HEADER TRANSFERASE 20-OCT-15 5FKW
TITLE CRYO-EM STRUCTURE OF THE E. COLI REPLICATIVE DNA POLYMERASE COMPLEX
TITLE 2 BOUND TO DNA (DNA POLYMERASE III ALPHA, BETA, EPSILON)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE III ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.7.7;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA POLYMERASE III BETA;
COMPND 9 CHAIN: B, C;
COMPND 10 EC: 2.7.7.7;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA POLYMERASE III EPSILON;
COMPND 14 CHAIN: D;
COMPND 15 EC: 2.7.7.7;
COMPND 16 ENGINEERED: YES;
COMPND 17 MUTATION: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: PRIMER-TEMPLATE DUPLEX DNA;
COMPND 20 CHAIN: P;
COMPND 21 ENGINEERED: YES;
COMPND 22 OTHER_DETAILS: TEMPLATE STRAND TCAGGAGTCCTTCGTCCTAGTACTACTCC PRIMER
COMPND 23 STRAND GGAGTAGTACTAGGACGAAGGACTC;
COMPND 24 MOL_ID: 5;
COMPND 25 MOLECULE: PRIMER-TEMPLATE DUPLEX DNA;
COMPND 26 CHAIN: T;
COMPND 27 ENGINEERED: YES;
COMPND 28 OTHER_DETAILS: TEMPLATE STRAND TCAGGAGTCCTTCGTCCTAGTACTACTCC PRIMER
COMPND 29 STRAND GGAGTAGTACTAGGACGAAGGACTC
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 ATCC: 10798;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 12 ORGANISM_TAXID: 83333;
SOURCE 13 ATCC: 10798;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET3D;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 21 ORGANISM_TAXID: 83333;
SOURCE 22 ATCC: 10798;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 25 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PET3D;
SOURCE 28 MOL_ID: 4;
SOURCE 29 SYNTHETIC: YES;
SOURCE 30 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 31 ORGANISM_TAXID: 32630;
SOURCE 32 MOL_ID: 5;
SOURCE 33 SYNTHETIC: YES;
SOURCE 34 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 35 ORGANISM_TAXID: 32630
KEYWDS TRANSFERASE, DNA REPLICATION, DNA POLYMERASE III ALPHA, DNA
KEYWDS 2 POLYMERASE III BETA, DNA POLYMERASE III EPSILON
EXPDTA ELECTRON MICROSCOPY
AUTHOR R.FERNANDEZ-LEIRO,J.CONRAD,S.H.W.SCHERES,M.H.LAMERS
REVDAT 4 27-FEB-19 5FKW 1 JRNL
REVDAT 3 19-APR-17 5FKW 1 REMARK
REVDAT 2 21-DEC-16 5FKW 1 JRNL
REVDAT 1 25-NOV-15 5FKW 0
JRNL AUTH R.FERNANDEZ-LEIRO,J.CONRAD,S.H.SCHERES,M.H.LAMERS
JRNL TITL CRYO-EM STRUCTURES OF THEE. COLIREPLICATIVE DNA POLYMERASE
JRNL TITL 2 REVEAL ITS DYNAMIC INTERACTIONS WITH THE DNA SLIDING CLAMP,
JRNL TITL 3 EXONUCLEASE ANDTAU.
JRNL REF ELIFE V. 4 2015
JRNL REFN ESSN 2050-084X
JRNL PMID 26499492
JRNL DOI 10.7554/ELIFE.11134
REMARK 2
REMARK 2 RESOLUTION. 7.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 7.300
REMARK 3 NUMBER OF PARTICLES : 40582
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 5FKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1290065339.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : VITREOUS ICE
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : DNA POLYMERASE III CATALYTIC
REMARK 245 COMPLEX (ALPHA, EPSILON, BETA,
REMARK 245 TAU)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00
REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : LIQUID ETHANE
REMARK 245 SAMPLE BUFFER : 25 MM HEPES PH 7.5, 150 MM
REMARK 245 NACL, AND 2 MM DTT
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 12-MAY-14
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 85.00
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 QUANTUM (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 2000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 4000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 40.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 64000
REMARK 245 CALIBRATED MAGNIFICATION : 28409
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, P, T
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 928
REMARK 465 GLU A 929
REMARK 465 GLU A 930
REMARK 465 PRO A 931
REMARK 465 GLU A 932
REMARK 465 GLN A 933
REMARK 465 ILE A 934
REMARK 465 GLU A 935
REMARK 465 GLN A 936
REMARK 465 SER A 937
REMARK 465 TYR A 938
REMARK 465 ALA A 939
REMARK 465 SER A 940
REMARK 465 CYS A 941
REMARK 465 GLN A 942
REMARK 465 PRO A 943
REMARK 465 TRP A 944
REMARK 465 PRO A 945
REMARK 465 GLU A 946
REMARK 465 GLN A 947
REMARK 465 VAL A 948
REMARK 465 VAL A 949
REMARK 465 LEU A 950
REMARK 465 ASP A 951
REMARK 465 GLY A 952
REMARK 465 GLU A 953
REMARK 465 ARG A 954
REMARK 465 GLU A 955
REMARK 465 THR A 956
REMARK 465 LEU A 957
REMARK 465 GLY A 958
REMARK 465 LEU A 959
REMARK 465 TYR A 960
REMARK 465 LEU A 961
REMARK 465 THR A 962
REMARK 465 GLY A 963
REMARK 465 HIS A 964
REMARK 465 PRO A 965
REMARK 465 ILE A 966
REMARK 465 ASN A 967
REMARK 465 GLN A 968
REMARK 465 TYR A 969
REMARK 465 LEU A 970
REMARK 465 LYS A 971
REMARK 465 GLU A 972
REMARK 465 ILE A 973
REMARK 465 GLU A 974
REMARK 465 ARG A 975
REMARK 465 TYR A 976
REMARK 465 VAL A 977
REMARK 465 GLY A 978
REMARK 465 GLY A 979
REMARK 465 VAL A 980
REMARK 465 ARG A 981
REMARK 465 LEU A 982
REMARK 465 LYS A 983
REMARK 465 ASP A 984
REMARK 465 MET A 985
REMARK 465 HIS A 986
REMARK 465 PRO A 987
REMARK 465 THR A 988
REMARK 465 GLU A 989
REMARK 465 ARG A 990
REMARK 465 GLY A 991
REMARK 465 LYS A 992
REMARK 465 VAL A 993
REMARK 465 ILE A 994
REMARK 465 THR A 995
REMARK 465 ALA A 996
REMARK 465 ALA A 997
REMARK 465 GLY A 998
REMARK 465 LEU A 999
REMARK 465 VAL A 1000
REMARK 465 VAL A 1001
REMARK 465 ALA A 1002
REMARK 465 ALA A 1003
REMARK 465 ARG A 1004
REMARK 465 VAL A 1005
REMARK 465 MET A 1006
REMARK 465 VAL A 1007
REMARK 465 THR A 1008
REMARK 465 LYS A 1009
REMARK 465 ARG A 1010
REMARK 465 GLY A 1011
REMARK 465 ASN A 1012
REMARK 465 ARG A 1013
REMARK 465 ILE A 1014
REMARK 465 GLY A 1015
REMARK 465 ILE A 1016
REMARK 465 CYS A 1017
REMARK 465 THR A 1018
REMARK 465 LEU A 1019
REMARK 465 ASP A 1020
REMARK 465 ASP A 1021
REMARK 465 ARG A 1022
REMARK 465 SER A 1023
REMARK 465 GLY A 1024
REMARK 465 ARG A 1025
REMARK 465 LEU A 1026
REMARK 465 GLU A 1027
REMARK 465 VAL A 1028
REMARK 465 MET A 1029
REMARK 465 LEU A 1030
REMARK 465 PHE A 1031
REMARK 465 THR A 1032
REMARK 465 ASP A 1033
REMARK 465 ALA A 1034
REMARK 465 LEU A 1035
REMARK 465 ASP A 1036
REMARK 465 LYS A 1037
REMARK 465 TYR A 1038
REMARK 465 GLN A 1039
REMARK 465 GLN A 1040
REMARK 465 LEU A 1041
REMARK 465 LEU A 1042
REMARK 465 GLU A 1043
REMARK 465 LYS A 1044
REMARK 465 ASP A 1045
REMARK 465 ARG A 1046
REMARK 465 ILE A 1047
REMARK 465 LEU A 1048
REMARK 465 ILE A 1049
REMARK 465 VAL A 1050
REMARK 465 SER A 1051
REMARK 465 GLY A 1052
REMARK 465 GLN A 1053
REMARK 465 VAL A 1054
REMARK 465 SER A 1055
REMARK 465 PHE A 1056
REMARK 465 ASP A 1057
REMARK 465 ASP A 1058
REMARK 465 PHE A 1059
REMARK 465 SER A 1060
REMARK 465 GLY A 1061
REMARK 465 GLY A 1062
REMARK 465 LEU A 1063
REMARK 465 LYS A 1064
REMARK 465 MET A 1065
REMARK 465 THR A 1066
REMARK 465 ALA A 1067
REMARK 465 ARG A 1068
REMARK 465 GLU A 1069
REMARK 465 VAL A 1070
REMARK 465 MET A 1071
REMARK 465 ASP A 1072
REMARK 465 ILE A 1073
REMARK 465 ASP A 1074
REMARK 465 GLU A 1075
REMARK 465 ALA A 1076
REMARK 465 ARG A 1077
REMARK 465 GLU A 1078
REMARK 465 LYS A 1079
REMARK 465 TYR A 1080
REMARK 465 ALA A 1081
REMARK 465 ARG A 1082
REMARK 465 GLY A 1083
REMARK 465 LEU A 1084
REMARK 465 ALA A 1085
REMARK 465 ILE A 1086
REMARK 465 SER A 1087
REMARK 465 LEU A 1088
REMARK 465 THR A 1089
REMARK 465 ASP A 1090
REMARK 465 ARG A 1091
REMARK 465 GLN A 1092
REMARK 465 ILE A 1093
REMARK 465 ASP A 1094
REMARK 465 ASP A 1095
REMARK 465 GLN A 1096
REMARK 465 LEU A 1097
REMARK 465 LEU A 1098
REMARK 465 ASN A 1099
REMARK 465 ARG A 1100
REMARK 465 LEU A 1101
REMARK 465 ARG A 1102
REMARK 465 GLN A 1103
REMARK 465 SER A 1104
REMARK 465 LEU A 1105
REMARK 465 GLU A 1106
REMARK 465 PRO A 1107
REMARK 465 HIS A 1108
REMARK 465 ARG A 1109
REMARK 465 SER A 1110
REMARK 465 GLY A 1111
REMARK 465 THR A 1112
REMARK 465 ILE A 1113
REMARK 465 PRO A 1114
REMARK 465 VAL A 1115
REMARK 465 HIS A 1116
REMARK 465 LEU A 1117
REMARK 465 TYR A 1118
REMARK 465 TYR A 1119
REMARK 465 GLN A 1120
REMARK 465 ARG A 1121
REMARK 465 ALA A 1122
REMARK 465 ASP A 1123
REMARK 465 ALA A 1124
REMARK 465 ARG A 1125
REMARK 465 ALA A 1126
REMARK 465 ARG A 1127
REMARK 465 LEU A 1128
REMARK 465 ARG A 1129
REMARK 465 PHE A 1130
REMARK 465 GLY A 1131
REMARK 465 ALA A 1132
REMARK 465 THR A 1133
REMARK 465 TRP A 1134
REMARK 465 ARG A 1135
REMARK 465 VAL A 1136
REMARK 465 SER A 1137
REMARK 465 PRO A 1138
REMARK 465 SER A 1139
REMARK 465 ASP A 1140
REMARK 465 ARG A 1141
REMARK 465 LEU A 1142
REMARK 465 LEU A 1143
REMARK 465 ASN A 1144
REMARK 465 ASP A 1145
REMARK 465 LEU A 1146
REMARK 465 ARG A 1147
REMARK 465 GLY A 1148
REMARK 465 LEU A 1149
REMARK 465 ILE A 1150
REMARK 465 GLY A 1151
REMARK 465 SER A 1152
REMARK 465 GLU A 1153
REMARK 465 GLN A 1154
REMARK 465 VAL A 1155
REMARK 465 GLU A 1156
REMARK 465 LEU A 1157
REMARK 465 GLU A 1158
REMARK 465 PHE A 1159
REMARK 465 ASP A 1160
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 THR D 3
REMARK 465 ALA D 4
REMARK 465 ILE D 5
REMARK 465 THR D 6
REMARK 465 GLU D 190
REMARK 465 GLY D 191
REMARK 465 GLU D 192
REMARK 465 THR D 193
REMARK 465 GLN D 194
REMARK 465 GLN D 195
REMARK 465 GLN D 196
REMARK 465 GLN D 197
REMARK 465 GLY D 198
REMARK 465 GLU D 199
REMARK 465 ALA D 200
REMARK 465 THR D 201
REMARK 465 ILE D 202
REMARK 465 GLN D 203
REMARK 465 ARG D 204
REMARK 465 ILE D 205
REMARK 465 VAL D 206
REMARK 465 ARG D 207
REMARK 465 DT T 9
REMARK 465 DC T 10
REMARK 465 DA T 11
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG A 560 N LEU A 562 1.87
REMARK 500 O GLY A 558 N ARG A 560 1.94
REMARK 500 N3 DC P 25 O6 DG T 13 2.09
REMARK 500 NH2 ARG A 639 O TYR A 754 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN A 687 CD GLN A 687 NE2 0.241
REMARK 500 GLU D 110 CD GLU D 110 OE2 0.074
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 614 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 PHE A 924 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 PHE A 924 N - CA - C ANGL. DEV. = 19.3 DEGREES
REMARK 500 ARG C 73 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 LEU D 212 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 LEU D 212 N - CA - CB ANGL. DEV. = -13.5 DEGREES
REMARK 500 LEU D 212 N - CA - C ANGL. DEV. = 18.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 2 -75.86 -57.47
REMARK 500 MET A 17 -42.67 68.19
REMARK 500 ASP A 19 -158.32 -158.60
REMARK 500 LEU A 21 -56.62 -136.32
REMARK 500 LEU A 39 125.46 -173.36
REMARK 500 ASN A 125 -57.06 -133.65
REMARK 500 PHE A 162 52.60 -140.85
REMARK 500 ASP A 164 16.03 56.64
REMARK 500 ARG A 232 68.22 -118.20
REMARK 500 GLN A 238 46.18 -78.68
REMARK 500 PHE A 281 145.59 -176.20
REMARK 500 THR A 283 -139.86 -128.45
REMARK 500 SER A 287 154.78 -47.03
REMARK 500 MET A 399 122.10 -38.45
REMARK 500 ASP A 403 62.38 39.23
REMARK 500 ASN A 507 -174.96 162.39
REMARK 500 HIS A 511 -154.40 -138.87
REMARK 500 LYS A 521 132.13 -33.74
REMARK 500 ASP A 531 -170.48 -69.32
REMARK 500 LEU A 559 42.61 -42.42
REMARK 500 THR A 561 -36.14 29.75
REMARK 500 ARG A 575 2.82 -57.71
REMARK 500 ASN A 579 39.01 -150.72
REMARK 500 GLN A 610 -9.77 83.45
REMARK 500 TYR A 778 71.20 -172.51
REMARK 500 PRO A 779 69.44 -63.47
REMARK 500 ALA A 780 -14.16 -153.92
REMARK 500 GLU A 781 -39.82 -131.81
REMARK 500 PHE A 782 -54.72 -29.82
REMARK 500 ASP A 790 51.59 -109.30
REMARK 500 LEU A 809 175.30 -54.37
REMARK 500 LYS A 810 138.09 92.19
REMARK 500 ILE A 811 136.75 175.31
REMARK 500 HIS A 822 -152.15 -119.60
REMARK 500 ARG A 895 19.42 -51.51
REMARK 500 ALA A 896 -35.22 -158.44
REMARK 500 GLN A 920 139.72 -171.52
REMARK 500 ASP A 922 -169.63 -107.38
REMARK 500 PHE A 924 -177.58 -1.57
REMARK 500 VAL A 926 156.43 172.75
REMARK 500 ARG B 24 60.46 38.68
REMARK 500 ASP B 39 -148.92 68.20
REMARK 500 LEU B 49 -24.94 73.43
REMARK 500 GLU B 125 -42.52 -132.80
REMARK 500 HIS B 148 -62.59 -96.42
REMARK 500 GLU B 163 121.96 -175.11
REMARK 500 HIS B 175 -53.10 -121.87
REMARK 500 ARG B 240 63.07 67.66
REMARK 500 ASN B 251 72.27 54.64
REMARK 500 ASN B 288 12.41 59.42
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 2 GLU A 3 125.53
REMARK 500 PRO A 400 ASP A 401 -132.42
REMARK 500 PHE A 433 GLY A 434 148.76
REMARK 500 GLY A 509 LYS A 510 -138.32
REMARK 500 LEU A 559 ARG A 560 -141.36
REMARK 500 ARG A 895 ALA A 896 -149.83
REMARK 500 LEU A 923 PHE A 924 -134.82
REMARK 500 LEU B 21 GLY B 22 134.79
REMARK 500 GLY D 67 ILE D 68 -145.94
REMARK 500 LYS D 211 LEU D 212 -125.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU A 559 12.40
REMARK 500 ARG A 576 -10.88
REMARK 500 LEU A 923 -13.37
REMARK 500 PHE A 924 12.28
REMARK 500 GLY D 67 -10.64
REMARK 500 LYS D 211 -12.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FKU RELATED DB: PDB
REMARK 900 CRYO-EM STRUCTURE OF THE E. COLI REPLICATIVE DNA POLYMERASE COMPLEX
REMARK 900 IN DNA FREE STATE (DNA POLYMERASE III ALPHA, BETA, EPSILON, TAU
REMARK 900 COMPLEX)
REMARK 900 RELATED ID: 5FKV RELATED DB: PDB
REMARK 900 CRYO-EM STRUCTURE OF THE E. COLI REPLICATIVE DNA POLYMERASE COMPLEX
REMARK 900 BOUND TO DNA (DNA POLYMERASE III ALPHA, BETA, EPSILON, TAU COMPLEX)
REMARK 900 RELATED ID: EMD-3202 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE E. COLI REPLICATIVE DNA POLYMERASE COMPLEX
REMARK 900 BOUND TO DNA (DNA POLYMERASE III ALPHA, BETA, AND EPSILON SUBUNITS)
DBREF 5FKW A 1 1160 UNP P10443 DPO3A_ECOLI 1 1160
DBREF 5FKW B 1 366 UNP P0A988 DPO3B_ECOLI 1 366
DBREF 5FKW C 1 366 UNP P0A988 DPO3B_ECOLI 1 366
DBREF 5FKW D 1 243 UNP P03007 DPO3E_ECOLI 1 243
DBREF 5FKW T 12 37 PDB 5FKW 5FKW 12 37
DBREF 5FKW P 1 25 PDB 5FKW 5FKW 1 25
SEQADV 5FKW LEU A 921 UNP P10443 ALA 921 ENGINEERED MUTATION
SEQADV 5FKW LEU A 923 UNP P10443 MET 923 ENGINEERED MUTATION
SEQADV 5FKW LEU D 183 UNP P03007 THR 183 ENGINEERED MUTATION
SEQADV 5FKW LEU D 185 UNP P03007 MET 185 ENGINEERED MUTATION
SEQADV 5FKW PRO D 186 UNP P03007 ALA 186 ENGINEERED MUTATION
SEQADV 5FKW LEU D 187 UNP P03007 PHE 187 ENGINEERED MUTATION
SEQRES 1 A 1160 MET SER GLU PRO ARG PHE VAL HIS LEU ARG VAL HIS SER
SEQRES 2 A 1160 ASP TYR SER MET ILE ASP GLY LEU ALA LYS THR ALA PRO
SEQRES 3 A 1160 LEU VAL LYS LYS ALA ALA ALA LEU GLY MET PRO ALA LEU
SEQRES 4 A 1160 ALA ILE THR ASP PHE THR ASN LEU CYS GLY LEU VAL LYS
SEQRES 5 A 1160 PHE TYR GLY ALA GLY HIS GLY ALA GLY ILE LYS PRO ILE
SEQRES 6 A 1160 VAL GLY ALA ASP PHE ASN VAL GLN CYS ASP LEU LEU GLY
SEQRES 7 A 1160 ASP GLU LEU THR HIS LEU THR VAL LEU ALA ALA ASN ASN
SEQRES 8 A 1160 THR GLY TYR GLN ASN LEU THR LEU LEU ILE SER LYS ALA
SEQRES 9 A 1160 TYR GLN ARG GLY TYR GLY ALA ALA GLY PRO ILE ILE ASP
SEQRES 10 A 1160 ARG ASP TRP LEU ILE GLU LEU ASN GLU GLY LEU ILE LEU
SEQRES 11 A 1160 LEU SER GLY GLY ARG MET GLY ASP VAL GLY ARG SER LEU
SEQRES 12 A 1160 LEU ARG GLY ASN SER ALA LEU VAL ASP GLU CYS VAL ALA
SEQRES 13 A 1160 PHE TYR GLU GLU HIS PHE PRO ASP ARG TYR PHE LEU GLU
SEQRES 14 A 1160 LEU ILE ARG THR GLY ARG PRO ASP GLU GLU SER TYR LEU
SEQRES 15 A 1160 HIS ALA ALA VAL GLU LEU ALA GLU ALA ARG GLY LEU PRO
SEQRES 16 A 1160 VAL VAL ALA THR ASN ASP VAL ARG PHE ILE ASP SER SER
SEQRES 17 A 1160 ASP PHE ASP ALA HIS GLU ILE ARG VAL ALA ILE HIS ASP
SEQRES 18 A 1160 GLY PHE THR LEU ASP ASP PRO LYS ARG PRO ARG ASN TYR
SEQRES 19 A 1160 SER PRO GLN GLN TYR MET ARG SER GLU GLU GLU MET CYS
SEQRES 20 A 1160 GLU LEU PHE ALA ASP ILE PRO GLU ALA LEU ALA ASN THR
SEQRES 21 A 1160 VAL GLU ILE ALA LYS ARG CYS ASN VAL THR VAL ARG LEU
SEQRES 22 A 1160 GLY GLU TYR PHE LEU PRO GLN PHE PRO THR GLY ASP MET
SEQRES 23 A 1160 SER THR GLU ASP TYR LEU VAL LYS ARG ALA LYS GLU GLY
SEQRES 24 A 1160 LEU GLU GLU ARG LEU ALA PHE LEU PHE PRO ASP GLU GLU
SEQRES 25 A 1160 GLU ARG LEU LYS ARG ARG PRO GLU TYR ASP GLU ARG LEU
SEQRES 26 A 1160 GLU THR GLU LEU GLN VAL ILE ASN GLN MET GLY PHE PRO
SEQRES 27 A 1160 GLY TYR PHE LEU ILE VAL MET GLU PHE ILE GLN TRP SER
SEQRES 28 A 1160 LYS ASP ASN GLY VAL PRO VAL GLY PRO GLY ARG GLY SER
SEQRES 29 A 1160 GLY ALA GLY SER LEU VAL ALA TYR ALA LEU LYS ILE THR
SEQRES 30 A 1160 ASP LEU ASP PRO LEU GLU PHE ASP LEU LEU PHE GLU ARG
SEQRES 31 A 1160 PHE LEU ASN PRO GLU ARG VAL SER MET PRO ASP PHE ASP
SEQRES 32 A 1160 VAL ASP PHE CYS MET GLU LYS ARG ASP GLN VAL ILE GLU
SEQRES 33 A 1160 HIS VAL ALA ASP MET TYR GLY ARG ASP ALA VAL SER GLN
SEQRES 34 A 1160 ILE ILE THR PHE GLY THR MET ALA ALA LYS ALA VAL ILE
SEQRES 35 A 1160 ARG ASP VAL GLY ARG VAL LEU GLY HIS PRO TYR GLY PHE
SEQRES 36 A 1160 VAL ASP ARG ILE SER LYS LEU ILE PRO PRO ASP PRO GLY
SEQRES 37 A 1160 MET THR LEU ALA LYS ALA PHE GLU ALA GLU PRO GLN LEU
SEQRES 38 A 1160 PRO GLU ILE TYR GLU ALA ASP GLU GLU VAL LYS ALA LEU
SEQRES 39 A 1160 ILE ASP MET ALA ARG LYS LEU GLU GLY VAL THR ARG ASN
SEQRES 40 A 1160 ALA GLY LYS HIS ALA GLY GLY VAL VAL ILE ALA PRO THR
SEQRES 41 A 1160 LYS ILE THR ASP PHE ALA PRO LEU TYR CYS ASP GLU GLU
SEQRES 42 A 1160 GLY LYS HIS PRO VAL THR GLN PHE ASP LYS SER ASP VAL
SEQRES 43 A 1160 GLU TYR ALA GLY LEU VAL LYS PHE ASP PHE LEU GLY LEU
SEQRES 44 A 1160 ARG THR LEU THR ILE ILE ASN TRP ALA LEU GLU MET ILE
SEQRES 45 A 1160 ASN LYS ARG ARG ALA LYS ASN GLY GLU PRO PRO LEU ASP
SEQRES 46 A 1160 ILE ALA ALA ILE PRO LEU ASP ASP LYS LYS SER PHE ASP
SEQRES 47 A 1160 MET LEU GLN ARG SER GLU THR THR ALA VAL PHE GLN LEU
SEQRES 48 A 1160 GLU SER ARG GLY MET LYS ASP LEU ILE LYS ARG LEU GLN
SEQRES 49 A 1160 PRO ASP CYS PHE GLU ASP MET ILE ALA LEU VAL ALA LEU
SEQRES 50 A 1160 PHE ARG PRO GLY PRO LEU GLN SER GLY MET VAL ASP ASN
SEQRES 51 A 1160 PHE ILE ASP ARG LYS HIS GLY ARG GLU GLU ILE SER TYR
SEQRES 52 A 1160 PRO ASP VAL GLN TRP GLN HIS GLU SER LEU LYS PRO VAL
SEQRES 53 A 1160 LEU GLU PRO THR TYR GLY ILE ILE LEU TYR GLN GLU GLN
SEQRES 54 A 1160 VAL MET GLN ILE ALA GLN VAL LEU SER GLY TYR THR LEU
SEQRES 55 A 1160 GLY GLY ALA ASP MET LEU ARG ARG ALA MET GLY LYS LYS
SEQRES 56 A 1160 LYS PRO GLU GLU MET ALA LYS GLN ARG SER VAL PHE ALA
SEQRES 57 A 1160 GLU GLY ALA GLU LYS ASN GLY ILE ASN ALA GLU LEU ALA
SEQRES 58 A 1160 MET LYS ILE PHE ASP LEU VAL GLU LYS PHE ALA GLY TYR
SEQRES 59 A 1160 GLY PHE ASN LYS SER HIS SER ALA ALA TYR ALA LEU VAL
SEQRES 60 A 1160 SER TYR GLN THR LEU TRP LEU LYS ALA HIS TYR PRO ALA
SEQRES 61 A 1160 GLU PHE MET ALA ALA VAL MET THR ALA ASP MET ASP ASN
SEQRES 62 A 1160 THR GLU LYS VAL VAL GLY LEU VAL ASP GLU CYS TRP ARG
SEQRES 63 A 1160 MET GLY LEU LYS ILE LEU PRO PRO ASP ILE ASN SER GLY
SEQRES 64 A 1160 LEU TYR HIS PHE HIS VAL ASN ASP ASP GLY GLU ILE VAL
SEQRES 65 A 1160 TYR GLY ILE GLY ALA ILE LYS GLY VAL GLY GLU GLY PRO
SEQRES 66 A 1160 ILE GLU ALA ILE ILE GLU ALA ARG ASN LYS GLY GLY TYR
SEQRES 67 A 1160 PHE ARG GLU LEU PHE ASP LEU CYS ALA ARG THR ASP THR
SEQRES 68 A 1160 LYS LYS LEU ASN ARG ARG VAL LEU GLU LYS LEU ILE MET
SEQRES 69 A 1160 SER GLY ALA PHE ASP ARG LEU GLY PRO HIS ARG ALA ALA
SEQRES 70 A 1160 LEU MET ASN SER LEU GLY ASP ALA LEU LYS ALA ALA ASP
SEQRES 71 A 1160 GLN HIS ALA LYS ALA GLU ALA ILE GLY GLN LEU ASP LEU
SEQRES 72 A 1160 PHE GLY VAL LEU ALA GLU GLU PRO GLU GLN ILE GLU GLN
SEQRES 73 A 1160 SER TYR ALA SER CYS GLN PRO TRP PRO GLU GLN VAL VAL
SEQRES 74 A 1160 LEU ASP GLY GLU ARG GLU THR LEU GLY LEU TYR LEU THR
SEQRES 75 A 1160 GLY HIS PRO ILE ASN GLN TYR LEU LYS GLU ILE GLU ARG
SEQRES 76 A 1160 TYR VAL GLY GLY VAL ARG LEU LYS ASP MET HIS PRO THR
SEQRES 77 A 1160 GLU ARG GLY LYS VAL ILE THR ALA ALA GLY LEU VAL VAL
SEQRES 78 A 1160 ALA ALA ARG VAL MET VAL THR LYS ARG GLY ASN ARG ILE
SEQRES 79 A 1160 GLY ILE CYS THR LEU ASP ASP ARG SER GLY ARG LEU GLU
SEQRES 80 A 1160 VAL MET LEU PHE THR ASP ALA LEU ASP LYS TYR GLN GLN
SEQRES 81 A 1160 LEU LEU GLU LYS ASP ARG ILE LEU ILE VAL SER GLY GLN
SEQRES 82 A 1160 VAL SER PHE ASP ASP PHE SER GLY GLY LEU LYS MET THR
SEQRES 83 A 1160 ALA ARG GLU VAL MET ASP ILE ASP GLU ALA ARG GLU LYS
SEQRES 84 A 1160 TYR ALA ARG GLY LEU ALA ILE SER LEU THR ASP ARG GLN
SEQRES 85 A 1160 ILE ASP ASP GLN LEU LEU ASN ARG LEU ARG GLN SER LEU
SEQRES 86 A 1160 GLU PRO HIS ARG SER GLY THR ILE PRO VAL HIS LEU TYR
SEQRES 87 A 1160 TYR GLN ARG ALA ASP ALA ARG ALA ARG LEU ARG PHE GLY
SEQRES 88 A 1160 ALA THR TRP ARG VAL SER PRO SER ASP ARG LEU LEU ASN
SEQRES 89 A 1160 ASP LEU ARG GLY LEU ILE GLY SER GLU GLN VAL GLU LEU
SEQRES 90 A 1160 GLU PHE ASP
SEQRES 1 B 366 MET LYS PHE THR VAL GLU ARG GLU HIS LEU LEU LYS PRO
SEQRES 2 B 366 LEU GLN GLN VAL SER GLY PRO LEU GLY GLY ARG PRO THR
SEQRES 3 B 366 LEU PRO ILE LEU GLY ASN LEU LEU LEU GLN VAL ALA ASP
SEQRES 4 B 366 GLY THR LEU SER LEU THR GLY THR ASP LEU GLU MET GLU
SEQRES 5 B 366 MET VAL ALA ARG VAL ALA LEU VAL GLN PRO HIS GLU PRO
SEQRES 6 B 366 GLY ALA THR THR VAL PRO ALA ARG LYS PHE PHE ASP ILE
SEQRES 7 B 366 CYS ARG GLY LEU PRO GLU GLY ALA GLU ILE ALA VAL GLN
SEQRES 8 B 366 LEU GLU GLY GLU ARG MET LEU VAL ARG SER GLY ARG SER
SEQRES 9 B 366 ARG PHE SER LEU SER THR LEU PRO ALA ALA ASP PHE PRO
SEQRES 10 B 366 ASN LEU ASP ASP TRP GLN SER GLU VAL GLU PHE THR LEU
SEQRES 11 B 366 PRO GLN ALA THR MET LYS ARG LEU ILE GLU ALA THR GLN
SEQRES 12 B 366 PHE SER MET ALA HIS GLN ASP VAL ARG TYR TYR LEU ASN
SEQRES 13 B 366 GLY MET LEU PHE GLU THR GLU GLY GLU GLU LEU ARG THR
SEQRES 14 B 366 VAL ALA THR ASP GLY HIS ARG LEU ALA VAL CYS SER MET
SEQRES 15 B 366 PRO ILE GLY GLN SER LEU PRO SER HIS SER VAL ILE VAL
SEQRES 16 B 366 PRO ARG LYS GLY VAL ILE GLU LEU MET ARG MET LEU ASP
SEQRES 17 B 366 GLY GLY ASP ASN PRO LEU ARG VAL GLN ILE GLY SER ASN
SEQRES 18 B 366 ASN ILE ARG ALA HIS VAL GLY ASP PHE ILE PHE THR SER
SEQRES 19 B 366 LYS LEU VAL ASP GLY ARG PHE PRO ASP TYR ARG ARG VAL
SEQRES 20 B 366 LEU PRO LYS ASN PRO ASP LYS HIS LEU GLU ALA GLY CYS
SEQRES 21 B 366 ASP LEU LEU LYS GLN ALA PHE ALA ARG ALA ALA ILE LEU
SEQRES 22 B 366 SER ASN GLU LYS PHE ARG GLY VAL ARG LEU TYR VAL SER
SEQRES 23 B 366 GLU ASN GLN LEU LYS ILE THR ALA ASN ASN PRO GLU GLN
SEQRES 24 B 366 GLU GLU ALA GLU GLU ILE LEU ASP VAL THR TYR SER GLY
SEQRES 25 B 366 ALA GLU MET GLU ILE GLY PHE ASN VAL SER TYR VAL LEU
SEQRES 26 B 366 ASP VAL LEU ASN ALA LEU LYS CYS GLU ASN VAL ARG MET
SEQRES 27 B 366 MET LEU THR ASP SER VAL SER SER VAL GLN ILE GLU ASP
SEQRES 28 B 366 ALA ALA SER GLN SER ALA ALA TYR VAL VAL MET PRO MET
SEQRES 29 B 366 ARG LEU
SEQRES 1 C 366 MET LYS PHE THR VAL GLU ARG GLU HIS LEU LEU LYS PRO
SEQRES 2 C 366 LEU GLN GLN VAL SER GLY PRO LEU GLY GLY ARG PRO THR
SEQRES 3 C 366 LEU PRO ILE LEU GLY ASN LEU LEU LEU GLN VAL ALA ASP
SEQRES 4 C 366 GLY THR LEU SER LEU THR GLY THR ASP LEU GLU MET GLU
SEQRES 5 C 366 MET VAL ALA ARG VAL ALA LEU VAL GLN PRO HIS GLU PRO
SEQRES 6 C 366 GLY ALA THR THR VAL PRO ALA ARG LYS PHE PHE ASP ILE
SEQRES 7 C 366 CYS ARG GLY LEU PRO GLU GLY ALA GLU ILE ALA VAL GLN
SEQRES 8 C 366 LEU GLU GLY GLU ARG MET LEU VAL ARG SER GLY ARG SER
SEQRES 9 C 366 ARG PHE SER LEU SER THR LEU PRO ALA ALA ASP PHE PRO
SEQRES 10 C 366 ASN LEU ASP ASP TRP GLN SER GLU VAL GLU PHE THR LEU
SEQRES 11 C 366 PRO GLN ALA THR MET LYS ARG LEU ILE GLU ALA THR GLN
SEQRES 12 C 366 PHE SER MET ALA HIS GLN ASP VAL ARG TYR TYR LEU ASN
SEQRES 13 C 366 GLY MET LEU PHE GLU THR GLU GLY GLU GLU LEU ARG THR
SEQRES 14 C 366 VAL ALA THR ASP GLY HIS ARG LEU ALA VAL CYS SER MET
SEQRES 15 C 366 PRO ILE GLY GLN SER LEU PRO SER HIS SER VAL ILE VAL
SEQRES 16 C 366 PRO ARG LYS GLY VAL ILE GLU LEU MET ARG MET LEU ASP
SEQRES 17 C 366 GLY GLY ASP ASN PRO LEU ARG VAL GLN ILE GLY SER ASN
SEQRES 18 C 366 ASN ILE ARG ALA HIS VAL GLY ASP PHE ILE PHE THR SER
SEQRES 19 C 366 LYS LEU VAL ASP GLY ARG PHE PRO ASP TYR ARG ARG VAL
SEQRES 20 C 366 LEU PRO LYS ASN PRO ASP LYS HIS LEU GLU ALA GLY CYS
SEQRES 21 C 366 ASP LEU LEU LYS GLN ALA PHE ALA ARG ALA ALA ILE LEU
SEQRES 22 C 366 SER ASN GLU LYS PHE ARG GLY VAL ARG LEU TYR VAL SER
SEQRES 23 C 366 GLU ASN GLN LEU LYS ILE THR ALA ASN ASN PRO GLU GLN
SEQRES 24 C 366 GLU GLU ALA GLU GLU ILE LEU ASP VAL THR TYR SER GLY
SEQRES 25 C 366 ALA GLU MET GLU ILE GLY PHE ASN VAL SER TYR VAL LEU
SEQRES 26 C 366 ASP VAL LEU ASN ALA LEU LYS CYS GLU ASN VAL ARG MET
SEQRES 27 C 366 MET LEU THR ASP SER VAL SER SER VAL GLN ILE GLU ASP
SEQRES 28 C 366 ALA ALA SER GLN SER ALA ALA TYR VAL VAL MET PRO MET
SEQRES 29 C 366 ARG LEU
SEQRES 1 D 243 MET SER THR ALA ILE THR ARG GLN ILE VAL LEU ASP THR
SEQRES 2 D 243 GLU THR THR GLY MET ASN GLN ILE GLY ALA HIS TYR GLU
SEQRES 3 D 243 GLY HIS LYS ILE ILE GLU ILE GLY ALA VAL GLU VAL VAL
SEQRES 4 D 243 ASN ARG ARG LEU THR GLY ASN ASN PHE HIS VAL TYR LEU
SEQRES 5 D 243 LYS PRO ASP ARG LEU VAL ASP PRO GLU ALA PHE GLY VAL
SEQRES 6 D 243 HIS GLY ILE ALA ASP GLU PHE LEU LEU ASP LYS PRO THR
SEQRES 7 D 243 PHE ALA GLU VAL ALA ASP GLU PHE MET ASP TYR ILE ARG
SEQRES 8 D 243 GLY ALA GLU LEU VAL ILE HIS ASN ALA ALA PHE ASP ILE
SEQRES 9 D 243 GLY PHE MET ASP TYR GLU PHE SER LEU LEU LYS ARG ASP
SEQRES 10 D 243 ILE PRO LYS THR ASN THR PHE CYS LYS VAL THR ASP SER
SEQRES 11 D 243 LEU ALA VAL ALA ARG LYS MET PHE PRO GLY LYS ARG ASN
SEQRES 12 D 243 SER LEU ASP ALA LEU CYS ALA ARG TYR GLU ILE ASP ASN
SEQRES 13 D 243 SER LYS ARG THR LEU HIS GLY ALA LEU LEU ASP ALA GLN
SEQRES 14 D 243 ILE LEU ALA GLU VAL TYR LEU ALA MET THR GLY GLY GLN
SEQRES 15 D 243 LEU SER LEU PRO LEU ALA MET GLU GLY GLU THR GLN GLN
SEQRES 16 D 243 GLN GLN GLY GLU ALA THR ILE GLN ARG ILE VAL ARG GLN
SEQRES 17 D 243 ALA SER LYS LEU ARG VAL VAL PHE ALA THR ASP GLU GLU
SEQRES 18 D 243 ILE ALA ALA HIS GLU ALA ARG LEU ASP LEU VAL GLN LYS
SEQRES 19 D 243 LYS GLY GLY SER CYS LEU TRP ARG ALA
SEQRES 1 P 25 DG DG DA DG DT DA DG DT DA DC DT DA DG
SEQRES 2 P 25 DG DA DC DG DA DA DG DG DA DC DT DC
SEQRES 1 T 29 DT DC DA DG DG DA DG DT DC DC DT DT DC
SEQRES 2 T 29 DG DT DC DC DT DA DG DT DA DC DT DA DC
SEQRES 3 T 29 DT DC DC
HELIX 1 1 SER A 13 MET A 17 5 5
HELIX 2 2 LYS A 23 LEU A 34 1 12
HELIX 3 3 GLY A 49 GLY A 61 1 13
HELIX 4 4 ASN A 90 GLY A 108 1 19
HELIX 5 5 ASP A 119 LEU A 124 1 6
HELIX 6 6 GLY A 133 MET A 136 5 4
HELIX 7 7 GLY A 137 GLY A 146 1 10
HELIX 8 8 ASN A 147 PHE A 162 1 16
HELIX 9 9 ASP A 177 GLY A 193 1 17
HELIX 10 10 ASP A 206 SER A 208 5 3
HELIX 11 11 ASP A 209 GLY A 222 1 14
HELIX 12 12 SER A 242 PHE A 250 1 9
HELIX 13 13 ILE A 253 CYS A 267 1 15
HELIX 14 14 SER A 287 PHE A 308 1 22
HELIX 15 15 ASP A 310 ARG A 318 1 9
HELIX 16 16 ARG A 318 GLY A 336 1 19
HELIX 17 17 PHE A 337 ASN A 354 1 18
HELIX 18 18 SER A 364 GLY A 367 5 4
HELIX 19 19 SER A 368 LEU A 374 1 7
HELIX 20 20 LEU A 387 PHE A 391 5 5
HELIX 21 21 CYS A 407 GLU A 409 5 3
HELIX 22 22 LYS A 410 GLY A 423 1 14
HELIX 23 23 ALA A 437 LEU A 449 1 13
HELIX 24 24 PRO A 452 LYS A 461 1 10
HELIX 25 25 THR A 470 GLU A 478 1 9
HELIX 26 26 PRO A 479 ASP A 488 1 10
HELIX 27 27 ASP A 488 GLU A 502 1 15
HELIX 28 28 LYS A 521 PHE A 525 5 5
HELIX 29 29 LYS A 543 ALA A 549 1 7
HELIX 30 30 THR A 561 ASN A 579 1 19
HELIX 31 31 ASP A 585 ILE A 589 5 5
HELIX 32 32 ASP A 593 ARG A 602 1 10
HELIX 33 33 SER A 613 GLN A 624 1 12
HELIX 34 34 CYS A 627 PHE A 638 1 12
HELIX 35 35 ARG A 639 GLN A 644 1 6
HELIX 36 36 GLY A 646 HIS A 656 1 11
HELIX 37 37 HIS A 670 SER A 672 5 3
HELIX 38 38 LEU A 673 GLU A 678 1 6
HELIX 39 39 PRO A 679 TYR A 681 5 3
HELIX 40 40 TYR A 686 LEU A 697 1 12
HELIX 41 41 THR A 701 LYS A 715 1 15
HELIX 42 42 LYS A 716 ASN A 734 1 19
HELIX 43 43 ASN A 737 GLY A 753 1 17
HELIX 44 44 ASN A 757 HIS A 777 1 21
HELIX 45 45 GLU A 781 ASP A 790 1 10
HELIX 46 46 ASN A 793 GLY A 808 1 16
HELIX 47 47 GLY A 842 GLY A 856 1 15
HELIX 48 48 GLU A 861 THR A 869 1 9
HELIX 49 49 ASN A 875 GLY A 886 1 12
HELIX 50 50 ALA A 896 ILE A 918 1 23
HELIX 51 51 ARG B 7 SER B 18 1 12
HELIX 52 52 LEU B 27 LEU B 30 5 4
HELIX 53 53 ALA B 72 LEU B 82 1 11
HELIX 54 54 PRO B 112 PHE B 116 5 5
HELIX 55 55 GLN B 132 ALA B 141 1 10
HELIX 56 56 THR B 142 MET B 146 5 5
HELIX 57 57 ARG B 152 LEU B 155 5 4
HELIX 58 58 ARG B 197 LEU B 207 1 11
HELIX 59 59 ASP B 243 LEU B 248 1 6
HELIX 60 60 CYS B 260 ILE B 272 1 13
HELIX 61 61 VAL B 321 LEU B 331 1 11
HELIX 62 62 ARG C 7 GLY C 19 1 13
HELIX 63 63 LEU C 27 LEU C 30 5 4
HELIX 64 64 ALA C 72 GLY C 81 1 10
HELIX 65 65 PRO C 112 PHE C 116 5 5
HELIX 66 66 GLN C 132 ALA C 141 1 10
HELIX 67 67 THR C 142 MET C 146 5 5
HELIX 68 68 ARG C 197 LEU C 207 1 11
HELIX 69 69 ASP C 243 LEU C 248 1 6
HELIX 70 70 CYS C 260 LEU C 273 1 14
HELIX 71 71 VAL C 321 LEU C 331 1 11
HELIX 72 72 ASP D 59 GLY D 67 1 9
HELIX 73 73 ALA D 69 LEU D 73 5 5
HELIX 74 74 VAL D 82 ARG D 91 1 10
HELIX 75 75 ASN D 99 LYS D 115 1 17
HELIX 76 76 LYS D 120 PHE D 124 5 5
HELIX 77 77 SER D 130 PHE D 138 1 9
HELIX 78 78 SER D 144 TYR D 152 1 9
HELIX 79 79 GLY D 163 THR D 179 1 17
HELIX 80 80 THR D 218 GLY D 237 1 20
HELIX 81 81 CYS D 239 ALA D 243 5 5
SHEET 1 AA 2 ALA A 38 ILE A 41 0
SHEET 2 AA 2 LYS A 63 GLN A 73 1 O LYS A 63 N LEU A 39
SHEET 1 AB 2 ILE A 116 ASP A 117 0
SHEET 2 AB 2 LYS A 63 GLN A 73 -1 O ASN A 71 N ILE A 116
SHEET 1 AC 6 VAL A 196 ALA A 198 0
SHEET 2 AC 6 TYR A 166 LEU A 170 1 O LEU A 168 N VAL A 197
SHEET 3 AC 6 LEU A 128 LEU A 131 1 O LEU A 130 N PHE A 167
SHEET 4 AC 6 THR A 82 ALA A 88 -1 O THR A 85 N LEU A 131
SHEET 5 AC 6 LYS A 63 GLN A 73 -1 O VAL A 66 N ALA A 88
SHEET 6 AC 6 ILE A 116 ASP A 117 -1 O ILE A 116 N GLN A 73
SHEET 1 AD 6 VAL A 196 ALA A 198 0
SHEET 2 AD 6 TYR A 166 LEU A 170 1 O LEU A 168 N VAL A 197
SHEET 3 AD 6 LEU A 128 LEU A 131 1 O LEU A 130 N PHE A 167
SHEET 4 AD 6 THR A 82 ALA A 88 -1 O THR A 85 N LEU A 131
SHEET 5 AD 6 LYS A 63 GLN A 73 -1 O VAL A 66 N ALA A 88
SHEET 6 AD 6 ALA A 38 ILE A 41 1 O LEU A 39 N ILE A 65
SHEET 1 AE 6 ASP A 405 PHE A 406 0
SHEET 2 AE 6 VAL A 552 PHE A 556 1 O ASP A 555 N PHE A 406
SHEET 3 AE 6 GLY A 514 ILE A 517 -1 O VAL A 515 N PHE A 554
SHEET 4 AE 6 VAL A 427 ILE A 431 -1 O SER A 428 N VAL A 516
SHEET 5 AE 6 VAL A 538 ASP A 542 1 O THR A 539 N ILE A 431
SHEET 6 AE 6 LEU A 528 TYR A 529 -1 O TYR A 529 N VAL A 538
SHEET 1 AF 2 GLY A 434 THR A 435 0
SHEET 2 AF 2 THR A 505 ASN A 507 -1 N ARG A 506 O GLY A 434
SHEET 1 BA 8 LYS B 2 GLU B 6 0
SHEET 2 BA 8 GLU B 87 GLU B 93 -1 O ILE B 88 N VAL B 5
SHEET 3 BA 8 ARG B 96 SER B 101 -1 O ARG B 96 N GLU B 93
SHEET 4 BA 8 SER B 104 SER B 109 -1 O SER B 104 N SER B 101
SHEET 5 BA 8 GLU C 301 ASP C 307 -1 O GLU C 301 N SER B 107
SHEET 6 BA 8 GLN C 289 ASN C 295 -1 O LEU C 290 N LEU C 306
SHEET 7 BA 8 GLY C 280 SER C 286 -1 O GLY C 280 N ASN C 295
SHEET 8 BA 8 MET C 315 ASN C 320 -1 O MET C 315 N VAL C 285
SHEET 1 BB 8 GLY B 66 PRO B 71 0
SHEET 2 BB 8 ASN B 32 ALA B 38 -1 O LEU B 33 N VAL B 70
SHEET 3 BB 8 THR B 41 THR B 47 -1 O THR B 41 N ALA B 38
SHEET 4 BB 8 MET B 51 ALA B 58 -1 O MET B 53 N GLY B 46
SHEET 5 BB 8 PHE B 230 LYS B 235 -1 O ILE B 231 N VAL B 54
SHEET 6 BB 8 ASN B 222 VAL B 227 -1 O ILE B 223 N SER B 234
SHEET 7 BB 8 PRO B 213 GLY B 219 -1 O ARG B 215 N HIS B 226
SHEET 8 BB 8 SER B 124 PRO B 131 -1 N GLU B 125 O ILE B 218
SHEET 1 BC 3 GLY B 157 THR B 172 0
SHEET 2 BC 3 ARG B 176 PRO B 196 -1 O ALA B 178 N ALA B 171
SHEET 3 BC 3 ALA B 357 VAL B 361 -1 O ALA B 358 N VAL B 179
SHEET 1 BD 4 THR B 309 SER B 311 0
SHEET 2 BD 4 LYS B 254 GLY B 259 -1 O HIS B 255 N SER B 311
SHEET 3 BD 4 ASN B 335 LEU B 340 -1 O VAL B 336 N ALA B 258
SHEET 4 BD 4 GLN B 348 ASP B 351 -1 O GLN B 348 N MET B 339
SHEET 1 BE 8 MET B 315 ASN B 320 0
SHEET 2 BE 8 GLY B 280 SER B 286 -1 O VAL B 281 N PHE B 319
SHEET 3 BE 8 GLN B 289 ALA B 294 -1 O GLN B 289 N SER B 286
SHEET 4 BE 8 GLU B 301 ASP B 307 -1 O ALA B 302 N ALA B 294
SHEET 5 BE 8 SER C 104 SER C 109 -1 O ARG C 105 N GLU B 303
SHEET 6 BE 8 ARG C 96 SER C 101 -1 O MET C 97 N LEU C 108
SHEET 7 BE 8 GLU C 87 GLU C 93 -1 O ALA C 89 N ARG C 100
SHEET 8 BE 8 LYS C 2 GLU C 6 -1 O PHE C 3 N VAL C 90
SHEET 1 CA 8 GLY C 66 PRO C 71 0
SHEET 2 CA 8 ASN C 32 ALA C 38 -1 O LEU C 33 N VAL C 70
SHEET 3 CA 8 THR C 41 THR C 47 -1 O THR C 41 N ALA C 38
SHEET 4 CA 8 MET C 51 ALA C 58 -1 O MET C 53 N GLY C 46
SHEET 5 CA 8 PHE C 230 LYS C 235 -1 O ILE C 231 N VAL C 54
SHEET 6 CA 8 ASN C 222 VAL C 227 -1 O ILE C 223 N SER C 234
SHEET 7 CA 8 PRO C 213 ILE C 218 -1 O ARG C 215 N HIS C 226
SHEET 8 CA 8 VAL C 126 PRO C 131 -1 O VAL C 126 N ILE C 218
SHEET 1 CB 9 HIS C 191 PRO C 196 0
SHEET 2 CB 9 GLY C 157 GLU C 163 -1 O MET C 158 N VAL C 195
SHEET 3 CB 9 GLU C 166 THR C 172 -1 O GLU C 166 N GLU C 163
SHEET 4 CB 9 ARG C 176 PRO C 183 -1 O ALA C 178 N ALA C 171
SHEET 5 CB 9 ALA C 357 VAL C 361 -1 O ALA C 358 N VAL C 179
SHEET 6 CB 9 VAL C 347 ASP C 351 -1 O VAL C 347 N VAL C 361
SHEET 7 CB 9 ASN C 335 LEU C 340 -1 O ARG C 337 N GLU C 350
SHEET 8 CB 9 LYS C 254 GLY C 259 -1 O LYS C 254 N LEU C 340
SHEET 9 CB 9 THR C 309 SER C 311 -1 O THR C 309 N GLU C 257
SHEET 1 DA 2 GLN D 8 THR D 15 0
SHEET 2 DA 2 ILE D 30 VAL D 39 -1 N ILE D 31 O GLU D 14
SHEET 1 DB 2 ARG D 42 LEU D 43 0
SHEET 2 DB 2 ILE D 30 VAL D 39 1 O VAL D 39 N ARG D 42
SHEET 1 DC 2 PHE D 48 TYR D 51 0
SHEET 2 DC 2 ILE D 30 VAL D 39 -1 O ILE D 33 N VAL D 50
SHEET 1 DD 2 GLU D 94 ILE D 97 0
SHEET 2 DD 2 LYS D 126 ASP D 129 1 O LYS D 126 N LEU D 95
CISPEP 1 TYR A 663 PRO A 664 0 5.19
CISPEP 2 LYS A 810 ILE A 811 0 -26.45
CISPEP 3 ILE A 918 GLY A 919 0 -27.84
CISPEP 4 GLY A 919 GLN A 920 0 -1.34
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END