6405 0.6477 0.6346 0.0065  0.0063  0.0387  252 VAL B CA  
12800 C C   . VAL B 248 ? 0.6475 0.6501 0.6474 0.0047  0.0027  0.0335  252 VAL B C   
12801 O O   . VAL B 248 ? 0.6751 0.6874 0.6862 -0.0045 0.0020  0.0309  252 VAL B O   
12802 C CB  . VAL B 248 ? 0.6671 0.6655 0.6540 -0.0057 0.0103  0.0445  252 VAL B CB  
12803 C CG1 . VAL B 248 ? 0.7193 0.6840 0.6885 -0.0092 0.0084  0.0482  252 VAL B CG1 
12804 C CG2 . VAL B 248 ? 0.6912 0.6952 0.6695 -0.0038 0.0146  0.0500  252 VAL B CG2 
12814 N N   . SER B 249 ? 0.6307 0.6202 0.6224 0.0142  0.0005  0.0324  253 SER B N   
12815 C CA  . SER B 249 ? 0.6883 0.6711 0.6800 0.0137  -0.0024 0.0272  253 SER B CA  
12816 C C   . SER B 249 ? 0.7225 0.6814 0.6963 0.0248  -0.0019 0.0276  253 SER B C   
12817 O O   . SER B 249 ? 0.7835 0.7378 0.7504 0.0354  0.0001  0.0322  253 SER B O   
12818 C CB  . SER B 249 ? 0.6847 0.6910 0.6925 0.0168  -0.0039 0.0232  253 SER B CB  
12819 O OG  . SER B 249 ? 0.6974 0.6967 0.7019 0.0168  -0.0067 0.0193  253 SER B OG  
12825 N N   . ASP B 250 ? 0.6657 0.6095 0.6308 0.0234  -0.0038 0.0226  254 ASP B N   
12826 C CA  . ASP B 250 ? 0.7085 0.6281 0.6542 0.0360  -0.0018 0.0210  254 ASP B CA  
12827 C C   . ASP B 250 ? 0.7169 0.6478 0.6659 0.0422  -0.0014 0.0162  254 ASP B C   
12828 O O   . ASP B 250 ? 0.7202 0.6290 0.6502 0.0486  0.0001  0.0122  254 ASP B O   
12829 C CB  . ASP B 250 ? 0.7387 0.6177 0.6595 0.0285  -0.0036 0.0191  254 ASP B CB  
12830 C CG  . ASP B 250 ? 0.7772 0.6536 0.6974 0.0123  -0.0095 0.0131  254 ASP B CG  
12831 O OD1 . ASP B 250 ? 0.7751 0.6816 0.7151 0.0086  -0.0118 0.0116  254 ASP B OD1 
12832 O OD2 . ASP B 250 ? 0.8274 0.6700 0.7259 0.0031  -0.0127 0.0104  254 ASP B OD2 
12837 N N   . ALA B 251 ? 0.7160 0.6784 0.6861 0.0404  -0.0023 0.0166  255 ALA B N   
12838 C CA  . ALA B 251 ? 0.7141 0.6874 0.6870 0.0438  -0.0019 0.0138  255 ALA B CA  
12839 C C   . ALA B 251 ? 0.6927 0.6968 0.6862 0.0465  -0.0008 0.0171  255 ALA B C   
12840 O O   . ALA B 251 ? 0.7211 0.7379 0.7266 0.0423  -0.0023 0.0194  255 ALA B O   
12841 C CB  . ALA B 251 ? 0.7258 0.6963 0.6978 0.0316  -0.0077 0.0097  255 ALA B CB  
12847 N N   . ASP B 252 ? 0.7154 0.7301 0.7103 0.0524  0.0020  0.0174  256 ASP B N   
12848 C CA  . ASP B 252 ? 0.7070 0.7481 0.7199 0.0508  0.0019  0.0206  256 ASP B CA  
12849 C C   . ASP B 252 ? 0.6270 0.6721 0.6485 0.0395  -0.0033 0.0188  256 ASP B C   
12850 O O   . ASP B 252 ? 0.6299 0.6636 0.6465 0.0339  -0.0068 0.0159  256 ASP B O   
12851 C CB  . ASP B 252 ? 0.8071 0.8592 0.8193 0.0575  0.0070  0.0226  256 ASP B CB  
12852 C CG  . ASP B 252 ? 0.9665 1.0033 0.9626 0.0569  0.0078  0.0190  256 ASP B CG  
12853 O OD1 . ASP B 252 ? 1.0413 1.0546 1.0223 0.0548  0.0050  0.0143  256 ASP B OD1 
12854 O OD2 . ASP B 252 ? 1.0218 1.0696 1.0187 0.0570  0.0108  0.0211  256 ASP B OD2 
12859 N N   . SER B 253 ? 0.6265 0.6880 0.6609 0.0364  -0.0043 0.0208  257 SER B N   
12860 C CA  . SER B 253 ? 0.6268 0.6900 0.6687 0.0292  -0.0085 0.0192  257 SER B CA  
12861 C C   . SER B 253 ? 0.6573 0.7243 0.7012 0.0267  -0.0094 0.0212  257 SER B C   
12862 O O   . SER B 253 ? 0.6808 0.7573 0.7266 0.0273  -0.0066 0.0246  257 SER B O   
12863 C CB  . SER B 253 ? 0.6035 0.6742 0.6533 0.0269  -0.0094 0.0188  257 SER B CB  
12864 O OG  . SER B 253 ? 0.6151 0.6809 0.6617 0.0277  -0.0085 0.0180  257 SER B OG  
12870 N N   . HIS B 254 ? 0.7022 0.7633 0.7464 0.0237  -0.0134 0.0201  258 HIS B N   
12871 C CA  . HIS B 254 ? 0.6754 0.7359 0.7203 0.0210  -0.0152 0.0230  258 HIS B CA  
12872 C C   . HIS B 254 ? 0.6000 0.6634 0.6525 0.0175  -0.0158 0.0231  258 HIS B C   
12873 O O   . HIS B 254 ? 0.5678 0.6325 0.6245 0.0179  -0.0160 0.0196  258 HIS B O   
12874 C CB  . HIS B 254 ? 0.6783 0.7320 0.7221 0.0211  -0.0206 0.0227  258 HIS B CB  
12875 C CG  . HIS B 254 ? 0.6963 0.7449 0.7278 0.0217  -0.0224 0.0235  258 HIS B CG  
12876 N ND1 . HIS B 254 ? 0.7189 0.7655 0.7391 0.0220  -0.0193 0.0270  258 HIS B ND1 
12877 C CD2 . HIS B 254 ? 0.6976 0.7425 0.7245 0.0209  -0.0271 0.0212  258 HIS B CD2 
12878 C CE1 . HIS B 254 ? 0.7362 0.7755 0.7423 0.0227  -0.0218 0.0259  258 HIS B CE1 
12879 N NE2 . HIS B 254 ? 0.7146 0.7522 0.7246 0.0211  -0.0276 0.0222  258 HIS B NE2 
12888 N N   . PHE B 255 ? 0.6100 0.6724 0.6614 0.0129  -0.0160 0.0271  259 PHE B N   
12889 C CA  . PHE B 255 ? 0.6123 0.6718 0.6668 0.0069  -0.0179 0.0266  259 PHE B CA  
12890 C C   . PHE B 255 ? 0.5768 0.6234 0.6260 0.0018  -0.0201 0.0311  259 PHE B C   
12891 O O   . PHE B 255 ? 0.4972 0.5439 0.5413 0.0016  -0.0187 0.0365  259 PHE B O   
12892 C CB  . PHE B 255 ? 0.6551 0.7308 0.7149 0.0022  -0.0162 0.0283  259 PHE B CB  
12893 C CG  . PHE B 255 ? 0.7062 0.7957 0.7675 0.0000  -0.0122 0.0352  259 PHE B CG  
12894 C CD1 . PHE B 255 ? 0.7197 0.8179 0.7793 0.0086  -0.0071 0.0362  259 PHE B CD1 
12895 C CD2 . PHE B 255 ? 0.7445 0.8371 0.8075 -0.0108 -0.0127 0.0407  259 PHE B CD2 
12896 C CE1 . PHE B 255 ? 0.7355 0.8480 0.7956 0.0091  -0.0012 0.0422  259 PHE B CE1 
12897 C CE2 . PHE B 255 ? 0.7502 0.8604 0.8162 -0.0130 -0.0071 0.0481  259 PHE B CE2 
12898 C CZ  . PHE B 255 ? 0.7422 0.8637 0.8070 -0.0017 -0.0006 0.0486  259 PHE B CZ  
12908 N N   . GLY B 256 ? 0.6092 0.6415 0.6563 -0.0020 -0.0232 0.0288  260 GLY B N   
12909 C CA  . GLY B 256 ? 0.6696 0.6830 0.7088 -0.0081 -0.0257 0.0335  260 GLY B CA  
12910 C C   . GLY B 256 ? 0.6408 0.6457 0.6738 -0.0030 -0.0267 0.0392  260 GLY B C   
12911 O O   . GLY B 256 ? 0.6012 0.6025 0.6350 0.0073  -0.0290 0.0368  260 GLY B O   
12915 N N   . MET B 257 ? 0.6443 0.6489 0.6713 -0.0106 -0.0251 0.0476  261 MET B N   
12916 C CA  . MET B 257 ? 0.6581 0.6498 0.6740 -0.0078 -0.0270 0.0548  261 MET B CA  
12917 C C   . MET B 257 ? 0.6108 0.6170 0.6243 -0.0010 -0.0252 0.0556  261 MET B C   
12918 O O   . MET B 257 ? 0.6135 0.6129 0.6146 -0.0005 -0.0263 0.0625  261 MET B O   
12919 C CB  . MET B 257 ? 0.6712 0.6536 0.6782 -0.0210 -0.0254 0.0646  261 MET B CB  
12920 C CG  . MET B 257 ? 0.6966 0.6552 0.7000 -0.0300 -0.0291 0.0638  261 MET B CG  
12921 S SD  . MET B 257 ? 0.6623 0.6382 0.6782 -0.0414 -0.0280 0.0570  261 MET B SD  
12922 C CE  . MET B 257 ? 0.6768 0.6721 0.6954 -0.0601 -0.0231 0.0691  261 MET B CE  
12932 N N   . ASP B 258 ? 0.5793 0.6018 0.6008 0.0038  -0.0230 0.0488  262 ASP B N   
12933 C CA  . ASP B 258 ? 0.6564 0.6846 0.6718 0.0100  -0.0233 0.0475  262 ASP B CA  
12934 C C   . ASP B 258 ? 0.6927 0.7103 0.7039 0.0156  -0.0314 0.0485  262 ASP B C   
12935 O O   . ASP B 258 ? 0.7093 0.7254 0.7084 0.0173  -0.0342 0.0515  262 ASP B O   
12936 C CB  . ASP B 258 ? 0.6671 0.7070 0.6904 0.0138  -0.0210 0.0399  262 ASP B CB  
12937 C CG  . ASP B 258 ? 0.6857 0.7391 0.7108 0.0122  -0.0133 0.0403  262 ASP B CG  
12938 O OD1 . ASP B 258 ? 0.6876 0.7461 0.7095 0.0076  -0.0089 0.0466  262 ASP B OD1 
12939 O OD2 . ASP B 258 ? 0.6643 0.7246 0.6947 0.0159  -0.0114 0.0354  262 ASP B OD2 
12944 N N   . SER B 259 ? 0.6689 0.6803 0.6894 0.0195  -0.0354 0.0462  263 SER B N   
12945 C CA  . SER B 259 ? 0.6535 0.6604 0.6749 0.0274  -0.0432 0.0480  263 SER B CA  
12946 C C   . SER B 259 ? 0.6569 0.6485 0.6634 0.0278  -0.0476 0.0577  263 SER B C   
12947 O O   . SER B 259 ? 0.6782 0.6691 0.6833 0.0350  -0.0555 0.0611  263 SER B O   
12948 C CB  . SER B 259 ? 0.6959 0.6989 0.7295 0.0338  -0.0439 0.0437  263 SER B CB  
12949 O OG  . SER B 259 ? 0.7421 0.7237 0.7688 0.0321  -0.0430 0.0464  263 SER B OG  
12955 N N   . LYS B 260 ? 0.6266 0.6079 0.6224 0.0196  -0.0430 0.0633  264 LYS B N   
12956 C CA  . LYS B 260 ? 0.6454 0.6097 0.6240 0.0184  -0.0462 0.0743  264 LYS B CA  
12957 C C   . LYS B 260 ? 0.6488 0.6203 0.6146 0.0213  -0.0504 0.0778  264 LYS B C   
12958 O O   . LYS B 260 ? 0.6226 0.5816 0.5749 0.0248  -0.0571 0.0866  264 LYS B O   
12959 C CB  . LYS B 260 ? 0.6655 0.6231 0.6361 0.0056  -0.0388 0.0803  264 LYS B CB  
12960 C CG  . LYS B 260 ? 0.6945 0.6332 0.6446 0.0015  -0.0404 0.0936  264 LYS B CG  
12961 C CD  . LYS B 260 ? 0.7421 0.6773 0.6886 -0.0144 -0.0325 0.0999  264 LYS B CD  
12962 C CE  . LYS B 260 ? 0.8064 0.7334 0.7312 -0.0212 -0.0298 0.1139  264 LYS B CE  
12963 N NZ  . LYS B 260 ? 0.8635 0.7550 0.7725 -0.0211 -0.0369 0.1242  264 LYS B NZ  
12977 N N   . LEU B 261 ? 0.6467 0.6352 0.6136 0.0201  -0.0472 0.0710  265 LEU B N   
12978 C CA  . LEU B 261 ? 0.6757 0.6676 0.6268 0.0220  -0.0525 0.0719  265 LEU B CA  
12979 C C   . LEU B 261 ? 0.6730 0.6672 0.6302 0.0294  -0.0656 0.0723  265 LEU B C   
12980 O O   . LEU B 261 ? 0.6764 0.6685 0.6177 0.0309  -0.0741 0.0774  265 LEU B O   
12981 C CB  . LEU B 261 ? 0.6858 0.6893 0.6352 0.0200  -0.0467 0.0628  265 LEU B CB  
12982 C CG  . LEU B 261 ? 0.7408 0.7487 0.6860 0.0159  -0.0333 0.0625  265 LEU B CG  
12983 C CD1 . LEU B 261 ? 0.7673 0.7799 0.7018 0.0180  -0.0290 0.0547  265 LEU B CD1 
12984 C CD2 . LEU B 261 ? 0.7696 0.7710 0.6987 0.0115  -0.0285 0.0735  265 LEU B CD2 
12996 N N   . ALA B 262 ? 0.6322 0.6334 0.6123 0.0343  -0.0675 0.0675  266 ALA B N   
12997 C CA  . ALA B 262 ? 0.6014 0.6125 0.5937 0.0425  -0.0786 0.0684  266 ALA B CA  
12998 C C   . ALA B 262 ? 0.6233 0.6209 0.6171 0.0525  -0.0833 0.0769  266 ALA B C   
12999 O O   . ALA B 262 ? 0.6367 0.6452 0.6446 0.0628  -0.0915 0.0786  266 ALA B O   
13000 C CB  . ALA B 262 ? 0.5312 0.5601 0.5474 0.0434  -0.0763 0.0591  266 ALA B CB  
13006 N N   . GLY B 263 ? 0.6359 0.6100 0.6157 0.0499  -0.0783 0.0829  267 GLY B N   
13007 C CA  . GLY B 263 ? 0.7207 0.6733 0.6974 0.0593  -0.0823 0.0909  267 GLY B CA  
13008 C C   . GLY B 263 ? 0.7189 0.6641 0.7113 0.0657  -0.0776 0.0845  267 GLY B C   
13009 O O   . GLY B 263 ? 0.7560 0.6845 0.7484 0.0784  -0.0816 0.0890  267 GLY B O   
13013 N N   . ILE B 264 ? 0.6940 0.6496 0.6974 0.0586  -0.0691 0.0741  268 ILE B N   
13014 C CA  . ILE B 264 ? 0.7216 0.6708 0.7364 0.0635  -0.0640 0.0664  268 ILE B CA  
13015 C C   . ILE B 264 ? 0.7838 0.7091 0.7857 0.0513  -0.0578 0.0663  268 ILE B C   
13016 O O   . ILE B 264 ? 0.7551 0.6914 0.7578 0.0387  -0.0521 0.0628  268 ILE B O   
13017 C CB  . ILE B 264 ? 0.6402 0.6177 0.6742 0.0630  -0.0600 0.0561  268 ILE B CB  
13018 C CG1 . ILE B 264 ? 0.5719 0.5754 0.6198 0.0712  -0.0673 0.0575  268 ILE B CG1 
13019 C CG2 . ILE B 264 ? 0.6356 0.6058 0.6770 0.0679  -0.0539 0.0480  268 ILE B CG2 
13020 C CD1 . ILE B 264 ? 0.5535 0.5842 0.6189 0.0677  -0.0638 0.0492  268 ILE B CD1 
13032 N N   . VAL B 265 ? 0.8252 0.7174 0.8149 0.0550  -0.0594 0.0708  269 VAL B N   
13033 C CA  . VAL B 265 ? 0.7950 0.6615 0.7701 0.0399  -0.0556 0.0728  269 VAL B CA  
13034 C C   . VAL B 265 ? 0.8512 0.6876 0.8214 0.0442  -0.0546 0.0662  269 VAL B C   
13035 O O   . VAL B 265 ? 0.9543 0.7558 0.9068 0.0348  -0.0550 0.0702  269 VAL B O   
13036 C CB  . VAL B 265 ? 0.7737 0.6197 0.7287 0.0338  -0.0588 0.0872  269 VAL B CB  
13037 C CG1 . VAL B 265 ? 0.7472 0.6209 0.7017 0.0260  -0.0572 0.0918  269 VAL B CG1 
13038 C CG2 . VAL B 265 ? 0.8003 0.6253 0.7474 0.0520  -0.0668 0.0947  269 VAL B CG2 
13048 N N   . CYS B 266 ? 0.8244 0.6720 0.8079 0.0574  -0.0528 0.0560  270 CYS B N   
13049 C CA  . CYS B 266 ? 0.8716 0.6916 0.8476 0.0622  -0.0501 0.0470  270 CYS B CA  
13050 C C   . CYS B 266 ? 0.8296 0.6701 0.8147 0.0527  -0.0446 0.0355  270 CYS B C   
13051 O O   . CYS B 266 ? 0.8173 0.6919 0.8203 0.0589  -0.0419 0.0310  270 CYS B O   
13052 C CB  . CYS B 266 ? 0.9100 0.7248 0.8912 0.0881  -0.0509 0.0449  270 CYS B CB  
13053 S SG  . CYS B 266 ? 1.0072 0.8067 0.9814 0.1034  -0.0596 0.0605  270 CYS B SG  
13058 N N   . PRO B 267 ? 0.8170 0.6386 0.7900 0.0365  -0.0436 0.0313  271 PRO B N   
13059 C CA  . PRO B 267 ? 0.7923 0.6376 0.7737 0.0264  -0.0400 0.0226  271 PRO B CA  
13060 C C   . PRO B 267 ? 0.7735 0.6288 0.7618 0.0415  -0.0357 0.0117  271 PRO B C   
13061 O O   . PRO B 267 ? 0.8280 0.6629 0.8101 0.0580  -0.0345 0.0079  271 PRO B O   
13062 C CB  . PRO B 267 ? 0.8548 0.6717 0.8188 0.0075  -0.0422 0.0205  271 PRO B CB  
13063 C CG  . PRO B 267 ? 0.8745 0.6613 0.8244 0.0017  -0.0460 0.0315  271 PRO B CG  
13064 C CD  . PRO B 267 ? 0.8669 0.6445 0.8171 0.0249  -0.0468 0.0353  271 PRO B CD  
13072 N N   . ASN B 268 ? 0.7220 0.6094 0.7227 0.0365  -0.0325 0.0074  272 ASN B N   
13073 C CA  . ASN B 268 ? 0.7336 0.6317 0.7385 0.0467  -0.0272 -0.0023 272 ASN B CA  
13074 C C   . ASN B 268 ? 0.7668 0.6294 0.7502 0.0474  -0.0263 -0.0120 272 ASN B C   
13075 O O   . ASN B 268 ? 0.8179 0.6561 0.7854 0.0321  -0.0307 -0.0127 272 ASN B O   
13076 C CB  . ASN B 268 ? 0.7617 0.6924 0.7775 0.0375  -0.0250 -0.0039 272 ASN B CB  
13077 C CG  . ASN B 268 ? 0.7980 0.7460 0.8207 0.0481  -0.0187 -0.0106 272 ASN B CG  
13078 O OD1 . ASN B 268 ? 0.7711 0.7081 0.7819 0.0490  -0.0156 -0.0191 272 ASN B OD1 
13079 N ND2 . ASN B 268 ? 0.8448 0.8199 0.8853 0.0547  -0.0169 -0.0065 272 ASN B ND2 
13086 N N   . ASP B 269 ? 0.7547 0.6148 0.7366 0.0648  -0.0203 -0.0198 273 ASP B N   
13087 C CA  . ASP B 269 ? 0.8031 0.6250 0.7599 0.0696  -0.0182 -0.0309 273 ASP B CA  
13088 C C   . ASP B 269 ? 0.7665 0.6000 0.7173 0.0678  -0.0128 -0.0415 273 ASP B C   
13089 O O   . ASP B 269 ? 0.8313 0.6331 0.7575 0.0723  -0.0102 -0.0526 273 ASP B O   
13090 C CB  . ASP B 269 ? 0.8934 0.6960 0.8472 0.0951  -0.0140 -0.0320 273 ASP B CB  
13091 C CG  . ASP B 269 ? 0.9541 0.7974 0.9317 0.1136  -0.0059 -0.0319 273 ASP B CG  
13092 O OD1 . ASP B 269 ? 0.9592 0.8411 0.9534 0.1050  -0.0039 -0.0306 273 ASP B OD1 
13093 O OD2 . ASP B 269 ? 0.9988 0.8358 0.9787 0.1367  -0.0014 -0.0325 273 ASP B OD2 
13098 N N   . GLY B 270 ? 0.7209 0.5951 0.6896 0.0617  -0.0110 -0.0385 274 GLY B N   
13099 C CA  . GLY B 270 ? 0.7465 0.6312 0.7073 0.0591  -0.0065 -0.0466 274 GLY B CA  
13100 C C   . GLY B 270 ? 0.7466 0.6281 0.7004 0.0787  0.0042  -0.0552 274 GLY B C   
13101 O O   . GLY B 270 ? 0.7762 0.6524 0.7120 0.0772  0.0081  -0.0642 274 GLY B O   
13105 N N   . LEU B 271 ? 0.7439 0.6307 0.7113 0.0978  0.0092  -0.0521 275 LEU B N   
13106 C CA  . LEU B 271 ? 0.7547 0.6457 0.7206 0.1195  0.0213  -0.0587 275 LEU B CA  
13107 C C   . LEU B 271 ? 0.7429 0.6851 0.7406 0.1252  0.0277  -0.0512 275 LEU B C   
13108 O O   . LEU B 271 ? 0.7180 0.6846 0.7380 0.1169  0.0216  -0.0409 275 LEU B O   
13109 C CB  . LEU B 271 ? 0.7686 0.6285 0.7270 0.1398  0.0226  -0.0604 275 LEU B CB  
13110 C CG  . LEU B 271 ? 0.7891 0.5901 0.7127 0.1338  0.0160  -0.0677 275 LEU B CG  
13111 C CD1 . LEU B 271 ? 0.8057 0.5751 0.7233 0.1560  0.0170  -0.0667 275 LEU B CD1 
13112 C CD2 . LEU B 271 ? 0.7858 0.5629 0.6772 0.1303  0.0207  -0.0827 275 LEU B CD2 
13124 N N   . CYS B 272 ? 0.7735 0.7310 0.7713 0.1387  0.0405  -0.0565 276 CYS B N   
13125 C CA  . CYS B 272 ? 0.7764 0.7833 0.8043 0.1425  0.0475  -0.0490 276 CYS B CA  
13126 C C   . CYS B 272 ? 0.7522 0.7767 0.8063 0.1590  0.0470  -0.0416 276 CYS B C   
13127 O O   . CYS B 272 ? 0.8020 0.8071 0.8492 0.1798  0.0509  -0.0457 276 CYS B O   
13128 C CB  . CYS B 272 ? 0.8328 0.8531 0.8524 0.1511  0.0628  -0.0558 276 CYS B CB  
13129 S SG  . CYS B 272 ? 0.8143 0.8964 0.8700 0.1494  0.0718  -0.0452 276 CYS B SG  
13134 N N   . HIS B 273 ? 0.6812 0.7406 0.7635 0.1503  0.0413  -0.0307 277 HIS B N   
13135 C CA  . HIS B 273 ? 0.6599 0.7416 0.7687 0.1627  0.0376  -0.0220 277 HIS B CA  
13136 C C   . HIS B 273 ? 0.6188 0.7538 0.7593 0.1570  0.0404  -0.0140 277 HIS B C   
13137 O O   . HIS B 273 ? 0.6273 0.7824 0.7872 0.1493  0.0305  -0.0050 277 HIS B O   
13138 C CB  . HIS B 273 ? 0.7049 0.7661 0.8109 0.1547  0.0226  -0.0158 277 HIS B CB  
13139 C CG  . HIS B 273 ? 0.7645 0.7747 0.8430 0.1610  0.0193  -0.0211 277 HIS B CG  
13140 N ND1 . HIS B 273 ? 0.7908 0.7823 0.8646 0.1850  0.0224  -0.0228 277 HIS B ND1 
13141 C CD2 . HIS B 273 ? 0.7821 0.7555 0.8359 0.1457  0.0131  -0.0244 277 HIS B CD2 
13142 C CE1 . HIS B 273 ? 0.8135 0.7534 0.8580 0.1829  0.0179  -0.0274 277 HIS B CE1 
13143 N NE2 . HIS B 273 ? 0.8163 0.7468 0.8496 0.1579  0.0120  -0.0282 277 HIS B NE2 
13151 N N   . LEU B 274 ? 0.6198 0.7768 0.7634 0.1591  0.0540  -0.0171 278 LEU B N   
13152 C CA  . LEU B 274 ? 0.6449 0.8530 0.8186 0.1526  0.0584  -0.0089 278 LEU B CA  
13153 C C   . LEU B 274 ? 0.6763 0.9191 0.8771 0.1757  0.0656  -0.0052 278 LEU B C   
13154 O O   . LEU B 274 ? 0.7155 0.9526 0.9077 0.1967  0.0788  -0.0120 278 LEU B O   
13155 C CB  . LEU B 274 ? 0.6556 0.8716 0.8185 0.1416  0.0699  -0.0120 278 LEU B CB  
13156 C CG  . LEU B 274 ? 0.6495 0.8395 0.7902 0.1196  0.0625  -0.0133 278 LEU B CG  
13157 C CD1 . LEU B 274 ? 0.6510 0.8496 0.7802 0.1114  0.0739  -0.0147 278 LEU B CD1 
13158 C CD2 . LEU B 274 ? 0.6539 0.8535 0.8096 0.1025  0.0491  -0.0047 278 LEU B CD2 
13170 N N   . ASP B 275 ? 0.6947 0.9738 0.9272 0.1725  0.0567  0.0054  279 ASP B N   
13171 C CA  . ASP B 275 ? 0.7390 1.0569 1.0023 0.1948  0.0602  0.0113  279 ASP B CA  
13172 C C   . ASP B 275 ? 0.7232 1.0968 1.0136 0.1928  0.0746  0.0157  279 ASP B C   
13173 O O   . ASP B 275 ? 0.6795 1.0531 0.9583 0.1774  0.0837  0.0129  279 ASP B O   
13174 C CB  . ASP B 275 ? 0.7531 1.0847 1.0363 0.1917  0.0417  0.0213  279 ASP B CB  
13175 C CG  . ASP B 275 ? 0.7384 1.0951 1.0356 0.1620  0.0316  0.0283  279 ASP B CG  
13176 O OD1 . ASP B 275 ? 0.7401 1.1109 1.0380 0.1456  0.0401  0.0275  279 ASP B OD1 
13177 O OD2 . ASP B 275 ? 0.7257 1.0848 1.0299 0.1550  0.0150  0.0347  279 ASP B OD2 
13182 N N   . SER B 276 ? 0.8005 1.2246 1.1282 0.2085  0.0766  0.0240  280 SER B N   
13183 C CA  . SER B 276 ? 0.8506 1.3338 1.2077 0.2084  0.0922  0.0294  280 SER B CA  
13184 C C   . SER B 276 ? 0.9159 1.4217 1.2826 0.1725  0.0877  0.0361  280 SER B C   
13185 O O   . SER B 276 ? 0.9790 1.5085 1.3493 0.1634  0.1028  0.0373  280 SER B O   
13186 C CB  . SER B 276 ? 0.8176 1.3568 1.2181 0.2308  0.0921  0.0390  280 SER B CB  
13187 O OG  . SER B 276 ? 0.7977 1.3429 1.2136 0.2232  0.0693  0.0472  280 SER B OG  
13193 N N   . LYS B 277 ? 0.8878 1.3837 1.2558 0.1519  0.0674  0.0406  281 LYS B N   
13194 C CA  . LYS B 277 ? 0.8388 1.3435 1.2087 0.1179  0.0616  0.0456  281 LYS B CA  
13195 C C   . LYS B 277 ? 0.7650 1.2173 1.0940 0.1035  0.0641  0.0376  281 LYS B C   
13196 O O   . LYS B 277 ? 0.7103 1.1569 1.0336 0.0772  0.0578  0.0409  281 LYS B O   
13197 C CB  . LYS B 277 ? 0.8873 1.3984 1.2700 0.1031  0.0389  0.0523  281 LYS B CB  
13198 C CG  . LYS B 277 ? 0.9588 1.5321 1.3864 0.1108  0.0334  0.0630  281 LYS B CG  
13199 C CD  . LYS B 277 ? 1.0291 1.5979 1.4606 0.1045  0.0093  0.0674  281 LYS B CD  
13200 C CE  . LYS B 277 ? 1.0877 1.6393 1.5052 0.0694  -0.0037 0.0681  281 LYS B CE  
13201 N NZ  . LYS B 277 ? 1.1206 1.6691 1.5390 0.0633  -0.0267 0.0719  281 LYS B NZ  
13215 N N   . ASN B 278 ? 0.7603 1.1741 1.0604 0.1204  0.0726  0.0274  282 ASN B N   
13216 C CA  . ASN B 278 ? 0.7324 1.0981 0.9944 0.1087  0.0727  0.0200  282 ASN B CA  
13217 C C   . ASN B 278 ? 0.6664 1.0022 0.9167 0.0922  0.0541  0.0209  282 ASN B C   
13218 O O   . ASN B 278 ? 0.6569 0.9733 0.8900 0.0734  0.0514  0.0207  282 ASN B O   
13219 C CB  . ASN B 278 ? 0.7903 1.1692 1.0470 0.0928  0.0851  0.0225  282 ASN B CB  
13220 C CG  . ASN B 278 ? 0.8750 1.2527 1.1166 0.1097  0.1047  0.0158  282 ASN B CG  
13221 O OD1 . ASN B 278 ? 0.8899 1.2423 1.1152 0.1309  0.1076  0.0064  282 ASN B OD1 
13222 N ND2 . ASN B 278 ? 0.9300 1.3316 1.1733 0.0994  0.1183  0.0204  282 ASN B ND2 
13229 N N   . GLU B 279 ? 0.6602 0.9919 0.9186 0.1009  0.0418  0.0223  283 GLU B N   
13230 C CA  . GLU B 279 ? 0.6878 0.9903 0.9326 0.0891  0.0257  0.0226  283 GLU B CA  
13231 C C   . GLU B 279 ? 0.6546 0.9163 0.8773 0.1040  0.0225  0.0162  283 GLU B C   
13232 O O   . GLU B 279 ? 0.6818 0.9437 0.9085 0.1256  0.0269  0.0143  283 GLU B O   
13233 C CB  . GLU B 279 ? 0.7851 1.1156 1.0541 0.0825  0.0119  0.0310  283 GLU B CB  
13234 C CG  . GLU B 279 ? 0.9023 1.2678 1.1904 0.0614  0.0114  0.0377  283 GLU B CG  
13235 C CD  . GLU B 279 ? 0.9858 1.3704 1.2901 0.0501  -0.0059 0.0444  283 GLU B CD  
13236 O OE1 . GLU B 279 ? 1.0035 1.3684 1.2986 0.0571  -0.0177 0.0438  283 GLU B OE1 
13237 O OE2 . GLU B 279 ? 1.0048 1.4234 1.3292 0.0328  -0.0080 0.0507  283 GLU B OE2 
13244 N N   . TYR B 280 ? 0.6049 0.8313 0.8042 0.0924  0.0152  0.0134  284 TYR B N   
13245 C CA  . TYR B 280 ? 0.6214 0.8090 0.7994 0.1008  0.0109  0.0089  284 TYR B CA  
13246 C C   . TYR B 280 ? 0.6353 0.8256 0.8239 0.1114  0.0007  0.0144  284 TYR B C   
13247 O O   . TYR B 280 ? 0.6414 0.8370 0.8344 0.1011  -0.0107 0.0200  284 TYR B O   
13248 C CB  . TYR B 280 ? 0.6115 0.7713 0.7680 0.0843  0.0054  0.0069  284 TYR B CB  
13249 C CG  . TYR B 280 ? 0.6277 0.7508 0.7638 0.0878  0.0006  0.0038  284 TYR B CG  
13250 C CD1 . TYR B 280 ? 0.6665 0.7681 0.7902 0.1010  0.0059  -0.0022 284 TYR B CD1 
13251 C CD2 . TYR B 280 ? 0.6160 0.7247 0.7433 0.0771  -0.0086 0.0069  284 TYR B CD2 
13252 C CE1 . TYR B 280 ? 0.7070 0.7730 0.8111 0.1006  0.0008  -0.0043 284 TYR B CE1 
13253 C CE2 . TYR B 280 ? 0.6245 0.7029 0.7346 0.0777  -0.0122 0.0056  284 TYR B CE2 
13254 C CZ  . TYR B 280 ? 0.6993 0.7561 0.7983 0.0881  -0.0082 0.0004  284 TYR B CZ  
13255 O OH  . TYR B 280 ? 0.7321 0.7568 0.8133 0.0854  -0.0125 -0.0002 284 TYR B OH  
13265 N N   . SER B 281 ? 0.6623 0.8464 0.8521 0.1330  0.0047  0.0128  285 SER B N   
13266 C CA  . SER B 281 ? 0.6724 0.8633 0.8745 0.1467  -0.0046 0.0199  285 SER B CA  
13267 C C   . SER B 281 ? 0.6573 0.8080 0.8369 0.1436  -0.0153 0.0214  285 SER B C   
13268 O O   . SER B 281 ? 0.7005 0.8573 0.8869 0.1465  -0.0267 0.0294  285 SER B O   
13269 C CB  . SER B 281 ? 0.7110 0.9082 0.9218 0.1744  0.0044  0.0184  285 SER B CB  
13270 O OG  . SER B 281 ? 0.7462 0.8995 0.9283 0.1826  0.0125  0.0085  285 SER B OG  
13276 N N   . MET B 282 ? 0.6626 0.7744 0.8154 0.1368  -0.0123 0.0146  286 MET B N   
13277 C CA  . MET B 282 ? 0.7024 0.7776 0.8342 0.1317  -0.0207 0.0168  286 MET B CA  
13278 C C   . MET B 282 ? 0.6496 0.7277 0.7770 0.1104  -0.0275 0.0199  286 MET B C   
13279 O O   . MET B 282 ? 0.6938 0.7441 0.8025 0.1024  -0.0314 0.0209  286 MET B O   
13280 C CB  . MET B 282 ? 0.7442 0.7780 0.8503 0.1327  -0.0150 0.0085  286 MET B CB  
13281 C CG  . MET B 282 ? 0.7831 0.8041 0.8858 0.1554  -0.0072 0.0033  286 MET B CG  
13282 S SD  . MET B 282 ? 0.8313 0.8431 0.9394 0.1792  -0.0141 0.0122  286 MET B SD  
13283 C CE  . MET B 282 ? 0.8800 0.8277 0.9517 0.1720  -0.0201 0.0118  286 MET B CE  
13293 N N   . SER B 283 ? 0.5949 0.7050 0.7380 0.1009  -0.0285 0.0216  287 SER B N   
13294 C CA  . SER B 283 ? 0.6033 0.7121 0.7388 0.0830  -0.0339 0.0233  287 SER B CA  
13295 C C   . SER B 283 ? 0.5402 0.6359 0.6661 0.0824  -0.0444 0.0299  287 SER B C   
13296 O O   . SER B 283 ? 0.5276 0.6058 0.6368 0.0717  -0.0460 0.0302  287 SER B O   
13297 C CB  . SER B 283 ? 0.6448 0.7856 0.7968 0.0737  -0.0347 0.0246  287 SER B CB  
13298 O OG  . SER B 283 ? 0.7042 0.8380 0.8448 0.0583  -0.0395 0.0250  287 SER B OG  
13304 N N   . THR B 284 ? 0.5736 0.6792 0.7094 0.0946  -0.0512 0.0362  288 THR B N   
13305 C CA  . THR B 284 ? 0.5778 0.6723 0.7028 0.0950  -0.0621 0.0440  288 THR B CA  
13306 C C   . THR B 284 ? 0.5711 0.6318 0.6807 0.1063  -0.0620 0.0470  288 THR B C   
13307 O O   . THR B 284 ? 0.5753 0.6248 0.6748 0.1092  -0.0708 0.0553  288 THR B O   
13308 C CB  . THR B 284 ? 0.5888 0.7156 0.7328 0.1007  -0.0725 0.0509  288 THR B CB  
13309 O OG1 . THR B 284 ? 0.6300 0.7696 0.7920 0.1210  -0.0702 0.0529  288 THR B OG1 
13310 C CG2 . THR B 284 ? 0.5745 0.7318 0.7324 0.0862  -0.0735 0.0482  288 THR B CG2 
13318 N N   . VAL B 285 ? 0.6110 0.6521 0.7152 0.1117  -0.0528 0.0405  289 VAL B N   
13319 C CA  . VAL B 285 ? 0.6696 0.6733 0.7572 0.1223  -0.0527 0.0423  289 VAL B CA  
13320 C C   . VAL B 285 ? 0.6961 0.6672 0.7617 0.1079  -0.0484 0.0380  289 VAL B C   
13321 O O   . VAL B 285 ? 0.7608 0.7002 0.8078 0.1056  -0.0519 0.0434  289 VAL B O   
13322 C CB  . VAL B 285 ? 0.7011 0.7047 0.7979 0.1438  -0.0465 0.0380  289 VAL B CB  
13323 C CG1 . VAL B 285 ? 0.7412 0.6988 0.8169 0.1563  -0.0474 0.0400  289 VAL B CG1 
13324 C CG2 . VAL B 285 ? 0.7149 0.7609 0.8397 0.1575  -0.0503 0.0434  289 VAL B CG2 
13334 N N   . LEU B 286 ? 0.6378 0.6171 0.7052 0.0972  -0.0414 0.0295  290 LEU B N   
13335 C CA  . LEU B 286 ? 0.6542 0.6087 0.7043 0.0840  -0.0380 0.0251  290 LEU B CA  
13336 C C   . LEU B 286 ? 0.6985 0.6684 0.7490 0.0664  -0.0381 0.0264  290 LEU B C   
13337 O O   . LEU B 286 ? 0.7017 0.6993 0.7646 0.0643  -0.0379 0.0260  290 LEU B O   
13338 C CB  . LEU B 286 ? 0.6631 0.6120 0.7113 0.0875  -0.0303 0.0142  290 LEU B CB  
13339 C CG  . LEU B 286 ? 0.6759 0.6049 0.7195 0.1075  -0.0275 0.0107  290 LEU B CG  
13340 C CD1 . LEU B 286 ? 0.7108 0.6359 0.7489 0.1105  -0.0187 -0.0012 290 LEU B CD1 
13341 C CD2 . LEU B 286 ? 0.6653 0.5496 0.6872 0.1086  -0.0324 0.0148  290 LEU B CD2 
13353 N N   . GLU B 287 ? 0.6988 0.6501 0.7353 0.0537  -0.0383 0.0282  291 GLU B N   
13354 C CA  . GLU B 287 ? 0.6809 0.6474 0.7179 0.0396  -0.0368 0.0295  291 GLU B CA  
13355 C C   . GLU B 287 ? 0.6569 0.6427 0.7029 0.0372  -0.0320 0.0217  291 GLU B C   
13356 O O   . GLU B 287 ? 0.6486 0.6320 0.6965 0.0429  -0.0290 0.0149  291 GLU B O   
13357 C CB  . GLU B 287 ? 0.7113 0.6593 0.7352 0.0262  -0.0368 0.0330  291 GLU B CB  
13358 C CG  . GLU B 287 ? 0.7876 0.7128 0.7987 0.0257  -0.0408 0.0426  291 GLU B CG  
13359 C CD  . GLU B 287 ? 0.8401 0.7472 0.8392 0.0093  -0.0402 0.0466  291 GLU B CD  
13360 O OE1 . GLU B 287 ? 0.8402 0.7478 0.8403 0.0001  -0.0383 0.0404  291 GLU B OE1 
13361 O OE2 . GLU B 287 ? 0.8678 0.7614 0.8559 0.0043  -0.0420 0.0567  291 GLU B OE2 
13368 N N   . TYR B 288 ? 0.6203 0.6234 0.6694 0.0297  -0.0306 0.0230  292 TYR B N   
13369 C CA  . TYR B 288 ? 0.6182 0.6348 0.6720 0.0262  -0.0265 0.0175  292 TYR B CA  
13370 C C   . TYR B 288 ? 0.6325 0.6373 0.6791 0.0194  -0.0258 0.0142  292 TYR B C   
13371 O O   . TYR B 288 ? 0.6731 0.6639 0.7120 0.0121  -0.0280 0.0178  292 TYR B O   
13372 C CB  . TYR B 288 ? 0.6000 0.6316 0.6550 0.0211  -0.0251 0.0203  292 TYR B CB  
13373 C CG  . TYR B 288 ? 0.6308 0.6699 0.6877 0.0247  -0.0271 0.0224  292 TYR B CG  
13374 C CD1 . TYR B 288 ? 0.6031 0.6533 0.6672 0.0272  -0.0266 0.0192  292 TYR B CD1 
13375 C CD2 . TYR B 288 ? 0.6855 0.7201 0.7349 0.0238  -0.0300 0.0280  292 TYR B CD2 
13376 C CE1 . TYR B 288 ? 0.6258 0.6816 0.6902 0.0273  -0.0302 0.0207  292 TYR B CE1 
13377 C CE2 . TYR B 288 ? 0.6901 0.7300 0.7376 0.0257  -0.0335 0.0291  292 TYR B CE2 
13378 C CZ  . TYR B 288 ? 0.6698 0.7200 0.7251 0.0267  -0.0343 0.0251  292 TYR B CZ  
13379 O OH  . TYR B 288 ? 0.6920 0.7462 0.7441 0.0256  -0.0395 0.0258  292 TYR B OH  
13389 N N   . PRO B 289 ? 0.6595 0.6691 0.7066 0.0199  -0.0233 0.0078  293 PRO B N   
13390 C CA  . PRO B 289 ? 0.6801 0.6800 0.7182 0.0111  -0.0246 0.0042  293 PRO B CA  
13391 C C   . PRO B 289 ? 0.6633 0.6774 0.7044 -0.0001 -0.0260 0.0094  293 PRO B C   
13392 O O   . PRO B 289 ? 0.6435 0.6763 0.6924 0.0017  -0.0239 0.0133  293 PRO B O   
13393 C CB  . PRO B 289 ? 0.6747 0.6805 0.7113 0.0155  -0.0213 -0.0030 293 PRO B CB  
13394 C CG  . PRO B 289 ? 0.6969 0.7220 0.7451 0.0224  -0.0178 -0.0009 293 PRO B CG  
13395 C CD  . PRO B 289 ? 0.6815 0.7049 0.7357 0.0270  -0.0195 0.0040  293 PRO B CD  
13403 N N   . THR B 290 ? 0.6874 0.6923 0.7220 -0.0118 -0.0296 0.0095  294 THR B N   
13404 C CA  . THR B 290 ? 0.6777 0.7026 0.7185 -0.0230 -0.0310 0.0148  294 THR B CA  
13405 C C   . THR B 290 ? 0.6598 0.6995 0.7017 -0.0245 -0.0326 0.0106  294 THR B C   
13406 O O   . THR B 290 ? 0.6431 0.6724 0.6767 -0.0197 -0.0326 0.0031  294 THR B O   
13407 C CB  . THR B 290 ? 0.7263 0.7381 0.7613 -0.0384 -0.0352 0.0186  294 THR B CB  
13408 O OG1 . THR B 290 ? 0.7290 0.7234 0.7522 -0.0466 -0.0405 0.0112  294 THR B OG1 
13409 C CG2 . THR B 290 ? 0.7363 0.7236 0.7639 -0.0357 -0.0345 0.0223  294 THR B CG2 
13417 N N   . ILE B 291 ? 0.6632 0.7288 0.7150 -0.0301 -0.0336 0.0162  295 ILE B N   
13418 C CA  . ILE B 291 ? 0.6586 0.7400 0.7110 -0.0314 -0.0369 0.0142  295 ILE B CA  
13419 C C   . ILE B 291 ? 0.6664 0.7313 0.7051 -0.0430 -0.0440 0.0074  295 ILE B C   
13420 O O   . ILE B 291 ? 0.6782 0.7379 0.7063 -0.0399 -0.0456 0.0008  295 ILE B O   
13421 C CB  . ILE B 291 ? 0.6948 0.8099 0.7624 -0.0337 -0.0372 0.0228  295 ILE B CB  
13422 C CG1 . ILE B 291 ? 0.8020 0.9286 0.8756 -0.0180 -0.0304 0.0258  295 ILE B CG1 
13423 C CG2 . ILE B 291 ? 0.6745 0.8062 0.7427 -0.0415 -0.0451 0.0225  295 ILE B CG2 
13424 C CD1 . ILE B 291 ? 0.9147 1.0276 0.9865 -0.0112 -0.0244 0.0261  295 ILE B CD1 
13436 N N   . GLY B 292 ? 0.6703 0.7237 0.7059 -0.0574 -0.0484 0.0090  296 GLY B N   
13437 C CA  . GLY B 292 ? 0.7239 0.7543 0.7418 -0.0704 -0.0561 0.0014  296 GLY B CA  
13438 C C   . GLY B 292 ? 0.7340 0.7304 0.7321 -0.0595 -0.0532 -0.0097 296 GLY B C   
13439 O O   . GLY B 292 ? 0.7527 0.7361 0.7334 -0.0626 -0.0573 -0.0185 296 GLY B O   
13443 N N   . GLN B 293 ? 0.7296 0.7130 0.7297 -0.0459 -0.0461 -0.0092 297 GLN B N   
13444 C CA  . GLN B 293 ? 0.7277 0.6856 0.7136 -0.0324 -0.0417 -0.0185 297 GLN B CA  
13445 C C   . GLN B 293 ? 0.6710 0.6465 0.6578 -0.0223 -0.0374 -0.0224 297 GLN B C   
13446 O O   . GLN B 293 ? 0.6542 0.6138 0.6236 -0.0182 -0.0360 -0.0318 297 GLN B O   
13447 C CB  . GLN B 293 ? 0.7516 0.6996 0.7439 -0.0200 -0.0364 -0.0150 297 GLN B CB  
13448 C CG  . GLN B 293 ? 0.8130 0.7338 0.7975 -0.0279 -0.0401 -0.0114 297 GLN B CG  
13449 C CD  . GLN B 293 ? 0.8495 0.7640 0.8402 -0.0146 -0.0363 -0.0060 297 GLN B CD  
13450 O OE1 . GLN B 293 ? 0.8591 0.7996 0.8658 -0.0080 -0.0331 -0.0003 297 GLN B OE1 
13451 N NE2 . GLN B 293 ? 0.8762 0.7542 0.8523 -0.0102 -0.0374 -0.0078 297 GLN B NE2 
13460 N N   . LEU B 294 ? 0.6135 0.6188 0.6176 -0.0180 -0.0346 -0.0152 298 LEU B N   
13461 C CA  . LEU B 294 ? 0.6394 0.6589 0.6428 -0.0102 -0.0308 -0.0169 298 LEU B CA  
13462 C C   . LEU B 294 ? 0.6982 0.7200 0.6875 -0.0186 -0.0369 -0.0208 298 LEU B C   
13463 O O   . LEU B 294 ? 0.7253 0.7416 0.7004 -0.0135 -0.0339 -0.0269 298 LEU B O   
13464 C CB  . LEU B 294 ? 0.5973 0.6419 0.6181 -0.0056 -0.0280 -0.0081 298 LEU B CB  
13465 C CG  . LEU B 294 ? 0.5580 0.6022 0.5894 0.0034  -0.0224 -0.0053 298 LEU B CG  
13466 C CD1 . LEU B 294 ? 0.5776 0.6404 0.6206 0.0053  -0.0212 0.0022  298 LEU B CD1 
13467 C CD2 . LEU B 294 ? 0.5487 0.5884 0.5772 0.0129  -0.0161 -0.0100 298 LEU B CD2 
13479 N N   . ILE B 295 ? 0.6812 0.7139 0.6743 -0.0320 -0.0455 -0.0168 299 ILE B N   
13480 C CA  . ILE B 295 ? 0.6920 0.7294 0.6719 -0.0420 -0.0542 -0.0200 299 ILE B CA  
13481 C C   . ILE B 295 ? 0.7208 0.7239 0.6725 -0.0450 -0.0556 -0.0328 299 ILE B C   
13482 O O   . ILE B 295 ? 0.7364 0.7362 0.6693 -0.0437 -0.0568 -0.0388 299 ILE B O   
13483 C CB  . ILE B 295 ? 0.6817 0.7391 0.6737 -0.0581 -0.0641 -0.0130 299 ILE B CB  
13484 C CG1 . ILE B 295 ? 0.7065 0.8000 0.7235 -0.0513 -0.0615 -0.0010 299 ILE B CG1 
13485 C CG2 . ILE B 295 ? 0.6411 0.7007 0.6172 -0.0719 -0.0762 -0.0173 299 ILE B CG2 
13486 C CD1 . ILE B 295 ? 0.7415 0.8619 0.7762 -0.0644 -0.0681 0.0077  299 ILE B CD1 
13498 N N   . ASP B 296 ? 0.7177 0.6921 0.6630 -0.0480 -0.0551 -0.0371 300 ASP B N   
13499 C CA  . ASP B 296 ? 0.7708 0.7060 0.6858 -0.0497 -0.0563 -0.0502 300 ASP B CA  
13500 C C   . ASP B 296 ? 0.7468 0.6745 0.6491 -0.0314 -0.0456 -0.0577 300 ASP B C   
13501 O O   . ASP B 296 ? 0.7713 0.6832 0.6464 -0.0323 -0.0467 -0.0678 300 ASP B O   
13502 C CB  . ASP B 296 ? 0.8775 0.7800 0.7887 -0.0520 -0.0560 -0.0515 300 ASP B CB  
13503 C CG  . ASP B 296 ? 1.0098 0.8654 0.8858 -0.0582 -0.0603 -0.0649 300 ASP B CG  
13504 O OD1 . ASP B 296 ? 1.0730 0.9217 0.9356 -0.0792 -0.0722 -0.0676 300 ASP B OD1 
13505 O OD2 . ASP B 296 ? 1.0685 0.8940 0.9298 -0.0419 -0.0519 -0.0729 300 ASP B OD2 
13510 N N   . LYS B 297 ? 0.7223 0.6630 0.6433 -0.0157 -0.0350 -0.0527 301 LYS B N   
13511 C CA  . LYS B 297 ? 0.7822 0.7199 0.6952 0.0010  -0.0234 -0.0584 301 LYS B CA  
13512 C C   . LYS B 297 ? 0.7937 0.7574 0.7068 0.0024  -0.0208 -0.0552 301 LYS B C   
13513 O O   . LYS B 297 ? 0.8740 0.8328 0.7705 0.0109  -0.0128 -0.0615 301 LYS B O   
13514 C CB  . LYS B 297 ? 0.7906 0.7336 0.7247 0.0152  -0.0147 -0.0538 301 LYS B CB  
13515 C CG  . LYS B 297 ? 0.9103 0.8233 0.8404 0.0177  -0.0163 -0.0565 301 LYS B CG  
13516 C CD  . LYS B 297 ? 1.0329 0.9079 0.9320 0.0236  -0.0137 -0.0701 301 LYS B CD  
13517 C CE  . LYS B 297 ? 1.1176 0.9562 1.0092 0.0264  -0.0161 -0.0719 301 LYS B CE  
13518 N NZ  . LYS B 297 ? 1.2409 1.0352 1.0975 0.0332  -0.0136 -0.0863 301 LYS B NZ  
13532 N N   . LEU B 298 ? 0.6916 0.6818 0.6215 -0.0045 -0.0264 -0.0449 302 LEU B N   
13533 C CA  . LEU B 298 ? 0.7257 0.7355 0.6519 -0.0030 -0.0252 -0.0406 302 LEU B CA  
13534 C C   . LEU B 298 ? 0.7895 0.7903 0.6870 -0.0112 -0.0328 -0.0475 302 LEU B C   
13535 O O   . LEU B 298 ? 0.8054 0.8074 0.6853 -0.0063 -0.0278 -0.0496 302 LEU B O   
13536 C CB  . LEU B 298 ? 0.6636 0.6997 0.6126 -0.0058 -0.0297 -0.0281 302 LEU B CB  
13537 C CG  . LEU B 298 ? 0.6600 0.7055 0.6317 0.0027  -0.0218 -0.0214 302 LEU B CG  
13538 C CD1 . LEU B 298 ? 0.6531 0.7180 0.6425 0.0003  -0.0266 -0.0111 302 LEU B CD1 
13539 C CD2 . LEU B 298 ? 0.6650 0.7146 0.6337 0.0115  -0.0115 -0.0205 302 LEU B CD2 
13551 N N   . VAL B 299 ? 0.7801 0.7719 0.6709 -0.0252 -0.0451 -0.0506 303 VAL B N   
13552 C CA  . VAL B 299 ? 0.7892 0.7705 0.6500 -0.0357 -0.0548 -0.0582 303 VAL B CA  
13553 C C   . VAL B 299 ? 0.8812 0.8269 0.7092 -0.0293 -0.0474 -0.0733 303 VAL B C   
13554 O O   . VAL B 299 ? 0.9559 0.8957 0.7556 -0.0280 -0.0466 -0.0795 303 VAL B O   
13555 C CB  . VAL B 299 ? 0.7621 0.7446 0.6264 -0.0554 -0.0708 -0.0572 303 VAL B CB  
13556 C CG1 . VAL B 299 ? 0.8037 0.7724 0.6342 -0.0690 -0.0831 -0.0665 303 VAL B CG1 
13557 C CG2 . VAL B 299 ? 0.7528 0.7757 0.6496 -0.0587 -0.0764 -0.0419 303 VAL B CG2 
13567 N N   . GLN B 300 ? 0.8892 0.8097 0.7187 -0.0237 -0.0413 -0.0792 304 GLN B N   
13568 C CA  . GLN B 300 ? 0.9711 0.8548 0.7690 -0.0145 -0.0334 -0.0941 304 GLN B CA  
13569 C C   . GLN B 300 ? 0.9214 0.8162 0.7132 0.0031  -0.0176 -0.0954 304 GLN B C   
13570 O O   . GLN B 300 ? 0.9452 0.8182 0.7027 0.0087  -0.0120 -0.1075 304 GLN B O   
13571 C CB  . GLN B 300 ? 1.1137 0.9715 0.9192 -0.0079 -0.0292 -0.0970 304 GLN B CB  
13572 C CG  . GLN B 300 ? 1.2924 1.1072 1.0648 0.0045  -0.0210 -0.1126 304 GLN B CG  
13573 C CD  . GLN B 300 ? 1.4250 1.2098 1.2025 0.0102  -0.0199 -0.1140 304 GLN B CD  
13574 O OE1 . GLN B 300 ? 1.4080 1.1956 1.2040 -0.0026 -0.0292 -0.1055 304 GLN B OE1 
13575 N NE2 . GLN B 300 ? 1.5465 1.3031 1.3070 0.0305  -0.0079 -0.1239 304 GLN B NE2 
13584 N N   . ASN B 301 ? 0.8790 0.8064 0.7019 0.0109  -0.0099 -0.0832 305 ASN B N   
13585 C CA  . ASN B 301 ? 0.8451 0.7874 0.6671 0.0247  0.0056  -0.0818 305 ASN B CA  
13586 C C   . ASN B 301 ? 0.8122 0.7772 0.6285 0.0189  0.0031  -0.0738 305 ASN B C   
13587 O O   . ASN B 301 ? 0.7765 0.7566 0.5938 0.0272  0.0156  -0.0694 305 ASN B O   
13588 C CB  . ASN B 301 ? 0.8370 0.7984 0.6947 0.0356  0.0154  -0.0734 305 ASN B CB  
13589 C CG  . ASN B 301 ? 0.9026 0.8427 0.7623 0.0473  0.0212  -0.0809 305 ASN B CG  
13590 O OD1 . ASN B 301 ? 0.9694 0.9062 0.8219 0.0628  0.0349  -0.0868 305 ASN B OD1 
13591 N ND2 . ASN B 301 ? 0.9161 0.8423 0.7854 0.0411  0.0113  -0.0798 305 ASN B ND2 
13598 N N   . ASN B 302 ? 0.8086 0.7774 0.6192 0.0047  -0.0128 -0.0706 306 ASN B N   
13599 C CA  . ASN B 302 ? 0.8205 0.8083 0.6223 0.0005  -0.0173 -0.0623 306 ASN B CA  
13600 C C   . ASN B 302 ? 0.7648 0.7778 0.5930 0.0075  -0.0086 -0.0482 306 ASN B C   
13601 O O   . ASN B 302 ? 0.7813 0.8019 0.5980 0.0119  -0.0004 -0.0436 306 ASN B O   
13602 C CB  . ASN B 302 ? 0.9249 0.8980 0.6845 0.0027  -0.0127 -0.0717 306 ASN B CB  
13603 C CG  . ASN B 302 ? 1.0557 1.0436 0.7991 -0.0041 -0.0222 -0.0636 306 ASN B CG  
13604 O OD1 . ASN B 302 ? 1.0917 1.0889 0.8397 -0.0153 -0.0396 -0.0590 306 ASN B OD1 
13605 N ND2 . ASN B 302 ? 1.1642 1.1564 0.8892 0.0030  -0.0106 -0.0606 306 ASN B ND2 
13612 N N   . VAL B 303 ? 0.7350 0.7585 0.5964 0.0075  -0.0104 -0.0413 307 VAL B N   
13613 C CA  . VAL B 303 ? 0.7102 0.7520 0.5957 0.0124  -0.0038 -0.0292 307 VAL B CA  
13614 C C   . VAL B 303 ? 0.6992 0.7555 0.5972 0.0072  -0.0155 -0.0184 307 VAL B C   
13615 O O   . VAL B 303 ? 0.7316 0.7901 0.6408 0.0015  -0.0255 -0.0188 307 VAL B O   
13616 C CB  . VAL B 303 ? 0.6963 0.7382 0.6073 0.0181  0.0037  -0.0299 307 VAL B CB  
13617 C CG1 . VAL B 303 ? 0.6811 0.7393 0.6148 0.0199  0.0075  -0.0181 307 VAL B CG1 
13618 C CG2 . VAL B 303 ? 0.6859 0.7186 0.5877 0.0270  0.0165  -0.0389 307 VAL B CG2 
13628 N N   . LEU B 304 ? 0.6884 0.7546 0.5844 0.0098  -0.0136 -0.0081 308 LEU B N   
13629 C CA  . LEU B 304 ? 0.6905 0.7698 0.5986 0.0096  -0.0225 0.0033  308 LEU B CA  
13630 C C   . LEU B 304 ? 0.7322 0.8141 0.6637 0.0144  -0.0157 0.0099  308 LEU B C   
13631 O O   . LEU B 304 ? 0.7935 0.8716 0.7240 0.0169  -0.0053 0.0126  308 LEU B O   
13632 C CB  . LEU B 304 ? 0.6971 0.7801 0.5844 0.0109  -0.0260 0.0115  308 LEU B CB  
13633 C CG  . LEU B 304 ? 0.7429 0.8236 0.6018 0.0053  -0.0348 0.0057  308 LEU B CG  
13634 C CD1 . LEU B 304 ? 0.7390 0.8248 0.5788 0.0081  -0.0388 0.0170  308 LEU B CD1 
13635 C CD2 . LEU B 304 ? 0.7238 0.8119 0.5900 -0.0028 -0.0497 0.0012  308 LEU B CD2 
13647 N N   . LEU B 305 ? 0.7243 0.8133 0.6758 0.0145  -0.0215 0.0127  309 LEU B N   
13648 C CA  . LEU B 305 ? 0.6768 0.7654 0.6471 0.0185  -0.0163 0.0170  309 LEU B CA  
13649 C C   . LEU B 305 ? 0.6666 0.7585 0.6377 0.0242  -0.0187 0.0281  309 LEU B C   
13650 O O   . LEU B 305 ? 0.6722 0.7752 0.6427 0.0262  -0.0274 0.0328  309 LEU B O   
13651 C CB  . LEU B 305 ? 0.6362 0.7278 0.6241 0.0164  -0.0195 0.0130  309 LEU B CB  
13652 C CG  . LEU B 305 ? 0.6292 0.7188 0.6335 0.0196  -0.0149 0.0155  309 LEU B CG  
13653 C CD1 . LEU B 305 ? 0.6791 0.7609 0.6836 0.0203  -0.0061 0.0137  309 LEU B CD1 
13654 C CD2 . LEU B 305 ? 0.5970 0.6884 0.6132 0.0164  -0.0180 0.0116  309 LEU B CD2 
13666 N N   . ILE B 306 ? 0.6668 0.7489 0.6388 0.0267  -0.0115 0.0326  310 ILE B N   
13667 C CA  . ILE B 306 ? 0.6530 0.7290 0.6220 0.0334  -0.0125 0.0426  310 ILE B CA  
13668 C C   . ILE B 306 ? 0.7194 0.7878 0.7017 0.0349  -0.0089 0.0419  310 ILE B C   
13669 O O   . ILE B 306 ? 0.8566 0.9166 0.8411 0.0297  -0.0027 0.0394  310 ILE B O   
13670 C CB  . ILE B 306 ? 0.6311 0.6947 0.5808 0.0326  -0.0078 0.0495  310 ILE B CB  
13671 C CG1 . ILE B 306 ? 0.6482 0.7188 0.5799 0.0319  -0.0124 0.0508  310 ILE B CG1 
13672 C CG2 . ILE B 306 ? 0.6067 0.6552 0.5512 0.0398  -0.0082 0.0596  310 ILE B CG2 
13673 C CD1 . ILE B 306 ? 0.6609 0.7200 0.5704 0.0298  -0.0062 0.0577  310 ILE B CD1 
13685 N N   . PHE B 307 ? 0.6609 0.7341 0.6517 0.0421  -0.0128 0.0443  311 PHE B N   
13686 C CA  . PHE B 307 ? 0.6650 0.7285 0.6631 0.0450  -0.0095 0.0434  311 PHE B CA  
13687 C C   . PHE B 307 ? 0.6719 0.7138 0.6563 0.0516  -0.0073 0.0506  311 PHE B C   
13688 O O   . PHE B 307 ? 0.6265 0.6687 0.6065 0.0632  -0.0100 0.0571  311 PHE B O   
13689 C CB  . PHE B 307 ? 0.6935 0.7724 0.7051 0.0503  -0.0126 0.0425  311 PHE B CB  
13690 C CG  . PHE B 307 ? 0.6786 0.7709 0.7018 0.0419  -0.0144 0.0358  311 PHE B CG  
13691 C CD1 . PHE B 307 ? 0.6831 0.7673 0.7098 0.0355  -0.0111 0.0297  311 PHE B CD1 
13692 C CD2 . PHE B 307 ? 0.6820 0.7943 0.7120 0.0400  -0.0204 0.0363  311 PHE B CD2 
13693 C CE1 . PHE B 307 ? 0.7122 0.8033 0.7466 0.0295  -0.0129 0.0244  311 PHE B CE1 
13694 C CE2 . PHE B 307 ? 0.6621 0.7801 0.6992 0.0309  -0.0224 0.0304  311 PHE B CE2 
13695 C CZ  . PHE B 307 ? 0.7081 0.8132 0.7463 0.0268  -0.0182 0.0246  311 PHE B CZ  
13705 N N   . ALA B 308 ? 0.6881 0.7110 0.6656 0.0442  -0.0027 0.0499  312 ALA B N   
13706 C CA  . ALA B 308 ? 0.7063 0.7007 0.6676 0.0471  -0.0006 0.0559  312 ALA B CA  
13707 C C   . ALA B 308 ? 0.7113 0.6917 0.6748 0.0479  0.0005  0.0509  312 ALA B C   
13708 O O   . ALA B 308 ? 0.6967 0.6696 0.6620 0.0363  0.0021  0.0469  312 ALA B O   
13709 C CB  . ALA B 308 ? 0.7290 0.7115 0.6798 0.0350  0.0033  0.0594  312 ALA B CB  
13715 N N   . VAL B 309 ? 0.7680 0.7472 0.7312 0.0620  -0.0004 0.0515  313 VAL B N   
13716 C CA  . VAL B 309 ? 0.7979 0.7668 0.7610 0.0647  0.0012  0.0458  313 VAL B CA  
13717 C C   . VAL B 309 ? 0.8083 0.7476 0.7521 0.0793  0.0032  0.0492  313 VAL B C   
13718 O O   . VAL B 309 ? 0.8239 0.7588 0.7601 0.0911  0.0027  0.0570  313 VAL B O   
13719 C CB  . VAL B 309 ? 0.7718 0.7701 0.7532 0.0686  0.0005  0.0419  313 VAL B CB  
13720 C CG1 . VAL B 309 ? 0.7508 0.7697 0.7470 0.0553  -0.0015 0.0378  313 VAL B CG1 
13721 C CG2 . VAL B 309 ? 0.7481 0.7666 0.7358 0.0828  -0.0007 0.0479  313 VAL B CG2 
13731 N N   . THR B 310 ? 0.7604 0.6776 0.6940 0.0793  0.0051  0.0432  314 THR B N   
13732 C CA  . THR B 310 ? 0.7906 0.6711 0.7005 0.0933  0.0080  0.0441  314 THR B CA  
13733 C C   . THR B 310 ? 0.8268 0.7248 0.7427 0.1167  0.0114  0.0462  314 THR B C   
13734 O O   . THR B 310 ? 0.8067 0.7451 0.7457 0.1183  0.0112  0.0462  314 THR B O   
13735 C CB  . THR B 310 ? 0.7639 0.6134 0.6572 0.0843  0.0082  0.0354  314 THR B CB  
13736 O OG1 . THR B 310 ? 0.7616 0.6366 0.6700 0.0805  0.0082  0.0286  314 THR B OG1 
13737 C CG2 . THR B 310 ? 0.7596 0.5905 0.6461 0.0615  0.0046  0.0356  314 THR B CG2 
13745 N N   . GLN B 311 ? 0.8563 0.7226 0.7508 0.1351  0.0149  0.0485  315 GLN B N   
13746 C CA  . GLN B 311 ? 0.8518 0.7360 0.7523 0.1611  0.0195  0.0523  315 GLN B CA  
13747 C C   . GLN B 311 ? 0.8345 0.7519 0.7529 0.1622  0.0235  0.0464  315 GLN B C   
13748 O O   . GLN B 311 ? 0.8211 0.7826 0.7635 0.1707  0.0243  0.0513  315 GLN B O   
13749 C CB  . GLN B 311 ? 0.8828 0.7176 0.7517 0.1812  0.0244  0.0525  315 GLN B CB  
13750 C CG  . GLN B 311 ? 0.9683 0.8066 0.8338 0.2057  0.0333  0.0488  315 GLN B CG  
13751 C CD  . GLN B 311 ? 1.0400 0.9275 0.9317 0.2276  0.0355  0.0584  315 GLN B CD  
13752 O OE1 . GLN B 311 ? 1.0566 0.9585 0.9575 0.2318  0.0298  0.0688  315 GLN B OE1 
13753 N NE2 . GLN B 311 ? 1.0897 1.0052 0.9931 0.2410  0.0436  0.0556  315 GLN B NE2 
13762 N N   . GLU B 312 ? 0.8822 0.7796 0.7884 0.1522  0.0253  0.0367  316 GLU B N   
13763 C CA  . GLU B 312 ? 0.8972 0.8196 0.8136 0.1546  0.0302  0.0320  316 GLU B CA  
13764 C C   . GLU B 312 ? 0.7703 0.7418 0.7190 0.1416  0.0265  0.0349  316 GLU B C   
13765 O O   . GLU B 312 ? 0.7423 0.7434 0.7046 0.1462  0.0310  0.0352  316 GLU B O   
13766 C CB  . GLU B 312 ? 1.0309 0.9208 0.9251 0.1433  0.0303  0.0214  316 GLU B CB  
13767 C CG  . GLU B 312 ? 1.2064 1.0423 1.0630 0.1555  0.0343  0.0160  316 GLU B CG  
13768 C CD  . GLU B 312 ? 1.3455 1.1409 1.1844 0.1463  0.0284  0.0178  316 GLU B CD  
13769 O OE1 . GLU B 312 ? 1.3476 1.1605 1.2043 0.1307  0.0222  0.0232  316 GLU B OE1 
13770 O OE2 . GLU B 312 ? 1.4355 1.1799 1.2407 0.1544  0.0306  0.0138  316 GLU B OE2 
13777 N N   . GLN B 313 ? 0.7037 0.6825 0.6627 0.1255  0.0191  0.0370  317 GLN B N   
13778 C CA  . GLN B 313 ? 0.7005 0.7158 0.6840 0.1118  0.0150  0.0378  317 GLN B CA  
13779 C C   . GLN B 313 ? 0.6681 0.7137 0.6689 0.1147  0.0111  0.0455  317 GLN B C   
13780 O O   . GLN B 313 ? 0.6677 0.7410 0.6864 0.1035  0.0073  0.0458  317 GLN B O   
13781 C CB  . GLN B 313 ? 0.7654 0.7687 0.7474 0.0914  0.0099  0.0330  317 GLN B CB  
13782 C CG  . GLN B 313 ? 0.8387 0.8150 0.8046 0.0850  0.0106  0.0258  317 GLN B CG  
13783 C CD  . GLN B 313 ? 0.8549 0.8453 0.8254 0.0853  0.0131  0.0224  317 GLN B CD  
13784 O OE1 . GLN B 313 ? 0.8588 0.8804 0.8481 0.0849  0.0136  0.0255  317 GLN B OE1 
13785 N NE2 . GLN B 313 ? 0.8970 0.8630 0.8481 0.0845  0.0142  0.0164  317 GLN B NE2 
13794 N N   . VAL B 314 ? 0.6642 0.7029 0.6580 0.1293  0.0110  0.0520  318 VAL B N   
13795 C CA  . VAL B 314 ? 0.6829 0.7482 0.6895 0.1302  0.0049  0.0597  318 VAL B CA  
13796 C C   . VAL B 314 ? 0.7235 0.8357 0.7557 0.1312  0.0038  0.0628  318 VAL B C   
13797 O O   . VAL B 314 ? 0.7535 0.8894 0.7990 0.1176  -0.0030 0.0634  318 VAL B O   
13798 C CB  . VAL B 314 ? 0.6565 0.7052 0.6492 0.1489  0.0047  0.0678  318 VAL B CB  
13799 C CG1 . VAL B 314 ? 0.6165 0.7021 0.6249 0.1544  -0.0024 0.0772  318 VAL B CG1 
13800 C CG2 . VAL B 314 ? 0.6614 0.6677 0.6304 0.1406  0.0034  0.0670  318 VAL B CG2 
13810 N N   . HIS B 315 ? 0.7791 0.9050 0.8174 0.1466  0.0107  0.0647  319 HIS B N   
13811 C CA  . HIS B 315 ? 0.7893 0.9647 0.8544 0.1470  0.0103  0.0699  319 HIS B CA  
13812 C C   . HIS B 315 ? 0.6964 0.8849 0.7727 0.1235  0.0073  0.0651  319 HIS B C   
13813 O O   . HIS B 315 ? 0.6881 0.9100 0.7832 0.1130  0.0009  0.0688  319 HIS B O   
13814 C CB  . HIS B 315 ? 0.8942 1.0817 0.9628 0.1675  0.0214  0.0723  319 HIS B CB  
13815 C CG  . HIS B 315 ? 0.9971 1.2416 1.0964 0.1688  0.0220  0.0801  319 HIS B CG  
13816 N ND1 . HIS B 315 ? 1.0200 1.2859 1.1308 0.1605  0.0286  0.0788  319 HIS B ND1 
13817 C CD2 . HIS B 315 ? 1.0276 1.3143 1.1488 0.1756  0.0161  0.0903  319 HIS B CD2 
13818 C CE1 . HIS B 315 ? 1.0187 1.3380 1.1585 0.1610  0.0276  0.0880  319 HIS B CE1 
13819 N NE2 . HIS B 315 ? 1.0159 1.3503 1.1635 0.1700  0.0193  0.0949  319 HIS B NE2 
13827 N N   . LEU B 316 ? 0.6735 0.8344 0.7370 0.1148  0.0110  0.0570  320 LEU B N   
13828 C CA  . LEU B 316 ? 0.6392 0.8068 0.7104 0.0948  0.0080  0.0530  320 LEU B CA  
13829 C C   . LEU B 316 ? 0.6223 0.7905 0.6962 0.0806  -0.0015 0.0518  320 LEU B C   
13830 O O   . LEU B 316 ? 0.6381 0.8288 0.7253 0.0686  -0.0067 0.0531  320 LEU B O   
13831 C CB  . LEU B 316 ? 0.6660 0.8027 0.7213 0.0902  0.0119  0.0455  320 LEU B CB  
13832 C CG  . LEU B 316 ? 0.7689 0.9056 0.8286 0.0723  0.0086  0.0417  320 LEU B CG  
13833 C CD1 . LEU B 316 ? 0.8179 0.9817 0.8912 0.0681  0.0116  0.0459  320 LEU B CD1 
13834 C CD2 . LEU B 316 ? 0.8424 0.9481 0.8855 0.0692  0.0097  0.0351  320 LEU B CD2 
13846 N N   . TYR B 317 ? 0.6017 0.7437 0.6608 0.0811  -0.0036 0.0494  321 TYR B N   
13847 C CA  . TYR B 317 ? 0.6178 0.7576 0.6753 0.0686  -0.0104 0.0472  321 TYR B CA  
13848 C C   . TYR B 317 ? 0.6294 0.7939 0.6940 0.0699  -0.0174 0.0532  321 TYR B C   
13849 O O   . TYR B 317 ? 0.6936 0.8642 0.7590 0.0576  -0.0238 0.0508  321 TYR B O   
13850 C CB  . TYR B 317 ? 0.6358 0.7445 0.6763 0.0680  -0.0090 0.0442  321 TYR B CB  
13851 C CG  . TYR B 317 ? 0.5969 0.6870 0.6333 0.0603  -0.0058 0.0375  321 TYR B CG  
13852 C CD1 . TYR B 317 ? 0.6022 0.6926 0.6423 0.0480  -0.0080 0.0326  321 TYR B CD1 
13853 C CD2 . TYR B 317 ? 0.5938 0.6661 0.6215 0.0661  -0.0012 0.0359  321 TYR B CD2 
13854 C CE1 . TYR B 317 ? 0.5732 0.6512 0.6120 0.0426  -0.0063 0.0278  321 TYR B CE1 
13855 C CE2 . TYR B 317 ? 0.6150 0.6733 0.6390 0.0581  -0.0005 0.0304  321 TYR B CE2 
13856 C CZ  . TYR B 317 ? 0.5869 0.6506 0.6184 0.0467  -0.0034 0.0271  321 TYR B CZ  
13857 O OH  . TYR B 317 ? 0.5860 0.6400 0.6162 0.0403  -0.0039 0.0230  321 TYR B OH  
13867 N N   . GLU B 318 ? 0.5914 0.7698 0.6599 0.0855  -0.0169 0.0610  322 GLU B N   
13868 C CA  . GLU B 318 ? 0.6052 0.8146 0.6839 0.0868  -0.0255 0.0681  322 GLU B CA  
13869 C C   . GLU B 318 ? 0.6169 0.8599 0.7159 0.0734  -0.0298 0.0683  322 GLU B C   
13870 O O   . GLU B 318 ? 0.6523 0.9113 0.7546 0.0615  -0.0398 0.0688  322 GLU B O   
13871 C CB  . GLU B 318 ? 0.6655 0.8860 0.7469 0.1094  -0.0237 0.0776  322 GLU B CB  
13872 C CG  . GLU B 318 ? 0.7872 0.9790 0.8473 0.1196  -0.0250 0.0810  322 GLU B CG  
13873 C CD  . GLU B 318 ? 0.9361 1.1347 0.9969 0.1449  -0.0233 0.0910  322 GLU B CD  
13874 O OE1 . GLU B 318 ? 0.9773 1.1971 1.0533 0.1570  -0.0174 0.0932  322 GLU B OE1 
13875 O OE2 . GLU B 318 ? 1.0102 1.1927 1.0555 0.1540  -0.0273 0.0973  322 GLU B OE2 
13882 N N   . ASN B 319 ? 0.6198 0.8719 0.7298 0.0737  -0.0225 0.0679  323 ASN B N   
13883 C CA  . ASN B 319 ? 0.6232 0.9031 0.7506 0.0578  -0.0257 0.0689  323 ASN B CA  
13884 C C   . ASN B 319 ? 0.6024 0.8612 0.7202 0.0373  -0.0312 0.0605  323 ASN B C   
13885 O O   . ASN B 319 ? 0.6266 0.9015 0.7511 0.0216  -0.0398 0.0607  323 ASN B O   
13886 C CB  . ASN B 319 ? 0.7076 0.9964 0.8440 0.0622  -0.0149 0.0706  323 ASN B CB  
13887 C CG  . ASN B 319 ? 0.8031 1.1256 0.9549 0.0813  -0.0094 0.0800  323 ASN B CG  
13888 O OD1 . ASN B 319 ? 0.8405 1.1492 0.9837 0.1000  0.0008  0.0797  323 ASN B OD1 
13889 N ND2 . ASN B 319 ? 0.8373 1.2049 1.0116 0.0769  -0.0163 0.0882  323 ASN B ND2 
13896 N N   . TYR B 320 ? 0.6221 0.8446 0.7235 0.0375  -0.0265 0.0530  324 TYR B N   
13897 C CA  . TYR B 320 ? 0.6235 0.8251 0.7147 0.0229  -0.0306 0.0450  324 TYR B CA  
13898 C C   . TYR B 320 ? 0.6240 0.8272 0.7070 0.0184  -0.0394 0.0437  324 TYR B C   
13899 O O   . TYR B 320 ? 0.6200 0.8213 0.6992 0.0040  -0.0461 0.0392  324 TYR B O   
13900 C CB  . TYR B 320 ? 0.5953 0.7646 0.6737 0.0267  -0.0242 0.0388  324 TYR B CB  
13901 C CG  . TYR B 320 ? 0.6473 0.8095 0.7284 0.0267  -0.0180 0.0379  324 TYR B CG  
13902 C CD1 . TYR B 320 ? 0.6953 0.8727 0.7869 0.0187  -0.0179 0.0408  324 TYR B CD1 
13903 C CD2 . TYR B 320 ? 0.7083 0.8484 0.7801 0.0329  -0.0127 0.0346  324 TYR B CD2 
13904 C CE1 . TYR B 320 ? 0.7615 0.9312 0.8520 0.0189  -0.0122 0.0409  324 TYR B CE1 
13905 C CE2 . TYR B 320 ? 0.7327 0.8659 0.8037 0.0327  -0.0085 0.0339  324 TYR B CE2 
13906 C CZ  . TYR B 320 ? 0.7766 0.9240 0.8560 0.0266  -0.0079 0.0371  324 TYR B CZ  
13907 O OH  . TYR B 320 ? 0.8162 0.9558 0.8915 0.0265  -0.0037 0.0373  324 TYR B OH  
13917 N N   . ALA B 321 ? 0.6214 0.8246 0.6979 0.0305  -0.0397 0.0478  325 ALA B N   
13918 C CA  . ALA B 321 ? 0.6335 0.8360 0.6975 0.0270  -0.0477 0.0472  325 ALA B CA  
13919 C C   . ALA B 321 ? 0.6290 0.8633 0.7029 0.0182  -0.0593 0.0513  325 ALA B C   
13920 O O   . ALA B 321 ? 0.6675 0.8991 0.7285 0.0085  -0.0680 0.0477  325 ALA B O   
13921 C CB  . ALA B 321 ? 0.6109 0.8049 0.6642 0.0421  -0.0454 0.0529  325 ALA B CB  
13927 N N   . LYS B 322 ? 0.5785 0.8443 0.6746 0.0208  -0.0598 0.0587  326 LYS B N   
13928 C CA  . LYS B 322 ? 0.6413 0.9429 0.7511 0.0089  -0.0718 0.0634  326 LYS B CA  
13929 C C   . LYS B 322 ? 0.7313 1.0206 0.8343 -0.0148 -0.0777 0.0547  326 LYS B C   
13930 O O   . LYS B 322 ? 0.7831 1.0840 0.8821 -0.0289 -0.0907 0.0537  326 LYS B O   
13931 C CB  . LYS B 322 ? 0.6203 0.9615 0.7585 0.0154  -0.0684 0.0735  326 LYS B CB  
13932 C CG  . LYS B 322 ? 0.6307 0.9863 0.7753 0.0413  -0.0637 0.0827  326 LYS B CG  
13933 C CD  . LYS B 322 ? 0.7022 1.1001 0.8755 0.0492  -0.0583 0.0921  326 LYS B CD  
13934 C CE  . LYS B 322 ? 0.8574 1.2629 1.0339 0.0790  -0.0515 0.1002  326 LYS B CE  
13935 N NZ  . LYS B 322 ? 0.9506 1.4004 1.1552 0.0899  -0.0440 0.1092  326 LYS B NZ  
13949 N N   . LEU B 323 ? 0.7183 0.9815 0.8175 -0.0191 -0.0692 0.0482  327 LEU B N   
13950 C CA  . LEU B 323 ? 0.6595 0.9049 0.7504 -0.0394 -0.0738 0.0404  327 LEU B CA  
13951 C C   . LEU B 323 ? 0.6708 0.8806 0.7341 -0.0420 -0.0759 0.0292  327 LEU B C   
13952 O O   . LEU B 323 ? 0.7105 0.9075 0.7609 -0.0582 -0.0840 0.0223  327 LEU B O   
13953 C CB  . LEU B 323 ? 0.5882 0.8198 0.6852 -0.0411 -0.0641 0.0395  327 LEU B CB  
13954 C CG  . LEU B 323 ? 0.5364 0.7997 0.6572 -0.0362 -0.0579 0.0500  327 LEU B CG  
13955 C CD1 . LEU B 323 ? 0.5558 0.7989 0.6752 -0.0360 -0.0480 0.0485  327 LEU B CD1 
13956 C CD2 . LEU B 323 ? 0.5508 0.8520 0.6898 -0.0528 -0.0669 0.0572  327 LEU B CD2 
13968 N N   . ILE B 324 ? 0.6621 0.8548 0.7147 -0.0268 -0.0682 0.0271  328 ILE B N   
13969 C CA  . ILE B 324 ? 0.6905 0.8518 0.7188 -0.0269 -0.0662 0.0171  328 ILE B CA  
13970 C C   . ILE B 324 ? 0.7836 0.9519 0.7962 -0.0278 -0.0748 0.0174  328 ILE B C   
13971 O O   . ILE B 324 ? 0.8783 1.0627 0.8948 -0.0166 -0.0750 0.0258  328 ILE B O   
13972 C CB  . ILE B 324 ? 0.6444 0.7884 0.6707 -0.0127 -0.0537 0.0162  328 ILE B CB  
13973 C CG1 . ILE B 324 ? 0.5861 0.7256 0.6265 -0.0116 -0.0470 0.0170  328 ILE B CG1 
13974 C CG2 . ILE B 324 ? 0.6783 0.7960 0.6832 -0.0125 -0.0499 0.0067  328 ILE B CG2 
13975 C CD1 . ILE B 324 ? 0.5445 0.6725 0.5858 0.0006  -0.0371 0.0175  328 ILE B CD1 
13987 N N   . PRO B 325 ? 0.7745 0.9284 0.7664 -0.0400 -0.0822 0.0085  329 PRO B N   
13988 C CA  . PRO B 325 ? 0.7418 0.9015 0.7143 -0.0413 -0.0912 0.0085  329 PRO B CA  
13989 C C   . PRO B 325 ? 0.7161 0.8642 0.6747 -0.0261 -0.0817 0.0099  329 PRO B C   
13990 O O   . PRO B 325 ? 0.7147 0.8388 0.6649 -0.0210 -0.0700 0.0034  329 PRO B O   
13991 C CB  . PRO B 325 ? 0.7259 0.8613 0.6730 -0.0571 -0.0981 -0.0046 329 PRO B CB  
13992 C CG  . PRO B 325 ? 0.7295 0.8550 0.6892 -0.0671 -0.0968 -0.0080 329 PRO B CG  
13993 C CD  . PRO B 325 ? 0.7321 0.8601 0.7134 -0.0530 -0.0832 -0.0022 329 PRO B CD  
14001 N N   . GLY B 326 ? 0.7123 0.8789 0.6691 -0.0191 -0.0870 0.0196  330 GLY B N   
14002 C CA  . GLY B 326 ? 0.7439 0.8988 0.6842 -0.0074 -0.0794 0.0230  330 GLY B CA  
14003 C C   . GLY B 326 ? 0.7141 0.8639 0.6689 0.0058  -0.0667 0.0292  330 GLY B C   
14004 O O   . GLY B 326 ? 0.7549 0.8946 0.6968 0.0139  -0.0607 0.0339  330 GLY B O   
14008 N N   . ALA B 327 ? 0.6760 0.8307 0.6545 0.0069  -0.0628 0.0296  331 ALA B N   
14009 C CA  . ALA B 327 ? 0.6942 0.8411 0.6830 0.0179  -0.0519 0.0341  331 ALA B CA  
14010 C C   . ALA B 327 ? 0.7164 0.8759 0.7102 0.0305  -0.0542 0.0466  331 ALA B C   
14011 O O   . ALA B 327 ? 0.7449 0.9294 0.7476 0.0321  -0.0638 0.0529  331 ALA B O   
14012 C CB  . ALA B 327 ? 0.6975 0.8449 0.7059 0.0155  -0.0477 0.0307  331 ALA B CB  
14018 N N   . THR B 328 ? 0.7351 0.8768 0.7228 0.0396  -0.0456 0.0505  332 THR B N   
14019 C CA  . THR B 328 ? 0.7469 0.8904 0.7354 0.0540  -0.0459 0.0618  332 THR B CA  
14020 C C   . THR B 328 ? 0.6701 0.7936 0.6629 0.0601  -0.0355 0.0615  332 THR B C   
14021 O O   . THR B 328 ? 0.6138 0.7246 0.6084 0.0524  -0.0290 0.0536  332 THR B O   
14022 C CB  . THR B 328 ? 0.8319 0.9660 0.7972 0.0580  -0.0486 0.0692  332 THR B CB  
14023 O OG1 . THR B 328 ? 0.8686 0.9775 0.8180 0.0519  -0.0393 0.0652  332 THR B OG1 
14024 C CG2 . THR B 328 ? 0.8820 1.0356 0.8393 0.0515  -0.0608 0.0692  332 THR B CG2 
14032 N N   . VAL B 329 ? 0.6713 0.7912 0.6644 0.0747  -0.0346 0.0700  333 VAL B N   
14033 C CA  . VAL B 329 ? 0.6752 0.7732 0.6683 0.0811  -0.0260 0.0692  333 VAL B CA  
14034 C C   . VAL B 329 ? 0.6851 0.7572 0.6588 0.0919  -0.0242 0.0781  333 VAL B C   
14035 O O   . VAL B 329 ? 0.6700 0.7498 0.6385 0.1033  -0.0299 0.0876  333 VAL B O   
14036 C CB  . VAL B 329 ? 0.6959 0.8111 0.7074 0.0901  -0.0249 0.0692  333 VAL B CB  
14037 C CG1 . VAL B 329 ? 0.6583 0.7462 0.6634 0.0975  -0.0164 0.0674  333 VAL B CG1 
14038 C CG2 . VAL B 329 ? 0.6971 0.8339 0.7255 0.0772  -0.0266 0.0619  333 VAL B CG2 
14048 N N   . GLY B 330 ? 0.7106 0.7515 0.6732 0.0878  -0.0171 0.0757  334 GLY B N   
14049 C CA  . GLY B 330 ? 0.7208 0.7289 0.6622 0.0957  -0.0147 0.0838  334 GLY B CA  
14050 C C   . GLY B 330 ? 0.7497 0.7305 0.6870 0.1000  -0.0089 0.0802  334 GLY B C   
14051 O O   . GLY B 330 ? 0.6884 0.6691 0.6343 0.0896  -0.0057 0.0711  334 GLY B O   
14055 N N   . LEU B 331 ? 0.8259 0.7815 0.7477 0.1162  -0.0081 0.0874  335 LEU B N   
14056 C CA  . LEU B 331 ? 0.8229 0.7464 0.7346 0.1226  -0.0028 0.0833  335 LEU B CA  
14057 C C   . LEU B 331 ? 0.7850 0.6685 0.6766 0.1061  0.0000  0.0821  335 LEU B C   
14058 O O   . LEU B 331 ? 0.7779 0.6356 0.6495 0.1055  -0.0005 0.0910  335 LEU B O   
14059 C CB  . LEU B 331 ? 0.8735 0.7831 0.7746 0.1491  -0.0024 0.0909  335 LEU B CB  
14060 C CG  . LEU B 331 ? 0.8843 0.7514 0.7666 0.1586  0.0037  0.0861  335 LEU B CG  
14061 C CD1 . LEU B 331 ? 0.8470 0.7263 0.7421 0.1508  0.0074  0.0735  335 LEU B CD1 
14062 C CD2 . LEU B 331 ? 0.9154 0.7758 0.7907 0.1898  0.0054  0.0934  335 LEU B CD2 
14074 N N   . LEU B 332 ? 0.7993 0.6790 0.6964 0.0918  0.0023  0.0722  336 LEU B N   
14075 C CA  . LEU B 332 ? 0.8206 0.6724 0.7052 0.0721  0.0038  0.0706  336 LEU B CA  
14076 C C   . LEU B 332 ? 0.8275 0.6329 0.6893 0.0753  0.0053  0.0675  336 LEU B C   
14077 O O   . LEU B 332 ? 0.8285 0.6326 0.6913 0.0865  0.0064  0.0605  336 LEU B O   
14078 C CB  . LEU B 332 ? 0.8290 0.7082 0.7345 0.0540  0.0038  0.0622  336 LEU B CB  
14079 C CG  . LEU B 332 ? 0.8587 0.7234 0.7597 0.0316  0.0049  0.0614  336 LEU B CG  
14080 C CD1 . LEU B 332 ? 0.9022 0.7723 0.7996 0.0227  0.0070  0.0702  336 LEU B CD1 
14081 C CD2 . LEU B 332 ? 0.8092 0.7000 0.7317 0.0204  0.0040  0.0523  336 LEU B CD2 
14093 N N   . GLN B 333 ? 0.8562 0.6215 0.6947 0.0647  0.0055  0.0727  337 GLN B N   
14094 C CA  . GLN B 333 ? 0.8761 0.5904 0.6884 0.0630  0.0058  0.0684  337 GLN B CA  
14095 C C   . GLN B 333 ? 0.8482 0.5690 0.6696 0.0436  0.0041  0.0570  337 GLN B C   
14096 O O   . GLN B 333 ? 0.8544 0.6146 0.7012 0.0292  0.0031  0.0548  337 GLN B O   
14097 C CB  . GLN B 333 ? 0.9490 0.6163 0.7329 0.0528  0.0058  0.0779  337 GLN B CB  
14098 C CG  . GLN B 333 ? 1.0253 0.6748 0.7925 0.0753  0.0064  0.0901  337 GLN B CG  
14099 C CD  . GLN B 333 ? 1.1222 0.7227 0.8590 0.0637  0.0065  0.1014  337 GLN B CD  
14100 O OE1 . GLN B 333 ? 1.2033 0.7759 0.9282 0.0388  0.0062  0.0992  337 GLN B OE1 
14101 N NE2 . GLN B 333 ? 1.1424 0.7331 0.8661 0.0806  0.0062  0.1146  337 GLN B NE2 
14110 N N   . LYS B 334 ? 0.9249 0.6048 0.7232 0.0444  0.0033  0.0497  338 LYS B N   
14111 C CA  . LYS B 334 ? 0.9706 0.6549 0.7738 0.0273  -0.0002 0.0389  338 LYS B CA  
14112 C C   . LYS B 334 ? 0.8933 0.5826 0.7040 -0.0037 -0.0040 0.0412  338 LYS B C   
14113 O O   . LYS B 334 ? 0.8452 0.5555 0.6705 -0.0188 -0.0081 0.0345  338 LYS B O   
14114 C CB  . LYS B 334 ? 1.1712 0.8037 0.9405 0.0341  -0.0007 0.0302  338 LYS B CB  
14115 C CG  . LYS B 334 ? 1.3447 0.9710 1.1049 0.0675  0.0054  0.0286  338 LYS B CG  
14116 C CD  . LYS B 334 ? 1.4169 1.1008 1.2093 0.0781  0.0077  0.0256  338 LYS B CD  
14117 C CE  . LYS B 334 ? 1.4819 1.1691 1.2707 0.1104  0.0147  0.0264  338 LYS B CE  
14118 N NZ  . LYS B 334 ? 1.5584 1.1945 1.3107 0.1235  0.0185  0.0180  338 LYS B NZ  
14132 N N   . ASP B 335 ? 0.9266 0.5997 0.7283 -0.0132 -0.0027 0.0517  339 ASP B N   
14133 C CA  . ASP B 335 ? 0.9545 0.6368 0.7651 -0.0431 -0.0044 0.0561  339 ASP B CA  
14134 C C   . ASP B 335 ? 0.9351 0.6573 0.7669 -0.0452 0.0005  0.0659  339 ASP B C   
14135 O O   . ASP B 335 ? 0.9641 0.6928 0.8006 -0.0676 0.0019  0.0724  339 ASP B O   
14136 C CB  . ASP B 335 ? 0.9951 0.6172 0.7711 -0.0594 -0.0066 0.0602  339 ASP B CB  
14137 C CG  . ASP B 335 ? 0.9926 0.5768 0.7425 -0.0437 -0.0025 0.0709  339 ASP B CG  
14138 O OD1 . ASP B 335 ? 0.9341 0.5441 0.6950 -0.0211 0.0013  0.0754  339 ASP B OD1 
14139 O OD2 . ASP B 335 ? 1.0552 0.5823 0.7722 -0.0545 -0.0040 0.0752  339 ASP B OD2 
14144 N N   . SER B 336 ? 0.8742 0.6237 0.7178 -0.0234 0.0034  0.0671  340 SER B N   
14145 C CA  . SER B 336 ? 0.8647 0.6482 0.7227 -0.0233 0.0075  0.0749  340 SER B CA  
14146 C C   . SER B 336 ? 0.9219 0.6758 0.7565 -0.0293 0.0105  0.0882  340 SER B C   
14147 O O   . SER B 336 ? 0.9271 0.7045 0.7688 -0.0370 0.0148  0.0954  340 SER B O   
14148 C CB  . SER B 336 ? 0.8214 0.6494 0.7084 -0.0403 0.0091  0.0716  340 SER B CB  
14149 O OG  . SER B 336 ? 0.7870 0.6417 0.6945 -0.0335 0.0060  0.0610  340 SER B OG  
14155 N N   . GLY B 337 ? 0.9507 0.6502 0.7541 -0.0250 0.0087  0.0918  341 GLY B N   
14156 C CA  . GLY B 337 ? 0.9660 0.6302 0.7431 -0.0312 0.0110  0.1058  341 GLY B CA  
14157 C C   . GLY B 337 ? 0.9376 0.6198 0.7134 -0.0149 0.0133  0.1161  341 GLY B C   
14158 O O   . GLY B 337 ? 0.9476 0.6160 0.7073 -0.0244 0.0165  0.1290  341 GLY B O   
14162 N N   . ASN B 338 ? 0.9329 0.6464 0.7243 0.0079  0.0114  0.1112  342 ASN B N   
14163 C CA  . ASN B 338 ? 0.9565 0.6875 0.7455 0.0244  0.0109  0.1201  342 ASN B CA  
14164 C C   . ASN B 338 ? 0.9144 0.7030 0.7311 0.0217  0.0119  0.1152  342 ASN B C   
14165 O O   . ASN B 338 ? 0.9292 0.7394 0.7482 0.0366  0.0091  0.1185  342 ASN B O   
14166 C CB  . ASN B 338 ? 0.9958 0.7153 0.7781 0.0542  0.0067  0.1204  342 ASN B CB  
14167 C CG  . ASN B 338 ? 1.0107 0.7621 0.8189 0.0641  0.0052  0.1068  342 ASN B CG  
14168 O OD1 . ASN B 338 ? 0.9788 0.7370 0.7996 0.0501  0.0064  0.0962  342 ASN B OD1 
14169 N ND2 . ASN B 338 ? 1.0257 0.7989 0.8425 0.0875  0.0023  0.1082  342 ASN B ND2 
14176 N N   . ILE B 339 ? 0.9234 0.8514 0.6920 -0.0187 0.0931  0.0755  343 ILE B N   
14177 C CA  . ILE B 339 ? 0.9152 0.8528 0.6713 -0.0114 0.0795  0.0925  343 ILE B CA  
14178 C C   . ILE B 339 ? 0.8512 0.8222 0.6565 0.0233  0.0653  0.1063  343 ILE B C   
14179 O O   . ILE B 339 ? 0.8186 0.8045 0.6376 0.0341  0.0662  0.1059  343 ILE B O   
14180 C CB  . ILE B 339 ? 0.9514 0.8679 0.6568 -0.0313 0.0540  0.1178  343 ILE B CB  
14181 C CG1 . ILE B 339 ? 0.9063 0.8307 0.6169 -0.0238 0.0373  0.1317  343 ILE B CG1 
14182 C CG2 . ILE B 339 ? 0.9760 0.9000 0.6957 -0.0191 0.0320  0.1382  343 ILE B CG2 
14183 C CD1 . ILE B 339 ? 0.8380 0.7554 0.5314 -0.0371 0.0571  0.1139  343 ILE B CD1 
14195 N N   . LEU B 340 ? 0.8499 0.8308 0.6751 0.0348  0.0524  0.1182  344 LEU B N   
14196 C CA  . LEU B 340 ? 0.8474 0.8550 0.7025 0.0531  0.0398  0.1304  344 LEU B CA  
14197 C C   . LEU B 340 ? 0.8478 0.8622 0.7412 0.0629  0.0449  0.1191  344 LEU B C   
14198 O O   . LEU B 340 ? 0.8626 0.8946 0.7646 0.0706  0.0405  0.1244  344 LEU B O   
14199 C CB  . LEU B 340 ? 0.8783 0.8892 0.7378 0.0531  0.0250  0.1447  344 LEU B CB  
14200 C CG  . LEU B 340 ? 0.9223 0.9537 0.7964 0.0566  0.0113  0.1575  344 LEU B CG  
14201 C CD1 . LEU B 340 ? 0.9483 1.0041 0.8153 0.0566  0.0156  0.1583  344 LEU B CD1 
14202 C CD2 . LEU B 340 ? 0.9639 0.9932 0.8309 0.0477  -0.0035 0.1720  344 LEU B CD2 
14214 N N   . GLN B 341 ? 0.8426 0.8433 0.7684 0.0611  0.0539  0.1005  345 GLN B N   
14215 C CA  . GLN B 341 ? 0.8596 0.8654 0.8451 0.0710  0.0533  0.0878  345 GLN B CA  
14216 C C   . GLN B 341 ? 0.8399 0.8523 0.8199 0.0709  0.0729  0.0721  345 GLN B C   
14217 O O   . GLN B 341 ? 0.8111 0.8360 0.8216 0.0816  0.0639  0.0755  345 GLN B O   
14218 C CB  . GLN B 341 ? 0.9837 0.9748 1.0293 0.0685  0.0615  0.0618  345 GLN B CB  
14219 C CG  . GLN B 341 ? 1.1337 1.1153 1.1947 0.0692  0.0371  0.0783  345 GLN B CG  
14220 C CD  . GLN B 341 ? 1.2303 1.2002 1.2353 0.0550  0.0501  0.0776  345 GLN B CD  
14221 O OE1 . GLN B 341 ? 1.2239 1.1978 1.1640 0.0495  0.0497  0.0950  345 GLN B OE1 
14222 N NE2 . GLN B 341 ? 1.2902 1.2444 1.3296 0.0478  0.0595  0.0558  345 GLN B NE2 
14231 N N   . LEU B 342 ? 0.8572 0.8575 0.7930 0.0535  0.0963  0.0573  346 LEU B N   
14232 C CA  . LEU B 342 ? 0.8407 0.8434 0.7609 0.0475  0.1123  0.0455  346 LEU B CA  
14233 C C   . LEU B 342 ? 0.8020 0.8229 0.7106 0.0626  0.0934  0.0702  346 LEU B C   
14234 O O   . LEU B 342 ? 0.7800 0.8131 0.7115 0.0714  0.0963  0.0647  346 LEU B O   
14235 C CB  . LEU B 342 ? 0.8819 0.8601 0.7358 0.0148  0.1295  0.0359  346 LEU B CB  
14236 C CG  . LEU B 342 ? 0.9703 0.9292 0.8224 -0.0141 0.1611  -0.0002 346 LEU B CG  
14237 C CD1 . LEU B 342 ? 1.0033 0.9306 0.7631 -0.0589 0.1685  0.0009  346 LEU B CD1 
14238 C CD2 . LEU B 342 ? 0.9899 0.9592 0.9055 -0.0151 0.1926  -0.0423 346 LEU B CD2 
14250 N N   . ILE B 343 ? 0.8025 0.8267 0.6828 0.0638  0.0761  0.0930  347 ILE B N   
14251 C CA  . ILE B 343 ? 0.8188 0.8626 0.6978 0.0731  0.0652  0.1062  347 ILE B CA  
14252 C C   . ILE B 343 ? 0.8201 0.8843 0.7293 0.0844  0.0584  0.1101  347 ILE B C   
14253 O O   . ILE B 343 ? 0.8085 0.8857 0.7247 0.0893  0.0604  0.1080  347 ILE B O   
14254 C CB  . ILE B 343 ? 0.8185 0.8651 0.6842 0.0700  0.0511  0.1212  347 ILE B CB  
14255 C CG1 . ILE B 343 ? 0.8228 0.8420 0.6567 0.0530  0.0461  0.1242  347 ILE B CG1 
14256 C CG2 . ILE B 343 ? 0.8169 0.8904 0.7020 0.0776  0.0468  0.1238  347 ILE B CG2 
14257 C CD1 . ILE B 343 ? 0.8259 0.8430 0.6621 0.0493  0.0256  0.1393  347 ILE B CD1 
14269 N N   . ILE B 344 ? 0.8188 0.8816 0.7422 0.0840  0.0458  0.1184  348 ILE B N   
14270 C CA  . ILE B 344 ? 0.8022 0.8748 0.7430 0.0833  0.0284  0.1297  348 ILE B CA  
14271 C C   . ILE B 344 ? 0.7671 0.8367 0.7480 0.0909  0.0286  0.1192  348 ILE B C   
14272 O O   . ILE B 344 ? 0.8029 0.8825 0.7865 0.0894  0.0194  0.1259  348 ILE B O   
14273 C CB  . ILE B 344 ? 0.8158 0.8786 0.7627 0.0751  0.0061  0.1455  348 ILE B CB  
14274 C CG1 . ILE B 344 ? 0.8744 0.9445 0.7838 0.0653  0.0082  0.1537  348 ILE B CG1 
14275 C CG2 . ILE B 344 ? 0.7634 0.8252 0.7207 0.0637  -0.0230 0.1636  348 ILE B CG2 
14276 C CD1 . ILE B 344 ? 0.9223 1.0167 0.8068 0.0530  0.0134  0.1555  348 ILE B CD1 
14288 N N   . SER B 345 ? 0.7281 0.7846 0.7438 0.0952  0.0417  0.0985  349 SER B N   
14289 C CA  . SER B 345 ? 0.7092 0.7661 0.7797 0.1015  0.0467  0.0804  349 SER B CA  
14290 C C   . SER B 345 ? 0.6860 0.7547 0.7295 0.1030  0.0627  0.0748  349 SER B C   
14291 O O   . SER B 345 ? 0.6579 0.7348 0.7278 0.1080  0.0529  0.0772  349 SER B O   
14292 C CB  . SER B 345 ? 0.6957 0.7405 0.8107 0.0986  0.0710  0.0464  349 SER B CB  
14293 O OG  . SER B 345 ? 0.7787 0.8123 0.9385 0.0996  0.0535  0.0485  349 SER B OG  
14299 N N   . ALA B 346 ? 0.7155 0.7817 0.7082 0.0964  0.0818  0.0699  350 ALA B N   
14300 C CA  . ALA B 346 ? 0.7121 0.7853 0.6824 0.0961  0.0918  0.0665  350 ALA B CA  
14301 C C   . ALA B 346 ? 0.7289 0.8211 0.6939 0.1028  0.0760  0.0839  350 ALA B C   
14302 O O   . ALA B 346 ? 0.7400 0.8413 0.7159 0.1067  0.0778  0.0802  350 ALA B O   
14303 C CB  . ALA B 346 ? 0.6994 0.7585 0.6189 0.0824  0.1003  0.0667  350 ALA B CB  
14309 N N   . TYR B 347 ? 0.7457 0.8448 0.6928 0.0994  0.0639  0.0991  351 TYR B N   
14310 C CA  . TYR B 347 ? 0.7460 0.8644 0.6834 0.0945  0.0571  0.1072  351 TYR B CA  
14311 C C   . TYR B 347 ? 0.7350 0.8538 0.6886 0.0899  0.0403  0.1154  351 TYR B C   
14312 O O   . TYR B 347 ? 0.7553 0.8850 0.7043 0.0860  0.0407  0.1145  351 TYR B O   
14313 C CB  . TYR B 347 ? 0.7578 0.8839 0.6765 0.0838  0.0527  0.1151  351 TYR B CB  
14314 C CG  . TYR B 347 ? 0.7486 0.8962 0.6530 0.0667  0.0545  0.1144  351 TYR B CG  
14315 C CD1 . TYR B 347 ? 0.7504 0.9168 0.6629 0.0675  0.0708  0.0980  351 TYR B CD1 
14316 C CD2 . TYR B 347 ? 0.7629 0.9094 0.6452 0.0432  0.0392  0.1281  351 TYR B CD2 
14317 C CE1 . TYR B 347 ? 0.7775 0.9659 0.6795 0.0452  0.0812  0.0875  351 TYR B CE1 
14318 C CE2 . TYR B 347 ? 0.7886 0.9527 0.6431 0.0142  0.0463  0.1229  351 TYR B CE2 
14319 C CZ  . TYR B 347 ? 0.7960 0.9835 0.6619 0.0152  0.0719  0.0986  351 TYR B CZ  
14320 O OH  . TYR B 347 ? 0.8379 1.0454 0.6790 -0.0200 0.0874  0.0839  351 TYR B OH  
14330 N N   . GLU B 348 ? 0.7500 0.8538 0.7281 0.0881  0.0207  0.1248  352 GLU B N   
14331 C CA  . GLU B 348 ? 0.8003 0.8965 0.8051 0.0801  -0.0094 0.1390  352 GLU B CA  
14332 C C   . GLU B 348 ? 0.7910 0.8893 0.8372 0.0930  -0.0028 0.1246  352 GLU B C   
14333 O O   . GLU B 348 ? 0.7925 0.8927 0.8405 0.0844  -0.0207 0.1352  352 GLU B O   
14334 C CB  . GLU B 348 ? 0.8360 0.9114 0.8809 0.0778  -0.0382 0.1508  352 GLU B CB  
14335 C CG  . GLU B 348 ? 0.9196 0.9907 0.9180 0.0578  -0.0526 0.1710  352 GLU B CG  
14336 C CD  . GLU B 348 ? 0.9798 1.0266 1.0214 0.0546  -0.0870 0.1855  352 GLU B CD  
14337 O OE1 . GLU B 348 ? 0.9868 1.0248 1.1006 0.0744  -0.0839 0.1676  352 GLU B OE1 
14338 O OE2 . GLU B 348 ? 1.0220 1.0578 1.0278 0.0281  -0.1162 0.2119  352 GLU B OE2 
14345 N N   . GLU B 349 ? 0.7900 0.8868 0.8641 0.1077  0.0238  0.0994  353 GLU B N   
14346 C CA  . GLU B 349 ? 0.8545 0.9557 0.9648 0.1157  0.0369  0.0805  353 GLU B CA  
14347 C C   . GLU B 349 ? 0.8192 0.9346 0.8842 0.1140  0.0468  0.0836  353 GLU B C   
14348 O O   . GLU B 349 ? 0.8366 0.9569 0.9236 0.1158  0.0414  0.0818  353 GLU B O   
14349 C CB  . GLU B 349 ? 0.9626 1.0586 1.0919 0.1185  0.0713  0.0483  353 GLU B CB  
14350 C CG  . GLU B 349 ? 1.0817 1.1827 1.2550 0.1209  0.0902  0.0219  353 GLU B CG  
14351 C CD  . GLU B 349 ? 1.2440 1.3383 1.4234 0.1094  0.1307  -0.0159 353 GLU B CD  
14352 O OE1 . GLU B 349 ? 1.3088 1.3920 1.4463 0.0988  0.1416  -0.0172 353 GLU B OE1 
14353 O OE2 . GLU B 349 ? 1.3001 1.3995 1.5233 0.1054  0.1530  -0.0460 353 GLU B OE2 
14360 N N   . LEU B 350 ? 0.7773 0.8992 0.7897 0.1106  0.0593  0.0863  354 LEU B N   
14361 C CA  . LEU B 350 ? 0.7608 0.8968 0.7469 0.1092  0.0681  0.0845  354 LEU B CA  
14362 C C   . LEU B 350 ? 0.7842 0.9301 0.7590 0.0956  0.0511  0.0975  354 LEU B C   
14363 O O   . LEU B 350 ? 0.7952 0.9483 0.7714 0.0942  0.0522  0.0943  354 LEU B O   
14364 C CB  . LEU B 350 ? 0.7551 0.8948 0.7131 0.1079  0.0789  0.0823  354 LEU B CB  
14365 C CG  . LEU B 350 ? 0.7773 0.9004 0.7277 0.1101  0.0899  0.0743  354 LEU B CG  
14366 C CD1 . LEU B 350 ? 0.7994 0.9213 0.7351 0.1067  0.0858  0.0795  354 LEU B CD1 
14367 C CD2 . LEU B 350 ? 0.7673 0.8872 0.7177 0.1107  0.0999  0.0640  354 LEU B CD2 
14379 N N   . ARG B 351 ? 0.8194 0.9630 0.7749 0.0789  0.0347  0.1126  355 ARG B N   
14380 C CA  . ARG B 351 ? 0.8692 1.0148 0.7965 0.0508  0.0157  0.1270  355 ARG B CA  
14381 C C   . ARG B 351 ? 0.8750 1.0044 0.8342 0.0478  -0.0170 0.1424  355 ARG B C   
14382 O O   . ARG B 351 ? 0.8920 1.0170 0.8222 0.0189  -0.0387 0.1579  355 ARG B O   
14383 C CB  . ARG B 351 ? 0.9191 1.0602 0.8108 0.0243  0.0032  0.1411  355 ARG B CB  
14384 C CG  . ARG B 351 ? 0.9366 1.0946 0.8125 0.0262  0.0321  0.1246  355 ARG B CG  
14385 C CD  . ARG B 351 ? 0.9476 1.1314 0.8114 0.0163  0.0611  0.1009  355 ARG B CD  
14386 N NE  . ARG B 351 ? 0.9604 1.1498 0.7803 -0.0260 0.0584  0.1023  355 ARG B NE  
14387 C CZ  . ARG B 351 ? 0.9862 1.1751 0.7593 -0.0686 0.0548  0.1077  355 ARG B CZ  
14388 N NH1 . ARG B 351 ? 1.0743 1.2594 0.8467 -0.0681 0.0520  0.1133  355 ARG B NH1 
14389 N NH2 . ARG B 351 ? 0.9782 1.1681 0.6976 -0.1181 0.0538  0.1075  355 ARG B NH2 
14403 N N   . SER B 352 ? 0.8964 1.0158 0.9187 0.0720  -0.0212 0.1360  356 SER B N   
14404 C CA  . SER B 352 ? 0.9360 1.0417 1.0197 0.0736  -0.0533 0.1445  356 SER B CA  
14405 C C   . SER B 352 ? 0.8850 1.0021 0.9970 0.0891  -0.0336 0.1248  356 SER B C   
14406 O O   . SER B 352 ? 0.8927 1.0016 1.0709 0.0932  -0.0569 0.1262  356 SER B O   
14407 C CB  . SER B 352 ? 1.0113 1.1020 1.1717 0.0879  -0.0669 0.1397  356 SER B CB  
14408 O OG  . SER B 352 ? 1.1200 1.2054 1.3728 0.0997  -0.0816 0.1293  356 SER B OG  
14414 N N   . GLU B 353 ? 0.8621 0.9959 0.9339 0.0967  0.0046  0.1070  357 GLU B N   
14415 C CA  . GLU B 353 ? 0.9049 1.0474 0.9960 0.1087  0.0244  0.0887  357 GLU B CA  
14416 C C   . GLU B 353 ? 0.8928 1.0495 0.9295 0.1006  0.0380  0.0879  357 GLU B C   
14417 O O   . GLU B 353 ? 0.9188 1.0827 0.9109 0.0895  0.0449  0.0908  357 GLU B O   
14418 C CB  . GLU B 353 ? 0.9942 1.1364 1.1021 0.1231  0.0582  0.0622  357 GLU B CB  
14419 C CG  . GLU B 353 ? 1.1359 1.2685 1.3135 0.1287  0.0573  0.0476  357 GLU B CG  
14420 C CD  . GLU B 353 ? 1.2173 1.3479 1.3922 0.1283  0.0976  0.0165  357 GLU B CD  
14421 O OE1 . GLU B 353 ? 1.2382 1.3683 1.3483 0.1230  0.1151  0.0170  357 GLU B OE1 
14422 O OE2 . GLU B 353 ? 1.2528 1.3802 1.4933 0.1282  0.1103  -0.0099 357 GLU B OE2 
14429 N N   . VAL B 354 ? 0.8574 1.0195 0.9086 0.1056  0.0440  0.0794  358 VAL B N   
14430 C CA  . VAL B 354 ? 0.8116 0.9872 0.8270 0.1012  0.0601  0.0722  358 VAL B CA  
14431 C C   . VAL B 354 ? 0.7336 0.9104 0.7726 0.1166  0.0786  0.0551  358 VAL B C   
14432 O O   . VAL B 354 ? 0.7316 0.9067 0.8081 0.1195  0.0706  0.0530  358 VAL B O   
14433 C CB  . VAL B 354 ? 0.8686 1.0467 0.8606 0.0774  0.0404  0.0853  358 VAL B CB  
14434 C CG1 . VAL B 354 ? 0.8607 1.0535 0.8331 0.0755  0.0614  0.0699  358 VAL B CG1 
14435 C CG2 . VAL B 354 ? 0.9096 1.0855 0.8573 0.0490  0.0283  0.0988  358 VAL B CG2 
14445 N N   . GLU B 355 ? 0.6544 0.8314 0.6744 0.1223  0.0995  0.0438  359 GLU B N   
14446 C CA  . GLU B 355 ? 0.6855 0.8582 0.7108 0.1268  0.1152  0.0302  359 GLU B CA  
14447 C C   . GLU B 355 ? 0.7079 0.8876 0.7142 0.1260  0.1191  0.0279  359 GLU B C   
14448 O O   . GLU B 355 ? 0.7221 0.9049 0.7171 0.1246  0.1186  0.0287  359 GLU B O   
14449 C CB  . GLU B 355 ? 0.7497 0.9064 0.7645 0.1235  0.1286  0.0223  359 GLU B CB  
14450 C CG  . GLU B 355 ? 0.8608 1.0072 0.8645 0.1147  0.1444  0.0090  359 GLU B CG  
14451 C CD  . GLU B 355 ? 1.0036 1.1289 0.9824 0.0966  0.1585  -0.0003 359 GLU B CD  
14452 O OE1 . GLU B 355 ? 1.0649 1.1870 1.0505 0.0962  0.1596  -0.0012 359 GLU B OE1 
14453 O OE2 . GLU B 355 ? 1.0730 1.1820 1.0195 0.0772  0.1674  -0.0062 359 GLU B OE2 
14460 N N   . LEU B 356 ? 0.7179 0.9010 0.7324 0.1269  0.1227  0.0218  360 LEU B N   
14461 C CA  . LEU B 356 ? 0.7016 0.8902 0.7085 0.1265  0.1257  0.0168  360 LEU B CA  
14462 C C   . LEU B 356 ? 0.6994 0.8696 0.6969 0.1249  0.1279  0.0147  360 LEU B C   
14463 O O   . LEU B 356 ? 0.6898 0.8437 0.6754 0.1177  0.1339  0.0131  360 LEU B O   
14464 C CB  . LEU B 356 ? 0.6623 0.8596 0.6782 0.1257  0.1257  0.0132  360 LEU B CB  
14465 C CG  . LEU B 356 ? 0.6423 0.8543 0.6503 0.1150  0.1189  0.0159  360 LEU B CG  
14466 C CD1 . LEU B 356 ? 0.6477 0.8644 0.6611 0.1123  0.1177  0.0127  360 LEU B CD1 
14467 C CD2 . LEU B 356 ? 0.6369 0.8601 0.6361 0.1076  0.1278  0.0054  360 LEU B CD2 
14479 N N   . GLU B 357 ? 0.6783 0.8490 0.6842 0.1258  0.1216  0.0128  361 GLU B N   
14480 C CA  . GLU B 357 ? 0.7130 0.8589 0.7146 0.1192  0.1088  0.0182  361 GLU B CA  
14481 C C   . GLU B 357 ? 0.7103 0.8605 0.7400 0.1224  0.1022  0.0112  361 GLU B C   
14482 O O   . GLU B 357 ? 0.7287 0.9023 0.7917 0.1292  0.1078  -0.0023 361 GLU B O   
14483 C CB  . GLU B 357 ? 0.8024 0.9384 0.8114 0.1178  0.0951  0.0257  361 GLU B CB  
14484 C CG  . GLU B 357 ? 0.9315 1.0291 0.9119 0.0995  0.0759  0.0411  361 GLU B CG  
14485 C CD  . GLU B 357 ? 1.0123 1.0994 1.0106 0.0987  0.0551  0.0507  361 GLU B CD  
14486 O OE1 . GLU B 357 ? 0.9807 1.0947 1.0222 0.1139  0.0603  0.0400  361 GLU B OE1 
14487 O OE2 . GLU B 357 ? 1.0907 1.1416 1.0575 0.0774  0.0338  0.0678  361 GLU B OE2 
14494 N N   . VAL B 358 ? 0.7094 0.8368 0.7252 0.1126  0.0926  0.0171  362 VAL B N   
14495 C CA  . VAL B 358 ? 0.7139 0.8402 0.7607 0.1149  0.0817  0.0120  362 VAL B CA  
14496 C C   . VAL B 358 ? 0.7833 0.8738 0.8439 0.1032  0.0457  0.0276  362 VAL B C   
14497 O O   . VAL B 358 ? 0.8675 0.9226 0.8778 0.0795  0.0314  0.0457  362 VAL B O   
14498 C CB  . VAL B 358 ? 0.7041 0.8298 0.7270 0.1096  0.0929  0.0092  362 VAL B CB  
14499 C CG1 . VAL B 358 ? 0.7293 0.8526 0.7864 0.1121  0.0801  0.0040  362 VAL B CG1 
14500 C CG2 . VAL B 358 ? 0.6683 0.8236 0.6880 0.1187  0.1170  -0.0010 362 VAL B CG2 
14510 N N   . LEU B 359 ? 0.7699 0.8677 0.9025 0.1141  0.0295  0.0187  363 LEU B N   
14511 C CA  . LEU B 359 ? 0.8241 0.8861 0.9978 0.1047  -0.0169 0.0349  363 LEU B CA  
14512 C C   . LEU B 359 ? 0.7990 0.8615 1.0441 0.1114  -0.0329 0.0229  363 LEU B C   
14513 O O   . LEU B 359 ? 0.7840 0.8824 1.0546 0.1251  -0.0015 -0.0048 363 LEU B O   
14514 C CB  . LEU B 359 ? 0.8527 0.9214 1.0821 0.1128  -0.0285 0.0310  363 LEU B CB  
14515 C CG  . LEU B 359 ? 0.9492 1.0080 1.1164 0.1036  -0.0240 0.0472  363 LEU B CG  
14516 C CD1 . LEU B 359 ? 0.8878 0.9811 1.0059 0.1124  0.0235  0.0333  363 LEU B CD1 
14517 C CD2 . LEU B 359 ? 1.0246 1.0837 1.2597 0.1096  -0.0458 0.0461  363 LEU B CD2 
14529 N N   . GLY B 360 ? 0.7933 0.8117 1.0702 0.0971  -0.0865 0.0454  364 GLY B N   
14530 C CA  . GLY B 360 ? 0.7970 0.8098 1.1604 0.1032  -0.1116 0.0356  364 GLY B CA  
14531 C C   . GLY B 360 ? 0.8532 0.8225 1.1606 0.0782  -0.1413 0.0635  364 GLY B C   
14532 O O   . GLY B 360 ? 0.9245 0.8524 1.1377 0.0456  -0.1608 0.0966  364 GLY B O   
14536 N N   . ASP B 361 ? 0.8533 0.8315 1.2146 0.0879  -0.1420 0.0472  365 ASP B N   
14537 C CA  . ASP B 361 ? 0.9348 0.8715 1.2532 0.0631  -0.1733 0.0722  365 ASP B CA  
14538 C C   . ASP B 361 ? 0.9151 0.8732 1.1302 0.0581  -0.1208 0.0651  365 ASP B C   
14539 O O   . ASP B 361 ? 0.8601 0.8471 1.0928 0.0733  -0.0928 0.0424  365 ASP B O   
14540 C CB  . ASP B 361 ? 0.9744 0.9100 1.4118 0.0769  -0.2011 0.0566  365 ASP B CB  
14541 C CG  . ASP B 361 ? 1.0751 0.9552 1.4786 0.0460  -0.2516 0.0908  365 ASP B CG  
14542 O OD1 . ASP B 361 ? 1.1450 0.9867 1.4251 0.0076  -0.2626 0.1252  365 ASP B OD1 
14543 O OD2 . ASP B 361 ? 1.0911 0.9655 1.5924 0.0557  -0.2789 0.0804  365 ASP B OD2 
14548 N N   . THR B 362 ? 0.9761 0.9191 1.0892 0.0340  -0.1079 0.0822  366 THR B N   
14549 C CA  . THR B 362 ? 1.0014 0.9660 1.0362 0.0286  -0.0582 0.0707  366 THR B CA  
14550 C C   . THR B 362 ? 1.0901 1.0115 1.0349 -0.0184 -0.0696 0.0911  366 THR B C   
14551 O O   . THR B 362 ? 1.0925 1.0325 0.9908 -0.0245 -0.0284 0.0759  366 THR B O   
14552 C CB  . THR B 362 ? 0.9789 0.9703 0.9816 0.0373  -0.0207 0.0606  366 THR B CB  
14553 O OG1 . THR B 362 ? 1.0579 1.0113 1.0197 0.0097  -0.0466 0.0837  366 THR B OG1 
14554 C CG2 . THR B 362 ? 0.9185 0.9558 0.9925 0.0756  -0.0011 0.0374  366 THR B CG2 
14563 N N   . GLU B 363 ? 1.1441 1.0064 1.0643 -0.0571 -0.1258 0.1244  367 GLU B N   
14564 C CA  . GLU B 363 ? 1.2037 1.0194 1.0226 -0.1159 -0.1367 0.1436  367 GLU B CA  
14565 C C   . GLU B 363 ? 1.1653 0.9932 0.9920 -0.1110 -0.1232 0.1318  367 GLU B C   
14566 O O   . GLU B 363 ? 1.1220 0.9556 1.0319 -0.0828 -0.1489 0.1311  367 GLU B O   
14567 C CB  . GLU B 363 ? 1.3515 1.0928 1.1459 -0.1644 -0.2151 0.1889  367 GLU B CB  
14568 C CG  . GLU B 363 ? 1.5243 1.2300 1.2258 -0.2131 -0.2211 0.2069  367 GLU B CG  
14569 C CD  . GLU B 363 ? 1.6804 1.3783 1.2549 -0.2679 -0.1713 0.1933  367 GLU B CD  
14570 O OE1 . GLU B 363 ? 1.7323 1.4304 1.2785 -0.2847 -0.1549 0.1845  367 GLU B OE1 
14571 O OE2 . GLU B 363 ? 1.7406 1.4341 1.2502 -0.2957 -0.1452 0.1868  367 GLU B OE2 
14578 N N   . GLY B 364 ? 1.2091 1.0423 0.9567 -0.1402 -0.0802 0.1180  368 GLY B N   
14579 C CA  . GLY B 364 ? 1.2093 1.0565 0.9587 -0.1380 -0.0619 0.1048  368 GLY B CA  
14580 C C   . GLY B 364 ? 1.1502 1.0644 0.9598 -0.0836 -0.0103 0.0694  368 GLY B C   
14581 O O   . GLY B 364 ? 1.1304 1.0592 0.9468 -0.0792 0.0051  0.0576  368 GLY B O   
14585 N N   . LEU B 365 ? 1.1283 1.0797 0.9772 -0.0470 0.0124  0.0549  369 LEU B N   
14586 C CA  . LEU B 365 ? 1.0626 1.0697 0.9586 -0.0049 0.0523  0.0277  369 LEU B CA  
14587 C C   . LEU B 365 ? 1.0558 1.0843 0.9211 -0.0129 0.0969  0.0088  369 LEU B C   
14588 O O   . LEU B 365 ? 1.1143 1.1267 0.9391 -0.0370 0.1036  0.0108  369 LEU B O   
14589 C CB  . LEU B 365 ? 0.9976 1.0310 0.9595 0.0345  0.0468  0.0225  369 LEU B CB  
14590 C CG  . LEU B 365 ? 1.0074 1.0490 1.0402 0.0571  0.0269  0.0170  369 LEU B CG  
14591 C CD1 . LEU B 365 ? 0.9333 1.0029 1.0234 0.0844  0.0325  0.0033  369 LEU B CD1 
14592 C CD2 . LEU B 365 ? 1.0288 1.0955 1.0711 0.0674  0.0489  0.0004  369 LEU B CD2 
14604 N N   . ASN B 366 ? 0.9843 1.0481 0.8779 0.0059  0.1254  -0.0112 370 ASN B N   
14605 C CA  . ASN B 366 ? 0.9373 1.0269 0.8386 0.0065  0.1629  -0.0333 370 ASN B CA  
14606 C C   . ASN B 366 ? 0.8056 0.9279 0.7568 0.0450  0.1647  -0.0360 370 ASN B C   
14607 O O   . ASN B 366 ? 0.7196 0.8599 0.7022 0.0689  0.1553  -0.0339 370 ASN B O   
14608 C CB  . ASN B 366 ? 0.9853 1.0899 0.8983 -0.0012 0.1857  -0.0521 370 ASN B CB  
14609 C CG  . ASN B 366 ? 1.0758 1.1468 0.9317 -0.0453 0.1828  -0.0486 370 ASN B CG  
14610 O OD1 . ASN B 366 ? 1.0694 1.1412 0.9311 -0.0450 0.1776  -0.0481 370 ASN B OD1 
14611 N ND2 . ASN B 366 ? 1.1594 1.1969 0.9522 -0.0895 0.1840  -0.0448 370 ASN B ND2 
14618 N N   . LEU B 367 ? 0.7925 0.9196 0.7454 0.0448  0.1768  -0.0413 371 LEU B N   
14619 C CA  . LEU B 367 ? 0.7407 0.8919 0.7311 0.0731  0.1740  -0.0398 371 LEU B CA  
14620 C C   . LEU B 367 ? 0.7401 0.9083 0.7655 0.0738  0.1952  -0.0577 371 LEU B C   
14621 O O   . LEU B 367 ? 0.7587 0.9179 0.7736 0.0507  0.2173  -0.0744 371 LEU B O   
14622 C CB  . LEU B 367 ? 0.7648 0.9034 0.7387 0.0759  0.1593  -0.0262 371 LEU B CB  
14623 C CG  . LEU B 367 ? 0.7895 0.9093 0.7554 0.0754  0.1329  -0.0117 371 LEU B CG  
14624 C CD1 . LEU B 367 ? 0.8055 0.9104 0.7637 0.0737  0.1179  -0.0001 371 LEU B CD1 
14625 C CD2 . LEU B 367 ? 0.7333 0.8760 0.7374 0.0973  0.1276  -0.0161 371 LEU B CD2 
14637 N N   . SER B 368 ? 0.7627 0.9533 0.8335 0.0951  0.1866  -0.0557 372 SER B N   
14638 C CA  . SER B 368 ? 0.7270 0.9314 0.8545 0.1000  0.1930  -0.0681 372 SER B CA  
14639 C C   . SER B 368 ? 0.6531 0.8630 0.7909 0.1151  0.1703  -0.0500 372 SER B C   
14640 O O   . SER B 368 ? 0.6322 0.8458 0.7503 0.1210  0.1522  -0.0337 372 SER B O   
14641 C CB  . SER B 368 ? 0.7388 0.9585 0.9229 0.1031  0.1929  -0.0792 372 SER B CB  
14642 O OG  . SER B 368 ? 0.7874 1.0175 1.0490 0.1043  0.2004  -0.0990 372 SER B OG  
14648 N N   . PHE B 369 ? 0.6430 0.8527 0.8098 0.1161  0.1737  -0.0561 373 PHE B N   
14649 C CA  . PHE B 369 ? 0.6356 0.8467 0.8089 0.1252  0.1507  -0.0379 373 PHE B CA  
14650 C C   . PHE B 369 ? 0.6313 0.8488 0.8866 0.1299  0.1353  -0.0418 373 PHE B C   
14651 O O   . PHE B 369 ? 0.6827 0.9032 0.9951 0.1276  0.1551  -0.0685 373 PHE B O   
14652 C CB  . PHE B 369 ? 0.6240 0.8246 0.7617 0.1224  0.1596  -0.0364 373 PHE B CB  
14653 C CG  . PHE B 369 ? 0.6488 0.8394 0.7251 0.1182  0.1617  -0.0280 373 PHE B CG  
14654 C CD1 . PHE B 369 ? 0.6657 0.8610 0.7220 0.1243  0.1465  -0.0135 373 PHE B CD1 
14655 C CD2 . PHE B 369 ? 0.6797 0.8538 0.7240 0.1025  0.1770  -0.0366 373 PHE B CD2 
14656 C CE1 . PHE B 369 ? 0.6963 0.8836 0.7247 0.1224  0.1455  -0.0109 373 PHE B CE1 
14657 C CE2 . PHE B 369 ? 0.7478 0.9068 0.7516 0.0976  0.1666  -0.0246 373 PHE B CE2 
14658 C CZ  . PHE B 369 ? 0.7350 0.9023 0.7425 0.1115  0.1503  -0.0133 373 PHE B CZ  
14668 N N   . THR B 370 ? 0.5998 0.8170 0.8646 0.1311  0.0986  -0.0173 374 THR B N   
14669 C CA  . THR B 370 ? 0.6381 0.8524 0.9830 0.1326  0.0655  -0.0095 374 THR B CA  
14670 C C   . THR B 370 ? 0.6826 0.8859 0.9884 0.1254  0.0356  0.0198  374 THR B C   
14671 O O   . THR B 370 ? 0.6837 0.8839 0.9216 0.1118  0.0216  0.0405  374 THR B O   
14672 C CB  . THR B 370 ? 0.6238 0.8393 1.0165 0.1290  0.0359  -0.0006 374 THR B CB  
14673 O OG1 . THR B 370 ? 0.6559 0.8838 1.0868 0.1337  0.0677  -0.0314 374 THR B OG1 
14674 C CG2 . THR B 370 ? 0.5882 0.7939 1.0785 0.1281  -0.0123 0.0129  374 THR B CG2 
14682 N N   . ALA B 371 ? 0.6891 0.8866 1.0370 0.1300  0.0295  0.0175  375 ALA B N   
14683 C CA  . ALA B 371 ? 0.6923 0.8777 1.0041 0.1205  0.0018  0.0445  375 ALA B CA  
14684 C C   . ALA B 371 ? 0.7205 0.8895 1.0945 0.1092  -0.0581 0.0714  375 ALA B C   
14685 O O   . ALA B 371 ? 0.7507 0.9185 1.2373 0.1197  -0.0730 0.0591  375 ALA B O   
14686 C CB  . ALA B 371 ? 0.6842 0.8691 1.0012 0.1297  0.0249  0.0301  375 ALA B CB  
14692 N N   . ILE B 372 ? 0.7567 0.9112 1.0615 0.0822  -0.0937 0.1061  376 ILE B N   
14693 C CA  . ILE B 372 ? 0.8504 0.9782 1.1900 0.0580  -0.1636 0.1431  376 ILE B CA  
14694 C C   . ILE B 372 ? 0.8616 0.9730 1.1377 0.0349  -0.1838 0.1680  376 ILE B C   
14695 O O   . ILE B 372 ? 0.8493 0.9639 1.0152 0.0111  -0.1657 0.1736  376 ILE B O   
14696 C CB  . ILE B 372 ? 0.9529 1.0713 1.2510 0.0293  -0.1935 0.1651  376 ILE B CB  
14697 C CG1 . ILE B 372 ? 1.1204 1.2051 1.3527 -0.0221 -0.2557 0.2122  376 ILE B CG1 
14698 C CG2 . ILE B 372 ? 0.8833 1.0251 1.0964 0.0318  -0.1370 0.1420  376 ILE B CG2 
14699 C CD1 . ILE B 372 ? 1.2326 1.2989 1.4281 -0.0611 -0.2974 0.2387  376 ILE B CD1 
14711 N N   . CYS B 373 ? 0.9230 1.0184 1.2765 0.0408  -0.2181 0.1781  377 CYS B N   
14712 C CA  . CYS B 373 ? 1.0954 1.1706 1.4014 0.0175  -0.2458 0.2049  377 CYS B CA  
14713 C C   . CYS B 373 ? 1.1746 1.2097 1.5344 -0.0125 -0.3355 0.2500  377 CYS B C   
14714 O O   . CYS B 373 ? 1.1825 1.2084 1.6382 -0.0072 -0.3736 0.2553  377 CYS B O   
14715 C CB  . CYS B 373 ? 1.1566 1.2434 1.5066 0.0490  -0.2113 0.1790  377 CYS B CB  
14716 S SG  . CYS B 373 ? 1.0956 1.2162 1.5085 0.0941  -0.1375 0.1211  377 CYS B SG  
14722 N N   . ASN B 374 ? 1.2357 1.2436 1.5392 -0.0472 -0.3746 0.2841  378 ASN B N   
14723 C CA  . ASN B 374 ? 1.3405 1.3011 1.6995 -0.0806 -0.4723 0.3335  378 ASN B CA  
14724 C C   . ASN B 374 ? 1.4364 1.3771 1.7741 -0.1156 -0.5186 0.3612  378 ASN B C   
14725 O O   . ASN B 374 ? 1.4651 1.4067 1.9266 -0.0911 -0.5422 0.3542  378 ASN B O   
14726 C CB  . ASN B 374 ? 1.3224 1.2786 1.8654 -0.0394 -0.4994 0.3201  378 ASN B CB  
14727 C CG  . ASN B 374 ? 1.2979 1.2780 1.8595 -0.0036 -0.4411 0.2837  378 ASN B CG  
14728 O OD1 . ASN B 374 ? 1.3242 1.3126 1.7639 -0.0160 -0.4041 0.2841  378 ASN B OD1 
14729 N ND2 . ASN B 374 ? 1.2522 1.2438 1.9714 0.0372  -0.4312 0.2484  378 ASN B ND2 
14736 N N   . ASN B 375 ? 1.5014 1.4243 1.6848 -0.1777 -0.5305 0.3896  379 ASN B N   
14737 C CA  . ASN B 375 ? 1.5477 1.4801 1.6403 -0.2047 -0.5074 0.3847  379 ASN B CA  
14738 C C   . ASN B 375 ? 1.4767 1.4241 1.6642 -0.1698 -0.5050 0.3678  379 ASN B C   
14739 O O   . ASN B 375 ? 1.3860 1.3753 1.5603 -0.1347 -0.4288 0.3236  379 ASN B O   
14740 C CB  . ASN B 375 ? 1.7499 1.6284 1.7333 -0.2954 -0.5858 0.4427  379 ASN B CB  
14741 C CG  . ASN B 375 ? 1.8909 1.7513 1.7572 -0.3471 -0.5881 0.4603  379 ASN B CG  
14742 O OD1 . ASN B 375 ? 1.9905 1.8604 1.7115 -0.3963 -0.5437 0.4480  379 ASN B OD1 
14743 N ND2 . ASN B 375 ? 1.9037 1.7385 1.8402 -0.3390 -0.6364 0.4838  379 ASN B ND2 
14750 N N   . GLY B 376 ? 1.5353 1.4492 1.8263 -0.1786 -0.5880 0.4010  380 GLY B N   
14751 C CA  . GLY B 376 ? 1.5029 1.4328 1.8890 -0.1481 -0.5845 0.3825  380 GLY B CA  
14752 C C   . GLY B 376 ? 1.4639 1.3988 2.0583 -0.0961 -0.6081 0.3648  380 GLY B C   
14753 O O   . GLY B 376 ? 1.4066 1.3598 2.1106 -0.0651 -0.5995 0.3398  380 GLY B O   
14757 N N   . THR B 377 ? 1.4746 1.3948 2.1289 -0.0886 -0.6338 0.3725  381 THR B N   
14758 C CA  . THR B 377 ? 1.4346 1.3452 2.2802 -0.0562 -0.6486 0.3457  381 THR B CA  
14759 C C   . THR B 377 ? 1.3530 1.3245 2.3086 0.0107  -0.5685 0.2788  381 THR B C   
14760 O O   . THR B 377 ? 1.4316 1.4047 2.5307 0.0305  -0.5594 0.2409  381 THR B O   
14761 C CB  . THR B 377 ? 1.4079 1.2821 2.2627 -0.0743 -0.6797 0.3621  381 THR B CB  
14762 O OG1 . THR B 377 ? 1.3344 1.2471 2.1219 -0.0486 -0.6259 0.3474  381 THR B OG1 
14763 C CG2 . THR B 377 ? 1.4804 1.2891 2.2192 -0.1520 -0.7539 0.4253  381 THR B CG2 
14771 N N   . LEU B 378 ? 1.2023 1.2100 2.0517 0.0291  -0.4823 0.2475  382 LEU B N   
14772 C CA  . LEU B 378 ? 1.0811 1.1328 1.9985 0.0760  -0.3955 0.1805  382 LEU B CA  
14773 C C   . LEU B 378 ? 1.0370 1.1212 1.8486 0.0842  -0.3202 0.1530  382 LEU B C   
14774 O O   . LEU B 378 ? 1.0784 1.1622 1.7334 0.0640  -0.3016 0.1716  382 LEU B O   
14775 C CB  . LEU B 378 ? 1.0656 1.1228 1.9611 0.0880  -0.3612 0.1647  382 LEU B CB  
14776 C CG  . LEU B 378 ? 1.0250 1.1200 1.9856 0.1245  -0.2764 0.0964  382 LEU B CG  
14777 C CD1 . LEU B 378 ? 1.0078 1.0973 2.0403 0.1350  -0.2762 0.0814  382 LEU B CD1 
14778 C CD2 . LEU B 378 ? 1.0126 1.1336 1.8241 0.1282  -0.1973 0.0761  382 LEU B CD2 
14790 N N   . PHE B 379 ? 0.9370 1.0492 1.8427 0.1109  -0.2765 0.1052  383 PHE B N   
14791 C CA  . PHE B 379 ? 0.8299 0.9715 1.6551 0.1204  -0.2042 0.0741  383 PHE B CA  
14792 C C   . PHE B 379 ? 0.7475 0.9173 1.6359 0.1446  -0.1317 0.0127  383 PHE B C   
14793 O O   . PHE B 379 ? 0.7775 0.9545 1.8231 0.1565  -0.1335 -0.0209 383 PHE B O   
14794 C CB  . PHE B 379 ? 0.8442 0.9880 1.7029 0.1153  -0.2242 0.0786  383 PHE B CB  
14795 C CG  . PHE B 379 ? 0.9104 1.0340 1.6421 0.0832  -0.2628 0.1276  383 PHE B CG  
14796 C CD1 . PHE B 379 ? 1.0063 1.0923 1.7531 0.0517  -0.3508 0.1793  383 PHE B CD1 
14797 C CD2 . PHE B 379 ? 0.8805 1.0198 1.4805 0.0786  -0.2128 0.1202  383 PHE B CD2 
14798 C CE1 . PHE B 379 ? 1.0654 1.1310 1.6822 0.0100  -0.3809 0.2197  383 PHE B CE1 
14799 C CE2 . PHE B 379 ? 0.9442 1.0678 1.4333 0.0440  -0.2396 0.1550  383 PHE B CE2 
14800 C CZ  . PHE B 379 ? 1.0318 1.1191 1.5216 0.0067  -0.3201 0.2032  383 PHE B CZ  
14810 N N   . GLN B 380 ? 0.7138 0.8976 1.4847 0.1466  -0.0695 -0.0039 384 GLN B N   
14811 C CA  . GLN B 380 ? 0.7003 0.9039 1.4968 0.1556  -0.0006 -0.0580 384 GLN B CA  
14812 C C   . GLN B 380 ? 0.6581 0.8722 1.3296 0.1504  0.0507  -0.0672 384 GLN B C   
14813 O O   . GLN B 380 ? 0.6707 0.8776 1.2274 0.1452  0.0410  -0.0345 384 GLN B O   
14814 C CB  . GLN B 380 ? 0.7609 0.9580 1.5575 0.1576  0.0089  -0.0644 384 GLN B CB  
14815 C CG  . GLN B 380 ? 0.8463 1.0386 1.8085 0.1650  -0.0221 -0.0803 384 GLN B CG  
14816 C CD  . GLN B 380 ? 0.9114 1.0955 1.8676 0.1661  -0.0151 -0.0840 384 GLN B CD  
14817 O OE1 . GLN B 380 ? 0.9408 1.1103 1.7856 0.1607  -0.0337 -0.0440 384 GLN B OE1 
14818 N NE2 . GLN B 380 ? 0.8734 1.0683 1.9539 0.1705  0.0157  -0.1372 384 GLN B NE2 
14827 N N   . HIS B 381 ? 0.6113 0.8410 1.3114 0.1473  0.1047  -0.1146 385 HIS B N   
14828 C CA  . HIS B 381 ? 0.6075 0.8412 1.1998 0.1372  0.1461  -0.1222 385 HIS B CA  
14829 C C   . HIS B 381 ? 0.6163 0.8419 1.1202 0.1273  0.1794  -0.1285 385 HIS B C   
14830 O O   . HIS B 381 ? 0.6373 0.8645 1.1250 0.1088  0.2269  -0.1646 385 HIS B O   
14831 C CB  . HIS B 381 ? 0.5782 0.8277 1.2319 0.1281  0.1836  -0.1665 385 HIS B CB  
14832 C CG  . HIS B 381 ? 0.5690 0.8266 1.3311 0.1381  0.1484  -0.1636 385 HIS B CG  
14833 N ND1 . HIS B 381 ? 0.5529 0.8014 1.2790 0.1442  0.0979  -0.1168 385 HIS B ND1 
14834 C CD2 . HIS B 381 ? 0.5718 0.8448 1.4829 0.1392  0.1556  -0.2038 385 HIS B CD2 
14835 C CE1 . HIS B 381 ? 0.5563 0.8102 1.3968 0.1484  0.0687  -0.1214 385 HIS B CE1 
14836 N NE2 . HIS B 381 ? 0.5727 0.8428 1.5362 0.1485  0.1019  -0.1745 385 HIS B NE2 
14844 N N   . GLN B 382 ? 0.6208 0.8350 1.0630 0.1337  0.1521  -0.0922 386 GLN B N   
14845 C CA  . GLN B 382 ? 0.6298 0.8340 0.9892 0.1263  0.1718  -0.0892 386 GLN B CA  
14846 C C   . GLN B 382 ? 0.6407 0.8390 0.9093 0.1301  0.1502  -0.0518 386 GLN B C   
14847 O O   . GLN B 382 ? 0.6712 0.8736 0.9349 0.1343  0.1255  -0.0321 386 GLN B O   
14848 C CB  . GLN B 382 ? 0.6350 0.8344 1.0380 0.1295  0.1659  -0.0937 386 GLN B CB  
14849 C CG  . GLN B 382 ? 0.7292 0.9372 1.2660 0.1316  0.1714  -0.1291 386 GLN B CG  
14850 C CD  . GLN B 382 ? 0.8296 1.0301 1.4173 0.1383  0.1513  -0.1247 386 GLN B CD  
14851 O OE1 . GLN B 382 ? 0.8327 1.0228 1.3975 0.1465  0.1054  -0.0825 386 GLN B OE1 
14852 N NE2 . GLN B 382 ? 0.8893 1.0943 1.5428 0.1295  0.1879  -0.1709 386 GLN B NE2 
14861 N N   . LYS B 383 ? 0.6460 0.8347 0.8479 0.1250  0.1607  -0.0456 387 LYS B N   
14862 C CA  . LYS B 383 ? 0.6718 0.8582 0.8108 0.1282  0.1440  -0.0190 387 LYS B CA  
14863 C C   . LYS B 383 ? 0.6872 0.8697 0.8190 0.1308  0.1291  -0.0043 387 LYS B C   
14864 O O   . LYS B 383 ? 0.7235 0.9040 0.8071 0.1296  0.1263  0.0077  387 LYS B O   
14865 C CB  . LYS B 383 ? 0.6951 0.8716 0.7747 0.1194  0.1598  -0.0213 387 LYS B CB  
14866 C CG  . LYS B 383 ? 0.8274 0.9875 0.8853 0.1029  0.1807  -0.0354 387 LYS B CG  
14867 C CD  . LYS B 383 ? 0.9697 1.1102 0.9653 0.0882  0.1791  -0.0261 387 LYS B CD  
14868 C CE  . LYS B 383 ? 1.0591 1.1988 1.0453 0.0835  0.1796  -0.0277 387 LYS B CE  
14869 N NZ  . LYS B 383 ? 1.1509 1.2624 1.0834 0.0614  0.1713  -0.0178 387 LYS B NZ  
14883 N N   . LYS B 384 ? 0.6663 0.8477 0.8554 0.1338  0.1181  -0.0070 388 LYS B N   
14884 C CA  . LYS B 384 ? 0.7072 0.8825 0.8906 0.1342  0.1016  0.0080  388 LYS B CA  
14885 C C   . LYS B 384 ? 0.6620 0.8339 0.9134 0.1355  0.0657  0.0200  388 LYS B C   
14886 O O   . LYS B 384 ? 0.6612 0.8351 0.9945 0.1399  0.0627  0.0038  388 LYS B O   
14887 C CB  . LYS B 384 ? 0.8584 1.0258 1.0374 0.1314  0.1265  -0.0098 388 LYS B CB  
14888 C CG  . LYS B 384 ? 1.0328 1.1936 1.2023 0.1324  0.1103  0.0061  388 LYS B CG  
14889 C CD  . LYS B 384 ? 1.1507 1.3016 1.2942 0.1255  0.1349  -0.0080 388 LYS B CD  
14890 C CE  . LYS B 384 ? 1.2079 1.3565 1.4128 0.1193  0.1587  -0.0424 388 LYS B CE  
14891 N NZ  . LYS B 384 ? 1.2409 1.3762 1.4075 0.1037  0.1822  -0.0557 388 LYS B NZ  
14905 N N   . CYS B 385 ? 0.6881 0.8530 0.9100 0.1275  0.0357  0.0480  389 CYS B N   
14906 C CA  . CYS B 385 ? 0.7486 0.9001 1.0245 0.1212  -0.0104 0.0685  389 CYS B CA  
14907 C C   . CYS B 385 ? 0.7818 0.9245 1.0549 0.1214  -0.0134 0.0730  389 CYS B C   
14908 O O   . CYS B 385 ? 0.8308 0.9768 1.0306 0.1174  0.0047  0.0766  389 CYS B O   
14909 C CB  . CYS B 385 ? 0.8454 0.9890 1.0729 0.0974  -0.0493 0.1023  389 CYS B CB  
14910 S SG  . CYS B 385 ? 1.0063 1.1508 1.2699 0.0931  -0.0692 0.1055  389 CYS B SG  
14916 N N   . SER B 386 ? 0.7893 0.9210 1.1534 0.1262  -0.0380 0.0708  390 SER B N   
14917 C CA  . SER B 386 ? 0.8002 0.9233 1.1770 0.1284  -0.0383 0.0694  390 SER B CA  
14918 C C   . SER B 386 ? 0.8151 0.9153 1.2453 0.1174  -0.1021 0.1013  390 SER B C   
14919 O O   . SER B 386 ? 0.7944 0.8828 1.2620 0.1068  -0.1487 0.1234  390 SER B O   
14920 C CB  . SER B 386 ? 0.8190 0.9495 1.2663 0.1420  0.0034  0.0236  390 SER B CB  
14921 O OG  . SER B 386 ? 0.8385 0.9828 1.2394 0.1427  0.0524  -0.0021 390 SER B OG  
14927 N N   . HIS B 387 ? 0.8518 0.9417 1.2838 0.1164  -0.1092 0.1066  391 HIS B N   
14928 C CA  . HIS B 387 ? 0.9276 0.9902 1.4168 0.1041  -0.1739 0.1376  391 HIS B CA  
14929 C C   . HIS B 387 ? 0.9933 1.0365 1.4036 0.0688  -0.2269 0.1878  391 HIS B C   
14930 O O   . HIS B 387 ? 1.0812 1.0967 1.5481 0.0511  -0.2950 0.2191  391 HIS B O   
14931 C CB  . HIS B 387 ? 0.9874 1.0430 1.6418 0.1189  -0.2006 0.1186  391 HIS B CB  
14932 C CG  . HIS B 387 ? 1.0406 1.1136 1.7781 0.1417  -0.1455 0.0617  391 HIS B CG  
14933 N ND1 . HIS B 387 ? 1.0437 1.1419 1.7893 0.1523  -0.0833 0.0154  391 HIS B ND1 
14934 C CD2 . HIS B 387 ? 1.0717 1.1386 1.8818 0.1487  -0.1414 0.0412  391 HIS B CD2 
14935 C CE1 . HIS B 387 ? 1.0432 1.1497 1.8555 0.1592  -0.0406 -0.0328 391 HIS B CE1 
14936 N NE2 . HIS B 387 ? 1.0537 1.1429 1.9102 0.1593  -0.0732 -0.0201 391 HIS B NE2 
14944 N N   . MET B 388 ? 0.9794 1.0351 1.2620 0.0526  -0.1972 0.1940  392 MET B N   
14945 C CA  . MET B 388 ? 1.0325 1.0742 1.2226 0.0086  -0.2310 0.2303  392 MET B CA  
14946 C C   . MET B 388 ? 1.0495 1.0847 1.1502 -0.0197 -0.2311 0.2468  392 MET B C   
14947 O O   . MET B 388 ? 1.0441 1.0992 1.1202 -0.0009 -0.1832 0.2234  392 MET B O   
14948 C CB  . MET B 388 ? 1.0276 1.0928 1.1536 0.0059  -0.1915 0.2145  392 MET B CB  
14949 C CG  . MET B 388 ? 0.9853 1.0819 1.0701 0.0298  -0.1217 0.1791  392 MET B CG  
14950 S SD  . MET B 388 ? 0.9596 1.0804 1.0086 0.0345  -0.0827 0.1574  392 MET B SD  
14951 C CE  . MET B 388 ? 1.0046 1.1150 0.9608 -0.0234 -0.1103 0.1839  392 MET B CE  
14961 N N   . LYS B 389 ? 1.0768 1.0810 1.1272 -0.0704 -0.2880 0.2883  393 LYS B N   
14962 C CA  . LYS B 389 ? 1.1208 1.1178 1.0746 -0.1102 -0.2882 0.3037  393 LYS B CA  
14963 C C   . LYS B 389 ? 1.1418 1.1678 0.9899 -0.1334 -0.2321 0.2814  393 LYS B C   
14964 O O   . LYS B 389 ? 1.1715 1.2065 0.9961 -0.1436 -0.2214 0.2741  393 LYS B O   
14965 C CB  . LYS B 389 ? 1.2386 1.1865 1.1634 -0.1696 -0.3719 0.3574  393 LYS B CB  
14966 C CG  . LYS B 389 ? 1.3538 1.2901 1.1667 -0.2243 -0.3745 0.3747  393 LYS B CG  
14967 C CD  . LYS B 389 ? 1.4941 1.3725 1.2670 -0.2945 -0.4669 0.4342  393 LYS B CD  
14968 C CE  . LYS B 389 ? 1.5784 1.4444 1.2315 -0.3583 -0.4640 0.4468  393 LYS B CE  
14969 N NZ  . LYS B 389 ? 1.6920 1.5030 1.3314 -0.4267 -0.5301 0.4779  393 LYS B NZ  
14983 N N   . VAL B 390 ? 1.1297 1.1716 0.9252 -0.1414 -0.1954 0.2669  394 VAL B N   
14984 C CA  . VAL B 390 ? 1.1160 1.1880 0.8342 -0.1652 -0.1408 0.2380  394 VAL B CA  
14985 C C   . VAL B 390 ? 1.1669 1.2204 0.7951 -0.2391 -0.1660 0.2575  394 VAL B C   
14986 O O   . VAL B 390 ? 1.2182 1.2341 0.7999 -0.2918 -0.2207 0.2969  394 VAL B O   
14987 C CB  . VAL B 390 ? 1.1116 1.2005 0.8031 -0.1672 -0.1059 0.2208  394 VAL B CB  
14988 C CG1 . VAL B 390 ? 1.1533 1.2760 0.7904 -0.1938 -0.0488 0.1829  394 VAL B CG1 
14989 C CG2 . VAL B 390 ? 0.9715 1.0728 0.7416 -0.1014 -0.0850 0.2043  394 VAL B CG2 
14999 N N   . GLY B 391 ? 1.1353 1.2117 0.7350 -0.2489 -0.1287 0.2307  395 GLY B N   
15000 C CA  . GLY B 391 ? 1.2135 1.2721 0.7288 -0.3197 -0.1488 0.2446  395 GLY B CA  
15001 C C   . GLY B 391 ? 1.2358 1.2776 0.7906 -0.3060 -0.1869 0.2643  395 GLY B C   
15002 O O   . GLY B 391 ? 1.3294 1.3656 0.8196 -0.3551 -0.1883 0.2646  395 GLY B O   
15006 N N   . ASP B 392 ? 1.1587 1.1932 0.8203 -0.2445 -0.2148 0.2766  396 ASP B N   
15007 C CA  . ASP B 392 ? 1.1194 1.1455 0.8393 -0.2237 -0.2420 0.2859  396 ASP B CA  
15008 C C   . ASP B 392 ? 1.0091 1.0753 0.7345 -0.1923 -0.1774 0.2420  396 ASP B C   
15009 O O   . ASP B 392 ? 0.9545 1.0539 0.6863 -0.1608 -0.1184 0.2052  396 ASP B O   
15010 C CB  . ASP B 392 ? 1.1030 1.1180 0.9512 -0.1674 -0.2757 0.2963  396 ASP B CB  
15011 C CG  . ASP B 392 ? 1.2121 1.1793 1.0823 -0.1992 -0.3586 0.3453  396 ASP B CG  
15012 O OD1 . ASP B 392 ? 1.3147 1.2471 1.1044 -0.2689 -0.4098 0.3834  396 ASP B OD1 
15013 O OD2 . ASP B 392 ? 1.1948 1.1565 1.1628 -0.1594 -0.3747 0.3455  396 ASP B OD2 
15018 N N   . THR B 393 ? 1.0076 1.0670 0.7350 -0.2027 -0.1950 0.2489  397 THR B N   
15019 C CA  . THR B 393 ? 0.9474 1.0390 0.6772 -0.1801 -0.1426 0.2121  397 THR B CA  
15020 C C   . THR B 393 ? 0.9024 0.9999 0.7371 -0.1194 -0.1472 0.2066  397 THR B C   
15021 O O   . THR B 393 ? 0.9294 1.0015 0.8214 -0.1176 -0.2021 0.2348  397 THR B O   
15022 C CB  . THR B 393 ? 1.0013 1.0833 0.6456 -0.2438 -0.1506 0.2177  397 THR B CB  
15023 O OG1 . THR B 393 ? 1.0652 1.1401 0.6053 -0.3134 -0.1427 0.2181  397 THR B OG1 
15024 C CG2 . THR B 393 ? 0.9893 1.1061 0.6404 -0.2207 -0.0932 0.1752  397 THR B CG2 
15032 N N   . ALA B 394 ? 0.8778 1.0069 0.7422 -0.0743 -0.0917 0.1693  398 ALA B N   
15033 C CA  . ALA B 394 ? 0.8557 0.9932 0.8035 -0.0256 -0.0836 0.1561  398 ALA B CA  
15034 C C   . ALA B 394 ? 0.8661 1.0211 0.7930 -0.0250 -0.0544 0.1358  398 ALA B C   
15035 O O   . ALA B 394 ? 0.8649 1.0408 0.7557 -0.0242 -0.0108 0.1098  398 ALA B O   
15036 C CB  . ALA B 394 ? 0.7958 0.9473 0.7881 0.0184  -0.0491 0.1335  398 ALA B CB  
15042 N N   . SER B 395 ? 0.8736 1.0194 0.8340 -0.0253 -0.0812 0.1466  399 SER B N   
15043 C CA  . SER B 395 ? 0.9058 1.0659 0.8533 -0.0234 -0.0580 0.1293  399 SER B CA  
15044 C C   . SER B 395 ? 0.8679 1.0423 0.8869 0.0254  -0.0318 0.1065  399 SER B C   
15045 O O   . SER B 395 ? 0.8816 1.0516 0.9695 0.0502  -0.0400 0.1059  399 SER B O   
15046 C CB  . SER B 395 ? 0.9760 1.1151 0.9079 -0.0604 -0.1049 0.1562  399 SER B CB  
15047 O OG  . SER B 395 ? 1.0851 1.2052 0.9308 -0.1203 -0.1299 0.1783  399 SER B OG  
15053 N N   . PHE B 396 ? 0.8434 1.0342 0.8452 0.0334  0.0016  0.0846  400 PHE B N   
15054 C CA  . PHE B 396 ? 0.8182 1.0190 0.8678 0.0684  0.0275  0.0637  400 PHE B CA  
15055 C C   . PHE B 396 ? 0.7946 1.0023 0.8351 0.0645  0.0353  0.0553  400 PHE B C   
15056 O O   . PHE B 396 ? 0.8348 1.0490 0.8244 0.0446  0.0467  0.0492  400 PHE B O   
15057 C CB  . PHE B 396 ? 0.7879 0.9975 0.8244 0.0863  0.0633  0.0446  400 PHE B CB  
15058 C CG  . PHE B 396 ? 0.7830 0.9860 0.8279 0.0915  0.0590  0.0507  400 PHE B CG  
15059 C CD1 . PHE B 396 ? 0.7550 0.9524 0.8513 0.1094  0.0609  0.0450  400 PHE B CD1 
15060 C CD2 . PHE B 396 ? 0.7885 0.9921 0.7918 0.0745  0.0570  0.0574  400 PHE B CD2 
15061 C CE1 . PHE B 396 ? 0.7450 0.9359 0.8502 0.1129  0.0581  0.0484  400 PHE B CE1 
15062 C CE2 . PHE B 396 ? 0.7702 0.9671 0.7805 0.0793  0.0520  0.0639  400 PHE B CE2 
15063 C CZ  . PHE B 396 ? 0.7541 0.9438 0.8151 0.0998  0.0511  0.0608  400 PHE B CZ  
15073 N N   . SER B 397 ? 0.7220 0.9299 0.8173 0.0810  0.0323  0.0504  401 SER B N   
15074 C CA  . SER B 397 ? 0.6986 0.9136 0.7921 0.0823  0.0433  0.0400  401 SER B CA  
15075 C C   . SER B 397 ? 0.6426 0.8649 0.7402 0.1036  0.0806  0.0167  401 SER B C   
15076 O O   . SER B 397 ? 0.6648 0.8856 0.8025 0.1168  0.0912  0.0063  401 SER B O   
15077 C CB  . SER B 397 ? 0.7119 0.9217 0.8665 0.0824  0.0149  0.0485  401 SER B CB  
15078 O OG  . SER B 397 ? 0.7800 0.9741 0.9252 0.0547  -0.0322 0.0779  401 SER B OG  
15084 N N   . VAL B 398 ? 0.6435 0.8713 0.7021 0.1010  0.0988  0.0069  402 VAL B N   
15085 C CA  . VAL B 398 ? 0.6813 0.9075 0.7385 0.1138  0.1216  -0.0078 402 VAL B CA  
15086 C C   . VAL B 398 ? 0.6705 0.8995 0.7298 0.1129  0.1264  -0.0155 402 VAL B C   
15087 O O   . VAL B 398 ? 0.7061 0.9414 0.7474 0.1042  0.1276  -0.0201 402 VAL B O   
15088 C CB  . VAL B 398 ? 0.7115 0.9384 0.7465 0.1135  0.1306  -0.0131 402 VAL B CB  
15089 C CG1 . VAL B 398 ? 0.7089 0.9245 0.7468 0.1218  0.1394  -0.0199 402 VAL B CG1 
15090 C CG2 . VAL B 398 ? 0.7328 0.9582 0.7621 0.1120  0.1250  -0.0045 402 VAL B CG2 
15100 N N   . THR B 399 ? 0.6391 0.8644 0.7218 0.1180  0.1327  -0.0213 403 THR B N   
15101 C CA  . THR B 399 ? 0.6708 0.8971 0.7550 0.1163  0.1379  -0.0285 403 THR B CA  
15102 C C   . THR B 399 ? 0.7231 0.9367 0.7857 0.1159  0.1490  -0.0347 403 THR B C   
15103 O O   . THR B 399 ? 0.7484 0.9493 0.8024 0.1123  0.1563  -0.0361 403 THR B O   
15104 C CB  . THR B 399 ? 0.6548 0.8843 0.7816 0.1164  0.1395  -0.0348 403 THR B CB  
15105 O OG1 . THR B 399 ? 0.6833 0.9183 0.8442 0.1154  0.1158  -0.0235 403 THR B OG1 
15106 C CG2 . THR B 399 ? 0.6662 0.8973 0.7920 0.1129  0.1449  -0.0418 403 THR B CG2 
15114 N N   . VAL B 400 ? 0.7421 0.9557 0.7972 0.1150  0.1469  -0.0380 404 VAL B N   
15115 C CA  . VAL B 400 ? 0.7502 0.9465 0.7972 0.1129  0.1444  -0.0394 404 VAL B CA  
15116 C C   . VAL B 400 ? 0.7236 0.9154 0.7714 0.1079  0.1445  -0.0434 404 VAL B C   
15117 O O   . VAL B 400 ? 0.6835 0.8900 0.7411 0.1098  0.1455  -0.0489 404 VAL B O   
15118 C CB  . VAL B 400 ? 0.7794 0.9795 0.8405 0.1175  0.1388  -0.0447 404 VAL B CB  
15119 C CG1 . VAL B 400 ? 0.8072 0.9835 0.8809 0.1157  0.1236  -0.0423 404 VAL B CG1 
15120 C CG2 . VAL B 400 ? 0.7794 0.9865 0.8374 0.1201  0.1406  -0.0417 404 VAL B CG2 
15130 N N   . ASN B 401 ? 0.7530 0.9218 0.7831 0.0953  0.1422  -0.0396 405 ASN B N   
15131 C CA  . ASN B 401 ? 0.8259 0.9858 0.8506 0.0857  0.1406  -0.0416 405 ASN B CA  
15132 C C   . ASN B 401 ? 0.8661 0.9905 0.8719 0.0697  0.1196  -0.0301 405 ASN B C   
15133 O O   . ASN B 401 ? 0.8734 0.9754 0.8522 0.0544  0.1125  -0.0201 405 ASN B O   
15134 C CB  . ASN B 401 ? 0.8585 1.0237 0.8770 0.0734  0.1600  -0.0500 405 ASN B CB  
15135 C CG  . ASN B 401 ? 0.8606 1.0122 0.8634 0.0560  0.1602  -0.0522 405 ASN B CG  
15136 O OD1 . ASN B 401 ? 0.8856 1.0465 0.9052 0.0650  0.1548  -0.0539 405 ASN B OD1 
15137 N ND2 . ASN B 401 ? 0.8491 0.9766 0.8129 0.0248  0.1673  -0.0528 405 ASN B ND2 
15144 N N   . ILE B 402 ? 0.8745 0.9905 0.8957 0.0698  0.1049  -0.0298 406 ILE B N   
15145 C CA  . ILE B 402 ? 0.9500 1.0257 0.9627 0.0510  0.0728  -0.0141 406 ILE B CA  
15146 C C   . ILE B 402 ? 0.9807 1.0402 0.9537 0.0248  0.0764  -0.0110 406 ILE B C   
15147 O O   . ILE B 402 ? 0.9209 1.0001 0.9112 0.0347  0.0885  -0.0226 406 ILE B O   
15148 C CB  . ILE B 402 ? 0.9830 1.0585 1.0609 0.0687  0.0498  -0.0194 406 ILE B CB  
15149 C CG1 . ILE B 402 ? 1.0560 1.0825 1.1416 0.0482  0.0029  0.0021  406 ILE B CG1 
15150 C CG2 . ILE B 402 ? 0.9818 1.0855 1.0859 0.0822  0.0677  -0.0393 406 ILE B CG2 
15151 C CD1 . ILE B 402 ? 1.1162 1.1100 1.1870 0.0326  -0.0261 0.0239  406 ILE B CD1 
15163 N N   . PRO B 403 ? 1.1234 1.1465 1.0369 -0.0149 0.0682  0.0027  407 PRO B N   
15164 C CA  . PRO B 403 ? 1.2080 1.2195 1.0771 -0.0481 0.0811  -0.0009 407 PRO B CA  
15165 C C   . PRO B 403 ? 1.2128 1.2043 1.0948 -0.0520 0.0516  0.0097  407 PRO B C   
15166 O O   . PRO B 403 ? 1.1907 1.2016 1.0813 -0.0472 0.0703  -0.0038 407 PRO B O   
15167 C CB  . PRO B 403 ? 1.3232 1.2937 1.1142 -0.1019 0.0770  0.0110  407 PRO B CB  
15168 C CG  . PRO B 403 ? 1.3056 1.2797 1.1061 -0.0876 0.0742  0.0151  407 PRO B CG  
15169 C CD  . PRO B 403 ? 1.2138 1.2055 1.0900 -0.0387 0.0512  0.0194  407 PRO B CD  
15177 N N   . HIS B 404 ? 1.2627 1.2139 1.1554 -0.0606 0.0017  0.0338  408 HIS B N   
15178 C CA  . HIS B 404 ? 1.3234 1.2473 1.2402 -0.0670 -0.0364 0.0463  408 HIS B CA  
15179 C C   . HIS B 404 ? 1.2385 1.1750 1.2563 -0.0248 -0.0598 0.0394  408 HIS B C   
15180 O O   . HIS B 404 ? 1.1903 1.1473 1.2459 -0.0002 -0.0526 0.0306  408 HIS B O   
15181 C CB  . HIS B 404 ? 1.5230 1.3780 1.3752 -0.1252 -0.0859 0.0819  408 HIS B CB  
15182 C CG  . HIS B 404 ? 1.7136 1.5543 1.4582 -0.1803 -0.0559 0.0812  408 HIS B CG  
15183 N ND1 . HIS B 404 ? 1.8276 1.6220 1.4933 -0.2345 -0.0757 0.1032  408 HIS B ND1 
15184 C CD2 . HIS B 404 ? 1.7455 1.6132 1.4543 -0.1943 -0.0044 0.0559  408 HIS B CD2 
15185 C CE1 . HIS B 404 ? 1.8796 1.6747 1.4612 -0.2829 -0.0313 0.0865  408 HIS B CE1 
15186 N NE2 . HIS B 404 ? 1.8187 1.6597 1.4333 -0.2572 0.0126  0.0563  408 HIS B NE2 
15194 N N   . CYS B 405 ? 1.2403 1.1657 1.3074 -0.0192 -0.0849 0.0388  409 CYS B N   
15195 C CA  . CYS B 405 ? 1.1959 1.1342 1.3745 0.0151  -0.1021 0.0219  409 CYS B CA  
15196 C C   . CYS B 405 ? 1.1952 1.0864 1.4212 0.0038  -0.1641 0.0466  409 CYS B C   
15197 O O   . CYS B 405 ? 1.2391 1.0727 1.4120 -0.0379 -0.2117 0.0850  409 CYS B O   
15198 C CB  . CYS B 405 ? 1.2248 1.1675 1.4555 0.0245  -0.1074 0.0071  409 CYS B CB  
15199 S SG  . CYS B 405 ? 1.2541 1.2242 1.6356 0.0628  -0.1102 -0.0328 409 CYS B SG  
15204 N N   . GLU B 406 ? 1.1497 1.0640 1.4772 0.0356  -0.1647 0.0237  410 GLU B N   
15205 C CA  . GLU B 406 ? 1.1595 1.0360 1.5660 0.0323  -0.2248 0.0405  410 GLU B CA  
15206 C C   . GLU B 406 ? 1.1054 1.0046 1.6702 0.0648  -0.2308 0.0012  410 GLU B C   
15207 O O   . GLU B 406 ? 1.0775 1.0224 1.6706 0.0854  -0.1821 -0.0396 410 GLU B O   
15208 C CB  . GLU B 406 ? 1.1530 1.0381 1.5317 0.0344  -0.2135 0.0461  410 GLU B CB  
15209 C CG  . GLU B 406 ? 1.2102 1.0811 1.4433 0.0020  -0.1950 0.0724  410 GLU B CG  
15210 C CD  . GLU B 406 ? 1.2454 1.1268 1.4576 0.0061  -0.1819 0.0745  410 GLU B CD  
15211 O OE1 . GLU B 406 ? 1.2161 1.1269 1.5183 0.0385  -0.1747 0.0512  410 GLU B OE1 
15212 O OE2 . GLU B 406 ? 1.3076 1.1685 1.4147 -0.0265 -0.1756 0.0955  410 GLU B OE2 
15219 N N   . ARG B 407 ? 1.0955 0.9608 1.7700 0.0651  -0.2918 0.0110  411 ARG B N   
15220 C CA  . ARG B 407 ? 1.0643 0.9521 1.9186 0.0941  -0.2972 -0.0355 411 ARG B CA  
15221 C C   . ARG B 407 ? 1.0558 0.9842 1.9829 0.1164  -0.2667 -0.0706 411 ARG B C   
15222 O O   . ARG B 407 ? 1.0168 1.0038 2.0036 0.1376  -0.2047 -0.1297 411 ARG B O   
15223 C CB  . ARG B 407 ? 1.1139 0.9363 2.0810 0.0806  -0.3930 -0.0069 411 ARG B CB  
15224 C CG  . ARG B 407 ? 1.1619 0.9629 2.1352 0.0712  -0.4126 -0.0023 411 ARG B CG  
15225 C CD  . ARG B 407 ? 1.2770 1.0164 2.4001 0.0624  -0.5116 0.0182  411 ARG B CD  
15226 N NE  . ARG B 407 ? 1.3059 1.0760 2.6468 0.0972  -0.5126 -0.0384 411 ARG B NE  
15227 C CZ  . ARG B 407 ? 1.3860 1.1442 2.8158 0.0855  -0.5597 -0.0319 411 ARG B CZ  
15228 N NH1 . ARG B 407 ? 1.3584 1.1674 2.9460 0.0942  -0.5336 -0.0967 411 ARG B NH1 
15229 N NH2 . ARG B 407 ? 1.4806 1.1780 2.8304 0.0541  -0.6285 0.0364  411 ARG B NH2 
15243 N N   . ARG B 408 ? 1.1107 1.0070 2.0260 0.1056  -0.3084 -0.0356 412 ARG B N   
15244 C CA  . ARG B 408 ? 1.0992 1.0310 2.0889 0.1251  -0.2841 -0.0672 412 ARG B CA  
15245 C C   . ARG B 408 ? 0.9647 0.9515 1.8366 0.1322  -0.2006 -0.0872 412 ARG B C   
15246 O O   . ARG B 408 ? 0.9347 0.9170 1.6575 0.1183  -0.1800 -0.0590 412 ARG B O   
15247 C CB  . ARG B 408 ? 1.2635 1.1419 2.2652 0.1088  -0.3562 -0.0193 412 ARG B CB  
15248 C CG  . ARG B 408 ? 1.4607 1.2735 2.5863 0.0958  -0.4572 0.0104  412 ARG B CG  
15249 C CD  . ARG B 408 ? 1.6070 1.3846 2.8098 0.0895  -0.5218 0.0358  412 ARG B CD  
15250 N NE  . ARG B 408 ? 1.7911 1.4860 2.9877 0.0436  -0.6269 0.0986  412 ARG B NE  
15251 C CZ  . ARG B 408 ? 1.8893 1.5720 3.2244 0.0250  -0.6831 0.0882  412 ARG B CZ  
15252 N NH1 . ARG B 408 ? 1.9890 1.6052 3.2964 -0.0263 -0.7797 0.1477  412 ARG B NH1 
15253 N NH2 . ARG B 408 ? 1.8733 1.6117 3.3718 0.0499  -0.6439 0.0169  412 ARG B NH2 
15267 N N   . SER B 409 ? 0.9116 0.9495 1.8596 0.1503  -0.1539 -0.1385 413 SER B N   
15268 C CA  . SER B 409 ? 0.8770 0.9589 1.7229 0.1521  -0.0883 -0.1517 413 SER B CA  
15269 C C   . SER B 409 ? 0.8351 0.8972 1.6335 0.1473  -0.1107 -0.1163 413 SER B C   
15270 O O   . SER B 409 ? 0.8433 0.8672 1.7147 0.1444  -0.1705 -0.0945 413 SER B O   
15271 C CB  . SER B 409 ? 0.9001 1.0421 1.8298 0.1611  -0.0265 -0.2223 413 SER B CB  
15272 O OG  . SER B 409 ? 0.9444 1.1057 1.9033 0.1596  0.0007  -0.2579 413 SER B OG  
15278 N N   . ARG B 410 ? 0.9662 1.0079 1.0508 0.1876  -0.0197 0.0058  414 ARG B N   
15279 C CA  . ARG B 410 ? 0.9604 1.0164 1.0273 0.1842  -0.0202 0.0120  414 ARG B CA  
15280 C C   . ARG B 410 ? 0.9289 1.0036 1.0018 0.1846  -0.0041 -0.0093 414 ARG B C   
15281 O O   . ARG B 410 ? 0.9258 1.0025 0.9880 0.1803  0.0121  -0.0218 414 ARG B O   
15282 C CB  . ARG B 410 ? 0.9907 1.0427 1.0136 0.1739  -0.0151 0.0269  414 ARG B CB  
15283 C CG  . ARG B 410 ? 1.0315 1.0677 1.0423 0.1692  -0.0303 0.0482  414 ARG B CG  
15284 C CD  . ARG B 410 ? 1.0848 1.1171 1.0596 0.1596  -0.0194 0.0558  414 ARG B CD  
15285 N NE  . ARG B 410 ? 1.1551 1.1768 1.1116 0.1505  -0.0315 0.0752  414 ARG B NE  
15286 C CZ  . ARG B 410 ? 1.2282 1.2554 1.1629 0.1399  -0.0335 0.0846  414 ARG B CZ  
15287 N NH1 . ARG B 410 ? 1.2444 1.2867 1.1745 0.1386  -0.0241 0.0766  414 ARG B NH1 
15288 N NH2 . ARG B 410 ? 1.2642 1.2819 1.1799 0.1279  -0.0440 0.1012  414 ARG B NH2 
15302 N N   . HIS B 411 ? 0.9207 1.0101 1.0092 0.1873  -0.0095 -0.0125 415 HIS B N   
15303 C CA  . HIS B 411 ? 0.8880 0.9962 0.9780 0.1852  0.0053  -0.0315 415 HIS B CA  
15304 C C   . HIS B 411 ? 0.8552 0.9683 0.9066 0.1760  0.0118  -0.0224 415 HIS B C   
15305 O O   . HIS B 411 ? 0.8666 0.9816 0.9101 0.1732  0.0003  -0.0082 415 HIS B O   
15306 C CB  . HIS B 411 ? 0.9155 1.0395 1.0499 0.1932  -0.0032 -0.0428 415 HIS B CB  
15307 C CG  . HIS B 411 ? 1.0150 1.1344 1.1958 0.2029  -0.0059 -0.0563 415 HIS B CG  
15308 N ND1 . HIS B 411 ? 1.0424 1.1731 1.2468 0.2029  0.0108  -0.0851 415 HIS B ND1 
15309 C CD2 . HIS B 411 ? 1.0631 1.1667 1.2721 0.2113  -0.0219 -0.0462 415 HIS B CD2 
15310 C CE1 . HIS B 411 ? 1.0616 1.1843 1.3094 0.2114  0.0069  -0.0944 415 HIS B CE1 
15311 N NE2 . HIS B 411 ? 1.0634 1.1682 1.3158 0.2177  -0.0135 -0.0703 415 HIS B NE2 
15319 N N   . ILE B 412 ? 0.8384 0.9530 0.8664 0.1697  0.0301  -0.0301 416 ILE B N   
15320 C CA  . ILE B 412 ? 0.8517 0.9664 0.8466 0.1617  0.0393  -0.0223 416 ILE B CA  
15321 C C   . ILE B 412 ? 0.8807 1.0065 0.8700 0.1568  0.0555  -0.0382 416 ILE B C   
15322 O O   . ILE B 412 ? 0.9168 1.0469 0.9163 0.1563  0.0628  -0.0527 416 ILE B O   
15323 C CB  . ILE B 412 ? 0.8494 0.9496 0.8200 0.1583  0.0437  -0.0088 416 ILE B CB  
15324 C CG1 . ILE B 412 ? 0.8531 0.9422 0.8250 0.1600  0.0281  0.0070  416 ILE B CG1 
15325 C CG2 . ILE B 412 ? 0.8792 0.9790 0.8239 0.1511  0.0565  -0.0039 416 ILE B CG2 
15326 C CD1 . ILE B 412 ? 0.8540 0.9311 0.8084 0.1571  0.0317  0.0178  416 ILE B CD1 
15338 N N   . ILE B 413 ? 0.8493 0.9792 0.8206 0.1506  0.0620  -0.0360 417 ILE B N   
15339 C CA  . ILE B 413 ? 0.7948 0.9322 0.7565 0.1440  0.0775  -0.0485 417 ILE B CA  
15340 C C   . ILE B 413 ? 0.7746 0.9003 0.7083 0.1379  0.0894  -0.0383 417 ILE B C   
15341 O O   . ILE B 413 ? 0.7981 0.9186 0.7207 0.1356  0.0879  -0.0278 417 ILE B O   
15342 C CB  . ILE B 413 ? 0.8154 0.9702 0.7881 0.1417  0.0757  -0.0592 417 ILE B CB  
15343 C CG1 . ILE B 413 ? 0.8523 1.0213 0.8616 0.1485  0.0681  -0.0740 417 ILE B CG1 
15344 C CG2 . ILE B 413 ? 0.8381 0.9959 0.7913 0.1318  0.0931  -0.0681 417 ILE B CG2 
15345 C CD1 . ILE B 413 ? 0.9226 1.1130 0.9507 0.1475  0.0637  -0.0840 417 ILE B CD1 
15357 N N   . ILE B 414 ? 0.7328 0.8548 0.6568 0.1337  0.1012  -0.0413 418 ILE B N   
15358 C CA  . ILE B 414 ? 0.7565 0.8677 0.6617 0.1287  0.1134  -0.0328 418 ILE B CA  
15359 C C   . ILE B 414 ? 0.7963 0.9127 0.6946 0.1206  0.1250  -0.0449 418 ILE B C   
15360 O O   . ILE B 414 ? 0.8106 0.9336 0.7111 0.1164  0.1271  -0.0546 418 ILE B O   
15361 C CB  . ILE B 414 ? 0.7727 0.8741 0.6737 0.1296  0.1145  -0.0208 418 ILE B CB  
15362 C CG1 . ILE B 414 ? 0.7734 0.8708 0.6808 0.1362  0.1032  -0.0108 418 ILE B CG1 
15363 C CG2 . ILE B 414 ? 0.7265 0.8164 0.6171 0.1265  0.1261  -0.0106 418 ILE B CG2 
15364 C CD1 . ILE B 414 ? 0.8034 0.8954 0.7088 0.1362  0.1023  0.0003  418 ILE B CD1 
15376 N N   . LYS B 415 ? 0.7840 0.8976 0.6726 0.1158  0.1337  -0.0456 419 LYS B N   
15377 C CA  . LYS B 415 ? 0.7772 0.8946 0.6577 0.1066  0.1452  -0.0574 419 LYS B CA  
15378 C C   . LYS B 415 ? 0.7902 0.8927 0.6573 0.1014  0.1590  -0.0516 419 LYS B C   
15379 O O   . LYS B 415 ? 0.7817 0.8771 0.6479 0.1036  0.1598  -0.0437 419 LYS B O   
15380 C CB  . LYS B 415 ? 0.7899 0.9273 0.6798 0.1044  0.1406  -0.0728 419 LYS B CB  
15381 C CG  . LYS B 415 ? 0.8510 0.9920 0.7391 0.1034  0.1362  -0.0691 419 LYS B CG  
15382 C CD  . LYS B 415 ? 0.9761 1.1400 0.8757 0.0999  0.1297  -0.0819 419 LYS B CD  
15383 C CE  . LYS B 415 ? 1.1400 1.3096 1.0345 0.0951  0.1224  -0.0754 419 LYS B CE  
15384 N NZ  . LYS B 415 ? 1.2547 1.4501 1.1649 0.0920  0.1118  -0.0843 419 LYS B NZ  
15398 N N   . PRO B 416 ? 0.8258 0.9224 0.6830 0.0929  0.1715  -0.0564 420 PRO B N   
15399 C CA  . PRO B 416 ? 0.8715 0.9530 0.7199 0.0871  0.1869  -0.0547 420 PRO B CA  
15400 C C   . PRO B 416 ? 0.9210 1.0134 0.7644 0.0803  0.1902  -0.0668 420 PRO B C   
15401 O O   . PRO B 416 ? 0.9726 1.0852 0.8187 0.0778  0.1826  -0.0780 420 PRO B O   
15402 C CB  . PRO B 416 ? 0.9019 0.9747 0.7410 0.0783  0.1967  -0.0569 420 PRO B CB  
15403 C CG  . PRO B 416 ? 0.8746 0.9579 0.7152 0.0783  0.1862  -0.0574 420 PRO B CG  
15404 C CD  . PRO B 416 ? 0.8256 0.9283 0.6787 0.0857  0.1733  -0.0650 420 PRO B CD  
15412 N N   . VAL B 417 ? 0.9106 0.9911 0.7485 0.0759  0.2022  -0.0649 421 VAL B N   
15413 C CA  . VAL B 417 ? 0.9296 1.0207 0.7578 0.0643  0.2070  -0.0761 421 VAL B CA  
15414 C C   . VAL B 417 ? 0.9260 1.0211 0.7446 0.0529  0.2176  -0.0902 421 VAL B C   
15415 O O   . VAL B 417 ? 0.9215 0.9980 0.7355 0.0494  0.2322  -0.0905 421 VAL B O   
15416 C CB  . VAL B 417 ? 0.9747 1.0515 0.7979 0.0583  0.2214  -0.0741 421 VAL B CB  
15417 C CG1 . VAL B 417 ? 0.9912 1.0802 0.7992 0.0409  0.2276  -0.0867 421 VAL B CG1 
15418 C CG2 . VAL B 417 ? 0.9882 1.0637 0.8198 0.0675  0.2108  -0.0614 421 VAL B CG2 
15428 N N   . GLY B 418 ? 0.9505 1.0702 0.7679 0.0467  0.2094  -0.1010 422 GLY B N   
15429 C CA  . GLY B 418 ? 0.9397 1.0681 0.7482 0.0341  0.2188  -0.1162 422 GLY B CA  
15430 C C   . GLY B 418 ? 0.8801 1.0204 0.6967 0.0372  0.2128  -0.1231 422 GLY B C   
15431 O O   . GLY B 418 ? 0.8583 1.0156 0.6720 0.0268  0.2163  -0.1380 422 GLY B O   
15435 N N   . LEU B 419 ? 0.8689 1.0027 0.6951 0.0486  0.2050  -0.1143 423 LEU B N   
15436 C CA  . LEU B 419 ? 0.8447 0.9898 0.6768 0.0480  0.2016  -0.1228 423 LEU B CA  
15437 C C   . LEU B 419 ? 0.8322 0.9995 0.6882 0.0590  0.1835  -0.1258 423 LEU B C   
15438 O O   . LEU B 419 ? 0.8276 0.9931 0.6932 0.0697  0.1718  -0.1144 423 LEU B O   
15439 C CB  . LEU B 419 ? 0.8706 0.9938 0.6948 0.0486  0.2062  -0.1116 423 LEU B CB  
15440 C CG  . LEU B 419 ? 0.9321 1.0278 0.7399 0.0408  0.2221  -0.1038 423 LEU B CG  
15441 C CD1 . LEU B 419 ? 0.9434 1.0220 0.7470 0.0405  0.2212  -0.0895 423 LEU B CD1 
15442 C CD2 . LEU B 419 ? 0.9794 1.0789 0.7734 0.0247  0.2356  -0.1198 423 LEU B CD2 
15454 N N   . GLY B 420 ? 0.8677 1.0552 0.7350 0.0553  0.1825  -0.1422 424 GLY B N   
15455 C CA  . GLY B 420 ? 0.9020 1.1102 0.7994 0.0658  0.1677  -0.1484 424 GLY B CA  
15456 C C   . GLY B 420 ? 0.9266 1.1258 0.8295 0.0722  0.1642  -0.1438 424 GLY B C   
15457 O O   . GLY B 420 ? 0.9872 1.1932 0.9138 0.0839  0.1513  -0.1424 424 GLY B O   
15461 N N   . ASP B 421 ? 0.8784 1.0620 0.7596 0.0630  0.1748  -0.1406 425 ASP B N   
15462 C CA  . ASP B 421 ? 0.8497 1.0259 0.7310 0.0646  0.1715  -0.1348 425 ASP B CA  
15463 C C   . ASP B 421 ? 0.8211 0.9865 0.7114 0.0799  0.1593  -0.1170 425 ASP B C   
15464 O O   . ASP B 421 ? 0.8651 1.0138 0.7442 0.0838  0.1596  -0.1003 425 ASP B O   
15465 C CB  . ASP B 421 ? 0.8867 1.0446 0.7396 0.0513  0.1814  -0.1254 425 ASP B CB  
15466 C CG  . ASP B 421 ? 0.9534 1.1198 0.7928 0.0328  0.1938  -0.1422 425 ASP B CG  
15467 O OD1 . ASP B 421 ? 0.9875 1.1534 0.8204 0.0289  0.2010  -0.1466 425 ASP B OD1 
15468 O OD2 . ASP B 421 ? 0.9761 1.1501 0.8095 0.0196  0.1974  -0.1521 425 ASP B OD2 
15473 N N   . ALA B 422 ? 0.7835 0.9583 0.6953 0.0875  0.1499  -0.1222 426 ALA B N   
15474 C CA  . ALA B 422 ? 0.7914 0.9580 0.7139 0.1012  0.1371  -0.1074 426 ALA B CA  
15475 C C   . ALA B 422 ? 0.7954 0.9583 0.7216 0.1015  0.1343  -0.1062 426 ALA B C   
15476 O O   . ALA B 422 ? 0.7951 0.9694 0.7283 0.0936  0.1393  -0.1235 426 ALA B O   
15477 C CB  . ALA B 422 ? 0.7970 0.9780 0.7474 0.1114  0.1249  -0.1129 426 ALA B CB  
15483 N N   . LEU B 423 ? 0.8410 0.9892 0.7619 0.1086  0.1275  -0.0870 427 LEU B N   
15484 C CA  . LEU B 423 ? 0.8234 0.9682 0.7479 0.1091  0.1229  -0.0838 427 LEU B CA  
15485 C C   . LEU B 423 ? 0.8223 0.9685 0.7719 0.1223  0.1104  -0.0841 427 LEU B C   
15486 O O   . LEU B 423 ? 0.8136 0.9511 0.7621 0.1306  0.1024  -0.0688 427 LEU B O   
15487 C CB  . LEU B 423 ? 0.8104 0.9396 0.7152 0.1074  0.1228  -0.0615 427 LEU B CB  
15488 C CG  . LEU B 423 ? 0.7896 0.9169 0.6918 0.1033  0.1188  -0.0560 427 LEU B CG  
15489 C CD1 . LEU B 423 ? 0.7845 0.9007 0.6697 0.0999  0.1190  -0.0330 427 LEU B CD1 
15490 C CD2 . LEU B 423 ? 0.8055 0.9311 0.7255 0.1143  0.1086  -0.0550 427 LEU B CD2 
15502 N N   . GLU B 424 ? 0.8793 1.0358 0.8522 0.1227  0.1094  -0.1020 428 GLU B N   
15503 C CA  . GLU B 424 ? 0.8996 1.0547 0.9012 0.1353  0.0968  -0.1018 428 GLU B CA  
15504 C C   . GLU B 424 ? 0.8454 0.9867 0.8396 0.1359  0.0928  -0.0902 428 GLU B C   
15505 O O   . GLU B 424 ? 0.8494 0.9915 0.8342 0.1253  0.1006  -0.0969 428 GLU B O   
15506 C CB  . GLU B 424 ? 0.9760 1.1470 1.0138 0.1367  0.0990  -0.1275 428 GLU B CB  
15507 C CG  . GLU B 424 ? 1.0863 1.2755 1.1306 0.1325  0.1057  -0.1424 428 GLU B CG  
15508 C CD  . GLU B 424 ? 1.1822 1.3884 1.2750 0.1415  0.1004  -0.1606 428 GLU B CD  
15509 O OE1 . GLU B 424 ? 1.2214 1.4247 1.3451 0.1489  0.0957  -0.1672 428 GLU B OE1 
15510 O OE2 . GLU B 424 ? 1.2142 1.4368 1.3172 0.1412  0.1008  -0.1681 428 GLU B OE2 
15517 N N   . LEU B 425 ? 0.8306 0.9604 0.8266 0.1456  0.0806  -0.0726 429 LEU B N   
15518 C CA  . LEU B 425 ? 0.8666 0.9836 0.8543 0.1458  0.0763  -0.0599 429 LEU B CA  
15519 C C   . LEU B 425 ? 0.8909 1.0009 0.9043 0.1560  0.0629  -0.0583 429 LEU B C   
15520 O O   . LEU B 425 ? 0.8856 0.9938 0.9070 0.1633  0.0518  -0.0489 429 LEU B O   
15521 C CB  . LEU B 425 ? 0.8795 0.9873 0.8409 0.1450  0.0759  -0.0378 429 LEU B CB  
15522 C CG  . LEU B 425 ? 0.8902 0.9872 0.8444 0.1452  0.0706  -0.0235 429 LEU B CG  
15523 C CD1 . LEU B 425 ? 0.9193 1.0195 0.8653 0.1350  0.0771  -0.0278 429 LEU B CD1 
15524 C CD2 . LEU B 425 ? 0.8760 0.9663 0.8133 0.1462  0.0706  -0.0045 429 LEU B CD2 
15536 N N   . LEU B 426 ? 0.9253 1.0308 0.9506 0.1544  0.0638  -0.0666 430 LEU B N   
15537 C CA  . LEU B 426 ? 0.9346 1.0286 0.9848 0.1632  0.0517  -0.0638 430 LEU B CA  
15538 C C   . LEU B 426 ? 0.9342 1.0141 0.9631 0.1595  0.0486  -0.0475 430 LEU B C   
15539 O O   . LEU B 426 ? 0.9374 1.0183 0.9536 0.1495  0.0576  -0.0529 430 LEU B O   
15540 C CB  . LEU B 426 ? 0.9515 1.0497 1.0376 0.1638  0.0573  -0.0893 430 LEU B CB  
15541 C CG  . LEU B 426 ? 0.9445 1.0296 1.0682 0.1757  0.0439  -0.0879 430 LEU B CG  
15542 C CD1 . LEU B 426 ? 0.9431 1.0321 1.0896 0.1879  0.0281  -0.0782 430 LEU B CD1 
15543 C CD2 . LEU B 426 ? 0.9220 1.0092 1.0817 0.1740  0.0549  -0.1165 430 LEU B CD2 
15555 N N   . VAL B 427 ? 0.9485 1.0172 0.9722 0.1651  0.0356  -0.0277 431 VAL B N   
15556 C CA  . VAL B 427 ? 0.9921 1.0483 0.9976 0.1614  0.0320  -0.0123 431 VAL B CA  
15557 C C   . VAL B 427 ? 1.0672 1.1087 1.0964 0.1658  0.0221  -0.0138 431 VAL B C   
15558 O O   . VAL B 427 ? 1.0981 1.1322 1.1459 0.1737  0.0081  -0.0069 431 VAL B O   
15559 C CB  . VAL B 427 ? 0.9788 1.0319 0.9623 0.1611  0.0264  0.0085  431 VAL B CB  
15560 C CG1 . VAL B 427 ? 0.9342 0.9773 0.9011 0.1561  0.0242  0.0224  431 VAL B CG1 
15561 C CG2 . VAL B 427 ? 0.9980 1.0631 0.9644 0.1577  0.0377  0.0081  431 VAL B CG2 
15571 N N   . SER B 428 ? 1.1110 1.1477 1.1398 0.1593  0.0287  -0.0220 432 SER B N   
15572 C CA  . SER B 428 ? 1.1712 1.1911 1.2230 0.1619  0.0225  -0.0261 432 SER B CA  
15573 C C   . SER B 428 ? 1.1925 1.2008 1.2204 0.1543  0.0198  -0.0113 432 SER B C   
15574 O O   . SER B 428 ? 1.1677 1.1854 1.1706 0.1438  0.0292  -0.0102 432 SER B O   
15575 C CB  . SER B 428 ? 1.1937 1.2180 1.2697 0.1579  0.0358  -0.0545 432 SER B CB  
15576 O OG  . SER B 428 ? 1.2009 1.2372 1.3047 0.1650  0.0387  -0.0704 432 SER B OG  
15582 N N   . PRO B 429 ? 1.2559 1.2448 1.2907 0.1579  0.0063  0.0015  433 PRO B N   
15583 C CA  . PRO B 429 ? 1.2523 1.2312 1.2634 0.1489  0.0044  0.0148  433 PRO B CA  
15584 C C   . PRO B 429 ? 1.1728 1.1458 1.1896 0.1404  0.0136  -0.0003 433 PRO B C   
15585 O O   . PRO B 429 ? 1.1357 1.1024 1.1827 0.1432  0.0179  -0.0196 433 PRO B O   
15586 C CB  . PRO B 429 ? 1.3249 1.2839 1.3421 0.1537  -0.0140 0.0328  433 PRO B CB  
15587 C CG  . PRO B 429 ? 1.3484 1.3013 1.4064 0.1656  -0.0213 0.0234  433 PRO B CG  
15588 C CD  . PRO B 429 ? 1.3147 1.2906 1.3801 0.1691  -0.0095 0.0066  433 PRO B CD  
15596 N N   . GLU B 430 ? 1.1544 1.1311 1.1434 0.1285  0.0178  0.0075  434 GLU B N   
15597 C CA  . GLU B 430 ? 1.1656 1.1368 1.1528 0.1160  0.0253  -0.0035 434 GLU B CA  
15598 C C   . GLU B 430 ? 1.1875 1.1488 1.1537 0.1093  0.0180  0.0154  434 GLU B C   
15599 O O   . GLU B 430 ? 1.1438 1.1208 1.0853 0.1001  0.0215  0.0246  434 GLU B O   
15600 C CB  . GLU B 430 ? 1.1436 1.1379 1.1162 0.1028  0.0397  -0.0157 434 GLU B CB  
15601 C CG  . GLU B 430 ? 1.1611 1.1626 1.1548 0.1027  0.0505  -0.0413 434 GLU B CG  
15602 C CD  . GLU B 430 ? 1.1872 1.2002 1.1701 0.0816  0.0652  -0.0596 434 GLU B CD  
15603 O OE1 . GLU B 430 ? 1.1878 1.2139 1.1414 0.0679  0.0657  -0.0478 434 GLU B OE1 
15604 O OE2 . GLU B 430 ? 1.2097 1.2202 1.2151 0.0773  0.0763  -0.0862 434 GLU B OE2 
15611 N N   . CYS B 431 ? 1.2706 1.2063 1.2489 0.1133  0.0072  0.0217  435 CYS B N   
15612 C CA  . CYS B 431 ? 1.3503 1.2735 1.3088 0.1045  0.0006  0.0376  435 CYS B CA  
15613 C C   . CYS B 431 ? 1.3409 1.2390 1.3135 0.0987  0.0009  0.0283  435 CYS B C   
15614 O O   . CYS B 431 ? 1.3374 1.2154 1.3018 0.0941  -0.0084 0.0420  435 CYS B O   
15615 C CB  . CYS B 431 ? 1.4283 1.3425 1.3794 0.1103  -0.0145 0.0594  435 CYS B CB  
15616 S SG  . CYS B 431 ? 1.4750 1.3568 1.4560 0.1204  -0.0329 0.0659  435 CYS B SG  
15621 N N   . ASN B 432 ? 1.3368 1.2350 1.3303 0.0969  0.0130  0.0040  436 ASN B N   
15622 C CA  . ASN B 432 ? 1.3775 1.2526 1.3874 0.0895  0.0183  -0.0105 436 ASN B CA  
15623 C C   . ASN B 432 ? 1.4071 1.2999 1.3989 0.0695  0.0360  -0.0279 436 ASN B C   
15624 O O   . ASN B 432 ? 1.3730 1.2950 1.3497 0.0641  0.0438  -0.0322 436 ASN B O   
15625 C CB  . ASN B 432 ? 1.3529 1.2105 1.4114 0.1030  0.0189  -0.0282 436 ASN B CB  
15626 C CG  . ASN B 432 ? 1.3395 1.1767 1.4193 0.1202  -0.0024 -0.0078 436 ASN B CG  
15627 O OD1 . ASN B 432 ? 1.3216 1.1660 1.4261 0.1348  -0.0076 -0.0093 436 ASN B OD1 
15628 N ND2 . ASN B 432 ? 1.3607 1.1735 1.4293 0.1162  -0.0156 0.0121  436 ASN B ND2 
15635 N N   . CYS B 433 ? 1.4729 1.3473 1.4654 0.0564  0.0416  -0.0369 437 CYS B N   
15636 C CA  . CYS B 433 ? 1.5150 1.4051 1.4880 0.0328  0.0576  -0.0533 437 CYS B CA  
15637 C C   . CYS B 433 ? 1.6036 1.4845 1.6064 0.0268  0.0750  -0.0877 437 CYS B C   
15638 O O   . CYS B 433 ? 1.6586 1.5111 1.7011 0.0399  0.0739  -0.0975 437 CYS B O   
15639 C CB  . CYS B 433 ? 1.5074 1.3863 1.4571 0.0175  0.0548  -0.0424 437 CYS B CB  
15640 S SG  . CYS B 433 ? 1.4445 1.3343 1.3630 0.0215  0.0376  -0.0061 437 CYS B SG  
15645 N N   . ASP B 434 ? 1.6248 1.5312 1.6101 0.0052  0.0912  -0.1061 438 ASP B N   
15646 C CA  . ASP B 434 ? 1.6730 1.5739 1.6827 -0.0068 0.1121  -0.1433 438 ASP B CA  
15647 C C   . ASP B 434 ? 1.6689 1.5366 1.6937 -0.0155 0.1188  -0.1561 438 ASP B C   
15648 O O   . ASP B 434 ? 1.6920 1.5375 1.7592 -0.0114 0.1309  -0.1827 438 ASP B O   
15649 C CB  . ASP B 434 ? 1.7324 1.6687 1.7108 -0.0351 0.1270  -0.1578 438 ASP B CB  
15650 C CG  . ASP B 434 ? 1.7538 1.7149 1.7346 -0.0284 0.1287  -0.1614 438 ASP B CG  
15651 O OD1 . ASP B 434 ? 1.7494 1.7061 1.7464 -0.0017 0.1154  -0.1456 438 ASP B OD1 
15652 O OD2 . ASP B 434 ? 1.7677 1.7529 1.7324 -0.0524 0.1435  -0.1804 438 ASP B OD2 
15657 N N   . CYS B 435 ? 1.6396 1.5033 1.6330 -0.0278 0.1121  -0.1382 439 CYS B N   
15658 C CA  . CYS B 435 ? 1.6522 1.4829 1.6551 -0.0385 0.1186  -0.1488 439 CYS B CA  
15659 C C   . CYS B 435 ? 1.7230 1.5109 1.7682 -0.0128 0.1062  -0.1409 439 CYS B C   
15660 O O   . CYS B 435 ? 1.8257 1.5797 1.8958 -0.0175 0.1143  -0.1564 439 CYS B O   
15661 C CB  . CYS B 435 ? 1.5720 1.4112 1.5300 -0.0570 0.1120  -0.1284 439 CYS B CB  
15662 S SG  . CYS B 435 ? 1.4526 1.2949 1.3908 -0.0370 0.0844  -0.0834 439 CYS B SG  
15667 N N   . GLN B 436 ? 1.6625 1.4508 1.7168 0.0127  0.0864  -0.1164 440 GLN B N   
15668 C CA  . GLN B 436 ? 1.6496 1.3999 1.7414 0.0350  0.0702  -0.1031 440 GLN B CA  
15669 C C   . GLN B 436 ? 1.6688 1.3973 1.8219 0.0452  0.0820  -0.1328 440 GLN B C   
15670 O O   . GLN B 436 ? 1.6871 1.3762 1.8777 0.0562  0.0740  -0.1290 440 GLN B O   
15671 C CB  . GLN B 436 ? 1.6119 1.3741 1.6986 0.0561  0.0483  -0.0737 440 GLN B CB  
15672 C CG  . GLN B 436 ? 1.6307 1.3635 1.7161 0.0657  0.0244  -0.0417 440 GLN B CG  
15673 C CD  . GLN B 436 ? 1.5978 1.3521 1.6510 0.0722  0.0078  -0.0122 440 GLN B CD  
15674 O OE1 . GLN B 436 ? 1.4991 1.2891 1.5261 0.0678  0.0147  -0.0133 440 GLN B OE1 
15675 N NE2 . GLN B 436 ? 1.6646 1.3967 1.7201 0.0810  -0.0139 0.0146  440 GLN B NE2 
15684 N N   . LYS B 437 ? 1.6708 1.4244 1.8372 0.0408  0.1012  -0.1624 441 LYS B N   
15685 C CA  . LYS B 437 ? 1.6909 1.4288 1.9217 0.0517  0.1143  -0.1934 441 LYS B CA  
15686 C C   . LYS B 437 ? 1.7326 1.4394 1.9874 0.0363  0.1339  -0.2213 441 LYS B C   
15687 O O   . LYS B 437 ? 1.7685 1.4451 2.0871 0.0512  0.1373  -0.2367 441 LYS B O   
15688 C CB  . LYS B 437 ? 1.6582 1.4336 1.8915 0.0463  0.1322  -0.2200 441 LYS B CB  
15689 C CG  . LYS B 437 ? 1.5896 1.3907 1.8123 0.0647  0.1147  -0.1968 441 LYS B CG  
15690 C CD  . LYS B 437 ? 1.5425 1.3788 1.7655 0.0567  0.1330  -0.2235 441 LYS B CD  
15691 C CE  . LYS B 437 ? 1.4821 1.3410 1.6960 0.0748  0.1165  -0.2011 441 LYS B CE  
15692 N NZ  . LYS B 437 ? 1.4617 1.3539 1.6726 0.0651  0.1338  -0.2258 441 LYS B NZ  
15706 N N   . GLU B 438 ? 1.7463 1.4601 1.9546 0.0064  0.1469  -0.2284 442 GLU B N   
15707 C CA  . GLU B 438 ? 1.8218 1.5066 2.0468 -0.0126 0.1676  -0.2563 442 GLU B CA  
15708 C C   . GLU B 438 ? 1.8161 1.4576 2.0452 -0.0036 0.1480  -0.2282 442 GLU B C   
15709 O O   . GLU B 438 ? 1.7564 1.3997 1.9342 -0.0186 0.1395  -0.2065 442 GLU B O   
15710 C CB  . GLU B 438 ? 1.8858 1.5992 2.0566 -0.0517 0.1887  -0.2747 442 GLU B CB  
15711 C CG  . GLU B 438 ? 1.9160 1.6678 2.0842 -0.0668 0.2107  -0.3065 442 GLU B CG  
15712 C CD  . GLU B 438 ? 1.9489 1.7306 2.0608 -0.1093 0.2285  -0.3212 442 GLU B CD  
15713 O OE1 . GLU B 438 ? 1.9665 1.7439 2.0401 -0.1246 0.2218  -0.3036 442 GLU B OE1 
15714 O OE2 . GLU B 438 ? 1.9520 1.7633 2.0574 -0.1294 0.2487  -0.3497 442 GLU B OE2 
15721 N N   . VAL B 439 ? 1.8787 1.4813 2.1720 0.0207  0.1400  -0.2279 443 VAL B N   
15722 C CA  . VAL B 439 ? 1.9119 1.4707 2.2122 0.0306  0.1172  -0.1967 443 VAL B CA  
15723 C C   . VAL B 439 ? 1.9322 1.4638 2.2150 0.0038  0.1334  -0.2109 443 VAL B C   
15724 O O   . VAL B 439 ? 1.9667 1.4900 2.2025 -0.0077 0.1201  -0.1840 443 VAL B O   
15725 C CB  . VAL B 439 ? 1.9374 1.4613 2.3165 0.0622  0.1030  -0.1917 443 VAL B CB  
15726 C CG1 . VAL B 439 ? 1.8829 1.4315 2.2653 0.0871  0.0778  -0.1640 443 VAL B CG1 
15727 C CG2 . VAL B 439 ? 1.9715 1.4849 2.4203 0.0639  0.1324  -0.2403 443 VAL B CG2 
15737 N N   . GLU B 440 ? 1.8985 1.4168 2.2189 -0.0085 0.1639  -0.2551 444 GLU B N   
15738 C CA  . GLU B 440 ? 1.8859 1.3758 2.1949 -0.0358 0.1830  -0.2739 444 GLU B CA  
15739 C C   . GLU B 440 ? 1.7830 1.2176 2.1109 -0.0237 0.1610  -0.2443 444 GLU B C   
15740 O O   . GLU B 440 ? 1.7431 1.1684 2.0202 -0.0403 0.1516  -0.2223 444 GLU B O   
15741 C CB  . GLU B 440 ? 1.9559 1.4836 2.1831 -0.0704 0.1911  -0.2721 444 GLU B CB  
15742 C CG  . GLU B 440 ? 1.9884 1.5716 2.1902 -0.0851 0.2082  -0.2943 444 GLU B CG  
15743 C CD  . GLU B 440 ? 2.0066 1.6307 2.1301 -0.1133 0.2060  -0.2796 444 GLU B CD  
15744 O OE1 . GLU B 440 ? 2.0355 1.6455 2.1259 -0.1244 0.1961  -0.2588 444 GLU B OE1 
15745 O OE2 . GLU B 440 ? 1.9880 1.6587 2.0849 -0.1249 0.2134  -0.2880 444 GLU B OE2 
15752 N N   . VAL B 441 ? 1.7399 1.1382 2.1442 0.0049  0.1521  -0.2436 445 VAL B N   
15753 C CA  . VAL B 441 ? 1.7203 1.0658 2.1473 0.0196  0.1250  -0.2089 445 VAL B CA  
15754 C C   . VAL B 441 ? 1.7239 1.0242 2.1544 -0.0031 0.1435  -0.2271 445 VAL B C   
15755 O O   . VAL B 441 ? 1.7312 1.0291 2.1833 -0.0205 0.1794  -0.2743 445 VAL B O   
15756 C CB  . VAL B 441 ? 1.7314 1.0526 2.2456 0.0565  0.1084  -0.2017 445 VAL B CB  
15757 C CG1 . VAL B 441 ? 1.7616 1.0325 2.2914 0.0704  0.0730  -0.1561 445 VAL B CG1 
15758 C CG2 . VAL B 441 ? 1.6821 1.0518 2.1957 0.0756  0.0967  -0.1929 445 VAL B CG2 
15768 N N   . ASN B 442 ? 1.7277 0.9916 2.1353 -0.0054 0.1196  -0.1901 446 ASN B N   
15769 C CA  . ASN B 442 ? 1.7738 0.9870 2.1858 -0.0251 0.1323  -0.2007 446 ASN B CA  
15770 C C   . ASN B 442 ? 1.8097 1.0475 2.1771 -0.0633 0.1702  -0.2417 446 ASN B C   
15771 O O   . ASN B 442 ? 1.8471 1.0559 2.2478 -0.0782 0.2002  -0.2806 446 ASN B O   
15772 C CB  . ASN B 442 ? 1.7767 0.9340 2.2875 -0.0042 0.1372  -0.2167 446 ASN B CB  
15773 C CG  . ASN B 442 ? 1.7298 0.8629 2.2873 0.0317  0.0962  -0.1724 446 ASN B CG  
15774 O OD1 . ASN B 442 ? 1.6962 0.8425 2.2046 0.0356  0.0633  -0.1266 446 ASN B OD1 
15775 N ND2 . ASN B 442 ? 1.7300 0.8289 2.3850 0.0567  0.0982  -0.1862 446 ASN B ND2 
15782 N N   . SER B 443 ? 1.7991 1.0915 2.0914 -0.0804 0.1685  -0.2324 447 SER B N   
15783 C CA  . SER B 443 ? 1.8100 1.1354 2.0554 -0.1180 0.1999  -0.2663 447 SER B CA  
15784 C C   . SER B 443 ? 1.8363 1.1350 2.0392 -0.1479 0.2040  -0.2610 447 SER B C   
15785 O O   . SER B 443 ? 1.7941 1.0662 1.9784 -0.1422 0.1776  -0.2222 447 SER B O   
15786 C CB  . SER B 443 ? 1.7659 1.1600 1.9522 -0.1242 0.1938  -0.2548 447 SER B CB  
15787 O OG  . SER B 443 ? 1.7747 1.2053 1.9330 -0.1570 0.2252  -0.2928 447 SER B OG  
15793 N N   . SER B 444 ? 1.7891 1.2471 1.6192 -0.0081 -0.1520 -0.1932 448 SER B N   
15794 C CA  . SER B 444 ? 1.8352 1.2689 1.6574 -0.0239 -0.1690 -0.2139 448 SER B CA  
15795 C C   . SER B 444 ? 1.7508 1.2181 1.6186 -0.0364 -0.2046 -0.2119 448 SER B C   
15796 O O   . SER B 444 ? 1.6948 1.1584 1.5883 -0.0459 -0.2154 -0.2211 448 SER B O   
15797 C CB  . SER B 444 ? 1.9609 1.3435 1.7068 -0.0347 -0.1756 -0.2319 448 SER B CB  
15798 O OG  . SER B 444 ? 2.0002 1.3940 1.7219 -0.0409 -0.2012 -0.2252 448 SER B OG  
15804 N N   . LYS B 445 ? 1.7208 1.2196 1.6040 -0.0355 -0.2204 -0.1980 449 LYS B N   
15805 C CA  . LYS B 445 ? 1.6405 1.1682 1.5653 -0.0453 -0.2508 -0.1936 449 LYS B CA  
15806 C C   . LYS B 445 ? 1.5196 1.0771 1.5046 -0.0370 -0.2448 -0.1879 449 LYS B C   
15807 O O   . LYS B 445 ? 1.4377 1.0174 1.4597 -0.0416 -0.2641 -0.1826 449 LYS B O   
15808 C CB  . LYS B 445 ? 1.6339 1.1815 1.5561 -0.0450 -0.2644 -0.1795 449 LYS B CB  
15809 C CG  . LYS B 445 ? 1.6969 1.2203 1.5611 -0.0549 -0.2799 -0.1823 449 LYS B CG  
15810 C CD  . LYS B 445 ? 1.7107 1.2468 1.5627 -0.0468 -0.2763 -0.1641 449 LYS B CD  
15811 C CE  . LYS B 445 ? 1.7453 1.2683 1.5735 -0.0305 -0.2405 -0.1588 449 LYS B CE  
15812 N NZ  . LYS B 445 ? 1.7819 1.3073 1.5868 -0.0231 -0.2347 -0.1402 449 LYS B NZ  
15826 N N   . CYS B 446 ? 1.5267 1.0850 1.5208 -0.0233 -0.2177 -0.1867 450 CYS B N   
15827 C CA  . CYS B 446 ? 1.5252 1.1109 1.5661 -0.0122 -0.2105 -0.1802 450 CYS B CA  
15828 C C   . CYS B 446 ? 1.5444 1.1149 1.5924 -0.0063 -0.1885 -0.1844 450 CYS B C   
15829 O O   . CYS B 446 ? 1.5040 1.0889 1.5679 0.0097  -0.1674 -0.1760 450 CYS B O   
15830 C CB  . CYS B 446 ? 1.5516 1.1646 1.6048 0.0013  -0.2022 -0.1688 450 CYS B CB  
15831 S SG  . CYS B 446 ? 1.5681 1.1976 1.6241 -0.0051 -0.2246 -0.1621 450 CYS B SG  
15836 N N   . HIS B 447 ? 1.5940 1.1353 1.6327 -0.0199 -0.1948 -0.1964 451 HIS B N   
15837 C CA  . HIS B 447 ? 1.5928 1.1167 1.6487 -0.0172 -0.1758 -0.2004 451 HIS B CA  
15838 C C   . HIS B 447 ? 1.6299 1.1366 1.6639 -0.0033 -0.1411 -0.1991 451 HIS B C   
15839 O O   . HIS B 447 ? 1.6444 1.1688 1.7056 0.0140  -0.1179 -0.1866 451 HIS B O   
15840 C CB  . HIS B 447 ? 1.5068 1.0616 1.6177 -0.0065 -0.1724 -0.1880 451 HIS B CB  
15841 C CG  . HIS B 447 ? 1.5037 1.0420 1.6453 -0.0085 -0.1605 -0.1896 451 HIS B CG  
15842 N ND1 . HIS B 447 ? 1.5289 1.0431 1.6789 -0.0300 -0.1798 -0.2010 451 HIS B ND1 
15843 C CD2 . HIS B 447 ? 1.4854 1.0290 1.6557 0.0081  -0.1318 -0.1793 451 HIS B CD2 
15844 C CE1 . HIS B 447 ? 1.5319 1.0354 1.7192 -0.0276 -0.1627 -0.1985 451 HIS B CE1 
15845 N NE2 . HIS B 447 ? 1.5048 1.0257 1.7042 -0.0032 -0.1314 -0.1843 451 HIS B NE2 
15853 N N   . HIS B 448 ? 1.6393 1.1107 1.6217 -0.0095 -0.1364 -0.2100 452 HIS B N   
15854 C CA  . HIS B 448 ? 1.6403 1.0843 1.5981 0.0028  -0.0998 -0.2095 452 HIS B CA  
15855 C C   . HIS B 448 ? 1.6481 1.1299 1.6296 0.0247  -0.0787 -0.1863 452 HIS B C   
15856 O O   . HIS B 448 ? 1.6610 1.1494 1.6674 0.0398  -0.0513 -0.1751 452 HIS B O   
15857 C CB  . HIS B 448 ? 1.5820 0.9955 1.5552 0.0015  -0.0809 -0.2185 452 HIS B CB  
15858 C CG  . HIS B 448 ? 1.5770 0.9652 1.5506 -0.0222 -0.1088 -0.2383 452 HIS B CG  
15859 N ND1 . HIS B 448 ? 1.6366 0.9772 1.5537 -0.0405 -0.1236 -0.2617 452 HIS B ND1 
15860 C CD2 . HIS B 448 ? 1.5438 0.9480 1.5693 -0.0304 -0.1252 -0.2365 452 HIS B CD2 
15861 C CE1 . HIS B 448 ? 1.6478 0.9789 1.5855 -0.0617 -0.1525 -0.2741 452 HIS B CE1 
15862 N NE2 . HIS B 448 ? 1.5885 0.9585 1.5967 -0.0556 -0.1522 -0.2575 452 HIS B NE2 
15870 N N   . GLY B 449 ? 1.6394 1.1472 1.6164 0.0255  -0.0933 -0.1776 453 GLY B N   
15871 C CA  . GLY B 449 ? 1.6237 1.1658 1.6232 0.0423  -0.0790 -0.1565 453 GLY B CA  
15872 C C   . GLY B 449 ? 1.5844 1.1706 1.6308 0.0513  -0.0862 -0.1454 453 GLY B C   
15873 O O   . GLY B 449 ? 1.5534 1.1674 1.6207 0.0657  -0.0738 -0.1278 453 GLY B O   
15877 N N   . ASN B 450 ? 1.5847 1.1780 1.6474 0.0442  -0.1060 -0.1536 454 ASN B N   
15878 C CA  . ASN B 450 ? 1.5255 1.1555 1.6224 0.0551  -0.1114 -0.1443 454 ASN B CA  
15879 C C   . ASN B 450 ? 1.4868 1.1455 1.5906 0.0529  -0.1364 -0.1424 454 ASN B C   
15880 O O   . ASN B 450 ? 1.4333 1.1185 1.5560 0.0622  -0.1428 -0.1377 454 ASN B O   
15881 C CB  . ASN B 450 ? 1.4839 1.1066 1.5994 0.0517  -0.1153 -0.1504 454 ASN B CB  
15882 C CG  . ASN B 450 ? 1.4250 1.0393 1.5567 0.0640  -0.0860 -0.1431 454 ASN B CG  
15883 O OD1 . ASN B 450 ? 1.3984 1.0354 1.5418 0.0824  -0.0686 -0.1272 454 ASN B OD1 
15884 N ND2 . ASN B 450 ? 1.4193 1.0014 1.5547 0.0533  -0.0816 -0.1533 454 ASN B ND2 
15891 N N   . GLY B 451 ? 1.5120 1.1633 1.5990 0.0418  -0.1492 -0.1460 455 GLY B N   
15892 C CA  . GLY B 451 ? 1.4884 1.1632 1.5872 0.0390  -0.1703 -0.1435 455 GLY B CA  
15893 C C   . GLY B 451 ? 1.4959 1.1615 1.5783 0.0320  -0.1718 -0.1398 455 GLY B C   
15894 O O   . GLY B 451 ? 1.4991 1.1393 1.5545 0.0314  -0.1550 -0.1394 455 GLY B O   
15898 N N   . SER B 452 ? 1.5001 1.1839 1.5983 0.0279  -0.1898 -0.1366 456 SER B N   
15899 C CA  . SER B 452 ? 1.5186 1.1982 1.6096 0.0228  -0.1910 -0.1286 456 SER B CA  
15900 C C   . SER B 452 ? 1.5661 1.2419 1.6562 0.0110  -0.2135 -0.1340 456 SER B C   
15901 O O   . SER B 452 ? 1.5711 1.2599 1.6839 0.0087  -0.2300 -0.1395 456 SER B O   
15902 C CB  . SER B 452 ? 1.4513 1.1583 1.5746 0.0285  -0.1903 -0.1143 456 SER B CB  
15903 O OG  . SER B 452 ? 1.4025 1.1314 1.5536 0.0263  -0.2120 -0.1202 456 SER B OG  
15909 N N   . PHE B 453 ? 1.5901 1.2470 1.6517 0.0054  -0.2123 -0.1307 457 PHE B N   
15910 C CA  . PHE B 453 ? 1.5729 1.2280 1.6328 -0.0049 -0.2329 -0.1306 457 PHE B CA  
15911 C C   . PHE B 453 ? 1.5575 1.2285 1.6417 -0.0037 -0.2351 -0.1156 457 PHE B C   
15912 O O   . PHE B 453 ? 1.5879 1.2525 1.6574 0.0007  -0.2203 -0.1027 457 PHE B O   
15913 C CB  . PHE B 453 ? 1.6070 1.2330 1.6174 -0.0115 -0.2337 -0.1346 457 PHE B CB  
15914 C CG  . PHE B 453 ? 1.6324 1.2586 1.6443 -0.0236 -0.2598 -0.1378 457 PHE B CG  
15915 C CD1 . PHE B 453 ? 1.6422 1.2745 1.6791 -0.0282 -0.2718 -0.1467 457 PHE B CD1 
15916 C CD2 . PHE B 453 ? 1.6554 1.2775 1.6466 -0.0287 -0.2710 -0.1280 457 PHE B CD2 
15917 C CE1 . PHE B 453 ? 1.6499 1.2857 1.6976 -0.0388 -0.2950 -0.1449 457 PHE B CE1 
15918 C CE2 . PHE B 453 ? 1.6687 1.2955 1.6665 -0.0395 -0.2965 -0.1267 457 PHE B CE2 
15919 C CZ  . PHE B 453 ? 1.6621 1.2964 1.6913 -0.0451 -0.3089 -0.1348 457 PHE B CZ  
15929 N N   . GLN B 454 ? 1.5160 1.2051 1.6393 -0.0069 -0.2512 -0.1167 458 GLN B N   
15930 C CA  . GLN B 454 ? 1.4762 1.1805 1.6351 -0.0070 -0.2540 -0.1047 458 GLN B CA  
15931 C C   . GLN B 454 ? 1.4477 1.1499 1.6132 -0.0130 -0.2643 -0.0947 458 GLN B C   
15932 O O   . GLN B 454 ? 1.4851 1.1868 1.6501 -0.0112 -0.2559 -0.0771 458 GLN B O   
15933 C CB  . GLN B 454 ? 1.4328 1.1535 1.6286 -0.0063 -0.2645 -0.1146 458 GLN B CB  
15934 C CG  . GLN B 454 ? 1.4139 1.1515 1.6464 -0.0055 -0.2638 -0.1051 458 GLN B CG  
15935 C CD  . GLN B 454 ? 1.3992 1.1496 1.6555 -0.0055 -0.2781 -0.1191 458 GLN B CD  
15936 O OE1 . GLN B 454 ? 1.3936 1.1533 1.6868 -0.0108 -0.2897 -0.1182 458 GLN B OE1 
15937 N NE2 . GLN B 454 ? 1.3864 1.1354 1.6203 0.0007  -0.2772 -0.1321 458 GLN B NE2 
15946 N N   . CYS B 455 ? 1.3859 1.0879 1.5608 -0.0183 -0.2800 -0.1018 459 CYS B N   
15947 C CA  . CYS B 455 ? 1.3954 1.0994 1.5860 -0.0229 -0.2902 -0.0892 459 CYS B CA  
15948 C C   . CYS B 455 ? 1.3509 1.0494 1.5259 -0.0282 -0.3034 -0.0922 459 CYS B C   
15949 O O   . CYS B 455 ? 1.2508 0.9555 1.4561 -0.0308 -0.3141 -0.0877 459 CYS B O   
15950 C CB  . CYS B 455 ? 1.4551 1.1688 1.6979 -0.0238 -0.2961 -0.0896 459 CYS B CB  
15951 S SG  . CYS B 455 ? 1.5168 1.2404 1.7938 -0.0222 -0.2879 -0.0826 459 CYS B SG  
15956 N N   . GLY B 456 ? 1.3976 1.0835 1.5295 -0.0303 -0.3027 -0.0988 460 GLY B N   
15957 C CA  . GLY B 456 ? 1.4031 1.0854 1.5286 -0.0376 -0.3181 -0.1032 460 GLY B CA  
15958 C C   . GLY B 456 ? 1.3830 1.0676 1.5307 -0.0356 -0.3170 -0.1170 460 GLY B C   
15959 O O   . GLY B 456 ? 1.4178 1.1037 1.5779 -0.0409 -0.3289 -0.1167 460 GLY B O   
15963 N N   . VAL B 457 ? 1.3346 1.0218 1.4900 -0.0271 -0.3031 -0.1261 461 VAL B N   
15964 C CA  . VAL B 457 ? 1.3058 0.9952 1.4757 -0.0211 -0.2983 -0.1372 461 VAL B CA  
15965 C C   . VAL B 457 ? 1.3297 1.0160 1.4793 -0.0141 -0.2823 -0.1447 461 VAL B C   
15966 O O   . VAL B 457 ? 1.3539 1.0418 1.4937 -0.0119 -0.2745 -0.1406 461 VAL B O   
15967 C CB  . VAL B 457 ? 1.2439 0.9422 1.4486 -0.0149 -0.2998 -0.1390 461 VAL B CB  
15968 C CG1 . VAL B 457 ? 1.2304 0.9286 1.4418 -0.0053 -0.2922 -0.1484 461 VAL B CG1 
15969 C CG2 . VAL B 457 ? 1.2329 0.9337 1.4633 -0.0202 -0.3113 -0.1275 461 VAL B CG2 
15979 N N   . CYS B 458 ? 1.3285 1.0120 1.4776 -0.0092 -0.2752 -0.1518 462 CYS B N   
15980 C CA  . CYS B 458 ? 1.3503 1.0325 1.4850 -0.0007 -0.2579 -0.1556 462 CYS B CA  
15981 C C   . CYS B 458 ? 1.2695 0.9682 1.4207 0.0111  -0.2540 -0.1577 462 CYS B C   
15982 O O   . CYS B 458 ? 1.2086 0.9114 1.3744 0.0167  -0.2570 -0.1615 462 CYS B O   
15983 C CB  . CYS B 458 ? 1.4397 1.1091 1.5675 -0.0010 -0.2504 -0.1602 462 CYS B CB  
15984 S SG  . CYS B 458 ? 1.5275 1.1691 1.6187 -0.0149 -0.2529 -0.1638 462 CYS B SG  
15989 N N   . ALA B 459 ? 1.2790 0.9869 1.4270 0.0155  -0.2475 -0.1542 463 ALA B N   
15990 C CA  . ALA B 459 ? 1.2991 1.0242 1.4570 0.0260  -0.2468 -0.1561 463 ALA B CA  
15991 C C   . ALA B 459 ? 1.3652 1.0925 1.5123 0.0366  -0.2283 -0.1522 463 ALA B C   
15992 O O   . ALA B 459 ? 1.3913 1.1178 1.5323 0.0376  -0.2156 -0.1440 463 ALA B O   
15993 C CB  . ALA B 459 ? 1.2648 1.0032 1.4376 0.0226  -0.2546 -0.1509 463 ALA B CB  
15999 N N   . CYS B 460 ? 1.3906 1.1196 1.5376 0.0466  -0.2233 -0.1557 464 CYS B N   
16000 C CA  . CYS B 460 ? 1.4235 1.1506 1.5653 0.0567  -0.2027 -0.1500 464 CYS B CA  
16001 C C   . CYS B 460 ? 1.4562 1.2047 1.5991 0.0691  -0.1948 -0.1405 464 CYS B C   
16002 O O   . CYS B 460 ? 1.4543 1.2216 1.6011 0.0720  -0.2093 -0.1414 464 CYS B O   
16003 C CB  . CYS B 460 ? 1.4323 1.1556 1.5802 0.0651  -0.1971 -0.1519 464 CYS B CB  
16004 S SG  . CYS B 460 ? 1.4421 1.1449 1.6011 0.0502  -0.2058 -0.1566 464 CYS B SG  
16009 N N   . HIS B 461 ? 1.4902 1.2350 1.6315 0.0759  -0.1725 -0.1310 465 HIS B N   
16010 C CA  . HIS B 461 ? 1.4957 1.2635 1.6437 0.0902  -0.1613 -0.1163 465 HIS B CA  
16011 C C   . HIS B 461 ? 1.4919 1.2755 1.6387 0.1069  -0.1595 -0.1135 465 HIS B C   
16012 O O   . HIS B 461 ? 1.4521 1.2231 1.5958 0.1093  -0.1568 -0.1203 465 HIS B O   
16013 C CB  . HIS B 461 ? 1.5105 1.2643 1.6588 0.0940  -0.1327 -0.1057 465 HIS B CB  
16014 C CG  . HIS B 461 ? 1.5282 1.2672 1.6704 0.0835  -0.1290 -0.1044 465 HIS B CG  
16015 N ND1 . HIS B 461 ? 1.5291 1.2724 1.6723 0.0719  -0.1498 -0.1087 465 HIS B ND1 
16016 C CD2 . HIS B 461 ? 1.5528 1.2699 1.6862 0.0851  -0.1034 -0.0981 465 HIS B CD2 
16017 C CE1 . HIS B 461 ? 1.5454 1.2728 1.6802 0.0679  -0.1368 -0.1028 465 HIS B CE1 
16018 N NE2 . HIS B 461 ? 1.5630 1.2724 1.6881 0.0760  -0.1084 -0.0975 465 HIS B NE2 
16026 N N   . PRO B 462 ? 1.5368 1.3493 1.6866 0.1198  -0.1606 -0.1009 466 PRO B N   
16027 C CA  . PRO B 462 ? 1.5624 1.3900 1.7021 0.1390  -0.1576 -0.0960 466 PRO B CA  
16028 C C   . PRO B 462 ? 1.5629 1.3770 1.7088 0.1506  -0.1270 -0.0869 466 PRO B C   
16029 O O   . PRO B 462 ? 1.5584 1.3631 1.7179 0.1501  -0.1051 -0.0771 466 PRO B O   
16030 C CB  . PRO B 462 ? 1.5869 1.4502 1.7317 0.1489  -0.1642 -0.0793 466 PRO B CB  
16031 C CG  . PRO B 462 ? 1.5807 1.4449 1.7485 0.1385  -0.1571 -0.0689 466 PRO B CG  
16032 C CD  . PRO B 462 ? 1.5534 1.3885 1.7180 0.1185  -0.1651 -0.0873 466 PRO B CD  
16040 N N   . GLY B 463 ? 1.5642 1.3744 1.7019 0.1618  -0.1236 -0.0897 467 GLY B N   
16041 C CA  . GLY B 463 ? 1.5500 1.3485 1.7027 0.1730  -0.0948 -0.0789 467 GLY B CA  
16042 C C   . GLY B 463 ? 1.5162 1.2831 1.6852 0.1557  -0.0915 -0.0902 467 GLY B C   
16043 O O   . GLY B 463 ? 1.5039 1.2573 1.6942 0.1594  -0.0687 -0.0820 467 GLY B O   
16047 N N   . HIS B 464 ? 1.4989 1.2542 1.6616 0.1364  -0.1149 -0.1074 468 HIS B N   
16048 C CA  . HIS B 464 ? 1.4905 1.2196 1.6674 0.1183  -0.1181 -0.1168 468 HIS B CA  
16049 C C   . HIS B 464 ? 1.4782 1.2058 1.6527 0.1113  -0.1397 -0.1274 468 HIS B C   
16050 O O   . HIS B 464 ? 1.4784 1.2105 1.6390 0.1025  -0.1596 -0.1365 468 HIS B O   
16051 C CB  . HIS B 464 ? 1.4892 1.2009 1.6598 0.0999  -0.1208 -0.1237 468 HIS B CB  
16052 C CG  . HIS B 464 ? 1.4663 1.1691 1.6424 0.1063  -0.0941 -0.1144 468 HIS B CG  
16053 N ND1 . HIS B 464 ? 1.4519 1.1721 1.6233 0.1188  -0.0817 -0.1017 468 HIS B ND1 
16054 C CD2 . HIS B 464 ? 1.4658 1.1431 1.6560 0.1020  -0.0766 -0.1149 468 HIS B CD2 
16055 C CE1 . HIS B 464 ? 1.4594 1.1641 1.6408 0.1238  -0.0542 -0.0938 468 HIS B CE1 
16056 N NE2 . HIS B 464 ? 1.4779 1.1539 1.6690 0.1131  -0.0509 -0.1036 468 HIS B NE2 
16064 N N   . MET B 465 ? 1.4654 1.1864 1.6595 0.1160  -0.1334 -0.1237 469 MET B N   
16065 C CA  . MET B 465 ? 1.4676 1.1856 1.6660 0.1132  -0.1472 -0.1293 469 MET B CA  
16066 C C   . MET B 465 ? 1.4656 1.1686 1.6933 0.0936  -0.1558 -0.1301 469 MET B C   
16067 O O   . MET B 465 ? 1.4991 1.1933 1.7502 0.0891  -0.1454 -0.1240 469 MET B O   
16068 C CB  . MET B 465 ? 1.5076 1.2314 1.7067 0.1386  -0.1304 -0.1198 469 MET B CB  
16069 C CG  . MET B 465 ? 1.5628 1.3022 1.7256 0.1591  -0.1261 -0.1192 469 MET B CG  
16070 S SD  . MET B 465 ? 1.6174 1.3592 1.7690 0.1936  -0.1009 -0.1057 469 MET B SD  
16071 C CE  . MET B 465 ? 1.6470 1.4086 1.7452 0.2105  -0.1089 -0.1093 469 MET B CE  
16081 N N   . GLY B 466 ? 1.4406 1.1409 1.6693 0.0811  -0.1762 -0.1370 470 GLY B N   
16082 C CA  . GLY B 466 ? 1.4125 1.1037 1.6692 0.0628  -0.1893 -0.1349 470 GLY B CA  
16083 C C   . GLY B 466 ? 1.3840 1.0724 1.6266 0.0440  -0.2135 -0.1435 470 GLY B C   
16084 O O   . GLY B 466 ? 1.3724 1.0634 1.5865 0.0428  -0.2181 -0.1511 470 GLY B O   
16088 N N   . PRO B 467 ? 1.3710 1.0565 1.6382 0.0297  -0.2294 -0.1388 471 PRO B N   
16089 C CA  . PRO B 467 ? 1.3914 1.0756 1.6451 0.0134  -0.2515 -0.1430 471 PRO B CA  
16090 C C   . PRO B 467 ? 1.4576 1.1316 1.6751 0.0023  -0.2556 -0.1519 471 PRO B C   
16091 O O   . PRO B 467 ? 1.4949 1.1703 1.6909 -0.0016 -0.2632 -0.1549 471 PRO B O   
16092 C CB  . PRO B 467 ? 1.3589 1.0444 1.6494 0.0004  -0.2675 -0.1321 471 PRO B CB  
16093 C CG  . PRO B 467 ? 1.3347 1.0253 1.6650 0.0149  -0.2507 -0.1205 471 PRO B CG  
16094 C CD  . PRO B 467 ? 1.3414 1.0281 1.6550 0.0289  -0.2279 -0.1256 471 PRO B CD  
16102 N N   . ARG B 468 ? 1.4607 1.1219 1.6727 -0.0017 -0.2478 -0.1551 472 ARG B N   
16103 C CA  . ARG B 468 ? 1.4311 1.0757 1.6046 -0.0086 -0.2445 -0.1640 472 ARG B CA  
16104 C C   . ARG B 468 ? 1.3886 1.0303 1.5555 0.0056  -0.2180 -0.1648 472 ARG B C   
16105 O O   . ARG B 468 ? 1.3643 0.9861 1.5075 0.0014  -0.2085 -0.1709 472 ARG B O   
16106 C CB  . ARG B 468 ? 1.4325 1.0557 1.5970 -0.0290 -0.2607 -0.1699 472 ARG B CB  
16107 C CG  . ARG B 468 ? 1.4547 1.0830 1.6172 -0.0430 -0.2888 -0.1661 472 ARG B CG  
16108 C CD  . ARG B 468 ? 1.5491 1.1564 1.6943 -0.0642 -0.3103 -0.1732 472 ARG B CD  
16109 N NE  . ARG B 468 ? 1.6207 1.2385 1.7663 -0.0759 -0.3387 -0.1648 472 ARG B NE  
16110 C CZ  . ARG B 468 ? 1.6730 1.2798 1.8056 -0.0955 -0.3667 -0.1674 472 ARG B CZ  
16111 N NH1 . ARG B 468 ? 1.6595 1.2394 1.7766 -0.1078 -0.3709 -0.1822 472 ARG B NH1 
16112 N NH2 . ARG B 468 ? 1.7083 1.3302 1.8438 -0.1033 -0.3916 -0.1550 472 ARG B NH2 
16126 N N   . CYS B 469 ? 1.3892 1.0488 1.5739 0.0238  -0.2047 -0.1579 473 CYS B N   
16127 C CA  . CYS B 469 ? 1.4204 1.0843 1.6001 0.0403  -0.1804 -0.1538 473 CYS B CA  
16128 C C   . CYS B 469 ? 1.4595 1.1049 1.6531 0.0383  -0.1647 -0.1529 473 CYS B C   
16129 O O   . CYS B 469 ? 1.4787 1.1116 1.6581 0.0409  -0.1476 -0.1540 473 CYS B O   
16130 C CB  . CYS B 469 ? 1.4499 1.1160 1.6011 0.0417  -0.1767 -0.1554 473 CYS B CB  
16131 S SG  . CYS B 469 ? 1.4700 1.1479 1.6111 0.0340  -0.1999 -0.1583 473 CYS B SG  
16136 N N   . GLU B 470 ? 1.4719 1.1149 1.6996 0.0339  -0.1691 -0.1491 474 GLU B N   
16137 C CA  . GLU B 470 ? 1.5070 1.1298 1.7583 0.0262  -0.1603 -0.1493 474 GLU B CA  
16138 C C   . GLU B 470 ? 1.4447 1.0774 1.7310 0.0471  -0.1323 -0.1335 474 GLU B C   
16139 O O   . GLU B 470 ? 1.4308 1.0461 1.7415 0.0434  -0.1188 -0.1319 474 GLU B O   
16140 C CB  . GLU B 470 ? 1.5859 1.2008 1.8624 0.0044  -0.1867 -0.1521 474 GLU B CB  
16141 C CG  . GLU B 470 ? 1.6449 1.2534 1.8858 -0.0141 -0.2154 -0.1635 474 GLU B CG  
16142 C CD  . GLU B 470 ? 1.6563 1.2662 1.9260 -0.0334 -0.2448 -0.1608 474 GLU B CD  
16143 O OE1 . GLU B 470 ? 1.6365 1.2690 1.9389 -0.0269 -0.2502 -0.1474 474 GLU B OE1 
16144 O OE2 . GLU B 470 ? 1.6764 1.2635 1.9354 -0.0549 -0.2629 -0.1718 474 GLU B OE2 
16151 N N   . SER B 471 ? 1.4055 1.0631 1.6927 0.0694  -0.1227 -0.1221 475 SER B N   
16152 C CA  . SER B 471 ? 1.4038 1.0731 1.7139 0.0943  -0.0936 -0.1041 475 SER B CA  
16153 C C   . SER B 471 ? 1.3679 1.0546 1.6432 0.1147  -0.0811 -0.1002 475 SER B C   
16154 O O   . SER B 471 ? 1.3543 1.0504 1.5967 0.1123  -0.0979 -0.1093 475 SER B O   
16155 C CB  . SER B 471 ? 1.4516 1.1337 1.7903 0.1066  -0.0915 -0.0913 475 SER B CB  
16156 O OG  . SER B 471 ? 1.5124 1.2067 1.8197 0.1131  -0.1047 -0.0972 475 SER B OG  
16162 N N   . GLY B 472 ? 1.3617 1.0543 1.6493 0.1345  -0.0524 -0.0842 476 GLY B N   
16163 C CA  . GLY B 472 ? 1.3719 1.0841 1.6319 0.1531  -0.0415 -0.0764 476 GLY B CA  
16164 C C   . GLY B 472 ? 1.3988 1.1341 1.6590 0.1844  -0.0223 -0.0562 476 GLY B C   
16165 O O   . GLY B 472 ? 1.3968 1.1294 1.6901 0.1975  0.0024  -0.0393 476 GLY B O   
16169 N N   . HIS B 473 ? 1.4388 1.1959 1.6613 0.1966  -0.0338 -0.0572 477 HIS B N   
16170 C CA  . HIS B 473 ? 1.5124 1.2911 1.7190 0.2280  -0.0186 -0.0395 477 HIS B CA  
16171 C C   . HIS B 473 ? 1.4927 1.2845 1.7129 0.2454  0.0092  -0.0160 477 HIS B C   
16172 O O   . HIS B 473 ? 1.4820 1.2907 1.6862 0.2470  0.0039  -0.0125 477 HIS B O   
16173 C CB  . HIS B 473 ? 1.6189 1.4146 1.7776 0.2325  -0.0443 -0.0507 477 HIS B CB  
16174 C CG  . HIS B 473 ? 1.7364 1.5524 1.8643 0.2646  -0.0336 -0.0356 477 HIS B CG  
16175 N ND1 . HIS B 473 ? 1.7784 1.6134 1.8613 0.2709  -0.0566 -0.0424 477 HIS B ND1 
16176 C CD2 . HIS B 473 ? 1.7764 1.5964 1.9102 0.2927  -0.0032 -0.0131 477 HIS B CD2 
16177 C CE1 . HIS B 473 ? 1.8145 1.6632 1.8686 0.3016  -0.0428 -0.0267 477 HIS B CE1 
16178 N NE2 . HIS B 473 ? 1.8091 1.6494 1.8930 0.3170  -0.0078 -0.0072 477 HIS B NE2 
16186 N N   . ASP C 1   ? 1.0309 1.1193 1.2259 -0.3764 -0.0268 -0.0469 1   ASP C N   
16187 C CA  . ASP C 1   ? 0.9832 1.0662 1.1469 -0.3534 -0.0434 -0.0506 1   ASP C CA  
16188 C C   . ASP C 1   ? 0.9600 1.0428 1.1532 -0.3320 -0.0543 -0.0843 1   ASP C C   
16189 O O   . ASP C 1   ? 1.0091 1.0941 1.2472 -0.3295 -0.0616 -0.0993 1   ASP C O   
16190 C CB  . ASP C 1   ? 0.9886 1.0433 1.1336 -0.3349 -0.0603 -0.0231 1   ASP C CB  
16191 C CG  . ASP C 1   ? 1.0351 1.0987 1.1564 -0.3484 -0.0493 0.0221  1   ASP C CG  
16192 O OD1 . ASP C 1   ? 1.0569 1.1468 1.1730 -0.3760 -0.0310 0.0300  1   ASP C OD1 
16193 O OD2 . ASP C 1   ? 1.0385 1.0856 1.1472 -0.3295 -0.0568 0.0534  1   ASP C OD2 
16200 N N   . ILE C 2   ? 0.9729 1.0568 1.1407 -0.3185 -0.0547 -0.0937 2   ILE C N   
16201 C CA  . ILE C 2   ? 0.9792 1.0628 1.1723 -0.2917 -0.0635 -0.1168 2   ILE C CA  
16202 C C   . ILE C 2   ? 0.9697 1.0307 1.1636 -0.2684 -0.0945 -0.1144 2   ILE C C   
16203 O O   . ILE C 2   ? 0.9895 1.0277 1.1471 -0.2615 -0.1039 -0.0974 2   ILE C O   
16204 C CB  . ILE C 2   ? 0.9910 1.0699 1.1516 -0.2855 -0.0474 -0.1261 2   ILE C CB  
16205 C CG1 . ILE C 2   ? 1.0268 1.1177 1.1712 -0.3160 -0.0101 -0.1327 2   ILE C CG1 
16206 C CG2 . ILE C 2   ? 0.9903 1.0689 1.1821 -0.2525 -0.0510 -0.1426 2   ILE C CG2 
16207 C CD1 . ILE C 2   ? 1.0387 1.1490 1.2370 -0.3162 0.0131  -0.1475 2   ILE C CD1 
16219 N N   . GLN C 3   ? 0.9771 1.0493 1.2120 -0.2578 -0.1093 -0.1301 3   GLN C N   
16220 C CA  . GLN C 3   ? 1.0227 1.0733 1.2518 -0.2417 -0.1372 -0.1343 3   GLN C CA  
16221 C C   . GLN C 3   ? 0.9708 1.0272 1.1944 -0.2101 -0.1490 -0.1422 3   GLN C C   
16222 O O   . GLN C 3   ? 0.9853 1.0779 1.2466 -0.1998 -0.1470 -0.1509 3   GLN C O   
16223 C CB  . GLN C 3   ? 1.1527 1.2179 1.4225 -0.2590 -0.1489 -0.1474 3   GLN C CB  
16224 C CG  . GLN C 3   ? 1.3128 1.3521 1.5664 -0.2518 -0.1750 -0.1582 3   GLN C CG  
16225 C CD  . GLN C 3   ? 1.4524 1.4277 1.6602 -0.2512 -0.1691 -0.1451 3   GLN C CD  
16226 O OE1 . GLN C 3   ? 1.5164 1.4682 1.7253 -0.2714 -0.1519 -0.1337 3   GLN C OE1 
16227 N NE2 . GLN C 3   ? 1.4950 1.4422 1.6653 -0.2250 -0.1795 -0.1425 3   GLN C NE2 
16236 N N   . MET C 4   ? 0.9388 0.9617 1.1193 -0.1924 -0.1581 -0.1348 4   MET C N   
16237 C CA  . MET C 4   ? 0.9389 0.9593 1.1074 -0.1619 -0.1678 -0.1389 4   MET C CA  
16238 C C   . MET C 4   ? 1.0018 1.0103 1.1632 -0.1503 -0.1960 -0.1462 4   MET C C   
16239 O O   . MET C 4   ? 1.0673 1.0381 1.2008 -0.1560 -0.2008 -0.1428 4   MET C O   
16240 C CB  . MET C 4   ? 0.9179 0.9124 1.0411 -0.1536 -0.1567 -0.1270 4   MET C CB  
16241 C CG  . MET C 4   ? 0.9232 0.9282 1.0378 -0.1760 -0.1290 -0.1232 4   MET C CG  
16242 S SD  . MET C 4   ? 0.9618 0.9909 1.1135 -0.1748 -0.1025 -0.1398 4   MET C SD  
16243 C CE  . MET C 4   ? 0.9477 0.9613 1.0939 -0.1340 -0.1051 -0.1425 4   MET C CE  
16253 N N   . THR C 5   ? 0.9962 1.0375 1.1812 -0.1341 -0.2116 -0.1541 5   THR C N   
16254 C CA  . THR C 5   ? 0.9994 1.0416 1.1736 -0.1305 -0.2409 -0.1640 5   THR C CA  
16255 C C   . THR C 5   ? 0.9813 1.0326 1.1411 -0.0948 -0.2519 -0.1579 5   THR C C   
16256 O O   . THR C 5   ? 0.9631 1.0538 1.1574 -0.0755 -0.2452 -0.1495 5   THR C O   
16257 C CB  . THR C 5   ? 0.9928 1.0878 1.2146 -0.1548 -0.2566 -0.1761 5   THR C CB  
16258 O OG1 . THR C 5   ? 0.9567 1.1111 1.2352 -0.1452 -0.2462 -0.1680 5   THR C OG1 
16259 C CG2 . THR C 5   ? 1.0039 1.0734 1.2283 -0.1928 -0.2466 -0.1841 5   THR C CG2 
16267 N N   . GLN C 6   ? 0.9920 1.0031 1.1014 -0.0838 -0.2636 -0.1596 6   GLN C N   
16268 C CA  . GLN C 6   ? 1.0196 1.0360 1.1072 -0.0518 -0.2767 -0.1531 6   GLN C CA  
16269 C C   . GLN C 6   ? 1.1334 1.1723 1.2093 -0.0636 -0.3094 -0.1670 6   GLN C C   
16270 O O   . GLN C 6   ? 1.1892 1.1806 1.2180 -0.0775 -0.3145 -0.1809 6   GLN C O   
16271 C CB  . GLN C 6   ? 1.0070 0.9652 1.0429 -0.0336 -0.2633 -0.1448 6   GLN C CB  
16272 C CG  . GLN C 6   ? 1.0029 0.9479 1.0446 -0.0324 -0.2335 -0.1333 6   GLN C CG  
16273 C CD  . GLN C 6   ? 1.0275 0.9281 1.0242 -0.0214 -0.2223 -0.1229 6   GLN C CD  
16274 O OE1 . GLN C 6   ? 1.0434 0.9298 1.0328 -0.0368 -0.2078 -0.1151 6   GLN C OE1 
16275 N NE2 . GLN C 6   ? 1.0397 0.9258 1.0083 0.0053  -0.2289 -0.1188 6   GLN C NE2 
16284 N N   . THR C 7   ? 1.1612 1.2751 1.2799 -0.0598 -0.3290 -0.1623 7   THR C N   
16285 C CA  . THR C 7   ? 1.2027 1.3597 1.3160 -0.0837 -0.3643 -0.1765 7   THR C CA  
16286 C C   . THR C 7   ? 1.1978 1.3087 1.2344 -0.0798 -0.3782 -0.1866 7   THR C C   
16287 O O   . THR C 7   ? 1.2526 1.3314 1.2494 -0.1148 -0.3868 -0.2129 7   THR C O   
16288 C CB  . THR C 7   ? 1.2561 1.5166 1.4289 -0.0680 -0.3846 -0.1566 7   THR C CB  
16289 O OG1 . THR C 7   ? 1.2876 1.5484 1.4586 -0.0171 -0.3737 -0.1286 7   THR C OG1 
16290 C CG2 . THR C 7   ? 1.2293 1.5393 1.4801 -0.0812 -0.3702 -0.1522 7   THR C CG2 
16298 N N   . THR C 8   ? 1.1609 1.2611 1.1726 -0.0388 -0.3753 -0.1671 8   THR C N   
16299 C CA  . THR C 8   ? 1.2033 1.2619 1.1407 -0.0308 -0.3852 -0.1736 8   THR C CA  
16300 C C   . THR C 8   ? 1.1854 1.1485 1.0803 -0.0269 -0.3540 -0.1795 8   THR C C   
16301 O O   . THR C 8   ? 1.0776 1.0176 0.9814 -0.0004 -0.3303 -0.1608 8   THR C O   
16302 C CB  . THR C 8   ? 1.2179 1.3117 1.1505 0.0129  -0.3941 -0.1450 8   THR C CB  
16303 O OG1 . THR C 8   ? 1.2654 1.3376 1.2267 0.0462  -0.3620 -0.1230 8   THR C OG1 
16304 C CG2 . THR C 8   ? 1.1714 1.3735 1.1498 0.0124  -0.4272 -0.1305 8   THR C CG2 
16312 N N   . SER C 9   ? 1.2999 1.2092 1.1497 -0.0550 -0.3512 -0.2042 9   SER C N   
16313 C CA  . SER C 9   ? 1.3670 1.1919 1.1825 -0.0476 -0.3193 -0.2035 9   SER C CA  
16314 C C   . SER C 9   ? 1.3907 1.1771 1.1493 -0.0166 -0.3129 -0.1950 9   SER C C   
16315 O O   . SER C 9   ? 1.4019 1.1312 1.1420 -0.0024 -0.2848 -0.1856 9   SER C O   
16316 C CB  . SER C 9   ? 1.4490 1.2197 1.2397 -0.0849 -0.3082 -0.2301 9   SER C CB  
16317 O OG  . SER C 9   ? 1.4633 1.2627 1.3068 -0.1144 -0.3087 -0.2358 9   SER C OG  
16323 N N   . SER C 10  ? 1.3728 1.1950 1.1062 -0.0051 -0.3375 -0.1938 10  SER C N   
16324 C CA  . SER C 10  ? 1.3369 1.1231 1.0123 0.0235  -0.3306 -0.1851 10  SER C CA  
16325 C C   . SER C 10  ? 1.3063 1.1575 0.9740 0.0395  -0.3611 -0.1726 10  SER C C   
16326 O O   . SER C 10  ? 1.3417 1.2570 1.0235 0.0169  -0.3925 -0.1813 10  SER C O   
16327 C CB  . SER C 10  ? 1.4043 1.1165 1.0083 0.0056  -0.3173 -0.2113 10  SER C CB  
16328 O OG  . SER C 10  ? 1.4097 1.0904 0.9553 0.0328  -0.3095 -0.2032 10  SER C OG  
16334 N N   . LEU C 11  ? 1.2721 1.1114 0.9198 0.0781  -0.3510 -0.1483 11  LEU C N   
16335 C CA  . LEU C 11  ? 1.2873 1.1834 0.9251 0.1015  -0.3747 -0.1270 11  LEU C CA  
16336 C C   . LEU C 11  ? 1.3083 1.1544 0.8840 0.1313  -0.3582 -0.1142 11  LEU C C   
16337 O O   . LEU C 11  ? 1.3080 1.0877 0.8699 0.1399  -0.3258 -0.1149 11  LEU C O   
16338 C CB  . LEU C 11  ? 1.2540 1.2092 0.9685 0.1265  -0.3737 -0.0967 11  LEU C CB  
16339 C CG  . LEU C 11  ? 1.2168 1.1295 0.9578 0.1532  -0.3347 -0.0785 11  LEU C CG  
16340 C CD1 . LEU C 11  ? 1.2657 1.1626 0.9764 0.1936  -0.3226 -0.0503 11  LEU C CD1 
16341 C CD2 . LEU C 11  ? 1.1520 1.1051 0.9709 0.1540  -0.3257 -0.0690 11  LEU C CD2 
16353 N N   . SER C 12  ? 1.3271 1.2136 0.8678 0.1469  -0.3810 -0.0985 12  SER C N   
16354 C CA  . SER C 12  ? 1.3578 1.2034 0.8328 0.1741  -0.3677 -0.0848 12  SER C CA  
16355 C C   . SER C 12  ? 1.2963 1.1819 0.7989 0.2188  -0.3663 -0.0395 12  SER C C   
16356 O O   . SER C 12  ? 1.2711 1.2376 0.8132 0.2268  -0.3924 -0.0184 12  SER C O   
16357 C CB  . SER C 12  ? 1.4588 1.3058 0.8468 0.1501  -0.3916 -0.1066 12  SER C CB  
16358 O OG  . SER C 12  ? 1.4982 1.4381 0.8998 0.1274  -0.4364 -0.1072 12  SER C OG  
16364 N N   . ALA C 13  ? 1.2648 1.0941 0.7496 0.2484  -0.3324 -0.0219 13  ALA C N   
16365 C CA  . ALA C 13  ? 1.2645 1.1095 0.7710 0.2915  -0.3186 0.0208  13  ALA C CA  
16366 C C   . ALA C 13  ? 1.2896 1.0774 0.7308 0.3141  -0.2951 0.0337  13  ALA C C   
16367 O O   . ALA C 13  ? 1.2867 1.0171 0.6831 0.2991  -0.2802 0.0104  13  ALA C O   
16368 C CB  . ALA C 13  ? 1.2095 1.0410 0.7908 0.2999  -0.2875 0.0297  13  ALA C CB  
16374 N N   . SER C 14  ? 1.3264 1.1300 0.7660 0.3531  -0.2877 0.0749  14  SER C N   
16375 C CA  . SER C 14  ? 1.3581 1.1108 0.7407 0.3783  -0.2619 0.0941  14  SER C CA  
16376 C C   . SER C 14  ? 1.3332 1.0397 0.7582 0.4003  -0.2147 0.1150  14  SER C C   
16377 O O   . SER C 14  ? 1.3233 1.0437 0.8158 0.4027  -0.2034 0.1210  14  SER C O   
16378 C CB  . SER C 14  ? 1.4268 1.2285 0.7635 0.4050  -0.2861 0.1293  14  SER C CB  
16379 O OG  . SER C 14  ? 1.4977 1.3437 0.7835 0.3747  -0.3301 0.1054  14  SER C OG  
16385 N N   . LEU C 15  ? 1.3499 0.9987 0.7312 0.4129  -0.1836 0.1242  15  LEU C N   
16386 C CA  . LEU C 15  ? 1.3209 0.9207 0.7329 0.4244  -0.1358 0.1397  15  LEU C CA  
16387 C C   . LEU C 15  ? 1.3026 0.9196 0.7531 0.4590  -0.1222 0.1786  15  LEU C C   
16388 O O   . LEU C 15  ? 1.3459 0.9969 0.7732 0.4914  -0.1379 0.2131  15  LEU C O   
16389 C CB  . LEU C 15  ? 1.3960 0.9409 0.7518 0.4339  -0.1067 0.1486  15  LEU C CB  
16390 C CG  . LEU C 15  ? 1.4278 0.9465 0.7527 0.4070  -0.1053 0.1173  15  LEU C CG  
16391 C CD1 . LEU C 15  ? 1.4641 0.9354 0.7379 0.4224  -0.0728 0.1332  15  LEU C CD1 
16392 C CD2 . LEU C 15  ? 1.3855 0.8984 0.7679 0.3754  -0.0930 0.0940  15  LEU C CD2 
16404 N N   . GLY C 16  ? 1.2897 0.8833 0.7975 0.4521  -0.0897 0.1751  16  GLY C N   
16405 C CA  . GLY C 16  ? 1.3080 0.9033 0.8588 0.4851  -0.0638 0.2096  16  GLY C CA  
16406 C C   . GLY C 16  ? 1.2865 0.9514 0.8941 0.4901  -0.0912 0.2133  16  GLY C C   
16407 O O   . GLY C 16  ? 1.2987 0.9608 0.9561 0.5157  -0.0607 0.2386  16  GLY C O   
16411 N N   . ASP C 17  ? 1.2989 1.0227 0.9021 0.4657  -0.1425 0.1890  17  ASP C N   
16412 C CA  . ASP C 17  ? 1.3327 1.1336 0.9916 0.4668  -0.1718 0.1934  17  ASP C CA  
16413 C C   . ASP C 17  ? 1.3364 1.1179 1.0586 0.4468  -0.1434 0.1717  17  ASP C C   
16414 O O   . ASP C 17  ? 1.3353 1.0556 1.0502 0.4182  -0.1150 0.1430  17  ASP C O   
16415 C CB  . ASP C 17  ? 1.3035 1.1616 0.9356 0.4344  -0.2292 0.1652  17  ASP C CB  
16416 C CG  . ASP C 17  ? 1.3733 1.2672 0.9403 0.4497  -0.2620 0.1861  17  ASP C CG  
16417 O OD1 . ASP C 17  ? 1.4152 1.3062 0.9684 0.4923  -0.2453 0.2316  17  ASP C OD1 
16418 O OD2 . ASP C 17  ? 1.3774 1.2988 0.9024 0.4170  -0.3015 0.1568  17  ASP C OD2 
16423 N N   . ARG C 18  ? 1.3302 1.1724 1.1150 0.4609  -0.1514 0.1880  18  ARG C N   
16424 C CA  . ARG C 18  ? 1.2577 1.0937 1.1009 0.4395  -0.1294 0.1657  18  ARG C CA  
16425 C C   . ARG C 18  ? 1.2137 1.1038 1.0670 0.3974  -0.1767 0.1302  18  ARG C C   
16426 O O   . ARG C 18  ? 1.2741 1.2437 1.1353 0.4005  -0.2222 0.1404  18  ARG C O   
16427 C CB  . ARG C 18  ? 1.2372 1.1033 1.1486 0.4818  -0.1014 0.2059  18  ARG C CB  
16428 C CG  . ARG C 18  ? 1.2117 1.1091 1.1886 0.4611  -0.0964 0.1861  18  ARG C CG  
16429 C CD  . ARG C 18  ? 1.3164 1.2077 1.3576 0.5042  -0.0430 0.2223  18  ARG C CD  
16430 N NE  . ARG C 18  ? 1.4331 1.2116 1.4529 0.5057  0.0272  0.2149  18  ARG C NE  
16431 C CZ  . ARG C 18  ? 1.5206 1.2555 1.5824 0.5353  0.0931  0.2354  18  ARG C CZ  
16432 N NH1 . ARG C 18  ? 1.5324 1.3334 1.6686 0.5731  0.0984  0.2705  18  ARG C NH1 
16433 N NH2 . ARG C 18  ? 1.5850 1.2096 1.6152 0.5251  0.1575  0.2208  18  ARG C NH2 
16447 N N   . VAL C 19  ? 1.1567 1.1018 0.7406 0.2913  -0.2926 -0.0408 19  VAL C N   
16448 C CA  . VAL C 19  ? 1.0668 1.0722 0.7149 0.2591  -0.2921 -0.0683 19  VAL C CA  
16449 C C   . VAL C 19  ? 1.0378 1.0798 0.7479 0.2480  -0.2942 -0.0790 19  VAL C C   
16450 O O   . VAL C 19  ? 1.0532 1.0576 0.7695 0.2412  -0.2796 -0.0597 19  VAL C O   
16451 C CB  . VAL C 19  ? 1.0160 0.9931 0.6699 0.2247  -0.2632 -0.0581 19  VAL C CB  
16452 C CG1 . VAL C 19  ? 0.9818 1.0031 0.6895 0.1935  -0.2610 -0.0853 19  VAL C CG1 
16453 C CG2 . VAL C 19  ? 1.0382 0.9820 0.6279 0.2384  -0.2583 -0.0475 19  VAL C CG2 
16463 N N   . ILE C 20  ? 0.9983 1.1153 0.7527 0.2440  -0.3117 -0.1107 20  ILE C N   
16464 C CA  . ILE C 20  ? 0.9520 1.1149 0.7670 0.2327  -0.3118 -0.1237 20  ILE C CA  
16465 C C   . ILE C 20  ? 0.9937 1.1948 0.8588 0.1878  -0.3018 -0.1466 20  ILE C C   
16466 O O   . ILE C 20  ? 1.0511 1.2940 0.9200 0.1786  -0.3150 -0.1717 20  ILE C O   
16467 C CB  . ILE C 20  ? 0.9110 1.1374 0.7343 0.2714  -0.3400 -0.1406 20  ILE C CB  
16468 C CG1 . ILE C 20  ? 0.9922 1.1607 0.7492 0.3211  -0.3485 -0.1158 20  ILE C CG1 
16469 C CG2 . ILE C 20  ? 0.8286 1.1083 0.7163 0.2589  -0.3357 -0.1542 20  ILE C CG2 
16470 C CD1 . ILE C 20  ? 1.1096 1.3359 0.8614 0.3727  -0.3781 -0.1304 20  ILE C CD1 
16482 N N   . ILE C 21  ? 0.9641 1.1453 0.8610 0.1597  -0.2790 -0.1386 21  ILE C N   
16483 C CA  . ILE C 21  ? 0.9426 1.1405 0.8763 0.1181  -0.2646 -0.1556 21  ILE C CA  
16484 C C   . ILE C 21  ? 0.9511 1.2025 0.9387 0.1073  -0.2642 -0.1700 21  ILE C C   
16485 O O   . ILE C 21  ? 0.9459 1.1871 0.9413 0.1228  -0.2603 -0.1555 21  ILE C O   
16486 C CB  . ILE C 21  ? 0.8952 1.0288 0.8170 0.0987  -0.2375 -0.1344 21  ILE C CB  
16487 C CG1 . ILE C 21  ? 0.9091 0.9997 0.7796 0.1102  -0.2348 -0.1206 21  ILE C CG1 
16488 C CG2 . ILE C 21  ? 0.8826 1.0198 0.8307 0.0614  -0.2216 -0.1502 21  ILE C CG2 
16489 C CD1 . ILE C 21  ? 0.8953 0.9348 0.7539 0.1039  -0.2107 -0.0933 21  ILE C CD1 
16501 N N   . SER C 22  ? 0.9747 1.2807 0.9960 0.0789  -0.2667 -0.1991 22  SER C N   
16502 C CA  . SER C 22  ? 0.9859 1.3552 1.0611 0.0644  -0.2636 -0.2155 22  SER C CA  
16503 C C   . SER C 22  ? 0.9974 1.3333 1.0898 0.0228  -0.2341 -0.2133 22  SER C C   
16504 O O   . SER C 22  ? 1.0329 1.3111 1.0994 0.0015  -0.2200 -0.2086 22  SER C O   
16505 C CB  . SER C 22  ? 1.0335 1.4965 1.1390 0.0545  -0.2844 -0.2508 22  SER C CB  
16506 O OG  . SER C 22  ? 1.0456 1.5803 1.2080 0.0367  -0.2777 -0.2671 22  SER C OG  
16512 N N   . CYS C 23  ? 0.9841 1.3546 1.1150 0.0161  -0.2242 -0.2164 23  CYS C N   
16513 C CA  . CYS C 23  ? 0.9712 1.3113 1.1144 -0.0196 -0.1957 -0.2137 23  CYS C CA  
16514 C C   . CYS C 23  ? 0.8543 1.2687 1.0470 -0.0302 -0.1901 -0.2294 23  CYS C C   
16515 O O   . CYS C 23  ? 0.8602 1.3142 1.0679 0.0046  -0.2007 -0.2258 23  CYS C O   
16516 C CB  . CYS C 23  ? 1.0098 1.2734 1.1264 -0.0053 -0.1814 -0.1826 23  CYS C CB  
16517 S SG  . CYS C 23  ? 1.0102 1.2303 1.1306 -0.0377 -0.1486 -0.1757 23  CYS C SG  
16522 N N   . ARG C 24  ? 0.7467 1.1767 0.9599 -0.0774 -0.1716 -0.2466 24  ARG C N   
16523 C CA  . ARG C 24  ? 0.7194 1.2271 0.9824 -0.0955 -0.1609 -0.2627 24  ARG C CA  
16524 C C   . ARG C 24  ? 0.7843 1.2373 1.0399 -0.1305 -0.1257 -0.2538 24  ARG C C   
16525 O O   . ARG C 24  ? 0.8876 1.2654 1.1083 -0.1588 -0.1110 -0.2501 24  ARG C O   
16526 C CB  . ARG C 24  ? 0.7377 1.3392 1.0385 -0.1270 -0.1726 -0.2982 24  ARG C CB  
16527 C CG  . ARG C 24  ? 0.8013 1.5002 1.1611 -0.1506 -0.1587 -0.3167 24  ARG C CG  
16528 C CD  . ARG C 24  ? 0.8793 1.6837 1.2822 -0.1870 -0.1724 -0.3545 24  ARG C CD  
16529 N NE  . ARG C 24  ? 0.9656 1.8798 1.4016 -0.1399 -0.2063 -0.3676 24  ARG C NE  
16530 C CZ  . ARG C 24  ? 1.0264 2.0470 1.5141 -0.1173 -0.2070 -0.3757 24  ARG C CZ  
16531 N NH1 . ARG C 24  ? 1.0492 2.1505 1.5511 -0.0655 -0.2368 -0.3831 24  ARG C NH1 
16532 N NH2 . ARG C 24  ? 1.0417 2.0748 1.5557 -0.1409 -0.1740 -0.3720 24  ARG C NH2 
16546 N N   . ALA C 25  ? 0.7574 1.2445 1.0391 -0.1239 -0.1118 -0.2501 25  ALA C N   
16547 C CA  . ALA C 25  ? 0.7459 1.1867 1.0178 -0.1523 -0.0777 -0.2409 25  ALA C CA  
16548 C C   . ALA C 25  ? 0.7528 1.2737 1.0698 -0.1959 -0.0588 -0.2648 25  ALA C C   
16549 O O   . ALA C 25  ? 0.7446 1.3760 1.1117 -0.1888 -0.0730 -0.2848 25  ALA C O   
16550 C CB  . ALA C 25  ? 0.7125 1.1231 0.9719 -0.1135 -0.0727 -0.2174 25  ALA C CB  
16556 N N   . SER C 26  ? 0.7881 1.2537 1.0848 -0.2405 -0.0255 -0.2622 26  SER C N   
16557 C CA  . SER C 26  ? 0.8191 1.3508 1.1535 -0.2913 -0.0004 -0.2827 26  SER C CA  
16558 C C   . SER C 26  ? 0.8373 1.4335 1.2054 -0.2706 0.0140  -0.2778 26  SER C C   
16559 O O   . SER C 26  ? 0.8829 1.5620 1.2947 -0.3074 0.0340  -0.2960 26  SER C O   
16560 C CB  . SER C 26  ? 0.8638 1.2964 1.1509 -0.3451 0.0342  -0.2787 26  SER C CB  
16561 O OG  . SER C 26  ? 0.8946 1.2294 1.1316 -0.3211 0.0523  -0.2485 26  SER C OG  
16567 N N   . GLN C 27  ? 0.8213 1.3824 1.1688 -0.2151 0.0055  -0.2551 27  GLN C N   
16568 C CA  . GLN C 27  ? 0.8600 1.4716 1.2290 -0.1884 0.0176  -0.2507 27  GLN C CA  
16569 C C   . GLN C 27  ? 0.8446 1.4459 1.2007 -0.1205 -0.0117 -0.2372 27  GLN C C   
16570 O O   . GLN C 27  ? 0.8412 1.3776 1.1643 -0.0999 -0.0340 -0.2251 27  GLN C O   
16571 C CB  . GLN C 27  ? 0.9687 1.5049 1.3000 -0.2066 0.0552  -0.2330 27  GLN C CB  
16572 C CG  . GLN C 27  ? 1.0785 1.5923 1.4024 -0.2754 0.0899  -0.2413 27  GLN C CG  
16573 C CD  . GLN C 27  ? 1.1580 1.5774 1.4276 -0.2839 0.1252  -0.2191 27  GLN C CD  
16574 O OE1 . GLN C 27  ? 1.1272 1.5253 1.3781 -0.2410 0.1252  -0.2021 27  GLN C OE1 
16575 N NE2 . GLN C 27  ? 1.2582 1.6135 1.4944 -0.3383 0.1549  -0.2195 27  GLN C NE2 
16584 N N   . ASP C 28  ? 0.8220 1.4850 1.2004 -0.0866 -0.0092 -0.2394 28  ASP C N   
16585 C CA  . ASP C 28  ? 0.7850 1.4184 1.1378 -0.0240 -0.0316 -0.2257 28  ASP C CA  
16586 C C   . ASP C 28  ? 0.7362 1.2451 1.0295 -0.0189 -0.0264 -0.1997 28  ASP C C   
16587 O O   . ASP C 28  ? 0.7586 1.2310 1.0334 -0.0342 0.0008  -0.1910 28  ASP C O   
16588 C CB  . ASP C 28  ? 0.8150 1.5243 1.1922 0.0101  -0.0231 -0.2331 28  ASP C CB  
16589 C CG  . ASP C 28  ? 0.8560 1.5292 1.1993 0.0757  -0.0471 -0.2222 28  ASP C CG  
16590 O OD1 . ASP C 28  ? 0.8590 1.4548 1.1647 0.0897  -0.0700 -0.2090 28  ASP C OD1 
16591 O OD2 . ASP C 28  ? 0.8719 1.5912 1.2225 0.1126  -0.0413 -0.2272 28  ASP C OD2 
16596 N N   . ILE C 29  ? 0.7008 1.1489 0.9635 0.0025  -0.0520 -0.1876 29  ILE C N   
16597 C CA  . ILE C 29  ? 0.7322 1.0773 0.9451 0.0075  -0.0513 -0.1649 29  ILE C CA  
16598 C C   . ILE C 29  ? 0.7380 1.0515 0.9240 0.0540  -0.0690 -0.1543 29  ILE C C   
16599 O O   . ILE C 29  ? 0.7568 0.9946 0.9051 0.0596  -0.0754 -0.1374 29  ILE C O   
16600 C CB  . ILE C 29  ? 0.7201 1.0143 0.9149 -0.0104 -0.0615 -0.1577 29  ILE C CB  
16601 C CG1 . ILE C 29  ? 0.6803 1.0030 0.8844 0.0108  -0.0910 -0.1637 29  ILE C CG1 
16602 C CG2 . ILE C 29  ? 0.7474 1.0435 0.9507 -0.0586 -0.0398 -0.1668 29  ILE C CG2 
16603 C CD1 . ILE C 29  ? 0.6576 0.9307 0.8397 -0.0019 -0.1000 -0.1559 29  ILE C CD1 
16615 N N   . SER C 30  ? 0.7448 1.1147 0.9468 0.0876  -0.0771 -0.1650 30  SER C N   
16616 C CA  . SER C 30  ? 0.7954 1.1257 0.9620 0.1318  -0.0890 -0.1573 30  SER C CA  
16617 C C   . SER C 30  ? 0.8028 1.0541 0.9295 0.1425  -0.1123 -0.1419 30  SER C C   
16618 O O   . SER C 30  ? 0.8410 1.0224 0.9279 0.1515  -0.1156 -0.1297 30  SER C O   
16619 C CB  . SER C 30  ? 0.8377 1.1349 0.9823 0.1303  -0.0676 -0.1514 30  SER C CB  
16620 O OG  . SER C 30  ? 0.8386 1.2076 1.0183 0.1149  -0.0408 -0.1638 30  SER C OG  
16626 N N   . ASN C 31  ? 0.7852 1.0504 0.9217 0.1391  -0.1282 -0.1434 31  ASN C N   
16627 C CA  . ASN C 31  ? 0.7832 0.9856 0.8844 0.1495  -0.1485 -0.1296 31  ASN C CA  
16628 C C   . ASN C 31  ? 0.7444 0.8802 0.8248 0.1215  -0.1429 -0.1129 31  ASN C C   
16629 O O   . ASN C 31  ? 0.7285 0.8145 0.7812 0.1251  -0.1562 -0.1002 31  ASN C O   
16630 C CB  . ASN C 31  ? 0.8486 1.0112 0.9096 0.1926  -0.1633 -0.1252 31  ASN C CB  
16631 C CG  . ASN C 31  ? 0.9308 1.1486 0.9996 0.2323  -0.1773 -0.1377 31  ASN C CG  
16632 O OD1 . ASN C 31  ? 0.9712 1.2498 1.0612 0.2543  -0.1710 -0.1516 31  ASN C OD1 
16633 N ND2 . ASN C 31  ? 0.9828 1.1837 1.0327 0.2446  -0.1959 -0.1326 31  ASN C ND2 
16640 N N   . TYR C 32  ? 0.7322 0.8669 0.8228 0.0950  -0.1229 -0.1122 32  TYR C N   
16641 C CA  . TYR C 32  ? 0.7376 0.8192 0.8092 0.0746  -0.1185 -0.0973 32  TYR C CA  
16642 C C   . TYR C 32  ? 0.7095 0.7994 0.7933 0.0531  -0.1172 -0.0975 32  TYR C C   
16643 O O   . TYR C 32  ? 0.6749 0.7662 0.7656 0.0294  -0.1003 -0.0999 32  TYR C O   
16644 C CB  . TYR C 32  ? 0.7629 0.8301 0.8274 0.0633  -0.0985 -0.0950 32  TYR C CB  
16645 C CG  . TYR C 32  ? 0.8580 0.8986 0.8971 0.0846  -0.1024 -0.0924 32  TYR C CG  
16646 C CD1 . TYR C 32  ? 0.9094 0.8977 0.9180 0.0891  -0.1167 -0.0808 32  TYR C CD1 
16647 C CD2 . TYR C 32  ? 0.9045 0.9746 0.9487 0.0988  -0.0914 -0.1031 32  TYR C CD2 
16648 C CE1 . TYR C 32  ? 0.9869 0.9442 0.9659 0.1055  -0.1220 -0.0813 32  TYR C CE1 
16649 C CE2 . TYR C 32  ? 0.9862 1.0248 0.9989 0.1209  -0.0950 -0.1023 32  TYR C CE2 
16650 C CZ  . TYR C 32  ? 1.0374 1.0151 1.0150 0.1234  -0.1114 -0.0921 32  TYR C CZ  
16651 O OH  . TYR C 32  ? 1.1213 1.0613 1.0616 0.1423  -0.1167 -0.0940 32  TYR C OH  
16661 N N   . LEU C 33  ? 0.7198 0.8070 0.7979 0.0633  -0.1347 -0.0947 33  LEU C N   
16662 C CA  . LEU C 33  ? 0.7312 0.8211 0.8126 0.0485  -0.1360 -0.0949 33  LEU C CA  
16663 C C   . LEU C 33  ? 0.7189 0.7677 0.7747 0.0558  -0.1474 -0.0781 33  LEU C C   
16664 O O   . LEU C 33  ? 0.7233 0.7570 0.7624 0.0750  -0.1611 -0.0727 33  LEU C O   
16665 C CB  . LEU C 33  ? 0.7560 0.9018 0.8590 0.0520  -0.1448 -0.1127 33  LEU C CB  
16666 C CG  . LEU C 33  ? 0.7677 0.9145 0.8695 0.0338  -0.1453 -0.1171 33  LEU C CG  
16667 C CD1 . LEU C 33  ? 0.8637 1.0735 0.9956 0.0187  -0.1450 -0.1414 33  LEU C CD1 
16668 C CD2 . LEU C 33  ? 0.7068 0.8319 0.7841 0.0519  -0.1625 -0.1067 33  LEU C CD2 
16680 N N   . SER C 34  ? 0.7652 0.7942 0.8143 0.0409  -0.1398 -0.0699 34  SER C N   
16681 C CA  . SER C 34  ? 0.7826 0.7835 0.8129 0.0432  -0.1455 -0.0536 34  SER C CA  
16682 C C   . SER C 34  ? 0.7523 0.7595 0.7782 0.0393  -0.1451 -0.0554 34  SER C C   
16683 O O   . SER C 34  ? 0.7684 0.7912 0.8028 0.0292  -0.1383 -0.0688 34  SER C O   
16684 C CB  . SER C 34  ? 0.8043 0.7833 0.8291 0.0353  -0.1368 -0.0411 34  SER C CB  
16685 O OG  . SER C 34  ? 0.8345 0.8057 0.8584 0.0386  -0.1376 -0.0417 34  SER C OG  
16691 N N   . TRP C 35  ? 0.7539 0.7450 0.7620 0.0450  -0.1510 -0.0424 35  TRP C N   
16692 C CA  . TRP C 35  ? 0.7693 0.7618 0.7652 0.0452  -0.1501 -0.0421 35  TRP C CA  
16693 C C   . TRP C 35  ? 0.7418 0.7185 0.7276 0.0409  -0.1400 -0.0247 35  TRP C C   
16694 O O   . TRP C 35  ? 0.7247 0.6914 0.7079 0.0390  -0.1413 -0.0104 35  TRP C O   
16695 C CB  . TRP C 35  ? 0.8004 0.7946 0.7787 0.0608  -0.1652 -0.0425 35  TRP C CB  
16696 C CG  . TRP C 35  ? 0.8454 0.8732 0.8366 0.0698  -0.1766 -0.0626 35  TRP C CG  
16697 C CD1 . TRP C 35  ? 0.8787 0.9182 0.8764 0.0846  -0.1861 -0.0677 35  TRP C CD1 
16698 C CD2 . TRP C 35  ? 0.8787 0.9393 0.8787 0.0647  -0.1800 -0.0823 35  TRP C CD2 
16699 N NE1 . TRP C 35  ? 0.9176 1.0069 0.9340 0.0910  -0.1949 -0.0887 35  TRP C NE1 
16700 C CE2 . TRP C 35  ? 0.8883 0.9923 0.9077 0.0754  -0.1923 -0.0989 35  TRP C CE2 
16701 C CE3 . TRP C 35  ? 0.8990 0.9566 0.8897 0.0524  -0.1742 -0.0891 35  TRP C CE3 
16702 C CZ2 . TRP C 35  ? 0.8699 1.0241 0.9066 0.0691  -0.2001 -0.1228 35  TRP C CZ2 
16703 C CZ3 . TRP C 35  ? 0.9209 1.0143 0.9209 0.0448  -0.1822 -0.1133 35  TRP C CZ3 
16704 C CH2 . TRP C 35  ? 0.9091 1.0552 0.9354 0.0507  -0.1956 -0.1303 35  TRP C CH2 
16715 N N   . TYR C 36  ? 0.7500 0.7264 0.7289 0.0392  -0.1297 -0.0275 36  TYR C N   
16716 C CA  . TYR C 36  ? 0.7426 0.7150 0.7135 0.0412  -0.1179 -0.0129 36  TYR C CA  
16717 C C   . TYR C 36  ? 0.8153 0.7850 0.7632 0.0485  -0.1149 -0.0124 36  TYR C C   
16718 O O   . TYR C 36  ? 0.8778 0.8437 0.8143 0.0494  -0.1188 -0.0283 36  TYR C O   
16719 C CB  . TYR C 36  ? 0.7403 0.7057 0.7133 0.0411  -0.1047 -0.0153 36  TYR C CB  
16720 C CG  . TYR C 36  ? 0.7655 0.7317 0.7544 0.0365  -0.1062 -0.0141 36  TYR C CG  
16721 C CD1 . TYR C 36  ? 0.7687 0.7270 0.7619 0.0298  -0.1043 -0.0278 36  TYR C CD1 
16722 C CD2 . TYR C 36  ? 0.8107 0.7882 0.8090 0.0369  -0.1089 -0.0004 36  TYR C CD2 
16723 C CE1 . TYR C 36  ? 0.7782 0.7347 0.7797 0.0282  -0.1039 -0.0263 36  TYR C CE1 
16724 C CE2 . TYR C 36  ? 0.8354 0.8110 0.8419 0.0344  -0.1121 -0.0009 36  TYR C CE2 
16725 C CZ  . TYR C 36  ? 0.8075 0.7701 0.8131 0.0323  -0.1090 -0.0131 36  TYR C CZ  
16726 O OH  . TYR C 36  ? 0.8106 0.7689 0.8185 0.0322  -0.1104 -0.0131 36  TYR C OH  
16736 N N   . GLN C 37  ? 0.8298 0.8051 0.7705 0.0521  -0.1076 0.0049  37  GLN C N   
16737 C CA  . GLN C 37  ? 0.8623 0.8355 0.7769 0.0618  -0.1002 0.0083  37  GLN C CA  
16738 C C   . GLN C 37  ? 0.8738 0.8544 0.7855 0.0713  -0.0825 0.0135  37  GLN C C   
16739 O O   . GLN C 37  ? 0.8832 0.8864 0.8147 0.0703  -0.0759 0.0264  37  GLN C O   
16740 C CB  . GLN C 37  ? 0.8687 0.8433 0.7714 0.0600  -0.1011 0.0255  37  GLN C CB  
16741 C CG  . GLN C 37  ? 0.9088 0.8958 0.7958 0.0666  -0.0834 0.0393  37  GLN C CG  
16742 C CD  . GLN C 37  ? 0.9531 0.9339 0.8209 0.0602  -0.0807 0.0572  37  GLN C CD  
16743 O OE1 . GLN C 37  ? 0.9787 0.9799 0.8591 0.0472  -0.0685 0.0743  37  GLN C OE1 
16744 N NE2 . GLN C 37  ? 0.9778 0.9310 0.8122 0.0687  -0.0916 0.0531  37  GLN C NE2 
16753 N N   . GLN C 38  ? 0.8498 0.8118 0.7337 0.0823  -0.0758 0.0022  38  GLN C N   
16754 C CA  . GLN C 38  ? 0.8540 0.8142 0.7221 0.1003  -0.0578 0.0063  38  GLN C CA  
16755 C C   . GLN C 38  ? 0.8585 0.8179 0.6943 0.1144  -0.0492 0.0097  38  GLN C C   
16756 O O   . GLN C 38  ? 0.8664 0.7997 0.6725 0.1147  -0.0558 -0.0051 38  GLN C O   
16757 C CB  . GLN C 38  ? 0.8711 0.7919 0.7197 0.1036  -0.0532 -0.0105 38  GLN C CB  
16758 C CG  . GLN C 38  ? 0.9007 0.8063 0.7191 0.1305  -0.0343 -0.0067 38  GLN C CG  
16759 C CD  . GLN C 38  ? 0.9267 0.7840 0.7227 0.1341  -0.0272 -0.0172 38  GLN C CD  
16760 O OE1 . GLN C 38  ? 0.9838 0.7996 0.7618 0.1159  -0.0310 -0.0360 38  GLN C OE1 
16761 N NE2 . GLN C 38  ? 0.9213 0.7850 0.7161 0.1571  -0.0165 -0.0051 38  GLN C NE2 
16770 N N   . LYS C 39  ? 0.8738 0.8669 0.7155 0.1255  -0.0345 0.0281  39  LYS C N   
16771 C CA  . LYS C 39  ? 0.9666 0.9634 0.7760 0.1414  -0.0214 0.0338  39  LYS C CA  
16772 C C   . LYS C 39  ? 1.0098 0.9854 0.7844 0.1702  -0.0063 0.0251  39  LYS C C   
16773 O O   . LYS C 39  ? 1.0121 0.9780 0.7914 0.1798  -0.0026 0.0211  39  LYS C O   
16774 C CB  . LYS C 39  ? 0.9897 1.0391 0.8230 0.1365  -0.0090 0.0578  39  LYS C CB  
16775 C CG  . LYS C 39  ? 1.0107 1.0577 0.8521 0.1106  -0.0202 0.0670  39  LYS C CG  
16776 C CD  . LYS C 39  ? 1.0312 1.1260 0.9016 0.0937  -0.0078 0.0893  39  LYS C CD  
16777 C CE  . LYS C 39  ? 1.0503 1.1217 0.9080 0.0699  -0.0145 0.1000  39  LYS C CE  
16778 N NZ  . LYS C 39  ? 1.0917 1.1332 0.8975 0.0827  -0.0087 0.1028  39  LYS C NZ  
16792 N N   . PRO C 40  ? 1.0763 1.0361 0.8066 0.1875  0.0033  0.0220  40  PRO C N   
16793 C CA  . PRO C 40  ? 1.1718 1.0931 0.8545 0.2168  0.0166  0.0098  40  PRO C CA  
16794 C C   . PRO C 40  ? 1.1966 1.1444 0.8904 0.2446  0.0345  0.0209  40  PRO C C   
16795 O O   . PRO C 40  ? 1.2706 1.1702 0.9233 0.2689  0.0426  0.0095  40  PRO C O   
16796 C CB  . PRO C 40  ? 1.2253 1.1415 0.8630 0.2328  0.0261  0.0106  40  PRO C CB  
16797 C CG  . PRO C 40  ? 1.1913 1.1173 0.8409 0.2070  0.0095  0.0141  40  PRO C CG  
16798 C CD  . PRO C 40  ? 1.1069 1.0729 0.8182 0.1831  0.0023  0.0289  40  PRO C CD  
16806 N N   . ASP C 41  ? 1.1480 1.1694 0.8925 0.2420  0.0402  0.0418  41  ASP C N   
16807 C CA  . ASP C 41  ? 1.1296 1.1939 0.8894 0.2724  0.0546  0.0516  41  ASP C CA  
16808 C C   . ASP C 41  ? 1.1113 1.1632 0.8919 0.2686  0.0431  0.0479  41  ASP C C   
16809 O O   . ASP C 41  ? 1.0937 1.1847 0.8878 0.2961  0.0509  0.0562  41  ASP C O   
16810 C CB  . ASP C 41  ? 1.0671 1.2284 0.8760 0.2673  0.0656  0.0734  41  ASP C CB  
16811 C CG  . ASP C 41  ? 0.9923 1.1846 0.8550 0.2221  0.0490  0.0814  41  ASP C CG  
16812 O OD1 . ASP C 41  ? 0.9730 1.1145 0.8342 0.1995  0.0293  0.0706  41  ASP C OD1 
16813 O OD2 . ASP C 41  ? 0.9580 1.2259 0.8630 0.2085  0.0565  0.0975  41  ASP C OD2 
16818 N N   . GLY C 42  ? 1.0951 1.0984 0.8773 0.2381  0.0252  0.0359  42  GLY C N   
16819 C CA  . GLY C 42  ? 1.0707 1.0580 0.8682 0.2317  0.0161  0.0328  42  GLY C CA  
16820 C C   . GLY C 42  ? 0.9602 0.9991 0.8168 0.2018  0.0013  0.0424  42  GLY C C   
16821 O O   . GLY C 42  ? 0.9572 0.9764 0.8243 0.1903  -0.0089 0.0377  42  GLY C O   
16825 N N   . THR C 43  ? 0.8910 0.9892 0.7802 0.1879  0.0017  0.0553  43  THR C N   
16826 C CA  . THR C 43  ? 0.8722 1.0087 0.8086 0.1564  -0.0119 0.0632  43  THR C CA  
16827 C C   . THR C 43  ? 0.8627 0.9486 0.7967 0.1302  -0.0295 0.0515  43  THR C C   
16828 O O   . THR C 43  ? 0.9250 0.9713 0.8335 0.1245  -0.0327 0.0420  43  THR C O   
16829 C CB  . THR C 43  ? 0.8934 1.0807 0.8503 0.1392  -0.0054 0.0778  43  THR C CB  
16830 O OG1 . THR C 43  ? 0.9028 1.1645 0.8825 0.1570  0.0094  0.0894  43  THR C OG1 
16831 C CG2 . THR C 43  ? 0.9200 1.1129 0.9060 0.1000  -0.0208 0.0822  43  THR C CG2 
16839 N N   . VAL C 44  ? 0.8035 0.8968 0.7639 0.1164  -0.0415 0.0514  44  VAL C N   
16840 C CA  . VAL C 44  ? 0.8124 0.8685 0.7749 0.0952  -0.0567 0.0410  44  VAL C CA  
16841 C C   . VAL C 44  ? 0.7922 0.8748 0.7852 0.0707  -0.0685 0.0492  44  VAL C C   
16842 O O   . VAL C 44  ? 0.7434 0.8679 0.7607 0.0683  -0.0690 0.0577  44  VAL C O   
16843 C CB  . VAL C 44  ? 0.8336 0.8570 0.7863 0.1030  -0.0575 0.0308  44  VAL C CB  
16844 C CG1 . VAL C 44  ? 0.7995 0.7966 0.7589 0.0813  -0.0704 0.0197  44  VAL C CG1 
16845 C CG2 . VAL C 44  ? 0.8718 0.8538 0.7836 0.1239  -0.0439 0.0222  44  VAL C CG2 
16855 N N   . LYS C 45  ? 0.8029 0.8598 0.7905 0.0540  -0.0789 0.0455  45  LYS C N   
16856 C CA  . LYS C 45  ? 0.8502 0.9101 0.8520 0.0317  -0.0901 0.0515  45  LYS C CA  
16857 C C   . LYS C 45  ? 0.7888 0.8122 0.7850 0.0277  -0.1041 0.0390  45  LYS C C   
16858 O O   . LYS C 45  ? 0.7778 0.7801 0.7592 0.0358  -0.1060 0.0278  45  LYS C O   
16859 C CB  . LYS C 45  ? 0.9957 1.0561 0.9859 0.0194  -0.0861 0.0638  45  LYS C CB  
16860 C CG  . LYS C 45  ? 1.1382 1.2462 1.1389 0.0187  -0.0694 0.0777  45  LYS C CG  
16861 C CD  . LYS C 45  ? 1.3023 1.4007 1.2838 0.0028  -0.0621 0.0910  45  LYS C CD  
16862 C CE  . LYS C 45  ? 1.3911 1.5470 1.3868 -0.0012 -0.0415 0.1053  45  LYS C CE  
16863 N NZ  . LYS C 45  ? 1.4715 1.6114 1.4419 -0.0200 -0.0303 0.1203  45  LYS C NZ  
16877 N N   . LEU C 46  ? 0.7504 0.7708 0.7579 0.0153  -0.1142 0.0394  46  LEU C N   
16878 C CA  . LEU C 46  ? 0.7285 0.7183 0.7290 0.0143  -0.1264 0.0289  46  LEU C CA  
16879 C C   . LEU C 46  ? 0.7428 0.7066 0.7225 0.0087  -0.1333 0.0342  46  LEU C C   
16880 O O   . LEU C 46  ? 0.7125 0.6726 0.6866 -0.0074 -0.1322 0.0468  46  LEU C O   
16881 C CB  . LEU C 46  ? 0.7243 0.7138 0.7360 0.0079  -0.1336 0.0261  46  LEU C CB  
16882 C CG  . LEU C 46  ? 0.7163 0.6753 0.7178 0.0094  -0.1449 0.0165  46  LEU C CG  
16883 C CD1 . LEU C 46  ? 0.6866 0.6448 0.6894 0.0226  -0.1423 0.0026  46  LEU C CD1 
16884 C CD2 . LEU C 46  ? 0.7149 0.6695 0.7198 0.0029  -0.1518 0.0143  46  LEU C CD2 
16896 N N   . LEU C 47  ? 0.7717 0.7176 0.7372 0.0216  -0.1403 0.0244  47  LEU C N   
16897 C CA  . LEU C 47  ? 0.7888 0.7028 0.7244 0.0261  -0.1487 0.0288  47  LEU C CA  
16898 C C   . LEU C 47  ? 0.8015 0.6913 0.7296 0.0336  -0.1616 0.0204  47  LEU C C   
16899 O O   . LEU C 47  ? 0.7918 0.6433 0.6958 0.0275  -0.1665 0.0284  47  LEU C O   
16900 C CB  . LEU C 47  ? 0.8374 0.7549 0.7568 0.0429  -0.1501 0.0232  47  LEU C CB  
16901 C CG  . LEU C 47  ? 0.9056 0.8429 0.8249 0.0425  -0.1371 0.0271  47  LEU C CG  
16902 C CD1 . LEU C 47  ? 0.9430 0.8832 0.8460 0.0589  -0.1436 0.0138  47  LEU C CD1 
16903 C CD2 . LEU C 47  ? 0.9218 0.8513 0.8240 0.0321  -0.1263 0.0478  47  LEU C CD2 
16915 N N   . ILE C 48  ? 0.8016 0.7110 0.7469 0.0459  -0.1656 0.0039  48  ILE C N   
16916 C CA  . ILE C 48  ? 0.8290 0.7266 0.7682 0.0605  -0.1761 -0.0061 48  ILE C CA  
16917 C C   . ILE C 48  ? 0.8169 0.7353 0.7836 0.0556  -0.1714 -0.0164 48  ILE C C   
16918 O O   . ILE C 48  ? 0.7293 0.6751 0.7180 0.0487  -0.1618 -0.0219 48  ILE C O   
16919 C CB  . ILE C 48  ? 0.8413 0.7553 0.7742 0.0841  -0.1854 -0.0178 48  ILE C CB  
16920 C CG1 . ILE C 48  ? 0.8877 0.7758 0.7837 0.0933  -0.1899 -0.0063 48  ILE C CG1 
16921 C CG2 . ILE C 48  ? 0.8973 0.8094 0.8260 0.1055  -0.1951 -0.0285 48  ILE C CG2 
16922 C CD1 . ILE C 48  ? 0.8917 0.7192 0.7431 0.0994  -0.1951 0.0072  48  ILE C CD1 
16934 N N   . PHE C 49  ? 0.8864 0.7833 0.8434 0.0602  -0.1768 -0.0187 49  PHE C N   
16935 C CA  . PHE C 49  ? 0.8681 0.7806 0.8427 0.0607  -0.1720 -0.0289 49  PHE C CA  
16936 C C   . PHE C 49  ? 0.8861 0.7889 0.8473 0.0831  -0.1796 -0.0389 49  PHE C C   
16937 O O   . PHE C 49  ? 0.9362 0.8035 0.8656 0.0973  -0.1900 -0.0353 49  PHE C O   
16938 C CB  . PHE C 49  ? 0.8281 0.7274 0.8021 0.0442  -0.1693 -0.0214 49  PHE C CB  
16939 C CG  . PHE C 49  ? 0.8043 0.6603 0.7494 0.0388  -0.1798 -0.0154 49  PHE C CG  
16940 C CD1 . PHE C 49  ? 0.7868 0.6229 0.7176 0.0236  -0.1824 -0.0027 49  PHE C CD1 
16941 C CD2 . PHE C 49  ? 0.8165 0.6476 0.7443 0.0464  -0.1853 -0.0231 49  PHE C CD2 
16942 C CE1 . PHE C 49  ? 0.8533 0.6413 0.7525 0.0110  -0.1904 0.0018  49  PHE C CE1 
16943 C CE2 . PHE C 49  ? 0.8275 0.6074 0.7205 0.0380  -0.1953 -0.0199 49  PHE C CE2 
16944 C CZ  . PHE C 49  ? 0.8840 0.6403 0.7625 0.0176  -0.1980 -0.0077 49  PHE C CZ  
16954 N N   . TYR C 50  ? 0.8514 0.7833 0.8324 0.0880  -0.1723 -0.0510 50  TYR C N   
16955 C CA  . TYR C 50  ? 0.8479 0.7886 0.8235 0.1135  -0.1758 -0.0630 50  TYR C CA  
16956 C C   . TYR C 50  ? 0.8600 0.8158 0.8294 0.1377  -0.1871 -0.0677 50  TYR C C   
16957 O O   . TYR C 50  ? 0.9014 0.8378 0.8439 0.1676  -0.1965 -0.0708 50  TYR C O   
16958 C CB  . TYR C 50  ? 0.8518 0.7398 0.7916 0.1221  -0.1816 -0.0602 50  TYR C CB  
16959 C CG  . TYR C 50  ? 0.8593 0.7620 0.7966 0.1478  -0.1784 -0.0736 50  TYR C CG  
16960 C CD1 . TYR C 50  ? 0.8277 0.7758 0.7953 0.1415  -0.1625 -0.0821 50  TYR C CD1 
16961 C CD2 . TYR C 50  ? 0.8875 0.7548 0.7865 0.1801  -0.1888 -0.0772 50  TYR C CD2 
16962 C CE1 . TYR C 50  ? 0.8456 0.8149 0.8127 0.1646  -0.1559 -0.0940 50  TYR C CE1 
16963 C CE2 . TYR C 50  ? 0.9064 0.7926 0.8023 0.2090  -0.1841 -0.0899 50  TYR C CE2 
16964 C CZ  . TYR C 50  ? 0.8709 0.8138 0.8046 0.2002  -0.1670 -0.0984 50  TYR C CZ  
16965 O OH  . TYR C 50  ? 0.8605 0.8297 0.7928 0.2285  -0.1588 -0.1107 50  TYR C OH  
16975 N N   . THR C 51  ? 0.8133 0.7997 0.8011 0.1281  -0.1870 -0.0684 51  THR C N   
16976 C CA  . THR C 51  ? 0.8125 0.8340 0.8030 0.1495  -0.1980 -0.0772 51  THR C CA  
16977 C C   . THR C 51  ? 0.8239 0.7964 0.7669 0.1729  -0.2126 -0.0657 51  THR C C   
16978 O O   . THR C 51  ? 0.8748 0.8692 0.8123 0.1890  -0.2227 -0.0692 51  THR C O   
16979 C CB  . THR C 51  ? 0.8452 0.9222 0.8578 0.1730  -0.1990 -0.0955 51  THR C CB  
16980 O OG1 . THR C 51  ? 0.9074 1.0306 0.9617 0.1472  -0.1820 -0.1061 51  THR C OG1 
16981 C CG2 . THR C 51  ? 0.8188 0.9453 0.8363 0.2004  -0.2144 -0.1068 51  THR C CG2 
16989 N N   . SER C 52  ? 0.8490 0.7511 0.7521 0.1729  -0.2137 -0.0523 52  SER C N   
16990 C CA  . SER C 52  ? 0.9443 0.7850 0.7920 0.1906  -0.2238 -0.0394 52  SER C CA  
16991 C C   . SER C 52  ? 1.0189 0.7854 0.8322 0.1637  -0.2191 -0.0215 52  SER C C   
16992 O O   . SER C 52  ? 1.1127 0.8148 0.8719 0.1726  -0.2239 -0.0092 52  SER C O   
16993 C CB  . SER C 52  ? 0.9722 0.7968 0.7858 0.2382  -0.2354 -0.0469 52  SER C CB  
16994 O OG  . SER C 52  ? 1.0101 0.8076 0.8146 0.2417  -0.2317 -0.0513 52  SER C OG  
17000 N N   . LYS C 53  ? 1.0035 0.7769 0.8431 0.1310  -0.2099 -0.0198 53  LYS C N   
17001 C CA  . LYS C 53  ? 1.0154 0.7311 0.8281 0.1037  -0.2080 -0.0074 53  LYS C CA  
17002 C C   . LYS C 53  ? 0.9305 0.6606 0.7585 0.0727  -0.1995 0.0062  53  LYS C C   
17003 O O   . LYS C 53  ? 0.8185 0.6045 0.6906 0.0611  -0.1920 0.0034  53  LYS C O   
17004 C CB  . LYS C 53  ? 1.0211 0.7415 0.8498 0.0915  -0.2061 -0.0154 53  LYS C CB  
17005 C CG  . LYS C 53  ? 1.0374 0.7582 0.8577 0.1245  -0.2101 -0.0304 53  LYS C CG  
17006 C CD  . LYS C 53  ? 1.1234 0.7733 0.8809 0.1539  -0.2199 -0.0291 53  LYS C CD  
17007 C CE  . LYS C 53  ? 1.1754 0.8312 0.9236 0.1927  -0.2226 -0.0446 53  LYS C CE  
17008 N NZ  . LYS C 53  ? 1.3070 0.8838 0.9834 0.2290  -0.2320 -0.0434 53  LYS C NZ  
17022 N N   . LEU C 54  ? 0.9968 0.6731 0.7836 0.0604  -0.1988 0.0212  54  LEU C N   
17023 C CA  . LEU C 54  ? 1.0025 0.6959 0.8021 0.0311  -0.1880 0.0353  54  LEU C CA  
17024 C C   . LEU C 54  ? 0.9537 0.6693 0.7836 -0.0039 -0.1832 0.0367  54  LEU C C   
17025 O O   . LEU C 54  ? 0.9618 0.6380 0.7720 -0.0192 -0.1886 0.0350  54  LEU C O   
17026 C CB  . LEU C 54  ? 1.1240 0.7512 0.8665 0.0246  -0.1851 0.0521  54  LEU C CB  
17027 C CG  . LEU C 54  ? 1.2382 0.8541 0.9492 0.0556  -0.1869 0.0570  54  LEU C CG  
17028 C CD1 . LEU C 54  ? 1.3131 0.8521 0.9599 0.0422  -0.1794 0.0775  54  LEU C CD1 
17029 C CD2 . LEU C 54  ? 1.2271 0.9155 0.9809 0.0577  -0.1809 0.0543  54  LEU C CD2 
17041 N N   . HIS C 55  ? 0.8909 0.6687 0.7643 -0.0140 -0.1741 0.0386  55  HIS C N   
17042 C CA  . HIS C 55  ? 0.8938 0.7037 0.7957 -0.0425 -0.1703 0.0416  55  HIS C CA  
17043 C C   . HIS C 55  ? 0.9222 0.7121 0.8063 -0.0762 -0.1643 0.0566  55  HIS C C   
17044 O O   . HIS C 55  ? 0.9388 0.7030 0.7956 -0.0762 -0.1569 0.0680  55  HIS C O   
17045 C CB  . HIS C 55  ? 0.8900 0.7666 0.8346 -0.0362 -0.1611 0.0405  55  HIS C CB  
17046 C CG  . HIS C 55  ? 0.9220 0.8417 0.8959 -0.0556 -0.1591 0.0430  55  HIS C CG  
17047 N ND1 . HIS C 55  ? 0.9273 0.8981 0.9254 -0.0623 -0.1476 0.0522  55  HIS C ND1 
17048 C CD2 . HIS C 55  ? 0.9372 0.8611 0.9184 -0.0662 -0.1683 0.0366  55  HIS C CD2 
17049 C CE1 . HIS C 55  ? 0.9331 0.9443 0.9557 -0.0748 -0.1508 0.0513  55  HIS C CE1 
17050 N NE2 . HIS C 55  ? 0.9349 0.9173 0.9468 -0.0787 -0.1643 0.0417  55  HIS C NE2 
17058 N N   . SER C 56  ? 0.9199 0.7233 0.8179 -0.1068 -0.1673 0.0559  56  SER C N   
17059 C CA  . SER C 56  ? 1.0000 0.7918 0.8862 -0.1487 -0.1605 0.0679  56  SER C CA  
17060 C C   . SER C 56  ? 0.9736 0.8170 0.8816 -0.1537 -0.1424 0.0821  56  SER C C   
17061 O O   . SER C 56  ? 0.9217 0.8398 0.8747 -0.1425 -0.1373 0.0806  56  SER C O   
17062 C CB  . SER C 56  ? 1.0986 0.9225 1.0097 -0.1815 -0.1688 0.0608  56  SER C CB  
17063 O OG  . SER C 56  ? 1.2144 1.0481 1.1263 -0.2292 -0.1602 0.0711  56  SER C OG  
17069 N N   . GLY C 57  ? 1.0186 0.8156 0.8871 -0.1673 -0.1314 0.0964  57  GLY C N   
17070 C CA  . GLY C 57  ? 1.0411 0.8803 0.9215 -0.1778 -0.1111 0.1117  57  GLY C CA  
17071 C C   . GLY C 57  ? 1.0588 0.8805 0.9137 -0.1410 -0.1046 0.1171  57  GLY C C   
17072 O O   . GLY C 57  ? 1.1289 0.9539 0.9680 -0.1499 -0.0867 0.1325  57  GLY C O   
17076 N N   . VAL C 58  ? 1.0083 0.8159 0.8584 -0.1016 -0.1181 0.1042  58  VAL C N   
17077 C CA  . VAL C 58  ? 1.0381 0.8399 0.8679 -0.0677 -0.1157 0.1050  58  VAL C CA  
17078 C C   . VAL C 58  ? 1.0961 0.8145 0.8574 -0.0612 -0.1175 0.1151  58  VAL C C   
17079 O O   . VAL C 58  ? 1.1331 0.7901 0.8625 -0.0673 -0.1269 0.1138  58  VAL C O   
17080 C CB  . VAL C 58  ? 1.0738 0.8998 0.9272 -0.0341 -0.1290 0.0856  58  VAL C CB  
17081 C CG1 . VAL C 58  ? 1.0181 0.9109 0.9253 -0.0383 -0.1247 0.0784  58  VAL C CG1 
17082 C CG2 . VAL C 58  ? 1.1341 0.9170 0.9711 -0.0225 -0.1462 0.0743  58  VAL C CG2 
17092 N N   . PRO C 59  ? 1.1489 0.8558 0.8776 -0.0457 -0.1086 0.1253  59  PRO C N   
17093 C CA  . PRO C 59  ? 1.2689 0.8892 0.9214 -0.0374 -0.1084 0.1385  59  PRO C CA  
17094 C C   . PRO C 59  ? 1.2537 0.8331 0.8762 0.0045  -0.1313 0.1254  59  PRO C C   
17095 O O   . PRO C 59  ? 1.1913 0.8186 0.8538 0.0282  -0.1453 0.1059  59  PRO C O   
17096 C CB  . PRO C 59  ? 1.3250 0.9584 0.9551 -0.0267 -0.0932 0.1509  59  PRO C CB  
17097 C CG  . PRO C 59  ? 1.2164 0.9349 0.9056 -0.0124 -0.0945 0.1362  59  PRO C CG  
17098 C CD  . PRO C 59  ? 1.1168 0.8828 0.8684 -0.0349 -0.0967 0.1264  59  PRO C CD  
17106 N N   . SER C 60  ? 1.3298 0.8176 0.8765 0.0140  -0.1332 0.1370  60  SER C N   
17107 C CA  . SER C 60  ? 1.3511 0.7965 0.8607 0.0595  -0.1545 0.1262  60  SER C CA  
17108 C C   . SER C 60  ? 1.3242 0.8133 0.8366 0.1060  -0.1673 0.1159  60  SER C C   
17109 O O   . SER C 60  ? 1.2911 0.7843 0.7989 0.1455  -0.1871 0.1008  60  SER C O   
17110 C CB  . SER C 60  ? 1.4934 0.8184 0.9070 0.0635  -0.1517 0.1435  60  SER C CB  
17111 O OG  . SER C 60  ? 1.6027 0.8917 0.9604 0.0682  -0.1385 0.1638  60  SER C OG  
17117 N N   . ARG C 61  ? 1.3309 0.8562 0.8495 0.1025  -0.1567 0.1223  61  ARG C N   
17118 C CA  . ARG C 61  ? 1.3171 0.8825 0.8338 0.1427  -0.1707 0.1099  61  ARG C CA  
17119 C C   . ARG C 61  ? 1.2266 0.8659 0.8098 0.1559  -0.1879 0.0819  61  ARG C C   
17120 O O   . ARG C 61  ? 1.2629 0.9232 0.8394 0.1938  -0.2079 0.0666  61  ARG C O   
17121 C CB  . ARG C 61  ? 1.3128 0.9118 0.8343 0.1311  -0.1547 0.1175  61  ARG C CB  
17122 C CG  . ARG C 61  ? 1.4073 0.9485 0.8751 0.1076  -0.1300 0.1465  61  ARG C CG  
17123 C CD  . ARG C 61  ? 1.3829 0.9601 0.8474 0.1085  -0.1153 0.1520  61  ARG C CD  
17124 N NE  . ARG C 61  ? 1.2472 0.9069 0.7883 0.0908  -0.1088 0.1383  61  ARG C NE  
17125 C CZ  . ARG C 61  ? 1.2180 0.9075 0.7954 0.0544  -0.0859 0.1486  61  ARG C CZ  
17126 N NH1 . ARG C 61  ? 1.2376 0.8882 0.7889 0.0231  -0.0662 0.1715  61  ARG C NH1 
17127 N NH2 . ARG C 61  ? 1.1647 0.9235 0.8023 0.0493  -0.0823 0.1354  61  ARG C NH2 
17141 N N   . PHE C 62  ? 1.1326 0.8147 0.7786 0.1246  -0.1798 0.0748  62  PHE C N   
17142 C CA  . PHE C 62  ? 1.0725 0.8180 0.7776 0.1308  -0.1906 0.0505  62  PHE C CA  
17143 C C   . PHE C 62  ? 1.0894 0.8160 0.7907 0.1487  -0.2043 0.0415  62  PHE C C   
17144 O O   . PHE C 62  ? 1.1796 0.8476 0.8524 0.1393  -0.2011 0.0526  62  PHE C O   
17145 C CB  . PHE C 62  ? 0.9660 0.7525 0.7270 0.0967  -0.1761 0.0486  62  PHE C CB  
17146 C CG  . PHE C 62  ? 0.9633 0.7752 0.7299 0.0862  -0.1617 0.0547  62  PHE C CG  
17147 C CD1 . PHE C 62  ? 0.9539 0.8083 0.7388 0.0973  -0.1653 0.0381  62  PHE C CD1 
17148 C CD2 . PHE C 62  ? 1.0099 0.8032 0.7607 0.0641  -0.1434 0.0759  62  PHE C CD2 
17149 C CE1 . PHE C 62  ? 0.9352 0.8050 0.7164 0.0922  -0.1516 0.0424  62  PHE C CE1 
17150 C CE2 . PHE C 62  ? 0.9963 0.8174 0.7505 0.0597  -0.1281 0.0814  62  PHE C CE2 
17151 C CZ  . PHE C 62  ? 0.9571 0.8123 0.7232 0.0767  -0.1325 0.0646  62  PHE C CZ  
17161 N N   . SER C 63  ? 1.0306 0.8081 0.7589 0.1737  -0.2190 0.0199  63  SER C N   
17162 C CA  . SER C 63  ? 1.0122 0.7875 0.7421 0.1967  -0.2308 0.0088  63  SER C CA  
17163 C C   . SER C 63  ? 1.0129 0.8738 0.8044 0.2004  -0.2367 -0.0165 63  SER C C   
17164 O O   . SER C 63  ? 1.0110 0.9218 0.8252 0.1965  -0.2388 -0.0271 63  SER C O   
17165 C CB  . SER C 63  ? 0.9989 0.7274 0.6632 0.2423  -0.2455 0.0136  63  SER C CB  
17166 O OG  . SER C 63  ? 1.0255 0.7945 0.6826 0.2681  -0.2577 0.0060  63  SER C OG  
17172 N N   . GLY C 64  ? 1.0078 0.8815 0.8217 0.2055  -0.2381 -0.0267 64  GLY C N   
17173 C CA  . GLY C 64  ? 0.9334 0.8857 0.8052 0.2028  -0.2388 -0.0493 64  GLY C CA  
17174 C C   . GLY C 64  ? 0.9264 0.9074 0.7980 0.2423  -0.2517 -0.0633 64  GLY C C   
17175 O O   . GLY C 64  ? 1.0289 0.9551 0.8559 0.2696  -0.2569 -0.0552 64  GLY C O   
17179 N N   . SER C 65  ? 0.8600 0.9285 0.7805 0.2446  -0.2559 -0.0857 65  SER C N   
17180 C CA  . SER C 65  ? 0.8538 0.9770 0.7875 0.2825  -0.2670 -0.1024 65  SER C CA  
17181 C C   . SER C 65  ? 0.7677 0.9845 0.7718 0.2575  -0.2587 -0.1252 65  SER C C   
17182 O O   . SER C 65  ? 0.7153 0.9485 0.7474 0.2163  -0.2487 -0.1292 65  SER C O   
17183 C CB  . SER C 65  ? 0.8952 1.0382 0.7978 0.3282  -0.2899 -0.1065 65  SER C CB  
17184 O OG  . SER C 65  ? 0.9573 1.1517 0.8826 0.3100  -0.2962 -0.1171 65  SER C OG  
17190 N N   . GLY C 66  ? 0.7651 1.0399 0.7933 0.2829  -0.2609 -0.1400 66  GLY C N   
17191 C CA  . GLY C 66  ? 0.7641 1.1372 0.8587 0.2599  -0.2518 -0.1630 66  GLY C CA  
17192 C C   . GLY C 66  ? 0.8055 1.1900 0.9174 0.2643  -0.2357 -0.1659 66  GLY C C   
17193 O O   . GLY C 66  ? 0.8547 1.1673 0.9257 0.2848  -0.2330 -0.1517 66  GLY C O   
17197 N N   . SER C 67  ? 0.7951 1.2705 0.9657 0.2417  -0.2236 -0.1858 67  SER C N   
17198 C CA  . SER C 67  ? 0.8032 1.3049 0.9956 0.2425  -0.2040 -0.1909 67  SER C CA  
17199 C C   . SER C 67  ? 0.7465 1.3461 1.0043 0.1998  -0.1878 -0.2120 67  SER C C   
17200 O O   . SER C 67  ? 0.7064 1.3606 0.9918 0.1781  -0.1970 -0.2261 67  SER C O   
17201 C CB  . SER C 67  ? 0.8514 1.3790 1.0280 0.3061  -0.2148 -0.1955 67  SER C CB  
17202 O OG  . SER C 67  ? 0.8954 1.5343 1.1083 0.3315  -0.2310 -0.2161 67  SER C OG  
17208 N N   . GLY C 68  ? 0.7594 1.3768 1.0372 0.1857  -0.1626 -0.2145 68  GLY C N   
17209 C CA  . GLY C 68  ? 0.7290 1.4305 1.0634 0.1396  -0.1413 -0.2327 68  GLY C CA  
17210 C C   . GLY C 68  ? 0.6934 1.3555 1.0280 0.0810  -0.1327 -0.2312 68  GLY C C   
17211 O O   . GLY C 68  ? 0.6834 1.2567 0.9870 0.0587  -0.1169 -0.2140 68  GLY C O   
17215 N N   . THR C 69  ? 0.6933 1.4207 1.0590 0.0586  -0.1443 -0.2504 69  THR C N   
17216 C CA  . THR C 69  ? 0.7294 1.4192 1.0904 0.0038  -0.1361 -0.2531 69  THR C CA  
17217 C C   . THR C 69  ? 0.8033 1.4597 1.1367 0.0139  -0.1632 -0.2511 69  THR C C   
17218 O O   . THR C 69  ? 0.8140 1.4159 1.1283 -0.0226 -0.1568 -0.2492 69  THR C O   
17219 C CB  . THR C 69  ? 0.6727 1.4579 1.0880 -0.0472 -0.1215 -0.2809 69  THR C CB  
17220 O OG1 . THR C 69  ? 0.6563 1.5541 1.1107 -0.0296 -0.1485 -0.3049 69  THR C OG1 
17221 C CG2 . THR C 69  ? 0.6711 1.4955 1.1135 -0.0592 -0.0901 -0.2824 69  THR C CG2 
17229 N N   . ASP C 70  ? 0.8306 1.5123 1.1544 0.0651  -0.1916 -0.2508 70  ASP C N   
17230 C CA  . ASP C 70  ? 0.8101 1.4649 1.1034 0.0785  -0.2169 -0.2488 70  ASP C CA  
17231 C C   . ASP C 70  ? 0.7712 1.3259 1.0066 0.1167  -0.2241 -0.2194 70  ASP C C   
17232 O O   . ASP C 70  ? 0.7683 1.3129 0.9900 0.1574  -0.2275 -0.2098 70  ASP C O   
17233 C CB  . ASP C 70  ? 0.8272 1.5892 1.1470 0.1071  -0.2454 -0.2720 70  ASP C CB  
17234 C CG  . ASP C 70  ? 0.8770 1.7466 1.2572 0.0597  -0.2411 -0.3047 70  ASP C CG  
17235 O OD1 . ASP C 70  ? 0.8997 1.8440 1.3273 0.0485  -0.2247 -0.3164 70  ASP C OD1 
17236 O OD2 . ASP C 70  ? 0.9210 1.7995 1.2988 0.0311  -0.2530 -0.3195 70  ASP C OD2 
17241 N N   . TYR C 71  ? 0.7784 1.2589 0.9776 0.1021  -0.2250 -0.2062 71  TYR C N   
17242 C CA  . TYR C 71  ? 0.8192 1.2075 0.9663 0.1265  -0.2283 -0.1786 71  TYR C CA  
17243 C C   . TYR C 71  ? 0.8786 1.2366 0.9935 0.1264  -0.2411 -0.1743 71  TYR C C   
17244 O O   . TYR C 71  ? 0.9559 1.3435 1.0841 0.0995  -0.2425 -0.1909 71  TYR C O   
17245 C CB  . TYR C 71  ? 0.7746 1.0935 0.9118 0.1026  -0.2045 -0.1607 71  TYR C CB  
17246 C CG  . TYR C 71  ? 0.7689 1.1093 0.9293 0.1033  -0.1901 -0.1638 71  TYR C CG  
17247 C CD1 . TYR C 71  ? 0.7452 1.1359 0.9451 0.0700  -0.1721 -0.1800 71  TYR C CD1 
17248 C CD2 . TYR C 71  ? 0.8253 1.1300 0.9620 0.1355  -0.1928 -0.1509 71  TYR C CD2 
17249 C CE1 . TYR C 71  ? 0.7561 1.1670 0.9734 0.0716  -0.1560 -0.1819 71  TYR C CE1 
17250 C CE2 . TYR C 71  ? 0.8428 1.1648 0.9947 0.1393  -0.1792 -0.1545 71  TYR C CE2 
17251 C CZ  . TYR C 71  ? 0.7948 1.1728 0.9881 0.1086  -0.1601 -0.1693 71  TYR C CZ  
17252 O OH  . TYR C 71  ? 0.7836 1.1790 0.9882 0.1133  -0.1436 -0.1719 71  TYR C OH  
17262 N N   . SER C 72  ? 0.8538 1.1477 0.9209 0.1549  -0.2489 -0.1523 72  SER C N   
17263 C CA  . SER C 72  ? 0.8616 1.1251 0.8912 0.1602  -0.2592 -0.1456 72  SER C CA  
17264 C C   . SER C 72  ? 0.8427 1.0170 0.8246 0.1688  -0.2522 -0.1154 72  SER C C   
17265 O O   . SER C 72  ? 0.8551 0.9951 0.8197 0.1884  -0.2520 -0.1024 72  SER C O   
17266 C CB  . SER C 72  ? 0.9538 1.2674 0.9714 0.1982  -0.2866 -0.1586 72  SER C CB  
17267 O OG  . SER C 72  ? 1.0471 1.3357 1.0333 0.2443  -0.2964 -0.1455 72  SER C OG  
17273 N N   . LEU C 73  ? 0.8579 0.9962 0.8174 0.1526  -0.2454 -0.1058 73  LEU C N   
17274 C CA  . LEU C 73  ? 0.8722 0.9395 0.7874 0.1575  -0.2387 -0.0785 73  LEU C CA  
17275 C C   . LEU C 73  ? 0.9114 0.9651 0.7787 0.1863  -0.2541 -0.0736 73  LEU C C   
17276 O O   . LEU C 73  ? 0.9567 1.0528 0.8257 0.1924  -0.2671 -0.0914 73  LEU C O   
17277 C CB  . LEU C 73  ? 0.8464 0.8890 0.7665 0.1257  -0.2184 -0.0694 73  LEU C CB  
17278 C CG  . LEU C 73  ? 0.8611 0.8477 0.7450 0.1241  -0.2079 -0.0425 73  LEU C CG  
17279 C CD1 . LEU C 73  ? 0.9115 0.8640 0.7941 0.1209  -0.2027 -0.0271 73  LEU C CD1 
17280 C CD2 . LEU C 73  ? 0.8175 0.8004 0.7073 0.1021  -0.1906 -0.0389 73  LEU C CD2 
17292 N N   . THR C 74  ? 0.9271 0.9175 0.7463 0.2023  -0.2524 -0.0496 74  THR C N   
17293 C CA  . THR C 74  ? 0.9653 0.9268 0.7251 0.2332  -0.2644 -0.0402 74  THR C CA  
17294 C C   . THR C 74  ? 1.0536 0.9447 0.7704 0.2186  -0.2459 -0.0117 74  THR C C   
17295 O O   . THR C 74  ? 1.0688 0.9147 0.7804 0.2034  -0.2331 0.0051  74  THR C O   
17296 C CB  . THR C 74  ? 0.9650 0.9136 0.6935 0.2773  -0.2821 -0.0396 74  THR C CB  
17297 O OG1 . THR C 74  ? 0.9483 0.9801 0.7252 0.2908  -0.2977 -0.0673 74  THR C OG1 
17298 C CG2 . THR C 74  ? 1.0137 0.9251 0.6700 0.3144  -0.2948 -0.0284 74  THR C CG2 
17306 N N   . ILE C 75  ? 1.1151 1.0011 0.8012 0.2216  -0.2443 -0.0076 75  ILE C N   
17307 C CA  . ILE C 75  ? 1.1825 1.0112 0.8246 0.2101  -0.2249 0.0195  75  ILE C CA  
17308 C C   . ILE C 75  ? 1.2432 1.0297 0.8094 0.2471  -0.2361 0.0306  75  ILE C C   
17309 O O   . ILE C 75  ? 1.2654 1.0770 0.8114 0.2670  -0.2485 0.0195  75  ILE C O   
17310 C CB  . ILE C 75  ? 1.1933 1.0459 0.8540 0.1862  -0.2087 0.0173  75  ILE C CB  
17311 C CG1 . ILE C 75  ? 1.1150 1.0097 0.8430 0.1589  -0.2016 0.0021  75  ILE C CG1 
17312 C CG2 . ILE C 75  ? 1.2446 1.0512 0.8716 0.1707  -0.1839 0.0464  75  ILE C CG2 
17313 C CD1 . ILE C 75  ? 1.0604 0.9729 0.7988 0.1434  -0.1873 -0.0032 75  ILE C CD1 
17325 N N   . SER C 76  ? 1.3129 1.0290 0.8299 0.2574  -0.2324 0.0520  76  SER C N   
17326 C CA  . SER C 76  ? 1.4390 1.0933 0.8681 0.2924  -0.2379 0.0688  76  SER C CA  
17327 C C   . SER C 76  ? 1.5286 1.1323 0.9163 0.2669  -0.2099 0.0960  76  SER C C   
17328 O O   . SER C 76  ? 1.5632 1.1538 0.9769 0.2249  -0.1865 0.1088  76  SER C O   
17329 C CB  . SER C 76  ? 1.4637 1.0511 0.8458 0.3185  -0.2458 0.0790  76  SER C CB  
17330 O OG  . SER C 76  ? 1.4614 0.9925 0.8442 0.2798  -0.2240 0.0967  76  SER C OG  
17336 N N   . ASN C 77  ? 1.5631 1.1453 0.8867 0.2932  -0.2122 0.1039  77  ASN C N   
17337 C CA  . ASN C 77  ? 1.5805 1.1183 0.8578 0.2732  -0.1832 0.1303  77  ASN C CA  
17338 C C   . ASN C 77  ? 1.4961 1.0932 0.8421 0.2318  -0.1623 0.1250  77  ASN C C   
17339 O O   . ASN C 77  ? 1.4994 1.0845 0.8652 0.1927  -0.1361 0.1419  77  ASN C O   
17340 C CB  . ASN C 77  ? 1.6630 1.1048 0.8840 0.2568  -0.1630 0.1613  77  ASN C CB  
17341 C CG  . ASN C 77  ? 1.7967 1.1726 0.9544 0.2998  -0.1842 0.1639  77  ASN C CG  
17342 O OD1 . ASN C 77  ? 1.8204 1.1970 1.0091 0.3006  -0.1958 0.1534  77  ASN C OD1 
17343 N ND2 . ASN C 77  ? 1.8967 1.2130 0.9592 0.3405  -0.1889 0.1782  77  ASN C ND2 
17350 N N   . LEU C 78  ? 1.4360 1.0983 0.8157 0.2420  -0.1753 0.0998  78  LEU C N   
17351 C CA  . LEU C 78  ? 1.3255 1.0392 0.7636 0.2120  -0.1585 0.0912  78  LEU C CA  
17352 C C   . LEU C 78  ? 1.3223 1.0140 0.7313 0.1939  -0.1246 0.1171  78  LEU C C   
17353 O O   . LEU C 78  ? 1.3494 1.0073 0.6894 0.2129  -0.1182 0.1301  78  LEU C O   
17354 C CB  . LEU C 78  ? 1.2685 1.0341 0.7223 0.2284  -0.1777 0.0604  78  LEU C CB  
17355 C CG  . LEU C 78  ? 1.1843 0.9897 0.6829 0.2054  -0.1618 0.0488  78  LEU C CG  
17356 C CD1 . LEU C 78  ? 1.1155 0.9689 0.6611 0.2040  -0.1837 0.0139  78  LEU C CD1 
17357 C CD2 . LEU C 78  ? 1.2383 1.0316 0.6851 0.2162  -0.1468 0.0555  78  LEU C CD2 
17369 N N   . ASP C 79  ? 1.2914 1.0079 0.7531 0.1586  -0.1024 0.1243  79  ASP C N   
17370 C CA  . ASP C 79  ? 1.3471 1.0651 0.7987 0.1376  -0.0678 0.1469  79  ASP C CA  
17371 C C   . ASP C 79  ? 1.3603 1.1331 0.8413 0.1415  -0.0580 0.1329  79  ASP C C   
17372 O O   . ASP C 79  ? 1.3324 1.1372 0.8510 0.1490  -0.0753 0.1067  79  ASP C O   
17373 C CB  . ASP C 79  ? 1.3266 1.0459 0.8175 0.0970  -0.0505 0.1630  79  ASP C CB  
17374 C CG  . ASP C 79  ? 1.3835 1.1066 0.8600 0.0714  -0.0136 0.1892  79  ASP C CG  
17375 O OD1 . ASP C 79  ? 1.4734 1.1366 0.8851 0.0664  -0.0006 0.2121  79  ASP C OD1 
17376 O OD2 . ASP C 79  ? 1.3342 1.1208 0.8617 0.0576  0.0037  0.1873  79  ASP C OD2 
17381 N N   . GLN C 80  ? 1.3976 1.1769 0.8560 0.1364  -0.0275 0.1509  80  GLN C N   
17382 C CA  . GLN C 80  ? 1.3593 1.1826 0.8339 0.1465  -0.0151 0.1391  80  GLN C CA  
17383 C C   . GLN C 80  ? 1.1921 1.0652 0.7437 0.1303  -0.0137 0.1273  80  GLN C C   
17384 O O   . GLN C 80  ? 1.1003 0.9943 0.6658 0.1447  -0.0180 0.1066  80  GLN C O   
17385 C CB  . GLN C 80  ? 1.4860 1.3146 0.9256 0.1447  0.0216  0.1632  80  GLN C CB  
17386 C CG  . GLN C 80  ? 1.5206 1.3918 0.9689 0.1615  0.0385  0.1528  80  GLN C CG  
17387 C CD  . GLN C 80  ? 1.5584 1.4060 0.9588 0.1957  0.0187  0.1279  80  GLN C CD  
17388 O OE1 . GLN C 80  ? 1.6042 1.4117 0.9573 0.2097  -0.0040 0.1226  80  GLN C OE1 
17389 N NE2 . GLN C 80  ? 1.5290 1.4003 0.9376 0.2105  0.0262  0.1112  80  GLN C NE2 
17398 N N   . GLU C 81  ? 1.1722 1.0587 0.7673 0.1010  -0.0079 0.1397  81  GLU C N   
17399 C CA  . GLU C 81  ? 1.1309 1.0638 0.7940 0.0886  -0.0085 0.1297  81  GLU C CA  
17400 C C   . GLU C 81  ? 1.0533 0.9758 0.7408 0.0936  -0.0383 0.1058  81  GLU C C   
17401 O O   . GLU C 81  ? 1.0088 0.9605 0.7456 0.0851  -0.0402 0.0973  81  GLU C O   
17402 C CB  . GLU C 81  ? 1.2497 1.2057 0.9493 0.0535  0.0062  0.1491  81  GLU C CB  
17403 C CG  . GLU C 81  ? 1.4372 1.3479 1.1316 0.0337  -0.0107 0.1533  81  GLU C CG  
17404 C CD  . GLU C 81  ? 1.5778 1.5019 1.2951 -0.0072 0.0055  0.1722  81  GLU C CD  
17405 O OE1 . GLU C 81  ? 1.6820 1.5596 1.3546 -0.0249 0.0164  0.1914  81  GLU C OE1 
17406 O OE2 . GLU C 81  ? 1.5707 1.5499 1.3468 -0.0227 0.0074  0.1676  81  GLU C OE2 
17413 N N   . ASP C 82  ? 1.0932 0.9799 0.7469 0.1084  -0.0608 0.0950  82  ASP C N   
17414 C CA  . ASP C 82  ? 1.0681 0.9563 0.7468 0.1129  -0.0871 0.0709  82  ASP C CA  
17415 C C   . ASP C 82  ? 1.0457 0.9480 0.7249 0.1265  -0.0935 0.0455  82  ASP C C   
17416 O O   . ASP C 82  ? 1.0268 0.9384 0.7348 0.1229  -0.1096 0.0248  82  ASP C O   
17417 C CB  . ASP C 82  ? 1.1337 0.9883 0.7792 0.1257  -0.1097 0.0691  82  ASP C CB  
17418 C CG  . ASP C 82  ? 1.1901 1.0132 0.8291 0.1111  -0.1061 0.0903  82  ASP C CG  
17419 O OD1 . ASP C 82  ? 1.1861 1.0232 0.8612 0.0850  -0.0918 0.1005  82  ASP C OD1 
17420 O OD2 . ASP C 82  ? 1.2612 1.0427 0.8545 0.1269  -0.1187 0.0956  82  ASP C OD2 
17425 N N   . ILE C 83  ? 1.0589 0.9591 0.7030 0.1401  -0.0799 0.0461  83  ILE C N   
17426 C CA  . ILE C 83  ? 1.0647 0.9650 0.6981 0.1509  -0.0848 0.0206  83  ILE C CA  
17427 C C   . ILE C 83  ? 1.0453 0.9618 0.7227 0.1405  -0.0744 0.0148  83  ILE C C   
17428 O O   . ILE C 83  ? 1.0308 0.9637 0.7185 0.1425  -0.0514 0.0300  83  ILE C O   
17429 C CB  . ILE C 83  ? 1.1237 1.0113 0.7014 0.1710  -0.0701 0.0234  83  ILE C CB  
17430 C CG1 . ILE C 83  ? 1.2103 1.0758 0.7341 0.1865  -0.0881 0.0201  83  ILE C CG1 
17431 C CG2 . ILE C 83  ? 1.1039 0.9837 0.6702 0.1791  -0.0667 -0.0002 83  ILE C CG2 
17432 C CD1 . ILE C 83  ? 1.2581 1.1101 0.7653 0.1855  -0.0842 0.0482  83  ILE C CD1 
17444 N N   . ALA C 84  ? 1.0491 0.9640 0.7507 0.1308  -0.0906 -0.0067 84  ALA C N   
17445 C CA  . ALA C 84  ? 1.0013 0.9223 0.7387 0.1213  -0.0823 -0.0109 84  ALA C CA  
17446 C C   . ALA C 84  ? 0.9823 0.8957 0.7331 0.1083  -0.1004 -0.0373 84  ALA C C   
17447 O O   . ALA C 84  ? 1.0310 0.9463 0.7701 0.1073  -0.1200 -0.0526 84  ALA C O   
17448 C CB  . ALA C 84  ? 0.9774 0.9219 0.7563 0.1104  -0.0757 0.0106  84  ALA C CB  
17454 N N   . THR C 85  ? 0.9432 0.8518 0.7175 0.0989  -0.0930 -0.0424 85  THR C N   
17455 C CA  . THR C 85  ? 0.9388 0.8427 0.7305 0.0805  -0.1042 -0.0646 85  THR C CA  
17456 C C   . THR C 85  ? 0.9068 0.8341 0.7437 0.0700  -0.1104 -0.0559 85  THR C C   
17457 O O   . THR C 85  ? 0.8880 0.8230 0.7420 0.0732  -0.1010 -0.0359 85  THR C O   
17458 C CB  . THR C 85  ? 0.9558 0.8235 0.7300 0.0768  -0.0891 -0.0760 85  THR C CB  
17459 O OG1 . THR C 85  ? 0.9974 0.8351 0.7210 0.0912  -0.0814 -0.0831 85  THR C OG1 
17460 C CG2 . THR C 85  ? 0.9760 0.8359 0.7623 0.0503  -0.0975 -0.1006 85  THR C CG2 
17468 N N   . TYR C 86  ? 0.8988 0.8421 0.7546 0.0580  -0.1268 -0.0724 86  TYR C N   
17469 C CA  . TYR C 86  ? 0.8775 0.8414 0.7696 0.0525  -0.1340 -0.0667 86  TYR C CA  
17470 C C   . TYR C 86  ? 0.9136 0.8826 0.8286 0.0333  -0.1324 -0.0850 86  TYR C C   
17471 O O   . TYR C 86  ? 0.9214 0.9005 0.8350 0.0210  -0.1396 -0.1082 86  TYR C O   
17472 C CB  . TYR C 86  ? 0.8424 0.8262 0.7332 0.0635  -0.1538 -0.0664 86  TYR C CB  
17473 C CG  . TYR C 86  ? 0.8941 0.8631 0.7569 0.0787  -0.1514 -0.0441 86  TYR C CG  
17474 C CD1 . TYR C 86  ? 0.9382 0.8972 0.7629 0.0897  -0.1507 -0.0450 86  TYR C CD1 
17475 C CD2 . TYR C 86  ? 0.8916 0.8532 0.7616 0.0790  -0.1482 -0.0227 86  TYR C CD2 
17476 C CE1 . TYR C 86  ? 0.9521 0.8966 0.7479 0.1013  -0.1441 -0.0229 86  TYR C CE1 
17477 C CE2 . TYR C 86  ? 0.8926 0.8378 0.7349 0.0856  -0.1423 -0.0018 86  TYR C CE2 
17478 C CZ  . TYR C 86  ? 0.9264 0.8643 0.7323 0.0970  -0.1389 -0.0009 86  TYR C CZ  
17479 O OH  . TYR C 86  ? 0.9182 0.8390 0.6934 0.1014  -0.1289 0.0215  86  TYR C OH  
17489 N N   . PHE C 87  ? 0.8910 0.8548 0.8254 0.0288  -0.1225 -0.0749 87  PHE C N   
17490 C CA  . PHE C 87  ? 0.8806 0.8431 0.8318 0.0108  -0.1157 -0.0875 87  PHE C CA  
17491 C C   . PHE C 87  ? 0.8644 0.8550 0.8472 0.0112  -0.1239 -0.0848 87  PHE C C   
17492 O O   . PHE C 87  ? 0.8298 0.8202 0.8165 0.0235  -0.1278 -0.0674 87  PHE C O   
17493 C CB  . PHE C 87  ? 0.8679 0.7923 0.8036 0.0107  -0.0955 -0.0781 87  PHE C CB  
17494 C CG  . PHE C 87  ? 0.9150 0.8011 0.8113 0.0137  -0.0842 -0.0831 87  PHE C CG  
17495 C CD1 . PHE C 87  ? 0.9997 0.8547 0.8755 -0.0067 -0.0764 -0.1036 87  PHE C CD1 
17496 C CD2 . PHE C 87  ? 0.9026 0.7817 0.7791 0.0359  -0.0795 -0.0680 87  PHE C CD2 
17497 C CE1 . PHE C 87  ? 1.0572 0.8633 0.8859 -0.0023 -0.0657 -0.1097 87  PHE C CE1 
17498 C CE2 . PHE C 87  ? 0.9693 0.8099 0.8034 0.0447  -0.0679 -0.0733 87  PHE C CE2 
17499 C CZ  . PHE C 87  ? 1.0344 0.8325 0.8407 0.0270  -0.0617 -0.0945 87  PHE C CZ  
17509 N N   . CYS C 88  ? 0.8710 0.8856 0.8743 -0.0038 -0.1254 -0.1031 88  CYS C N   
17510 C CA  . CYS C 88  ? 0.8622 0.9006 0.8921 -0.0021 -0.1278 -0.1023 88  CYS C CA  
17511 C C   . CYS C 88  ? 0.8992 0.9151 0.9302 -0.0172 -0.1077 -0.1009 88  CYS C C   
17512 O O   . CYS C 88  ? 0.9417 0.9287 0.9554 -0.0336 -0.0929 -0.1069 88  CYS C O   
17513 C CB  . CYS C 88  ? 0.8524 0.9457 0.9076 -0.0039 -0.1413 -0.1228 88  CYS C CB  
17514 S SG  . CYS C 88  ? 0.9060 1.0263 0.9725 -0.0383 -0.1357 -0.1528 88  CYS C SG  
17519 N N   . GLN C 89  ? 0.9139 0.9348 0.9569 -0.0096 -0.1069 -0.0925 89  GLN C N   
17520 C CA  . GLN C 89  ? 0.9057 0.9014 0.9422 -0.0182 -0.0885 -0.0879 89  GLN C CA  
17521 C C   . GLN C 89  ? 0.8845 0.9062 0.9409 -0.0142 -0.0897 -0.0906 89  GLN C C   
17522 O O   . GLN C 89  ? 0.8798 0.9086 0.9396 0.0046  -0.1037 -0.0831 89  GLN C O   
17523 C CB  . GLN C 89  ? 0.8766 0.8353 0.8906 -0.0048 -0.0847 -0.0677 89  GLN C CB  
17524 C CG  . GLN C 89  ? 0.8514 0.7844 0.8525 -0.0046 -0.0702 -0.0605 89  GLN C CG  
17525 C CD  . GLN C 89  ? 0.7883 0.7289 0.7953 0.0100  -0.0808 -0.0491 89  GLN C CD  
17526 O OE1 . GLN C 89  ? 0.7824 0.7325 0.7942 0.0192  -0.0954 -0.0408 89  GLN C OE1 
17527 N NE2 . GLN C 89  ? 0.7894 0.7218 0.7912 0.0098  -0.0724 -0.0491 89  GLN C NE2 
17536 N N   . GLN C 90  ? 0.8814 0.9124 0.9458 -0.0325 -0.0731 -0.1015 90  GLN C N   
17537 C CA  . GLN C 90  ? 0.8703 0.9251 0.9494 -0.0270 -0.0690 -0.1038 90  GLN C CA  
17538 C C   . GLN C 90  ? 0.8610 0.8708 0.9138 -0.0189 -0.0590 -0.0876 90  GLN C C   
17539 O O   . GLN C 90  ? 0.8258 0.7922 0.8521 -0.0262 -0.0454 -0.0798 90  GLN C O   
17540 C CB  . GLN C 90  ? 0.8698 0.9629 0.9709 -0.0530 -0.0523 -0.1224 90  GLN C CB  
17541 C CG  . GLN C 90  ? 0.8979 0.9451 0.9742 -0.0818 -0.0247 -0.1214 90  GLN C CG  
17542 C CD  . GLN C 90  ? 0.8843 0.9070 0.9433 -0.0785 -0.0055 -0.1113 90  GLN C CD  
17543 O OE1 . GLN C 90  ? 0.8553 0.9041 0.9264 -0.0580 -0.0120 -0.1089 90  GLN C OE1 
17544 N NE2 . GLN C 90  ? 0.9239 0.8887 0.9462 -0.0962 0.0188  -0.1052 90  GLN C NE2 
17553 N N   . GLY C 91  ? 0.8516 0.8688 0.9060 -0.0004 -0.0669 -0.0836 91  GLY C N   
17554 C CA  . GLY C 91  ? 0.8360 0.8168 0.8645 0.0088  -0.0618 -0.0709 91  GLY C CA  
17555 C C   . GLY C 91  ? 0.8469 0.8398 0.8753 0.0135  -0.0512 -0.0763 91  GLY C C   
17556 O O   . GLY C 91  ? 0.8833 0.8509 0.8885 0.0266  -0.0525 -0.0684 91  GLY C O   
17560 N N   . ASN C 92  ? 0.8468 0.8841 0.9012 0.0029  -0.0406 -0.0911 92  ASN C N   
17561 C CA  . ASN C 92  ? 0.8664 0.9272 0.9246 0.0097  -0.0278 -0.0974 92  ASN C CA  
17562 C C   . ASN C 92  ? 0.8717 0.9020 0.9048 -0.0066 0.0016  -0.0921 92  ASN C C   
17563 O O   . ASN C 92  ? 0.9149 0.9437 0.9338 0.0047  0.0125  -0.0910 92  ASN C O   
17564 C CB  . ASN C 92  ? 0.8735 1.0087 0.9742 0.0057  -0.0262 -0.1160 92  ASN C CB  
17565 C CG  . ASN C 92  ? 0.9491 1.1204 1.0569 0.0209  -0.0142 -0.1232 92  ASN C CG  
17566 O OD1 . ASN C 92  ? 0.9943 1.1330 1.0734 0.0457  -0.0189 -0.1158 92  ASN C OD1 
17567 N ND2 . ASN C 92  ? 1.0057 1.2481 1.1512 0.0052  0.0018  -0.1390 92  ASN C ND2 
17574 N N   . THR C 93  ? 0.8538 0.8521 0.8729 -0.0306 0.0159  -0.0883 93  THR C N   
17575 C CA  . THR C 93  ? 0.9177 0.8746 0.9023 -0.0467 0.0470  -0.0820 93  THR C CA  
17576 C C   . THR C 93  ? 0.9126 0.8054 0.8609 -0.0556 0.0525  -0.0717 93  THR C C   
17577 O O   . THR C 93  ? 0.8293 0.7258 0.7910 -0.0644 0.0417  -0.0765 93  THR C O   
17578 C CB  . THR C 93  ? 0.9606 0.9615 0.9705 -0.0788 0.0742  -0.0968 93  THR C CB  
17579 O OG1 . THR C 93  ? 1.0525 0.9969 1.0187 -0.1006 0.1082  -0.0886 93  THR C OG1 
17580 C CG2 . THR C 93  ? 0.9351 0.9792 0.9845 -0.1050 0.0672  -0.1133 93  THR C CG2 
17588 N N   . PHE C 94  ? 0.9848 0.8164 0.8812 -0.0488 0.0696  -0.0575 94  PHE C N   
17589 C CA  . PHE C 94  ? 1.0330 0.7958 0.8836 -0.0501 0.0784  -0.0469 94  PHE C CA  
17590 C C   . PHE C 94  ? 1.0645 0.7974 0.8996 -0.0910 0.1100  -0.0549 94  PHE C C   
17591 O O   . PHE C 94  ? 1.0804 0.8318 0.9238 -0.1164 0.1337  -0.0621 94  PHE C O   
17592 C CB  . PHE C 94  ? 1.1133 0.8199 0.9065 -0.0214 0.0832  -0.0284 94  PHE C CB  
17593 C CG  . PHE C 94  ? 1.1455 0.8734 0.9472 0.0137  0.0505  -0.0211 94  PHE C CG  
17594 C CD1 . PHE C 94  ? 1.1221 0.8741 0.9514 0.0212  0.0258  -0.0218 94  PHE C CD1 
17595 C CD2 . PHE C 94  ? 1.1794 0.9029 0.9587 0.0361  0.0453  -0.0144 94  PHE C CD2 
17596 C CE1 . PHE C 94  ? 1.0651 0.8393 0.9035 0.0453  -0.0017 -0.0158 94  PHE C CE1 
17597 C CE2 . PHE C 94  ? 1.1419 0.8860 0.9287 0.0609  0.0144  -0.0106 94  PHE C CE2 
17598 C CZ  . PHE C 94  ? 1.0865 0.8575 0.9050 0.0630  -0.0083 -0.0112 94  PHE C CZ  
17608 N N   . PRO C 95  ? 1.0851 0.7705 0.8951 -0.1000 0.1125  -0.0548 95  PRO C N   
17609 C CA  . PRO C 95  ? 1.0885 0.7589 0.8900 -0.0701 0.0885  -0.0469 95  PRO C CA  
17610 C C   . PRO C 95  ? 0.9945 0.7359 0.8559 -0.0708 0.0602  -0.0591 95  PRO C C   
17611 O O   . PRO C 95  ? 0.9514 0.7362 0.8495 -0.0998 0.0617  -0.0768 95  PRO C O   
17612 C CB  . PRO C 95  ? 1.1656 0.7519 0.9094 -0.0827 0.1093  -0.0451 95  PRO C CB  
17613 C CG  . PRO C 95  ? 1.1838 0.7704 0.9359 -0.1350 0.1338  -0.0621 95  PRO C CG  
17614 C CD  . PRO C 95  ? 1.1573 0.7939 0.9383 -0.1429 0.1430  -0.0632 95  PRO C CD  
17622 N N   . TYR C 96  ? 0.9640 0.7200 0.8337 -0.0395 0.0351  -0.0498 96  TYR C N   
17623 C CA  . TYR C 96  ? 0.9563 0.7643 0.8692 -0.0385 0.0111  -0.0580 96  TYR C CA  
17624 C C   . TYR C 96  ? 0.9985 0.7867 0.9020 -0.0577 0.0168  -0.0685 96  TYR C C   
17625 O O   . TYR C 96  ? 1.0758 0.8027 0.9333 -0.0521 0.0286  -0.0619 96  TYR C O   
17626 C CB  . TYR C 96  ? 0.9380 0.7568 0.8539 -0.0071 -0.0113 -0.0441 96  TYR C CB  
17627 C CG  . TYR C 96  ? 0.9338 0.7792 0.8640 0.0079  -0.0247 -0.0386 96  TYR C CG  
17628 C CD1 . TYR C 96  ? 0.9694 0.8329 0.9117 -0.0004 -0.0185 -0.0464 96  TYR C CD1 
17629 C CD2 . TYR C 96  ? 0.9214 0.7754 0.8517 0.0291  -0.0432 -0.0272 96  TYR C CD2 
17630 C CE1 . TYR C 96  ? 0.9559 0.8338 0.9019 0.0154  -0.0310 -0.0431 96  TYR C CE1 
17631 C CE2 . TYR C 96  ? 0.9115 0.7819 0.8485 0.0385  -0.0568 -0.0249 96  TYR C CE2 
17632 C CZ  . TYR C 96  ? 0.9262 0.8028 0.8672 0.0332  -0.0510 -0.0330 96  TYR C CZ  
17633 O OH  . TYR C 96  ? 0.9184 0.8019 0.8572 0.0445  -0.0645 -0.0324 96  TYR C OH  
17643 N N   . THR C 97  ? 0.9716 0.8099 0.9138 -0.0773 0.0073  -0.0860 97  THR C N   
17644 C CA  . THR C 97  ? 1.0016 0.8279 0.9362 -0.0989 0.0091  -0.1006 97  THR C CA  
17645 C C   . THR C 97  ? 0.9669 0.8400 0.9302 -0.0850 -0.0179 -0.1049 97  THR C C   
17646 O O   . THR C 97  ? 0.9302 0.8568 0.9290 -0.0713 -0.0355 -0.1038 97  THR C O   
17647 C CB  . THR C 97  ? 0.9927 0.8397 0.9435 -0.1423 0.0241  -0.1219 97  THR C CB  
17648 O OG1 . THR C 97  ? 0.9607 0.8936 0.9676 -0.1420 0.0108  -0.1313 97  THR C OG1 
17649 C CG2 . THR C 97  ? 1.0053 0.7931 0.9172 -0.1607 0.0562  -0.1160 97  THR C CG2 
17657 N N   . PHE C 98  ? 0.9841 0.8285 0.9231 -0.0865 -0.0195 -0.1093 98  PHE C N   
17658 C CA  . PHE C 98  ? 0.9185 0.7960 0.8721 -0.0729 -0.0416 -0.1121 98  PHE C CA  
17659 C C   . PHE C 98  ? 0.8946 0.7941 0.8562 -0.1005 -0.0470 -0.1377 98  PHE C C   
17660 O O   . PHE C 98  ? 0.9251 0.7971 0.8703 -0.1332 -0.0310 -0.1528 98  PHE C O   
17661 C CB  . PHE C 98  ? 0.9353 0.7703 0.8528 -0.0477 -0.0405 -0.0974 98  PHE C CB  
17662 C CG  . PHE C 98  ? 0.9045 0.7349 0.8202 -0.0201 -0.0401 -0.0743 98  PHE C CG  
17663 C CD1 . PHE C 98  ? 0.9491 0.7360 0.8368 -0.0148 -0.0230 -0.0649 98  PHE C CD1 
17664 C CD2 . PHE C 98  ? 0.8555 0.7237 0.7936 -0.0009 -0.0571 -0.0624 98  PHE C CD2 
17665 C CE1 . PHE C 98  ? 0.9391 0.7312 0.8263 0.0112  -0.0263 -0.0462 98  PHE C CE1 
17666 C CE2 . PHE C 98  ? 0.8500 0.7215 0.7896 0.0182  -0.0585 -0.0443 98  PHE C CE2 
17667 C CZ  . PHE C 98  ? 0.9006 0.7394 0.8173 0.0253  -0.0449 -0.0372 98  PHE C CZ  
17677 N N   . GLY C 99  ? 0.8561 0.8034 0.8389 -0.0881 -0.0702 -0.1429 99  GLY C N   
17678 C CA  . GLY C 99  ? 0.8741 0.8438 0.8581 -0.1074 -0.0806 -0.1671 99  GLY C CA  
17679 C C   . GLY C 99  ? 0.9309 0.8412 0.8650 -0.1047 -0.0765 -0.1684 99  GLY C C   
17680 O O   . GLY C 99  ? 0.9270 0.7935 0.8322 -0.0794 -0.0690 -0.1482 99  GLY C O   
17684 N N   . GLY C 100 ? 1.0228 0.9364 0.9464 -0.1307 -0.0820 -0.1943 100 GLY C N   
17685 C CA  . GLY C 100 ? 1.0722 0.9209 0.9395 -0.1294 -0.0770 -0.1997 100 GLY C CA  
17686 C C   . GLY C 100 ? 1.0513 0.8993 0.9021 -0.0880 -0.0882 -0.1827 100 GLY C C   
17687 O O   . GLY C 100 ? 1.0667 0.8553 0.8683 -0.0731 -0.0775 -0.1769 100 GLY C O   
17691 N N   . GLY C 101 ? 0.9918 0.9019 0.8784 -0.0679 -0.1075 -0.1741 101 GLY C N   
17692 C CA  . GLY C 101 ? 0.9701 0.8801 0.8402 -0.0338 -0.1155 -0.1566 101 GLY C CA  
17693 C C   . GLY C 101 ? 0.9771 0.9146 0.8356 -0.0292 -0.1369 -0.1724 101 GLY C C   
17694 O O   . GLY C 101 ? 1.0148 0.9441 0.8544 -0.0509 -0.1415 -0.1988 101 GLY C O   
17698 N N   . THR C 102 ? 0.9531 0.9189 0.8172 -0.0019 -0.1502 -0.1568 102 THR C N   
17699 C CA  . THR C 102 ? 0.9768 0.9637 0.8200 0.0115  -0.1708 -0.1667 102 THR C CA  
17700 C C   . THR C 102 ? 1.0011 0.9554 0.8049 0.0392  -0.1625 -0.1439 102 THR C C   
17701 O O   . THR C 102 ? 0.9520 0.9034 0.7659 0.0534  -0.1534 -0.1169 102 THR C O   
17702 C CB  . THR C 102 ? 0.9518 0.9981 0.8269 0.0231  -0.1936 -0.1682 102 THR C CB  
17703 O OG1 . THR C 102 ? 0.9633 1.0541 0.8788 -0.0023 -0.1999 -0.1918 102 THR C OG1 
17704 C CG2 . THR C 102 ? 0.9699 1.0330 0.8135 0.0448  -0.2158 -0.1752 102 THR C CG2 
17712 N N   . LYS C 103 ? 0.9267 0.7056 0.8671 -0.1301 -0.0773 -0.0756 103 LYS C N   
17713 C CA  . LYS C 103 ? 0.9914 0.7303 0.8788 -0.1116 -0.0778 -0.0442 103 LYS C CA  
17714 C C   . LYS C 103 ? 1.0353 0.7725 0.8738 -0.0602 -0.0996 -0.0497 103 LYS C C   
17715 O O   . LYS C 103 ? 1.0697 0.8483 0.9204 -0.0331 -0.1230 -0.0909 103 LYS C O   
17716 C CB  . LYS C 103 ? 1.0778 0.8169 0.9799 -0.1242 -0.0741 -0.0543 103 LYS C CB  
17717 C CG  . LYS C 103 ? 1.1581 0.8985 1.1061 -0.1683 -0.0512 -0.0625 103 LYS C CG  
17718 C CD  . LYS C 103 ? 1.2061 0.9504 1.1722 -0.1787 -0.0465 -0.0833 103 LYS C CD  
17719 C CE  . LYS C 103 ? 1.1873 0.9455 1.2078 -0.2153 -0.0238 -0.1165 103 LYS C CE  
17720 N NZ  . LYS C 103 ? 1.1385 0.8665 1.1584 -0.2414 0.0007  -0.0929 103 LYS C NZ  
17734 N N   . VAL C 104 ? 1.0655 0.7529 0.8464 -0.0448 -0.0895 -0.0121 104 VAL C N   
17735 C CA  . VAL C 104 ? 1.1249 0.7869 0.8390 0.0073  -0.1006 -0.0097 104 VAL C CA  
17736 C C   . VAL C 104 ? 1.1456 0.7660 0.8116 0.0239  -0.0947 0.0074  104 VAL C C   
17737 O O   . VAL C 104 ? 1.1094 0.6907 0.7632 0.0007  -0.0701 0.0394  104 VAL C O   
17738 C CB  . VAL C 104 ? 1.1296 0.7535 0.8066 0.0129  -0.0845 0.0175  104 VAL C CB  
17739 C CG1 . VAL C 104 ? 1.1815 0.7549 0.7703 0.0689  -0.0856 0.0261  104 VAL C CG1 
17740 C CG2 . VAL C 104 ? 1.1042 0.7715 0.8249 0.0030  -0.0941 -0.0026 104 VAL C CG2 
17750 N N   . GLU C 105 ? 1.2157 0.8482 0.8558 0.0663  -0.1180 -0.0178 105 GLU C N   
17751 C CA  . GLU C 105 ? 1.2569 0.8531 0.8498 0.0874  -0.1157 -0.0070 105 GLU C CA  
17752 C C   . GLU C 105 ? 1.3046 0.8524 0.8037 0.1517  -0.1209 -0.0023 105 GLU C C   
17753 O O   . GLU C 105 ? 1.3311 0.8995 0.8124 0.1914  -0.1424 -0.0262 105 GLU C O   
17754 C CB  . GLU C 105 ? 1.2829 0.9330 0.9247 0.0828  -0.1373 -0.0435 105 GLU C CB  
17755 C CG  . GLU C 105 ? 1.4276 1.0698 1.0195 0.1337  -0.1569 -0.0595 105 GLU C CG  
17756 C CD  . GLU C 105 ? 1.4921 1.2131 1.1375 0.1477  -0.1897 -0.1187 105 GLU C CD  
17757 O OE1 . GLU C 105 ? 1.5049 1.2806 1.1985 0.1446  -0.2032 -0.1533 105 GLU C OE1 
17758 O OE2 . GLU C 105 ? 1.5355 1.2666 1.1792 0.1604  -0.2005 -0.1346 105 GLU C OE2 
17765 N N   . MET C 106 ? 1.2926 0.7718 0.7268 0.1646  -0.0987 0.0271  106 MET C N   
17766 C CA  . MET C 106 ? 1.3799 0.7934 0.7082 0.2293  -0.0956 0.0347  106 MET C CA  
17767 C C   . MET C 106 ? 1.3774 0.8259 0.6845 0.2855  -0.1359 -0.0038 106 MET C C   
17768 O O   . MET C 106 ? 1.3354 0.8371 0.6982 0.2692  -0.1547 -0.0269 106 MET C O   
17769 C CB  . MET C 106 ? 1.5033 0.8302 0.7698 0.2247  -0.0549 0.0720  106 MET C CB  
17770 C CG  . MET C 106 ? 1.6345 0.8925 0.8631 0.2093  -0.0098 0.1042  106 MET C CG  
17771 S SD  . MET C 106 ? 1.7763 0.9891 0.9216 0.2672  -0.0091 0.1039  106 MET C SD  
17772 C CE  . MET C 106 ? 1.9691 1.1238 1.0049 0.3452  -0.0088 0.0943  106 MET C CE  
17782 N N   . ARG C 107 ? 1.4461 0.8624 0.6679 0.3558  -0.1485 -0.0128 107 ARG C N   
17783 C CA  . ARG C 107 ? 1.5201 0.9686 0.7091 0.4229  -0.1898 -0.0538 107 ARG C CA  
17784 C C   . ARG C 107 ? 1.5689 0.9396 0.6650 0.4614  -0.1758 -0.0329 107 ARG C C   
17785 O O   . ARG C 107 ? 1.5709 0.8430 0.5962 0.4566  -0.1311 0.0123  107 ARG C O   
17786 C CB  . ARG C 107 ? 1.6411 1.0936 0.7732 0.4922  -0.2149 -0.0783 107 ARG C CB  
17787 C CG  . ARG C 107 ? 1.6515 1.2241 0.8840 0.4843  -0.2566 -0.1361 107 ARG C CG  
17788 C CD  . ARG C 107 ? 1.8030 1.3983 0.9731 0.5768  -0.2979 -0.1800 107 ARG C CD  
17789 N NE  . ARG C 107 ? 1.8146 1.5199 1.0814 0.5652  -0.3300 -0.2352 107 ARG C NE  
17790 C CZ  . ARG C 107 ? 1.8808 1.5878 1.1522 0.5609  -0.3257 -0.2309 107 ARG C CZ  
17791 N NH1 . ARG C 107 ? 1.9515 1.5558 1.1360 0.5673  -0.2900 -0.1740 107 ARG C NH1 
17792 N NH2 . ARG C 107 ? 1.8624 1.6743 1.2283 0.5484  -0.3541 -0.2867 107 ARG C NH2 
17806 N N   . ARG C 108 ? 1.5864 1.0031 0.6853 0.4992  -0.2122 -0.0704 108 ARG C N   
17807 C CA  . ARG C 108 ? 1.6366 0.9900 0.6580 0.5328  -0.2028 -0.0549 108 ARG C CA  
17808 C C   . ARG C 108 ? 1.6223 1.0326 0.6301 0.6026  -0.2522 -0.1089 108 ARG C C   
17809 O O   . ARG C 108 ? 1.5545 1.0736 0.6463 0.6000  -0.2942 -0.1625 108 ARG C O   
17810 C CB  . ARG C 108 ? 1.6153 0.9762 0.7060 0.4593  -0.1804 -0.0344 108 ARG C CB  
17811 C CG  . ARG C 108 ? 1.7083 0.9741 0.7112 0.4772  -0.1495 0.0000  108 ARG C CG  
17812 C CD  . ARG C 108 ? 1.6325 0.9316 0.7071 0.4235  -0.1464 0.0018  108 ARG C CD  
17813 N NE  . ARG C 108 ? 1.7277 0.9442 0.7205 0.4462  -0.1208 0.0268  108 ARG C NE  
17814 C CZ  . ARG C 108 ? 1.8465 1.0615 0.7951 0.5014  -0.1367 0.0026  108 ARG C CZ  
17815 N NH1 . ARG C 108 ? 1.8824 1.1625 0.8363 0.5541  -0.1881 -0.0427 108 ARG C NH1 
17816 N NH2 . ARG C 108 ? 1.9267 1.0820 0.8323 0.5030  -0.1006 0.0177  108 ARG C NH2 
17830 N N   . ALA C 109 ? 1.6879 1.0350 0.6243 0.6512  -0.2328 -0.1039 109 ALA C N   
17831 C CA  . ALA C 109 ? 1.7573 1.1582 0.7006 0.7113  -0.2712 -0.1532 109 ALA C CA  
17832 C C   . ALA C 109 ? 1.7109 1.1847 0.7311 0.6695  -0.2978 -0.1716 109 ALA C C   
17833 O O   . ALA C 109 ? 1.7017 1.1357 0.7212 0.6151  -0.2732 -0.1329 109 ALA C O   
17834 C CB  . ALA C 109 ? 1.9003 1.2034 0.7368 0.7697  -0.2393 -0.1420 109 ALA C CB  
17840 N N   . ASP C 110 ? 1.6859 1.2701 0.7807 0.6924  -0.3445 -0.2347 110 ASP C N   
17841 C CA  . ASP C 110 ? 1.5827 1.2441 0.7629 0.6459  -0.3649 -0.2654 110 ASP C CA  
17842 C C   . ASP C 110 ? 1.5730 1.1668 0.6992 0.6470  -0.3456 -0.2319 110 ASP C C   
17843 O O   . ASP C 110 ? 1.6262 1.1542 0.6735 0.7069  -0.3324 -0.2177 110 ASP C O   
17844 C CB  . ASP C 110 ? 1.6250 1.4118 0.8985 0.6770  -0.4072 -0.3420 110 ASP C CB  
17845 C CG  . ASP C 110 ? 1.6247 1.4985 0.9860 0.6531  -0.4228 -0.3832 110 ASP C CG  
17846 O OD1 . ASP C 110 ? 1.6040 1.4405 0.9516 0.6108  -0.4044 -0.3531 110 ASP C OD1 
17847 O OD2 . ASP C 110 ? 1.6290 1.6095 1.0763 0.6760  -0.4513 -0.4470 110 ASP C OD2 
17852 N N   . ALA C 111 ? 1.5348 1.1436 0.7224 0.5736  -0.3331 -0.2198 111 ALA C N   
17853 C CA  . ALA C 111 ? 1.6212 1.1762 0.7749 0.5639  -0.3141 -0.1892 111 ALA C CA  
17854 C C   . ALA C 111 ? 1.5979 1.2422 0.8606 0.5213  -0.3317 -0.2299 111 ALA C C   
17855 O O   . ALA C 111 ? 1.5567 1.2830 0.9288 0.4721  -0.3388 -0.2638 111 ALA C O   
17856 C CB  . ALA C 111 ? 1.5811 1.0479 0.7154 0.5057  -0.2601 -0.1199 111 ALA C CB  
17862 N N   . ALA C 112 ? 1.6118 1.2333 0.8403 0.5400  -0.3342 -0.2265 112 ALA C N   
17863 C CA  . ALA C 112 ? 1.4984 1.1954 0.8224 0.5014  -0.3470 -0.2638 112 ALA C CA  
17864 C C   . ALA C 112 ? 1.4248 1.0774 0.7775 0.4276  -0.3072 -0.2137 112 ALA C C   
17865 O O   . ALA C 112 ? 1.4514 1.0130 0.7265 0.4320  -0.2792 -0.1596 112 ALA C O   
17866 C CB  . ALA C 112 ? 1.5272 1.2433 0.8063 0.5711  -0.3811 -0.3020 112 ALA C CB  
17872 N N   . PRO C 113 ? 1.3730 1.0842 0.8327 0.3609  -0.3011 -0.2328 113 PRO C N   
17873 C CA  . PRO C 113 ? 1.3316 1.0007 0.8123 0.2979  -0.2659 -0.1873 113 PRO C CA  
17874 C C   . PRO C 113 ? 1.3230 0.9601 0.7620 0.3159  -0.2662 -0.1763 113 PRO C C   
17875 O O   . PRO C 113 ? 1.3353 1.0190 0.7858 0.3477  -0.2943 -0.2209 113 PRO C O   
17876 C CB  . PRO C 113 ? 1.2505 0.9885 0.8447 0.2356  -0.2614 -0.2200 113 PRO C CB  
17877 C CG  . PRO C 113 ? 1.2515 1.0764 0.8907 0.2682  -0.2968 -0.2943 113 PRO C CG  
17878 C CD  . PRO C 113 ? 1.3212 1.1350 0.8850 0.3406  -0.3215 -0.2993 113 PRO C CD  
17886 N N   . THR C 114 ? 1.0379 1.1886 0.8949 0.3564  -0.1508 -0.0124 114 THR C N   
17887 C CA  . THR C 114 ? 1.0775 1.2226 0.8914 0.3690  -0.1464 -0.0030 114 THR C CA  
17888 C C   . THR C 114 ? 1.1378 1.2646 0.9508 0.3320  -0.1484 -0.0336 114 THR C C   
17889 O O   . THR C 114 ? 1.2232 1.3172 1.0573 0.3046  -0.1329 -0.0262 114 THR C O   
17890 C CB  . THR C 114 ? 1.0604 1.1784 0.8743 0.3841  -0.1219 0.0486  114 THR C CB  
17891 O OG1 . THR C 114 ? 1.1027 1.2359 0.9262 0.4188  -0.1177 0.0817  114 THR C OG1 
17892 C CG2 . THR C 114 ? 1.0813 1.2005 0.8466 0.4036  -0.1148 0.0622  114 THR C CG2 
17900 N N   . VAL C 115 ? 1.1202 1.2681 0.9120 0.3324  -0.1688 -0.0687 115 VAL C N   
17901 C CA  . VAL C 115 ? 1.0962 1.2282 0.8975 0.2968  -0.1726 -0.0994 115 VAL C CA  
17902 C C   . VAL C 115 ? 1.1282 1.2390 0.8819 0.3081  -0.1680 -0.0965 115 VAL C C   
17903 O O   . VAL C 115 ? 1.1752 1.3029 0.8834 0.3467  -0.1782 -0.0949 115 VAL C O   
17904 C CB  . VAL C 115 ? 1.0929 1.2583 0.9182 0.2846  -0.2005 -0.1419 115 VAL C CB  
17905 C CG1 . VAL C 115 ? 1.0566 1.2025 0.9029 0.2468  -0.2014 -0.1673 115 VAL C CG1 
17906 C CG2 . VAL C 115 ? 1.0631 1.2556 0.9327 0.2793  -0.2025 -0.1400 115 VAL C CG2 
17916 N N   . SER C 116 ? 1.1216 1.1984 0.8824 0.2793  -0.1519 -0.0950 116 SER C N   
17917 C CA  . SER C 116 ? 1.1463 1.2001 0.8638 0.2881  -0.1448 -0.0918 116 SER C CA  
17918 C C   . SER C 116 ? 1.1412 1.1733 0.8767 0.2515  -0.1464 -0.1213 116 SER C C   
17919 O O   . SER C 116 ? 1.1661 1.1894 0.9440 0.2188  -0.1340 -0.1192 116 SER C O   
17920 C CB  . SER C 116 ? 1.1582 1.1911 0.8664 0.2959  -0.1157 -0.0442 116 SER C CB  
17921 O OG  . SER C 116 ? 1.2156 1.2666 0.9214 0.3273  -0.1108 -0.0097 116 SER C OG  
17927 N N   . ILE C 117 ? 1.1260 1.1498 0.8294 0.2607  -0.1617 -0.1482 117 ILE C N   
17928 C CA  . ILE C 117 ? 1.1172 1.1150 0.8392 0.2291  -0.1628 -0.1738 117 ILE C CA  
17929 C C   . ILE C 117 ? 1.1214 1.0856 0.7967 0.2406  -0.1444 -0.1582 117 ILE C C   
17930 O O   . ILE C 117 ? 1.1300 1.0970 0.7502 0.2802  -0.1436 -0.1437 117 ILE C O   
17931 C CB  . ILE C 117 ? 1.2041 1.2124 0.9387 0.2265  -0.1993 -0.2229 117 ILE C CB  
17932 C CG1 . ILE C 117 ? 1.2153 1.1975 0.9949 0.1857  -0.1969 -0.2424 117 ILE C CG1 
17933 C CG2 . ILE C 117 ? 1.2855 1.2915 0.9530 0.2704  -0.2202 -0.2412 117 ILE C CG2 
17934 C CD1 . ILE C 117 ? 1.2540 1.2468 1.0737 0.1726  -0.2339 -0.2889 117 ILE C CD1 
17946 N N   . PHE C 118 ? 1.1445 1.0812 0.8416 0.2094  -0.1275 -0.1579 118 PHE C N   
17947 C CA  . PHE C 118 ? 1.1687 1.0747 0.8263 0.2177  -0.1075 -0.1415 118 PHE C CA  
17948 C C   . PHE C 118 ? 1.1795 1.0550 0.8487 0.1963  -0.1118 -0.1706 118 PHE C C   
17949 O O   . PHE C 118 ? 1.1198 0.9963 0.8463 0.1616  -0.1122 -0.1830 118 PHE C O   
17950 C CB  . PHE C 118 ? 1.1214 1.0238 0.7940 0.2045  -0.0754 -0.1001 118 PHE C CB  
17951 C CG  . PHE C 118 ? 1.1551 1.0782 0.8225 0.2255  -0.0694 -0.0667 118 PHE C CG  
17952 C CD1 . PHE C 118 ? 1.1484 1.0932 0.8553 0.2169  -0.0767 -0.0660 118 PHE C CD1 
17953 C CD2 . PHE C 118 ? 1.1914 1.1131 0.8187 0.2558  -0.0553 -0.0325 118 PHE C CD2 
17954 C CE1 . PHE C 118 ? 1.1634 1.1217 0.8724 0.2362  -0.0711 -0.0338 118 PHE C CE1 
17955 C CE2 . PHE C 118 ? 1.1984 1.1388 0.8333 0.2741  -0.0479 0.0043  118 PHE C CE2 
17956 C CZ  . PHE C 118 ? 1.1837 1.1392 0.8607 0.2633  -0.0564 0.0027  118 PHE C CZ  
17966 N N   . PRO C 119 ? 1.2457 1.0941 0.8637 0.2188  -0.1135 -0.1790 119 PRO C N   
17967 C CA  . PRO C 119 ? 1.2727 1.0840 0.9038 0.1997  -0.1159 -0.2043 119 PRO C CA  
17968 C C   . PRO C 119 ? 1.2237 1.0178 0.8700 0.1771  -0.0787 -0.1725 119 PRO C C   
17969 O O   . PRO C 119 ? 1.1836 0.9924 0.8201 0.1815  -0.0551 -0.1346 119 PRO C O   
17970 C CB  . PRO C 119 ? 1.3808 1.1708 0.9402 0.2424  -0.1316 -0.2238 119 PRO C CB  
17971 C CG  . PRO C 119 ? 1.4146 1.2268 0.9212 0.2788  -0.1123 -0.1816 119 PRO C CG  
17972 C CD  . PRO C 119 ? 1.3425 1.1933 0.8889 0.2661  -0.1088 -0.1597 119 PRO C CD  
17980 N N   . PRO C 120 ? 1.2474 1.0119 0.9220 0.1538  -0.0734 -0.1860 120 PRO C N   
17981 C CA  . PRO C 120 ? 1.2190 0.9710 0.9012 0.1388  -0.0370 -0.1547 120 PRO C CA  
17982 C C   . PRO C 120 ? 1.2494 0.9858 0.8638 0.1697  -0.0199 -0.1321 120 PRO C C   
17983 O O   . PRO C 120 ? 1.3051 1.0205 0.8686 0.1994  -0.0340 -0.1496 120 PRO C O   
17984 C CB  . PRO C 120 ? 1.2561 0.9779 0.9826 0.1136  -0.0378 -0.1750 120 PRO C CB  
17985 C CG  . PRO C 120 ? 1.3379 1.0390 1.0536 0.1263  -0.0764 -0.2201 120 PRO C CG  
17986 C CD  . PRO C 120 ? 1.3283 1.0678 1.0304 0.1429  -0.1010 -0.2295 120 PRO C CD  
17994 N N   . SER C 121 ? 1.2141 0.9644 0.8289 0.1653  0.0093  -0.0936 121 SER C N   
17995 C CA  . SER C 121 ? 1.2058 0.9501 0.7669 0.1924  0.0282  -0.0648 121 SER C CA  
17996 C C   . SER C 121 ? 1.2379 0.9422 0.7727 0.1987  0.0384  -0.0733 121 SER C C   
17997 O O   . SER C 121 ? 1.2147 0.8983 0.7866 0.1737  0.0421  -0.0878 121 SER C O   
17998 C CB  . SER C 121 ? 1.1489 0.9183 0.7301 0.1814  0.0531  -0.0254 121 SER C CB  
17999 O OG  . SER C 121 ? 1.1379 0.8983 0.7431 0.1600  0.0739  -0.0195 121 SER C OG  
18005 N N   . SER C 122 ? 1.2799 0.9744 0.7518 0.2355  0.0447  -0.0608 122 SER C N   
18006 C CA  . SER C 122 ? 1.3246 0.9794 0.7647 0.2472  0.0565  -0.0660 122 SER C CA  
18007 C C   . SER C 122 ? 1.2726 0.9284 0.7403 0.2242  0.0899  -0.0365 122 SER C C   
18008 O O   . SER C 122 ? 1.3000 0.9213 0.7728 0.2170  0.0998  -0.0455 122 SER C O   
18009 C CB  . SER C 122 ? 1.4119 1.0650 0.7746 0.2979  0.0598  -0.0525 122 SER C CB  
18010 O OG  . SER C 122 ? 1.4842 1.1521 0.8183 0.3261  0.0321  -0.0710 122 SER C OG  
18016 N N   . GLU C 123 ? 1.2357 0.9307 0.7237 0.2142  0.1061  -0.0020 123 GLU C N   
18017 C CA  . GLU C 123 ? 1.2041 0.9084 0.7184 0.1955  0.1338  0.0222  123 GLU C CA  
18018 C C   . GLU C 123 ? 1.1982 0.8927 0.7656 0.1642  0.1343  0.0030  123 GLU C C   
18019 O O   . GLU C 123 ? 1.2068 0.8870 0.7825 0.1582  0.1560  0.0119  123 GLU C O   
18020 C CB  . GLU C 123 ? 1.1801 0.9288 0.7162 0.1892  0.1414  0.0529  123 GLU C CB  
18021 C CG  . GLU C 123 ? 1.2844 1.0503 0.7847 0.2171  0.1502  0.0871  123 GLU C CG  
18022 C CD  . GLU C 123 ? 1.4482 1.2181 0.9219 0.2414  0.1313  0.0836  123 GLU C CD  
18023 O OE1 . GLU C 123 ? 1.5311 1.2822 0.9983 0.2425  0.1093  0.0477  123 GLU C OE1 
18024 O OE2 . GLU C 123 ? 1.4909 1.2866 0.9543 0.2610  0.1386  0.1190  123 GLU C OE2 
18031 N N   . GLN C 124 ? 1.1968 0.9029 0.8031 0.1466  0.1126  -0.0189 124 GLN C N   
18032 C CA  . GLN C 124 ? 1.1673 0.8749 0.8327 0.1183  0.1154  -0.0297 124 GLN C CA  
18033 C C   . GLN C 124 ? 1.2286 0.8908 0.9043 0.1138  0.1109  -0.0522 124 GLN C C   
18034 O O   . GLN C 124 ? 1.2314 0.8862 0.9478 0.0974  0.1297  -0.0439 124 GLN C O   
18035 C CB  . GLN C 124 ? 1.0913 0.8273 0.7955 0.1039  0.0931  -0.0452 124 GLN C CB  
18036 C CG  . GLN C 124 ? 1.0774 0.8188 0.8466 0.0781  0.0927  -0.0567 124 GLN C CG  
18037 C CD  . GLN C 124 ? 1.0474 0.8250 0.8533 0.0673  0.0746  -0.0665 124 GLN C CD  
18038 O OE1 . GLN C 124 ? 1.0473 0.8309 0.8332 0.0774  0.0511  -0.0796 124 GLN C OE1 
18039 N NE2 . GLN C 124 ? 1.0288 0.8340 0.8871 0.0510  0.0873  -0.0574 124 GLN C NE2 
18048 N N   . LEU C 125 ? 1.2890 0.9208 0.9310 0.1307  0.0852  -0.0807 125 LEU C N   
18049 C CA  . LEU C 125 ? 1.3607 0.9436 1.0198 0.1256  0.0724  -0.1105 125 LEU C CA  
18050 C C   . LEU C 125 ? 1.4182 0.9665 1.0621 0.1324  0.1023  -0.0920 125 LEU C C   
18051 O O   . LEU C 125 ? 1.4591 0.9755 1.1503 0.1150  0.1072  -0.0995 125 LEU C O   
18052 C CB  . LEU C 125 ? 1.3738 0.9334 0.9876 0.1515  0.0352  -0.1492 125 LEU C CB  
18053 C CG  . LEU C 125 ? 1.3272 0.9152 0.9688 0.1428  0.0008  -0.1756 125 LEU C CG  
18054 C CD1 . LEU C 125 ? 1.3475 0.9269 0.9253 0.1811  -0.0320 -0.2061 125 LEU C CD1 
18055 C CD2 . LEU C 125 ? 1.3254 0.9029 1.0522 0.1068  -0.0151 -0.2003 125 LEU C CD2 
18067 N N   . THR C 126 ? 1.4235 0.9796 1.0079 0.1578  0.1239  -0.0643 126 THR C N   
18068 C CA  . THR C 126 ? 1.4484 0.9783 1.0172 0.1666  0.1551  -0.0427 126 THR C CA  
18069 C C   . THR C 126 ? 1.3759 0.9285 1.0037 0.1407  0.1846  -0.0152 126 THR C C   
18070 O O   . THR C 126 ? 1.3834 0.9075 1.0254 0.1398  0.2074  -0.0036 126 THR C O   
18071 C CB  . THR C 126 ? 1.4540 0.9999 0.9534 0.1990  0.1727  -0.0139 126 THR C CB  
18072 O OG1 . THR C 126 ? 1.4186 1.0221 0.9320 0.1896  0.1843  0.0155  126 THR C OG1 
18073 C CG2 . THR C 126 ? 1.4753 1.0070 0.9124 0.2329  0.1476  -0.0344 126 THR C CG2 
18081 N N   . SER C 127 ? 1.3385 0.9432 0.9990 0.1242  0.1855  -0.0037 127 SER C N   
18082 C CA  . SER C 127 ? 1.3673 1.0021 1.0802 0.1067  0.2114  0.0203  127 SER C CA  
18083 C C   . SER C 127 ? 1.3653 0.9838 1.1507 0.0823  0.2071  0.0079  127 SER C C   
18084 O O   . SER C 127 ? 1.3818 1.0245 1.2143 0.0723  0.2332  0.0329  127 SER C O   
18085 C CB  . SER C 127 ? 1.4108 1.1046 1.1334 0.1017  0.2089  0.0307  127 SER C CB  
18086 O OG  . SER C 127 ? 1.4894 1.1987 1.1603 0.1202  0.2080  0.0422  127 SER C OG  
18092 N N   . GLY C 128 ? 1.3627 0.9452 1.1613 0.0748  0.1746  -0.0284 128 GLY C N   
18093 C CA  . GLY C 128 ? 1.3537 0.9325 1.2353 0.0469  0.1630  -0.0416 128 GLY C CA  
18094 C C   . GLY C 128 ? 1.3208 0.9546 1.2311 0.0343  0.1484  -0.0451 128 GLY C C   
18095 O O   . GLY C 128 ? 1.3212 0.9991 1.2062 0.0431  0.1614  -0.0250 128 GLY C O   
18099 N N   . GLY C 129 ? 1.3074 0.9392 1.2722 0.0150  0.1194  -0.0720 129 GLY C N   
18100 C CA  . GLY C 129 ? 1.2368 0.9198 1.2267 0.0059  0.1032  -0.0774 129 GLY C CA  
18101 C C   . GLY C 129 ? 1.2074 0.8921 1.1356 0.0230  0.0715  -0.1039 129 GLY C C   
18102 O O   . GLY C 129 ? 1.1785 0.8444 1.0351 0.0466  0.0730  -0.1032 129 GLY C O   
18106 N N   . ALA C 130 ? 1.2163 0.9289 1.1759 0.0134  0.0439  -0.1236 130 ALA C N   
18107 C CA  . ALA C 130 ? 1.2111 0.9309 1.1196 0.0319  0.0138  -0.1463 130 ALA C CA  
18108 C C   . ALA C 130 ? 1.1597 0.9319 1.1017 0.0235  0.0053  -0.1434 130 ALA C C   
18109 O O   . ALA C 130 ? 1.1580 0.9505 1.1715 0.0018  -0.0008 -0.1482 130 ALA C O   
18110 C CB  . ALA C 130 ? 1.2709 0.9546 1.1733 0.0371  -0.0248 -0.1902 130 ALA C CB  
18116 N N   . SER C 131 ? 1.1289 0.9230 1.0246 0.0415  0.0057  -0.1330 131 SER C N   
18117 C CA  . SER C 131 ? 1.0828 0.9215 1.0015 0.0390  -0.0026 -0.1305 131 SER C CA  
18118 C C   . SER C 131 ? 1.1019 0.9440 0.9840 0.0580  -0.0335 -0.1508 131 SER C C   
18119 O O   . SER C 131 ? 1.1492 0.9768 0.9708 0.0815  -0.0330 -0.1444 131 SER C O   
18120 C CB  . SER C 131 ? 1.0609 0.9224 0.9660 0.0451  0.0229  -0.1005 131 SER C CB  
18121 O OG  . SER C 131 ? 1.0415 0.9090 0.9766 0.0343  0.0518  -0.0811 131 SER C OG  
18127 N N   . VAL C 132 ? 1.0726 0.9389 0.9933 0.0505  -0.0587 -0.1716 132 VAL C N   
18128 C CA  . VAL C 132 ? 1.0888 0.9701 0.9796 0.0716  -0.0870 -0.1880 132 VAL C CA  
18129 C C   . VAL C 132 ? 1.0137 0.9333 0.9176 0.0740  -0.0802 -0.1691 132 VAL C C   
18130 O O   . VAL C 132 ? 0.9682 0.9163 0.9274 0.0564  -0.0767 -0.1667 132 VAL C O   
18131 C CB  . VAL C 132 ? 1.1650 1.0513 1.0893 0.0653  -0.1238 -0.2268 132 VAL C CB  
18132 C CG1 . VAL C 132 ? 1.2171 1.1166 1.0922 0.0975  -0.1528 -0.2448 132 VAL C CG1 
18133 C CG2 . VAL C 132 ? 1.2164 1.0598 1.1516 0.0547  -0.1303 -0.2479 132 VAL C CG2 
18143 N N   . VAL C 133 ? 1.0173 0.9380 0.8739 0.0976  -0.0775 -0.1535 133 VAL C N   
18144 C CA  . VAL C 133 ? 1.0164 0.9628 0.8835 0.1022  -0.0712 -0.1350 133 VAL C CA  
18145 C C   . VAL C 133 ? 1.0602 1.0275 0.9152 0.1230  -0.0956 -0.1442 133 VAL C C   
18146 O O   . VAL C 133 ? 1.1374 1.0960 0.9492 0.1461  -0.1085 -0.1504 133 VAL C O   
18147 C CB  . VAL C 133 ? 1.0205 0.9521 0.8583 0.1110  -0.0487 -0.1053 133 VAL C CB  
18148 C CG1 . VAL C 133 ? 1.0200 0.9707 0.8715 0.1181  -0.0488 -0.0909 133 VAL C CG1 
18149 C CG2 . VAL C 133 ? 0.9965 0.9161 0.8470 0.0936  -0.0247 -0.0961 133 VAL C CG2 
18159 N N   . CYS C 134 ? 1.0127 1.0106 0.9028 0.1197  -0.1009 -0.1441 134 CYS C N   
18160 C CA  . CYS C 134 ? 1.0500 1.0724 0.9326 0.1412  -0.1213 -0.1489 134 CYS C CA  
18161 C C   . CYS C 134 ? 1.0007 1.0326 0.8936 0.1486  -0.1104 -0.1262 134 CYS C C   
18162 O O   . CYS C 134 ? 0.9503 0.9963 0.8808 0.1346  -0.1031 -0.1262 134 CYS C O   
18163 C CB  . CYS C 134 ? 1.1426 1.1964 1.0654 0.1318  -0.1455 -0.1773 134 CYS C CB  
18164 S SG  . CYS C 134 ? 1.2477 1.3342 1.1496 0.1646  -0.1761 -0.1897 134 CYS C SG  
18169 N N   . PHE C 135 ? 1.0123 1.0370 0.8742 0.1732  -0.1093 -0.1059 135 PHE C N   
18170 C CA  . PHE C 135 ? 0.9701 0.9970 0.8469 0.1821  -0.1029 -0.0848 135 PHE C CA  
18171 C C   . PHE C 135 ? 0.9628 1.0184 0.8434 0.2037  -0.1204 -0.0884 135 PHE C C   
18172 O O   . PHE C 135 ? 0.9794 1.0434 0.8283 0.2284  -0.1302 -0.0851 135 PHE C O   
18173 C CB  . PHE C 135 ? 0.9895 0.9908 0.8448 0.1942  -0.0882 -0.0525 135 PHE C CB  
18174 C CG  . PHE C 135 ? 1.0021 0.9796 0.8580 0.1749  -0.0706 -0.0457 135 PHE C CG  
18175 C CD1 . PHE C 135 ? 0.9877 0.9641 0.8747 0.1558  -0.0639 -0.0531 135 PHE C CD1 
18176 C CD2 . PHE C 135 ? 1.0175 0.9781 0.8398 0.1813  -0.0603 -0.0307 135 PHE C CD2 
18177 C CE1 . PHE C 135 ? 0.9709 0.9310 0.8561 0.1423  -0.0484 -0.0468 135 PHE C CE1 
18178 C CE2 . PHE C 135 ? 1.0169 0.9597 0.8399 0.1656  -0.0438 -0.0229 135 PHE C CE2 
18179 C CZ  . PHE C 135 ? 0.9933 0.9365 0.8483 0.1455  -0.0383 -0.0313 135 PHE C CZ  
18189 N N   . LEU C 136 ? 0.9383 1.0122 0.8541 0.1994  -0.1237 -0.0944 136 LEU C N   
18190 C CA  . LEU C 136 ? 0.9692 1.0701 0.8917 0.2220  -0.1372 -0.0932 136 LEU C CA  
18191 C C   . LEU C 136 ? 0.9271 1.0109 0.8664 0.2307  -0.1275 -0.0722 136 LEU C C   
18192 O O   . LEU C 136 ? 0.9051 0.9888 0.8718 0.2192  -0.1236 -0.0807 136 LEU C O   
18193 C CB  . LEU C 136 ? 1.0065 1.1478 0.9602 0.2128  -0.1518 -0.1191 136 LEU C CB  
18194 C CG  . LEU C 136 ? 1.0557 1.2036 1.0377 0.1816  -0.1485 -0.1377 136 LEU C CG  
18195 C CD1 . LEU C 136 ? 1.0798 1.2719 1.1080 0.1765  -0.1553 -0.1485 136 LEU C CD1 
18196 C CD2 . LEU C 136 ? 1.1061 1.2504 1.0739 0.1731  -0.1608 -0.1557 136 LEU C CD2 
18208 N N   . ASN C 137 ? 0.9262 0.9964 0.8519 0.2538  -0.1242 -0.0444 137 ASN C N   
18209 C CA  . ASN C 137 ? 0.9295 0.9713 0.8789 0.2588  -0.1158 -0.0219 137 ASN C CA  
18210 C C   . ASN C 137 ? 0.9366 0.9897 0.8967 0.2876  -0.1220 -0.0071 137 ASN C C   
18211 O O   . ASN C 137 ? 0.9371 1.0204 0.8762 0.3102  -0.1295 -0.0038 137 ASN C O   
18212 C CB  . ASN C 137 ? 0.9398 0.9505 0.8812 0.2586  -0.1017 0.0091  137 ASN C CB  
18213 C CG  . ASN C 137 ? 0.9410 0.9421 0.8648 0.2356  -0.0940 -0.0016 137 ASN C CG  
18214 O OD1 . ASN C 137 ? 0.9115 0.9129 0.8464 0.2136  -0.0941 -0.0263 137 ASN C OD1 
18215 N ND2 . ASN C 137 ? 0.9748 0.9700 0.8700 0.2448  -0.0853 0.0199  137 ASN C ND2 
18222 N N   . ASN C 138 ? 0.9603 0.9881 0.9534 0.2890  -0.1203 0.0002  138 ASN C N   
18223 C CA  . ASN C 138 ? 1.0104 1.0334 1.0216 0.3166  -0.1222 0.0226  138 ASN C CA  
18224 C C   . ASN C 138 ? 1.0824 1.1512 1.0810 0.3379  -0.1333 0.0103  138 ASN C C   
18225 O O   . ASN C 138 ? 1.1780 1.2694 1.1579 0.3651  -0.1342 0.0299  138 ASN C O   
18226 C CB  . ASN C 138 ? 0.9908 0.9970 1.0008 0.3331  -0.1100 0.0686  138 ASN C CB  
18227 C CG  . ASN C 138 ? 0.9677 0.9340 0.9994 0.3111  -0.1000 0.0837  138 ASN C CG  
18228 O OD1 . ASN C 138 ? 0.9531 0.9223 0.9604 0.2984  -0.0929 0.0847  138 ASN C OD1 
18229 N ND2 . ASN C 138 ? 0.9905 0.9190 1.0707 0.3074  -0.1016 0.0936  138 ASN C ND2 
18236 N N   . PHE C 139 ? 1.0543 1.1420 1.0647 0.3279  -0.1415 -0.0212 139 PHE C N   
18237 C CA  . PHE C 139 ? 1.0332 1.1691 1.0426 0.3450  -0.1530 -0.0343 139 PHE C CA  
18238 C C   . PHE C 139 ? 0.9987 1.1315 1.0349 0.3534  -0.1554 -0.0448 139 PHE C C   
18239 O O   . PHE C 139 ? 0.9849 1.0896 1.0355 0.3396  -0.1517 -0.0566 139 PHE C O   
18240 C CB  . PHE C 139 ? 1.0207 1.1989 1.0217 0.3259  -0.1617 -0.0621 139 PHE C CB  
18241 C CG  . PHE C 139 ? 0.9835 1.1546 1.0007 0.2954  -0.1559 -0.0822 139 PHE C CG  
18242 C CD1 . PHE C 139 ? 0.9431 1.1417 0.9854 0.2945  -0.1576 -0.0979 139 PHE C CD1 
18243 C CD2 . PHE C 139 ? 0.9778 1.1195 0.9840 0.2722  -0.1467 -0.0818 139 PHE C CD2 
18244 C CE1 . PHE C 139 ? 0.9119 1.1109 0.9677 0.2731  -0.1489 -0.1109 139 PHE C CE1 
18245 C CE2 . PHE C 139 ? 0.9260 1.0652 0.9457 0.2488  -0.1391 -0.0967 139 PHE C CE2 
18246 C CZ  . PHE C 139 ? 0.9088 1.0776 0.9531 0.2503  -0.1397 -0.1102 139 PHE C CZ  
18256 N N   . TYR C 140 ? 1.0141 1.1788 1.0534 0.3809  -0.1624 -0.0416 140 TYR C N   
18257 C CA  . TYR C 140 ? 1.0079 1.1787 1.0672 0.3964  -0.1656 -0.0524 140 TYR C CA  
18258 C C   . TYR C 140 ? 1.0306 1.2702 1.0897 0.4108  -0.1754 -0.0616 140 TYR C C   
18259 O O   . TYR C 140 ? 1.1224 1.3909 1.1664 0.4248  -0.1816 -0.0508 140 TYR C O   
18260 C CB  . TYR C 140 ? 0.9879 1.1129 1.0609 0.4230  -0.1630 -0.0305 140 TYR C CB  
18261 C CG  . TYR C 140 ? 0.9768 1.0970 1.0667 0.4415  -0.1676 -0.0467 140 TYR C CG  
18262 C CD1 . TYR C 140 ? 0.9941 1.1562 1.0840 0.4715  -0.1721 -0.0454 140 TYR C CD1 
18263 C CD2 . TYR C 140 ? 0.9683 1.0454 1.0709 0.4333  -0.1687 -0.0651 140 TYR C CD2 
18264 C CE1 . TYR C 140 ? 1.0424 1.2015 1.1434 0.4937  -0.1754 -0.0600 140 TYR C CE1 
18265 C CE2 . TYR C 140 ? 1.0196 1.0929 1.1308 0.4573  -0.1747 -0.0836 140 TYR C CE2 
18266 C CZ  . TYR C 140 ? 1.0781 1.1915 1.1876 0.4879  -0.1769 -0.0799 140 TYR C CZ  
18267 O OH  . TYR C 140 ? 1.1496 1.2602 1.2636 0.5168  -0.1819 -0.0978 140 TYR C OH  
18277 N N   . PRO C 141 ? 0.9351 1.2077 1.0117 0.4111  -0.1775 -0.0803 141 PRO C N   
18278 C CA  . PRO C 141 ? 0.9142 1.1680 1.0030 0.4045  -0.1710 -0.0954 141 PRO C CA  
18279 C C   . PRO C 141 ? 0.9325 1.1805 1.0211 0.3688  -0.1643 -0.1072 141 PRO C C   
18280 O O   . PRO C 141 ? 0.9583 1.1979 1.0357 0.3476  -0.1642 -0.1027 141 PRO C O   
18281 C CB  . PRO C 141 ? 0.8983 1.2138 1.0034 0.4233  -0.1739 -0.1043 141 PRO C CB  
18282 C CG  . PRO C 141 ? 0.9255 1.2796 1.0288 0.4435  -0.1835 -0.0924 141 PRO C CG  
18283 C CD  . PRO C 141 ? 0.9101 1.2532 0.9964 0.4263  -0.1875 -0.0851 141 PRO C CD  
18291 N N   . LYS C 142 ? 0.9339 1.1885 1.0322 0.3672  -0.1579 -0.1210 142 LYS C N   
18292 C CA  . LYS C 142 ? 0.9480 1.1952 1.0460 0.3386  -0.1485 -0.1287 142 LYS C CA  
18293 C C   . LYS C 142 ? 0.9922 1.2958 1.1085 0.3159  -0.1458 -0.1306 142 LYS C C   
18294 O O   . LYS C 142 ? 1.0290 1.3212 1.1431 0.2877  -0.1402 -0.1316 142 LYS C O   
18295 C CB  . LYS C 142 ? 1.0255 1.2619 1.1238 0.3526  -0.1424 -0.1416 142 LYS C CB  
18296 C CG  . LYS C 142 ? 1.1521 1.3843 1.2476 0.3290  -0.1306 -0.1471 142 LYS C CG  
18297 C CD  . LYS C 142 ? 1.2697 1.5004 1.3597 0.3517  -0.1263 -0.1619 142 LYS C CD  
18298 C CE  . LYS C 142 ? 1.3090 1.5428 1.3947 0.3323  -0.1126 -0.1637 142 LYS C CE  
18299 N NZ  . LYS C 142 ? 1.3482 1.5859 1.4218 0.3613  -0.1097 -0.1800 142 LYS C NZ  
18313 N N   . ASP C 143 ? 1.0160 1.3798 1.1559 0.3273  -0.1501 -0.1305 143 ASP C N   
18314 C CA  . ASP C 143 ? 0.9944 1.4142 1.1689 0.3039  -0.1489 -0.1315 143 ASP C CA  
18315 C C   . ASP C 143 ? 0.9868 1.3997 1.1576 0.2793  -0.1618 -0.1355 143 ASP C C   
18316 O O   . ASP C 143 ? 0.9863 1.3948 1.1386 0.2926  -0.1763 -0.1349 143 ASP C O   
18317 C CB  . ASP C 143 ? 0.9936 1.4838 1.2016 0.3229  -0.1531 -0.1279 143 ASP C CB  
18318 C CG  . ASP C 143 ? 1.0108 1.5168 1.2210 0.3518  -0.1388 -0.1246 143 ASP C CG  
18319 O OD1 . ASP C 143 ? 1.0062 1.4912 1.2077 0.3482  -0.1241 -0.1262 143 ASP C OD1 
18320 O OD2 . ASP C 143 ? 1.0454 1.5870 1.2628 0.3823  -0.1426 -0.1211 143 ASP C OD2 
18325 N N   . ILE C 144 ? 0.9811 1.3942 1.1681 0.2478  -0.1564 -0.1392 144 ILE C N   
18326 C CA  . ILE C 144 ? 0.9724 1.3737 1.1532 0.2262  -0.1700 -0.1481 144 ILE C CA  
18327 C C   . ILE C 144 ? 0.9681 1.3833 1.1876 0.1930  -0.1625 -0.1513 144 ILE C C   
18328 O O   . ILE C 144 ? 0.9604 1.3693 1.1889 0.1868  -0.1406 -0.1420 144 ILE C O   
18329 C CB  . ILE C 144 ? 0.9752 1.3115 1.1030 0.2303  -0.1678 -0.1445 144 ILE C CB  
18330 C CG1 . ILE C 144 ? 1.0006 1.3311 1.1118 0.2208  -0.1844 -0.1547 144 ILE C CG1 
18331 C CG2 . ILE C 144 ? 0.9315 1.2270 1.0495 0.2163  -0.1471 -0.1394 144 ILE C CG2 
18332 C CD1 . ILE C 144 ? 0.9942 1.2733 1.0541 0.2329  -0.1811 -0.1441 144 ILE C CD1 
18344 N N   . ASN C 145 ? 0.9940 1.4286 1.2382 0.1742  -0.1819 -0.1649 145 ASN C N   
18345 C CA  . ASN C 145 ? 1.0048 1.4463 1.2948 0.1404  -0.1781 -0.1682 145 ASN C CA  
18346 C C   . ASN C 145 ? 0.9927 1.3896 1.2535 0.1259  -0.1924 -0.1857 145 ASN C C   
18347 O O   . ASN C 145 ? 0.9939 1.3800 1.2146 0.1424  -0.2133 -0.1988 145 ASN C O   
18348 C CB  . ASN C 145 ? 1.0875 1.5980 1.4559 0.1275  -0.1918 -0.1709 145 ASN C CB  
18349 C CG  . ASN C 145 ? 1.1598 1.7174 1.5732 0.1334  -0.1668 -0.1460 145 ASN C CG  
18350 O OD1 . ASN C 145 ? 1.1252 1.6819 1.5660 0.1185  -0.1425 -0.1301 145 ASN C OD1 
18351 N ND2 . ASN C 145 ? 1.2521 1.8544 1.6713 0.1598  -0.1713 -0.1406 145 ASN C ND2 
18358 N N   . VAL C 146 ? 1.0130 1.3864 1.2925 0.0995  -0.1795 -0.1841 146 VAL C N   
18359 C CA  . VAL C 146 ? 1.0650 1.3932 1.3180 0.0866  -0.1905 -0.2009 146 VAL C CA  
18360 C C   . VAL C 146 ? 1.1531 1.4939 1.4770 0.0531  -0.1968 -0.2099 146 VAL C C   
18361 O O   . VAL C 146 ? 1.1750 1.5390 1.5547 0.0373  -0.1744 -0.1895 146 VAL C O   
18362 C CB  . VAL C 146 ? 1.0193 1.2905 1.2157 0.0901  -0.1654 -0.1874 146 VAL C CB  
18363 C CG1 . VAL C 146 ? 1.0029 1.2567 1.1404 0.1203  -0.1639 -0.1787 146 VAL C CG1 
18364 C CG2 . VAL C 146 ? 0.9966 1.2721 1.2219 0.0782  -0.1335 -0.1658 146 VAL C CG2 
18374 N N   . LYS C 147 ? 1.2078 1.5342 1.5319 0.0452  -0.2279 -0.2398 147 LYS C N   
18375 C CA  . LYS C 147 ? 1.1968 1.5233 1.5926 0.0119  -0.2404 -0.2541 147 LYS C CA  
18376 C C   . LYS C 147 ? 1.2011 1.4650 1.5491 0.0100  -0.2513 -0.2768 147 LYS C C   
18377 O O   . LYS C 147 ? 1.2544 1.5012 1.5347 0.0356  -0.2732 -0.2982 147 LYS C O   
18378 C CB  . LYS C 147 ? 1.2186 1.5994 1.6822 0.0040  -0.2793 -0.2778 147 LYS C CB  
18379 C CG  . LYS C 147 ? 1.2063 1.6564 1.7294 0.0049  -0.2679 -0.2529 147 LYS C CG  
18380 C CD  . LYS C 147 ? 1.2406 1.7486 1.8337 -0.0031 -0.3093 -0.2770 147 LYS C CD  
18381 C CE  . LYS C 147 ? 1.2169 1.7996 1.8716 0.0002  -0.2955 -0.2479 147 LYS C CE  
18382 N NZ  . LYS C 147 ? 1.2400 1.8864 1.9686 -0.0077 -0.3369 -0.2698 147 LYS C NZ  
18396 N N   . TRP C 148 ? 1.1475 1.3798 1.5291 -0.0159 -0.2342 -0.2693 148 TRP C N   
18397 C CA  . TRP C 148 ? 1.1550 1.3254 1.4953 -0.0175 -0.2417 -0.2895 148 TRP C CA  
18398 C C   . TRP C 148 ? 1.2202 1.3873 1.6262 -0.0393 -0.2820 -0.3278 148 TRP C C   
18399 O O   . TRP C 148 ? 1.1964 1.3825 1.7025 -0.0721 -0.2789 -0.3191 148 TRP C O   
18400 C CB  . TRP C 148 ? 1.0909 1.2246 1.4259 -0.0296 -0.1991 -0.2588 148 TRP C CB  
18401 C CG  . TRP C 148 ? 1.0388 1.1568 1.2926 -0.0052 -0.1695 -0.2339 148 TRP C CG  
18402 C CD1 . TRP C 148 ? 0.9953 1.1379 1.2516 -0.0001 -0.1381 -0.2015 148 TRP C CD1 
18403 C CD2 . TRP C 148 ? 1.0342 1.1103 1.1982 0.0188  -0.1706 -0.2399 148 TRP C CD2 
18404 N NE1 . TRP C 148 ? 0.9777 1.0927 1.1574 0.0215  -0.1232 -0.1903 148 TRP C NE1 
18405 C CE2 . TRP C 148 ? 1.0035 1.0798 1.1290 0.0323  -0.1404 -0.2095 148 TRP C CE2 
18406 C CE3 . TRP C 148 ? 1.0639 1.1051 1.1775 0.0333  -0.1947 -0.2676 148 TRP C CE3 
18407 C CZ2 . TRP C 148 ? 0.9858 1.0303 1.0358 0.0545  -0.1326 -0.2016 148 TRP C CZ2 
18408 C CZ3 . TRP C 148 ? 1.0691 1.0822 1.0993 0.0605  -0.1832 -0.2566 148 TRP C CZ3 
18409 C CH2 . TRP C 148 ? 1.0171 1.0328 1.0216 0.0683  -0.1519 -0.2217 148 TRP C CH2 
18420 N N   . LYS C 149 ? 1.3095 1.4546 1.6626 -0.0188 -0.3203 -0.3696 149 LYS C N   
18421 C CA  . LYS C 149 ? 1.3973 1.5296 1.8008 -0.0337 -0.3669 -0.4173 149 LYS C CA  
18422 C C   . LYS C 149 ? 1.4354 1.4965 1.7705 -0.0201 -0.3716 -0.4395 149 LYS C C   
18423 O O   . LYS C 149 ? 1.4573 1.5020 1.6881 0.0193  -0.3713 -0.4439 149 LYS C O   
18424 C CB  . LYS C 149 ? 1.4475 1.6260 1.8471 -0.0128 -0.4170 -0.4561 149 LYS C CB  
18425 C CG  . LYS C 149 ? 1.4122 1.6651 1.8601 -0.0155 -0.4121 -0.4331 149 LYS C CG  
18426 C CD  . LYS C 149 ? 1.4062 1.6998 1.9914 -0.0573 -0.4293 -0.4373 149 LYS C CD  
18427 C CE  . LYS C 149 ? 1.3901 1.7648 2.0131 -0.0504 -0.4350 -0.4237 149 LYS C CE  
18428 N NZ  . LYS C 149 ? 1.3935 1.8183 2.1586 -0.0907 -0.4442 -0.4157 149 LYS C NZ  
18442 N N   . ILE C 150 ? 1.4237 1.4436 1.8202 -0.0504 -0.3743 -0.4501 150 ILE C N   
18443 C CA  . ILE C 150 ? 1.4049 1.3537 1.7413 -0.0372 -0.3782 -0.4717 150 ILE C CA  
18444 C C   . ILE C 150 ? 1.4359 1.3696 1.7694 -0.0233 -0.4425 -0.5401 150 ILE C C   
18445 O O   . ILE C 150 ? 1.4967 1.4157 1.7274 0.0218  -0.4618 -0.5667 150 ILE C O   
18446 C CB  . ILE C 150 ? 1.3701 1.2761 1.7694 -0.0725 -0.3454 -0.4462 150 ILE C CB  
18447 C CG1 . ILE C 150 ? 1.2379 1.1594 1.6188 -0.0750 -0.2834 -0.3829 150 ILE C CG1 
18448 C CG2 . ILE C 150 ? 1.4715 1.3017 1.8166 -0.0583 -0.3557 -0.4751 150 ILE C CG2 
18449 C CD1 . ILE C 150 ? 1.1807 1.1004 1.6598 -0.1127 -0.2493 -0.3460 150 ILE C CD1 
18461 N N   . ASP C 151 ? 1.3977 1.3387 1.8467 -0.0593 -0.4771 -0.5682 151 ASP C N   
18462 C CA  . ASP C 151 ? 1.4440 1.3744 1.9100 -0.0505 -0.5466 -0.6405 151 ASP C CA  
18463 C C   . ASP C 151 ? 1.3911 1.3940 1.9508 -0.0693 -0.5840 -0.6573 151 ASP C C   
18464 O O   . ASP C 151 ? 1.4478 1.4491 2.0991 -0.0938 -0.6211 -0.6878 151 ASP C O   
18465 C CB  . ASP C 151 ? 1.5403 1.3986 2.0683 -0.0776 -0.5635 -0.6692 151 ASP C CB  
18466 C CG  . ASP C 151 ? 1.5872 1.3732 2.0041 -0.0451 -0.5444 -0.6726 151 ASP C CG  
18467 O OD1 . ASP C 151 ? 1.5856 1.3797 1.8756 0.0046  -0.5363 -0.6701 151 ASP C OD1 
18468 O OD2 . ASP C 151 ? 1.6201 1.3431 2.0802 -0.0679 -0.5363 -0.6745 151 ASP C OD2 
18473 N N   . GLY C 152 ? 1.3151 1.3827 1.8460 -0.0540 -0.5632 -0.6237 152 GLY C N   
18474 C CA  . GLY C 152 ? 1.3312 1.4754 1.9472 -0.0692 -0.5896 -0.6289 152 GLY C CA  
18475 C C   . GLY C 152 ? 1.3472 1.5260 2.0884 -0.1183 -0.5540 -0.5774 152 GLY C C   
18476 O O   . GLY C 152 ? 1.3409 1.5895 2.1628 -0.1324 -0.5718 -0.5750 152 GLY C O   
18480 N N   . SER C 153 ? 1.3707 1.5083 2.1294 -0.1404 -0.5033 -0.5337 153 SER C N   
18481 C CA  . SER C 153 ? 1.3487 1.5204 2.2197 -0.1796 -0.4628 -0.4780 153 SER C CA  
18482 C C   . SER C 153 ? 1.2455 1.4309 2.0460 -0.1614 -0.3985 -0.4177 153 SER C C   
18483 O O   . SER C 153 ? 1.1503 1.2929 1.8348 -0.1323 -0.3779 -0.4141 153 SER C O   
18484 C CB  . SER C 153 ? 1.4214 1.5390 2.3842 -0.2188 -0.4552 -0.4729 153 SER C CB  
18485 O OG  . SER C 153 ? 1.4543 1.4958 2.3217 -0.2013 -0.4308 -0.4719 153 SER C OG  
18491 N N   . GLU C 154 ? 1.2767 1.5240 2.1517 -0.1771 -0.3683 -0.3708 154 GLU C N   
18492 C CA  . GLU C 154 ? 1.2792 1.5462 2.0974 -0.1580 -0.3125 -0.3181 154 GLU C CA  
18493 C C   . GLU C 154 ? 1.2855 1.5197 2.1327 -0.1758 -0.2633 -0.2754 154 GLU C C   
18494 O O   . GLU C 154 ? 1.2977 1.5515 2.2642 -0.2082 -0.2527 -0.2512 154 GLU C O   
18495 C CB  . GLU C 154 ? 1.2563 1.6098 2.1313 -0.1569 -0.3050 -0.2905 154 GLU C CB  
18496 C CG  . GLU C 154 ? 1.2050 1.5790 1.9963 -0.1240 -0.2646 -0.2552 154 GLU C CG  
18497 C CD  . GLU C 154 ? 1.1813 1.6391 2.0212 -0.1166 -0.2622 -0.2340 154 GLU C CD  
18498 O OE1 . GLU C 154 ? 1.1722 1.6790 2.1250 -0.1406 -0.2501 -0.2051 154 GLU C OE1 
18499 O OE2 . GLU C 154 ? 1.1732 1.6493 1.9414 -0.0850 -0.2712 -0.2432 154 GLU C OE2 
18506 N N   . ARG C 155 ? 1.2613 1.4495 2.0043 -0.1535 -0.2325 -0.2631 155 ARG C N   
18507 C CA  . ARG C 155 ? 1.2274 1.3879 1.9861 -0.1641 -0.1846 -0.2222 155 ARG C CA  
18508 C C   . ARG C 155 ? 1.1314 1.3538 1.9238 -0.1594 -0.1385 -0.1664 155 ARG C C   
18509 O O   . ARG C 155 ? 1.1334 1.3836 2.0277 -0.1812 -0.1148 -0.1302 155 ARG C O   
18510 C CB  . ARG C 155 ? 1.2313 1.3281 1.8696 -0.1403 -0.1696 -0.2286 155 ARG C CB  
18511 C CG  . ARG C 155 ? 1.2201 1.2947 1.8616 -0.1446 -0.1183 -0.1850 155 ARG C CG  
18512 C CD  . ARG C 155 ? 1.2896 1.2863 1.8910 -0.1461 -0.1212 -0.2037 155 ARG C CD  
18513 N NE  . ARG C 155 ? 1.3244 1.3059 1.9493 -0.1531 -0.0728 -0.1595 155 ARG C NE  
18514 C CZ  . ARG C 155 ? 1.3984 1.3540 2.1104 -0.1793 -0.0650 -0.1484 155 ARG C CZ  
18515 N NH1 . ARG C 155 ? 1.4248 1.3731 2.1482 -0.1784 -0.0162 -0.1025 155 ARG C NH1 
18516 N NH2 . ARG C 155 ? 1.4361 1.3726 2.2264 -0.2048 -0.1067 -0.1831 155 ARG C NH2 
18530 N N   . GLN C 156 ? 1.0541 1.2992 1.7636 -0.1280 -0.1252 -0.1577 156 GLN C N   
18531 C CA  . GLN C 156 ? 1.0536 1.3617 1.7848 -0.1147 -0.0896 -0.1142 156 GLN C CA  
18532 C C   . GLN C 156 ? 1.0504 1.3577 1.8072 -0.1170 -0.0392 -0.0675 156 GLN C C   
18533 O O   . GLN C 156 ? 1.0436 1.4113 1.8565 -0.1116 -0.0092 -0.0262 156 GLN C O   
18534 C CB  . GLN C 156 ? 1.1112 1.4911 1.9441 -0.1280 -0.1066 -0.1084 156 GLN C CB  
18535 C CG  . GLN C 156 ? 1.1159 1.5686 1.9632 -0.1058 -0.0752 -0.0679 156 GLN C CG  
18536 C CD  . GLN C 156 ? 1.1405 1.6681 2.0920 -0.1183 -0.0925 -0.0603 156 GLN C CD  
18537 O OE1 . GLN C 156 ? 1.1629 1.6887 2.1695 -0.1430 -0.1346 -0.0921 156 GLN C OE1 
18538 N NE2 . GLN C 156 ? 1.1316 1.7288 2.1111 -0.0985 -0.0614 -0.0189 156 GLN C NE2 
18547 N N   . ASN C 157 ? 1.0681 1.3120 1.7823 -0.1201 -0.0275 -0.0706 157 ASN C N   
18548 C CA  . ASN C 157 ? 1.0650 1.3091 1.8043 -0.1200 0.0204  -0.0254 157 ASN C CA  
18549 C C   . ASN C 157 ? 1.0762 1.2906 1.7073 -0.0917 0.0461  -0.0185 157 ASN C C   
18550 O O   . ASN C 157 ? 1.0788 1.3305 1.7019 -0.0707 0.0837  0.0179  157 ASN C O   
18551 C CB  . ASN C 157 ? 1.0841 1.2843 1.8980 -0.1526 0.0173  -0.0256 157 ASN C CB  
18552 C CG  . ASN C 157 ? 1.0665 1.3019 1.9742 -0.1609 0.0636  0.0334  157 ASN C CG  
18553 O OD1 . ASN C 157 ? 1.0023 1.2748 1.8808 -0.1339 0.1060  0.0733  157 ASN C OD1 
18554 N ND2 . ASN C 157 ? 1.1199 1.3461 2.1447 -0.1959 0.0550  0.0399  157 ASN C ND2 
18561 N N   . GLY C 158 ? 1.0868 1.2397 1.6361 -0.0876 0.0262  -0.0520 158 GLY C N   
18562 C CA  . GLY C 158 ? 1.0898 1.2141 1.5495 -0.0651 0.0496  -0.0434 158 GLY C CA  
18563 C C   . GLY C 158 ? 1.0967 1.2192 1.4693 -0.0412 0.0331  -0.0639 158 GLY C C   
18564 O O   . GLY C 158 ? 1.0880 1.1730 1.3853 -0.0279 0.0377  -0.0691 158 GLY C O   
18568 N N   . VAL C 159 ? 0.9942 1.1623 1.6719 0.0279  0.0236  -0.0417 159 VAL C N   
18569 C CA  . VAL C 159 ? 0.9668 1.1445 1.5397 0.0380  -0.0035 -0.0524 159 VAL C CA  
18570 C C   . VAL C 159 ? 0.8720 1.0915 1.4144 0.0460  0.0435  -0.0129 159 VAL C C   
18571 O O   . VAL C 159 ? 0.7802 1.0347 1.4114 0.0437  0.0756  0.0137  159 VAL C O   
18572 C CB  . VAL C 159 ? 0.9754 1.1551 1.5963 0.0331  -0.0634 -0.0868 159 VAL C CB  
18573 C CG1 . VAL C 159 ? 0.9920 1.2088 1.7524 0.0209  -0.0503 -0.0718 159 VAL C CG1 
18574 C CG2 . VAL C 159 ? 0.9655 1.1487 1.4747 0.0465  -0.0882 -0.0928 159 VAL C CG2 
18584 N N   . LEU C 160 ? 0.8890 1.1075 1.3083 0.0573  0.0475  -0.0103 160 LEU C N   
18585 C CA  . LEU C 160 ? 0.8528 1.1088 1.2343 0.0665  0.0805  0.0158  160 LEU C CA  
18586 C C   . LEU C 160 ? 0.8383 1.0854 1.1384 0.0692  0.0443  -0.0001 160 LEU C C   
18587 O O   . LEU C 160 ? 0.8507 1.0661 1.0698 0.0711  0.0170  -0.0189 160 LEU C O   
18588 C CB  . LEU C 160 ? 0.8657 1.1337 1.1841 0.0785  0.1312  0.0383  160 LEU C CB  
18589 C CG  . LEU C 160 ? 0.9116 1.1980 1.3026 0.0844  0.1817  0.0670  160 LEU C CG  
18590 C CD1 . LEU C 160 ? 0.9081 1.2088 1.2186 0.1026  0.2261  0.0842  160 LEU C CD1 
18591 C CD2 . LEU C 160 ? 0.8836 1.2151 1.3689 0.0881  0.2047  0.0913  160 LEU C CD2 
18603 N N   . ASN C 161 ? 0.8084 1.0835 1.1300 0.0722  0.0458  0.0094  161 ASN C N   
18604 C CA  . ASN C 161 ? 0.7969 1.0602 1.0575 0.0753  0.0123  -0.0021 161 ASN C CA  
18605 C C   . ASN C 161 ? 0.7360 1.0238 0.9501 0.0830  0.0430  0.0161  161 ASN C C   
18606 O O   . ASN C 161 ? 0.6866 1.0118 0.9345 0.0897  0.0845  0.0349  161 ASN C O   
18607 C CB  . ASN C 161 ? 0.7891 1.0577 1.1230 0.0737  -0.0261 -0.0154 161 ASN C CB  
18608 C CG  . ASN C 161 ? 0.8209 1.0672 1.2041 0.0673  -0.0655 -0.0428 161 ASN C CG  
18609 O OD1 . ASN C 161 ? 0.8951 1.1114 1.2306 0.0672  -0.0767 -0.0573 161 ASN C OD1 
18610 N ND2 . ASN C 161 ? 0.7986 1.0629 1.2810 0.0636  -0.0885 -0.0534 161 ASN C ND2 
18617 N N   . SER C 162 ? 0.7681 1.0351 0.9061 0.0844  0.0219  0.0097  162 SER C N   
18618 C CA  . SER C 162 ? 0.7911 1.0747 0.8890 0.0894  0.0438  0.0205  162 SER C CA  
18619 C C   . SER C 162 ? 0.8479 1.1032 0.9050 0.0900  0.0092  0.0141  162 SER C C   
18620 O O   . SER C 162 ? 0.8689 1.0877 0.8728 0.0889  -0.0196 0.0058  162 SER C O   
18621 C CB  . SER C 162 ? 0.7622 1.0483 0.7889 0.0890  0.0752  0.0259  162 SER C CB  
18622 O OG  . SER C 162 ? 0.7649 1.0714 0.7660 0.0931  0.0946  0.0307  162 SER C OG  
18628 N N   . TRP C 163 ? 0.8634 1.1357 0.9436 0.0959  0.0126  0.0186  163 TRP C N   
18629 C CA  . TRP C 163 ? 0.8756 1.1193 0.9240 0.0990  -0.0162 0.0161  163 TRP C CA  
18630 C C   . TRP C 163 ? 0.8316 1.0732 0.8317 0.0975  0.0055  0.0226  163 TRP C C   
18631 O O   . TRP C 163 ? 0.8056 1.0820 0.8165 0.0989  0.0397  0.0246  163 TRP C O   
18632 C CB  . TRP C 163 ? 0.8593 1.1202 0.9792 0.1086  -0.0353 0.0126  163 TRP C CB  
18633 C CG  . TRP C 163 ? 0.8909 1.1589 1.0746 0.1083  -0.0591 0.0029  163 TRP C CG  
18634 C CD1 . TRP C 163 ? 0.9910 1.2367 1.1793 0.1134  -0.1042 -0.0108 163 TRP C CD1 
18635 C CD2 . TRP C 163 ? 0.8103 1.1112 1.0688 0.1037  -0.0392 0.0051  163 TRP C CD2 
18636 N NE1 . TRP C 163 ? 0.9906 1.2558 1.2582 0.1098  -0.1166 -0.0222 163 TRP C NE1 
18637 C CE2 . TRP C 163 ? 0.8650 1.1611 1.1796 0.1019  -0.0755 -0.0104 163 TRP C CE2 
18638 C CE3 . TRP C 163 ? 0.7136 1.0480 0.9990 0.1032  0.0066  0.0194  163 TRP C CE3 
18639 C CZ2 . TRP C 163 ? 0.7844 1.1046 1.1899 0.0944  -0.0664 -0.0115 163 TRP C CZ2 
18640 C CZ3 . TRP C 163 ? 0.6699 1.0259 1.0374 0.0991  0.0186  0.0236  163 TRP C CZ3 
18641 C CH2 . TRP C 163 ? 0.6811 1.0283 1.1124 0.0922  -0.0172 0.0085  163 TRP C CH2 
18652 N N   . THR C 164 ? 0.8307 1.0319 0.7803 0.0965  -0.0147 0.0253  164 THR C N   
18653 C CA  . THR C 164 ? 0.8211 1.0130 0.7374 0.0920  0.0016  0.0305  164 THR C CA  
18654 C C   . THR C 164 ? 0.8844 1.0734 0.8377 0.1015  -0.0118 0.0276  164 THR C C   
18655 O O   . THR C 164 ? 0.9185 1.0960 0.8963 0.1116  -0.0412 0.0259  164 THR C O   
18656 C CB  . THR C 164 ? 0.8358 0.9815 0.6742 0.0848  -0.0058 0.0416  164 THR C CB  
18657 O OG1 . THR C 164 ? 0.8974 1.0049 0.7206 0.0953  -0.0422 0.0458  164 THR C OG1 
18658 C CG2 . THR C 164 ? 0.8322 0.9818 0.6283 0.0795  0.0048  0.0426  164 THR C CG2 
18666 N N   . ASP C 165 ? 0.9011 1.1027 0.8603 0.1004  0.0081  0.0236  165 ASP C N   
18667 C CA  . ASP C 165 ? 0.9343 1.1208 0.9164 0.1095  -0.0068 0.0195  165 ASP C CA  
18668 C C   . ASP C 165 ? 0.8969 1.0192 0.8334 0.1071  -0.0326 0.0329  165 ASP C C   
18669 O O   . ASP C 165 ? 0.8716 0.9645 0.7514 0.0970  -0.0307 0.0458  165 ASP C O   
18670 C CB  . ASP C 165 ? 1.0523 1.2569 1.0437 0.1075  0.0159  0.0080  165 ASP C CB  
18671 C CG  . ASP C 165 ? 1.0936 1.3673 1.1296 0.1216  0.0393  -0.0058 165 ASP C CG  
18672 O OD1 . ASP C 165 ? 1.1026 1.4067 1.1807 0.1366  0.0349  -0.0045 165 ASP C OD1 
18673 O OD2 . ASP C 165 ? 1.1044 1.4051 1.1352 0.1200  0.0629  -0.0174 165 ASP C OD2 
18678 N N   . GLN C 166 ? 0.9161 1.0185 0.8746 0.1209  -0.0559 0.0314  166 GLN C N   
18679 C CA  . GLN C 166 ? 0.9770 1.0175 0.8908 0.1252  -0.0792 0.0472  166 GLN C CA  
18680 C C   . GLN C 166 ? 1.0055 1.0071 0.8739 0.1085  -0.0591 0.0622  166 GLN C C   
18681 O O   . GLN C 166 ? 1.0219 1.0299 0.9147 0.0994  -0.0407 0.0536  166 GLN C O   
18682 C CB  . GLN C 166 ? 0.9871 1.0131 0.9338 0.1448  -0.1037 0.0422  166 GLN C CB  
18683 C CG  . GLN C 166 ? 1.0439 1.0036 0.9419 0.1552  -0.1264 0.0616  166 GLN C CG  
18684 C CD  . GLN C 166 ? 1.0668 1.0112 0.9954 0.1778  -0.1512 0.0559  166 GLN C CD  
18685 O OE1 . GLN C 166 ? 1.0678 1.0197 1.0356 0.1792  -0.1436 0.0438  166 GLN C OE1 
18686 N NE2 . GLN C 166 ? 1.0847 1.0100 0.9945 0.1992  -0.1831 0.0616  166 GLN C NE2 
18695 N N   . ASP C 167 ? 1.0611 1.0258 0.8666 0.1065  -0.0629 0.0837  167 ASP C N   
18696 C CA  . ASP C 167 ? 1.1487 1.0765 0.9131 0.0911  -0.0412 0.1049  167 ASP C CA  
18697 C C   . ASP C 167 ? 1.2097 1.0930 0.9947 0.0926  -0.0443 0.1118  167 ASP C C   
18698 O O   . ASP C 167 ? 1.2364 1.1021 1.0395 0.1125  -0.0702 0.1086  167 ASP C O   
18699 C CB  . ASP C 167 ? 1.2589 1.1556 0.9485 0.0987  -0.0477 0.1308  167 ASP C CB  
18700 C CG  . ASP C 167 ? 1.3380 1.2168 0.9867 0.0802  -0.0158 0.1542  167 ASP C CG  
18701 O OD1 . ASP C 167 ? 1.3838 1.2288 1.0453 0.0693  -0.0015 0.1683  167 ASP C OD1 
18702 O OD2 . ASP C 167 ? 1.3546 1.2543 0.9634 0.0763  -0.0048 0.1578  167 ASP C OD2 
18707 N N   . SER C 168 ? 1.2426 1.1087 1.0304 0.0715  -0.0178 0.1196  168 SER C N   
18708 C CA  . SER C 168 ? 1.3025 1.1225 1.1205 0.0690  -0.0183 0.1235  168 SER C CA  
18709 C C   . SER C 168 ? 1.3695 1.1166 1.1376 0.0748  -0.0196 0.1659  168 SER C C   
18710 O O   . SER C 168 ? 1.4051 1.1059 1.1805 0.0918  -0.0380 0.1743  168 SER C O   
18711 C CB  . SER C 168 ? 1.3207 1.1601 1.1821 0.0429  0.0093  0.1058  168 SER C CB  
18712 O OG  . SER C 168 ? 1.2704 1.1745 1.1809 0.0476  0.0081  0.0659  168 SER C OG  
18718 N N   . LYS C 169 ? 1.4088 1.1464 1.1237 0.0648  0.0012  0.1948  169 LYS C N   
18719 C CA  . LYS C 169 ? 1.5383 1.2115 1.1999 0.0750  0.0063  0.2417  169 LYS C CA  
18720 C C   . LYS C 169 ? 1.5306 1.1832 1.1510 0.1139  -0.0296 0.2504  169 LYS C C   
18721 O O   . LYS C 169 ? 1.5980 1.1999 1.2219 0.1316  -0.0433 0.2644  169 LYS C O   
18722 C CB  . LYS C 169 ? 1.6589 1.3413 1.2657 0.0639  0.0345  0.2696  169 LYS C CB  
18723 C CG  . LYS C 169 ? 1.7053 1.4206 1.3524 0.0266  0.0688  0.2570  169 LYS C CG  
18724 C CD  . LYS C 169 ? 1.7776 1.5094 1.3663 0.0200  0.0951  0.2841  169 LYS C CD  
18725 C CE  . LYS C 169 ? 1.7645 1.5340 1.3957 -0.0159 0.1289  0.2704  169 LYS C CE  
18726 N NZ  . LYS C 169 ? 1.8031 1.5903 1.3771 -0.0208 0.1562  0.2992  169 LYS C NZ  
18740 N N   . ASP C 170 ? 1.4750 1.1669 1.0592 0.1288  -0.0464 0.2395  170 ASP C N   
18741 C CA  . ASP C 170 ? 1.4396 1.1333 1.0077 0.1635  -0.0868 0.2296  170 ASP C CA  
18742 C C   . ASP C 170 ? 1.3843 1.1283 1.0234 0.1591  -0.1043 0.1855  170 ASP C C   
18743 O O   . ASP C 170 ? 1.4154 1.1991 1.0995 0.1341  -0.0847 0.1642  170 ASP C O   
18744 C CB  . ASP C 170 ? 1.4137 1.1241 0.9135 0.1840  -0.0994 0.2365  170 ASP C CB  
18745 C CG  . ASP C 170 ? 1.3385 1.1054 0.8485 0.1629  -0.0875 0.2126  170 ASP C CG  
18746 O OD1 . ASP C 170 ? 1.2753 1.0854 0.8369 0.1587  -0.1025 0.1773  170 ASP C OD1 
18747 O OD2 . ASP C 170 ? 1.3736 1.1422 0.8410 0.1521  -0.0613 0.2314  170 ASP C OD2 
18752 N N   . SER C 171 ? 1.3126 1.0586 0.9620 0.1869  -0.1402 0.1732  171 SER C N   
18753 C CA  . SER C 171 ? 1.2410 1.0360 0.9614 0.1873  -0.1561 0.1369  171 SER C CA  
18754 C C   . SER C 171 ? 1.2714 1.1171 0.9976 0.1935  -0.1744 0.1161  171 SER C C   
18755 O O   . SER C 171 ? 1.2968 1.1736 1.0695 0.2071  -0.1996 0.0941  171 SER C O   
18756 C CB  . SER C 171 ? 1.2413 1.0109 0.9846 0.2126  -0.1826 0.1342  171 SER C CB  
18757 O OG  . SER C 171 ? 1.2553 0.9761 1.0063 0.2048  -0.1657 0.1489  171 SER C OG  
18763 N N   . THR C 172 ? 1.2830 1.1385 0.9677 0.1835  -0.1616 0.1219  172 THR C N   
18764 C CA  . THR C 172 ? 1.2412 1.1356 0.9291 0.1895  -0.1802 0.1018  172 THR C CA  
18765 C C   . THR C 172 ? 1.1204 1.0665 0.8616 0.1640  -0.1570 0.0821  172 THR C C   
18766 O O   . THR C 172 ? 1.0619 1.0175 0.8258 0.1444  -0.1262 0.0836  172 THR C O   
18767 C CB  . THR C 172 ? 1.2808 1.1551 0.8859 0.2012  -0.1837 0.1178  172 THR C CB  
18768 O OG1 . THR C 172 ? 1.2572 1.1314 0.8353 0.1765  -0.1446 0.1326  172 THR C OG1 
18769 C CG2 . THR C 172 ? 1.3527 1.1753 0.8963 0.2318  -0.1997 0.1449  172 THR C CG2 
18777 N N   . TYR C 173 ? 1.0999 1.0799 0.8629 0.1672  -0.1729 0.0623  173 TYR C N   
18778 C CA  . TYR C 173 ? 1.0487 1.0751 0.8588 0.1481  -0.1512 0.0474  173 TYR C CA  
18779 C C   . TYR C 173 ? 1.0311 1.0591 0.7971 0.1457  -0.1514 0.0445  173 TYR C C   
18780 O O   . TYR C 173 ? 1.0736 1.0745 0.7793 0.1628  -0.1740 0.0493  173 TYR C O   
18781 C CB  . TYR C 173 ? 0.9991 1.0667 0.8960 0.1530  -0.1668 0.0267  173 TYR C CB  
18782 C CG  . TYR C 173 ? 0.9764 1.0507 0.9190 0.1598  -0.1672 0.0267  173 TYR C CG  
18783 C CD1 . TYR C 173 ? 1.0455 1.0918 0.9782 0.1809  -0.1983 0.0287  173 TYR C CD1 
18784 C CD2 . TYR C 173 ? 0.9358 1.0469 0.9285 0.1505  -0.1374 0.0233  173 TYR C CD2 
18785 C CE1 . TYR C 173 ? 1.0434 1.0948 1.0164 0.1900  -0.2003 0.0267  173 TYR C CE1 
18786 C CE2 . TYR C 173 ? 0.9592 1.0795 0.9916 0.1617  -0.1401 0.0199  173 TYR C CE2 
18787 C CZ  . TYR C 173 ? 1.0119 1.1008 1.0352 0.1802  -0.1718 0.0213  173 TYR C CZ  
18788 O OH  . TYR C 173 ? 1.0197 1.1170 1.0815 0.1940  -0.1758 0.0160  173 TYR C OH  
18798 N N   . SER C 174 ? 0.9759 1.0373 0.7697 0.1289  -0.1262 0.0364  174 SER C N   
18799 C CA  . SER C 174 ? 0.9969 1.0616 0.7555 0.1271  -0.1253 0.0305  174 SER C CA  
18800 C C   . SER C 174 ? 0.9341 1.0383 0.7637 0.1173  -0.1156 0.0136  174 SER C C   
18801 O O   . SER C 174 ? 0.9136 1.0476 0.8074 0.1102  -0.0965 0.0133  174 SER C O   
18802 C CB  . SER C 174 ? 1.0056 1.0589 0.6955 0.1167  -0.0930 0.0486  174 SER C CB  
18803 O OG  . SER C 174 ? 1.0590 1.0729 0.6841 0.1272  -0.1006 0.0693  174 SER C OG  
18809 N N   . PHE C 175 ? 0.9449 1.0488 0.7619 0.1200  -0.1280 0.0005  175 PHE C N   
18810 C CA  . PHE C 175 ? 0.9393 1.0709 0.8314 0.1132  -0.1266 -0.0160 175 PHE C CA  
18811 C C   . PHE C 175 ? 0.9550 1.0818 0.8064 0.1104  -0.1162 -0.0213 175 PHE C C   
18812 O O   . PHE C 175 ? 1.0285 1.1311 0.8105 0.1230  -0.1385 -0.0271 175 PHE C O   
18813 C CB  . PHE C 175 ? 0.9763 1.1092 0.9251 0.1243  -0.1722 -0.0382 175 PHE C CB  
18814 C CG  . PHE C 175 ? 0.9829 1.1472 1.0376 0.1139  -0.1682 -0.0513 175 PHE C CG  
18815 C CD1 . PHE C 175 ? 1.0763 1.2463 1.1471 0.1037  -0.1484 -0.0551 175 PHE C CD1 
18816 C CD2 . PHE C 175 ? 0.9710 1.1589 1.1125 0.1155  -0.1833 -0.0577 175 PHE C CD2 
18817 C CE1 . PHE C 175 ? 1.1046 1.2992 1.2796 0.0939  -0.1409 -0.0618 175 PHE C CE1 
18818 C CE2 . PHE C 175 ? 0.9950 1.2137 1.2425 0.1051  -0.1759 -0.0649 175 PHE C CE2 
18819 C CZ  . PHE C 175 ? 1.0521 1.2722 1.3183 0.0935  -0.1534 -0.0654 175 PHE C CZ  
18829 N N   . SER C 176 ? 0.9012 1.0526 0.7922 0.0984  -0.0819 -0.0184 176 SER C N   
18830 C CA  . SER C 176 ? 0.9142 1.0623 0.7797 0.0971  -0.0713 -0.0251 176 SER C CA  
18831 C C   . SER C 176 ? 0.9018 1.0642 0.8619 0.0917  -0.0717 -0.0374 176 SER C C   
18832 O O   . SER C 176 ? 0.8816 1.0727 0.9135 0.0848  -0.0451 -0.0259 176 SER C O   
18833 C CB  . SER C 176 ? 0.8733 1.0360 0.6924 0.0907  -0.0245 -0.0075 176 SER C CB  
18834 O OG  . SER C 176 ? 0.8617 1.0256 0.6692 0.0913  -0.0112 -0.0137 176 SER C OG  
18840 N N   . SER C 177 ? 0.9064 1.0499 0.8692 0.0967  -0.1011 -0.0606 177 SER C N   
18841 C CA  . SER C 177 ? 0.8959 1.0455 0.9557 0.0892  -0.1033 -0.0742 177 SER C CA  
18842 C C   . SER C 177 ? 0.8919 1.0232 0.9156 0.0920  -0.0968 -0.0841 177 SER C C   
18843 O O   . SER C 177 ? 0.9203 1.0292 0.8637 0.1057  -0.1239 -0.1003 177 SER C O   
18844 C CB  . SER C 177 ? 0.9333 1.0776 1.0589 0.0929  -0.1559 -0.1033 177 SER C CB  
18845 O OG  . SER C 177 ? 0.9272 1.0784 1.1638 0.0813  -0.1557 -0.1157 177 SER C OG  
18851 N N   . THR C 178 ? 0.8755 1.0172 0.9564 0.0831  -0.0601 -0.0728 178 THR C N   
18852 C CA  . THR C 178 ? 0.9351 1.0593 0.9830 0.0872  -0.0466 -0.0782 178 THR C CA  
18853 C C   . THR C 178 ? 0.9210 1.0372 1.0819 0.0783  -0.0458 -0.0876 178 THR C C   
18854 O O   . THR C 178 ? 0.8871 1.0258 1.1277 0.0693  -0.0076 -0.0628 178 THR C O   
18855 C CB  . THR C 178 ? 0.9214 1.0654 0.9107 0.0894  0.0080  -0.0489 178 THR C CB  
18856 O OG1 . THR C 178 ? 0.9254 1.0787 0.8308 0.0929  0.0089  -0.0396 178 THR C OG1 
18857 C CG2 . THR C 178 ? 0.9406 1.0661 0.8795 0.0981  0.0184  -0.0560 178 THR C CG2 
18865 N N   . LEU C 179 ? 0.9403 1.0255 1.1110 0.0828  -0.0872 -0.1231 179 LEU C N   
18866 C CA  . LEU C 179 ? 0.9433 1.0119 1.2219 0.0731  -0.0876 -0.1357 179 LEU C CA  
18867 C C   . LEU C 179 ? 0.9533 1.0023 1.1834 0.0807  -0.0555 -0.1271 179 LEU C C   
18868 O O   . LEU C 179 ? 0.9714 0.9986 1.1107 0.0965  -0.0789 -0.1495 179 LEU C O   
18869 C CB  . LEU C 179 ? 0.9803 1.0266 1.3058 0.0757  -0.1545 -0.1865 179 LEU C CB  
18870 C CG  . LEU C 179 ? 0.9725 0.9961 1.4221 0.0630  -0.1603 -0.2060 179 LEU C CG  
18871 C CD1 . LEU C 179 ? 0.9459 0.9948 1.5376 0.0399  -0.1292 -0.1794 179 LEU C CD1 
18872 C CD2 . LEU C 179 ? 1.0335 1.0344 1.5068 0.0724  -0.2335 -0.2674 179 LEU C CD2 
18884 N N   . THR C 180 ? 0.9722 1.0315 1.2596 0.0736  -0.0011 -0.0935 180 THR C N   
18885 C CA  . THR C 180 ? 1.0695 1.1127 1.3167 0.0838  0.0354  -0.0806 180 THR C CA  
18886 C C   . THR C 180 ? 1.0500 1.0575 1.4066 0.0757  0.0321  -0.0925 180 THR C C   
18887 O O   . THR C 180 ? 1.0250 1.0405 1.5080 0.0596  0.0465  -0.0779 180 THR C O   
18888 C CB  . THR C 180 ? 1.1578 1.2387 1.3839 0.0891  0.1016  -0.0331 180 THR C CB  
18889 O OG1 . THR C 180 ? 1.2338 1.3378 1.5775 0.0780  0.1287  -0.0067 180 THR C OG1 
18890 C CG2 . THR C 180 ? 1.1180 1.2304 1.2416 0.0954  0.1028  -0.0265 180 THR C CG2 
18898 N N   . LEU C 181 ? 1.0754 1.0438 1.3871 0.0875  0.0136  -0.1188 181 LEU C N   
18899 C CA  . LEU C 181 ? 1.0895 1.0145 1.4987 0.0815  0.0074  -0.1352 181 LEU C CA  
18900 C C   . LEU C 181 ? 1.1039 1.0066 1.4469 0.0998  0.0455  -0.1194 181 LEU C C   
18901 O O   . LEU C 181 ? 1.0732 0.9998 1.2980 0.1166  0.0733  -0.0993 181 LEU C O   
18902 C CB  . LEU C 181 ? 1.1444 1.0373 1.5756 0.0825  -0.0690 -0.1984 181 LEU C CB  
18903 C CG  . LEU C 181 ? 1.1645 1.0815 1.6138 0.0764  -0.1202 -0.2250 181 LEU C CG  
18904 C CD1 . LEU C 181 ? 1.2114 1.1022 1.6276 0.0936  -0.1951 -0.2896 181 LEU C CD1 
18905 C CD2 . LEU C 181 ? 1.1579 1.0899 1.7685 0.0495  -0.1139 -0.2152 181 LEU C CD2 
18917 N N   . THR C 182 ? 1.1586 1.0153 1.5836 0.0968  0.0462  -0.1299 182 THR C N   
18918 C CA  . THR C 182 ? 1.2070 1.0313 1.5642 0.1184  0.0664  -0.1286 182 THR C CA  
18919 C C   . THR C 182 ? 1.2312 1.0302 1.4978 0.1365  0.0036  -0.1855 182 THR C C   
18920 O O   . THR C 182 ? 1.2540 1.0477 1.5455 0.1313  -0.0580 -0.2303 182 THR C O   
18921 C CB  . THR C 182 ? 1.3163 1.0945 1.7990 0.1102  0.0934  -0.1156 182 THR C CB  
18922 O OG1 . THR C 182 ? 1.4274 1.1672 2.0228 0.0924  0.0354  -0.1653 182 THR C OG1 
18923 C CG2 . THR C 182 ? 1.2603 1.0688 1.8316 0.0983  0.1599  -0.0537 182 THR C CG2 
18931 N N   . LYS C 183 ? 1.2463 1.0345 1.4030 0.1625  0.0194  -0.1840 183 LYS C N   
18932 C CA  . LYS C 183 ? 1.2961 1.0627 1.3635 0.1859  -0.0366 -0.2359 183 LYS C CA  
18933 C C   . LYS C 183 ? 1.3692 1.0801 1.5398 0.1821  -0.0886 -0.2877 183 LYS C C   
18934 O O   . LYS C 183 ? 1.4534 1.1565 1.5970 0.1946  -0.1551 -0.3422 183 LYS C O   
18935 C CB  . LYS C 183 ? 1.2937 1.0596 1.2375 0.2154  -0.0060 -0.2234 183 LYS C CB  
18936 C CG  . LYS C 183 ? 1.3472 1.0905 1.2014 0.2450  -0.0608 -0.2760 183 LYS C CG  
18937 C CD  . LYS C 183 ? 1.4060 1.1483 1.1495 0.2752  -0.0291 -0.2641 183 LYS C CD  
18938 C CE  . LYS C 183 ? 1.5843 1.2792 1.3001 0.3035  -0.0788 -0.3184 183 LYS C CE  
18939 N NZ  . LYS C 183 ? 1.6733 1.3912 1.2339 0.3402  -0.0740 -0.3214 183 LYS C NZ  
18953 N N   . ASP C 184 ? 1.3495 1.0221 1.6416 0.1672  -0.0590 -0.2719 184 ASP C N   
18954 C CA  . ASP C 184 ? 1.4221 1.0396 1.8369 0.1583  -0.1064 -0.3218 184 ASP C CA  
18955 C C   . ASP C 184 ? 1.4098 1.0454 1.9138 0.1372  -0.1611 -0.3578 184 ASP C C   
18956 O O   . ASP C 184 ? 1.4392 1.0616 1.9353 0.1503  -0.2337 -0.4232 184 ASP C O   
18957 C CB  . ASP C 184 ? 1.4358 1.0123 1.9803 0.1412  -0.0533 -0.2853 184 ASP C CB  
18958 C CG  . ASP C 184 ? 1.4559 1.0072 1.9153 0.1684  -0.0057 -0.2569 184 ASP C CG  
18959 O OD1 . ASP C 184 ? 1.4681 1.0339 1.7738 0.1990  -0.0187 -0.2718 184 ASP C OD1 
18960 O OD2 . ASP C 184 ? 1.4580 0.9769 2.0049 0.1612  0.0465  -0.2176 184 ASP C OD2 
18965 N N   . GLU C 185 ? 1.3615 1.0323 1.9470 0.1090  -0.1280 -0.3169 185 GLU C N   
18966 C CA  . GLU C 185 ? 1.3746 1.0658 2.0554 0.0889  -0.1765 -0.3486 185 GLU C CA  
18967 C C   . GLU C 185 ? 1.3968 1.1180 1.9556 0.1116  -0.2349 -0.3878 185 GLU C C   
18968 O O   . GLU C 185 ? 1.4493 1.1697 2.0580 0.1127  -0.3022 -0.4444 185 GLU C O   
18969 C CB  . GLU C 185 ? 1.3056 1.0379 2.0707 0.0610  -0.1247 -0.2913 185 GLU C CB  
18970 C CG  . GLU C 185 ? 1.3346 1.0846 2.2359 0.0362  -0.1672 -0.3205 185 GLU C CG  
18971 C CD  . GLU C 185 ? 1.3036 1.0966 2.2904 0.0120  -0.1129 -0.2619 185 GLU C CD  
18972 O OE1 . GLU C 185 ? 1.2705 1.0950 2.1693 0.0208  -0.0575 -0.2074 185 GLU C OE1 
18973 O OE2 . GLU C 185 ? 1.3036 1.1027 2.4485 -0.0140 -0.1265 -0.2725 185 GLU C OE2 
18980 N N   . TYR C 186 ? 1.3625 1.1126 1.7639 0.1316  -0.2094 -0.3583 186 TYR C N   
18981 C CA  . TYR C 186 ? 1.3869 1.1634 1.6683 0.1557  -0.2577 -0.3873 186 TYR C CA  
18982 C C   . TYR C 186 ? 1.4812 1.2259 1.7190 0.1873  -0.3231 -0.4541 186 TYR C C   
18983 O O   . TYR C 186 ? 1.5398 1.2948 1.7683 0.2029  -0.3877 -0.5026 186 TYR C O   
18984 C CB  . TYR C 186 ? 1.3381 1.1488 1.4702 0.1689  -0.2124 -0.3405 186 TYR C CB  
18985 C CG  . TYR C 186 ? 1.3554 1.1877 1.3559 0.1975  -0.2552 -0.3643 186 TYR C CG  
18986 C CD1 . TYR C 186 ? 1.3295 1.1917 1.3293 0.1936  -0.2816 -0.3668 186 TYR C CD1 
18987 C CD2 . TYR C 186 ? 1.4068 1.2303 1.2833 0.2316  -0.2676 -0.3816 186 TYR C CD2 
18988 C CE1 . TYR C 186 ? 1.3611 1.2411 1.2409 0.2233  -0.3164 -0.3823 186 TYR C CE1 
18989 C CE2 . TYR C 186 ? 1.4403 1.2865 1.1974 0.2611  -0.3018 -0.3971 186 TYR C CE2 
18990 C CZ  . TYR C 186 ? 1.4113 1.2842 1.1711 0.2570  -0.3251 -0.3959 186 TYR C CZ  
18991 O OH  . TYR C 186 ? 1.4290 1.3228 1.0698 0.2896  -0.3547 -0.4051 186 TYR C OH  
19001 N N   . GLU C 187 ? 1.4928 1.2005 1.7004 0.2019  -0.3083 -0.4589 187 GLU C N   
19002 C CA  . GLU C 187 ? 1.5735 1.2523 1.7281 0.2380  -0.3687 -0.5229 187 GLU C CA  
19003 C C   . GLU C 187 ? 1.6445 1.2872 1.9457 0.2302  -0.4299 -0.5883 187 GLU C C   
19004 O O   . GLU C 187 ? 1.7822 1.4044 2.0497 0.2636  -0.4919 -0.6528 187 GLU C O   
19005 C CB  . GLU C 187 ? 1.5995 1.2491 1.6804 0.2573  -0.3330 -0.5082 187 GLU C CB  
19006 C CG  . GLU C 187 ? 1.5788 1.2689 1.4970 0.2751  -0.2880 -0.4613 187 GLU C CG  
19007 C CD  . GLU C 187 ? 1.6115 1.2778 1.4528 0.2996  -0.2595 -0.4540 187 GLU C CD  
19008 O OE1 . GLU C 187 ? 1.6393 1.2546 1.5672 0.2940  -0.2516 -0.4636 187 GLU C OE1 
19009 O OE2 . GLU C 187 ? 1.6012 1.3001 1.2982 0.3251  -0.2442 -0.4377 187 GLU C OE2 
19016 N N   . ARG C 188 ? 1.5527 1.1908 2.0182 0.1890  -0.4155 -0.5755 188 ARG C N   
19017 C CA  . ARG C 188 ? 1.5572 1.1642 2.1804 0.1771  -0.4731 -0.6395 188 ARG C CA  
19018 C C   . ARG C 188 ? 1.5705 1.2139 2.2009 0.1896  -0.5475 -0.6947 188 ARG C C   
19019 O O   . ARG C 188 ? 1.6114 1.2498 2.2996 0.2042  -0.6110 -0.7566 188 ARG C O   
19020 C CB  . ARG C 188 ? 1.4982 1.0891 2.3055 0.1281  -0.4251 -0.6015 188 ARG C CB  
19021 C CG  . ARG C 188 ? 1.4962 1.0386 2.3256 0.1212  -0.3622 -0.5599 188 ARG C CG  
19022 C CD  . ARG C 188 ? 1.5029 1.0124 2.5435 0.0798  -0.3369 -0.5466 188 ARG C CD  
19023 N NE  . ARG C 188 ? 1.5644 1.0078 2.6352 0.0837  -0.3053 -0.5364 188 ARG C NE  
19024 C CZ  . ARG C 188 ? 1.6806 1.0696 2.7963 0.0957  -0.3575 -0.6011 188 ARG C CZ  
19025 N NH1 . ARG C 188 ? 1.7181 1.1401 2.8364 0.1064  -0.4378 -0.6669 188 ARG C NH1 
19026 N NH2 . ARG C 188 ? 1.7390 1.0727 2.8724 0.0994  -0.3204 -0.5801 188 ARG C NH2 
19040 N N   . HIS C 189 ? 1.5472 1.2426 2.1156 0.1869  -0.5330 -0.6590 189 HIS C N   
19041 C CA  . HIS C 189 ? 1.5946 1.3275 2.1592 0.2028  -0.5979 -0.7033 189 HIS C CA  
19042 C C   . HIS C 189 ? 1.6723 1.4294 2.0391 0.2529  -0.6220 -0.7104 189 HIS C C   
19043 O O   . HIS C 189 ? 1.6980 1.4499 1.9370 0.2686  -0.5821 -0.6744 189 HIS C O   
19044 C CB  . HIS C 189 ? 1.4702 1.2426 2.1110 0.1675  -0.5675 -0.6593 189 HIS C CB  
19045 C CG  . HIS C 189 ? 1.3946 1.1507 2.2217 0.1193  -0.5293 -0.6365 189 HIS C CG  
19046 N ND1 . HIS C 189 ? 1.3357 1.0769 2.1763 0.0959  -0.4473 -0.5673 189 HIS C ND1 
19047 C CD2 . HIS C 189 ? 1.3990 1.1545 2.4092 0.0926  -0.5600 -0.6722 189 HIS C CD2 
19048 C CE1 . HIS C 189 ? 1.3238 1.0545 2.3444 0.0582  -0.4259 -0.5564 189 HIS C CE1 
19049 N NE2 . HIS C 189 ? 1.3644 1.1035 2.4954 0.0527  -0.4928 -0.6192 189 HIS C NE2 
19057 N N   . ASN C 190 ? 1.6816 1.4804 2.0265 0.2801  -0.6707 -0.7340 190 ASN C N   
19058 C CA  . ASN C 190 ? 1.6814 1.5102 1.8586 0.3329  -0.6836 -0.7252 190 ASN C CA  
19059 C C   . ASN C 190 ? 1.6470 1.5145 1.7501 0.3371  -0.6718 -0.6890 190 ASN C C   
19060 O O   . ASN C 190 ? 1.6430 1.5227 1.6060 0.3529  -0.6379 -0.6456 190 ASN C O   
19061 C CB  . ASN C 190 ? 1.7069 1.5475 1.9065 0.3760  -0.7405 -0.7746 190 ASN C CB  
19062 C CG  . ASN C 190 ? 1.7048 1.5537 1.7539 0.4300  -0.7415 -0.7676 190 ASN C CG  
19063 O OD1 . ASN C 190 ? 1.6663 1.4901 1.6847 0.4366  -0.7310 -0.7705 190 ASN C OD1 
19064 N ND2 . ASN C 190 ? 1.7455 1.6284 1.7053 0.4692  -0.7496 -0.7555 190 ASN C ND2 
19071 N N   . SER C 191 ? 1.6164 1.5050 1.8145 0.3230  -0.6949 -0.7017 191 SER C N   
19072 C CA  . SER C 191 ? 1.5612 1.4834 1.6943 0.3299  -0.6865 -0.6691 191 SER C CA  
19073 C C   . SER C 191 ? 1.4943 1.4187 1.6660 0.2812  -0.6484 -0.6327 191 SER C C   
19074 O O   . SER C 191 ? 1.4934 1.4013 1.7898 0.2391  -0.6173 -0.6211 191 SER C O   
19075 C CB  . SER C 191 ? 1.5551 1.5019 1.7594 0.3478  -0.7319 -0.7028 191 SER C CB  
19076 O OG  . SER C 191 ? 1.5059 1.4538 1.8832 0.3051  -0.7414 -0.7226 191 SER C OG  
19082 N N   . TYR C 192 ? 1.4326 1.3813 1.5032 0.2887  -0.6245 -0.5874 192 TYR C N   
19083 C CA  . TYR C 192 ? 1.3542 1.3154 1.4569 0.2483  -0.5595 -0.5214 192 TYR C CA  
19084 C C   . TYR C 192 ? 1.3341 1.3245 1.3796 0.2631  -0.5713 -0.5037 192 TYR C C   
19085 O O   . TYR C 192 ? 1.3808 1.3769 1.2925 0.3023  -0.5880 -0.5021 192 TYR C O   
19086 C CB  . TYR C 192 ? 1.3264 1.2768 1.3462 0.2371  -0.4901 -0.4659 192 TYR C CB  
19087 C CG  . TYR C 192 ? 1.3376 1.2586 1.4314 0.2167  -0.4654 -0.4707 192 TYR C CG  
19088 C CD1 . TYR C 192 ? 1.2770 1.1965 1.4933 0.1752  -0.4191 -0.4394 192 TYR C CD1 
19089 C CD2 . TYR C 192 ? 1.4166 1.3114 1.4574 0.2430  -0.4876 -0.5052 192 TYR C CD2 
19090 C CE1 . TYR C 192 ? 1.2860 1.1754 1.5703 0.1596  -0.3928 -0.4384 192 TYR C CE1 
19091 C CE2 . TYR C 192 ? 1.4302 1.2925 1.5389 0.2264  -0.4646 -0.5084 192 TYR C CE2 
19092 C CZ  . TYR C 192 ? 1.3647 1.2227 1.5957 0.1843  -0.4160 -0.4732 192 TYR C CZ  
19093 O OH  . TYR C 192 ? 1.3651 1.1876 1.6634 0.1707  -0.3892 -0.4710 192 TYR C OH  
19103 N N   . THR C 193 ? 1.2751 1.2840 1.4220 0.2343  -0.5605 -0.4879 193 THR C N   
19104 C CA  . THR C 193 ? 1.2848 1.3189 1.4005 0.2500  -0.5817 -0.4811 193 THR C CA  
19105 C C   . THR C 193 ? 1.2533 1.3025 1.4125 0.2143  -0.5261 -0.4243 193 THR C C   
19106 O O   . THR C 193 ? 1.1971 1.2487 1.4699 0.1773  -0.4922 -0.4096 193 THR C O   
19107 C CB  . THR C 193 ? 1.2816 1.3324 1.4899 0.2656  -0.6544 -0.5454 193 THR C CB  
19108 O OG1 . THR C 193 ? 1.3033 1.3363 1.4683 0.3029  -0.6809 -0.5818 193 THR C OG1 
19109 C CG2 . THR C 193 ? 1.3397 1.4120 1.5079 0.2854  -0.6618 -0.5275 193 THR C CG2 
19117 N N   . CYS C 194 ? 1.2841 1.3437 1.3524 0.2290  -0.5169 -0.3923 194 CYS C N   
19118 C CA  . CYS C 194 ? 1.2459 1.3205 1.3397 0.2036  -0.4718 -0.3432 194 CYS C CA  
19119 C C   . CYS C 194 ? 1.2337 1.3264 1.3317 0.2236  -0.5122 -0.3552 194 CYS C C   
19120 O O   . CYS C 194 ? 1.2832 1.3705 1.2698 0.2595  -0.5350 -0.3544 194 CYS C O   
19121 C CB  . CYS C 194 ? 1.2603 1.3256 1.2397 0.2009  -0.4168 -0.2905 194 CYS C CB  
19122 S SG  . CYS C 194 ? 1.3148 1.3936 1.2683 0.1924  -0.3842 -0.2410 194 CYS C SG  
19127 N N   . GLU C 195 ? 1.1565 1.2724 1.3821 0.2032  -0.5190 -0.3639 195 GLU C N   
19128 C CA  . GLU C 195 ? 1.1790 1.3169 1.4284 0.2229  -0.5625 -0.3831 195 GLU C CA  
19129 C C   . GLU C 195 ? 1.1784 1.3295 1.4350 0.2072  -0.5224 -0.3348 195 GLU C C   
19130 O O   . GLU C 195 ? 1.1493 1.3141 1.4935 0.1731  -0.4798 -0.3105 195 GLU C O   
19131 C CB  . GLU C 195 ? 1.1314 1.2930 1.5305 0.2147  -0.6078 -0.4366 195 GLU C CB  
19132 C CG  . GLU C 195 ? 1.2218 1.3743 1.6123 0.2433  -0.6673 -0.4990 195 GLU C CG  
19133 C CD  . GLU C 195 ? 1.2807 1.4487 1.8202 0.2329  -0.6951 -0.5443 195 GLU C CD  
19134 O OE1 . GLU C 195 ? 1.3529 1.5048 1.9083 0.2488  -0.7231 -0.5887 195 GLU C OE1 
19135 O OE2 . GLU C 195 ? 1.2658 1.4633 1.9076 0.2108  -0.6871 -0.5343 195 GLU C OE2 
19142 N N   . ALA C 196 ? 1.1842 1.3312 1.3496 0.2357  -0.5363 -0.3211 196 ALA C N   
19143 C CA  . ALA C 196 ? 1.1352 1.2898 1.2983 0.2271  -0.5056 -0.2802 196 ALA C CA  
19144 C C   . ALA C 196 ? 1.1892 1.3671 1.3967 0.2492  -0.5531 -0.3048 196 ALA C C   
19145 O O   . ALA C 196 ? 1.2188 1.3944 1.3749 0.2880  -0.6052 -0.3362 196 ALA C O   
19146 C CB  . ALA C 196 ? 1.1161 1.2412 1.1395 0.2401  -0.4759 -0.2377 196 ALA C CB  
19152 N N   . THR C 197 ? 1.1950 1.3996 1.4952 0.2289  -0.5353 -0.2909 197 THR C N   
19153 C CA  . THR C 197 ? 1.2621 1.4945 1.6114 0.2483  -0.5749 -0.3104 197 THR C CA  
19154 C C   . THR C 197 ? 1.2519 1.4756 1.5484 0.2525  -0.5444 -0.2654 197 THR C C   
19155 O O   . THR C 197 ? 1.2091 1.4454 1.5567 0.2248  -0.4985 -0.2355 197 THR C O   
19156 C CB  . THR C 197 ? 1.2485 1.5260 1.7657 0.2233  -0.5835 -0.3361 197 THR C CB  
19157 O OG1 . THR C 197 ? 1.2371 1.5317 1.8119 0.1943  -0.5281 -0.2944 197 THR C OG1 
19158 C CG2 . THR C 197 ? 1.2075 1.4838 1.7922 0.2046  -0.5922 -0.3686 197 THR C CG2 
19166 N N   . HIS C 198 ? 0.9466 1.6000 1.4177 0.1578  -0.2080 -0.3020 198 HIS C N   
19167 C CA  . HIS C 198 ? 0.9613 1.5612 1.3302 0.1991  -0.1887 -0.2734 198 HIS C CA  
19168 C C   . HIS C 198 ? 1.0091 1.6578 1.3926 0.2771  -0.2460 -0.3174 198 HIS C C   
19169 O O   . HIS C 198 ? 1.0830 1.7693 1.4999 0.3070  -0.3089 -0.3618 198 HIS C O   
19170 C CB  . HIS C 198 ? 1.0148 1.4736 1.1927 0.2101  -0.1786 -0.2282 198 HIS C CB  
19171 C CG  . HIS C 198 ? 1.0867 1.4708 1.1535 0.2261  -0.1464 -0.1846 198 HIS C CG  
19172 N ND1 . HIS C 198 ? 1.0466 1.4563 1.1678 0.1914  -0.0926 -0.1609 198 HIS C ND1 
19173 C CD2 . HIS C 198 ? 1.1869 1.4612 1.0808 0.2698  -0.1624 -0.1596 198 HIS C CD2 
19174 C CE1 . HIS C 198 ? 1.1041 1.4197 1.0897 0.2158  -0.0786 -0.1252 198 HIS C CE1 
19175 N NE2 . HIS C 198 ? 1.1844 1.4158 1.0313 0.2618  -0.1214 -0.1225 198 HIS C NE2 
19183 N N   . LYS C 199 ? 0.9903 1.6340 1.3455 0.3122  -0.2268 -0.3056 199 LYS C N   
19184 C CA  . LYS C 199 ? 1.0407 1.7284 1.4087 0.3950  -0.2810 -0.3461 199 LYS C CA  
19185 C C   . LYS C 199 ? 1.1424 1.7184 1.3438 0.4586  -0.3427 -0.3487 199 LYS C C   
19186 O O   . LYS C 199 ? 1.1780 1.7881 1.3918 0.5282  -0.4065 -0.3890 199 LYS C O   
19187 C CB  . LYS C 199 ? 1.0764 1.7709 1.4394 0.4227  -0.2424 -0.3330 199 LYS C CB  
19188 C CG  . LYS C 199 ? 1.2230 1.9790 1.6207 0.5149  -0.2958 -0.3785 199 LYS C CG  
19189 C CD  . LYS C 199 ? 1.3087 2.0769 1.7090 0.5452  -0.2518 -0.3705 199 LYS C CD  
19190 C CE  . LYS C 199 ? 1.4177 2.0012 1.6002 0.5637  -0.2335 -0.3204 199 LYS C CE  
19191 N NZ  . LYS C 199 ? 1.5530 2.0258 1.5808 0.6385  -0.3070 -0.3263 199 LYS C NZ  
19205 N N   . THR C 200 ? 1.2286 1.6761 1.2754 0.4353  -0.3261 -0.3059 200 THR C N   
19206 C CA  . THR C 200 ? 1.4208 1.7550 1.2928 0.4882  -0.3787 -0.3026 200 THR C CA  
19207 C C   . THR C 200 ? 1.5119 1.8844 1.4175 0.5116  -0.4478 -0.3518 200 THR C C   
19208 O O   . THR C 200 ? 1.6906 1.9878 1.4692 0.5672  -0.5058 -0.3618 200 THR C O   
19209 C CB  . THR C 200 ? 1.4495 1.6562 1.1618 0.4475  -0.3372 -0.2428 200 THR C CB  
19210 O OG1 . THR C 200 ? 1.6439 1.7316 1.1672 0.4975  -0.3816 -0.2313 200 THR C OG1 
19211 C CG2 . THR C 200 ? 1.3307 1.5616 1.0917 0.3892  -0.3173 -0.2421 200 THR C CG2 
19219 N N   . SER C 201 ? 1.3826 1.8600 1.4456 0.4681  -0.4461 -0.3817 201 SER C N   
19220 C CA  . SER C 201 ? 1.3489 1.8615 1.4486 0.4850  -0.5149 -0.4309 201 SER C CA  
19221 C C   . SER C 201 ? 1.1943 1.8567 1.5112 0.4445  -0.5177 -0.4686 201 SER C C   
19222 O O   . SER C 201 ? 1.0874 1.7950 1.4971 0.3800  -0.4557 -0.4483 201 SER C O   
19223 C CB  . SER C 201 ? 1.3727 1.7898 1.3543 0.4596  -0.5122 -0.4169 201 SER C CB  
19224 O OG  . SER C 201 ? 1.4716 1.7598 1.2496 0.4991  -0.5235 -0.3884 201 SER C OG  
19230 N N   . THR C 202 ? 1.2010 1.9167 1.5829 0.4704  -0.5778 -0.5143 202 THR C N   
19231 C CA  . THR C 202 ? 1.1004 1.9322 1.6644 0.4195  -0.5738 -0.5406 202 THR C CA  
19232 C C   . THR C 202 ? 1.1054 1.9188 1.6903 0.3590  -0.5742 -0.5468 202 THR C C   
19233 O O   . THR C 202 ? 0.9830 1.8718 1.7037 0.2973  -0.5532 -0.5523 202 THR C O   
19234 C CB  . THR C 202 ? 1.1241 1.9970 1.7317 0.4584  -0.6278 -0.5760 202 THR C CB  
19235 O OG1 . THR C 202 ? 1.0764 2.0610 1.8519 0.4028  -0.6220 -0.5927 202 THR C OG1 
19236 C CG2 . THR C 202 ? 1.2141 1.9846 1.6935 0.4931  -0.6880 -0.5932 202 THR C CG2 
19244 N N   . SER C 203 ? 1.2644 1.9685 1.7049 0.3747  -0.5947 -0.5432 203 SER C N   
19245 C CA  . SER C 203 ? 1.3295 2.0014 1.7710 0.3266  -0.5949 -0.5518 203 SER C CA  
19246 C C   . SER C 203 ? 1.2688 1.9063 1.6852 0.2814  -0.5265 -0.5106 203 SER C C   
19247 O O   . SER C 203 ? 1.2856 1.8270 1.5536 0.3033  -0.4939 -0.4715 203 SER C O   
19248 C CB  . SER C 203 ? 1.4775 2.0403 1.7671 0.3662  -0.6397 -0.5665 203 SER C CB  
19249 O OG  . SER C 203 ? 1.5437 2.0155 1.6655 0.4150  -0.6326 -0.5384 203 SER C OG  
19255 N N   . PRO C 204 ? 1.1894 1.8804 1.7309 0.2113  -0.4900 -0.5055 204 PRO C N   
19256 C CA  . PRO C 204 ? 1.0960 1.7322 1.6031 0.1642  -0.4120 -0.4538 204 PRO C CA  
19257 C C   . PRO C 204 ? 1.1331 1.6503 1.4859 0.1781  -0.4049 -0.4388 204 PRO C C   
19258 O O   . PRO C 204 ? 1.1547 1.6421 1.4817 0.1867  -0.4487 -0.4746 204 PRO C O   
19259 C CB  . PRO C 204 ? 1.0328 1.7399 1.6986 0.0887  -0.3977 -0.4637 204 PRO C CB  
19260 C CG  . PRO C 204 ? 1.0613 1.8687 1.8454 0.0919  -0.4374 -0.4983 204 PRO C CG  
19261 C CD  . PRO C 204 ? 1.1726 1.9518 1.8719 0.1651  -0.5049 -0.5315 204 PRO C CD  
19269 N N   . ILE C 205 ? 1.1667 1.6174 1.4144 0.1798  -0.3490 -0.3854 205 ILE C N   
19270 C CA  . ILE C 205 ? 1.2756 1.6309 1.3889 0.1868  -0.3297 -0.3645 205 ILE C CA  
19271 C C   . ILE C 205 ? 1.2751 1.6305 1.4595 0.1321  -0.3010 -0.3618 205 ILE C C   
19272 O O   . ILE C 205 ? 1.1642 1.5604 1.4523 0.0785  -0.2617 -0.3387 205 ILE C O   
19273 C CB  . ILE C 205 ? 1.2716 1.5653 1.2613 0.1961  -0.2798 -0.3042 205 ILE C CB  
19274 C CG1 . ILE C 205 ? 1.3674 1.6419 1.2708 0.2547  -0.3176 -0.3097 205 ILE C CG1 
19275 C CG2 . ILE C 205 ? 1.2904 1.5061 1.1569 0.1970  -0.2527 -0.2792 205 ILE C CG2 
19276 C CD1 . ILE C 205 ? 1.4137 1.6076 1.1680 0.2654  -0.2808 -0.2520 205 ILE C CD1 
19288 N N   . VAL C 206 ? 1.3804 1.6831 1.5017 0.1473  -0.3220 -0.3862 206 VAL C N   
19289 C CA  . VAL C 206 ? 1.3427 1.6325 1.5220 0.1070  -0.3087 -0.3944 206 VAL C CA  
19290 C C   . VAL C 206 ? 1.3841 1.5975 1.4394 0.1251  -0.2714 -0.3688 206 VAL C C   
19291 O O   . VAL C 206 ? 1.4765 1.6433 1.3997 0.1748  -0.2861 -0.3767 206 VAL C O   
19292 C CB  . VAL C 206 ? 1.3504 1.6527 1.5873 0.1086  -0.3780 -0.4601 206 VAL C CB  
19293 C CG1 . VAL C 206 ? 1.3112 1.5920 1.6139 0.0618  -0.3676 -0.4677 206 VAL C CG1 
19294 C CG2 . VAL C 206 ? 1.3054 1.6999 1.6612 0.0982  -0.4200 -0.4865 206 VAL C CG2 
19304 N N   . LYS C 207 ? 1.3149 1.5192 1.4132 0.0843  -0.2232 -0.3372 207 LYS C N   
19305 C CA  . LYS C 207 ? 1.3302 1.4794 1.3394 0.0994  -0.1869 -0.3165 207 LYS C CA  
19306 C C   . LYS C 207 ? 1.2761 1.4138 1.3712 0.0651  -0.1824 -0.3294 207 LYS C C   
19307 O O   . LYS C 207 ? 1.1835 1.3523 1.3909 0.0105  -0.1676 -0.3104 207 LYS C O   
19308 C CB  . LYS C 207 ? 1.2816 1.4265 1.2342 0.0887  -0.1241 -0.2458 207 LYS C CB  
19309 C CG  . LYS C 207 ? 1.2865 1.4268 1.1442 0.1179  -0.1297 -0.2273 207 LYS C CG  
19310 C CD  . LYS C 207 ? 1.3489 1.4424 1.0600 0.1751  -0.1538 -0.2497 207 LYS C CD  
19311 C CE  . LYS C 207 ? 1.3202 1.3815 0.9214 0.1805  -0.1001 -0.2018 207 LYS C CE  
19312 N NZ  . LYS C 207 ? 1.4062 1.4236 0.8445 0.2270  -0.1161 -0.2054 207 LYS C NZ  
19326 N N   . SER C 208 ? 1.3397 1.4263 1.3747 0.0978  -0.1962 -0.3624 208 SER C N   
19327 C CA  . SER C 208 ? 1.3109 1.3688 1.4145 0.0742  -0.2058 -0.3851 208 SER C CA  
19328 C C   . SER C 208 ? 1.3553 1.3565 1.3637 0.1195  -0.1847 -0.3926 208 SER C C   
19329 O O   . SER C 208 ? 1.3973 1.3870 1.2870 0.1671  -0.1682 -0.3876 208 SER C O   
19330 C CB  . SER C 208 ? 1.3487 1.4036 1.5121 0.0634  -0.2778 -0.4483 208 SER C CB  
19331 O OG  . SER C 208 ? 1.4627 1.4879 1.5253 0.1190  -0.3225 -0.4951 208 SER C OG  
19337 N N   . PHE C 209 ? 1.3698 1.3347 1.4295 0.1043  -0.1854 -0.4048 209 PHE C N   
19338 C CA  . PHE C 209 ? 1.4785 1.3901 1.4627 0.1522  -0.1684 -0.4206 209 PHE C CA  
19339 C C   . PHE C 209 ? 1.5428 1.3930 1.5813 0.1396  -0.2105 -0.4664 209 PHE C C   
19340 O O   . PHE C 209 ? 1.5109 1.3670 1.6517 0.0829  -0.2434 -0.4729 209 PHE C O   
19341 C CB  . PHE C 209 ? 1.4499 1.3861 1.4288 0.1512  -0.0967 -0.3563 209 PHE C CB  
19342 C CG  . PHE C 209 ? 1.4000 1.3466 1.4980 0.0909  -0.0793 -0.3170 209 PHE C CG  
19343 C CD1 . PHE C 209 ? 1.3213 1.3180 1.4832 0.0356  -0.0603 -0.2677 209 PHE C CD1 
19344 C CD2 . PHE C 209 ? 1.4308 1.3285 1.5679 0.0913  -0.0836 -0.3301 209 PHE C CD2 
19345 C CE1 . PHE C 209 ? 1.2621 1.2620 1.5223 -0.0226 -0.0444 -0.2307 209 PHE C CE1 
19346 C CE2 . PHE C 209 ? 1.3712 1.2690 1.6086 0.0338  -0.0719 -0.2920 209 PHE C CE2 
19347 C CZ  . PHE C 209 ? 1.2928 1.2428 1.5906 -0.0256 -0.0514 -0.2415 209 PHE C CZ  
19357 N N   . ASN C 210 ? 1.6397 1.4281 1.6036 0.1928  -0.2089 -0.4984 210 ASN C N   
19358 C CA  . ASN C 210 ? 1.7149 1.4227 1.7063 0.1908  -0.2490 -0.5430 210 ASN C CA  
19359 C C   . ASN C 210 ? 1.7289 1.4153 1.7260 0.2116  -0.2008 -0.5154 210 ASN C C   
19360 O O   . ASN C 210 ? 1.7435 1.4426 1.6595 0.2699  -0.1551 -0.5062 210 ASN C O   
19361 C CB  . ASN C 210 ? 1.8612 1.4971 1.7498 0.2433  -0.3022 -0.6179 210 ASN C CB  
19362 C CG  . ASN C 210 ? 1.8488 1.5004 1.7533 0.2158  -0.3660 -0.6500 210 ASN C CG  
19363 O OD1 . ASN C 210 ? 1.7439 1.4393 1.7623 0.1498  -0.3861 -0.6333 210 ASN C OD1 
19364 N ND2 . ASN C 210 ? 1.9547 1.5746 1.7455 0.2666  -0.3979 -0.6958 210 ASN C ND2 
19371 N N   . ARG C 211 ? 1.7221 1.3795 1.8160 0.1627  -0.2119 -0.5012 211 ARG C N   
19372 C CA  . ARG C 211 ? 1.6924 1.3333 1.8087 0.1774  -0.1712 -0.4687 211 ARG C CA  
19373 C C   . ARG C 211 ? 1.7911 1.3706 1.8116 0.2643  -0.1677 -0.5146 211 ARG C C   
19374 O O   . ARG C 211 ? 1.7803 1.3998 1.7638 0.3129  -0.1103 -0.4879 211 ARG C O   
19375 C CB  . ARG C 211 ? 1.6535 1.2465 1.8735 0.1107  -0.2013 -0.4578 211 ARG C CB  
19376 C CG  . ARG C 211 ? 1.6278 1.1924 1.8781 0.1231  -0.1712 -0.4249 211 ARG C CG  
19377 C CD  . ARG C 211 ? 1.5744 1.0873 1.9200 0.0459  -0.2043 -0.4080 211 ARG C CD  
19378 N NE  . ARG C 211 ? 1.6455 1.0654 1.9850 0.0270  -0.2776 -0.4699 211 ARG C NE  
19379 C CZ  . ARG C 211 ? 1.7723 1.0768 2.0713 0.0645  -0.3164 -0.5155 211 ARG C CZ  
19380 N NH1 . ARG C 211 ? 1.8184 1.0934 2.0859 0.1306  -0.2863 -0.5089 211 ARG C NH1 
19381 N NH2 . ARG C 211 ? 1.8630 1.0811 2.1526 0.0364  -0.3877 -0.5683 211 ARG C NH2 
19395 N N   . ASN C 212 ? 1.8896 1.3723 1.8678 0.2842  -0.2288 -0.5844 212 ASN C N   
19396 C CA  . ASN C 212 ? 2.0203 1.4324 1.8940 0.3721  -0.2281 -0.6363 212 ASN C CA  
19397 C C   . ASN C 212 ? 2.0541 1.5276 1.8213 0.4344  -0.1806 -0.6366 212 ASN C C   
19398 O O   . ASN C 212 ? 2.0848 1.5764 1.8032 0.4981  -0.1281 -0.6303 212 ASN C O   
19399 C CB  . ASN C 212 ? 2.1256 1.4180 1.9534 0.3759  -0.3099 -0.7133 212 ASN C CB  
19400 C CG  . ASN C 212 ? 2.2776 1.4977 1.9651 0.4714  -0.3124 -0.7766 212 ASN C CG  
19401 O OD1 . ASN C 212 ? 2.2842 1.5353 1.8808 0.5016  -0.3050 -0.7912 212 ASN C OD1 
19402 N ND2 . ASN C 212 ? 2.3945 1.5374 2.0679 0.5058  -0.3150 -0.7907 212 ASN C ND2 
19409 N N   . GLU C 213 ? 2.0613 1.5703 1.7917 0.4163  -0.1986 -0.6425 213 GLU C N   
19410 C CA  . GLU C 213 ? 2.1363 1.6798 1.7440 0.4724  -0.1670 -0.6506 213 GLU C CA  
19411 C C   . GLU C 213 ? 2.0681 1.7165 1.6865 0.4745  -0.0852 -0.5775 213 GLU C C   
19412 O O   . GLU C 213 ? 1.9212 1.6219 1.6450 0.4245  -0.0588 -0.5178 213 GLU C O   
19413 C CB  . GLU C 213 ? 2.1172 1.6664 1.6876 0.4492  -0.2153 -0.6719 213 GLU C CB  
19414 C CG  . GLU C 213 ? 2.1946 1.6496 1.7571 0.4393  -0.3020 -0.7415 213 GLU C CG  
19415 C CD  . GLU C 213 ? 2.1883 1.6537 1.7017 0.4303  -0.3513 -0.7664 213 GLU C CD  
19416 O OE1 . GLU C 213 ? 2.0932 1.6382 1.5962 0.4229  -0.3207 -0.7248 213 GLU C OE1 
19417 O OE2 . GLU C 213 ? 2.2822 1.6907 1.7809 0.4201  -0.4146 -0.8033 213 GLU C OE2 
19424 N N   . CYS C 214 ? 2.1794 1.8550 1.6795 0.5295  -0.0467 -0.5817 214 CYS C N   
19425 C CA  . CYS C 214 ? 2.1309 1.9048 1.6204 0.5324  0.0296  -0.5145 214 CYS C CA  
19426 C C   . CYS C 214 ? 2.1689 1.9563 1.5056 0.5817  0.0531  -0.5300 214 CYS C C   
19427 O O   . CYS C 214 ? 2.1672 1.9279 1.4359 0.5741  0.0124  -0.5530 214 CYS C O   
19428 C CB  . CYS C 214 ? 2.1837 1.9849 1.7287 0.5590  0.0799  -0.4904 214 CYS C CB  
19429 S SG  . CYS C 214 ? 2.1537 2.0816 1.6703 0.5747  0.1755  -0.4161 214 CYS C SG  
19434 N N   . GLN D 1   ? 1.4302 1.0780 1.0810 -0.0600 0.0673  0.0201  1   GLN D N   
19435 C CA  . GLN D 1   ? 1.3201 1.0248 1.0147 -0.0731 0.0955  0.0016  1   GLN D CA  
19436 C C   . GLN D 1   ? 1.1554 0.9549 0.9240 -0.0508 0.0610  -0.0065 1   GLN D C   
19437 O O   . GLN D 1   ? 1.1118 0.9846 0.9511 -0.0567 0.0722  -0.0301 1   GLN D O   
19438 C CB  . GLN D 1   ? 1.3838 1.1117 1.1281 -0.1089 0.1443  -0.0257 1   GLN D CB  
19439 C CG  . GLN D 1   ? 1.6488 1.2692 1.3110 -0.1377 0.1929  -0.0186 1   GLN D CG  
19440 C CD  . GLN D 1   ? 1.8130 1.4582 1.5370 -0.1786 0.2455  -0.0516 1   GLN D CD  
19441 O OE1 . GLN D 1   ? 1.7831 1.5255 1.6119 -0.1807 0.2343  -0.0798 1   GLN D OE1 
19442 N NE2 . GLN D 1   ? 1.9798 1.5328 1.6358 -0.2117 0.3045  -0.0510 1   GLN D NE2 
19453 N N   . VAL D 2   ? 1.0679 0.8610 0.8178 -0.0242 0.0195  0.0105  2   VAL D N   
19454 C CA  . VAL D 2   ? 0.9640 0.8241 0.7641 -0.0041 -0.0082 0.0071  2   VAL D CA  
19455 C C   . VAL D 2   ? 0.9857 0.8413 0.7635 0.0031  -0.0039 0.0089  2   VAL D C   
19456 O O   . VAL D 2   ? 1.0668 0.8600 0.7772 0.0062  -0.0040 0.0209  2   VAL D O   
19457 C CB  . VAL D 2   ? 0.9272 0.7827 0.7255 0.0154  -0.0463 0.0184  2   VAL D CB  
19458 C CG1 . VAL D 2   ? 0.8474 0.7552 0.6844 0.0318  -0.0654 0.0162  2   VAL D CG1 
19459 C CG2 . VAL D 2   ? 0.9283 0.7908 0.7513 0.0091  -0.0497 0.0140  2   VAL D CG2 
19469 N N   . GLN D 3   ? 0.9392 0.8566 0.7686 0.0091  -0.0027 -0.0047 3   GLN D N   
19470 C CA  . GLN D 3   ? 0.9685 0.8870 0.7853 0.0171  0.0019  -0.0064 3   GLN D CA  
19471 C C   . GLN D 3   ? 0.8897 0.8576 0.7480 0.0387  -0.0219 -0.0092 3   GLN D C   
19472 O O   . GLN D 3   ? 0.8502 0.8669 0.7569 0.0442  -0.0281 -0.0205 3   GLN D O   
19473 C CB  . GLN D 3   ? 1.0488 0.9796 0.8791 -0.0010 0.0419  -0.0267 3   GLN D CB  
19474 C CG  . GLN D 3   ? 1.1974 1.0630 0.9729 -0.0270 0.0774  -0.0237 3   GLN D CG  
19475 C CD  . GLN D 3   ? 1.3190 1.1984 1.1140 -0.0500 0.1263  -0.0491 3   GLN D CD  
19476 O OE1 . GLN D 3   ? 1.3533 1.2874 1.1957 -0.0413 0.1284  -0.0681 3   GLN D OE1 
19477 N NE2 . GLN D 3   ? 1.3971 1.2235 1.1558 -0.0798 0.1685  -0.0520 3   GLN D NE2 
19486 N N   . LEU D 4   ? 0.8853 0.8333 0.7181 0.0519  -0.0351 -0.0001 4   LEU D N   
19487 C CA  . LEU D 4   ? 0.8529 0.8282 0.7101 0.0709  -0.0508 -0.0010 4   LEU D CA  
19488 C C   . LEU D 4   ? 0.8407 0.8133 0.6889 0.0763  -0.0393 -0.0089 4   LEU D C   
19489 O O   . LEU D 4   ? 0.8525 0.7858 0.6597 0.0748  -0.0386 -0.0031 4   LEU D O   
19490 C CB  . LEU D 4   ? 0.8476 0.8014 0.6919 0.0787  -0.0732 0.0119  4   LEU D CB  
19491 C CG  . LEU D 4   ? 0.8221 0.7757 0.6751 0.0740  -0.0845 0.0171  4   LEU D CG  
19492 C CD1 . LEU D 4   ? 0.8161 0.7585 0.6715 0.0805  -0.1012 0.0213  4   LEU D CD1 
19493 C CD2 . LEU D 4   ? 0.7845 0.7778 0.6721 0.0746  -0.0819 0.0107  4   LEU D CD2 
19505 N N   . GLN D 5   ? 0.8357 0.8502 0.7224 0.0856  -0.0331 -0.0255 5   GLN D N   
19506 C CA  . GLN D 5   ? 0.8673 0.8866 0.7557 0.0931  -0.0214 -0.0384 5   GLN D CA  
19507 C C   . GLN D 5   ? 0.7997 0.8196 0.6918 0.1190  -0.0422 -0.0342 5   GLN D C   
19508 O O   . GLN D 5   ? 0.7547 0.8004 0.6717 0.1366  -0.0566 -0.0382 5   GLN D O   
19509 C CB  . GLN D 5   ? 0.9572 1.0247 0.8939 0.0881  -0.0001 -0.0676 5   GLN D CB  
19510 C CG  . GLN D 5   ? 1.1333 1.2103 1.0788 0.0941  0.0169  -0.0870 5   GLN D CG  
19511 C CD  . GLN D 5   ? 1.3337 1.3584 1.2217 0.0751  0.0415  -0.0792 5   GLN D CD  
19512 O OE1 . GLN D 5   ? 1.4312 1.4192 1.2785 0.0847  0.0301  -0.0662 5   GLN D OE1 
19513 N NE2 . GLN D 5   ? 1.4013 1.4165 1.2806 0.0478  0.0767  -0.0890 5   GLN D NE2 
19522 N N   . GLN D 6   ? 0.8443 0.8286 0.7051 0.1222  -0.0435 -0.0271 6   GLN D N   
19523 C CA  . GLN D 6   ? 0.8585 0.8282 0.7152 0.1428  -0.0569 -0.0228 6   GLN D CA  
19524 C C   . GLN D 6   ? 0.8809 0.8623 0.7495 0.1587  -0.0493 -0.0407 6   GLN D C   
19525 O O   . GLN D 6   ? 0.8584 0.8520 0.7318 0.1489  -0.0301 -0.0559 6   GLN D O   
19526 C CB  . GLN D 6   ? 0.9300 0.8560 0.7556 0.1356  -0.0633 -0.0104 6   GLN D CB  
19527 C CG  . GLN D 6   ? 0.9497 0.8678 0.7740 0.1247  -0.0737 0.0019  6   GLN D CG  
19528 C CD  . GLN D 6   ? 0.9955 0.8812 0.8072 0.1199  -0.0819 0.0041  6   GLN D CD  
19529 O OE1 . GLN D 6   ? 1.0305 0.9057 0.8329 0.1099  -0.0905 0.0033  6   GLN D OE1 
19530 N NE2 . GLN D 6   ? 1.0052 0.8724 0.8176 0.1283  -0.0801 0.0035  6   GLN D NE2 
19539 N N   . SER D 7   ? 0.9604 0.9317 0.8290 0.1840  -0.0625 -0.0396 7   SER D N   
19540 C CA  . SER D 7   ? 0.9606 0.9413 0.8429 0.2063  -0.0609 -0.0585 7   SER D CA  
19541 C C   . SER D 7   ? 0.9228 0.8732 0.7818 0.1971  -0.0477 -0.0611 7   SER D C   
19542 O O   . SER D 7   ? 0.8637 0.7848 0.6939 0.1769  -0.0445 -0.0490 7   SER D O   
19543 C CB  . SER D 7   ? 1.0355 0.9939 0.9063 0.2398  -0.0810 -0.0532 7   SER D CB  
19544 O OG  . SER D 7   ? 1.1077 1.0057 0.9378 0.2359  -0.0809 -0.0325 7   SER D OG  
19550 N N   . GLY D 8   ? 0.9614 0.9201 0.8340 0.2156  -0.0431 -0.0809 8   GLY D N   
19551 C CA  . GLY D 8   ? 0.9945 0.9280 0.8460 0.2091  -0.0294 -0.0886 8   GLY D CA  
19552 C C   . GLY D 8   ? 0.9921 0.8708 0.8126 0.2171  -0.0402 -0.0757 8   GLY D C   
19553 O O   . GLY D 8   ? 1.0033 0.8571 0.8151 0.2272  -0.0536 -0.0600 8   GLY D O   
19557 N N   . ALA D 9   ? 0.9828 0.8383 0.7835 0.2106  -0.0305 -0.0851 9   ALA D N   
19558 C CA  . ALA D 9   ? 1.0077 0.8123 0.7852 0.2129  -0.0371 -0.0797 9   ALA D CA  
19559 C C   . ALA D 9   ? 1.0875 0.8674 0.8688 0.2415  -0.0450 -0.0775 9   ALA D C   
19560 O O   . ALA D 9   ? 1.1166 0.9189 0.9173 0.2673  -0.0473 -0.0909 9   ALA D O   
19561 C CB  . ALA D 9   ? 0.9856 0.7744 0.7438 0.2070  -0.0269 -0.0973 9   ALA D CB  
19567 N N   . GLU D 10  ? 1.1069 0.8364 0.8681 0.2378  -0.0484 -0.0631 10  GLU D N   
19568 C CA  . GLU D 10  ? 1.1377 0.8175 0.8807 0.2632  -0.0519 -0.0560 10  GLU D CA  
19569 C C   . GLU D 10  ? 1.1702 0.7952 0.8970 0.2606  -0.0429 -0.0643 10  GLU D C   
19570 O O   . GLU D 10  ? 1.1823 0.7980 0.9108 0.2330  -0.0369 -0.0690 10  GLU D O   
19571 C CB  . GLU D 10  ? 1.1821 0.8332 0.9064 0.2578  -0.0535 -0.0325 10  GLU D CB  
19572 C CG  . GLU D 10  ? 1.1685 0.8669 0.9054 0.2649  -0.0648 -0.0254 10  GLU D CG  
19573 C CD  . GLU D 10  ? 1.2288 0.9275 0.9586 0.3076  -0.0807 -0.0295 10  GLU D CD  
19574 O OE1 . GLU D 10  ? 1.2738 0.9399 0.9909 0.3338  -0.0836 -0.0388 10  GLU D OE1 
19575 O OE2 . GLU D 10  ? 1.2312 0.9626 0.9688 0.3176  -0.0934 -0.0265 10  GLU D OE2 
19582 N N   . LEU D 11  ? 1.1773 0.7660 0.8901 0.2918  -0.0448 -0.0698 11  LEU D N   
19583 C CA  . LEU D 11  ? 1.1796 0.7031 0.8728 0.2928  -0.0349 -0.0768 11  LEU D CA  
19584 C C   . LEU D 11  ? 1.2382 0.6810 0.8880 0.3159  -0.0337 -0.0586 11  LEU D C   
19585 O O   . LEU D 11  ? 1.2714 0.7142 0.9060 0.3506  -0.0491 -0.0508 11  LEU D O   
19586 C CB  . LEU D 11  ? 1.1913 0.7312 0.8980 0.3118  -0.0355 -0.1031 11  LEU D CB  
19587 C CG  . LEU D 11  ? 1.1665 0.7815 0.9025 0.2990  -0.0331 -0.1217 11  LEU D CG  
19588 C CD1 . LEU D 11  ? 1.1847 0.8130 0.9345 0.3235  -0.0295 -0.1497 11  LEU D CD1 
19589 C CD2 . LEU D 11  ? 1.1690 0.7857 0.8991 0.2620  -0.0270 -0.1249 11  LEU D CD2 
19601 N N   . ALA D 12  ? 1.2785 0.6477 0.9049 0.2972  -0.0149 -0.0542 12  ALA D N   
19602 C CA  . ALA D 12  ? 1.3645 0.6354 0.9327 0.3149  -0.0052 -0.0342 12  ALA D CA  
19603 C C   . ALA D 12  ? 1.4522 0.6424 1.0052 0.2946  0.0210  -0.0422 12  ALA D C   
19604 O O   . ALA D 12  ? 1.4258 0.6416 1.0187 0.2566  0.0322  -0.0601 12  ALA D O   
19605 C CB  . ALA D 12  ? 1.3462 0.6051 0.8921 0.3008  0.0015  -0.0096 12  ALA D CB  
19611 N N   . GLU D 13  ? 1.5526 0.6413 1.0454 0.3225  0.0288  -0.0312 13  GLU D N   
19612 C CA  . GLU D 13  ? 1.5818 0.5762 1.0526 0.3028  0.0596  -0.0376 13  GLU D CA  
19613 C C   . GLU D 13  ? 1.5781 0.5188 1.0323 0.2598  0.0956  -0.0245 13  GLU D C   
19614 O O   . GLU D 13  ? 1.5425 0.4933 0.9777 0.2580  0.0953  -0.0034 13  GLU D O   
19615 C CB  . GLU D 13  ? 1.7276 0.6328 1.1360 0.3458  0.0562  -0.0281 13  GLU D CB  
19616 C CG  . GLU D 13  ? 1.7608 0.7177 1.1957 0.3871  0.0251  -0.0489 13  GLU D CG  
19617 C CD  . GLU D 13  ? 1.8788 0.7822 1.2675 0.4246  0.0139  -0.0390 13  GLU D CD  
19618 O OE1 . GLU D 13  ? 1.9481 0.8190 1.2821 0.4431  0.0055  -0.0135 13  GLU D OE1 
19619 O OE2 . GLU D 13  ? 1.9347 0.8259 1.3376 0.4366  0.0124  -0.0587 13  GLU D OE2 
19626 N N   . PRO D 14  ? 1.6507 0.5360 1.1169 0.2229  0.1294  -0.0412 14  PRO D N   
19627 C CA  . PRO D 14  ? 1.7119 0.5442 1.1708 0.1779  0.1719  -0.0359 14  PRO D CA  
19628 C C   . PRO D 14  ? 1.8322 0.5833 1.2031 0.1946  0.1872  0.0021  14  PRO D C   
19629 O O   . PRO D 14  ? 1.9001 0.6004 1.2133 0.2284  0.1784  0.0174  14  PRO D O   
19630 C CB  . PRO D 14  ? 1.7694 0.5516 1.2568 0.1429  0.2040  -0.0660 14  PRO D CB  
19631 C CG  . PRO D 14  ? 1.7106 0.5614 1.2446 0.1595  0.1705  -0.0933 14  PRO D CG  
19632 C CD  . PRO D 14  ? 1.6904 0.5671 1.1870 0.2168  0.1322  -0.0721 14  PRO D CD  
19640 N N   . GLY D 15  ? 1.8548 0.6054 1.2177 0.1698  0.2075  0.0149  15  GLY D N   
19641 C CA  . GLY D 15  ? 1.9515 0.6386 1.2284 0.1805  0.2229  0.0482  15  GLY D CA  
19642 C C   . GLY D 15  ? 1.9313 0.6537 1.1666 0.2307  0.1791  0.0713  15  GLY D C   
19643 O O   . GLY D 15  ? 2.0240 0.7069 1.1910 0.2375  0.1885  0.0946  15  GLY D O   
19647 N N   . ALA D 16  ? 1.7977 0.5971 1.0741 0.2650  0.1329  0.0610  16  ALA D N   
19648 C CA  . ALA D 16  ? 1.7366 0.5880 0.9934 0.3109  0.0892  0.0739  16  ALA D CA  
19649 C C   . ALA D 16  ? 1.6422 0.5506 0.9292 0.2928  0.0877  0.0782  16  ALA D C   
19650 O O   . ALA D 16  ? 1.6684 0.5824 0.9881 0.2422  0.1213  0.0727  16  ALA D O   
19651 C CB  . ALA D 16  ? 1.6821 0.6004 0.9821 0.3497  0.0474  0.0549  16  ALA D CB  
19657 N N   . SER D 17  ? 1.5853 0.5643 0.8798 0.3276  0.0470  0.0820  17  SER D N   
19658 C CA  . SER D 17  ? 1.5647 0.6331 0.9042 0.3055  0.0400  0.0828  17  SER D CA  
19659 C C   . SER D 17  ? 1.4472 0.6364 0.8527 0.3269  -0.0026 0.0666  17  SER D C   
19660 O O   . SER D 17  ? 1.4601 0.6575 0.8629 0.3683  -0.0292 0.0573  17  SER D O   
19661 C CB  . SER D 17  ? 1.7584 0.7647 1.0158 0.3206  0.0453  0.1086  17  SER D CB  
19662 O OG  . SER D 17  ? 1.8720 0.9044 1.1001 0.3695  0.0042  0.1091  17  SER D OG  
19668 N N   . VAL D 18  ? 1.3733 0.6536 0.8395 0.2974  -0.0060 0.0605  18  VAL D N   
19669 C CA  . VAL D 18  ? 1.3256 0.7141 0.8508 0.3087  -0.0369 0.0459  18  VAL D CA  
19670 C C   . VAL D 18  ? 1.2754 0.7076 0.8070 0.3006  -0.0438 0.0551  18  VAL D C   
19671 O O   . VAL D 18  ? 1.2928 0.6934 0.8058 0.2741  -0.0217 0.0675  18  VAL D O   
19672 C CB  . VAL D 18  ? 1.2715 0.7269 0.8661 0.2784  -0.0337 0.0249  18  VAL D CB  
19673 C CG1 . VAL D 18  ? 1.3178 0.7367 0.9078 0.2902  -0.0298 0.0118  18  VAL D CG1 
19674 C CG2 . VAL D 18  ? 1.2094 0.6710 0.8295 0.2310  -0.0126 0.0245  18  VAL D CG2 
19684 N N   . LYS D 19  ? 1.2150 0.7219 0.7782 0.3225  -0.0723 0.0447  19  LYS D N   
19685 C CA  . LYS D 19  ? 1.1459 0.7033 0.7232 0.3167  -0.0823 0.0484  19  LYS D CA  
19686 C C   . LYS D 19  ? 1.0871 0.7457 0.7395 0.3035  -0.0932 0.0285  19  LYS D C   
19687 O O   . LYS D 19  ? 1.1434 0.8403 0.8234 0.3260  -0.1078 0.0096  19  LYS D O   
19688 C CB  . LYS D 19  ? 1.2079 0.7384 0.7330 0.3633  -0.1069 0.0540  19  LYS D CB  
19689 C CG  . LYS D 19  ? 1.2349 0.7951 0.7572 0.3563  -0.1130 0.0602  19  LYS D CG  
19690 C CD  . LYS D 19  ? 1.2967 0.8301 0.7625 0.4088  -0.1444 0.0607  19  LYS D CD  
19691 C CE  . LYS D 19  ? 1.3114 0.8628 0.7635 0.4020  -0.1486 0.0668  19  LYS D CE  
19692 N NZ  . LYS D 19  ? 1.3868 0.9406 0.8078 0.4359  -0.1760 0.0524  19  LYS D NZ  
19706 N N   . MET D 20  ? 1.0298 0.7262 0.7130 0.2674  -0.0836 0.0308  20  MET D N   
19707 C CA  . MET D 20  ? 0.9886 0.7616 0.7270 0.2504  -0.0878 0.0159  20  MET D CA  
19708 C C   . MET D 20  ? 0.9885 0.8037 0.7422 0.2450  -0.0961 0.0180  20  MET D C   
19709 O O   . MET D 20  ? 1.0049 0.7919 0.7306 0.2431  -0.0941 0.0321  20  MET D O   
19710 C CB  . MET D 20  ? 0.9679 0.7410 0.7233 0.2158  -0.0734 0.0140  20  MET D CB  
19711 C CG  . MET D 20  ? 0.9796 0.7311 0.7304 0.1898  -0.0632 0.0248  20  MET D CG  
19712 S SD  . MET D 20  ? 0.9943 0.7387 0.7658 0.1600  -0.0550 0.0132  20  MET D SD  
19713 C CE  . MET D 20  ? 0.9961 0.6744 0.7412 0.1699  -0.0417 0.0108  20  MET D CE  
19723 N N   . SER D 21  ? 0.9502 0.8295 0.7472 0.2406  -0.1013 0.0018  21  SER D N   
19724 C CA  . SER D 21  ? 0.9201 0.8434 0.7388 0.2365  -0.1092 -0.0019 21  SER D CA  
19725 C C   . SER D 21  ? 0.8691 0.8196 0.7132 0.2010  -0.0972 -0.0021 21  SER D C   
19726 O O   . SER D 21  ? 0.8452 0.7877 0.6902 0.1847  -0.0864 -0.0035 21  SER D O   
19727 C CB  . SER D 21  ? 0.9278 0.9022 0.7799 0.2629  -0.1247 -0.0271 21  SER D CB  
19728 O OG  . SER D 21  ? 0.9535 0.9683 0.8475 0.2500  -0.1119 -0.0474 21  SER D OG  
19734 N N   . CYS D 22  ? 0.8587 0.8354 0.7166 0.1921  -0.1012 -0.0015 22  CYS D N   
19735 C CA  . CYS D 22  ? 0.8521 0.8446 0.7256 0.1627  -0.0925 -0.0003 22  CYS D CA  
19736 C C   . CYS D 22  ? 0.7944 0.8296 0.6957 0.1619  -0.0976 -0.0112 22  CYS D C   
19737 O O   . CYS D 22  ? 0.7654 0.7981 0.6592 0.1650  -0.1061 -0.0043 22  CYS D O   
19738 C CB  . CYS D 22  ? 0.8782 0.8365 0.7329 0.1472  -0.0907 0.0155  22  CYS D CB  
19739 S SG  . CYS D 22  ? 0.9212 0.8906 0.7881 0.1214  -0.0899 0.0171  22  CYS D SG  
19744 N N   . LYS D 23  ? 0.7541 0.8274 0.6888 0.1558  -0.0890 -0.0313 23  LYS D N   
19745 C CA  . LYS D 23  ? 0.7733 0.8925 0.7462 0.1525  -0.0911 -0.0497 23  LYS D CA  
19746 C C   . LYS D 23  ? 0.7763 0.8879 0.7488 0.1208  -0.0763 -0.0430 23  LYS D C   
19747 O O   . LYS D 23  ? 0.8488 0.9373 0.8055 0.1019  -0.0583 -0.0387 23  LYS D O   
19748 C CB  . LYS D 23  ? 0.8476 1.0157 0.8686 0.1598  -0.0847 -0.0831 23  LYS D CB  
19749 C CG  . LYS D 23  ? 0.9280 1.1521 1.0024 0.1566  -0.0876 -0.1119 23  LYS D CG  
19750 C CD  . LYS D 23  ? 1.0172 1.2983 1.1552 0.1609  -0.0778 -0.1543 23  LYS D CD  
19751 C CE  . LYS D 23  ? 1.0473 1.3899 1.2513 0.1530  -0.0782 -0.1909 23  LYS D CE  
19752 N NZ  . LYS D 23  ? 1.0609 1.4212 1.2639 0.1869  -0.1196 -0.1961 23  LYS D NZ  
19766 N N   . ALA D 24  ? 0.7514 0.8753 0.7335 0.1177  -0.0850 -0.0428 24  ALA D N   
19767 C CA  . ALA D 24  ? 0.7673 0.8766 0.7451 0.0923  -0.0751 -0.0357 24  ALA D CA  
19768 C C   . ALA D 24  ? 0.7985 0.9450 0.8188 0.0770  -0.0617 -0.0606 24  ALA D C   
19769 O O   . ALA D 24  ? 0.8264 1.0216 0.8880 0.0900  -0.0707 -0.0854 24  ALA D O   
19770 C CB  . ALA D 24  ? 0.7602 0.8539 0.7220 0.0961  -0.0903 -0.0205 24  ALA D CB  
19776 N N   . SER D 25  ? 0.8098 0.9284 0.8173 0.0503  -0.0404 -0.0564 25  SER D N   
19777 C CA  . SER D 25  ? 0.8321 0.9719 0.8753 0.0278  -0.0189 -0.0793 25  SER D CA  
19778 C C   . SER D 25  ? 0.8559 0.9400 0.8600 0.0069  -0.0082 -0.0612 25  SER D C   
19779 O O   . SER D 25  ? 0.8959 0.9269 0.8462 0.0095  -0.0141 -0.0362 25  SER D O   
19780 C CB  . SER D 25  ? 0.8800 1.0378 0.9490 0.0139  0.0126  -0.1039 25  SER D CB  
19781 O OG  . SER D 25  ? 0.9662 1.0655 0.9776 0.0033  0.0319  -0.0845 25  SER D OG  
19787 N N   . GLY D 26  ? 0.8421 0.9376 0.8748 -0.0116 0.0048  -0.0775 26  GLY D N   
19788 C CA  . GLY D 26  ? 0.8621 0.8988 0.8563 -0.0290 0.0145  -0.0627 26  GLY D CA  
19789 C C   . GLY D 26  ? 0.8365 0.8734 0.8309 -0.0169 -0.0143 -0.0524 26  GLY D C   
19790 O O   . GLY D 26  ? 0.8955 0.8854 0.8630 -0.0275 -0.0104 -0.0433 26  GLY D O   
19794 N N   . TYR D 27  ? 0.7676 0.8487 0.7852 0.0058  -0.0413 -0.0542 27  TYR D N   
19795 C CA  . TYR D 27  ? 0.7487 0.8328 0.7680 0.0153  -0.0627 -0.0487 27  TYR D CA  
19796 C C   . TYR D 27  ? 0.7644 0.9013 0.8107 0.0362  -0.0814 -0.0614 27  TYR D C   
19797 O O   . TYR D 27  ? 0.7929 0.9583 0.8522 0.0480  -0.0834 -0.0711 27  TYR D O   
19798 C CB  . TYR D 27  ? 0.7071 0.7470 0.6854 0.0245  -0.0766 -0.0238 27  TYR D CB  
19799 C CG  . TYR D 27  ? 0.7149 0.7620 0.6824 0.0422  -0.0881 -0.0139 27  TYR D CG  
19800 C CD1 . TYR D 27  ? 0.7605 0.7913 0.7077 0.0432  -0.0810 -0.0076 27  TYR D CD1 
19801 C CD2 . TYR D 27  ? 0.7337 0.7965 0.7063 0.0563  -0.1020 -0.0118 27  TYR D CD2 
19802 C CE1 . TYR D 27  ? 0.7759 0.8084 0.7141 0.0581  -0.0898 -0.0002 27  TYR D CE1 
19803 C CE2 . TYR D 27  ? 0.7770 0.8348 0.7350 0.0692  -0.1064 -0.0029 27  TYR D CE2 
19804 C CZ  . TYR D 27  ? 0.8068 0.8505 0.7504 0.0701  -0.1014 0.0025  27  TYR D CZ  
19805 O OH  . TYR D 27  ? 0.8223 0.8566 0.7523 0.0816  -0.1042 0.0096  27  TYR D OH  
19815 N N   . THR D 28  ? 0.7324 0.8763 0.7807 0.0433  -0.0957 -0.0621 28  THR D N   
19816 C CA  . THR D 28  ? 0.7185 0.8962 0.7717 0.0661  -0.1142 -0.0720 28  THR D CA  
19817 C C   . THR D 28  ? 0.7505 0.9034 0.7643 0.0835  -0.1211 -0.0498 28  THR D C   
19818 O O   . THR D 28  ? 0.7158 0.8408 0.7090 0.0816  -0.1207 -0.0347 28  THR D O   
19819 C CB  . THR D 28  ? 0.6552 0.8423 0.7163 0.0655  -0.1224 -0.0821 28  THR D CB  
19820 O OG1 . THR D 28  ? 0.6133 0.8192 0.7142 0.0459  -0.1127 -0.1052 28  THR D OG1 
19821 C CG2 . THR D 28  ? 0.6186 0.8295 0.6672 0.0926  -0.1425 -0.0925 28  THR D CG2 
19829 N N   . PHE D 29  ? 0.7653 0.9285 0.7736 0.1001  -0.1258 -0.0519 29  PHE D N   
19830 C CA  . PHE D 29  ? 0.7537 0.8850 0.7236 0.1136  -0.1272 -0.0317 29  PHE D CA  
19831 C C   . PHE D 29  ? 0.7640 0.8734 0.6993 0.1250  -0.1321 -0.0225 29  PHE D C   
19832 O O   . PHE D 29  ? 0.7976 0.8722 0.7093 0.1210  -0.1227 -0.0060 29  PHE D O   
19833 C CB  . PHE D 29  ? 0.7326 0.8786 0.7029 0.1341  -0.1342 -0.0402 29  PHE D CB  
19834 C CG  . PHE D 29  ? 0.7296 0.8364 0.6567 0.1499  -0.1348 -0.0213 29  PHE D CG  
19835 C CD1 . PHE D 29  ? 0.7109 0.7902 0.6301 0.1371  -0.1219 -0.0066 29  PHE D CD1 
19836 C CD2 . PHE D 29  ? 0.7759 0.8666 0.6646 0.1790  -0.1484 -0.0198 29  PHE D CD2 
19837 C CE1 . PHE D 29  ? 0.7745 0.8165 0.6592 0.1486  -0.1195 0.0070  29  PHE D CE1 
19838 C CE2 . PHE D 29  ? 0.7834 0.8259 0.6263 0.1915  -0.1438 -0.0021 29  PHE D CE2 
19839 C CZ  . PHE D 29  ? 0.8133 0.8342 0.6598 0.1741  -0.1278 0.0103  29  PHE D CZ  
19849 N N   . SER D 30  ? 0.7508 0.8791 0.6830 0.1379  -0.1442 -0.0365 30  SER D N   
19850 C CA  . SER D 30  ? 0.8073 0.9058 0.6908 0.1514  -0.1453 -0.0284 30  SER D CA  
19851 C C   . SER D 30  ? 0.7948 0.8765 0.6812 0.1302  -0.1294 -0.0213 30  SER D C   
19852 O O   . SER D 30  ? 0.8210 0.8688 0.6675 0.1337  -0.1181 -0.0126 30  SER D O   
19853 C CB  . SER D 30  ? 0.8604 0.9822 0.7334 0.1745  -0.1668 -0.0491 30  SER D CB  
19854 O OG  . SER D 30  ? 0.9703 1.1163 0.8519 0.1987  -0.1868 -0.0640 30  SER D OG  
19860 N N   . SER D 31  ? 0.7329 0.8324 0.6630 0.1092  -0.1264 -0.0267 31  SER D N   
19861 C CA  . SER D 31  ? 0.7170 0.8078 0.6587 0.0946  -0.1179 -0.0273 31  SER D CA  
19862 C C   . SER D 31  ? 0.7209 0.7891 0.6712 0.0828  -0.1083 -0.0169 31  SER D C   
19863 O O   . SER D 31  ? 0.7150 0.7803 0.6848 0.0733  -0.1045 -0.0225 31  SER D O   
19864 C CB  . SER D 31  ? 0.6853 0.7992 0.6639 0.0829  -0.1237 -0.0418 31  SER D CB  
19865 O OG  . SER D 31  ? 0.7263 0.8667 0.7062 0.0925  -0.1337 -0.0593 31  SER D OG  
19871 N N   . PHE D 32  ? 0.7246 0.7796 0.6651 0.0852  -0.1066 -0.0064 32  PHE D N   
19872 C CA  . PHE D 32  ? 0.7012 0.7389 0.6538 0.0760  -0.1025 -0.0023 32  PHE D CA  
19873 C C   . PHE D 32  ? 0.6662 0.6811 0.5951 0.0807  -0.0925 0.0066  32  PHE D C   
19874 O O   . PHE D 32  ? 0.6894 0.7008 0.5943 0.0929  -0.0948 0.0132  32  PHE D O   
19875 C CB  . PHE D 32  ? 0.7142 0.7516 0.6797 0.0706  -0.1127 -0.0013 32  PHE D CB  
19876 C CG  . PHE D 32  ? 0.7426 0.7858 0.7243 0.0642  -0.1189 -0.0088 32  PHE D CG  
19877 C CD1 . PHE D 32  ? 0.7414 0.7735 0.7390 0.0613  -0.1259 -0.0149 32  PHE D CD1 
19878 C CD2 . PHE D 32  ? 0.7731 0.8326 0.7584 0.0618  -0.1182 -0.0140 32  PHE D CD2 
19879 C CE1 . PHE D 32  ? 0.7506 0.7780 0.7568 0.0578  -0.1321 -0.0210 32  PHE D CE1 
19880 C CE2 . PHE D 32  ? 0.7631 0.8201 0.7616 0.0531  -0.1198 -0.0217 32  PHE D CE2 
19881 C CZ  . PHE D 32  ? 0.7561 0.7921 0.7598 0.0519  -0.1268 -0.0228 32  PHE D CZ  
19891 N N   . TRP D 33  ? 0.6623 0.6624 0.6031 0.0713  -0.0810 0.0027  33  TRP D N   
19892 C CA  . TRP D 33  ? 0.6899 0.6625 0.6131 0.0708  -0.0669 0.0081  33  TRP D CA  
19893 C C   . TRP D 33  ? 0.6737 0.6451 0.5981 0.0747  -0.0791 0.0130  33  TRP D C   
19894 O O   . TRP D 33  ? 0.6692 0.6547 0.6101 0.0734  -0.0950 0.0103  33  TRP D O   
19895 C CB  . TRP D 33  ? 0.6884 0.6535 0.6417 0.0546  -0.0494 -0.0064 33  TRP D CB  
19896 C CG  . TRP D 33  ? 0.7702 0.7310 0.7201 0.0472  -0.0280 -0.0139 33  TRP D CG  
19897 C CD1 . TRP D 33  ? 0.8047 0.7614 0.7166 0.0565  -0.0258 -0.0067 33  TRP D CD1 
19898 C CD2 . TRP D 33  ? 0.8348 0.7960 0.8222 0.0289  -0.0042 -0.0350 33  TRP D CD2 
19899 N NE1 . TRP D 33  ? 0.8509 0.7988 0.7641 0.0449  -0.0002 -0.0183 33  TRP D NE1 
19900 C CE2 . TRP D 33  ? 0.8624 0.8148 0.8260 0.0261  0.0163  -0.0367 33  TRP D CE2 
19901 C CE3 . TRP D 33  ? 0.8283 0.7998 0.8721 0.0147  0.0017  -0.0578 33  TRP D CE3 
19902 C CZ2 . TRP D 33  ? 0.8960 0.8479 0.8897 0.0068  0.0484  -0.0593 33  TRP D CZ2 
19903 C CZ3 . TRP D 33  ? 0.8429 0.8211 0.9277 -0.0040 0.0307  -0.0842 33  TRP D CZ3 
19904 C CH2 . TRP D 33  ? 0.8896 0.8572 0.9492 -0.0093 0.0567  -0.0842 33  TRP D CH2 
19915 N N   . MET D 34  ? 0.8562 0.6547 0.6600 0.1030  -0.0415 -0.0446 34  MET D N   
19916 C CA  . MET D 34  ? 0.8629 0.6913 0.6872 0.1060  -0.0469 -0.0390 34  MET D CA  
19917 C C   . MET D 34  ? 0.9124 0.7295 0.7407 0.1053  -0.0315 -0.0443 34  MET D C   
19918 O O   . MET D 34  ? 0.9512 0.7376 0.7531 0.1052  -0.0215 -0.0449 34  MET D O   
19919 C CB  . MET D 34  ? 0.8433 0.6831 0.6481 0.1163  -0.0580 -0.0310 34  MET D CB  
19920 C CG  . MET D 34  ? 0.8372 0.7165 0.6597 0.1266  -0.0640 -0.0279 34  MET D CG  
19921 S SD  . MET D 34  ? 0.8320 0.7704 0.6934 0.1142  -0.0795 -0.0168 34  MET D SD  
19922 C CE  . MET D 34  ? 0.8779 0.8381 0.7275 0.1073  -0.0994 0.0000  34  MET D CE  
19932 N N   . HIS D 35  ? 0.9092 0.7516 0.7682 0.1006  -0.0321 -0.0455 35  HIS D N   
19933 C CA  . HIS D 35  ? 0.8966 0.7318 0.7600 0.0933  -0.0230 -0.0495 35  HIS D CA  
19934 C C   . HIS D 35  ? 0.9166 0.7522 0.7688 0.1012  -0.0321 -0.0537 35  HIS D C   
19935 O O   . HIS D 35  ? 0.9614 0.8260 0.8167 0.1136  -0.0428 -0.0519 35  HIS D O   
19936 C CB  . HIS D 35  ? 0.8337 0.6997 0.7361 0.0828  -0.0191 -0.0485 35  HIS D CB  
19937 C CG  . HIS D 35  ? 0.8334 0.6979 0.7445 0.0834  -0.0075 -0.0479 35  HIS D CG  
19938 N ND1 . HIS D 35  ? 0.8575 0.7323 0.7810 0.0755  0.0084  -0.0464 35  HIS D ND1 
19939 C CD2 . HIS D 35  ? 0.8619 0.7165 0.7674 0.0925  -0.0099 -0.0496 35  HIS D CD2 
19940 C CE1 . HIS D 35  ? 0.8894 0.7660 0.8154 0.0863  0.0184  -0.0488 35  HIS D CE1 
19941 N NE2 . HIS D 35  ? 0.8728 0.7287 0.7843 0.0968  0.0064  -0.0530 35  HIS D NE2 
19949 N N   . TRP D 36  ? 0.9020 0.7055 0.7381 0.0939  -0.0285 -0.0590 36  TRP D N   
19950 C CA  . TRP D 36  ? 0.8720 0.6597 0.6879 0.1041  -0.0377 -0.0691 36  TRP D CA  
19951 C C   . TRP D 36  ? 0.8847 0.6699 0.7101 0.0821  -0.0388 -0.0751 36  TRP D C   
19952 O O   . TRP D 36  ? 0.9237 0.6986 0.7574 0.0582  -0.0313 -0.0686 36  TRP D O   
19953 C CB  . TRP D 36  ? 0.8944 0.6214 0.6649 0.1180  -0.0399 -0.0706 36  TRP D CB  
19954 C CG  . TRP D 36  ? 0.8673 0.6066 0.6274 0.1422  -0.0428 -0.0638 36  TRP D CG  
19955 C CD1 . TRP D 36  ? 0.8571 0.5945 0.6136 0.1383  -0.0382 -0.0526 36  TRP D CD1 
19956 C CD2 . TRP D 36  ? 0.8654 0.6293 0.6167 0.1735  -0.0518 -0.0667 36  TRP D CD2 
19957 N NE1 . TRP D 36  ? 0.8683 0.6256 0.6153 0.1605  -0.0465 -0.0467 36  TRP D NE1 
19958 C CE2 . TRP D 36  ? 0.8532 0.6327 0.6003 0.1834  -0.0539 -0.0534 36  TRP D CE2 
19959 C CE3 . TRP D 36  ? 0.9156 0.6964 0.6605 0.1954  -0.0579 -0.0794 36  TRP D CE3 
19960 C CZ2 . TRP D 36  ? 0.8388 0.6583 0.5820 0.2127  -0.0623 -0.0483 36  TRP D CZ2 
19961 C CZ3 . TRP D 36  ? 0.9173 0.7388 0.6565 0.2297  -0.0632 -0.0766 36  TRP D CZ3 
19962 C CH2 . TRP D 36  ? 0.8714 0.7159 0.6131 0.2372  -0.0655 -0.0591 36  TRP D CH2 
19973 N N   . VAL D 37  ? 0.8876 0.6905 0.7112 0.0894  -0.0485 -0.0864 37  VAL D N   
19974 C CA  . VAL D 37  ? 0.9176 0.7256 0.7483 0.0667  -0.0538 -0.0931 37  VAL D CA  
19975 C C   . VAL D 37  ? 0.9256 0.6905 0.7106 0.0802  -0.0659 -0.1143 37  VAL D C   
19976 O O   . VAL D 37  ? 0.9449 0.7174 0.7112 0.1141  -0.0688 -0.1232 37  VAL D O   
19977 C CB  . VAL D 37  ? 0.9353 0.8193 0.8117 0.0600  -0.0552 -0.0861 37  VAL D CB  
19978 C CG1 . VAL D 37  ? 0.9553 0.8513 0.8386 0.0347  -0.0628 -0.0912 37  VAL D CG1 
19979 C CG2 . VAL D 37  ? 0.9054 0.8173 0.8199 0.0541  -0.0452 -0.0688 37  VAL D CG2 
19989 N N   . LYS D 38  ? 0.9700 0.6914 0.7353 0.0540  -0.0742 -0.1222 38  LYS D N   
19990 C CA  . LYS D 38  ? 1.0306 0.6921 0.7427 0.0635  -0.0894 -0.1471 38  LYS D CA  
19991 C C   . LYS D 38  ? 1.0512 0.7500 0.7719 0.0428  -0.0995 -0.1576 38  LYS D C   
19992 O O   . LYS D 38  ? 1.0376 0.7750 0.7964 0.0058  -0.0987 -0.1426 38  LYS D O   
19993 C CB  . LYS D 38  ? 1.1023 0.6631 0.7717 0.0437  -0.0978 -0.1475 38  LYS D CB  
19994 C CG  . LYS D 38  ? 1.1956 0.6700 0.8008 0.0485  -0.1188 -0.1755 38  LYS D CG  
19995 C CD  . LYS D 38  ? 1.2667 0.6395 0.8348 0.0145  -0.1314 -0.1676 38  LYS D CD  
19996 C CE  . LYS D 38  ? 1.3717 0.6366 0.8668 0.0170  -0.1576 -0.1974 38  LYS D CE  
19997 N NZ  . LYS D 38  ? 1.4928 0.6546 0.9519 -0.0273 -0.1749 -0.1840 38  LYS D NZ  
20011 N N   . GLN D 39  ? 1.0754 0.7691 0.7597 0.0692  -0.1088 -0.1830 39  GLN D N   
20012 C CA  . GLN D 39  ? 1.0796 0.8076 0.7608 0.0520  -0.1204 -0.1963 39  GLN D CA  
20013 C C   . GLN D 39  ? 1.1686 0.8189 0.7737 0.0729  -0.1363 -0.2338 39  GLN D C   
20014 O O   . GLN D 39  ? 1.1549 0.8135 0.7325 0.1227  -0.1326 -0.2514 39  GLN D O   
20015 C CB  . GLN D 39  ? 1.0175 0.8566 0.7416 0.0670  -0.1128 -0.1861 39  GLN D CB  
20016 C CG  . GLN D 39  ? 1.0396 0.9254 0.7619 0.0486  -0.1250 -0.1958 39  GLN D CG  
20017 C CD  . GLN D 39  ? 0.9530 0.9502 0.7213 0.0572  -0.1192 -0.1770 39  GLN D CD  
20018 O OE1 . GLN D 39  ? 0.9178 0.9525 0.6989 0.0873  -0.1092 -0.1676 39  GLN D OE1 
20019 N NE2 . GLN D 39  ? 0.9058 0.9582 0.6993 0.0275  -0.1279 -0.1678 39  GLN D NE2 
20028 N N   . ARG D 40  ? 1.2920 0.8684 0.8612 0.0357  -0.1551 -0.2459 40  ARG D N   
20029 C CA  . ARG D 40  ? 1.4680 0.9542 0.9553 0.0536  -0.1748 -0.2861 40  ARG D CA  
20030 C C   . ARG D 40  ? 1.4960 1.0511 0.9719 0.0674  -0.1790 -0.3085 40  ARG D C   
20031 O O   . ARG D 40  ? 1.4507 1.1061 0.9806 0.0408  -0.1749 -0.2890 40  ARG D O   
20032 C CB  . ARG D 40  ? 1.6157 0.9987 1.0643 0.0002  -0.1993 -0.2904 40  ARG D CB  
20033 C CG  . ARG D 40  ? 1.7444 1.0177 1.1640 -0.0013 -0.2032 -0.2814 40  ARG D CG  
20034 C CD  . ARG D 40  ? 1.9831 1.1253 1.3330 -0.0419 -0.2363 -0.2982 40  ARG D CD  
20035 N NE  . ARG D 40  ? 2.1201 1.1906 1.4694 -0.0774 -0.2412 -0.2688 40  ARG D NE  
20036 C CZ  . ARG D 40  ? 2.1798 1.2943 1.5785 -0.1414 -0.2399 -0.2317 40  ARG D CZ  
20037 N NH1 . ARG D 40  ? 2.1232 1.3491 1.5781 -0.1741 -0.2348 -0.2199 40  ARG D NH1 
20038 N NH2 . ARG D 40  ? 2.2749 1.3283 1.6674 -0.1709 -0.2435 -0.2039 40  ARG D NH2 
20052 N N   . PRO D 41  ? 1.5749 1.0794 0.9785 0.1120  -0.1873 -0.3493 41  PRO D N   
20053 C CA  . PRO D 41  ? 1.5908 1.1651 0.9749 0.1266  -0.1907 -0.3726 41  PRO D CA  
20054 C C   . PRO D 41  ? 1.6392 1.2369 1.0333 0.0635  -0.2088 -0.3690 41  PRO D C   
20055 O O   . PRO D 41  ? 1.6862 1.1864 1.0382 0.0231  -0.2327 -0.3822 41  PRO D O   
20056 C CB  . PRO D 41  ? 1.7114 1.1857 0.9974 0.1794  -0.2020 -0.4238 41  PRO D CB  
20057 C CG  . PRO D 41  ? 1.7220 1.1242 1.0008 0.2152  -0.1938 -0.4169 41  PRO D CG  
20058 C CD  . PRO D 41  ? 1.6568 1.0416 0.9912 0.1571  -0.1933 -0.3755 41  PRO D CD  
20066 N N   . GLY D 42  ? 1.6432 1.3712 1.0932 0.0520  -0.2003 -0.3476 42  GLY D N   
20067 C CA  . GLY D 42  ? 1.7005 1.4699 1.1675 -0.0044 -0.2173 -0.3390 42  GLY D CA  
20068 C C   . GLY D 42  ? 1.6626 1.4307 1.1881 -0.0624 -0.2207 -0.3021 42  GLY D C   
20069 O O   . GLY D 42  ? 1.6464 1.4475 1.1869 -0.1121 -0.2373 -0.2927 42  GLY D O   
20073 N N   . GLN D 43  ? 1.6167 1.3564 1.1754 -0.0566 -0.2053 -0.2799 43  GLN D N   
20074 C CA  . GLN D 43  ? 1.5456 1.2898 1.1574 -0.1048 -0.2042 -0.2449 43  GLN D CA  
20075 C C   . GLN D 43  ? 1.4225 1.2694 1.1200 -0.0940 -0.1797 -0.2067 43  GLN D C   
20076 O O   . GLN D 43  ? 1.3420 1.2539 1.0584 -0.0580 -0.1677 -0.2043 43  GLN D O   
20077 C CB  . GLN D 43  ? 1.5556 1.1810 1.1304 -0.1106 -0.2077 -0.2488 43  GLN D CB  
20078 C CG  . GLN D 43  ? 1.6316 1.1408 1.1256 -0.1400 -0.2393 -0.2787 43  GLN D CG  
20079 C CD  . GLN D 43  ? 1.6258 1.1672 1.1385 -0.2107 -0.2606 -0.2639 43  GLN D CD  
20080 O OE1 . GLN D 43  ? 1.7201 1.2311 1.1799 -0.2310 -0.2869 -0.2913 43  GLN D OE1 
20081 N NE2 . GLN D 43  ? 1.5489 1.1567 1.1354 -0.2472 -0.2498 -0.2207 43  GLN D NE2 
20090 N N   . GLY D 44  ? 1.3830 1.2441 1.1300 -0.1263 -0.1735 -0.1761 44  GLY D N   
20091 C CA  . GLY D 44  ? 1.2262 1.1682 1.0477 -0.1164 -0.1526 -0.1431 44  GLY D CA  
20092 C C   . GLY D 44  ? 1.1075 1.0120 0.9294 -0.0835 -0.1334 -0.1390 44  GLY D C   
20093 O O   . GLY D 44  ? 1.1610 0.9924 0.9302 -0.0579 -0.1345 -0.1607 44  GLY D O   
20097 N N   . LEU D 45  ? 0.9495 0.9043 0.8297 -0.0821 -0.1168 -0.1112 45  LEU D N   
20098 C CA  . LEU D 45  ? 0.9024 0.8339 0.7869 -0.0537 -0.0994 -0.1050 45  LEU D CA  
20099 C C   . LEU D 45  ? 0.9223 0.8137 0.8083 -0.0759 -0.0918 -0.0924 45  LEU D C   
20100 O O   . LEU D 45  ? 0.8919 0.8207 0.8119 -0.1082 -0.0910 -0.0745 45  LEU D O   
20101 C CB  . LEU D 45  ? 0.8070 0.8114 0.7449 -0.0349 -0.0881 -0.0855 45  LEU D CB  
20102 C CG  . LEU D 45  ? 0.7826 0.8391 0.7239 -0.0177 -0.0959 -0.0891 45  LEU D CG  
20103 C CD1 . LEU D 45  ? 0.7063 0.8246 0.7009 -0.0088 -0.0902 -0.0641 45  LEU D CD1 
20104 C CD2 . LEU D 45  ? 0.7959 0.8184 0.6890 0.0144  -0.0963 -0.1098 45  LEU D CD2 
20116 N N   . GLU D 46  ? 0.9617 0.7859 0.8119 -0.0580 -0.0862 -0.0988 46  GLU D N   
20117 C CA  . GLU D 46  ? 1.0103 0.7926 0.8528 -0.0782 -0.0795 -0.0851 46  GLU D CA  
20118 C C   . GLU D 46  ? 0.9999 0.7806 0.8486 -0.0476 -0.0616 -0.0774 46  GLU D C   
20119 O O   . GLU D 46  ? 0.9864 0.7400 0.8091 -0.0138 -0.0627 -0.0897 46  GLU D O   
20120 C CB  . GLU D 46  ? 1.1011 0.7832 0.8797 -0.0936 -0.0970 -0.0989 46  GLU D CB  
20121 C CG  . GLU D 46  ? 1.2365 0.8905 1.0123 -0.1395 -0.0988 -0.0776 46  GLU D CG  
20122 C CD  . GLU D 46  ? 1.4317 0.9790 1.1423 -0.1647 -0.1247 -0.0900 46  GLU D CD  
20123 O OE1 . GLU D 46  ? 1.5188 0.9978 1.1786 -0.1322 -0.1364 -0.1182 46  GLU D OE1 
20124 O OE2 . GLU D 46  ? 1.5136 1.0454 1.2223 -0.2168 -0.1344 -0.0709 46  GLU D OE2 
20131 N N   . TRP D 47  ? 0.9600 0.7753 0.8417 -0.0586 -0.0457 -0.0573 47  TRP D N   
20132 C CA  . TRP D 47  ? 0.9294 0.7475 0.8155 -0.0329 -0.0296 -0.0513 47  TRP D CA  
20133 C C   . TRP D 47  ? 0.9832 0.7328 0.8254 -0.0375 -0.0277 -0.0472 47  TRP D C   
20134 O O   . TRP D 47  ? 1.0574 0.7926 0.8932 -0.0704 -0.0270 -0.0337 47  TRP D O   
20135 C CB  . TRP D 47  ? 0.9181 0.8037 0.8534 -0.0362 -0.0129 -0.0356 47  TRP D CB  
20136 C CG  . TRP D 47  ? 0.9055 0.7901 0.8392 -0.0104 0.0016  -0.0336 47  TRP D CG  
20137 C CD1 . TRP D 47  ? 0.8707 0.7646 0.8115 0.0173  0.0002  -0.0400 47  TRP D CD1 
20138 C CD2 . TRP D 47  ? 0.9285 0.8032 0.8490 -0.0138 0.0176  -0.0240 47  TRP D CD2 
20139 N NE1 . TRP D 47  ? 0.8689 0.7516 0.7985 0.0312  0.0124  -0.0381 47  TRP D NE1 
20140 C CE2 . TRP D 47  ? 0.8950 0.7684 0.8112 0.0150  0.0248  -0.0294 47  TRP D CE2 
20141 C CE3 . TRP D 47  ? 0.9488 0.8182 0.8584 -0.0416 0.0252  -0.0092 47  TRP D CE3 
20142 C CZ2 . TRP D 47  ? 0.9056 0.7719 0.8031 0.0207  0.0404  -0.0248 47  TRP D CZ2 
20143 C CZ3 . TRP D 47  ? 0.9571 0.8275 0.8521 -0.0361 0.0426  -0.0007 47  TRP D CZ3 
20144 C CH2 . TRP D 47  ? 0.9306 0.7991 0.8179 -0.0032 0.0506  -0.0105 47  TRP D CH2 
20155 N N   . ILE D 48  ? 0.9845 0.6981 0.7980 -0.0066 -0.0284 -0.0547 48  ILE D N   
20156 C CA  . ILE D 48  ? 1.0295 0.6760 0.7988 -0.0056 -0.0293 -0.0489 48  ILE D CA  
20157 C C   . ILE D 48  ? 1.0329 0.7040 0.8119 -0.0050 -0.0108 -0.0332 48  ILE D C   
20158 O O   . ILE D 48  ? 1.0333 0.6889 0.7998 -0.0293 -0.0046 -0.0167 48  ILE D O   
20159 C CB  . ILE D 48  ? 0.9992 0.6015 0.7323 0.0314  -0.0403 -0.0632 48  ILE D CB  
20160 C CG1 . ILE D 48  ? 0.9955 0.5784 0.7136 0.0371  -0.0565 -0.0836 48  ILE D CG1 
20161 C CG2 . ILE D 48  ? 1.0622 0.5906 0.7488 0.0346  -0.0441 -0.0540 48  ILE D CG2 
20162 C CD1 . ILE D 48  ? 1.0016 0.5608 0.6888 0.0817  -0.0645 -0.0991 48  ILE D CD1 
20174 N N   . GLY D 49  ? 1.0357 0.7449 0.8330 0.0205  -0.0035 -0.0376 49  GLY D N   
20175 C CA  . GLY D 49  ? 1.0546 0.7794 0.8507 0.0254  0.0119  -0.0289 49  GLY D CA  
20176 C C   . GLY D 49  ? 1.0136 0.7605 0.8188 0.0524  0.0106  -0.0374 49  GLY D C   
20177 O O   . GLY D 49  ? 0.9785 0.7429 0.8004 0.0636  -0.0002 -0.0454 49  GLY D O   
20181 N N   . TYR D 50  ? 1.0025 0.7494 0.7930 0.0595  0.0202  -0.0341 50  TYR D N   
20182 C CA  . TYR D 50  ? 0.9661 0.7224 0.7555 0.0785  0.0147  -0.0407 50  TYR D CA  
20183 C C   . TYR D 50  ? 0.9800 0.7081 0.7269 0.0846  0.0152  -0.0361 50  TYR D C   
20184 O O   . TYR D 50  ? 1.0104 0.7177 0.7322 0.0747  0.0237  -0.0265 50  TYR D O   
20185 C CB  . TYR D 50  ? 0.9632 0.7524 0.7807 0.0821  0.0231  -0.0464 50  TYR D CB  
20186 C CG  . TYR D 50  ? 0.9994 0.7895 0.7986 0.0840  0.0414  -0.0469 50  TYR D CG  
20187 C CD1 . TYR D 50  ? 0.9961 0.7655 0.7603 0.0948  0.0394  -0.0528 50  TYR D CD1 
20188 C CD2 . TYR D 50  ? 1.0402 0.8598 0.8556 0.0746  0.0604  -0.0410 50  TYR D CD2 
20189 C CE1 . TYR D 50  ? 1.0463 0.8190 0.7866 0.0995  0.0571  -0.0565 50  TYR D CE1 
20190 C CE2 . TYR D 50  ? 1.0786 0.9120 0.8758 0.0803  0.0802  -0.0414 50  TYR D CE2 
20191 C CZ  . TYR D 50  ? 1.0695 0.8768 0.8265 0.0945  0.0791  -0.0511 50  TYR D CZ  
20192 O OH  . TYR D 50  ? 1.1117 0.9348 0.8436 0.1030  0.0996  -0.0547 50  TYR D OH  
20202 N N   . ILE D 51  ? 0.9970 0.7281 0.7355 0.0972  0.0038  -0.0397 51  ILE D N   
20203 C CA  . ILE D 51  ? 0.9965 0.7087 0.6948 0.1021  0.0006  -0.0350 51  ILE D CA  
20204 C C   . ILE D 51  ? 0.9895 0.7114 0.6848 0.1052  -0.0057 -0.0440 51  ILE D C   
20205 O O   . ILE D 51  ? 0.9653 0.7042 0.6867 0.1064  -0.0181 -0.0477 51  ILE D O   
20206 C CB  . ILE D 51  ? 0.9607 0.6605 0.6423 0.1137  -0.0153 -0.0261 51  ILE D CB  
20207 C CG1 . ILE D 51  ? 0.9962 0.6864 0.6394 0.1179  -0.0218 -0.0182 51  ILE D CG1 
20208 C CG2 . ILE D 51  ? 0.9354 0.6669 0.6458 0.1231  -0.0301 -0.0293 51  ILE D CG2 
20209 C CD1 . ILE D 51  ? 1.0106 0.6905 0.6355 0.1341  -0.0354 -0.0052 51  ILE D CD1 
20221 N N   . ASN D 52  ? 1.0005 0.7082 0.6593 0.1047  0.0009  -0.0468 52  ASN D N   
20222 C CA  . ASN D 52  ? 1.0150 0.7152 0.6540 0.1062  -0.0107 -0.0574 52  ASN D CA  
20223 C C   . ASN D 52  ? 1.0468 0.7469 0.6640 0.1044  -0.0329 -0.0461 52  ASN D C   
20224 O O   . ASN D 52  ? 1.1163 0.8064 0.6972 0.1047  -0.0315 -0.0377 52  ASN D O   
20225 C CB  . ASN D 52  ? 1.0784 0.7657 0.6810 0.1092  0.0065  -0.0693 52  ASN D CB  
20226 C CG  . ASN D 52  ? 1.1720 0.8362 0.7447 0.1114  -0.0080 -0.0865 52  ASN D CG  
20227 O OD1 . ASN D 52  ? 1.2010 0.8582 0.7650 0.1029  -0.0341 -0.0820 52  ASN D OD1 
20228 N ND2 . ASN D 52  ? 1.2468 0.9000 0.8016 0.1232  0.0076  -0.1062 52  ASN D ND2 
20235 N N   . PRO D 53  ? 1.0303 0.7494 0.6699 0.1017  -0.0544 -0.0416 53  PRO D N   
20236 C CA  . PRO D 53  ? 1.0116 0.7506 0.6398 0.1025  -0.0741 -0.0253 53  PRO D CA  
20237 C C   . PRO D 53  ? 1.0057 0.7303 0.5857 0.0950  -0.0845 -0.0242 53  PRO D C   
20238 O O   . PRO D 53  ? 1.0214 0.7564 0.5819 0.1006  -0.0909 -0.0086 53  PRO D O   
20239 C CB  . PRO D 53  ? 1.0237 0.7975 0.6868 0.0953  -0.0943 -0.0195 53  PRO D CB  
20240 C CG  . PRO D 53  ? 1.0238 0.7931 0.7206 0.0949  -0.0829 -0.0304 53  PRO D CG  
20241 C CD  . PRO D 53  ? 1.0305 0.7612 0.7066 0.0970  -0.0628 -0.0469 53  PRO D CD  
20249 N N   . ASN D 54  ? 1.0452 0.7433 0.6017 0.0845  -0.0878 -0.0412 54  ASN D N   
20250 C CA  . ASN D 54  ? 1.1323 0.8146 0.6360 0.0744  -0.1019 -0.0435 54  ASN D CA  
20251 C C   . ASN D 54  ? 1.1643 0.8331 0.6272 0.0821  -0.0819 -0.0434 54  ASN D C   
20252 O O   . ASN D 54  ? 1.1989 0.8676 0.6190 0.0755  -0.0942 -0.0364 54  ASN D O   
20253 C CB  . ASN D 54  ? 1.2170 0.8609 0.6981 0.0634  -0.1132 -0.0667 54  ASN D CB  
20254 C CG  . ASN D 54  ? 1.3162 0.9494 0.7522 0.0423  -0.1449 -0.0653 54  ASN D CG  
20255 O OD1 . ASN D 54  ? 1.2829 0.9564 0.7284 0.0309  -0.1660 -0.0409 54  ASN D OD1 
20256 N ND2 . ASN D 54  ? 1.4707 1.0518 0.8552 0.0380  -0.1492 -0.0918 54  ASN D ND2 
20263 N N   . SER D 55  ? 1.1501 0.8134 0.6253 0.0923  -0.0531 -0.0474 55  SER D N   
20264 C CA  . SER D 55  ? 1.1574 0.8139 0.5955 0.0944  -0.0331 -0.0428 55  SER D CA  
20265 C C   . SER D 55  ? 1.1953 0.8572 0.6503 0.0982  -0.0234 -0.0194 55  SER D C   
20266 O O   . SER D 55  ? 1.2360 0.8917 0.6581 0.0952  -0.0126 -0.0066 55  SER D O   
20267 C CB  . SER D 55  ? 1.1538 0.8033 0.5830 0.0997  -0.0069 -0.0644 55  SER D CB  
20268 O OG  . SER D 55  ? 1.1250 0.7877 0.6047 0.1040  0.0100  -0.0631 55  SER D OG  
20274 N N   . GLY D 56  ? 1.1928 0.8620 0.6931 0.1039  -0.0285 -0.0135 56  GLY D N   
20275 C CA  . GLY D 56  ? 1.1810 0.8392 0.6906 0.1087  -0.0231 0.0039  56  GLY D CA  
20276 C C   . GLY D 56  ? 1.1709 0.8200 0.6899 0.0995  0.0006  0.0033  56  GLY D C   
20277 O O   . GLY D 56  ? 1.2114 0.8411 0.7374 0.0980  0.0015  0.0164  56  GLY D O   
20281 N N   . TYR D 57  ? 1.1550 0.8180 0.6729 0.0938  0.0182  -0.0111 57  TYR D N   
20282 C CA  . TYR D 57  ? 1.1468 0.8207 0.6810 0.0839  0.0412  -0.0083 57  TYR D CA  
20283 C C   . TYR D 57  ? 1.1224 0.7998 0.7066 0.0825  0.0386  -0.0108 57  TYR D C   
20284 O O   . TYR D 57  ? 1.0849 0.7697 0.6964 0.0917  0.0270  -0.0234 57  TYR D O   
20285 C CB  . TYR D 57  ? 1.2019 0.9013 0.7292 0.0882  0.0608  -0.0263 57  TYR D CB  
20286 C CG  . TYR D 57  ? 1.2566 0.9887 0.8096 0.0804  0.0859  -0.0217 57  TYR D CG  
20287 C CD1 . TYR D 57  ? 1.3208 1.0684 0.8523 0.0641  0.1022  0.0000  57  TYR D CD1 
20288 C CD2 . TYR D 57  ? 1.2545 1.0096 0.8549 0.0871  0.0918  -0.0347 57  TYR D CD2 
20289 C CE1 . TYR D 57  ? 1.3562 1.1479 0.9149 0.0523  0.1240  0.0092  57  TYR D CE1 
20290 C CE2 . TYR D 57  ? 1.3000 1.0981 0.9282 0.0795  0.1135  -0.0270 57  TYR D CE2 
20291 C CZ  . TYR D 57  ? 1.3622 1.1820 0.9706 0.0609  0.1298  -0.0048 57  TYR D CZ  
20292 O OH  . TYR D 57  ? 1.4052 1.2813 1.0448 0.0487  0.1504  0.0076  57  TYR D OH  
20302 N N   . THR D 58  ? 1.1743 0.8469 0.7674 0.0670  0.0473  0.0034  58  THR D N   
20303 C CA  . THR D 58  ? 1.1366 0.8089 0.7689 0.0615  0.0429  0.0010  58  THR D CA  
20304 C C   . THR D 58  ? 1.1338 0.8317 0.7848 0.0391  0.0610  0.0101  58  THR D C   
20305 O O   . THR D 58  ? 1.1564 0.8629 0.7846 0.0245  0.0745  0.0262  58  THR D O   
20306 C CB  . THR D 58  ? 1.1368 0.7628 0.7562 0.0637  0.0241  0.0104  58  THR D CB  
20307 O OG1 . THR D 58  ? 1.1785 0.7706 0.7661 0.0457  0.0260  0.0325  58  THR D OG1 
20308 C CG2 . THR D 58  ? 1.1461 0.7629 0.7489 0.0876  0.0073  0.0074  58  THR D CG2 
20316 N N   . GLU D 59  ? 1.0860 0.8047 0.7794 0.0346  0.0604  0.0028  59  GLU D N   
20317 C CA  . GLU D 59  ? 1.1052 0.8518 0.8226 0.0084  0.0711  0.0152  59  GLU D CA  
20318 C C   . GLU D 59  ? 1.1039 0.8264 0.8397 -0.0023 0.0531  0.0126  59  GLU D C   
20319 O O   . GLU D 59  ? 1.0558 0.7795 0.8101 0.0157  0.0425  -0.0041 59  GLU D O   
20320 C CB  . GLU D 59  ? 1.1025 0.9173 0.8565 0.0155  0.0912  0.0081  59  GLU D CB  
20321 C CG  . GLU D 59  ? 1.1910 1.0340 0.9213 0.0274  0.1125  0.0079  59  GLU D CG  
20322 C CD  . GLU D 59  ? 1.2114 1.1258 0.9770 0.0375  0.1351  0.0037  59  GLU D CD  
20323 O OE1 . GLU D 59  ? 1.1941 1.1503 0.9994 0.0185  0.1389  0.0167  59  GLU D OE1 
20324 O OE2 . GLU D 59  ? 1.2319 1.1602 0.9835 0.0660  0.1476  -0.0132 59  GLU D OE2 
20331 N N   . CYS D 60  ? 1.1802 0.8799 0.9067 -0.0340 0.0482  0.0297  60  CYS D N   
20332 C CA  . CYS D 60  ? 1.2062 0.8685 0.9360 -0.0468 0.0283  0.0248  60  CYS D CA  
20333 C C   . CYS D 60  ? 1.1541 0.8578 0.9155 -0.0842 0.0318  0.0369  60  CYS D C   
20334 O O   . CYS D 60  ? 1.1517 0.9020 0.9232 -0.1062 0.0483  0.0575  60  CYS D O   
20335 C CB  . CYS D 60  ? 1.3390 0.9122 1.0179 -0.0529 0.0095  0.0331  60  CYS D CB  
20336 S SG  . CYS D 60  ? 1.4235 0.9530 1.0693 -0.0059 -0.0008 0.0207  60  CYS D SG  
20342 N N   . ASN D 61  ? 1.1077 0.8033 0.8847 -0.0913 0.0162  0.0250  61  ASN D N   
20343 C CA  . ASN D 61  ? 1.1047 0.8208 0.8998 -0.1356 0.0099  0.0389  61  ASN D CA  
20344 C C   . ASN D 61  ? 1.1872 0.8346 0.9380 -0.1733 -0.0030 0.0605  61  ASN D C   
20345 O O   . ASN D 61  ? 1.1852 0.7436 0.8876 -0.1603 -0.0178 0.0546  61  ASN D O   
20346 C CB  . ASN D 61  ? 1.0951 0.8019 0.9017 -0.1354 -0.0090 0.0190  61  ASN D CB  
20347 C CG  . ASN D 61  ? 1.1234 0.8618 0.9521 -0.1840 -0.0183 0.0328  61  ASN D CG  
20348 O OD1 . ASN D 61  ? 1.1635 0.9125 0.9903 -0.2244 -0.0160 0.0597  61  ASN D OD1 
20349 N ND2 . ASN D 61  ? 1.0988 0.8587 0.9481 -0.1837 -0.0303 0.0174  61  ASN D ND2 
20356 N N   . GLU D 62  ? 1.2463 0.9382 1.0143 -0.2205 0.0016  0.0888  62  GLU D N   
20357 C CA  . GLU D 62  ? 1.3945 1.0230 1.1209 -0.2657 -0.0132 0.1167  62  GLU D CA  
20358 C C   . GLU D 62  ? 1.4219 0.9277 1.0994 -0.2742 -0.0485 0.1017  62  GLU D C   
20359 O O   . GLU D 62  ? 1.4852 0.8980 1.1106 -0.2890 -0.0651 0.1158  62  GLU D O   
20360 C CB  . GLU D 62  ? 1.5364 1.2442 1.2958 -0.3233 -0.0078 0.1514  62  GLU D CB  
20361 C CG  . GLU D 62  ? 1.5916 1.4180 1.3885 -0.3134 0.0288  0.1701  62  GLU D CG  
20362 C CD  . GLU D 62  ? 1.6725 1.5928 1.5046 -0.3697 0.0350  0.2093  62  GLU D CD  
20363 O OE1 . GLU D 62  ? 1.7301 1.6211 1.5591 -0.4223 0.0076  0.2226  62  GLU D OE1 
20364 O OE2 . GLU D 62  ? 1.6632 1.6898 1.5242 -0.3613 0.0666  0.2268  62  GLU D OE2 
20371 N N   . ILE D 63  ? 1.3982 0.8995 1.0875 -0.2623 -0.0610 0.0729  63  ILE D N   
20372 C CA  . ILE D 63  ? 1.4957 0.8816 1.1329 -0.2639 -0.0937 0.0520  63  ILE D CA  
20373 C C   . ILE D 63  ? 1.5331 0.8319 1.1216 -0.2144 -0.0981 0.0377  63  ILE D C   
20374 O O   . ILE D 63  ? 1.7039 0.8914 1.2354 -0.2246 -0.1208 0.0436  63  ILE D O   
20375 C CB  . ILE D 63  ? 1.4813 0.8969 1.1403 -0.2516 -0.1016 0.0212  63  ILE D CB  
20376 C CG1 . ILE D 63  ? 1.4614 0.9625 1.1674 -0.3038 -0.1019 0.0394  63  ILE D CG1 
20377 C CG2 . ILE D 63  ? 1.5783 0.8740 1.1747 -0.2418 -0.1331 -0.0079 63  ILE D CG2 
20378 C CD1 . ILE D 63  ? 1.4083 0.9656 1.1469 -0.2905 -0.1051 0.0154  63  ILE D CD1 
20390 N N   . PHE D 64  ? 1.4240 0.7720 1.0342 -0.1608 -0.0790 0.0211  64  PHE D N   
20391 C CA  . PHE D 64  ? 1.4651 0.7526 1.0382 -0.1090 -0.0838 0.0059  64  PHE D CA  
20392 C C   . PHE D 64  ? 1.4886 0.7710 1.0471 -0.1012 -0.0720 0.0305  64  PHE D C   
20393 O O   . PHE D 64  ? 1.4768 0.7430 1.0190 -0.0554 -0.0707 0.0218  64  PHE D O   
20394 C CB  . PHE D 64  ? 1.4014 0.7504 1.0049 -0.0611 -0.0736 -0.0214 64  PHE D CB  
20395 C CG  . PHE D 64  ? 1.4049 0.7779 1.0265 -0.0681 -0.0824 -0.0431 64  PHE D CG  
20396 C CD1 . PHE D 64  ? 1.4637 0.7670 1.0440 -0.0493 -0.1036 -0.0694 64  PHE D CD1 
20397 C CD2 . PHE D 64  ? 1.3457 0.8122 1.0227 -0.0904 -0.0698 -0.0374 64  PHE D CD2 
20398 C CE1 . PHE D 64  ? 1.4546 0.7837 1.0461 -0.0569 -0.1122 -0.0898 64  PHE D CE1 
20399 C CE2 . PHE D 64  ? 1.3388 0.8318 1.0317 -0.0985 -0.0797 -0.0541 64  PHE D CE2 
20400 C CZ  . PHE D 64  ? 1.3844 0.8100 1.0333 -0.0840 -0.1009 -0.0804 64  PHE D CZ  
20410 N N   . ARG D 65  ? 1.5452 0.8495 1.1087 -0.1457 -0.0638 0.0631  65  ARG D N   
20411 C CA  . ARG D 65  ? 1.6063 0.9190 1.1546 -0.1393 -0.0506 0.0869  65  ARG D CA  
20412 C C   . ARG D 65  ? 1.6155 0.8186 1.1046 -0.1175 -0.0718 0.0916  65  ARG D C   
20413 O O   . ARG D 65  ? 1.5820 0.7914 1.0593 -0.0827 -0.0646 0.0943  65  ARG D O   
20414 C CB  . ARG D 65  ? 1.7295 1.0881 1.2887 -0.1940 -0.0391 0.1241  65  ARG D CB  
20415 C CG  . ARG D 65  ? 1.9047 1.1819 1.4283 -0.2487 -0.0652 0.1507  65  ARG D CG  
20416 C CD  . ARG D 65  ? 1.9330 1.2843 1.4757 -0.3051 -0.0506 0.1930  65  ARG D CD  
20417 N NE  . ARG D 65  ? 2.0428 1.3101 1.5430 -0.3625 -0.0778 0.2291  65  ARG D NE  
20418 C CZ  . ARG D 65  ? 2.0964 1.3286 1.5944 -0.4152 -0.1024 0.2369  65  ARG D CZ  
20419 N NH1 . ARG D 65  ? 2.0324 1.3132 1.5700 -0.4157 -0.1018 0.2107  65  ARG D NH1 
20420 N NH2 . ARG D 65  ? 2.2230 1.3683 1.6764 -0.4708 -0.1307 0.2730  65  ARG D NH2 
20434 N N   . ASP D 66  ? 1.6789 0.7778 1.1280 -0.1365 -0.1004 0.0925  66  ASP D N   
20435 C CA  . ASP D 66  ? 1.7680 0.7490 1.1573 -0.1101 -0.1241 0.0956  66  ASP D CA  
20436 C C   . ASP D 66  ? 1.7603 0.6937 1.1331 -0.0529 -0.1374 0.0550  66  ASP D C   
20437 O O   . ASP D 66  ? 1.8300 0.6734 1.1557 -0.0159 -0.1553 0.0531  66  ASP D O   
20438 C CB  . ASP D 66  ? 1.9162 0.7917 1.2597 -0.1644 -0.1517 0.1234  66  ASP D CB  
20439 C CG  . ASP D 66  ? 1.9590 0.8670 1.3021 -0.2112 -0.1417 0.1729  66  ASP D CG  
20440 O OD1 . ASP D 66  ? 1.9305 0.8804 1.2749 -0.1841 -0.1246 0.1854  66  ASP D OD1 
20441 O OD2 . ASP D 66  ? 2.0259 0.9232 1.3661 -0.2774 -0.1518 0.2009  66  ASP D OD2 
20446 N N   . LYS D 67  ? 1.7073 0.7038 1.1170 -0.0422 -0.1290 0.0244  67  LYS D N   
20447 C CA  . LYS D 67  ? 1.7648 0.7326 1.1593 0.0108  -0.1392 -0.0135 67  LYS D CA  
20448 C C   . LYS D 67  ? 1.6478 0.6913 1.0677 0.0676  -0.1220 -0.0227 67  LYS D C   
20449 O O   . LYS D 67  ? 1.6552 0.6561 1.0449 0.1198  -0.1317 -0.0330 67  LYS D O   
20450 C CB  . LYS D 67  ? 1.8606 0.8626 1.2786 -0.0087 -0.1412 -0.0389 67  LYS D CB  
20451 C CG  . LYS D 67  ? 2.0781 0.9975 1.4640 -0.0644 -0.1657 -0.0349 67  LYS D CG  
20452 C CD  . LYS D 67  ? 2.0977 1.0666 1.5098 -0.0839 -0.1676 -0.0587 67  LYS D CD  
20453 C CE  . LYS D 67  ? 2.1980 1.0856 1.5755 -0.1454 -0.1965 -0.0545 67  LYS D CE  
20454 N NZ  . LYS D 67  ? 2.1475 1.0913 1.5505 -0.1669 -0.2001 -0.0759 67  LYS D NZ  
20468 N N   . ALA D 68  ? 1.5554 0.7106 1.0294 0.0585  -0.0984 -0.0180 68  ALA D N   
20469 C CA  . ALA D 68  ? 1.5154 0.7474 1.0169 0.1017  -0.0859 -0.0273 68  ALA D CA  
20470 C C   . ALA D 68  ? 1.4934 0.7604 1.0003 0.1006  -0.0735 -0.0026 68  ALA D C   
20471 O O   . ALA D 68  ? 1.5465 0.8199 1.0558 0.0619  -0.0645 0.0186  68  ALA D O   
20472 C CB  . ALA D 68  ? 1.4498 0.7738 1.0036 0.0950  -0.0733 -0.0434 68  ALA D CB  
20478 N N   . THR D 69  ? 1.4383 0.7348 0.9456 0.1430  -0.0735 -0.0050 69  THR D N   
20479 C CA  . THR D 69  ? 1.3933 0.7337 0.9053 0.1448  -0.0640 0.0134  69  THR D CA  
20480 C C   . THR D 69  ? 1.2913 0.7152 0.8377 0.1701  -0.0590 0.0008  69  THR D C   
20481 O O   . THR D 69  ? 1.2501 0.6841 0.7978 0.2064  -0.0680 -0.0112 69  THR D O   
20482 C CB  . THR D 69  ? 1.4478 0.7283 0.9149 0.1658  -0.0770 0.0337  69  THR D CB  
20483 O OG1 . THR D 69  ? 1.5366 0.8012 0.9921 0.2175  -0.0906 0.0214  69  THR D OG1 
20484 C CG2 . THR D 69  ? 1.5099 0.6989 0.9396 0.1350  -0.0862 0.0512  69  THR D CG2 
20492 N N   . MET D 70  ? 1.2210 0.7042 0.7924 0.1510  -0.0459 0.0041  70  MET D N   
20493 C CA  . MET D 70  ? 1.1211 0.6763 0.7242 0.1637  -0.0446 -0.0049 70  MET D CA  
20494 C C   . MET D 70  ? 1.1345 0.7119 0.7229 0.1719  -0.0478 0.0088  70  MET D C   
20495 O O   . MET D 70  ? 1.1725 0.7319 0.7378 0.1553  -0.0417 0.0211  70  MET D O   
20496 C CB  . MET D 70  ? 1.0770 0.6735 0.7165 0.1378  -0.0317 -0.0143 70  MET D CB  
20497 C CG  . MET D 70  ? 1.0692 0.6551 0.7260 0.1250  -0.0302 -0.0254 70  MET D CG  
20498 S SD  . MET D 70  ? 1.0451 0.6777 0.7430 0.0951  -0.0141 -0.0290 70  MET D SD  
20499 C CE  . MET D 70  ? 1.1487 0.7633 0.8572 0.0793  -0.0193 -0.0374 70  MET D CE  
20509 N N   . THR D 71  ? 1.1440 0.7677 0.7449 0.1951  -0.0582 0.0083  71  THR D N   
20510 C CA  . THR D 71  ? 1.1704 0.8252 0.7600 0.1990  -0.0661 0.0216  71  THR D CA  
20511 C C   . THR D 71  ? 1.0387 0.7628 0.6616 0.1977  -0.0731 0.0169  71  THR D C   
20512 O O   . THR D 71  ? 0.9579 0.7068 0.6113 0.1984  -0.0714 0.0057  71  THR D O   
20513 C CB  . THR D 71  ? 1.2842 0.9227 0.8467 0.2308  -0.0790 0.0382  71  THR D CB  
20514 O OG1 . THR D 71  ? 1.3333 0.9916 0.9109 0.2654  -0.0859 0.0315  71  THR D OG1 
20515 C CG2 . THR D 71  ? 1.3487 0.9082 0.8734 0.2266  -0.0762 0.0483  71  THR D CG2 
20523 N N   . ALA D 72  ? 0.9807 0.7361 0.5949 0.1919  -0.0837 0.0277  72  ALA D N   
20524 C CA  . ALA D 72  ? 0.9396 0.7553 0.5807 0.1816  -0.0957 0.0284  72  ALA D CA  
20525 C C   . ALA D 72  ? 0.9902 0.8437 0.6163 0.1833  -0.1146 0.0474  72  ALA D C   
20526 O O   . ALA D 72  ? 1.0115 0.8376 0.6019 0.1776  -0.1161 0.0541  72  ALA D O   
20527 C CB  . ALA D 72  ? 0.9143 0.7170 0.5628 0.1515  -0.0896 0.0143  72  ALA D CB  
20533 N N   . ASP D 73  ? 1.0075 0.9322 0.6611 0.1888  -0.1296 0.0589  73  ASP D N   
20534 C CA  . ASP D 73  ? 1.0610 1.0414 0.7094 0.1830  -0.1518 0.0808  73  ASP D CA  
20535 C C   . ASP D 73  ? 0.9902 0.9979 0.6535 0.1435  -0.1670 0.0806  73  ASP D C   
20536 O O   . ASP D 73  ? 0.9479 1.0021 0.6479 0.1386  -0.1709 0.0836  73  ASP D O   
20537 C CB  . ASP D 73  ? 1.1432 1.1961 0.8124 0.2202  -0.1592 0.0998  73  ASP D CB  
20538 C CG  . ASP D 73  ? 1.2517 1.3772 0.9201 0.2140  -0.1834 0.1281  73  ASP D CG  
20539 O OD1 . ASP D 73  ? 1.2977 1.4113 0.9462 0.1755  -0.1974 0.1309  73  ASP D OD1 
20540 O OD2 . ASP D 73  ? 1.3033 1.5000 0.9891 0.2491  -0.1892 0.1471  73  ASP D OD2 
20545 N N   . THR D 74  ? 0.8876 1.0676 0.7939 0.2381  -0.3297 -0.1503 74  THR D N   
20546 C CA  . THR D 74  ? 0.8559 1.0981 0.8411 0.2068  -0.3138 -0.1701 74  THR D CA  
20547 C C   . THR D 74  ? 0.8666 1.1935 0.9519 0.2159  -0.3257 -0.2171 74  THR D C   
20548 O O   . THR D 74  ? 0.8703 1.2415 1.0342 0.1827  -0.2960 -0.2292 74  THR D O   
20549 C CB  . THR D 74  ? 0.9058 1.1340 0.8482 0.2078  -0.3252 -0.1720 74  THR D CB  
20550 O OG1 . THR D 74  ? 0.9484 1.1146 0.8299 0.1809  -0.2975 -0.1340 74  THR D OG1 
20551 C CG2 . THR D 74  ? 0.8940 1.1968 0.9241 0.1882  -0.3208 -0.2062 74  THR D CG2 
20559 N N   . SER D 75  ? 0.9169 1.2644 0.9994 0.2616  -0.3676 -0.2470 75  SER D N   
20560 C CA  . SER D 75  ? 0.9058 1.3418 1.0935 0.2704  -0.3789 -0.3014 75  SER D CA  
20561 C C   . SER D 75  ? 0.8552 1.3201 1.1162 0.2451  -0.3446 -0.3048 75  SER D C   
20562 O O   . SER D 75  ? 0.8627 1.3966 1.2235 0.2250  -0.3271 -0.3437 75  SER D O   
20563 C CB  . SER D 75  ? 1.0200 1.4424 1.1757 0.3195  -0.4113 -0.3230 75  SER D CB  
20564 O OG  . SER D 75  ? 1.1313 1.5022 1.2301 0.3444  -0.4201 -0.2991 75  SER D OG  
20570 N N   . SER D 76  ? 0.8143 1.2226 1.0249 0.2438  -0.3305 -0.2661 76  SER D N   
20571 C CA  . SER D 76  ? 0.7786 1.2026 1.0431 0.2230  -0.2980 -0.2659 76  SER D CA  
20572 C C   . SER D 76  ? 0.7303 1.1121 0.9744 0.1794  -0.2529 -0.2248 76  SER D C   
20573 O O   . SER D 76  ? 0.7077 1.0865 0.9761 0.1634  -0.2246 -0.2175 76  SER D O   
20574 C CB  . SER D 76  ? 0.8302 1.2282 1.0610 0.2583  -0.3180 -0.2598 76  SER D CB  
20575 O OG  . SER D 76  ? 0.8738 1.1859 0.9986 0.2656  -0.3212 -0.2120 76  SER D OG  
20581 N N   . SER D 77  ? 0.7264 1.0757 0.9255 0.1623  -0.2467 -0.2004 77  SER D N   
20582 C CA  . SER D 77  ? 0.7111 1.0242 0.8918 0.1261  -0.2098 -0.1665 77  SER D CA  
20583 C C   . SER D 77  ? 0.7564 1.0233 0.8971 0.1277  -0.1989 -0.1369 77  SER D C   
20584 O O   . SER D 77  ? 0.7839 1.0456 0.9443 0.1063  -0.1690 -0.1272 77  SER D O   
20585 C CB  . SER D 77  ? 0.6684 1.0201 0.9227 0.0944  -0.1757 -0.1847 77  SER D CB  
20586 O OG  . SER D 77  ? 0.7013 1.0912 0.9908 0.0881  -0.1819 -0.2110 77  SER D OG  
20592 N N   . THR D 78  ? 0.7839 1.0110 0.8616 0.1549  -0.2231 -0.1233 78  THR D N   
20593 C CA  . THR D 78  ? 0.7981 0.9814 0.8377 0.1600  -0.2160 -0.1001 78  THR D CA  
20594 C C   . THR D 78  ? 0.7622 0.8768 0.7158 0.1596  -0.2175 -0.0688 78  THR D C   
20595 O O   . THR D 78  ? 0.7815 0.8709 0.6848 0.1793  -0.2392 -0.0687 78  THR D O   
20596 C CB  . THR D 78  ? 0.8416 1.0380 0.8913 0.1957  -0.2397 -0.1192 78  THR D CB  
20597 O OG1 . THR D 78  ? 0.8430 1.1104 0.9825 0.1939  -0.2359 -0.1569 78  THR D OG1 
20598 C CG2 . THR D 78  ? 0.8100 0.9638 0.8281 0.1976  -0.2280 -0.0971 78  THR D CG2 
20606 N N   . ALA D 79  ? 0.7354 0.8180 0.6710 0.1375  -0.1930 -0.0456 79  ALA D N   
20607 C CA  . ALA D 79  ? 0.8194 0.8379 0.6832 0.1327  -0.1871 -0.0214 79  ALA D CA  
20608 C C   . ALA D 79  ? 0.9031 0.8834 0.7349 0.1485  -0.1884 -0.0120 79  ALA D C   
20609 O O   . ALA D 79  ? 0.9120 0.9156 0.7829 0.1493  -0.1825 -0.0172 79  ALA D O   
20610 C CB  . ALA D 79  ? 0.7790 0.7926 0.6502 0.0985  -0.1612 -0.0093 79  ALA D CB  
20616 N N   . TYR D 80  ? 0.9503 0.8659 0.7063 0.1607  -0.1930 0.0015  80  TYR D N   
20617 C CA  . TYR D 80  ? 0.9729 0.8403 0.6880 0.1768  -0.1929 0.0109  80  TYR D CA  
20618 C C   . TYR D 80  ? 1.0114 0.8144 0.6716 0.1538  -0.1672 0.0296  80  TYR D C   
20619 O O   . TYR D 80  ? 1.0651 0.8443 0.6948 0.1372  -0.1565 0.0348  80  TYR D O   
20620 C CB  . TYR D 80  ? 0.9882 0.8243 0.6526 0.2211  -0.2230 0.0056  80  TYR D CB  
20621 C CG  . TYR D 80  ? 0.9310 0.8364 0.6557 0.2479  -0.2519 -0.0223 80  TYR D CG  
20622 C CD1 . TYR D 80  ? 0.8984 0.8414 0.6416 0.2540  -0.2694 -0.0391 80  TYR D CD1 
20623 C CD2 . TYR D 80  ? 0.8943 0.8298 0.6616 0.2664  -0.2606 -0.0365 80  TYR D CD2 
20624 C CE1 . TYR D 80  ? 0.8987 0.9112 0.7067 0.2767  -0.2945 -0.0724 80  TYR D CE1 
20625 C CE2 . TYR D 80  ? 0.8645 0.8692 0.6971 0.2885  -0.2839 -0.0696 80  TYR D CE2 
20626 C CZ  . TYR D 80  ? 0.8908 0.9353 0.7459 0.2932  -0.3009 -0.0890 80  TYR D CZ  
20627 O OH  . TYR D 80  ? 0.9092 1.0289 0.8390 0.3133  -0.3228 -0.1295 80  TYR D OH  
20637 N N   . MET D 81  ? 0.9893 0.7664 0.6415 0.1513  -0.1552 0.0359  81  MET D N   
20638 C CA  . MET D 81  ? 1.0447 0.7560 0.6448 0.1322  -0.1301 0.0475  81  MET D CA  
20639 C C   . MET D 81  ? 1.0943 0.7488 0.6464 0.1554  -0.1323 0.0538  81  MET D C   
20640 O O   . MET D 81  ? 1.0500 0.7343 0.6376 0.1711  -0.1435 0.0483  81  MET D O   
20641 C CB  . MET D 81  ? 1.0130 0.7538 0.6609 0.0977  -0.1078 0.0439  81  MET D CB  
20642 C CG  . MET D 81  ? 1.1383 0.8203 0.7454 0.0744  -0.0798 0.0467  81  MET D CG  
20643 S SD  . MET D 81  ? 1.3028 1.0285 0.9708 0.0394  -0.0610 0.0332  81  MET D SD  
20644 C CE  . MET D 81  ? 1.3349 1.0908 1.0386 0.0559  -0.0725 0.0317  81  MET D CE  
20654 N N   . GLN D 82  ? 1.1643 0.7317 0.6326 0.1568  -0.1184 0.0646  82  GLN D N   
20655 C CA  . GLN D 82  ? 1.2564 0.7515 0.6643 0.1779  -0.1156 0.0724  82  GLN D CA  
20656 C C   . GLN D 82  ? 1.3495 0.7912 0.7336 0.1424  -0.0755 0.0756  82  GLN D C   
20657 O O   . GLN D 82  ? 1.4097 0.8179 0.7655 0.1147  -0.0498 0.0766  82  GLN D O   
20658 C CB  . GLN D 82  ? 1.3288 0.7488 0.6417 0.2166  -0.1325 0.0811  82  GLN D CB  
20659 C CG  . GLN D 82  ? 1.4232 0.7673 0.6705 0.2490  -0.1365 0.0885  82  GLN D CG  
20660 C CD  . GLN D 82  ? 1.5236 0.7870 0.6659 0.2960  -0.1585 0.0965  82  GLN D CD  
20661 O OE1 . GLN D 82  ? 1.5573 0.7601 0.6277 0.2898  -0.1452 0.1055  82  GLN D OE1 
20662 N NE2 . GLN D 82  ? 1.5640 0.8247 0.6941 0.3461  -0.1932 0.0910  82  GLN D NE2 
20671 N N   . LEU D 83  ? 1.3601 0.7971 0.7602 0.1420  -0.0688 0.0732  83  LEU D N   
20672 C CA  . LEU D 83  ? 1.3687 0.7570 0.7517 0.1106  -0.0319 0.0702  83  LEU D CA  
20673 C C   . LEU D 83  ? 1.4490 0.7324 0.7413 0.1328  -0.0226 0.0814  83  LEU D C   
20674 O O   . LEU D 83  ? 1.4812 0.7640 0.7710 0.1658  -0.0441 0.0840  83  LEU D O   
20675 C CB  . LEU D 83  ? 1.2808 0.7359 0.7434 0.0944  -0.0306 0.0569  83  LEU D CB  
20676 C CG  . LEU D 83  ? 1.2043 0.7530 0.7467 0.0779  -0.0403 0.0469  83  LEU D CG  
20677 C CD1 . LEU D 83  ? 1.1691 0.7704 0.7709 0.0736  -0.0439 0.0363  83  LEU D CD1 
20678 C CD2 . LEU D 83  ? 1.1751 0.7208 0.7211 0.0425  -0.0168 0.0385  83  LEU D CD2 
20690 N N   . SER D 84  ? 1.5189 0.7097 0.7347 0.1148  0.0120  0.0867  84  SER D N   
20691 C CA  . SER D 84  ? 1.6687 0.7373 0.7776 0.1358  0.0269  0.0998  84  SER D CA  
20692 C C   . SER D 84  ? 1.6846 0.6987 0.7845 0.0970  0.0752  0.0903  84  SER D C   
20693 O O   . SER D 84  ? 1.5966 0.6569 0.7603 0.0515  0.1005  0.0716  84  SER D O   
20694 C CB  . SER D 84  ? 1.8203 0.8008 0.8243 0.1501  0.0333  0.1144  84  SER D CB  
20695 O OG  . SER D 84  ? 1.8679 0.8573 0.8866 0.1053  0.0650  0.1067  84  SER D OG  
20701 N N   . GLY D 85  ? 1.8004 0.7153 0.8211 0.1175  0.0869  0.1001  85  GLY D N   
20702 C CA  . GLY D 85  ? 1.8479 0.7018 0.8553 0.0827  0.1346  0.0890  85  GLY D CA  
20703 C C   . GLY D 85  ? 1.7520 0.7093 0.8756 0.0569  0.1314  0.0656  85  GLY D C   
20704 O O   . GLY D 85  ? 1.7456 0.7192 0.9132 0.0096  0.1664  0.0426  85  GLY D O   
20708 N N   . LEU D 86  ? 1.6999 0.7260 0.8724 0.0892  0.0897  0.0681  86  LEU D N   
20709 C CA  . LEU D 86  ? 1.6276 0.7585 0.9055 0.0716  0.0794  0.0484  86  LEU D CA  
20710 C C   . LEU D 86  ? 1.6910 0.7894 0.9774 0.0442  0.1129  0.0299  86  LEU D C   
20711 O O   . LEU D 86  ? 1.7687 0.7696 0.9847 0.0522  0.1339  0.0363  86  LEU D O   
20712 C CB  . LEU D 86  ? 1.5968 0.7940 0.9135 0.1124  0.0340  0.0551  86  LEU D CB  
20713 C CG  . LEU D 86  ? 1.5654 0.8321 0.9127 0.1309  0.0001  0.0620  86  LEU D CG  
20714 C CD1 . LEU D 86  ? 1.5286 0.8387 0.9006 0.1732  -0.0375 0.0650  86  LEU D CD1 
20715 C CD2 . LEU D 86  ? 1.4757 0.8320 0.9038 0.0978  0.0019  0.0479  86  LEU D CD2 
20727 N N   . THR D 87  ? 1.6531 0.8333 1.0254 0.0137  0.1164  0.0044  87  THR D N   
20728 C CA  . THR D 87  ? 1.6698 0.8450 1.0707 -0.0110 0.1403  -0.0211 87  THR D CA  
20729 C C   . THR D 87  ? 1.6103 0.8917 1.0959 -0.0042 0.1092  -0.0352 87  THR D C   
20730 O O   . THR D 87  ? 1.5365 0.8804 1.0486 0.0201  0.0743  -0.0218 87  THR D O   
20731 C CB  . THR D 87  ? 1.6454 0.8002 1.0593 -0.0614 0.1853  -0.0494 87  THR D CB  
20732 O OG1 . THR D 87  ? 1.5639 0.8183 1.0562 -0.0784 0.1707  -0.0679 87  THR D OG1 
20733 C CG2 . THR D 87  ? 1.7280 0.7750 1.0509 -0.0698 0.2198  -0.0335 87  THR D CG2 
20741 N N   . SER D 88  ? 1.6281 0.9267 1.1529 -0.0253 0.1233  -0.0641 88  SER D N   
20742 C CA  . SER D 88  ? 1.5144 0.9054 1.1082 -0.0178 0.0950  -0.0791 88  SER D CA  
20743 C C   . SER D 88  ? 1.4200 0.8886 1.0708 -0.0342 0.0844  -0.0955 88  SER D C   
20744 O O   . SER D 88  ? 1.3397 0.8790 1.0299 -0.0179 0.0545  -0.0959 88  SER D O   
20745 C CB  . SER D 88  ? 1.5218 0.9064 1.1358 -0.0313 0.1097  -0.1081 88  SER D CB  
20746 O OG  . SER D 88  ? 1.5572 0.9299 1.1923 -0.0726 0.1435  -0.1427 88  SER D OG  
20752 N N   . GLU D 89  ? 1.4251 0.8764 1.0771 -0.0656 0.1109  -0.1102 89  GLU D N   
20753 C CA  . GLU D 89  ? 1.3765 0.8994 1.0825 -0.0794 0.1008  -0.1278 89  GLU D CA  
20754 C C   . GLU D 89  ? 1.3265 0.8774 1.0237 -0.0566 0.0738  -0.0967 89  GLU D C   
20755 O O   . GLU D 89  ? 1.2840 0.9006 1.0258 -0.0586 0.0570  -0.1066 89  GLU D O   
20756 C CB  . GLU D 89  ? 1.4859 0.9804 1.1973 -0.1209 0.1410  -0.1547 89  GLU D CB  
20757 C CG  . GLU D 89  ? 1.6343 1.1244 1.3802 -0.1507 0.1687  -0.2000 89  GLU D CG  
20758 C CD  . GLU D 89  ? 1.7138 1.2956 1.5456 -0.1665 0.1573  -0.2472 89  GLU D CD  
20759 O OE1 . GLU D 89  ? 1.7513 1.3561 1.6073 -0.1855 0.1668  -0.2604 89  GLU D OE1 
20760 O OE2 . GLU D 89  ? 1.7378 1.3681 1.6109 -0.1571 0.1370  -0.2728 89  GLU D OE2 
20767 N N   . ASP D 90  ? 1.3406 0.8433 0.9822 -0.0334 0.0684  -0.0628 90  ASP D N   
20768 C CA  . ASP D 90  ? 1.2930 0.8259 0.9316 -0.0106 0.0420  -0.0381 90  ASP D CA  
20769 C C   . ASP D 90  ? 1.2292 0.8164 0.8967 0.0180  0.0106  -0.0296 90  ASP D C   
20770 O O   . ASP D 90  ? 1.2068 0.8318 0.8871 0.0328  -0.0094 -0.0162 90  ASP D O   
20771 C CB  . ASP D 90  ? 1.3835 0.8432 0.9501 0.0053  0.0469  -0.0115 90  ASP D CB  
20772 C CG  . ASP D 90  ? 1.4811 0.8780 1.0062 -0.0225 0.0816  -0.0159 90  ASP D CG  
20773 O OD1 . ASP D 90  ? 1.4657 0.9002 1.0313 -0.0513 0.0933  -0.0356 90  ASP D OD1 
20774 O OD2 . ASP D 90  ? 1.5745 0.8801 1.0228 -0.0143 0.0986  -0.0008 90  ASP D OD2 
20779 N N   . SER D 91  ? 1.2011 0.7901 0.8784 0.0244  0.0093  -0.0391 91  SER D N   
20780 C CA  . SER D 91  ? 1.1600 0.7952 0.8616 0.0482  -0.0139 -0.0341 91  SER D CA  
20781 C C   . SER D 91  ? 1.1225 0.8226 0.8676 0.0423  -0.0263 -0.0462 91  SER D C   
20782 O O   . SER D 91  ? 1.1096 0.8287 0.8781 0.0277  -0.0228 -0.0715 91  SER D O   
20783 C CB  . SER D 91  ? 1.1759 0.7928 0.8732 0.0541  -0.0092 -0.0442 91  SER D CB  
20784 O OG  . SER D 91  ? 1.2807 0.8313 0.9324 0.0638  0.0013  -0.0320 91  SER D OG  
20790 N N   . ALA D 92  ? 1.1121 0.8447 0.8673 0.0552  -0.0412 -0.0312 92  ALA D N   
20791 C CA  . ALA D 92  ? 1.1000 0.8822 0.8854 0.0526  -0.0517 -0.0392 92  ALA D CA  
20792 C C   . ALA D 92  ? 1.0162 0.8209 0.8064 0.0676  -0.0623 -0.0201 92  ALA D C   
20793 O O   . ALA D 92  ? 1.0187 0.8086 0.7964 0.0796  -0.0638 -0.0057 92  ALA D O   
20794 C CB  . ALA D 92  ? 1.1720 0.9623 0.9718 0.0289  -0.0445 -0.0550 92  ALA D CB  
20800 N N   . VAL D 93  ? 0.9506 0.7902 0.7594 0.0684  -0.0698 -0.0236 93  VAL D N   
20801 C CA  . VAL D 93  ? 0.9742 0.8350 0.7921 0.0766  -0.0746 -0.0100 93  VAL D CA  
20802 C C   . VAL D 93  ? 0.9116 0.7808 0.7367 0.0632  -0.0751 -0.0082 93  VAL D C   
20803 O O   . VAL D 93  ? 0.8871 0.7630 0.7201 0.0494  -0.0740 -0.0215 93  VAL D O   
20804 C CB  . VAL D 93  ? 1.0834 0.9628 0.9051 0.0862  -0.0778 -0.0130 93  VAL D CB  
20805 C CG1 . VAL D 93  ? 1.1052 1.0017 0.9378 0.0893  -0.0760 -0.0021 93  VAL D CG1 
20806 C CG2 . VAL D 93  ? 1.1408 1.0073 0.9493 0.0996  -0.0745 -0.0146 93  VAL D CG2 
20816 N N   . TYR D 94  ? 0.9007 0.7725 0.7260 0.0681  -0.0774 0.0043  94  TYR D N   
20817 C CA  . TYR D 94  ? 0.9223 0.7985 0.7489 0.0574  -0.0780 0.0069  94  TYR D CA  
20818 C C   . TYR D 94  ? 0.9478 0.8569 0.7969 0.0620  -0.0830 0.0112  94  TYR D C   
20819 O O   . TYR D 94  ? 0.9463 0.8652 0.8043 0.0746  -0.0855 0.0156  94  TYR D O   
20820 C CB  . TYR D 94  ? 0.9309 0.7726 0.7282 0.0612  -0.0774 0.0152  94  TYR D CB  
20821 C CG  . TYR D 94  ? 0.9634 0.7595 0.7311 0.0518  -0.0650 0.0108  94  TYR D CG  
20822 C CD1 . TYR D 94  ? 0.9733 0.7446 0.7264 0.0628  -0.0632 0.0114  94  TYR D CD1 
20823 C CD2 . TYR D 94  ? 0.9951 0.7710 0.7512 0.0296  -0.0510 0.0035  94  TYR D CD2 
20824 C CE1 . TYR D 94  ? 1.0345 0.7589 0.7600 0.0519  -0.0477 0.0056  94  TYR D CE1 
20825 C CE2 . TYR D 94  ? 1.0458 0.7754 0.7764 0.0163  -0.0322 -0.0042 94  TYR D CE2 
20826 C CZ  . TYR D 94  ? 1.0760 0.7784 0.7904 0.0274  -0.0306 -0.0027 94  TYR D CZ  
20827 O OH  . TYR D 94  ? 1.1495 0.8009 0.8380 0.0120  -0.0081 -0.0121 94  TYR D OH  
20837 N N   . TYR D 95  ? 0.9493 0.8759 0.8108 0.0515  -0.0829 0.0063  95  TYR D N   
20838 C CA  . TYR D 95  ? 0.8897 0.8409 0.7697 0.0532  -0.0838 0.0091  95  TYR D CA  
20839 C C   . TYR D 95  ? 0.8376 0.7966 0.7223 0.0449  -0.0864 0.0111  95  TYR D C   
20840 O O   . TYR D 95  ? 0.8514 0.7962 0.7228 0.0341  -0.0850 0.0088  95  TYR D O   
20841 C CB  . TYR D 95  ? 0.8734 0.8332 0.7571 0.0523  -0.0840 0.0022  95  TYR D CB  
20842 C CG  . TYR D 95  ? 0.8299 0.7786 0.6998 0.0651  -0.0832 -0.0004 95  TYR D CG  
20843 C CD1 . TYR D 95  ? 0.8231 0.7670 0.6875 0.0753  -0.0748 0.0060  95  TYR D CD1 
20844 C CD2 . TYR D 95  ? 0.8317 0.7723 0.6929 0.0659  -0.0882 -0.0120 95  TYR D CD2 
20845 C CE1 . TYR D 95  ? 0.8495 0.7751 0.6907 0.0881  -0.0719 0.0043  95  TYR D CE1 
20846 C CE2 . TYR D 95  ? 0.8481 0.7774 0.6918 0.0801  -0.0898 -0.0160 95  TYR D CE2 
20847 C CZ  . TYR D 95  ? 0.8673 0.7863 0.6964 0.0923  -0.0820 -0.0061 95  TYR D CZ  
20848 O OH  . TYR D 95  ? 0.9580 0.8577 0.7593 0.1077  -0.0815 -0.0093 95  TYR D OH  
20858 N N   . CYS D 96  ? 0.7989 0.7786 0.7021 0.0486  -0.0872 0.0129  96  CYS D N   
20859 C CA  . CYS D 96  ? 0.8133 0.8067 0.7251 0.0411  -0.0903 0.0118  96  CYS D CA  
20860 C C   . CYS D 96  ? 0.8066 0.8177 0.7376 0.0350  -0.0845 0.0088  96  CYS D C   
20861 O O   . CYS D 96  ? 0.7883 0.8018 0.7272 0.0406  -0.0767 0.0089  96  CYS D O   
20862 C CB  . CYS D 96  ? 0.8440 0.8493 0.7646 0.0518  -0.0980 0.0106  96  CYS D CB  
20863 S SG  . CYS D 96  ? 0.8743 0.9093 0.8345 0.0592  -0.0908 0.0023  96  CYS D SG  
20868 N N   . ALA D 97  ? 0.8037 0.8207 0.7372 0.0240  -0.0857 0.0055  97  ALA D N   
20869 C CA  . ALA D 97  ? 0.7684 0.7960 0.7146 0.0206  -0.0815 0.0021  97  ALA D CA  
20870 C C   . ALA D 97  ? 0.7876 0.8304 0.7462 0.0103  -0.0827 -0.0013 97  ALA D C   
20871 O O   . ALA D 97  ? 0.8430 0.8822 0.7924 0.0018  -0.0857 -0.0037 97  ALA D O   
20872 C CB  . ALA D 97  ? 0.7491 0.7693 0.6866 0.0214  -0.0843 -0.0045 97  ALA D CB  
20878 N N   . SER D 98  ? 0.7292 0.7846 0.7060 0.0096  -0.0768 -0.0028 98  SER D N   
20879 C CA  . SER D 98  ? 0.7111 0.7826 0.7020 0.0001  -0.0777 -0.0082 98  SER D CA  
20880 C C   . SER D 98  ? 0.6820 0.7515 0.6702 -0.0067 -0.0779 -0.0124 98  SER D C   
20881 O O   . SER D 98  ? 0.6638 0.7231 0.6452 -0.0002 -0.0775 -0.0135 98  SER D O   
20882 C CB  . SER D 98  ? 0.7403 0.8251 0.7562 -0.0012 -0.0675 -0.0130 98  SER D CB  
20883 O OG  . SER D 98  ? 0.7769 0.8439 0.7872 0.0011  -0.0542 -0.0105 98  SER D OG  
20889 N N   . PHE D 99  ? 0.6525 0.7322 0.6453 -0.0173 -0.0800 -0.0177 99  PHE D N   
20890 C CA  . PHE D 99  ? 0.6277 0.7110 0.6246 -0.0253 -0.0794 -0.0266 99  PHE D CA  
20891 C C   . PHE D 99  ? 0.6531 0.7441 0.6661 -0.0244 -0.0754 -0.0302 99  PHE D C   
20892 O O   . PHE D 99  ? 0.6442 0.7458 0.6691 -0.0301 -0.0720 -0.0312 99  PHE D O   
20893 C CB  . PHE D 99  ? 0.6886 0.7716 0.6764 -0.0388 -0.0783 -0.0312 99  PHE D CB  
20894 C CG  . PHE D 99  ? 0.7076 0.7958 0.7044 -0.0502 -0.0737 -0.0457 99  PHE D CG  
20895 C CD1 . PHE D 99  ? 0.7261 0.8173 0.7330 -0.0457 -0.0759 -0.0561 99  PHE D CD1 
20896 C CD2 . PHE D 99  ? 0.7072 0.7995 0.7040 -0.0642 -0.0677 -0.0532 99  PHE D CD2 
20897 C CE1 . PHE D 99  ? 0.7408 0.8455 0.7666 -0.0553 -0.0728 -0.0773 99  PHE D CE1 
20898 C CE2 . PHE D 99  ? 0.7054 0.8066 0.7175 -0.0763 -0.0606 -0.0714 99  PHE D CE2 
20899 C CZ  . PHE D 99  ? 0.7279 0.8384 0.7589 -0.0720 -0.0634 -0.0854 99  PHE D CZ  
20909 N N   . LEU D 100 ? 0.7177 0.8008 0.7283 -0.0149 -0.0769 -0.0343 100 LEU D N   
20910 C CA  . LEU D 100 ? 0.7350 0.8133 0.7505 -0.0105 -0.0724 -0.0371 100 LEU D CA  
20911 C C   . LEU D 100 ? 0.7193 0.8161 0.7525 -0.0219 -0.0740 -0.0493 100 LEU D C   
20912 O O   . LEU D 100 ? 0.7319 0.8289 0.7738 -0.0248 -0.0676 -0.0509 100 LEU D O   
20913 C CB  . LEU D 100 ? 0.7918 0.8478 0.7871 0.0107  -0.0779 -0.0387 100 LEU D CB  
20914 C CG  . LEU D 100 ? 0.8376 0.8744 0.8236 0.0224  -0.0751 -0.0417 100 LEU D CG  
20915 C CD1 . LEU D 100 ? 0.8887 0.8987 0.8634 0.0200  -0.0540 -0.0296 100 LEU D CD1 
20916 C CD2 . LEU D 100 ? 0.8421 0.8584 0.8017 0.0502  -0.0898 -0.0485 100 LEU D CD2 
20928 N N   . GLY D 101 ? 0.7013 0.8115 0.7405 -0.0306 -0.0786 -0.0598 101 GLY D N   
20929 C CA  . GLY D 101 ? 0.6751 0.8013 0.7325 -0.0379 -0.0791 -0.0774 101 GLY D CA  
20930 C C   . GLY D 101 ? 0.6804 0.8104 0.7451 -0.0219 -0.0900 -0.0938 101 GLY D C   
20931 O O   . GLY D 101 ? 0.6871 0.8026 0.7359 -0.0033 -0.0979 -0.0893 101 GLY D O   
20935 N N   . ARG D 102 ? 0.6276 0.7788 0.7172 -0.0271 -0.0916 -0.1165 102 ARG D N   
20936 C CA  . ARG D 102 ? 0.6210 0.7859 0.7269 -0.0090 -0.1066 -0.1416 102 ARG D CA  
20937 C C   . ARG D 102 ? 0.6526 0.8223 0.7597 -0.0072 -0.1118 -0.1507 102 ARG D C   
20938 O O   . ARG D 102 ? 0.6735 0.8449 0.7794 0.0177  -0.1296 -0.1641 102 ARG D O   
20939 C CB  . ARG D 102 ? 0.6222 0.7634 0.7058 0.0231  -0.1194 -0.1354 102 ARG D CB  
20940 C CG  . ARG D 102 ? 0.6051 0.7279 0.6783 0.0201  -0.1084 -0.1196 102 ARG D CG  
20941 C CD  . ARG D 102 ? 0.6139 0.7613 0.7182 0.0104  -0.1069 -0.1397 102 ARG D CD  
20942 N NE  . ARG D 102 ? 0.7058 0.8497 0.8111 0.0402  -0.1239 -0.1585 102 ARG D NE  
20943 C CZ  . ARG D 102 ? 0.8319 1.0114 0.9738 0.0453  -0.1363 -0.1929 102 ARG D CZ  
20944 N NH1 . ARG D 102 ? 0.8973 1.1152 1.0778 0.0171  -0.1272 -0.2123 102 ARG D NH1 
20945 N NH2 . ARG D 102 ? 0.9096 1.0826 1.0475 0.0799  -0.1564 -0.2104 102 ARG D NH2 
20959 N N   . GLY D 103 ? 0.6551 0.8222 0.7591 -0.0313 -0.0969 -0.1441 103 GLY D N   
20960 C CA  . GLY D 103 ? 0.6300 0.7980 0.7358 -0.0342 -0.0969 -0.1541 103 GLY D CA  
20961 C C   . GLY D 103 ? 0.6431 0.7927 0.7231 -0.0099 -0.1104 -0.1393 103 GLY D C   
20962 O O   . GLY D 103 ? 0.6638 0.8219 0.7521 -0.0013 -0.1196 -0.1577 103 GLY D O   
20966 N N   . ALA D 104 ? 0.6755 0.8003 0.7260 0.0002  -0.1097 -0.1100 104 ALA D N   
20967 C CA  . ALA D 104 ? 0.6622 0.7631 0.6832 0.0214  -0.1167 -0.0950 104 ALA D CA  
20968 C C   . ALA D 104 ? 0.6516 0.7340 0.6541 0.0123  -0.1037 -0.0675 104 ALA D C   
20969 O O   . ALA D 104 ? 0.6628 0.7499 0.6719 -0.0038 -0.0941 -0.0597 104 ALA D O   
20970 C CB  . ALA D 104 ? 0.6864 0.7691 0.6869 0.0501  -0.1276 -0.0938 104 ALA D CB  
20976 N N   . MET D 105 ? 0.6612 0.7244 0.6412 0.0249  -0.1050 -0.0563 105 MET D N   
20977 C CA  . MET D 105 ? 0.7048 0.7548 0.6731 0.0201  -0.0944 -0.0361 105 MET D CA  
20978 C C   . MET D 105 ? 0.7390 0.7627 0.6835 0.0374  -0.0892 -0.0246 105 MET D C   
20979 O O   . MET D 105 ? 0.7546 0.7596 0.6751 0.0558  -0.0954 -0.0261 105 MET D O   
20980 C CB  . MET D 105 ? 0.7702 0.8177 0.7335 0.0157  -0.0949 -0.0353 105 MET D CB  
20981 C CG  . MET D 105 ? 0.8395 0.8976 0.8149 -0.0041 -0.0916 -0.0453 105 MET D CG  
20982 S SD  . MET D 105 ? 0.9175 0.9664 0.8874 -0.0088 -0.0903 -0.0558 105 MET D SD  
20983 C CE  . MET D 105 ? 0.9154 0.9836 0.9037 0.0045  -0.1042 -0.0836 105 MET D CE  
20993 N N   . ASP D 106 ? 0.7376 0.7566 0.6865 0.0310  -0.0755 -0.0156 106 ASP D N   
20994 C CA  . ASP D 106 ? 0.7971 0.7823 0.7213 0.0429  -0.0621 -0.0080 106 ASP D CA  
20995 C C   . ASP D 106 ? 0.7536 0.7210 0.6657 0.0443  -0.0468 0.0016  106 ASP D C   
20996 O O   . ASP D 106 ? 0.7880 0.7147 0.6641 0.0578  -0.0345 0.0074  106 ASP D O   
20997 C CB  . ASP D 106 ? 0.8391 0.8257 0.7782 0.0322  -0.0492 -0.0087 106 ASP D CB  
20998 C CG  . ASP D 106 ? 0.8114 0.8333 0.7880 0.0113  -0.0461 -0.0114 106 ASP D CG  
20999 O OD1 . ASP D 106 ? 0.7853 0.8245 0.7699 0.0075  -0.0543 -0.0106 106 ASP D OD1 
21000 O OD2 . ASP D 106 ? 0.7925 0.8214 0.7867 0.0011  -0.0365 -0.0155 106 ASP D OD2 
21005 N N   . TYR D 107 ? 0.7385 0.7305 0.6752 0.0328  -0.0463 0.0021  107 TYR D N   
21006 C CA  . TYR D 107 ? 0.7610 0.7436 0.6962 0.0338  -0.0316 0.0062  107 TYR D CA  
21007 C C   . TYR D 107 ? 0.7342 0.7315 0.6740 0.0355  -0.0447 0.0067  107 TYR D C   
21008 O O   . TYR D 107 ? 0.7253 0.7450 0.6806 0.0285  -0.0577 0.0039  107 TYR D O   
21009 C CB  . TYR D 107 ? 0.7704 0.7694 0.7390 0.0198  -0.0139 0.0003  107 TYR D CB  
21010 C CG  . TYR D 107 ? 0.7967 0.7703 0.7565 0.0161  0.0069  -0.0006 107 TYR D CG  
21011 C CD1 . TYR D 107 ? 0.8184 0.7448 0.7456 0.0215  0.0337  0.0040  107 TYR D CD1 
21012 C CD2 . TYR D 107 ? 0.7834 0.7722 0.7606 0.0075  0.0026  -0.0058 107 TYR D CD2 
21013 C CE1 . TYR D 107 ? 0.8666 0.7557 0.7750 0.0186  0.0570  0.0044  107 TYR D CE1 
21014 C CE2 . TYR D 107 ? 0.8129 0.7722 0.7787 0.0046  0.0232  -0.0066 107 TYR D CE2 
21015 C CZ  . TYR D 107 ? 0.8370 0.7435 0.7664 0.0104  0.0511  -0.0010 107 TYR D CZ  
21016 O OH  . TYR D 107 ? 0.8480 0.7117 0.7559 0.0081  0.0758  -0.0008 107 TYR D OH  
21026 N N   . TRP D 108 ? 0.7597 0.7367 0.6794 0.0456  -0.0388 0.0105  108 TRP D N   
21027 C CA  . TRP D 108 ? 0.7461 0.7279 0.6629 0.0499  -0.0498 0.0110  108 TRP D CA  
21028 C C   . TRP D 108 ? 0.7654 0.7485 0.6931 0.0513  -0.0370 0.0109  108 TRP D C   
21029 O O   . TRP D 108 ? 0.7679 0.7350 0.6912 0.0518  -0.0153 0.0105  108 TRP D O   
21030 C CB  . TRP D 108 ? 0.7948 0.7544 0.6789 0.0632  -0.0584 0.0105  108 TRP D CB  
21031 C CG  . TRP D 108 ? 0.7995 0.7678 0.6837 0.0632  -0.0745 0.0022  108 TRP D CG  
21032 C CD1 . TRP D 108 ? 0.8265 0.7960 0.7121 0.0634  -0.0761 -0.0010 108 TRP D CD1 
21033 C CD2 . TRP D 108 ? 0.7749 0.7533 0.6627 0.0619  -0.0889 -0.0085 108 TRP D CD2 
21034 N NE1 . TRP D 108 ? 0.8449 0.8297 0.7387 0.0635  -0.0924 -0.0147 108 TRP D NE1 
21035 C CE2 . TRP D 108 ? 0.8060 0.7972 0.7033 0.0608  -0.0987 -0.0210 108 TRP D CE2 
21036 C CE3 . TRP D 108 ? 0.7631 0.7399 0.6493 0.0606  -0.0919 -0.0115 108 TRP D CE3 
21037 C CZ2 . TRP D 108 ? 0.8201 0.8273 0.7315 0.0560  -0.1094 -0.0400 108 TRP D CZ2 
21038 C CZ3 . TRP D 108 ? 0.7822 0.7689 0.6774 0.0547  -0.1010 -0.0280 108 TRP D CZ3 
21039 C CH2 . TRP D 108 ? 0.8140 0.8180 0.7247 0.0514  -0.1087 -0.0438 108 TRP D CH2 
21050 N N   . GLY D 109 ? 0.8017 0.7997 0.7414 0.0524  -0.0480 0.0094  109 GLY D N   
21051 C CA  . GLY D 109 ? 0.7740 0.7753 0.7248 0.0583  -0.0402 0.0059  109 GLY D CA  
21052 C C   . GLY D 109 ? 0.7799 0.7534 0.7007 0.0678  -0.0348 0.0101  109 GLY D C   
21053 O O   . GLY D 109 ? 0.7819 0.7364 0.6734 0.0721  -0.0418 0.0139  109 GLY D O   
21057 N N   . GLN D 110 ? 0.8221 0.7963 0.7529 0.0725  -0.0230 0.0055  110 GLN D N   
21058 C CA  . GLN D 110 ? 0.8708 0.8168 0.7707 0.0819  -0.0156 0.0085  110 GLN D CA  
21059 C C   . GLN D 110 ? 0.8619 0.8032 0.7473 0.0887  -0.0357 0.0108  110 GLN D C   
21060 O O   . GLN D 110 ? 0.9041 0.8225 0.7601 0.0966  -0.0352 0.0117  110 GLN D O   
21061 C CB  . GLN D 110 ? 0.9499 0.8986 0.8683 0.0829  0.0071  -0.0002 110 GLN D CB  
21062 C CG  . GLN D 110 ? 1.0199 0.9956 0.9707 0.0893  -0.0043 -0.0093 110 GLN D CG  
21063 C CD  . GLN D 110 ? 1.0530 1.0682 1.0488 0.0863  -0.0144 -0.0203 110 GLN D CD  
21064 O OE1 . GLN D 110 ? 0.9874 1.0126 0.9933 0.0761  -0.0128 -0.0205 110 GLN D OE1 
21065 N NE2 . GLN D 110 ? 1.1335 1.1705 1.1545 0.0982  -0.0269 -0.0314 110 GLN D NE2 
21074 N N   . GLY D 111 ? 0.8387 0.7956 0.7391 0.0861  -0.0515 0.0104  111 GLY D N   
21075 C CA  . GLY D 111 ? 0.8823 0.8255 0.7657 0.0892  -0.0639 0.0116  111 GLY D CA  
21076 C C   . GLY D 111 ? 0.9064 0.8480 0.7959 0.0997  -0.0663 0.0096  111 GLY D C   
21077 O O   . GLY D 111 ? 0.9019 0.8508 0.8057 0.1067  -0.0560 0.0046  111 GLY D O   
21081 N N   . THR D 112 ? 0.9238 0.8515 0.7999 0.1014  -0.0776 0.0120  112 THR D N   
21082 C CA  . THR D 112 ? 0.9066 0.8217 0.7768 0.1163  -0.0832 0.0109  112 THR D CA  
21083 C C   . THR D 112 ? 0.9824 0.8628 0.8227 0.1144  -0.0814 0.0125  112 THR D C   
21084 O O   . THR D 112 ? 1.0688 0.9289 0.8896 0.1033  -0.0822 0.0144  112 THR D O   
21085 C CB  . THR D 112 ? 0.8664 0.7803 0.7326 0.1246  -0.0972 0.0121  112 THR D CB  
21086 O OG1 . THR D 112 ? 0.8738 0.8271 0.7765 0.1271  -0.0999 0.0040  112 THR D OG1 
21087 C CG2 . THR D 112 ? 0.8817 0.7709 0.7292 0.1459  -0.1061 0.0111  112 THR D CG2 
21095 N N   . SER D 113 ? 0.9696 0.8432 0.8085 0.1233  -0.0761 0.0088  113 SER D N   
21096 C CA  . SER D 113 ? 1.0151 0.8570 0.8292 0.1220  -0.0738 0.0068  113 SER D CA  
21097 C C   . SER D 113 ? 1.0255 0.8344 0.8178 0.1320  -0.0788 0.0105  113 SER D C   
21098 O O   . SER D 113 ? 0.9929 0.8072 0.7920 0.1506  -0.0866 0.0110  113 SER D O   
21099 C CB  . SER D 113 ? 1.0688 0.9114 0.8840 0.1297  -0.0663 0.0010  113 SER D CB  
21100 O OG  . SER D 113 ? 1.1547 1.0057 0.9850 0.1453  -0.0647 -0.0009 113 SER D OG  
21106 N N   . VAL D 114 ? 1.0483 0.8203 0.8129 0.1208  -0.0734 0.0102  114 VAL D N   
21107 C CA  . VAL D 114 ? 1.1093 0.8297 0.8364 0.1296  -0.0725 0.0151  114 VAL D CA  
21108 C C   . VAL D 114 ? 1.0954 0.7847 0.8081 0.1233  -0.0606 0.0071  114 VAL D C   
21109 O O   . VAL D 114 ? 1.0414 0.7370 0.7630 0.1027  -0.0517 -0.0041 114 VAL D O   
21110 C CB  . VAL D 114 ? 1.1829 0.8728 0.8807 0.1177  -0.0688 0.0212  114 VAL D CB  
21111 C CG1 . VAL D 114 ? 1.2749 0.8920 0.9162 0.1276  -0.0625 0.0276  114 VAL D CG1 
21112 C CG2 . VAL D 114 ? 1.1697 0.8915 0.8813 0.1260  -0.0827 0.0269  114 VAL D CG2 
21122 N N   . THR D 115 ? 1.1341 0.7930 0.8279 0.1427  -0.0619 0.0091  115 THR D N   
21123 C CA  . THR D 115 ? 1.1681 0.7941 0.8474 0.1387  -0.0499 0.0006  115 THR D CA  
21124 C C   . THR D 115 ? 1.2325 0.7850 0.8596 0.1479  -0.0432 0.0077  115 THR D C   
21125 O O   . THR D 115 ? 1.2579 0.7935 0.8652 0.1759  -0.0565 0.0172  115 THR D O   
21126 C CB  . THR D 115 ? 1.1586 0.8113 0.8606 0.1549  -0.0545 -0.0053 115 THR D CB  
21127 O OG1 . THR D 115 ? 1.0956 0.8039 0.8325 0.1510  -0.0586 -0.0079 115 THR D OG1 
21128 C CG2 . THR D 115 ? 1.2163 0.8448 0.9090 0.1464  -0.0425 -0.0179 115 THR D CG2 
21136 N N   . VAL D 116 ? 1.2837 0.7902 0.8871 0.1257  -0.0219 0.0001  116 VAL D N   
21137 C CA  . VAL D 116 ? 1.3818 0.8005 0.9227 0.1292  -0.0066 0.0072  116 VAL D CA  
21138 C C   . VAL D 116 ? 1.4502 0.8350 0.9835 0.1253  0.0087  -0.0051 116 VAL D C   
21139 O O   . VAL D 116 ? 1.4767 0.8651 1.0286 0.0953  0.0275  -0.0244 116 VAL D O   
21140 C CB  . VAL D 116 ? 1.4155 0.7959 0.9294 0.1003  0.0155  0.0066  116 VAL D CB  
21141 C CG1 . VAL D 116 ? 1.5435 0.8155 0.9767 0.1054  0.0369  0.0163  116 VAL D CG1 
21142 C CG2 . VAL D 116 ? 1.3601 0.7798 0.8857 0.1031  -0.0003 0.0168  116 VAL D CG2 
21152 N N   . SER D 117 ? 1.4720 0.8272 0.9818 0.1567  -0.0005 0.0022  117 SER D N   
21153 C CA  . SER D 117 ? 1.5140 0.8260 1.0083 0.1563  0.0147  -0.0079 117 SER D CA  
21154 C C   . SER D 117 ? 1.5499 0.7910 0.9861 0.1935  0.0085  0.0062  117 SER D C   
21155 O O   . SER D 117 ? 1.5129 0.7610 0.9368 0.2250  -0.0153 0.0191  117 SER D O   
21156 C CB  . SER D 117 ? 1.5103 0.8889 1.0594 0.1578  0.0054  -0.0227 117 SER D CB  
21157 O OG  . SER D 117 ? 1.5298 0.9388 1.0929 0.1922  -0.0168 -0.0153 117 SER D OG  
21163 N N   . SER D 118 ? 1.5804 0.7524 0.9808 0.1915  0.0290  0.0006  118 SER D N   
21164 C CA  . SER D 118 ? 1.6644 0.7595 1.0033 0.2305  0.0234  0.0121  118 SER D CA  
21165 C C   . SER D 118 ? 1.7216 0.8634 1.0984 0.2624  0.0003  0.0054  118 SER D C   
21166 O O   . SER D 118 ? 1.8171 0.9194 1.1577 0.3049  -0.0163 0.0125  118 SER D O   
21167 C CB  . SER D 118 ? 1.7107 0.6984 0.9875 0.2132  0.0611  0.0088  118 SER D CB  
21168 O OG  . SER D 118 ? 1.7120 0.6619 0.9648 0.1747  0.0912  0.0079  118 SER D OG  
21174 N N   . ALA D 119 ? 1.6800 0.9019 1.1252 0.2451  -0.0010 -0.0101 119 ALA D N   
21175 C CA  . ALA D 119 ? 1.6854 0.9483 1.1658 0.2702  -0.0155 -0.0191 119 ALA D CA  
21176 C C   . ALA D 119 ? 1.6396 0.9437 1.1384 0.3080  -0.0455 -0.0136 119 ALA D C   
21177 O O   . ALA D 119 ? 1.5896 0.9264 1.0994 0.3064  -0.0575 -0.0062 119 ALA D O   
21178 C CB  . ALA D 119 ? 1.6276 0.9653 1.1678 0.2450  -0.0106 -0.0349 119 ALA D CB  
21184 N N   . LYS D 120 ? 1.6527 0.9579 1.1594 0.3420  -0.0573 -0.0215 120 LYS D N   
21185 C CA  . LYS D 120 ? 1.6071 0.9633 1.1475 0.3788  -0.0854 -0.0274 120 LYS D CA  
21186 C C   . LYS D 120 ? 1.4769 0.9199 1.0927 0.3715  -0.0831 -0.0451 120 LYS D C   
21187 O O   . LYS D 120 ? 1.4327 0.8829 1.0608 0.3474  -0.0637 -0.0512 120 LYS D O   
21188 C CB  . LYS D 120 ? 1.7065 1.0021 1.2028 0.4281  -0.1023 -0.0288 120 LYS D CB  
21189 C CG  . LYS D 120 ? 1.8201 1.0107 1.2226 0.4403  -0.1017 -0.0092 120 LYS D CG  
21190 C CD  . LYS D 120 ? 1.9363 1.0791 1.2942 0.5022  -0.1313 -0.0111 120 LYS D CD  
21191 C CE  . LYS D 120 ? 2.0758 1.1081 1.3269 0.5131  -0.1281 0.0105  120 LYS D CE  
21192 N NZ  . LYS D 120 ? 2.1699 1.1929 1.3879 0.5590  -0.1584 0.0055  120 LYS D NZ  
21206 N N   . THR D 121 ? 1.4143 0.9210 1.0786 0.3926  -0.1016 -0.0560 121 THR D N   
21207 C CA  . THR D 121 ? 1.3126 0.8968 1.0458 0.3831  -0.0929 -0.0739 121 THR D CA  
21208 C C   . THR D 121 ? 1.2762 0.8472 1.0133 0.3875  -0.0789 -0.0863 121 THR D C   
21209 O O   . THR D 121 ? 1.2843 0.8202 1.0046 0.4198  -0.0887 -0.0932 121 THR D O   
21210 C CB  . THR D 121 ? 1.3192 0.9660 1.1066 0.4099  -0.1128 -0.0920 121 THR D CB  
21211 O OG1 . THR D 121 ? 1.2434 0.9553 1.0950 0.3990  -0.0959 -0.1126 121 THR D OG1 
21212 C CG2 . THR D 121 ? 1.4522 1.0690 1.2224 0.4602  -0.1391 -0.1026 121 THR D CG2 
21220 N N   . THR D 122 ? 1.2386 0.8342 0.9928 0.3576  -0.0569 -0.0895 122 THR D N   
21221 C CA  . THR D 122 ? 1.2274 0.8099 0.9807 0.3575  -0.0413 -0.1014 122 THR D CA  
21222 C C   . THR D 122 ? 1.2278 0.8680 1.0233 0.3426  -0.0235 -0.1144 122 THR D C   
21223 O O   . THR D 122 ? 1.2464 0.9129 1.0477 0.3188  -0.0165 -0.1073 122 THR D O   
21224 C CB  . THR D 122 ? 1.1790 0.7052 0.8842 0.3352  -0.0293 -0.0926 122 THR D CB  
21225 O OG1 . THR D 122 ? 1.2008 0.6632 0.8591 0.3431  -0.0376 -0.0793 122 THR D OG1 
21226 C CG2 . THR D 122 ? 1.1966 0.7044 0.8978 0.3396  -0.0160 -0.1072 122 THR D CG2 
21234 N N   . ALA D 123 ? 1.2312 0.8845 1.0509 0.3574  -0.0140 -0.1338 123 ALA D N   
21235 C CA  . ALA D 123 ? 1.1907 0.8867 1.0418 0.3438  0.0097  -0.1475 123 ALA D CA  
21236 C C   . ALA D 123 ? 1.1855 0.8549 0.9967 0.3214  0.0269  -0.1426 123 ALA D C   
21237 O O   . ALA D 123 ? 1.2221 0.8472 0.9979 0.3213  0.0230  -0.1392 123 ALA D O   
21238 C CB  . ALA D 123 ? 1.2037 0.9242 1.0978 0.3671  0.0167  -0.1744 123 ALA D CB  
21244 N N   . PRO D 124 ? 1.1589 0.8509 0.9717 0.3036  0.0464  -0.1443 124 PRO D N   
21245 C CA  . PRO D 124 ? 1.1454 0.8118 0.9138 0.2890  0.0578  -0.1427 124 PRO D CA  
21246 C C   . PRO D 124 ? 1.2196 0.8708 0.9807 0.2981  0.0743  -0.1601 124 PRO D C   
21247 O O   . PRO D 124 ? 1.1972 0.8675 0.9937 0.3111  0.0863  -0.1757 124 PRO D O   
21248 C CB  . PRO D 124 ? 1.0773 0.7644 0.8408 0.2737  0.0730  -0.1379 124 PRO D CB  
21249 C CG  . PRO D 124 ? 1.0961 0.8226 0.9128 0.2787  0.0840  -0.1472 124 PRO D CG  
21250 C CD  . PRO D 124 ? 1.1358 0.8720 0.9847 0.2965  0.0584  -0.1480 124 PRO D CD  
21258 N N   . SER D 125 ? 0.7589 0.7872 0.8961 0.1458  -0.0147 -0.0215 125 SER D N   
21259 C CA  . SER D 125 ? 0.8258 0.8745 0.9874 0.1659  0.0085  -0.0372 125 SER D CA  
21260 C C   . SER D 125 ? 0.8633 0.9229 0.9941 0.1583  0.0106  -0.0524 125 SER D C   
21261 O O   . SER D 125 ? 0.8988 0.9306 0.9974 0.1495  0.0067  -0.0725 125 SER D O   
21262 C CB  . SER D 125 ? 0.8481 0.8618 1.0191 0.1822  0.0243  -0.0632 125 SER D CB  
21263 O OG  . SER D 125 ? 0.8889 0.8934 1.0956 0.1912  0.0246  -0.0428 125 SER D OG  
21269 N N   . VAL D 126 ? 0.8301 0.9346 0.9773 0.1626  0.0177  -0.0366 126 VAL D N   
21270 C CA  . VAL D 126 ? 0.8319 0.9545 0.9539 0.1565  0.0207  -0.0404 126 VAL D CA  
21271 C C   . VAL D 126 ? 0.8693 0.9999 0.9758 0.1814  0.0468  -0.0667 126 VAL D C   
21272 O O   . VAL D 126 ? 0.9058 1.0599 1.0369 0.2053  0.0697  -0.0627 126 VAL D O   
21273 C CB  . VAL D 126 ? 0.7851 0.9535 0.9364 0.1445  0.0134  -0.0014 126 VAL D CB  
21274 C CG1 . VAL D 126 ? 0.7712 0.9567 0.8999 0.1377  0.0173  0.0011  126 VAL D CG1 
21275 C CG2 . VAL D 126 ? 0.7551 0.9054 0.9126 0.1182  -0.0193 0.0178  126 VAL D CG2 
21285 N N   . TYR D 127 ? 0.8655 0.9756 0.9296 0.1771  0.0430  -0.0936 127 TYR D N   
21286 C CA  . TYR D 127 ? 0.8726 0.9813 0.9036 0.1967  0.0587  -0.1253 127 TYR D CA  
21287 C C   . TYR D 127 ? 0.9363 1.0760 0.9311 0.1925  0.0589  -0.1173 127 TYR D C   
21288 O O   . TYR D 127 ? 0.9475 1.0800 0.9327 0.1714  0.0391  -0.1095 127 TYR D O   
21289 C CB  . TYR D 127 ? 0.8072 0.8650 0.8231 0.1931  0.0463  -0.1632 127 TYR D CB  
21290 C CG  . TYR D 127 ? 0.7740 0.7990 0.8285 0.1985  0.0483  -0.1677 127 TYR D CG  
21291 C CD1 . TYR D 127 ? 0.7768 0.8095 0.8599 0.2219  0.0695  -0.1633 127 TYR D CD1 
21292 C CD2 . TYR D 127 ? 0.7800 0.7695 0.8480 0.1825  0.0322  -0.1703 127 TYR D CD2 
21293 C CE1 . TYR D 127 ? 0.7877 0.7914 0.9118 0.2279  0.0710  -0.1612 127 TYR D CE1 
21294 C CE2 . TYR D 127 ? 0.7817 0.7440 0.8869 0.1879  0.0355  -0.1671 127 TYR D CE2 
21295 C CZ  . TYR D 127 ? 0.8049 0.7733 0.9380 0.2099  0.0530  -0.1624 127 TYR D CZ  
21296 O OH  . TYR D 127 ? 0.8592 0.8012 1.0346 0.2162  0.0559  -0.1534 127 TYR D OH  
21306 N N   . PRO D 128 ? 0.9595 1.1341 0.9338 0.2145  0.0838  -0.1155 128 PRO D N   
21307 C CA  . PRO D 128 ? 0.9870 1.1917 0.9195 0.2126  0.0846  -0.1055 128 PRO D CA  
21308 C C   . PRO D 128 ? 1.0608 1.2345 0.9362 0.2108  0.0673  -0.1460 128 PRO D C   
21309 O O   . PRO D 128 ? 1.1434 1.2770 1.0041 0.2191  0.0641  -0.1874 128 PRO D O   
21310 C CB  . PRO D 128 ? 1.0098 1.2606 0.9341 0.2427  0.1230  -0.0911 128 PRO D CB  
21311 C CG  . PRO D 128 ? 1.0318 1.2556 0.9666 0.2671  0.1413  -0.1208 128 PRO D CG  
21312 C CD  . PRO D 128 ? 0.9901 1.1788 0.9769 0.2463  0.1166  -0.1198 128 PRO D CD  
21320 N N   . LEU D 129 ? 1.0205 1.2129 0.8703 0.1981  0.0530  -0.1308 129 LEU D N   
21321 C CA  . LEU D 129 ? 1.0145 1.1886 0.8164 0.1926  0.0291  -0.1601 129 LEU D CA  
21322 C C   . LEU D 129 ? 1.0276 1.2451 0.7710 0.2038  0.0367  -0.1454 129 LEU D C   
21323 O O   . LEU D 129 ? 1.0468 1.2952 0.8022 0.1920  0.0311  -0.1044 129 LEU D O   
21324 C CB  . LEU D 129 ? 1.0008 1.1545 0.8369 0.1659  -0.0002 -0.1503 129 LEU D CB  
21325 C CG  . LEU D 129 ? 0.9873 1.1005 0.8738 0.1557  -0.0052 -0.1584 129 LEU D CG  
21326 C CD1 . LEU D 129 ? 0.9344 1.0323 0.8474 0.1355  -0.0254 -0.1447 129 LEU D CD1 
21327 C CD2 . LEU D 129 ? 1.0534 1.1304 0.9345 0.1644  -0.0072 -0.2015 129 LEU D CD2 
21339 N N   . ALA D 130 ? 1.0426 1.2586 0.7188 0.2285  0.0509  -0.1786 130 ALA D N   
21340 C CA  . ALA D 130 ? 1.0987 1.3526 0.6984 0.2432  0.0586  -0.1696 130 ALA D CA  
21341 C C   . ALA D 130 ? 1.1319 1.3633 0.6709 0.2320  0.0170  -0.2044 130 ALA D C   
21342 O O   . ALA D 130 ? 1.1608 1.3420 0.7075 0.2214  -0.0087 -0.2483 130 ALA D O   
21343 C CB  . ALA D 130 ? 1.1901 1.4553 0.7375 0.2818  0.1029  -0.1859 130 ALA D CB  
21349 N N   . PRO D 131 ? 1.1218 1.3920 0.6056 0.2326  0.0068  -0.1814 131 PRO D N   
21350 C CA  . PRO D 131 ? 1.1950 1.4503 0.6187 0.2211  -0.0393 -0.2116 131 PRO D CA  
21351 C C   . PRO D 131 ? 1.3843 1.6018 0.7114 0.2417  -0.0395 -0.2773 131 PRO D C   
21352 O O   . PRO D 131 ? 1.5022 1.7166 0.7915 0.2732  0.0052  -0.2920 131 PRO D O   
21353 C CB  . PRO D 131 ? 1.1745 1.4896 0.5634 0.2214  -0.0438 -0.1593 131 PRO D CB  
21354 C CG  . PRO D 131 ? 1.1499 1.5068 0.5416 0.2447  0.0105  -0.1184 131 PRO D CG  
21355 C CD  . PRO D 131 ? 1.0772 1.4099 0.5576 0.2421  0.0340  -0.1206 131 PRO D CD  
21363 N N   . VAL D 132 ? 1.4210 1.6071 0.7116 0.2236  -0.0915 -0.3171 132 VAL D N   
21364 C CA  . VAL D 132 ? 1.5672 1.7013 0.7628 0.2378  -0.1022 -0.3889 132 VAL D CA  
21365 C C   . VAL D 132 ? 1.6908 1.8491 0.7758 0.2568  -0.0840 -0.3798 132 VAL D C   
21366 O O   . VAL D 132 ? 1.7041 1.9227 0.7633 0.2552  -0.0917 -0.3315 132 VAL D O   
21367 C CB  . VAL D 132 ? 1.6142 1.7047 0.8207 0.2039  -0.1703 -0.4290 132 VAL D CB  
21368 C CG1 . VAL D 132 ? 1.7136 1.7240 0.8805 0.2028  -0.1712 -0.4903 132 VAL D CG1 
21369 C CG2 . VAL D 132 ? 1.5058 1.5894 0.8511 0.1746  -0.1842 -0.4031 132 VAL D CG2 
21379 N N   . CYS D 133 ? 1.8134 1.9220 0.8386 0.2739  -0.0572 -0.4216 133 CYS D N   
21380 C CA  . CYS D 133 ? 1.9907 2.1121 0.9069 0.2927  -0.0344 -0.4179 133 CYS D CA  
21381 C C   . CYS D 133 ? 1.9586 2.0903 0.8069 0.2664  -0.0937 -0.4161 133 CYS D C   
21382 O O   . CYS D 133 ? 1.9192 2.1075 0.7194 0.2738  -0.0868 -0.3699 133 CYS D O   
21383 C CB  . CYS D 133 ? 2.2580 2.3097 1.1189 0.3112  -0.0040 -0.4753 133 CYS D CB  
21384 S SG  . CYS D 133 ? 2.3134 2.2968 1.2726 0.3109  0.0079  -0.5166 133 CYS D SG  
21389 N N   . GLY D 138 ? 1.7987 2.5021 0.8925 0.2168  -0.1789 0.2578  138 GLY D N   
21390 C CA  . GLY D 138 ? 1.7240 2.4171 0.8517 0.2304  -0.1263 0.2420  138 GLY D CA  
21391 C C   . GLY D 138 ? 1.6687 2.4050 0.8727 0.2388  -0.0768 0.3208  138 GLY D C   
21392 O O   . GLY D 138 ? 1.7478 2.5026 0.9221 0.2597  -0.0254 0.3331  138 GLY D O   
21395 N N   . SER D 139 ? 1.5311 2.2800 0.8430 0.2219  -0.0923 0.3758  139 SER D N   
21396 C CA  . SER D 139 ? 1.4349 2.2127 0.8366 0.2225  -0.0537 0.4522  139 SER D CA  
21397 C C   . SER D 139 ? 1.3471 2.0990 0.8344 0.2159  -0.0298 0.4484  139 SER D C   
21398 O O   . SER D 139 ? 1.3677 2.1388 0.9011 0.2205  0.0135  0.4903  139 SER D O   
21399 C CB  . SER D 139 ? 1.3768 2.1694 0.8540 0.2074  -0.0819 0.5156  139 SER D CB  
21400 O OG  . SER D 139 ? 1.2957 2.0557 0.8368 0.1906  -0.1216 0.4990  139 SER D OG  
21406 N N   . SER D 140 ? 1.2793 1.9713 0.8110 0.1985  -0.0562 0.3894  140 SER D N   
21407 C CA  . SER D 140 ? 1.2146 1.8568 0.8324 0.1861  -0.0363 0.3637  140 SER D CA  
21408 C C   . SER D 140 ? 1.1834 1.7832 0.7566 0.1886  -0.0415 0.2781  140 SER D C   
21409 O O   . SER D 140 ? 1.1883 1.7803 0.6927 0.1906  -0.0734 0.2345  140 SER D O   
21410 C CB  . SER D 140 ? 1.1813 1.7836 0.9093 0.1636  -0.0572 0.3821  140 SER D CB  
21411 O OG  . SER D 140 ? 1.1744 1.7357 0.9057 0.1544  -0.0908 0.3274  140 SER D OG  
21417 N N   . VAL D 141 ? 1.1621 1.7338 0.7808 0.1868  -0.0131 0.2571  141 VAL D N   
21418 C CA  . VAL D 141 ? 1.2148 1.7454 0.8061 0.1910  -0.0113 0.1841  141 VAL D CA  
21419 C C   . VAL D 141 ? 1.1456 1.6241 0.8318 0.1707  -0.0153 0.1682  141 VAL D C   
21420 O O   . VAL D 141 ? 1.1154 1.5937 0.8737 0.1608  0.0003  0.2075  141 VAL D O   
21421 C CB  . VAL D 141 ? 1.3052 1.8601 0.8439 0.2171  0.0337  0.1748  141 VAL D CB  
21422 C CG1 . VAL D 141 ? 1.2668 1.8520 0.8835 0.2157  0.0708  0.2348  141 VAL D CG1 
21423 C CG2 . VAL D 141 ? 1.3296 1.8360 0.8519 0.2227  0.0366  0.1021  141 VAL D CG2 
21433 N N   . THR D 142 ? 1.1161 1.5489 0.8000 0.1637  -0.0377 0.1117  142 THR D N   
21434 C CA  . THR D 142 ? 1.0157 1.3977 0.7732 0.1479  -0.0405 0.0928  142 THR D CA  
21435 C C   . THR D 142 ? 1.0057 1.3636 0.7484 0.1566  -0.0229 0.0456  142 THR D C   
21436 O O   . THR D 142 ? 1.0373 1.3823 0.7260 0.1655  -0.0318 -0.0012 142 THR D O   
21437 C CB  . THR D 142 ? 0.9902 1.3422 0.7737 0.1343  -0.0751 0.0760  142 THR D CB  
21438 O OG1 . THR D 142 ? 1.0147 1.3891 0.8259 0.1290  -0.0885 0.1262  142 THR D OG1 
21439 C CG2 . THR D 142 ? 0.9205 1.2194 0.7658 0.1229  -0.0717 0.0551  142 THR D CG2 
21447 N N   . LEU D 143 ? 0.9609 1.3110 0.7545 0.1532  -0.0011 0.0591  143 LEU D N   
21448 C CA  . LEU D 143 ? 0.9569 1.2840 0.7572 0.1600  0.0140  0.0238  143 LEU D CA  
21449 C C   . LEU D 143 ? 0.9369 1.2135 0.7933 0.1414  -0.0008 0.0099  143 LEU D C   
21450 O O   . LEU D 143 ? 0.9309 1.1913 0.8227 0.1255  -0.0149 0.0310  143 LEU D O   
21451 C CB  . LEU D 143 ? 0.9425 1.3074 0.7621 0.1712  0.0483  0.0552  143 LEU D CB  
21452 C CG  . LEU D 143 ? 0.9573 1.3804 0.7262 0.1930  0.0736  0.0836  143 LEU D CG  
21453 C CD1 . LEU D 143 ? 0.9481 1.4125 0.7603 0.2033  0.1108  0.1219  143 LEU D CD1 
21454 C CD2 . LEU D 143 ? 1.0087 1.4264 0.6835 0.2166  0.0760  0.0344  143 LEU D CD2 
21466 N N   . GLY D 144 ? 0.9169 1.1663 0.7786 0.1462  0.0052  -0.0248 144 GLY D N   
21467 C CA  . GLY D 144 ? 0.8617 1.0643 0.7629 0.1322  -0.0067 -0.0393 144 GLY D CA  
21468 C C   . GLY D 144 ? 0.8665 1.0592 0.7919 0.1364  0.0074  -0.0467 144 GLY D C   
21469 O O   . GLY D 144 ? 0.8997 1.1193 0.8155 0.1533  0.0281  -0.0471 144 GLY D O   
21473 N N   . CYS D 145 ? 0.8340 0.9886 0.7899 0.1232  -0.0025 -0.0499 145 CYS D N   
21474 C CA  . CYS D 145 ? 0.8319 0.9756 0.8127 0.1245  0.0039  -0.0527 145 CYS D CA  
21475 C C   . CYS D 145 ? 0.8218 0.9167 0.8095 0.1174  -0.0072 -0.0727 145 CYS D C   
21476 O O   . CYS D 145 ? 0.7993 0.8685 0.7886 0.1052  -0.0177 -0.0671 145 CYS D O   
21477 C CB  . CYS D 145 ? 0.8679 1.0290 0.8820 0.1119  0.0024  -0.0155 145 CYS D CB  
21478 S SG  . CYS D 145 ? 0.9446 1.1148 0.9964 0.1152  0.0070  -0.0075 145 CYS D SG  
21483 N N   . LEU D 146 ? 0.8272 0.9087 0.8209 0.1276  -0.0011 -0.0929 146 LEU D N   
21484 C CA  . LEU D 146 ? 0.8057 0.8460 0.8088 0.1239  -0.0069 -0.1073 146 LEU D CA  
21485 C C   . LEU D 146 ? 0.8022 0.8342 0.8249 0.1232  -0.0056 -0.0943 146 LEU D C   
21486 O O   . LEU D 146 ? 0.8118 0.8606 0.8510 0.1359  0.0042  -0.0939 146 LEU D O   
21487 C CB  . LEU D 146 ? 0.8711 0.8980 0.8715 0.1339  -0.0053 -0.1387 146 LEU D CB  
21488 C CG  . LEU D 146 ? 0.9243 0.9132 0.9473 0.1302  -0.0087 -0.1479 146 LEU D CG  
21489 C CD1 . LEU D 146 ? 0.9592 0.9344 0.9851 0.1179  -0.0160 -0.1368 146 LEU D CD1 
21490 C CD2 . LEU D 146 ? 0.9705 0.9443 0.9997 0.1370  -0.0112 -0.1792 146 LEU D CD2 
21502 N N   . VAL D 147 ? 0.8109 0.8164 0.8292 0.1104  -0.0154 -0.0830 147 VAL D N   
21503 C CA  . VAL D 147 ? 0.8424 0.8374 0.8676 0.1065  -0.0220 -0.0689 147 VAL D CA  
21504 C C   . VAL D 147 ? 0.8547 0.8124 0.8738 0.1104  -0.0181 -0.0781 147 VAL D C   
21505 O O   . VAL D 147 ? 0.9136 0.8413 0.9107 0.1048  -0.0186 -0.0794 147 VAL D O   
21506 C CB  . VAL D 147 ? 0.8508 0.8380 0.8626 0.0881  -0.0393 -0.0508 147 VAL D CB  
21507 C CG1 . VAL D 147 ? 0.9076 0.8898 0.9225 0.0816  -0.0545 -0.0355 147 VAL D CG1 
21508 C CG2 . VAL D 147 ? 0.7955 0.8215 0.8242 0.0826  -0.0405 -0.0356 147 VAL D CG2 
21518 N N   . LYS D 148 ? 0.8248 0.7840 0.8678 0.1223  -0.0105 -0.0812 148 LYS D N   
21519 C CA  . LYS D 148 ? 0.8327 0.7623 0.8845 0.1275  -0.0029 -0.0869 148 LYS D CA  
21520 C C   . LYS D 148 ? 0.8743 0.7963 0.9356 0.1321  -0.0038 -0.0669 148 LYS D C   
21521 O O   . LYS D 148 ? 0.8715 0.8159 0.9564 0.1390  -0.0058 -0.0567 148 LYS D O   
21522 C CB  . LYS D 148 ? 0.7919 0.7215 0.8702 0.1366  0.0048  -0.1104 148 LYS D CB  
21523 C CG  . LYS D 148 ? 0.8510 0.7514 0.9531 0.1367  0.0099  -0.1139 148 LYS D CG  
21524 C CD  . LYS D 148 ? 0.9073 0.8012 1.0346 0.1403  0.0083  -0.1423 148 LYS D CD  
21525 C CE  . LYS D 148 ? 0.9869 0.8541 1.1541 0.1352  0.0093  -0.1411 148 LYS D CE  
21526 N NZ  . LYS D 148 ? 1.0736 0.9242 1.2666 0.1419  0.0207  -0.1168 148 LYS D NZ  
21540 N N   . GLY D 149 ? 0.9489 0.8425 0.9933 0.1307  -0.0002 -0.0570 149 GLY D N   
21541 C CA  . GLY D 149 ? 0.9657 0.8509 1.0168 0.1372  0.0007  -0.0343 149 GLY D CA  
21542 C C   . GLY D 149 ? 0.9836 0.8779 1.0047 0.1304  -0.0196 -0.0129 149 GLY D C   
21543 O O   . GLY D 149 ? 1.0144 0.9275 1.0644 0.1366  -0.0263 0.0070  149 GLY D O   
21547 N N   . TYR D 150 ? 0.9961 0.8750 0.9629 0.1175  -0.0320 -0.0162 150 TYR D N   
21548 C CA  . TYR D 150 ? 1.0239 0.9028 0.9544 0.1055  -0.0601 0.0002  150 TYR D CA  
21549 C C   . TYR D 150 ? 1.0607 0.8942 0.9148 0.1043  -0.0606 0.0015  150 TYR D C   
21550 O O   . TYR D 150 ? 1.0523 0.8576 0.8847 0.1122  -0.0359 -0.0107 150 TYR D O   
21551 C CB  . TYR D 150 ? 1.0306 0.9245 0.9607 0.0882  -0.0805 -0.0063 150 TYR D CB  
21552 C CG  . TYR D 150 ? 1.0276 0.8893 0.9195 0.0813  -0.0746 -0.0281 150 TYR D CG  
21553 C CD1 . TYR D 150 ? 0.9544 0.8270 0.8746 0.0875  -0.0547 -0.0429 150 TYR D CD1 
21554 C CD2 . TYR D 150 ? 1.0782 0.8956 0.9037 0.0695  -0.0905 -0.0339 150 TYR D CD2 
21555 C CE1 . TYR D 150 ? 0.9492 0.7966 0.8445 0.0831  -0.0495 -0.0562 150 TYR D CE1 
21556 C CE2 . TYR D 150 ? 1.0743 0.8576 0.8716 0.0671  -0.0816 -0.0524 150 TYR D CE2 
21557 C CZ  . TYR D 150 ? 1.0073 0.8092 0.8456 0.0743  -0.0605 -0.0601 150 TYR D CZ  
21558 O OH  . TYR D 150 ? 0.9886 0.7606 0.8083 0.0738  -0.0517 -0.0721 150 TYR D OH  
21568 N N   . PHE D 151 ? 1.0956 0.9240 0.9081 0.0954  -0.0891 0.0182  151 PHE D N   
21569 C CA  . PHE D 151 ? 1.1441 0.9247 0.8631 0.0957  -0.0923 0.0167  151 PHE D CA  
21570 C C   . PHE D 151 ? 1.1866 0.9659 0.8612 0.0765  -0.1405 0.0282  151 PHE D C   
21571 O O   . PHE D 151 ? 1.1526 0.9772 0.8809 0.0722  -0.1626 0.0549  151 PHE D O   
21572 C CB  . PHE D 151 ? 1.1429 0.9159 0.8538 0.1169  -0.0630 0.0368  151 PHE D CB  
21573 C CG  . PHE D 151 ? 1.2355 0.9606 0.8395 0.1233  -0.0576 0.0375  151 PHE D CG  
21574 C CD1 . PHE D 151 ? 1.3405 1.0598 0.8803 0.1189  -0.0877 0.0579  151 PHE D CD1 
21575 C CD2 . PHE D 151 ? 1.2588 0.9455 0.8236 0.1359  -0.0219 0.0193  151 PHE D CD2 
21576 C CE1 . PHE D 151 ? 1.4588 1.1292 0.8819 0.1277  -0.0813 0.0553  151 PHE D CE1 
21577 C CE2 . PHE D 151 ? 1.3684 1.0075 0.8264 0.1477  -0.0093 0.0185  151 PHE D CE2 
21578 C CZ  . PHE D 151 ? 1.4759 1.1040 0.8552 0.1440  -0.0386 0.0341  151 PHE D CZ  
21588 N N   . PRO D 152 ? 1.2574 0.9844 0.8379 0.0647  -0.1599 0.0091  152 PRO D N   
21589 C CA  . PRO D 152 ? 1.2728 0.9424 0.7920 0.0727  -0.1325 -0.0222 152 PRO D CA  
21590 C C   . PRO D 152 ? 1.2286 0.8924 0.7792 0.0569  -0.1408 -0.0450 152 PRO D C   
21591 O O   . PRO D 152 ? 1.1672 0.8733 0.7826 0.0389  -0.1675 -0.0349 152 PRO D O   
21592 C CB  . PRO D 152 ? 1.3917 1.0028 0.7855 0.0691  -0.1546 -0.0311 152 PRO D CB  
21593 C CG  . PRO D 152 ? 1.4111 1.0468 0.8133 0.0404  -0.2165 -0.0169 152 PRO D CG  
21594 C CD  . PRO D 152 ? 1.3315 1.0476 0.8535 0.0436  -0.2138 0.0180  152 PRO D CD  
21602 N N   . GLU D 153 ? 1.2604 0.8754 0.7715 0.0659  -0.1150 -0.0700 153 GLU D N   
21603 C CA  . GLU D 153 ? 1.2695 0.8626 0.7895 0.0489  -0.1300 -0.0895 153 GLU D CA  
21604 C C   . GLU D 153 ? 1.2829 0.8463 0.7535 0.0194  -0.1858 -0.0956 153 GLU D C   
21605 O O   . GLU D 153 ? 1.3118 0.8483 0.7048 0.0177  -0.2066 -0.0954 153 GLU D O   
21606 C CB  . GLU D 153 ? 1.4105 0.9459 0.8874 0.0670  -0.0932 -0.1131 153 GLU D CB  
21607 C CG  . GLU D 153 ? 1.4400 1.0107 0.9849 0.0892  -0.0471 -0.1045 153 GLU D CG  
21608 C CD  . GLU D 153 ? 1.4549 1.0498 1.0696 0.0806  -0.0479 -0.1068 153 GLU D CD  
21609 O OE1 . GLU D 153 ? 1.5062 1.0575 1.1019 0.0847  -0.0366 -0.1210 153 GLU D OE1 
21610 O OE2 . GLU D 153 ? 1.4074 1.0633 1.0930 0.0721  -0.0579 -0.0929 153 GLU D OE2 
21617 N N   . PRO D 154 ? 1.3063 0.8751 0.8213 -0.0059 -0.2141 -0.0980 154 PRO D N   
21618 C CA  . PRO D 154 ? 1.2849 0.8853 0.8819 -0.0057 -0.1944 -0.0942 154 PRO D CA  
21619 C C   . PRO D 154 ? 1.3030 0.9911 1.0010 -0.0135 -0.2023 -0.0637 154 PRO D C   
21620 O O   . PRO D 154 ? 1.3618 1.0873 1.0797 -0.0225 -0.2280 -0.0429 154 PRO D O   
21621 C CB  . PRO D 154 ? 1.3111 0.8533 0.8837 -0.0297 -0.2233 -0.1119 154 PRO D CB  
21622 C CG  . PRO D 154 ? 1.3776 0.9029 0.9093 -0.0578 -0.2803 -0.1103 154 PRO D CG  
21623 C CD  . PRO D 154 ? 1.3881 0.9185 0.8610 -0.0392 -0.2724 -0.1061 154 PRO D CD  
21631 N N   . VAL D 155 ? 1.2580 0.9787 1.0170 -0.0072 -0.1781 -0.0593 155 VAL D N   
21632 C CA  . VAL D 155 ? 1.1882 0.9840 1.0337 -0.0132 -0.1813 -0.0333 155 VAL D CA  
21633 C C   . VAL D 155 ? 1.1603 0.9533 1.0366 -0.0272 -0.1848 -0.0297 155 VAL D C   
21634 O O   . VAL D 155 ? 1.2484 0.9966 1.0967 -0.0203 -0.1680 -0.0471 155 VAL D O   
21635 C CB  . VAL D 155 ? 1.1484 0.9931 1.0329 0.0136  -0.1440 -0.0294 155 VAL D CB  
21636 C CG1 . VAL D 155 ? 1.1590 0.9869 1.0367 0.0288  -0.1123 -0.0461 155 VAL D CG1 
21637 C CG2 . VAL D 155 ? 1.0851 1.0030 1.0451 0.0125  -0.1446 -0.0043 155 VAL D CG2 
21647 N N   . THR D 156 ? 1.0660 0.9093 1.0067 -0.0454 -0.2046 -0.0015 156 THR D N   
21648 C CA  . THR D 156 ? 1.0594 0.9101 1.0422 -0.0600 -0.2077 0.0131  156 THR D CA  
21649 C C   . THR D 156 ? 1.0110 0.9426 1.0578 -0.0440 -0.1779 0.0378  156 THR D C   
21650 O O   . THR D 156 ? 1.0378 1.0276 1.1224 -0.0363 -0.1733 0.0554  156 THR D O   
21651 C CB  . THR D 156 ? 1.1018 0.9436 1.1125 -0.0976 -0.2560 0.0314  156 THR D CB  
21652 O OG1 . THR D 156 ? 1.0939 1.0127 1.1711 -0.1036 -0.2683 0.0662  156 THR D OG1 
21653 C CG2 . THR D 156 ? 1.1931 0.9496 1.1219 -0.1130 -0.2909 0.0008  156 THR D CG2 
21661 N N   . LEU D 157 ? 0.9608 0.8940 1.0155 -0.0366 -0.1566 0.0396  157 LEU D N   
21662 C CA  . LEU D 157 ? 0.8858 0.8880 0.9791 -0.0188 -0.1273 0.0585  157 LEU D CA  
21663 C C   . LEU D 157 ? 0.8971 0.9154 1.0292 -0.0317 -0.1282 0.0883  157 LEU D C   
21664 O O   . LEU D 157 ? 0.9331 0.8977 1.0487 -0.0411 -0.1359 0.0815  157 LEU D O   
21665 C CB  . LEU D 157 ? 0.8734 0.8697 0.9300 0.0088  -0.0980 0.0320  157 LEU D CB  
21666 C CG  . LEU D 157 ? 0.8574 0.9144 0.9319 0.0285  -0.0714 0.0418  157 LEU D CG  
21667 C CD1 . LEU D 157 ? 0.8185 0.8727 0.8649 0.0512  -0.0542 0.0118  157 LEU D CD1 
21668 C CD2 . LEU D 157 ? 0.8697 0.9300 0.9474 0.0271  -0.0655 0.0561  157 LEU D CD2 
21680 N N   . THR D 158 ? 0.8760 0.9678 1.0619 -0.0292 -0.1164 0.1244  158 THR D N   
21681 C CA  . THR D 158 ? 0.8812 1.0026 1.1101 -0.0380 -0.1108 0.1630  158 THR D CA  
21682 C C   . THR D 158 ? 0.8689 1.0693 1.1103 -0.0108 -0.0735 0.1837  158 THR D C   
21683 O O   . THR D 158 ? 0.8540 1.0845 1.0833 0.0106  -0.0561 0.1696  158 THR D O   
21684 C CB  . THR D 158 ? 0.8778 1.0069 1.1739 -0.0724 -0.1418 0.2002  158 THR D CB  
21685 O OG1 . THR D 158 ? 0.8563 1.0442 1.1953 -0.0713 -0.1431 0.2196  158 THR D OG1 
21686 C CG2 . THR D 158 ? 0.9245 0.9622 1.1919 -0.1001 -0.1825 0.1730  158 THR D CG2 
21694 N N   . TRP D 159 ? 0.8822 1.1118 1.1437 -0.0102 -0.0602 0.2174  159 TRP D N   
21695 C CA  . TRP D 159 ? 0.8942 1.1975 1.1546 0.0163  -0.0237 0.2406  159 TRP D CA  
21696 C C   . TRP D 159 ? 0.9120 1.2760 1.2499 0.0040  -0.0169 0.3044  159 TRP D C   
21697 O O   . TRP D 159 ? 0.9039 1.2525 1.2818 -0.0204 -0.0332 0.3365  159 TRP D O   
21698 C CB  . TRP D 159 ? 0.9037 1.1991 1.1139 0.0316  -0.0118 0.2319  159 TRP D CB  
21699 C CG  . TRP D 159 ? 0.8947 1.1477 1.0415 0.0463  -0.0142 0.1765  159 TRP D CG  
21700 C CD1 . TRP D 159 ? 0.8880 1.0740 1.0147 0.0372  -0.0329 0.1480  159 TRP D CD1 
21701 C CD2 . TRP D 159 ? 0.8995 1.1732 1.0007 0.0729  0.0042  0.1450  159 TRP D CD2 
21702 N NE1 . TRP D 159 ? 0.8826 1.0544 0.9638 0.0547  -0.0274 0.1071  159 TRP D NE1 
21703 C CE2 . TRP D 159 ? 0.8877 1.1086 0.9526 0.0745  -0.0082 0.1023  159 TRP D CE2 
21704 C CE3 . TRP D 159 ? 0.9186 1.2463 1.0070 0.0970  0.0318  0.1483  159 TRP D CE3 
21705 C CZ2 . TRP D 159 ? 0.8923 1.1124 0.9166 0.0938  -0.0001 0.0644  159 TRP D CZ2 
21706 C CZ3 . TRP D 159 ? 0.9385 1.2565 0.9748 0.1189  0.0408  0.1036  159 TRP D CZ3 
21707 C CH2 . TRP D 159 ? 0.9117 1.1760 0.9202 0.1144  0.0218  0.0628  159 TRP D CH2 
21718 N N   . ASN D 160 ? 0.9322 1.3644 1.2980 0.0221  0.0095  0.3256  160 ASN D N   
21719 C CA  . ASN D 160 ? 0.9344 1.4364 1.3893 0.0127  0.0208  0.3932  160 ASN D CA  
21720 C C   . ASN D 160 ? 0.9765 1.4461 1.5062 -0.0343 -0.0267 0.4156  160 ASN D C   
21721 O O   . ASN D 160 ? 1.0181 1.5041 1.6129 -0.0576 -0.0345 0.4667  160 ASN D O   
21722 C CB  . ASN D 160 ? 0.8990 1.4490 1.3511 0.0266  0.0528  0.4372  160 ASN D CB  
21723 C CG  . ASN D 160 ? 0.8784 1.4827 1.2702 0.0736  0.1031  0.4296  160 ASN D CG  
21724 O OD1 . ASN D 160 ? 0.8444 1.4740 1.2366 0.0955  0.1234  0.4148  160 ASN D OD1 
21725 N ND2 . ASN D 160 ? 0.9250 1.5442 1.2616 0.0904  0.1225  0.4394  160 ASN D ND2 
21732 N N   . SER D 161 ? 0.9644 1.3838 1.4815 -0.0490 -0.0609 0.3767  161 SER D N   
21733 C CA  . SER D 161 ? 0.9872 1.3684 1.5589 -0.0942 -0.1136 0.3878  161 SER D CA  
21734 C C   . SER D 161 ? 0.9911 1.2977 1.5501 -0.1212 -0.1401 0.3815  161 SER D C   
21735 O O   . SER D 161 ? 1.0208 1.3115 1.6476 -0.1598 -0.1749 0.4126  161 SER D O   
21736 C CB  . SER D 161 ? 0.9872 1.4495 1.6774 -0.1115 -0.1167 0.4569  161 SER D CB  
21737 O OG  . SER D 161 ? 0.9382 1.4744 1.6463 -0.0783 -0.0813 0.4684  161 SER D OG  
21743 N N   . GLY D 162 ? 0.9617 1.2204 1.4402 -0.1012 -0.1248 0.3424  162 GLY D N   
21744 C CA  . GLY D 162 ? 0.9616 1.1468 1.4277 -0.1188 -0.1429 0.3353  162 GLY D CA  
21745 C C   . GLY D 162 ? 0.9398 1.1631 1.4565 -0.1196 -0.1237 0.3915  162 GLY D C   
21746 O O   . GLY D 162 ? 0.9441 1.1069 1.4581 -0.1307 -0.1351 0.3908  162 GLY D O   
21750 N N   . SER D 163 ? 0.9331 1.2541 1.4957 -0.1054 -0.0916 0.4432  163 SER D N   
21751 C CA  . SER D 163 ? 0.9761 1.3415 1.5811 -0.1026 -0.0684 0.5040  163 SER D CA  
21752 C C   . SER D 163 ? 0.9489 1.2910 1.4785 -0.0763 -0.0497 0.4837  163 SER D C   
21753 O O   . SER D 163 ? 0.9270 1.2681 1.4847 -0.0814 -0.0457 0.5249  163 SER D O   
21754 C CB  . SER D 163 ? 1.0543 1.5329 1.7029 -0.0822 -0.0274 0.5590  163 SER D CB  
21755 O OG  . SER D 163 ? 1.1689 1.6968 1.8305 -0.0687 0.0043  0.6146  163 SER D OG  
21761 N N   . LEU D 164 ? 0.9451 1.2709 1.3876 -0.0496 -0.0403 0.4257  164 LEU D N   
21762 C CA  . LEU D 164 ? 0.9597 1.2670 1.3353 -0.0265 -0.0289 0.4043  164 LEU D CA  
21763 C C   . LEU D 164 ? 1.0332 1.2427 1.3763 -0.0364 -0.0561 0.3501  164 LEU D C   
21764 O O   . LEU D 164 ? 1.1079 1.2903 1.4053 -0.0292 -0.0612 0.2982  164 LEU D O   
21765 C CB  . LEU D 164 ? 0.8902 1.2491 1.1961 0.0095  -0.0002 0.3797  164 LEU D CB  
21766 C CG  . LEU D 164 ? 0.8686 1.3205 1.1886 0.0281  0.0351  0.4227  164 LEU D CG  
21767 C CD1 . LEU D 164 ? 0.8667 1.3438 1.1043 0.0636  0.0586  0.3798  164 LEU D CD1 
21768 C CD2 . LEU D 164 ? 0.8940 1.3930 1.2394 0.0304  0.0518  0.4898  164 LEU D CD2 
21780 N N   . SER D 165 ? 1.0516 1.2072 1.4202 -0.0504 -0.0697 0.3650  165 SER D N   
21781 C CA  . SER D 165 ? 1.0793 1.1399 1.4155 -0.0531 -0.0866 0.3180  165 SER D CA  
21782 C C   . SER D 165 ? 1.0435 1.0982 1.3529 -0.0293 -0.0725 0.3186  165 SER D C   
21783 O O   . SER D 165 ? 0.9935 1.0195 1.2530 -0.0126 -0.0695 0.2742  165 SER D O   
21784 C CB  . SER D 165 ? 1.2444 1.2291 1.6299 -0.0861 -0.1150 0.3264  165 SER D CB  
21785 O OG  . SER D 165 ? 1.3646 1.3613 1.8122 -0.0941 -0.1113 0.3846  165 SER D OG  
21791 N N   . ALA D 166 ? 1.0970 1.1830 1.4459 -0.0278 -0.0646 0.3740  166 ALA D N   
21792 C CA  . ALA D 166 ? 1.1312 1.2282 1.4601 -0.0046 -0.0544 0.3845  166 ALA D CA  
21793 C C   . ALA D 166 ? 1.1596 1.3253 1.4266 0.0197  -0.0413 0.3665  166 ALA D C   
21794 O O   . ALA D 166 ? 1.1332 1.3593 1.3851 0.0229  -0.0303 0.3733  166 ALA D O   
21795 C CB  . ALA D 166 ? 1.1329 1.2591 1.5183 -0.0080 -0.0494 0.4569  166 ALA D CB  
21801 N N   . GLY D 167 ? 1.1941 1.3479 1.4288 0.0372  -0.0428 0.3436  167 GLY D N   
21802 C CA  . GLY D 167 ? 1.1785 1.3828 1.3542 0.0559  -0.0385 0.3186  167 GLY D CA  
21803 C C   . GLY D 167 ? 1.1224 1.3064 1.2628 0.0563  -0.0387 0.2599  167 GLY D C   
21804 O O   . GLY D 167 ? 1.1084 1.3326 1.2032 0.0693  -0.0343 0.2380  167 GLY D O   
21808 N N   . VAL D 168 ? 1.3338 1.0309 1.1733 0.1679  -0.0423 0.1779  168 VAL D N   
21809 C CA  . VAL D 168 ? 1.2215 0.9409 1.0822 0.1482  -0.0465 0.1321  168 VAL D CA  
21810 C C   . VAL D 168 ? 1.1988 0.9126 1.0704 0.1571  -0.0684 0.0967  168 VAL D C   
21811 O O   . VAL D 168 ? 1.2910 0.9626 1.1779 0.1650  -0.0775 0.1015  168 VAL D O   
21812 C CB  . VAL D 168 ? 1.1616 0.8586 1.0687 0.1163  -0.0355 0.1353  168 VAL D CB  
21813 C CG1 . VAL D 168 ? 1.0445 0.7621 0.9673 0.1026  -0.0423 0.0933  168 VAL D CG1 
21814 C CG2 . VAL D 168 ? 1.2043 0.9187 1.1123 0.1079  -0.0076 0.1729  168 VAL D CG2 
21824 N N   . HIS D 169 ? 1.0996 0.8547 0.9674 0.1567  -0.0740 0.0618  169 HIS D N   
21825 C CA  . HIS D 169 ? 1.0689 0.8309 0.9537 0.1630  -0.0866 0.0308  169 HIS D CA  
21826 C C   . HIS D 169 ? 1.0838 0.8591 0.9856 0.1417  -0.0797 0.0040  169 HIS D C   
21827 O O   . HIS D 169 ? 1.1256 0.9367 1.0260 0.1375  -0.0776 -0.0123 169 HIS D O   
21828 C CB  . HIS D 169 ? 1.0494 0.8553 0.9236 0.1863  -0.1009 0.0211  169 HIS D CB  
21829 C CG  . HIS D 169 ? 1.1373 0.9302 0.9954 0.2155  -0.1117 0.0492  169 HIS D CG  
21830 N ND1 . HIS D 169 ? 1.1855 0.9358 1.0613 0.2292  -0.1158 0.0569  169 HIS D ND1 
21831 C CD2 . HIS D 169 ? 1.2018 1.0165 1.0239 0.2381  -0.1199 0.0722  169 HIS D CD2 
21832 C CE1 . HIS D 169 ? 1.2513 0.9938 1.1094 0.2584  -0.1251 0.0873  169 HIS D CE1 
21833 N NE2 . HIS D 169 ? 1.2585 1.0424 1.0805 0.2649  -0.1281 0.0995  169 HIS D NE2 
21841 N N   . THR D 170 ? 1.0580 0.8018 0.9750 0.1300  -0.0783 -0.0010 170 THR D N   
21842 C CA  . THR D 170 ? 1.0217 0.7752 0.9484 0.1162  -0.0732 -0.0203 170 THR D CA  
21843 C C   . THR D 170 ? 1.0253 0.7873 0.9559 0.1277  -0.0745 -0.0402 170 THR D C   
21844 O O   . THR D 170 ? 1.0839 0.8225 1.0122 0.1418  -0.0807 -0.0443 170 THR D O   
21845 C CB  . THR D 170 ? 1.0013 0.7262 0.9382 0.1007  -0.0749 -0.0162 170 THR D CB  
21846 O OG1 . THR D 170 ? 0.9701 0.6964 0.9156 0.0895  -0.0679 0.0063  170 THR D OG1 
21847 C CG2 . THR D 170 ? 0.9710 0.7087 0.9102 0.0930  -0.0719 -0.0309 170 THR D CG2 
21855 N N   . PHE D 171 ? 0.9683 0.7621 0.9088 0.1225  -0.0660 -0.0518 171 PHE D N   
21856 C CA  . PHE D 171 ? 0.9232 0.7376 0.8767 0.1325  -0.0600 -0.0647 171 PHE D CA  
21857 C C   . PHE D 171 ? 0.8981 0.7015 0.8427 0.1288  -0.0485 -0.0685 171 PHE D C   
21858 O O   . PHE D 171 ? 0.8547 0.6480 0.7930 0.1153  -0.0461 -0.0629 171 PHE D O   
21859 C CB  . PHE D 171 ? 0.9003 0.7594 0.8821 0.1268  -0.0566 -0.0733 171 PHE D CB  
21860 C CG  . PHE D 171 ? 0.9314 0.8106 0.9122 0.1358  -0.0732 -0.0734 171 PHE D CG  
21861 C CD1 . PHE D 171 ? 0.9332 0.8066 0.8923 0.1297  -0.0779 -0.0675 171 PHE D CD1 
21862 C CD2 . PHE D 171 ? 0.9373 0.8464 0.9361 0.1550  -0.0835 -0.0782 171 PHE D CD2 
21863 C CE1 . PHE D 171 ? 0.9574 0.8522 0.9009 0.1435  -0.0930 -0.0655 171 PHE D CE1 
21864 C CE2 . PHE D 171 ? 0.9516 0.8834 0.9420 0.1686  -0.1033 -0.0760 171 PHE D CE2 
21865 C CZ  . PHE D 171 ? 0.9738 0.8973 0.9306 0.1632  -0.1083 -0.0693 171 PHE D CZ  
21875 N N   . PRO D 172 ? 0.9439 0.7526 0.8845 0.1453  -0.0408 -0.0768 172 PRO D N   
21876 C CA  . PRO D 172 ? 0.9848 0.7881 0.9030 0.1479  -0.0280 -0.0780 172 PRO D CA  
21877 C C   . PRO D 172 ? 0.9859 0.8132 0.9230 0.1326  -0.0088 -0.0661 172 PRO D C   
21878 O O   . PRO D 172 ? 0.9701 0.8247 0.9470 0.1220  -0.0026 -0.0655 172 PRO D O   
21879 C CB  . PRO D 172 ? 1.0231 0.8368 0.9339 0.1742  -0.0176 -0.0899 172 PRO D CB  
21880 C CG  . PRO D 172 ? 0.9770 0.8190 0.9274 0.1808  -0.0202 -0.0914 172 PRO D CG  
21881 C CD  . PRO D 172 ? 0.9432 0.7659 0.8961 0.1679  -0.0420 -0.0844 172 PRO D CD  
21889 N N   . ALA D 173 ? 1.0230 0.8377 0.9329 0.1327  -0.0020 -0.0574 173 ALA D N   
21890 C CA  . ALA D 173 ? 1.0313 0.8555 0.9584 0.1201  0.0169  -0.0397 173 ALA D CA  
21891 C C   . ALA D 173 ? 1.0648 0.9198 1.0152 0.1236  0.0478  -0.0306 173 ALA D C   
21892 O O   . ALA D 173 ? 1.1244 0.9959 1.0617 0.1427  0.0578  -0.0368 173 ALA D O   
21893 C CB  . ALA D 173 ? 1.0309 0.8344 0.9190 0.1251  0.0125  -0.0274 173 ALA D CB  
21899 N N   . VAL D 174 ? 1.0541 0.9165 1.0459 0.1051  0.0654  -0.0158 174 VAL D N   
21900 C CA  . VAL D 174 ? 1.0594 0.9520 1.0921 0.1005  0.0996  -0.0004 174 VAL D CA  
21901 C C   . VAL D 174 ? 1.0480 0.9199 1.0767 0.0942  0.1229  0.0323  174 VAL D C   
21902 O O   . VAL D 174 ? 1.0270 0.8660 1.0448 0.0882  0.1090  0.0366  174 VAL D O   
21903 C CB  . VAL D 174 ? 1.0303 0.9540 1.1424 0.0788  0.0971  -0.0157 174 VAL D CB  
21904 C CG1 . VAL D 174 ? 1.0813 1.0496 1.2504 0.0742  0.1325  -0.0017 174 VAL D CG1 
21905 C CG2 . VAL D 174 ? 0.9653 0.9013 1.0728 0.0878  0.0656  -0.0436 174 VAL D CG2 
21915 N N   . LEU D 175 ? 1.0785 0.9714 1.1182 0.0986  0.1616  0.0593  175 LEU D N   
21916 C CA  . LEU D 175 ? 1.1186 0.9903 1.1610 0.0934  0.1901  0.1004  175 LEU D CA  
21917 C C   . LEU D 175 ? 1.1157 0.9804 1.2525 0.0579  0.1998  0.1031  175 LEU D C   
21918 O O   . LEU D 175 ? 1.1059 1.0057 1.3145 0.0390  0.2037  0.0853  175 LEU D O   
21919 C CB  . LEU D 175 ? 1.1855 1.0832 1.1998 0.1135  0.2342  0.1350  175 LEU D CB  
21920 C CG  . LEU D 175 ? 1.2621 1.1555 1.1664 0.1533  0.2270  0.1365  175 LEU D CG  
21921 C CD1 . LEU D 175 ? 1.3787 1.3054 1.2531 0.1764  0.2776  0.1701  175 LEU D CD1 
21922 C CD2 . LEU D 175 ? 1.2639 1.1151 1.1145 0.1618  0.2037  0.1510  175 LEU D CD2 
21934 N N   . GLN D 176 ? 1.1736 0.9928 1.3137 0.0507  0.2009  0.1226  176 GLN D N   
21935 C CA  . GLN D 176 ? 1.2614 1.0579 1.4871 0.0185  0.2033  0.1158  176 GLN D CA  
21936 C C   . GLN D 176 ? 1.4076 1.1543 1.6324 0.0208  0.2280  0.1624  176 GLN D C   
21937 O O   . GLN D 176 ? 1.4230 1.1337 1.6033 0.0370  0.2091  0.1658  176 GLN D O   
21938 C CB  . GLN D 176 ? 1.2510 1.0353 1.4796 0.0118  0.1606  0.0682  176 GLN D CB  
21939 C CG  . GLN D 176 ? 1.3185 1.0785 1.6258 -0.0172 0.1562  0.0466  176 GLN D CG  
21940 C CD  . GLN D 176 ? 1.3454 1.0955 1.6339 -0.0144 0.1180  0.0019  176 GLN D CD  
21941 O OE1 . GLN D 176 ? 1.3556 1.0794 1.5932 0.0041  0.1073  0.0065  176 GLN D OE1 
21942 N NE2 . GLN D 176 ? 1.3619 1.1396 1.6911 -0.0305 0.0975  -0.0403 176 GLN D NE2 
21951 N N   . SER D 177 ? 1.5320 1.2789 1.8118 0.0056  0.2716  0.2018  177 SER D N   
21952 C CA  . SER D 177 ? 1.6254 1.3220 1.9041 0.0110  0.3022  0.2589  177 SER D CA  
21953 C C   . SER D 177 ? 1.5603 1.2526 1.7229 0.0556  0.2997  0.2919  177 SER D C   
21954 O O   . SER D 177 ? 1.5998 1.2468 1.7344 0.0722  0.2948  0.3192  177 SER D O   
21955 C CB  . SER D 177 ? 1.7068 1.3411 2.0390 -0.0062 0.2855  0.2433  177 SER D CB  
21956 O OG  . SER D 177 ? 1.7279 1.3648 2.1662 -0.0474 0.2839  0.2075  177 SER D OG  
21962 N N   . SER D 178 ? 1.4288 1.1702 1.5255 0.0775  0.2994  0.2852  178 SER D N   
21963 C CA  . SER D 178 ? 1.3449 1.0917 1.3269 0.1206  0.2908  0.3045  178 SER D CA  
21964 C C   . SER D 178 ? 1.2391 0.9699 1.1754 0.1340  0.2357  0.2680  178 SER D C   
21965 O O   . SER D 178 ? 1.2197 0.9434 1.0798 0.1656  0.2206  0.2865  178 SER D O   
21966 C CB  . SER D 178 ? 1.4194 1.1399 1.3689 0.1406  0.3282  0.3771  178 SER D CB  
21967 O OG  . SER D 178 ? 1.4641 1.2047 1.4565 0.1284  0.3867  0.4189  178 SER D OG  
21973 N N   . LEU D 179 ? 1.1834 0.9142 1.1665 0.1117  0.2054  0.2177  179 LEU D N   
21974 C CA  . LEU D 179 ? 1.1426 0.8675 1.0933 0.1212  0.1594  0.1845  179 LEU D CA  
21975 C C   . LEU D 179 ? 1.1372 0.8885 1.1025 0.1078  0.1365  0.1337  179 LEU D C   
21976 O O   . LEU D 179 ? 1.1336 0.9012 1.1537 0.0868  0.1492  0.1188  179 LEU D O   
21977 C CB  . LEU D 179 ? 1.1106 0.7960 1.1032 0.1135  0.1489  0.1861  179 LEU D CB  
21978 C CG  . LEU D 179 ? 1.1406 0.7933 1.1134 0.1355  0.1614  0.2373  179 LEU D CG  
21979 C CD1 . LEU D 179 ? 1.1119 0.7245 1.1373 0.1298  0.1520  0.2304  179 LEU D CD1 
21980 C CD2 . LEU D 179 ? 1.1686 0.8415 1.0535 0.1712  0.1375  0.2495  179 LEU D CD2 
21992 N N   . TYR D 180 ? 1.1412 0.8979 1.0625 0.1204  0.1013  0.1094  180 TYR D N   
21993 C CA  . TYR D 180 ? 1.0932 0.8683 1.0203 0.1126  0.0801  0.0694  180 TYR D CA  
21994 C C   . TYR D 180 ? 1.0816 0.8480 1.0575 0.0927  0.0654  0.0465  180 TYR D C   
21995 O O   . TYR D 180 ? 1.1214 0.8679 1.1069 0.0926  0.0580  0.0517  180 TYR D O   
21996 C CB  . TYR D 180 ? 1.0518 0.8304 0.9198 0.1311  0.0501  0.0540  180 TYR D CB  
21997 C CG  . TYR D 180 ? 1.1044 0.8955 0.9122 0.1553  0.0597  0.0607  180 TYR D CG  
21998 C CD1 . TYR D 180 ? 1.1093 0.9209 0.9189 0.1589  0.0780  0.0494  180 TYR D CD1 
21999 C CD2 . TYR D 180 ? 1.1506 0.9376 0.8969 0.1791  0.0494  0.0763  180 TYR D CD2 
22000 C CE1 . TYR D 180 ? 1.1517 0.9767 0.9006 0.1864  0.0910  0.0521  180 TYR D CE1 
22001 C CE2 . TYR D 180 ? 1.2134 1.0135 0.8909 0.2065  0.0578  0.0779  180 TYR D CE2 
22002 C CZ  . TYR D 180 ? 1.2222 1.0400 0.8998 0.2106  0.0812  0.0650  180 TYR D CZ  
22003 O OH  . TYR D 180 ? 1.3278 1.1605 0.9318 0.2431  0.0938  0.0635  180 TYR D OH  
22013 N N   . THR D 181 ? 0.9993 0.7843 1.0027 0.0805  0.0613  0.0210  181 THR D N   
22014 C CA  . THR D 181 ? 0.9444 0.7283 0.9772 0.0674  0.0452  -0.0043 181 THR D CA  
22015 C C   . THR D 181 ? 0.9174 0.7201 0.9324 0.0720  0.0255  -0.0252 181 THR D C   
22016 O O   . THR D 181 ? 0.9147 0.7364 0.9262 0.0780  0.0295  -0.0283 181 THR D O   
22017 C CB  . THR D 181 ? 0.9213 0.7080 1.0147 0.0475  0.0579  -0.0141 181 THR D CB  
22018 O OG1 . THR D 181 ? 1.0010 0.7582 1.1169 0.0429  0.0787  0.0097  181 THR D OG1 
22019 C CG2 . THR D 181 ? 0.8693 0.6574 0.9771 0.0401  0.0380  -0.0462 181 THR D CG2 
22027 N N   . LEU D 182 ? 0.9007 0.6978 0.9069 0.0716  0.0076  -0.0361 182 LEU D N   
22028 C CA  . LEU D 182 ? 0.9174 0.7226 0.9054 0.0770  -0.0095 -0.0467 182 LEU D CA  
22029 C C   . LEU D 182 ? 0.9602 0.7713 0.9565 0.0722  -0.0175 -0.0586 182 LEU D C   
22030 O O   . LEU D 182 ? 1.0661 0.8700 1.0724 0.0682  -0.0127 -0.0605 182 LEU D O   
22031 C CB  . LEU D 182 ? 0.9460 0.7361 0.9032 0.0851  -0.0218 -0.0389 182 LEU D CB  
22032 C CG  . LEU D 182 ? 0.9683 0.7531 0.9164 0.0865  -0.0383 -0.0436 182 LEU D CG  
22033 C CD1 . LEU D 182 ? 0.9871 0.7550 0.9124 0.0943  -0.0511 -0.0459 182 LEU D CD1 
22034 C CD2 . LEU D 182 ? 0.9772 0.7623 0.9361 0.0791  -0.0410 -0.0373 182 LEU D CD2 
22046 N N   . SER D 183 ? 0.9001 0.7243 0.8880 0.0774  -0.0288 -0.0659 183 SER D N   
22047 C CA  . SER D 183 ? 0.9045 0.7392 0.8847 0.0791  -0.0361 -0.0740 183 SER D CA  
22048 C C   . SER D 183 ? 0.8993 0.7302 0.8550 0.0890  -0.0459 -0.0611 183 SER D C   
22049 O O   . SER D 183 ? 0.8790 0.6993 0.8311 0.0946  -0.0507 -0.0550 183 SER D O   
22050 C CB  . SER D 183 ? 0.9173 0.7781 0.9169 0.0770  -0.0423 -0.0970 183 SER D CB  
22051 O OG  . SER D 183 ? 0.9372 0.8181 0.9489 0.0828  -0.0494 -0.0985 183 SER D OG  
22057 N N   . SER D 184 ? 0.9125 0.7493 0.8507 0.0930  -0.0462 -0.0561 184 SER D N   
22058 C CA  . SER D 184 ? 0.9685 0.7976 0.8867 0.1015  -0.0504 -0.0349 184 SER D CA  
22059 C C   . SER D 184 ? 0.9867 0.8379 0.8761 0.1131  -0.0497 -0.0333 184 SER D C   
22060 O O   . SER D 184 ? 0.9916 0.8557 0.8749 0.1122  -0.0408 -0.0454 184 SER D O   
22061 C CB  . SER D 184 ? 1.0130 0.8199 0.9410 0.0918  -0.0437 -0.0149 184 SER D CB  
22062 O OG  . SER D 184 ? 1.0683 0.8614 0.9882 0.0956  -0.0445 0.0096  184 SER D OG  
22068 N N   . SER D 185 ? 1.0076 0.8621 0.8748 0.1285  -0.0593 -0.0186 185 SER D N   
22069 C CA  . SER D 185 ? 1.0448 0.9226 0.8695 0.1465  -0.0603 -0.0109 185 SER D CA  
22070 C C   . SER D 185 ? 1.0839 0.9412 0.8909 0.1527  -0.0477 0.0344  185 SER D C   
22071 O O   . SER D 185 ? 1.1017 0.9262 0.9287 0.1494  -0.0511 0.0535  185 SER D O   
22072 C CB  . SER D 185 ? 1.0627 0.9694 0.8749 0.1646  -0.0853 -0.0275 185 SER D CB  
22073 O OG  . SER D 185 ? 1.0963 0.9874 0.9090 0.1784  -0.0942 -0.0021 185 SER D OG  
22079 N N   . VAL D 186 ? 1.0972 0.9721 0.8684 0.1623  -0.0309 0.0511  186 VAL D N   
22080 C CA  . VAL D 186 ? 1.1357 0.9969 0.8905 0.1688  -0.0121 0.1024  186 VAL D CA  
22081 C C   . VAL D 186 ? 1.1906 1.0834 0.8744 0.2009  -0.0124 0.1153  186 VAL D C   
22082 O O   . VAL D 186 ? 1.2244 1.1534 0.8726 0.2125  -0.0150 0.0829  186 VAL D O   
22083 C CB  . VAL D 186 ? 1.1180 0.9777 0.9030 0.1496  0.0184  0.1209  186 VAL D CB  
22084 C CG1 . VAL D 186 ? 1.1237 1.0225 0.8836 0.1582  0.0335  0.0966  186 VAL D CG1 
22085 C CG2 . VAL D 186 ? 1.1604 1.0050 0.9454 0.1502  0.0417  0.1798  186 VAL D CG2 
22095 N N   . THR D 187 ? 1.2260 1.1023 0.8866 0.2180  -0.0115 0.1616  187 THR D N   
22096 C CA  . THR D 187 ? 1.3269 1.2331 0.9096 0.2553  -0.0147 0.1829  187 THR D CA  
22097 C C   . THR D 187 ? 1.3982 1.2881 0.9601 0.2614  0.0230  0.2529  187 THR D C   
22098 O O   . THR D 187 ? 1.4057 1.2469 1.0091 0.2497  0.0305  0.2946  187 THR D O   
22099 C CB  . THR D 187 ? 1.3389 1.2457 0.9098 0.2791  -0.0522 0.1795  187 THR D CB  
22100 O OG1 . THR D 187 ? 1.2917 1.2206 0.8958 0.2693  -0.0818 0.1175  187 THR D OG1 
22101 C CG2 . THR D 187 ? 1.4125 1.3569 0.8956 0.3230  -0.0617 0.2019  187 THR D CG2 
22109 N N   . VAL D 188 ? 1.4355 1.3650 0.9358 0.2802  0.0486  0.2652  188 VAL D N   
22110 C CA  . VAL D 188 ? 1.4630 1.3889 0.9399 0.2883  0.0936  0.3372  188 VAL D CA  
22111 C C   . VAL D 188 ? 1.5208 1.4884 0.8830 0.3385  0.0947  0.3576  188 VAL D C   
22112 O O   . VAL D 188 ? 1.5130 1.5148 0.8212 0.3634  0.0567  0.3074  188 VAL D O   
22113 C CB  . VAL D 188 ? 1.4164 1.3591 0.9348 0.2636  0.1372  0.3404  188 VAL D CB  
22114 C CG1 . VAL D 188 ? 1.3239 1.2283 0.9518 0.2173  0.1314  0.3259  188 VAL D CG1 
22115 C CG2 . VAL D 188 ? 1.4034 1.3975 0.8751 0.2796  0.1366  0.2814  188 VAL D CG2 
22125 N N   . VAL D 189 ? 1.5845 1.5516 0.9116 0.3532  0.1389  0.4334  189 VAL D N   
22126 C CA  . VAL D 189 ? 1.6907 1.7001 0.8944 0.4064  0.1463  0.4627  189 VAL D CA  
22127 C C   . VAL D 189 ? 1.7490 1.8201 0.8902 0.4236  0.1535  0.4041  189 VAL D C   
22128 O O   . VAL D 189 ? 1.7535 1.8331 0.9459 0.3973  0.1834  0.3816  189 VAL D O   
22129 C CB  . VAL D 189 ? 1.7204 1.7139 0.9235 0.4087  0.1990  0.5554  189 VAL D CB  
22130 C CG1 . VAL D 189 ? 1.8261 1.8602 0.9331 0.4524  0.1955  0.5675  189 VAL D CG1 
22131 C CG2 . VAL D 189 ? 1.6877 1.6057 0.9759 0.3822  0.1938  0.6041  189 VAL D CG2 
22141 N N   . ALA D 190 ? 1.7831 1.8972 0.8231 0.4674  0.1219  0.3724  190 ALA D N   
22142 C CA  . ALA D 190 ? 1.7491 1.9142 0.7334 0.4843  0.1214  0.3035  190 ALA D CA  
22143 C C   . ALA D 190 ? 1.8125 2.0009 0.7834 0.4883  0.1887  0.3377  190 ALA D C   
22144 O O   . ALA D 190 ? 1.7988 2.0139 0.7610 0.4902  0.2047  0.2865  190 ALA D O   
22145 C CB  . ALA D 190 ? 1.7798 1.9832 0.6902 0.5199  0.0711  0.2594  190 ALA D CB  
22151 N N   . SER D 191 ? 1.8895 2.0679 0.8673 0.4893  0.2289  0.4222  191 SER D N   
22152 C CA  . SER D 191 ? 1.9501 2.1565 0.9274 0.4919  0.2953  0.4616  191 SER D CA  
22153 C C   . SER D 191 ? 1.9434 2.1350 1.0251 0.4498  0.3407  0.4849  191 SER D C   
22154 O O   . SER D 191 ? 1.9740 2.2007 1.0709 0.4502  0.3938  0.5005  191 SER D O   
22155 C CB  . SER D 191 ? 2.0026 2.2038 0.9568 0.5063  0.3219  0.5449  191 SER D CB  
22156 O OG  . SER D 191 ? 1.9351 2.0770 0.9693 0.4745  0.3220  0.6043  191 SER D OG  
22162 N N   . THR D 192 ? 1.9095 2.0536 1.0673 0.4148  0.3203  0.4870  192 THR D N   
22163 C CA  . THR D 192 ? 1.8440 1.9726 1.1240 0.3674  0.3514  0.5001  192 THR D CA  
22164 C C   . THR D 192 ? 1.7358 1.8753 1.0620 0.3504  0.3262  0.4090  192 THR D C   
22165 O O   . THR D 192 ? 1.6328 1.7569 1.0728 0.3083  0.3325  0.4029  192 THR D O   
22166 C CB  . THR D 192 ? 1.7832 1.8436 1.1612 0.3256  0.3309  0.5369  192 THR D CB  
22167 O OG1 . THR D 192 ? 1.7185 1.7461 1.0929 0.3241  0.2634  0.4794  192 THR D OG1 
22168 C CG2 . THR D 192 ? 1.8727 1.9114 1.2326 0.3355  0.3576  0.6264  192 THR D CG2 
22176 N N   . TRP D 193 ? 1.7459 1.9099 0.9889 0.3826  0.2955  0.3382  193 TRP D N   
22177 C CA  . TRP D 193 ? 1.6509 1.8207 0.9330 0.3710  0.2780  0.2561  193 TRP D CA  
22178 C C   . TRP D 193 ? 1.6865 1.8955 0.8533 0.4190  0.2691  0.1975  193 TRP D C   
22179 O O   . TRP D 193 ? 1.7474 1.9636 0.8226 0.4488  0.2357  0.1895  193 TRP D O   
22180 C CB  . TRP D 193 ? 1.5659 1.6886 0.9190 0.3361  0.2196  0.2101  193 TRP D CB  
22181 C CG  . TRP D 193 ? 1.5132 1.6339 0.9179 0.3211  0.2079  0.1405  193 TRP D CG  
22182 C CD1 . TRP D 193 ? 1.4532 1.5659 0.9558 0.2908  0.2270  0.1425  193 TRP D CD1 
22183 C CD2 . TRP D 193 ? 1.4964 1.6215 0.8613 0.3370  0.1734  0.0603  193 TRP D CD2 
22184 N NE1 . TRP D 193 ? 1.3826 1.4908 0.9033 0.2905  0.2092  0.0742  193 TRP D NE1 
22185 C CE2 . TRP D 193 ? 1.3975 1.5091 0.8388 0.3159  0.1776  0.0224  193 TRP D CE2 
22186 C CE3 . TRP D 193 ? 1.5405 1.6800 0.8178 0.3665  0.1363  0.0161  193 TRP D CE3 
22187 C CZ2 . TRP D 193 ? 1.3432 1.4456 0.7789 0.3217  0.1509  -0.0541 193 TRP D CZ2 
22188 C CZ3 . TRP D 193 ? 1.4899 1.6252 0.7675 0.3683  0.1061  -0.0666 193 TRP D CZ3 
22189 C CH2 . TRP D 193 ? 1.3880 1.5003 0.7458 0.3451  0.1159  -0.0991 193 TRP D CH2 
22200 N N   . PRO D 194 ? 1.6542 1.8889 0.8226 0.4305  0.2941  0.1515  194 PRO D N   
22201 C CA  . PRO D 194 ? 1.5641 1.8001 0.8396 0.4034  0.3288  0.1529  194 PRO D CA  
22202 C C   . PRO D 194 ? 1.6108 1.8898 0.9039 0.4105  0.4031  0.2268  194 PRO D C   
22203 O O   . PRO D 194 ? 1.5773 1.8782 0.9440 0.4022  0.4364  0.2202  194 PRO D O   
22204 C CB  . PRO D 194 ? 1.5567 1.8013 0.8072 0.4258  0.3179  0.0635  194 PRO D CB  
22205 C CG  . PRO D 194 ? 1.6223 1.8670 0.7604 0.4571  0.2712  0.0101  194 PRO D CG  
22206 C CD  . PRO D 194 ? 1.6993 1.9612 0.7621 0.4751  0.2776  0.0786  194 PRO D CD  
22214 N N   . SER D 195 ? 1.6881 1.9815 0.9210 0.4267  0.4302  0.2999  195 SER D N   
22215 C CA  . SER D 195 ? 1.7256 2.0557 1.0010 0.4229  0.4972  0.3730  195 SER D CA  
22216 C C   . SER D 195 ? 1.6183 1.9382 1.0437 0.3714  0.5187  0.4126  195 SER D C   
22217 O O   . SER D 195 ? 1.5784 1.9436 1.0747 0.3650  0.5719  0.4391  195 SER D O   
22218 C CB  . SER D 195 ? 1.8325 2.1569 1.0544 0.4334  0.5027  0.4401  195 SER D CB  
22219 O OG  . SER D 195 ? 1.8003 2.0710 1.0503 0.4071  0.4719  0.4778  195 SER D OG  
22225 N N   . GLN D 196 ? 1.5747 1.8343 1.0661 0.3299  0.4660  0.4072  196 GLN D N   
22226 C CA  . GLN D 196 ? 1.5083 1.7472 1.1478 0.2758  0.4609  0.4217  196 GLN D CA  
22227 C C   . GLN D 196 ? 1.4070 1.6143 1.0868 0.2587  0.4035  0.3416  196 GLN D C   
22228 O O   . GLN D 196 ? 1.3858 1.5642 0.9979 0.2728  0.3572  0.2912  196 GLN D O   
22229 C CB  . GLN D 196 ? 1.5569 1.7461 1.2410 0.2428  0.4506  0.4847  196 GLN D CB  
22230 C CG  . GLN D 196 ? 1.7314 1.9421 1.3882 0.2553  0.5112  0.5773  196 GLN D CG  
22231 C CD  . GLN D 196 ? 1.8480 1.9928 1.5191 0.2350  0.4926  0.6328  196 GLN D CD  
22232 O OE1 . GLN D 196 ? 1.9188 2.0269 1.5056 0.2575  0.4508  0.6179  196 GLN D OE1 
22233 N NE2 . GLN D 196 ? 1.8720 2.0014 1.6592 0.1924  0.5205  0.6931  196 GLN D NE2 
22242 N N   . SER D 197 ? 1.3667 1.5839 1.1610 0.2287  0.4071  0.3334  197 SER D N   
22243 C CA  . SER D 197 ? 1.3555 1.5486 1.1875 0.2175  0.3619  0.2660  197 SER D CA  
22244 C C   . SER D 197 ? 1.3229 1.4558 1.1973 0.1805  0.3095  0.2619  197 SER D C   
22245 O O   . SER D 197 ? 1.3196 1.4382 1.2628 0.1486  0.3122  0.3067  197 SER D O   
22246 C CB  . SER D 197 ? 1.3694 1.6044 1.3003 0.2090  0.3859  0.2607  197 SER D CB  
22247 O OG  . SER D 197 ? 1.3626 1.5873 1.4077 0.1638  0.3716  0.2886  197 SER D OG  
22253 N N   . ILE D 198 ? 1.3073 1.4051 1.1442 0.1851  0.2635  0.2064  198 ILE D N   
22254 C CA  . ILE D 198 ? 1.2435 1.2898 1.1148 0.1567  0.2162  0.1933  198 ILE D CA  
22255 C C   . ILE D 198 ? 1.1973 1.2366 1.1174 0.1468  0.1934  0.1462  198 ILE D C   
22256 O O   . ILE D 198 ? 1.2087 1.2566 1.0962 0.1683  0.1927  0.1038  198 ILE D O   
22257 C CB  . ILE D 198 ? 1.2300 1.2465 1.0219 0.1713  0.1844  0.1771  198 ILE D CB  
22258 C CG1 . ILE D 198 ? 1.2467 1.2661 0.9906 0.1845  0.2054  0.2338  198 ILE D CG1 
22259 C CG2 . ILE D 198 ? 1.1982 1.1682 1.0274 0.1468  0.1402  0.1569  198 ILE D CG2 
22260 C CD1 . ILE D 198 ? 1.2576 1.2572 0.9256 0.2050  0.1727  0.2240  198 ILE D CD1 
22272 N N   . THR D 199 ? 1.1521 1.1727 1.1478 0.1162  0.1736  0.1533  199 THR D N   
22273 C CA  . THR D 199 ? 1.1013 1.1182 1.1442 0.1089  0.1533  0.1204  199 THR D CA  
22274 C C   . THR D 199 ? 1.0870 1.0576 1.1383 0.0892  0.1107  0.1054  199 THR D C   
22275 O O   . THR D 199 ? 1.0894 1.0375 1.1566 0.0707  0.0993  0.1275  199 THR D O   
22276 C CB  . THR D 199 ? 1.0731 1.1306 1.2051 0.0970  0.1715  0.1420  199 THR D CB  
22277 O OG1 . THR D 199 ? 1.1219 1.2297 1.2475 0.1203  0.2177  0.1551  199 THR D OG1 
22278 C CG2 . THR D 199 ? 1.0188 1.0727 1.1940 0.0949  0.1457  0.1126  199 THR D CG2 
22286 N N   . CYS D 200 ? 1.0880 1.0420 1.1292 0.0950  0.0904  0.0685  200 CYS D N   
22287 C CA  . CYS D 200 ? 1.0995 1.0171 1.1453 0.0813  0.0563  0.0538  200 CYS D CA  
22288 C C   . CYS D 200 ? 1.0755 1.0007 1.1819 0.0696  0.0441  0.0558  200 CYS D C   
22289 O O   . CYS D 200 ? 1.0908 1.0298 1.2147 0.0809  0.0482  0.0440  200 CYS D O   
22290 C CB  . CYS D 200 ? 1.1189 1.0177 1.1245 0.0930  0.0451  0.0193  200 CYS D CB  
22291 S SG  . CYS D 200 ? 1.1048 0.9692 1.1175 0.0812  0.0146  0.0050  200 CYS D SG  
22296 N N   . ASN D 201 ? 1.0535 0.9682 1.1922 0.0492  0.0261  0.0690  201 ASN D N   
22297 C CA  . ASN D 201 ? 1.0229 0.9487 1.2155 0.0384  0.0046  0.0665  201 ASN D CA  
22298 C C   . ASN D 201 ? 0.9896 0.8806 1.1494 0.0402  -0.0257 0.0438  201 ASN D C   
22299 O O   . ASN D 201 ? 1.0141 0.8718 1.1447 0.0346  -0.0381 0.0381  201 ASN D O   
22300 C CB  . ASN D 201 ? 1.0606 0.9956 1.3136 0.0132  -0.0013 0.0871  201 ASN D CB  
22301 C CG  . ASN D 201 ? 1.0947 1.0537 1.3657 0.0097  0.0366  0.1198  201 ASN D CG  
22302 O OD1 . ASN D 201 ? 1.1248 1.0562 1.3720 0.0037  0.0441  0.1369  201 ASN D OD1 
22303 N ND2 . ASN D 201 ? 1.0871 1.0991 1.3989 0.0175  0.0632  0.1318  201 ASN D ND2 
22310 N N   . VAL D 202 ? 0.9714 0.8707 1.1355 0.0518  -0.0344 0.0341  202 VAL D N   
22311 C CA  . VAL D 202 ? 0.9834 0.8559 1.1122 0.0579  -0.0558 0.0196  202 VAL D CA  
22312 C C   . VAL D 202 ? 1.0068 0.8989 1.1657 0.0602  -0.0816 0.0204  202 VAL D C   
22313 O O   . VAL D 202 ? 1.0275 0.9549 1.2316 0.0667  -0.0773 0.0301  202 VAL D O   
22314 C CB  . VAL D 202 ? 0.9982 0.8555 1.0929 0.0737  -0.0396 0.0118  202 VAL D CB  
22315 C CG1 . VAL D 202 ? 1.0341 0.8686 1.0972 0.0798  -0.0539 0.0063  202 VAL D CG1 
22316 C CG2 . VAL D 202 ? 0.9723 0.8188 1.0388 0.0724  -0.0225 0.0049  202 VAL D CG2 
22326 N N   . ALA D 203 ? 1.0271 0.9004 1.1591 0.0589  -0.1095 0.0085  203 ALA D N   
22327 C CA  . ALA D 203 ? 1.0551 0.9487 1.2011 0.0651  -0.1422 0.0048  203 ALA D CA  
22328 C C   . ALA D 203 ? 1.0638 0.9319 1.1415 0.0823  -0.1541 -0.0039 203 ALA D C   
22329 O O   . ALA D 203 ? 1.0955 0.9334 1.1323 0.0792  -0.1549 -0.0176 203 ALA D O   
22330 C CB  . ALA D 203 ? 1.0974 1.0032 1.2899 0.0428  -0.1720 -0.0060 203 ALA D CB  
22336 N N   . HIS D 204 ? 1.0539 0.9357 1.1200 0.1038  -0.1605 0.0077  204 HIS D N   
22337 C CA  . HIS D 204 ? 1.0690 0.9335 1.0673 0.1245  -0.1684 0.0086  204 HIS D CA  
22338 C C   . HIS D 204 ? 1.0649 0.9591 1.0595 0.1385  -0.2117 0.0044  204 HIS D C   
22339 O O   . HIS D 204 ? 1.0508 0.9703 1.0644 0.1571  -0.2178 0.0248  204 HIS D O   
22340 C CB  . HIS D 204 ? 1.0595 0.9079 1.0403 0.1409  -0.1358 0.0330  204 HIS D CB  
22341 C CG  . HIS D 204 ? 1.1321 0.9595 1.0453 0.1576  -0.1285 0.0415  204 HIS D CG  
22342 N ND1 . HIS D 204 ? 1.1834 1.0075 1.0721 0.1825  -0.1219 0.0710  204 HIS D ND1 
22343 C CD2 . HIS D 204 ? 1.1608 0.9715 1.0271 0.1558  -0.1228 0.0281  204 HIS D CD2 
22344 C CE1 . HIS D 204 ? 1.2302 1.0388 1.0580 0.1933  -0.1093 0.0783  204 HIS D CE1 
22345 N NE2 . HIS D 204 ? 1.2175 1.0208 1.0320 0.1782  -0.1094 0.0501  204 HIS D NE2 
22353 N N   . PRO D 205 ? 1.0595 0.9518 1.0308 0.1333  -0.2459 -0.0242 205 PRO D N   
22354 C CA  . PRO D 205 ? 1.0918 1.0200 1.0664 0.1447  -0.2969 -0.0368 205 PRO D CA  
22355 C C   . PRO D 205 ? 1.1938 1.1320 1.1017 0.1839  -0.3041 -0.0156 205 PRO D C   
22356 O O   . PRO D 205 ? 1.2702 1.2502 1.1989 0.2003  -0.3379 -0.0085 205 PRO D O   
22357 C CB  . PRO D 205 ? 1.0758 0.9837 1.0259 0.1320  -0.3280 -0.0798 205 PRO D CB  
22358 C CG  . PRO D 205 ? 1.0692 0.9300 0.9658 0.1330  -0.2897 -0.0809 205 PRO D CG  
22359 C CD  . PRO D 205 ? 1.0298 0.8857 0.9659 0.1220  -0.2426 -0.0497 205 PRO D CD  
22367 N N   . ALA D 206 ? 1.2210 1.1257 1.0535 0.2009  -0.2721 -0.0014 206 ALA D N   
22368 C CA  . ALA D 206 ? 1.2906 1.2007 1.0551 0.2394  -0.2715 0.0287  206 ALA D CA  
22369 C C   . ALA D 206 ? 1.2495 1.1735 1.0598 0.2532  -0.2595 0.0696  206 ALA D C   
22370 O O   . ALA D 206 ? 1.2788 1.2147 1.0466 0.2886  -0.2707 0.0988  206 ALA D O   
22371 C CB  . ALA D 206 ? 1.3599 1.2333 1.0545 0.2490  -0.2274 0.0431  206 ALA D CB  
22377 N N   . SER D 207 ? 1.1961 1.1173 1.0871 0.2307  -0.2362 0.0730  207 SER D N   
22378 C CA  . SER D 207 ? 1.1977 1.1287 1.1395 0.2461  -0.2229 0.1047  207 SER D CA  
22379 C C   . SER D 207 ? 1.1273 1.1076 1.1600 0.2354  -0.2469 0.0920  207 SER D C   
22380 O O   . SER D 207 ? 1.0814 1.0737 1.1681 0.2486  -0.2322 0.1127  207 SER D O   
22381 C CB  . SER D 207 ? 1.2355 1.1214 1.1932 0.2356  -0.1685 0.1192  207 SER D CB  
22382 O OG  . SER D 207 ? 1.3423 1.1896 1.2347 0.2436  -0.1425 0.1369  207 SER D OG  
22388 N N   . SER D 208 ? 1.1461 1.1550 1.2038 0.2123  -0.2811 0.0587  208 SER D N   
22389 C CA  . SER D 208 ? 1.1591 1.2197 1.3182 0.1948  -0.2977 0.0491  208 SER D CA  
22390 C C   . SER D 208 ? 1.1668 1.2179 1.3807 0.1823  -0.2473 0.0611  208 SER D C   
22391 O O   . SER D 208 ? 1.1853 1.2791 1.4758 0.1885  -0.2424 0.0719  208 SER D O   
22392 C CB  . SER D 208 ? 1.1496 1.2701 1.3450 0.2240  -0.3386 0.0619  208 SER D CB  
22393 O OG  . SER D 208 ? 1.1777 1.3158 1.3214 0.2349  -0.3936 0.0424  208 SER D OG  
22399 N N   . THR D 209 ? 1.1364 1.1358 1.3094 0.1678  -0.2104 0.0568  209 THR D N   
22400 C CA  . THR D 209 ? 1.0572 1.0421 1.2603 0.1597  -0.1650 0.0622  209 THR D CA  
22401 C C   . THR D 209 ? 1.0121 1.0070 1.2511 0.1265  -0.1575 0.0464  209 THR D C   
22402 O O   . THR D 209 ? 1.0371 1.0129 1.2488 0.1072  -0.1721 0.0301  209 THR D O   
22403 C CB  . THR D 209 ? 1.0591 0.9861 1.2011 0.1648  -0.1326 0.0670  209 THR D CB  
22404 O OG1 . THR D 209 ? 1.1493 1.0608 1.2588 0.1942  -0.1355 0.0899  209 THR D OG1 
22405 C CG2 . THR D 209 ? 0.9769 0.8906 1.1463 0.1603  -0.0928 0.0649  209 THR D CG2 
22413 N N   . LYS D 210 ? 1.0000 1.0232 1.2988 0.1234  -0.1317 0.0534  210 LYS D N   
22414 C CA  . LYS D 210 ? 1.0674 1.0984 1.3957 0.0961  -0.1130 0.0494  210 LYS D CA  
22415 C C   . LYS D 210 ? 1.1333 1.1679 1.4715 0.1076  -0.0676 0.0565  210 LYS D C   
22416 O O   . LYS D 210 ? 1.2234 1.2993 1.6154 0.1248  -0.0560 0.0659  210 LYS D O   
22417 C CB  . LYS D 210 ? 1.0951 1.1800 1.5062 0.0759  -0.1363 0.0510  210 LYS D CB  
22418 C CG  . LYS D 210 ? 1.1466 1.2098 1.5472 0.0486  -0.1696 0.0337  210 LYS D CG  
22419 C CD  . LYS D 210 ? 1.1921 1.3054 1.6934 0.0210  -0.1896 0.0344  210 LYS D CD  
22420 C CE  . LYS D 210 ? 1.2782 1.3568 1.7741 -0.0076 -0.2231 0.0116  210 LYS D CE  
22421 N NZ  . LYS D 210 ? 1.3571 1.4139 1.7871 0.0086  -0.2690 -0.0160 210 LYS D NZ  
22435 N N   . VAL D 211 ? 1.0869 1.0820 1.3733 0.1016  -0.0439 0.0489  211 VAL D N   
22436 C CA  . VAL D 211 ? 1.0290 1.0206 1.3057 0.1153  -0.0058 0.0458  211 VAL D CA  
22437 C C   . VAL D 211 ? 1.0738 1.0704 1.3400 0.0986  0.0146  0.0481  211 VAL D C   
22438 O O   . VAL D 211 ? 1.1080 1.0803 1.3468 0.0795  0.0015  0.0471  211 VAL D O   
22439 C CB  . VAL D 211 ? 0.9274 0.8671 1.1487 0.1281  0.0003  0.0320  211 VAL D CB  
22440 C CG1 . VAL D 211 ? 0.8936 0.8263 1.1016 0.1405  0.0330  0.0175  211 VAL D CG1 
22441 C CG2 . VAL D 211 ? 0.8984 0.8289 1.1296 0.1481  -0.0136 0.0401  211 VAL D CG2 
22451 N N   . ASP D 212 ? 1.0716 1.0991 1.3562 0.1103  0.0485  0.0530  212 ASP D N   
22452 C CA  . ASP D 212 ? 1.0605 1.0955 1.3226 0.1030  0.0746  0.0612  212 ASP D CA  
22453 C C   . ASP D 212 ? 1.0229 1.0490 1.2359 0.1288  0.1022  0.0415  212 ASP D C   
22454 O O   . ASP D 212 ? 1.0110 1.0614 1.2482 0.1525  0.1229  0.0355  212 ASP D O   
22455 C CB  . ASP D 212 ? 1.0650 1.1574 1.3977 0.0927  0.0939  0.0898  212 ASP D CB  
22456 C CG  . ASP D 212 ? 1.0604 1.1613 1.4529 0.0634  0.0606  0.1015  212 ASP D CG  
22457 O OD1 . ASP D 212 ? 1.0529 1.1083 1.4106 0.0474  0.0320  0.0927  212 ASP D OD1 
22458 O OD2 . ASP D 212 ? 1.0806 1.2364 1.5585 0.0577  0.0617  0.1158  212 ASP D OD2 
22463 N N   . LYS D 213 ? 0.9956 0.9882 1.1425 0.1266  0.0999  0.0278  213 LYS D N   
22464 C CA  . LYS D 213 ? 1.0112 0.9928 1.1063 0.1487  0.1164  -0.0004 213 LYS D CA  
22465 C C   . LYS D 213 ? 1.0395 1.0389 1.0860 0.1526  0.1355  0.0093  213 LYS D C   
22466 O O   . LYS D 213 ? 1.0578 1.0476 1.0887 0.1353  0.1240  0.0287  213 LYS D O   
22467 C CB  . LYS D 213 ? 1.0106 0.9427 1.0731 0.1451  0.0922  -0.0295 213 LYS D CB  
22468 C CG  . LYS D 213 ? 1.0236 0.9323 1.1224 0.1467  0.0791  -0.0339 213 LYS D CG  
22469 C CD  . LYS D 213 ? 1.1006 1.0197 1.2290 0.1732  0.0996  -0.0436 213 LYS D CD  
22470 C CE  . LYS D 213 ? 1.1511 1.0326 1.3044 0.1797  0.0872  -0.0474 213 LYS D CE  
22471 N NZ  . LYS D 213 ? 1.2009 1.0943 1.3964 0.2092  0.1042  -0.0483 213 LYS D NZ  
22485 N N   . LYS D 214 ? 1.0718 1.0949 1.0897 0.1798  0.1650  -0.0043 214 LYS D N   
22486 C CA  . LYS D 214 ? 1.1474 1.1939 1.1054 0.1928  0.1876  0.0071  214 LYS D CA  
22487 C C   . LYS D 214 ? 1.2119 1.2362 1.0922 0.2116  0.1746  -0.0389 214 LYS D C   
22488 O O   . LYS D 214 ? 1.2380 1.2361 1.1222 0.2192  0.1623  -0.0821 214 LYS D O   
22489 C CB  . LYS D 214 ? 1.1950 1.2970 1.1705 0.2145  0.2351  0.0270  214 LYS D CB  
22490 C CG  . LYS D 214 ? 1.2658 1.3991 1.1885 0.2239  0.2656  0.0616  214 LYS D CG  
22491 C CD  . LYS D 214 ? 1.3317 1.5281 1.2766 0.2467  0.3212  0.0858  214 LYS D CD  
22492 C CE  . LYS D 214 ? 1.3221 1.5521 1.3804 0.2183  0.3342  0.1327  214 LYS D CE  
22493 N NZ  . LYS D 214 ? 1.3855 1.6824 1.4633 0.2299  0.3941  0.1801  214 LYS D NZ  
22507 N N   . ILE D 215 ? 1.2411 1.2755 1.0548 0.2190  0.1755  -0.0285 215 ILE D N   
22508 C CA  . ILE D 215 ? 1.2671 1.2891 1.0077 0.2351  0.1535  -0.0726 215 ILE D CA  
22509 C C   . ILE D 215 ? 1.3320 1.3921 0.9967 0.2736  0.1834  -0.0815 215 ILE D C   
22510 O O   . ILE D 215 ? 1.4009 1.4871 1.0134 0.2846  0.1979  -0.0440 215 ILE D O   
22511 C CB  . ILE D 215 ? 1.2452 1.2517 0.9638 0.2190  0.1219  -0.0568 215 ILE D CB  
22512 C CG1 . ILE D 215 ? 1.1650 1.1361 0.9510 0.1863  0.0963  -0.0534 215 ILE D CG1 
22513 C CG2 . ILE D 215 ? 1.3010 1.3082 0.9518 0.2365  0.0947  -0.1022 215 ILE D CG2 
22514 C CD1 . ILE D 215 ? 1.1876 1.1449 0.9650 0.1728  0.0720  -0.0323 215 ILE D CD1 
22526 N N   . GLU D 216 ? 1.3341 1.3957 0.9898 0.2977  0.1955  -0.1291 216 GLU D N   
22527 C CA  . GLU D 216 ? 1.4540 1.5562 1.0383 0.3404  0.2318  -0.1403 216 GLU D CA  
22528 C C   . GLU D 216 ? 1.5888 1.6947 1.0664 0.3671  0.2083  -0.1865 216 GLU D C   
22529 O O   . GLU D 216 ? 1.6580 1.8040 1.0538 0.3943  0.2295  -0.1607 216 GLU D O   
22530 C CB  . GLU D 216 ? 1.4686 1.5711 1.0925 0.3609  0.2576  -0.1739 216 GLU D CB  
22531 C CG  . GLU D 216 ? 1.4692 1.6089 1.1703 0.3563  0.3001  -0.1184 216 GLU D CG  
22532 C CD  . GLU D 216 ? 1.4891 1.6073 1.2791 0.3531  0.2982  -0.1379 216 GLU D CD  
22533 O OE1 . GLU D 216 ? 1.5722 1.6872 1.3514 0.3880  0.3148  -0.1837 216 GLU D OE1 
22534 O OE2 . GLU D 216 ? 1.4347 1.5374 1.3017 0.3193  0.2789  -0.1082 216 GLU D OE2 
22541 N N   . PRO D 217 ? 1.6430 1.7113 1.1189 0.3609  0.1640  -0.2531 217 PRO D N   
22542 C CA  . PRO D 217 ? 1.7532 1.8349 1.1296 0.3898  0.1381  -0.3060 217 PRO D CA  
22543 C C   . PRO D 217 ? 1.8013 1.8818 1.1588 0.3713  0.0895  -0.2998 217 PRO D C   
22544 O O   . PRO D 217 ? 1.8650 1.9293 1.2190 0.3656  0.0435  -0.3615 217 PRO D O   
22545 C CB  . PRO D 217 ? 1.7534 1.7952 1.1542 0.3941  0.1198  -0.3898 217 PRO D CB  
22546 C CG  . PRO D 217 ? 1.6813 1.6766 1.1984 0.3503  0.1094  -0.3734 217 PRO D CG  
22547 C CD  . PRO D 217 ? 1.6043 1.6207 1.1646 0.3340  0.1404  -0.2883 217 PRO D CD  
# 
