HEADER HYDROLASE 17-MAR-16 5G06
TITLE CRYO-EM STRUCTURE OF YEAST CYTOPLASMIC EXOSOME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXOSOME COMPLEX COMPONENT RRP45;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 45;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: EXOSOME COMPLEX COMPONENT SKI6;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: EXTRACELLULAR MUTANT PROTEIN 20, RIBOSOMAL RNA-PROCESSING
COMPND 9 PROTEIN 41, SUPERKILLER PROTEIN 6;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: EXOSOME COMPLEX COMPONENT RRP43;
COMPND 12 CHAIN: C;
COMPND 13 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 43;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: EXOSOME COMPLEX COMPONENT RRP46;
COMPND 16 CHAIN: D;
COMPND 17 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 46;
COMPND 18 MOL_ID: 5;
COMPND 19 MOLECULE: EXOSOME COMPLEX COMPONENT RRP42;
COMPND 20 CHAIN: E;
COMPND 21 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 42;
COMPND 22 MOL_ID: 6;
COMPND 23 MOLECULE: EXOSOME COMPLEX COMPONENT MTR3;
COMPND 24 CHAIN: F;
COMPND 25 SYNONYM: MRNA TRANSPORT REGULATOR 3;
COMPND 26 MOL_ID: 7;
COMPND 27 MOLECULE: EXOSOME COMPLEX COMPONENT RRP40;
COMPND 28 CHAIN: G;
COMPND 29 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 40;
COMPND 30 MOL_ID: 8;
COMPND 31 MOLECULE: EXOSOME COMPLEX COMPONENT RRP4;
COMPND 32 CHAIN: H;
COMPND 33 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 4;
COMPND 34 MOL_ID: 9;
COMPND 35 MOLECULE: EXOSOME COMPLEX COMPONENT CSL4;
COMPND 36 CHAIN: I;
COMPND 37 SYNONYM: CEP1 SYNTHETIC LETHAL PROTEIN 4;
COMPND 38 MOL_ID: 10;
COMPND 39 MOLECULE: EXOSOME COMPLEX EXONUCLEASE DIS3;
COMPND 40 CHAIN: J;
COMPND 41 SYNONYM: CHROMOSOME DISJUNCTION PROTEIN 3, RIBOSOMAL RNA-PROCESSING
COMPND 42 PROTEIN 44;
COMPND 43 EC: 3.1.13.1;
COMPND 44 MOL_ID: 11;
COMPND 45 MOLECULE: SUPERKILLER PROTEIN 7;
COMPND 46 CHAIN: P;
COMPND 47 FRAGMENT: N TERMINAL FRAGMENT;
COMPND 48 SYNONYM: CYTOPLASMIC EXOSOME COMPONENT SKI7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 8 ORGANISM_TAXID: 4932;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 4932;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 15 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 16 ORGANISM_TAXID: 4932;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 4932;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 27 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 28 ORGANISM_TAXID: 4932;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 31 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 32 ORGANISM_TAXID: 4932;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 35 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 36 ORGANISM_TAXID: 4932;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 39 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 40 ORGANISM_TAXID: 4932;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 4932
KEYWDS HYDROLASE, RNA DECAY, EXOSOME, RNA QUALITY CONTROL
EXPDTA ELECTRON MICROSCOPY
AUTHOR J.J.LIU,C.Y.NIU,Y.WU,D.TAN,Y.WANG,M.D.YE,Y.LIU,W.W.ZHAO,K.ZHOU,
AUTHOR 2 Q.S.LIU,J.B.DAI,X.R.YANG,M.Q.DONG,N.HUANG,H.W.WANG
REVDAT 4 02-AUG-17 5G06 1
REVDAT 3 19-APR-17 5G06 1 REMARK
REVDAT 2 13-JUL-16 5G06 1 JRNL MASTER
REVDAT 1 15-JUN-16 5G06 0
JRNL AUTH J.LIU,C.NIU,Y.WU,D.TAN,Y.WANG,M.YE,Y.LIU,W.ZHAO,K.ZHOU,
JRNL AUTH 2 Q.LIU,J.DAI,X.YANG,M.DONG,N.HUANG,H.WANG
JRNL TITL CRYOEM STRUCTURE OF YEAST CYTOPLASMIC EXOSOME COMPLEX.
JRNL REF CELL RES. V. 26 822 2016
JRNL REFN ISSN 1001-0602
JRNL PMID 27174052
JRNL DOI 10.1038/CR.2016.56
REMARK 2
REMARK 2 RESOLUTION. 4.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : EMAN, IMAGIC, RELION
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) : 1.320
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.200
REMARK 3 NUMBER OF PARTICLES : 25000
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD
REMARK 3 -3366. (DEPOSITION ID: 14342).
REMARK 4
REMARK 4 5G06 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_1290066514.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : CRYO EM
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : RNA-FREE EXO10-SKI7
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00
REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : 150MM NACL, 50MM TRIS-HCL, 1MM
REMARK 245 EGTA,1MMDTT
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 20-OCT-14
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3500.00
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) : 21.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 22500
REMARK 245 CALIBRATED MAGNIFICATION : NULL
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: UNDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: P
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 MET A 1
REMARK 465 GLU A 304
REMARK 465 ILE A 305
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ALA B 243
REMARK 465 SER B 244
REMARK 465 ALA B 245
REMARK 465 ARG B 246
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 SER C 4
REMARK 465 THR C 5
REMARK 465 THR C 6
REMARK 465 THR C 99
REMARK 465 SER C 100
REMARK 465 ALA C 101
REMARK 465 ALA C 102
REMARK 465 ILE C 103
REMARK 465 LYS C 104
REMARK 465 ASP C 105
REMARK 465 LEU C 106
REMARK 465 ASP C 107
REMARK 465 ASP C 108
REMARK 465 PHE C 109
REMARK 465 GLY C 110
REMARK 465 GLU C 111
REMARK 465 GLU C 112
REMARK 465 GLU C 113
REMARK 465 LEU C 114
REMARK 465 PHE C 115
REMARK 465 GLU C 116
REMARK 465 VAL C 117
REMARK 465 THR C 118
REMARK 465 LYS C 119
REMARK 465 GLU C 120
REMARK 465 LEU C 193
REMARK 465 GLU C 194
REMARK 465 ASP C 195
REMARK 465 ASP C 196
REMARK 465 THR C 197
REMARK 465 LEU C 198
REMARK 465 ASN C 199
REMARK 465 GLU C 200
REMARK 465 THR C 201
REMARK 465 ASN C 202
REMARK 465 LEU C 203
REMARK 465 LYS C 204
REMARK 465 MET C 205
REMARK 465 GLN C 309
REMARK 465 ASN C 310
REMARK 465 SER C 311
REMARK 465 ASP C 312
REMARK 465 ASN C 313
REMARK 465 SER C 314
REMARK 465 GLU C 315
REMARK 465 GLU C 316
REMARK 465 GLU C 317
REMARK 465 GLU C 318
REMARK 465 VAL C 319
REMARK 465 ASP C 320
REMARK 465 ILE C 321
REMARK 465 ASP C 322
REMARK 465 MET C 323
REMARK 465 ASP C 324
REMARK 465 LYS C 325
REMARK 465 LEU C 326
REMARK 465 MET F 1
REMARK 465 ASN F 2
REMARK 465 VAL F 3
REMARK 465 ASN F 22
REMARK 465 THR F 23
REMARK 465 THR F 24
REMARK 465 THR F 25
REMARK 465 HIS F 26
REMARK 465 VAL F 27
REMARK 465 PRO F 28
REMARK 465 GLU F 29
REMARK 465 LYS F 30
REMARK 465 LYS F 31
REMARK 465 SER F 32
REMARK 465 THR F 33
REMARK 465 ASP F 34
REMARK 465 LEU F 35
REMARK 465 THR F 36
REMARK 465 PRO F 37
REMARK 465 LYS F 38
REMARK 465 GLY F 39
REMARK 465 ASN F 40
REMARK 465 GLU F 41
REMARK 465 ASN F 149
REMARK 465 ASN F 150
REMARK 465 PRO F 151
REMARK 465 GLN F 152
REMARK 465 ASP F 153
REMARK 465 ASP F 154
REMARK 465 ASP F 155
REMARK 465 SER F 156
REMARK 465 GLN F 157
REMARK 465 SER F 158
REMARK 465 LYS F 159
REMARK 465 MET F 160
REMARK 465 MET F 161
REMARK 465 SER F 162
REMARK 465 GLU F 249
REMARK 465 THR F 250
REMARK 465 VAL G 237
REMARK 465 LYS G 238
REMARK 465 GLU G 239
REMARK 465 GLU G 240
REMARK 465 MET H 1
REMARK 465 SER H 17
REMARK 465 SER H 18
REMARK 465 ASN H 19
REMARK 465 LEU H 20
REMARK 465 SER H 21
REMARK 465 TYR H 22
REMARK 465 ASN H 23
REMARK 465 ASN H 24
REMARK 465 THR H 25
REMARK 465 GLY H 26
REMARK 465 ILE H 27
REMARK 465 SER H 28
REMARK 465 ASP H 29
REMARK 465 ASP H 30
REMARK 465 GLU H 31
REMARK 465 ASN H 32
REMARK 465 ASP H 33
REMARK 465 GLU H 34
REMARK 465 GLU H 35
REMARK 465 ASP H 36
REMARK 465 ILE H 37
REMARK 465 TYR H 38
REMARK 465 MET H 39
REMARK 465 HIS H 40
REMARK 465 ASP H 41
REMARK 465 VAL H 42
REMARK 465 ASN H 43
REMARK 465 SER H 44
REMARK 465 ALA H 45
REMARK 465 SER H 46
REMARK 465 LYS H 47
REMARK 465 SER H 48
REMARK 465 GLU H 49
REMARK 465 THR H 245
REMARK 465 PRO H 246
REMARK 465 SER H 247
REMARK 465 ALA H 248
REMARK 465 ASN H 249
REMARK 465 ASN H 250
REMARK 465 SER H 251
REMARK 465 SER H 252
REMARK 465 SER H 253
REMARK 465 ILE H 254
REMARK 465 LYS H 255
REMARK 465 SER H 256
REMARK 465 THR H 257
REMARK 465 GLY H 258
REMARK 465 PRO H 259
REMARK 465 THR H 260
REMARK 465 GLY H 261
REMARK 465 ALA H 262
REMARK 465 VAL H 263
REMARK 465 SER H 264
REMARK 465 LEU H 265
REMARK 465 ASN H 266
REMARK 465 PRO H 267
REMARK 465 SER H 268
REMARK 465 ILE H 269
REMARK 465 THR H 270
REMARK 465 ARG H 271
REMARK 465 LEU H 272
REMARK 465 GLU H 273
REMARK 465 GLU H 274
REMARK 465 GLY H 358
REMARK 465 ASN H 359
REMARK 465 LYS I 71
REMARK 465 THR I 72
REMARK 465 ASP I 73
REMARK 465 GLN I 74
REMARK 465 GLU I 75
REMARK 465 GLU I 76
REMARK 465 GLU I 77
REMARK 465 ARG I 78
REMARK 465 GLU I 79
REMARK 465 GLY I 80
REMARK 465 THR I 81
REMARK 465 ASP I 82
REMARK 465 GLN I 83
REMARK 465 SER I 84
REMARK 465 THR I 85
REMARK 465 GLU I 86
REMARK 465 GLU I 87
REMARK 465 GLU I 88
REMARK 465 LYS I 89
REMARK 465 SER I 90
REMARK 465 VAL I 91
REMARK 465 ASP I 92
REMARK 465 ALA I 93
REMARK 465 SER I 94
REMARK 465 PRO I 95
REMARK 465 ASN I 96
REMARK 465 ASP I 97
REMARK 465 VAL I 98
REMARK 465 GLY I 113
REMARK 465 THR I 114
REMARK 465 GLU I 115
REMARK 465 LYS I 116
REMARK 465 GLY I 117
REMARK 465 ARG I 118
REMARK 465 LYS I 119
REMARK 465 THR I 120
REMARK 465 ASN I 121
REMARK 465 LYS I 122
REMARK 465 TYR I 123
REMARK 465 ALA I 124
REMARK 465 ASN I 125
REMARK 465 PRO I 162
REMARK 465 SER I 163
REMARK 465 PRO I 164
REMARK 465 ILE I 165
REMARK 465 ASP I 166
REMARK 465 SER I 167
REMARK 465 GLY I 168
REMARK 465 ILE I 169
REMARK 465 GLY I 170
REMARK 465 SER I 171
REMARK 465 ASN I 172
REMARK 465 GLY I 173
REMARK 465 SER I 174
REMARK 465 GLY I 175
REMARK 465 ILE I 176
REMARK 465 VAL I 177
REMARK 465 ALA I 178
REMARK 465 ALA I 179
REMARK 465 GLY I 180
REMARK 465 GLY I 181
REMARK 465 GLY I 182
REMARK 465 SER I 183
REMARK 465 GLY I 184
REMARK 465 PHE I 292
REMARK 465 MET J 1
REMARK 465 SER J 2
REMARK 465 VAL J 3
REMARK 465 PRO J 4
REMARK 465 ALA J 5
REMARK 465 ILE J 6
REMARK 465 ALA J 7
REMARK 465 PRO J 8
REMARK 465 MET P -144
REMARK 465 SER P -143
REMARK 465 LEU P -142
REMARK 465 LEU P -141
REMARK 465 GLU P -140
REMARK 465 GLN P -139
REMARK 465 LEU P -138
REMARK 465 ALA P -137
REMARK 465 ARG P -136
REMARK 465 LYS P -135
REMARK 465 ARG P -134
REMARK 465 ILE P -133
REMARK 465 GLU P -132
REMARK 465 LYS P -131
REMARK 465 SER P -130
REMARK 465 LYS P -129
REMARK 465 GLY P -128
REMARK 465 LEU P -127
REMARK 465 LEU P -126
REMARK 465 SER P -125
REMARK 465 ALA P -124
REMARK 465 ASP P -123
REMARK 465 GLN P -122
REMARK 465 SER P -121
REMARK 465 HIS P -120
REMARK 465 SER P -119
REMARK 465 THR P -118
REMARK 465 SER P -117
REMARK 465 LYS P -116
REMARK 465 SER P -115
REMARK 465 ALA P -114
REMARK 465 SER P -113
REMARK 465 LEU P -112
REMARK 465 LEU P -111
REMARK 465 GLU P -110
REMARK 465 ARG P -109
REMARK 465 LEU P -108
REMARK 465 HIS P -107
REMARK 465 LYS P -106
REMARK 465 ASN P -105
REMARK 465 ARG P -104
REMARK 465 GLU P -103
REMARK 465 THR P -102
REMARK 465 LYS P -101
REMARK 465 ASP P -100
REMARK 465 ASN P -99
REMARK 465 ASN P -98
REMARK 465 ALA P -97
REMARK 465 GLU P -96
REMARK 465 THR P -95
REMARK 465 LYS P -94
REMARK 465 ARG P -93
REMARK 465 LYS P -92
REMARK 465 ASP P -91
REMARK 465 LEU P -90
REMARK 465 LYS P -89
REMARK 465 THR P -88
REMARK 465 LEU P -87
REMARK 465 LEU P -86
REMARK 465 ALA P -85
REMARK 465 LYS P -84
REMARK 465 ASP P -83
REMARK 465 LYS P -82
REMARK 465 VAL P -81
REMARK 465 LYS P -80
REMARK 465 ARG P -79
REMARK 465 SER P -78
REMARK 465 ASP P -77
REMARK 465 PHE P -76
REMARK 465 THR P -75
REMARK 465 PRO P -74
REMARK 465 ASN P -73
REMARK 465 GLN P -72
REMARK 465 HIS P -71
REMARK 465 SER P -70
REMARK 465 VAL P -69
REMARK 465 SER P -68
REMARK 465 LEU P -67
REMARK 465 SER P -66
REMARK 465 LEU P -65
REMARK 465 LYS P -64
REMARK 465 LEU P -63
REMARK 465 SER P -62
REMARK 465 ALA P -61
REMARK 465 LEU P -60
REMARK 465 LYS P -59
REMARK 465 LYS P -58
REMARK 465 SER P -57
REMARK 465 ASN P -56
REMARK 465 SER P -55
REMARK 465 ASP P -54
REMARK 465 LEU P -53
REMARK 465 GLU P -52
REMARK 465 LYS P -51
REMARK 465 GLN P -50
REMARK 465 GLY P -49
REMARK 465 LYS P -48
REMARK 465 SER P -47
REMARK 465 VAL P -46
REMARK 465 THR P -45
REMARK 465 LEU P -44
REMARK 465 ASP P -43
REMARK 465 SER P -42
REMARK 465 LYS P -41
REMARK 465 GLU P -40
REMARK 465 ASN P -39
REMARK 465 GLU P -38
REMARK 465 LEU P -37
REMARK 465 PRO P -36
REMARK 465 THR P -35
REMARK 465 LYS P -34
REMARK 465 ARG P -33
REMARK 465 LYS P -32
REMARK 465 SER P -31
REMARK 465 PRO P -30
REMARK 465 ASP P -29
REMARK 465 ASP P -28
REMARK 465 LYS P -27
REMARK 465 LEU P -26
REMARK 465 ASN P -25
REMARK 465 LEU P -24
REMARK 465 GLU P -23
REMARK 465 GLU P -22
REMARK 465 SER P -21
REMARK 465 TRP P -20
REMARK 465 LYS P -19
REMARK 465 ALA P -18
REMARK 465 ILE P -17
REMARK 465 LYS P -16
REMARK 465 GLU P -15
REMARK 465 MET P -14
REMARK 465 ASN P -13
REMARK 465 HIS P -12
REMARK 465 TYR P -11
REMARK 465 CYS P -10
REMARK 465 PHE P -9
REMARK 465 LEU P -8
REMARK 465 LYS P -7
REMARK 465 ASN P -6
REMARK 465 ASP P -5
REMARK 465 PRO P -4
REMARK 465 CYS P -3
REMARK 465 ILE P -2
REMARK 465 ASN P -1
REMARK 465 GLN P 0
REMARK 465 LYS P 96
REMARK 465 LYS P 97
REMARK 465 GLU P 98
REMARK 465 PRO P 99
REMARK 465 ILE P 100
REMARK 465 ASN P 101
REMARK 465 LEU P 102
REMARK 465 GLN P 103
REMARK 465 THR P 104
REMARK 465 PRO P 105
REMARK 465 PRO P 106
REMARK 465 THR P 107
REMARK 465 GLU P 108
REMARK 465 SER P 109
REMARK 465 ILE P 110
REMARK 465 ASP P 111
REMARK 465 ILE P 112
REMARK 465 HIS P 113
REMARK 465 SER P 114
REMARK 465 PHE P 115
REMARK 465 ILE P 116
REMARK 465 ALA P 117
REMARK 465 THR P 118
REMARK 465 HIS P 119
REMARK 465 PRO P 120
REMARK 465 LEU P 121
REMARK 465 ASN P 122
REMARK 465 LEU P 123
REMARK 465 THR P 124
REMARK 465 CYS P 125
REMARK 465 LEU P 126
REMARK 465 PHE P 127
REMARK 465 LEU P 128
REMARK 465 GLY P 129
REMARK 465 ASP P 130
REMARK 465 THR P 131
REMARK 465 ASN P 132
REMARK 465 ALA P 133
REMARK 465 GLY P 134
REMARK 465 LYS P 135
REMARK 465 SER P 136
REMARK 465 THR P 137
REMARK 465 LEU P 138
REMARK 465 LEU P 139
REMARK 465 GLY P 140
REMARK 465 HIS P 141
REMARK 465 LEU P 142
REMARK 465 LEU P 143
REMARK 465 TYR P 144
REMARK 465 ASP P 145
REMARK 465 LEU P 146
REMARK 465 ASN P 147
REMARK 465 GLU P 148
REMARK 465 ILE P 149
REMARK 465 SER P 150
REMARK 465 MET P 151
REMARK 465 SER P 152
REMARK 465 SER P 153
REMARK 465 MET P 154
REMARK 465 ARG P 155
REMARK 465 GLU P 156
REMARK 465 LEU P 157
REMARK 465 GLN P 158
REMARK 465 LYS P 159
REMARK 465 LYS P 160
REMARK 465 SER P 161
REMARK 465 SER P 162
REMARK 465 ASN P 163
REMARK 465 LEU P 164
REMARK 465 ASP P 165
REMARK 465 PRO P 166
REMARK 465 SER P 167
REMARK 465 SER P 168
REMARK 465 SER P 169
REMARK 465 ASN P 170
REMARK 465 SER P 171
REMARK 465 PHE P 172
REMARK 465 LYS P 173
REMARK 465 VAL P 174
REMARK 465 ILE P 175
REMARK 465 LEU P 176
REMARK 465 ASP P 177
REMARK 465 ASN P 178
REMARK 465 THR P 179
REMARK 465 LYS P 180
REMARK 465 THR P 181
REMARK 465 GLU P 182
REMARK 465 ARG P 183
REMARK 465 GLU P 184
REMARK 465 ASN P 185
REMARK 465 GLY P 186
REMARK 465 PHE P 187
REMARK 465 SER P 188
REMARK 465 MET P 189
REMARK 465 PHE P 190
REMARK 465 LYS P 191
REMARK 465 LYS P 192
REMARK 465 VAL P 193
REMARK 465 ILE P 194
REMARK 465 GLN P 195
REMARK 465 VAL P 196
REMARK 465 GLU P 197
REMARK 465 ASN P 198
REMARK 465 ASP P 199
REMARK 465 LEU P 200
REMARK 465 LEU P 201
REMARK 465 PRO P 202
REMARK 465 PRO P 203
REMARK 465 SER P 204
REMARK 465 SER P 205
REMARK 465 THR P 206
REMARK 465 LEU P 207
REMARK 465 THR P 208
REMARK 465 LEU P 209
REMARK 465 ILE P 210
REMARK 465 ASP P 211
REMARK 465 THR P 212
REMARK 465 PRO P 213
REMARK 465 GLY P 214
REMARK 465 SER P 215
REMARK 465 ILE P 216
REMARK 465 LYS P 217
REMARK 465 TYR P 218
REMARK 465 PHE P 219
REMARK 465 ASN P 220
REMARK 465 LYS P 221
REMARK 465 GLU P 222
REMARK 465 THR P 223
REMARK 465 LEU P 224
REMARK 465 ASN P 225
REMARK 465 SER P 226
REMARK 465 ILE P 227
REMARK 465 LEU P 228
REMARK 465 THR P 229
REMARK 465 PHE P 230
REMARK 465 ASP P 231
REMARK 465 PRO P 232
REMARK 465 GLU P 233
REMARK 465 VAL P 234
REMARK 465 TYR P 235
REMARK 465 VAL P 236
REMARK 465 LEU P 237
REMARK 465 VAL P 238
REMARK 465 ILE P 239
REMARK 465 ASP P 240
REMARK 465 CYS P 241
REMARK 465 ASN P 242
REMARK 465 TYR P 243
REMARK 465 ASP P 244
REMARK 465 SER P 245
REMARK 465 TRP P 246
REMARK 465 GLU P 247
REMARK 465 LYS P 248
REMARK 465 SER P 249
REMARK 465 LEU P 250
REMARK 465 ASP P 251
REMARK 465 GLY P 252
REMARK 465 PRO P 253
REMARK 465 ASN P 254
REMARK 465 ASN P 255
REMARK 465 GLN P 256
REMARK 465 ILE P 257
REMARK 465 TYR P 258
REMARK 465 GLU P 259
REMARK 465 ILE P 260
REMARK 465 LEU P 261
REMARK 465 LYS P 262
REMARK 465 VAL P 263
REMARK 465 ILE P 264
REMARK 465 SER P 265
REMARK 465 TYR P 266
REMARK 465 LEU P 267
REMARK 465 ASN P 268
REMARK 465 LYS P 269
REMARK 465 ASN P 270
REMARK 465 SER P 271
REMARK 465 ALA P 272
REMARK 465 CYS P 273
REMARK 465 LYS P 274
REMARK 465 LYS P 275
REMARK 465 HIS P 276
REMARK 465 LEU P 277
REMARK 465 ILE P 278
REMARK 465 ILE P 279
REMARK 465 LEU P 280
REMARK 465 LEU P 281
REMARK 465 ASN P 282
REMARK 465 LYS P 283
REMARK 465 ALA P 284
REMARK 465 ASP P 285
REMARK 465 LEU P 286
REMARK 465 ILE P 287
REMARK 465 SER P 288
REMARK 465 TRP P 289
REMARK 465 ASP P 290
REMARK 465 LYS P 291
REMARK 465 HIS P 292
REMARK 465 ARG P 293
REMARK 465 LEU P 294
REMARK 465 GLU P 295
REMARK 465 MET P 296
REMARK 465 ILE P 297
REMARK 465 GLN P 298
REMARK 465 SER P 299
REMARK 465 GLU P 300
REMARK 465 LEU P 301
REMARK 465 ASN P 302
REMARK 465 TYR P 303
REMARK 465 VAL P 304
REMARK 465 LEU P 305
REMARK 465 LYS P 306
REMARK 465 GLU P 307
REMARK 465 ASN P 308
REMARK 465 PHE P 309
REMARK 465 GLN P 310
REMARK 465 TRP P 311
REMARK 465 THR P 312
REMARK 465 ASP P 313
REMARK 465 ALA P 314
REMARK 465 GLU P 315
REMARK 465 PHE P 316
REMARK 465 GLN P 317
REMARK 465 PHE P 318
REMARK 465 ILE P 319
REMARK 465 PRO P 320
REMARK 465 CYS P 321
REMARK 465 SER P 322
REMARK 465 GLY P 323
REMARK 465 LEU P 324
REMARK 465 LEU P 325
REMARK 465 GLY P 326
REMARK 465 SER P 327
REMARK 465 ASN P 328
REMARK 465 LEU P 329
REMARK 465 ASN P 330
REMARK 465 LYS P 331
REMARK 465 THR P 332
REMARK 465 GLU P 333
REMARK 465 ASN P 334
REMARK 465 ILE P 335
REMARK 465 THR P 336
REMARK 465 LYS P 337
REMARK 465 SER P 338
REMARK 465 LYS P 339
REMARK 465 TYR P 340
REMARK 465 LYS P 341
REMARK 465 SER P 342
REMARK 465 GLU P 343
REMARK 465 PHE P 344
REMARK 465 ASP P 345
REMARK 465 SER P 346
REMARK 465 ILE P 347
REMARK 465 ASN P 348
REMARK 465 TYR P 349
REMARK 465 VAL P 350
REMARK 465 PRO P 351
REMARK 465 GLU P 352
REMARK 465 TRP P 353
REMARK 465 TYR P 354
REMARK 465 GLU P 355
REMARK 465 GLY P 356
REMARK 465 PRO P 357
REMARK 465 THR P 358
REMARK 465 PHE P 359
REMARK 465 PHE P 360
REMARK 465 SER P 361
REMARK 465 GLN P 362
REMARK 465 LEU P 363
REMARK 465 TYR P 364
REMARK 465 LEU P 365
REMARK 465 LEU P 366
REMARK 465 VAL P 367
REMARK 465 GLU P 368
REMARK 465 HIS P 369
REMARK 465 ASN P 370
REMARK 465 MET P 371
REMARK 465 ASN P 372
REMARK 465 LYS P 373
REMARK 465 ILE P 374
REMARK 465 GLU P 375
REMARK 465 THR P 376
REMARK 465 THR P 377
REMARK 465 LEU P 378
REMARK 465 GLU P 379
REMARK 465 GLU P 380
REMARK 465 PRO P 381
REMARK 465 PHE P 382
REMARK 465 VAL P 383
REMARK 465 GLY P 384
REMARK 465 THR P 385
REMARK 465 ILE P 386
REMARK 465 LEU P 387
REMARK 465 GLN P 388
REMARK 465 SER P 389
REMARK 465 SER P 390
REMARK 465 VAL P 391
REMARK 465 LEU P 392
REMARK 465 GLN P 393
REMARK 465 PRO P 394
REMARK 465 ILE P 395
REMARK 465 ALA P 396
REMARK 465 GLU P 397
REMARK 465 ILE P 398
REMARK 465 ASN P 399
REMARK 465 TYR P 400
REMARK 465 VAL P 401
REMARK 465 SER P 402
REMARK 465 LEU P 403
REMARK 465 LYS P 404
REMARK 465 VAL P 405
REMARK 465 LEU P 406
REMARK 465 ILE P 407
REMARK 465 ASN P 408
REMARK 465 SER P 409
REMARK 465 GLY P 410
REMARK 465 TYR P 411
REMARK 465 ILE P 412
REMARK 465 GLN P 413
REMARK 465 SER P 414
REMARK 465 GLY P 415
REMARK 465 GLN P 416
REMARK 465 THR P 417
REMARK 465 ILE P 418
REMARK 465 GLU P 419
REMARK 465 ILE P 420
REMARK 465 HIS P 421
REMARK 465 THR P 422
REMARK 465 GLN P 423
REMARK 465 TYR P 424
REMARK 465 GLU P 425
REMARK 465 ASP P 426
REMARK 465 PHE P 427
REMARK 465 HIS P 428
REMARK 465 TYR P 429
REMARK 465 TYR P 430
REMARK 465 GLY P 431
REMARK 465 ILE P 432
REMARK 465 VAL P 433
REMARK 465 SER P 434
REMARK 465 ARG P 435
REMARK 465 MET P 436
REMARK 465 LYS P 437
REMARK 465 ASN P 438
REMARK 465 SER P 439
REMARK 465 LYS P 440
REMARK 465 GLN P 441
REMARK 465 ILE P 442
REMARK 465 LEU P 443
REMARK 465 GLU P 444
REMARK 465 THR P 445
REMARK 465 ASN P 446
REMARK 465 THR P 447
REMARK 465 LYS P 448
REMARK 465 ASN P 449
REMARK 465 ASN P 450
REMARK 465 ILE P 451
REMARK 465 SER P 452
REMARK 465 VAL P 453
REMARK 465 GLY P 454
REMARK 465 LEU P 455
REMARK 465 ASN P 456
REMARK 465 PRO P 457
REMARK 465 ASP P 458
REMARK 465 ILE P 459
REMARK 465 LEU P 460
REMARK 465 GLU P 461
REMARK 465 VAL P 462
REMARK 465 LEU P 463
REMARK 465 VAL P 464
REMARK 465 LYS P 465
REMARK 465 ILE P 466
REMARK 465 HIS P 467
REMARK 465 ASN P 468
REMARK 465 THR P 469
REMARK 465 GLU P 470
REMARK 465 ASP P 471
REMARK 465 PHE P 472
REMARK 465 THR P 473
REMARK 465 LYS P 474
REMARK 465 LYS P 475
REMARK 465 GLN P 476
REMARK 465 PHE P 477
REMARK 465 HIS P 478
REMARK 465 ILE P 479
REMARK 465 ARG P 480
REMARK 465 LYS P 481
REMARK 465 GLY P 482
REMARK 465 ASP P 483
REMARK 465 ILE P 484
REMARK 465 ILE P 485
REMARK 465 ILE P 486
REMARK 465 HIS P 487
REMARK 465 SER P 488
REMARK 465 ARG P 489
REMARK 465 LYS P 490
REMARK 465 THR P 491
REMARK 465 ASN P 492
REMARK 465 THR P 493
REMARK 465 LEU P 494
REMARK 465 SER P 495
REMARK 465 PRO P 496
REMARK 465 ASN P 497
REMARK 465 LEU P 498
REMARK 465 PRO P 499
REMARK 465 ASN P 500
REMARK 465 THR P 501
REMARK 465 LEU P 502
REMARK 465 LYS P 503
REMARK 465 LEU P 504
REMARK 465 LEU P 505
REMARK 465 ALA P 506
REMARK 465 LEU P 507
REMARK 465 ARG P 508
REMARK 465 LEU P 509
REMARK 465 ILE P 510
REMARK 465 LYS P 511
REMARK 465 LEU P 512
REMARK 465 SER P 513
REMARK 465 ILE P 514
REMARK 465 GLN P 515
REMARK 465 THR P 516
REMARK 465 HIS P 517
REMARK 465 ALA P 518
REMARK 465 LEU P 519
REMARK 465 SER P 520
REMARK 465 ASP P 521
REMARK 465 PRO P 522
REMARK 465 VAL P 523
REMARK 465 ASP P 524
REMARK 465 LEU P 525
REMARK 465 GLY P 526
REMARK 465 SER P 527
REMARK 465 GLU P 528
REMARK 465 LEU P 529
REMARK 465 LEU P 530
REMARK 465 LEU P 531
REMARK 465 TYR P 532
REMARK 465 HIS P 533
REMARK 465 ASN P 534
REMARK 465 LEU P 535
REMARK 465 THR P 536
REMARK 465 HIS P 537
REMARK 465 ASN P 538
REMARK 465 ALA P 539
REMARK 465 VAL P 540
REMARK 465 LYS P 541
REMARK 465 LEU P 542
REMARK 465 VAL P 543
REMARK 465 LYS P 544
REMARK 465 ILE P 545
REMARK 465 LEU P 546
REMARK 465 GLY P 547
REMARK 465 THR P 548
REMARK 465 ASN P 549
REMARK 465 ASP P 550
REMARK 465 ILE P 551
REMARK 465 SER P 552
REMARK 465 ILE P 553
REMARK 465 ASN P 554
REMARK 465 PRO P 555
REMARK 465 ASN P 556
REMARK 465 GLN P 557
REMARK 465 SER P 558
REMARK 465 LEU P 559
REMARK 465 ILE P 560
REMARK 465 VAL P 561
REMARK 465 GLU P 562
REMARK 465 VAL P 563
REMARK 465 GLU P 564
REMARK 465 ILE P 565
REMARK 465 ILE P 566
REMARK 465 GLU P 567
REMARK 465 PRO P 568
REMARK 465 ASP P 569
REMARK 465 PHE P 570
REMARK 465 ALA P 571
REMARK 465 LEU P 572
REMARK 465 ASN P 573
REMARK 465 VAL P 574
REMARK 465 ILE P 575
REMARK 465 ASP P 576
REMARK 465 SER P 577
REMARK 465 LYS P 578
REMARK 465 TYR P 579
REMARK 465 ILE P 580
REMARK 465 THR P 581
REMARK 465 ASN P 582
REMARK 465 ASN P 583
REMARK 465 ILE P 584
REMARK 465 VAL P 585
REMARK 465 LEU P 586
REMARK 465 THR P 587
REMARK 465 SER P 588
REMARK 465 ILE P 589
REMARK 465 ASP P 590
REMARK 465 HIS P 591
REMARK 465 LYS P 592
REMARK 465 VAL P 593
REMARK 465 ILE P 594
REMARK 465 ALA P 595
REMARK 465 VAL P 596
REMARK 465 GLY P 597
REMARK 465 ARG P 598
REMARK 465 ILE P 599
REMARK 465 ALA P 600
REMARK 465 CYS P 601
REMARK 465 GLN P 602
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 OE2 GLU C 48 CB ASN P 49 1.19
REMARK 500 CD2 TRP I 272 NZ LYS P 82 1.32
REMARK 500 CD GLU C 48 CB ASN P 49 1.41
REMARK 500 CD LYS C 81 CD LYS P 35 1.48
REMARK 500 N LEU I 16 NZ LYS P 15 1.54
REMARK 500 CG GLU C 48 CB ASN P 49 1.62
REMARK 500 OD1 ASN I 250 CD1 LEU P 86 1.71
REMARK 500 CE2 TRP I 272 NZ LYS P 82 1.73
REMARK 500 OE2 GLU C 48 CA ASN P 49 1.78
REMARK 500 OE2 GLU C 48 C ASN P 49 1.78
REMARK 500 CG TRP I 272 NZ LYS P 82 1.84
REMARK 500 OD2 ASP F 239 O LEU P 18 1.94
REMARK 500 CG GLU C 48 CG ASN P 49 2.01
REMARK 500 CG TRP I 272 CE LYS P 82 2.05
REMARK 500 NE2 HIS F 49 CD LYS P 36 2.12
REMARK 500 CE3 TRP I 272 NZ LYS P 82 2.14
REMARK 500 CG ASN I 250 CD1 LEU P 86 2.17
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 ARG A 24 CD ARG A 24 NE 0.123
REMARK 500 ARG A 34 CZ ARG A 34 NH2 0.103
REMARK 500 ARG A 114 CD ARG A 114 NE 0.113
REMARK 500 ARG A 135 NE ARG A 135 CZ 0.085
REMARK 500 HIS A 161 CE1 HIS A 161 NE2 -0.071
REMARK 500 GLU A 267 CD GLU A 267 OE1 0.070
REMARK 500 ARG B 3 CD ARG B 3 NE 0.115
REMARK 500 ARG B 13 CZ ARG B 13 NH2 0.080
REMARK 500 GLU B 21 CD GLU B 21 OE2 0.079
REMARK 500 PHE B 108 CG PHE B 108 CD1 0.091
REMARK 500 GLY B 188 CA GLY B 188 C -0.110
REMARK 500 ARG B 223 CZ ARG B 223 NH2 0.080
REMARK 500 ARG C 50 NE ARG C 50 CZ 0.095
REMARK 500 ARG C 222 CZ ARG C 222 NH1 0.089
REMARK 500 GLY C 298 CA GLY C 298 C -0.120
REMARK 500 GLU C 301 CD GLU C 301 OE2 0.072
REMARK 500 SER C 381 CA SER C 381 CB 0.101
REMARK 500 ARG C 384 NE ARG C 384 CZ 0.088
REMARK 500 TYR E 120 CD1 TYR E 120 CE1 0.114
REMARK 500 PHE E 143 CB PHE E 143 CG 0.135
REMARK 500 TYR E 175 CB TYR E 175 CG -0.096
REMARK 500 ARG E 227 NE ARG E 227 CZ 0.079
REMARK 500 GLU F 109 CD GLU F 109 OE1 0.070
REMARK 500 ARG F 129 CD ARG F 129 NE 0.116
REMARK 500 ARG F 229 CZ ARG F 229 NH2 0.078
REMARK 500 TYR F 234 CG TYR F 234 CD2 0.082
REMARK 500 ARG F 238 CZ ARG F 238 NH2 0.078
REMARK 500 TYR G 99 CG TYR G 99 CD1 0.100
REMARK 500 ARG G 110 CZ ARG G 110 NH2 0.128
REMARK 500 ARG G 122 CZ ARG G 122 NH2 0.083
REMARK 500 ARG G 143 CD ARG G 143 NE 0.109
REMARK 500 TRP G 195 CB TRP G 195 CG 0.133
REMARK 500 PHE G 231 CG PHE G 231 CD1 0.095
REMARK 500 ARG H 10 CZ ARG H 10 NH1 0.091
REMARK 500 GLY H 58 CA GLY H 58 C -0.101
REMARK 500 TYR H 74 CZ TYR H 74 OH 0.145
REMARK 500 SER H 96 CA SER H 96 CB 0.118
REMARK 500 ARG H 150 CZ ARG H 150 NH1 0.085
REMARK 500 ARG H 195 CD ARG H 195 NE 0.110
REMARK 500 TYR H 281 CG TYR H 281 CD2 0.100
REMARK 500 ARG H 318 NE ARG H 318 CZ 0.081
REMARK 500 TYR H 323 CZ TYR H 323 OH 0.107
REMARK 500 CYS I 18 CA CYS I 18 CB 0.145
REMARK 500 GLU I 69 CG GLU I 69 CD 0.091
REMARK 500 GLU I 69 CD GLU I 69 OE2 0.067
REMARK 500 ARG I 202 NE ARG I 202 CZ 0.085
REMARK 500 SER I 212 CA SER I 212 CB 0.103
REMARK 500 GLU I 222 CD GLU I 222 OE1 0.068
REMARK 500 ARG I 249 NE ARG I 249 CZ 0.097
REMARK 500 ARG I 258 CD ARG I 258 NE 0.113
REMARK 500
REMARK 500 THIS ENTRY HAS 84 BOND DEVIATIONS.
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 20 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 TYR A 23 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 TYR A 23 CG - CD1 - CE1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 24 NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 PHE A 30 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 46 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 CYS A 58 CB - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 CYS A 62 N - CA - CB ANGL. DEV. = 10.3 DEGREES
REMARK 500 TYR A 68 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 MET A 86 CG - SD - CE ANGL. DEV. = -10.3 DEGREES
REMARK 500 PHE A 91 CB - CG - CD1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 GLY A 116 N - CA - C ANGL. DEV. = -15.2 DEGREES
REMARK 500 ASP A 119 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ALA A 136 N - CA - CB ANGL. DEV. = 8.8 DEGREES
REMARK 500 PHE A 140 CB - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 PHE A 140 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 PHE A 147 CB - CG - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 PHE A 162 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 PHE A 198 CB - CG - CD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 232 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 243 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG A 243 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 MET A 262 CG - SD - CE ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP A 277 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP A 277 CB - CG - OD2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 ARG A 303 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 3 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TYR B 7 CB - CG - CD2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 TYR B 7 CB - CG - CD1 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ARG B 17 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 18 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 TYR B 41 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 PHE B 81 CB - CG - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 PHE B 81 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 95 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 106 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG B 106 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU B 139 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 ARG B 209 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP B 226 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ILE C 12 C - N - CA ANGL. DEV. = 16.1 DEGREES
REMARK 500 ARG C 24 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 PRO C 27 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG C 33 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 33 NE - CZ - NH2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 LEU C 43 C - N - CA ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG C 44 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG C 44 NE - CZ - NH2 ANGL. DEV. = -7.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 350 ANGLE DEVIATIONS.
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 ASN A 22 37.81 79.47
REMARK 500 MET A 86 7.99 -153.36
REMARK 500 SER A 89 7.24 -151.90
REMARK 500 ILE A 96 -18.42 -153.51
REMARK 500 THR A 97 -65.92 -146.34
REMARK 500 ALA A 117 -0.62 -168.20
REMARK 500 SER A 129 -58.52 -148.74
REMARK 500 ASP A 144 46.53 -147.33
REMARK 500 GLN A 204 -140.79 -99.27
REMARK 500 GLU A 213 -3.65 -151.08
REMARK 500 SER A 216 1.89 -159.98
REMARK 500 ASN A 242 5.27 -165.01
REMARK 500 ALA A 251 79.31 174.86
REMARK 500 LEU A 297 31.59 -98.38
REMARK 500 LEU B 4 154.12 67.39
REMARK 500 ASN B 30 79.29 62.67
REMARK 500 HIS B 32 65.94 -156.71
REMARK 500 ALA B 35 8.09 -171.12
REMARK 500 LYS B 92 30.90 -87.35
REMARK 500 ASN B 93 37.33 -166.22
REMARK 500 ARG B 119 61.10 37.05
REMARK 500 ASP B 132 29.14 -153.19
REMARK 500 TYR B 166 66.25 -108.64
REMARK 500 ASP B 167 -78.48 84.59
REMARK 500 ASP B 173 158.34 78.83
REMARK 500 LYS B 204 109.55 -59.09
REMARK 500 GLU C 8 -31.57 88.09
REMARK 500 ILE C 10 166.90 84.47
REMARK 500 GLU C 11 -103.88 164.64
REMARK 500 ILE C 12 8.51 -16.99
REMARK 500 PRO C 18 152.75 -47.63
REMARK 500 SER C 26 103.41 -167.13
REMARK 500 PHE C 49 -156.73 -135.45
REMARK 500 LEU C 59 -15.56 -140.74
REMARK 500 ASN C 73 0.32 -171.90
REMARK 500 ASP C 122 12.09 -158.58
REMARK 500 TYR C 131 66.25 -114.26
REMARK 500 ALA C 143 48.04 179.04
REMARK 500 CYS C 144 46.07 -164.98
REMARK 500 ARG C 163 35.06 78.63
REMARK 500 ASP C 191 5.73 172.26
REMARK 500 SER C 221 60.57 60.32
REMARK 500 PRO C 244 160.59 -49.12
REMARK 500 THR C 258 15.86 -145.23
REMARK 500 ARG C 264 40.69 75.06
REMARK 500 SER C 265 169.03 60.69
REMARK 500 ASP C 333 159.50 81.32
REMARK 500 PRO C 353 63.38 -109.29
REMARK 500 SER C 354 10.04 -154.20
REMARK 500 GLN C 359 134.10 172.18
REMARK 500
REMARK 500 THIS ENTRY HAS 174 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 PRO D 36 LYS D 37 149.83
REMARK 500 ASP F 222 LEU F 223 -149.25
REMARK 500 LEU J 72 SER J 73 -146.80
REMARK 500 SER J 633 ALA J 634 149.81
REMARK 500 GLU J 865 PRO J 866 147.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE A 44 0.09 SIDE CHAIN
REMARK 500 TYR A 269 0.10 SIDE CHAIN
REMARK 500 ARG A 303 0.09 SIDE CHAIN
REMARK 500 ARG B 3 0.08 SIDE CHAIN
REMARK 500 ARG B 23 0.09 SIDE CHAIN
REMARK 500 TYR B 41 0.10 SIDE CHAIN
REMARK 500 ARG B 96 0.12 SIDE CHAIN
REMARK 500 ARG B 106 0.10 SIDE CHAIN
REMARK 500 PHE B 155 0.08 SIDE CHAIN
REMARK 500 ARG B 225 0.11 SIDE CHAIN
REMARK 500 ARG C 40 0.09 SIDE CHAIN
REMARK 500 ARG C 44 0.07 SIDE CHAIN
REMARK 500 TYR C 46 0.07 SIDE CHAIN
REMARK 500 TYR C 127 0.07 SIDE CHAIN
REMARK 500 TYR C 131 0.08 SIDE CHAIN
REMARK 500 ARG C 222 0.09 SIDE CHAIN
REMARK 500 TYR C 236 0.09 SIDE CHAIN
REMARK 500 ARG C 256 0.08 SIDE CHAIN
REMARK 500 ARG C 269 0.14 SIDE CHAIN
REMARK 500 ARG C 382 0.08 SIDE CHAIN
REMARK 500 ARG D 71 0.08 SIDE CHAIN
REMARK 500 TYR E 12 0.10 SIDE CHAIN
REMARK 500 ARG E 22 0.08 SIDE CHAIN
REMARK 500 PHE E 40 0.10 SIDE CHAIN
REMARK 500 TYR E 175 0.10 SIDE CHAIN
REMARK 500 PHE F 20 0.08 SIDE CHAIN
REMARK 500 ARG F 84 0.11 SIDE CHAIN
REMARK 500 PHE F 138 0.08 SIDE CHAIN
REMARK 500 TYR F 140 0.07 SIDE CHAIN
REMARK 500 TYR G 26 0.08 SIDE CHAIN
REMARK 500 ARG G 35 0.09 SIDE CHAIN
REMARK 500 TYR G 59 0.08 SIDE CHAIN
REMARK 500 TYR G 120 0.07 SIDE CHAIN
REMARK 500 ARG G 143 0.10 SIDE CHAIN
REMARK 500 PHE G 147 0.08 SIDE CHAIN
REMARK 500 PHE G 231 0.08 SIDE CHAIN
REMARK 500 ARG H 10 0.09 SIDE CHAIN
REMARK 500 HIS H 71 0.09 SIDE CHAIN
REMARK 500 TYR H 104 0.08 SIDE CHAIN
REMARK 500 ARG H 209 0.12 SIDE CHAIN
REMARK 500 ARG H 294 0.11 SIDE CHAIN
REMARK 500 TYR I 21 0.13 SIDE CHAIN
REMARK 500 TYR I 46 0.09 SIDE CHAIN
REMARK 500 ARG I 51 0.09 SIDE CHAIN
REMARK 500 ARG I 215 0.08 SIDE CHAIN
REMARK 500 ARG I 217 0.10 SIDE CHAIN
REMARK 500 TYR I 244 0.09 SIDE CHAIN
REMARK 500 ARG J 12 0.11 SIDE CHAIN
REMARK 500 ARG J 26 0.12 SIDE CHAIN
REMARK 500 ARG J 37 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 71 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "GC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "HE" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "IC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "JE" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "JF" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "JG" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-3366 RELATED DB: EMDB
DBREF 5G06 A 1 305 UNP Q05636 RRP45_YEAST 1 305
DBREF 5G06 B 1 246 UNP P46948 RRP41_YEAST 1 246
DBREF 5G06 C 1 394 UNP P25359 RRP43_YEAST 1 394
DBREF 5G06 D 1 223 UNP P53256 RRP46_YEAST 1 223
DBREF 5G06 E 1 265 UNP Q12277 RRP42_YEAST 1 265
DBREF 5G06 F 1 250 UNP P48240 MTR3_YEAST 1 250
DBREF 5G06 G 1 240 UNP Q08285 RRP40_YEAST 1 240
DBREF 5G06 H 1 359 UNP P38792 RRP4_YEAST 1 359
DBREF 5G06 I 1 292 UNP P53859 CSL4_YEAST 1 292
DBREF 5G06 J 1 1001 UNP Q08162 RRP44_YEAST 1 1001
DBREF 5G06 P -144 602 UNP Q08491 SKI7_YEAST 1 747
SEQADV 5G06 MET C 363 UNP P25359 VAL 363 CONFLICT
SEQADV 5G06 ILE E 138 UNP Q12277 VAL 138 CONFLICT
SEQADV 5G06 SER F 75 UNP P48240 THR 75 CONFLICT
SEQADV 5G06 ASN J 171 UNP Q08162 ASP 171 CONFLICT
SEQADV 5G06 ASN J 551 UNP Q08162 ASP 551 CONFLICT
SEQRES 1 A 305 MET ALA LYS ASP ILE GLU ILE SER ALA SER GLU SER LYS
SEQRES 2 A 305 PHE ILE LEU GLU ALA LEU ARG GLN ASN TYR ARG LEU ASP
SEQRES 3 A 305 GLY ARG SER PHE ASP GLN PHE ARG ASP VAL GLU ILE THR
SEQRES 4 A 305 PHE GLY LYS GLU PHE GLY ASP VAL SER VAL LYS MET GLY
SEQRES 5 A 305 ASN THR LYS VAL HIS CYS ARG ILE SER CYS GLN ILE ALA
SEQRES 6 A 305 GLN PRO TYR GLU ASP ARG PRO PHE GLU GLY LEU PHE VAL
SEQRES 7 A 305 ILE SER THR GLU ILE SER PRO MET ALA GLY SER GLN PHE
SEQRES 8 A 305 GLU ASN GLY ASN ILE THR GLY GLU ASP GLU VAL LEU CYS
SEQRES 9 A 305 SER ARG ILE ILE GLU LYS SER VAL ARG ARG SER GLY ALA
SEQRES 10 A 305 LEU ASP VAL GLU GLY LEU CYS ILE VAL ALA GLY SER LYS
SEQRES 11 A 305 CYS TRP ALA VAL ARG ALA ASP VAL HIS PHE LEU ASP CYS
SEQRES 12 A 305 ASP GLY GLY PHE ILE ASP ALA SER CYS ILE ALA VAL MET
SEQRES 13 A 305 ALA GLY LEU MET HIS PHE LYS LYS PRO ASP ILE THR VAL
SEQRES 14 A 305 HIS GLY GLU GLN ILE ILE VAL HIS PRO VAL ASN GLU ARG
SEQRES 15 A 305 GLU PRO VAL PRO LEU GLY ILE LEU HIS ILE PRO ILE CYS
SEQRES 16 A 305 VAL THR PHE SER PHE PHE ASN PRO GLN ASP THR GLU GLU
SEQRES 17 A 305 ASN ILE LYS GLY GLU THR ASN SER GLU ILE SER ILE ILE
SEQRES 18 A 305 ASP ALA THR LEU LYS GLU GLU LEU LEU ARG ASP GLY VAL
SEQRES 19 A 305 LEU THR VAL THR LEU ASN LYS ASN ARG GLU VAL VAL GLN
SEQRES 20 A 305 VAL SER LYS ALA GLY GLY LEU PRO MET ASP ALA LEU THR
SEQRES 21 A 305 LEU MET LYS CYS CYS HIS GLU ALA TYR SER ILE ILE GLU
SEQRES 22 A 305 LYS ILE THR ASP GLN ILE LEU GLN LEU LEU LYS GLU ASP
SEQRES 23 A 305 SER GLU LYS ARG ASN LYS TYR ALA ALA MET LEU THR SER
SEQRES 24 A 305 GLU ASN ALA ARG GLU ILE
SEQRES 1 B 246 MET SER ARG LEU GLU ILE TYR SER PRO GLU GLY LEU ARG
SEQRES 2 B 246 LEU ASP GLY ARG ARG TRP ASN GLU LEU ARG ARG PHE GLU
SEQRES 3 B 246 SER SER ILE ASN THR HIS PRO HIS ALA ALA ASP GLY SER
SEQRES 4 B 246 SER TYR MET GLU GLN GLY ASN ASN LYS ILE ILE THR LEU
SEQRES 5 B 246 VAL LYS GLY PRO LYS GLU PRO ARG LEU LYS SER GLN MET
SEQRES 6 B 246 ASP THR SER LYS ALA LEU LEU ASN VAL SER VAL ASN ILE
SEQRES 7 B 246 THR LYS PHE SER LYS PHE GLU ARG SER LYS SER SER HIS
SEQRES 8 B 246 LYS ASN GLU ARG ARG VAL LEU GLU ILE GLN THR SER LEU
SEQRES 9 B 246 VAL ARG MET PHE GLU LYS ASN VAL MET LEU ASN ILE TYR
SEQRES 10 B 246 PRO ARG THR VAL ILE ASP ILE GLU ILE HIS VAL LEU GLU
SEQRES 11 B 246 GLN ASP GLY GLY ILE MET GLY SER LEU ILE ASN GLY ILE
SEQRES 12 B 246 THR LEU ALA LEU ILE ASP ALA GLY ILE SER MET PHE ASP
SEQRES 13 B 246 TYR ILE SER GLY ILE SER VAL GLY LEU TYR ASP THR THR
SEQRES 14 B 246 PRO LEU LEU ASP THR ASN SER LEU GLU GLU ASN ALA MET
SEQRES 15 B 246 SER THR VAL THR LEU GLY VAL VAL GLY LYS SER GLU LYS
SEQRES 16 B 246 LEU SER LEU LEU LEU VAL GLU ASP LYS ILE PRO LEU ASP
SEQRES 17 B 246 ARG LEU GLU ASN VAL LEU ALA ILE GLY ILE ALA GLY ALA
SEQRES 18 B 246 HIS ARG VAL ARG ASP LEU MET ASP GLU GLU LEU ARG LYS
SEQRES 19 B 246 HIS ALA GLN LYS ARG VAL SER ASN ALA SER ALA ARG
SEQRES 1 C 394 MET ALA GLU SER THR THR LEU GLU THR ILE GLU ILE HIS
SEQRES 2 C 394 PRO ILE THR PHE PRO PRO GLU VAL LEU ALA ARG ILE SER
SEQRES 3 C 394 PRO GLU LEU SER LEU GLN ARG HIS LEU SER LEU GLY ILE
SEQRES 4 C 394 ARG PRO CYS LEU ARG LYS TYR GLU GLU PHE ARG ASP VAL
SEQRES 5 C 394 ALA ILE GLU ASN ASN THR LEU SER ARG TYR ALA ASP ALA
SEQRES 6 C 394 GLY ASN ILE ASP THR LYS ASN ASN ILE LEU GLY SER ASN
SEQRES 7 C 394 VAL LEU LYS SER GLY LYS THR ILE VAL ILE THR SER ILE
SEQRES 8 C 394 THR GLY GLY ILE ILE GLU GLU THR SER ALA ALA ILE LYS
SEQRES 9 C 394 ASP LEU ASP ASP PHE GLY GLU GLU GLU LEU PHE GLU VAL
SEQRES 10 C 394 THR LYS GLU GLU ASP ILE ILE ALA ASN TYR ALA SER VAL
SEQRES 11 C 394 TYR PRO VAL VAL GLU VAL GLU ARG GLY ARG VAL GLY ALA
SEQRES 12 C 394 CYS THR ASP GLU GLU MET THR ILE SER GLN LYS LEU HIS
SEQRES 13 C 394 ASP SER ILE LEU HIS SER ARG ILE LEU PRO LYS LYS ALA
SEQRES 14 C 394 LEU LYS VAL LYS ALA GLY VAL ARG SER ALA ASN GLU ASP
SEQRES 15 C 394 GLY THR PHE SER VAL LEU TYR PRO ASP GLU LEU GLU ASP
SEQRES 16 C 394 ASP THR LEU ASN GLU THR ASN LEU LYS MET LYS ARG LYS
SEQRES 17 C 394 TRP SER TYR VAL LEU TYR ALA LYS ILE VAL VAL LEU SER
SEQRES 18 C 394 ARG THR GLY PRO VAL PHE ASP LEU CYS TRP ASN SER LEU
SEQRES 19 C 394 MET TYR ALA LEU GLN SER VAL LYS LEU PRO ARG ALA PHE
SEQRES 20 C 394 ILE ASP GLU ARG ALA SER ASP LEU ARG MET THR ILE ARG
SEQRES 21 C 394 THR ARG GLY ARG SER ALA THR ILE ARG GLU THR TYR GLU
SEQRES 22 C 394 ILE ILE CYS ASP GLN THR LYS SER VAL PRO LEU MET ILE
SEQRES 23 C 394 ASN ALA LYS ASN ILE ALA PHE ALA SER ASN TYR GLY ILE
SEQRES 24 C 394 VAL GLU LEU ASP PRO GLU CYS GLN LEU GLN ASN SER ASP
SEQRES 25 C 394 ASN SER GLU GLU GLU GLU VAL ASP ILE ASP MET ASP LYS
SEQRES 26 C 394 LEU ASN THR VAL LEU ILE ALA ASP LEU ASP THR GLU ALA
SEQRES 27 C 394 GLU GLU THR SER ILE HIS SER THR ILE SER ILE LEU ALA
SEQRES 28 C 394 ALA PRO SER GLY ASN TYR LYS GLN LEU THR LEU MET GLY
SEQRES 29 C 394 GLY GLY ALA LYS ILE THR PRO GLU MET ILE LYS ARG SER
SEQRES 30 C 394 LEU LEU LEU SER ARG VAL ARG ALA ASP ASP LEU SER THR
SEQRES 31 C 394 ARG PHE ASN ILE
SEQRES 1 D 223 MET SER VAL GLN ALA GLU ILE GLY ILE LEU ASP HIS VAL
SEQRES 2 D 223 ASP GLY SER SER GLU PHE VAL SER GLN ASP THR LYS VAL
SEQRES 3 D 223 ILE CYS SER VAL THR GLY PRO ILE GLU PRO LYS ALA ARG
SEQRES 4 D 223 GLN GLU LEU PRO THR GLN LEU ALA LEU GLU ILE ILE VAL
SEQRES 5 D 223 ARG PRO ALA LYS GLY VAL ALA THR THR ARG GLU LYS VAL
SEQRES 6 D 223 LEU GLU ASP LYS LEU ARG ALA VAL LEU THR PRO LEU ILE
SEQRES 7 D 223 THR ARG HIS CYS TYR PRO ARG GLN LEU CYS GLN ILE THR
SEQRES 8 D 223 CYS GLN ILE LEU GLU SER GLY GLU ASP GLU ALA GLU PHE
SEQRES 9 D 223 SER LEU ARG GLU LEU SER CYS CYS ILE ASN ALA ALA PHE
SEQRES 10 D 223 LEU ALA LEU VAL ASP ALA GLY ILE ALA LEU ASN SER MET
SEQRES 11 D 223 CYS ALA SER ILE PRO ILE ALA ILE ILE LYS ASP THR SER
SEQRES 12 D 223 ASP ILE ILE VAL ASP PRO THR ALA GLU GLN LEU LYS ILE
SEQRES 13 D 223 SER LEU SER VAL HIS THR LEU ALA LEU GLU PHE VAL ASN
SEQRES 14 D 223 GLY GLY LYS VAL VAL LYS ASN VAL LEU LEU LEU ASP SER
SEQRES 15 D 223 ASN GLY ASP PHE ASN GLU ASP GLN LEU PHE SER LEU LEU
SEQRES 16 D 223 GLU LEU GLY GLU GLN LYS CYS GLN GLU LEU VAL THR ASN
SEQRES 17 D 223 ILE ARG ARG ILE ILE GLN ASP ASN ILE SER PRO ARG LEU
SEQRES 18 D 223 VAL VAL
SEQRES 1 E 265 MET SER LEU SER VAL ALA GLU LYS SER TYR LEU TYR ASP
SEQRES 2 E 265 SER LEU ALA SER THR PRO SER ILE ARG PRO ASP GLY ARG
SEQRES 3 E 265 LEU PRO HIS GLN PHE ARG PRO ILE GLU ILE PHE THR ASP
SEQRES 4 E 265 PHE LEU PRO SER SER ASN GLY SER SER ARG ILE ILE ALA
SEQRES 5 E 265 SER ASP GLY SER GLU CYS ILE VAL SER ILE LYS SER LYS
SEQRES 6 E 265 VAL VAL ASP HIS HIS VAL GLU ASN GLU LEU LEU GLN VAL
SEQRES 7 E 265 ASP VAL ASP ILE ALA GLY GLN ARG ASP ASP ALA LEU VAL
SEQRES 8 E 265 VAL GLU THR ILE THR SER LEU LEU ASN LYS VAL LEU LYS
SEQRES 9 E 265 SER GLY SER GLY VAL ASP SER SER LYS LEU GLN LEU THR
SEQRES 10 E 265 LYS LYS TYR SER PHE LYS ILE PHE VAL ASP VAL LEU VAL
SEQRES 11 E 265 ILE SER SER HIS SER HIS PRO ILE SER LEU ILE SER PHE
SEQRES 12 E 265 ALA ILE TYR SER ALA LEU ASN SER THR TYR LEU PRO LYS
SEQRES 13 E 265 LEU ILE SER ALA PHE ASP ASP LEU GLU VAL GLU GLU LEU
SEQRES 14 E 265 PRO THR PHE HIS ASP TYR ASP MET VAL LYS LEU ASP ILE
SEQRES 15 E 265 ASN PRO PRO LEU VAL PHE ILE LEU ALA VAL VAL GLY ASN
SEQRES 16 E 265 ASN MET LEU LEU ASP PRO ALA ALA ASN GLU SER GLU VAL
SEQRES 17 E 265 ALA ASN ASN GLY LEU ILE ILE SER TRP SER ASN GLY LYS
SEQRES 18 E 265 ILE THR SER PRO ILE ARG SER VAL ALA LEU ASN ASP SER
SEQRES 19 E 265 ASN VAL LYS SER PHE LYS PRO HIS LEU LEU LYS GLN GLY
SEQRES 20 E 265 LEU ALA MET VAL GLU LYS TYR ALA PRO ASP VAL VAL ARG
SEQRES 21 E 265 SER LEU GLU ASN LEU
SEQRES 1 F 250 MET ASN VAL GLN ASP ARG ARG ARG LEU LEU GLY PRO ALA
SEQRES 2 F 250 ALA ALA LYS PRO MET ALA PHE SER ASN THR THR THR HIS
SEQRES 3 F 250 VAL PRO GLU LYS LYS SER THR ASP LEU THR PRO LYS GLY
SEQRES 4 F 250 ASN GLU SER GLU GLN GLU LEU SER LEU HIS THR GLY PHE
SEQRES 5 F 250 ILE GLU ASN CYS ASN GLY SER ALA LEU VAL GLU ALA ARG
SEQRES 6 F 250 SER LEU GLY HIS GLN THR SER LEU ILE SER ALA VAL TYR
SEQRES 7 F 250 GLY PRO ARG SER ILE ARG GLY SER PHE THR SER GLN GLY
SEQRES 8 F 250 THR ILE SER ILE GLN LEU LYS ASN GLY LEU LEU GLU LYS
SEQRES 9 F 250 TYR ASN THR ASN GLU LEU LYS GLU VAL SER SER PHE LEU
SEQRES 10 F 250 MET GLY ILE PHE ASN SER VAL VAL ASN LEU SER ARG TYR
SEQRES 11 F 250 PRO LYS SER GLY ILE ASP ILE PHE VAL TYR LEU THR TYR
SEQRES 12 F 250 ASP LYS ASP LEU THR ASN ASN PRO GLN ASP ASP ASP SER
SEQRES 13 F 250 GLN SER LYS MET MET SER SER GLN ILE SER SER LEU ILE
SEQRES 14 F 250 PRO HIS CYS ILE THR SER ILE THR LEU ALA LEU ALA ASP
SEQRES 15 F 250 ALA GLY ILE GLU LEU VAL ASP MET ALA GLY ALA GLY GLU
SEQRES 16 F 250 ALA ASN GLY THR VAL VAL SER PHE ILE LYS ASN GLY GLU
SEQRES 17 F 250 GLU ILE VAL GLY PHE TRP LYS ASP ASP GLY ASP ASP GLU
SEQRES 18 F 250 ASP LEU LEU GLU CYS LEU ASP ARG CYS LYS GLU GLN TYR
SEQRES 19 F 250 ASN ARG TYR ARG ASP LEU MET ILE SER CYS LEU MET ASN
SEQRES 20 F 250 GLN GLU THR
SEQRES 1 G 240 MET SER THR PHE ILE PHE PRO GLY ASP SER PHE PRO VAL
SEQRES 2 G 240 ASP PRO THR THR PRO VAL LYS LEU GLY PRO GLY ILE TYR
SEQRES 3 G 240 CYS ASP PRO ASN THR GLN GLU ILE ARG PRO VAL ASN THR
SEQRES 4 G 240 GLY VAL LEU HIS VAL SER ALA LYS GLY LYS SER GLY VAL
SEQRES 5 G 240 GLN THR ALA TYR ILE ASP TYR SER SER LYS ARG TYR ILE
SEQRES 6 G 240 PRO SER VAL ASN ASP PHE VAL ILE GLY VAL ILE ILE GLY
SEQRES 7 G 240 THR PHE SER ASP SER TYR LYS VAL SER LEU GLN ASN PHE
SEQRES 8 G 240 SER SER SER VAL SER LEU SER TYR MET ALA PHE PRO ASN
SEQRES 9 G 240 ALA SER LYS LYS ASN ARG PRO THR LEU GLN VAL GLY ASP
SEQRES 10 G 240 LEU VAL TYR ALA ARG VAL CYS THR ALA GLU LYS GLU LEU
SEQRES 11 G 240 GLU ALA GLU ILE GLU CYS PHE ASP SER THR THR GLY ARG
SEQRES 12 G 240 ASP ALA GLY PHE GLY ILE LEU GLU ASP GLY MET ILE ILE
SEQRES 13 G 240 ASP VAL ASN LEU ASN PHE ALA ARG GLN LEU LEU PHE ASN
SEQRES 14 G 240 ASN ASP PHE PRO LEU LEU LYS VAL LEU ALA ALA HIS THR
SEQRES 15 G 240 LYS PHE GLU VAL ALA ILE GLY LEU ASN GLY LYS ILE TRP
SEQRES 16 G 240 VAL LYS CYS GLU GLU LEU SER ASN THR LEU ALA CYS TYR
SEQRES 17 G 240 ARG THR ILE MET GLU CYS CYS GLN LYS ASN ASP THR ALA
SEQRES 18 G 240 ALA PHE LYS ASP ILE ALA LYS ARG GLN PHE LYS GLU ILE
SEQRES 19 G 240 LEU THR VAL LYS GLU GLU
SEQRES 1 H 359 MET SER GLU VAL ILE THR ILE THR LYS ARG ASN GLY ALA
SEQRES 2 H 359 PHE GLN ASN SER SER ASN LEU SER TYR ASN ASN THR GLY
SEQRES 3 H 359 ILE SER ASP ASP GLU ASN ASP GLU GLU ASP ILE TYR MET
SEQRES 4 H 359 HIS ASP VAL ASN SER ALA SER LYS SER GLU SER ASP SER
SEQRES 5 H 359 GLN ILE VAL THR PRO GLY GLU LEU VAL THR ASP ASP PRO
SEQRES 6 H 359 ILE TRP MET ARG GLY HIS GLY THR TYR PHE LEU ASP ASN
SEQRES 7 H 359 MET THR TYR SER SER VAL ALA GLY THR VAL SER ARG VAL
SEQRES 8 H 359 ASN ARG LEU LEU SER VAL ILE PRO LEU LYS GLY ARG TYR
SEQRES 9 H 359 ALA PRO GLU THR GLY ASP HIS VAL VAL GLY ARG ILE ALA
SEQRES 10 H 359 GLU VAL GLY ASN LYS ARG TRP LYS VAL ASP ILE GLY GLY
SEQRES 11 H 359 LYS GLN HIS ALA VAL LEU MET LEU GLY SER VAL ASN LEU
SEQRES 12 H 359 PRO GLY GLY ILE LEU ARG ARG LYS SER GLU SER ASP GLU
SEQRES 13 H 359 LEU GLN MET ARG SER PHE LEU LYS GLU GLY ASP LEU LEU
SEQRES 14 H 359 ASN ALA GLU VAL GLN SER LEU PHE GLN ASP GLY SER ALA
SEQRES 15 H 359 SER LEU HIS THR ARG SER LEU LYS TYR GLY LYS LEU ARG
SEQRES 16 H 359 ASN GLY MET PHE CYS GLN VAL PRO SER SER LEU ILE VAL
SEQRES 17 H 359 ARG ALA LYS ASN HIS THR HIS ASN LEU PRO GLY ASN ILE
SEQRES 18 H 359 THR VAL VAL LEU GLY VAL ASN GLY TYR ILE TRP LEU ARG
SEQRES 19 H 359 LYS THR SER GLN MET ASP LEU ALA ARG ASP THR PRO SER
SEQRES 20 H 359 ALA ASN ASN SER SER SER ILE LYS SER THR GLY PRO THR
SEQRES 21 H 359 GLY ALA VAL SER LEU ASN PRO SER ILE THR ARG LEU GLU
SEQRES 22 H 359 GLU GLU SER SER TRP GLN ILE TYR SER ASP GLU ASN ASP
SEQRES 23 H 359 PRO SER ILE SER ASN ASN ILE ARG GLN ALA ILE CYS ARG
SEQRES 24 H 359 TYR ALA ASN VAL ILE LYS ALA LEU ALA PHE CYS GLU ILE
SEQRES 25 H 359 GLY ILE THR GLN GLN ARG ILE VAL SER ALA TYR GLU ALA
SEQRES 26 H 359 SER MET VAL TYR SER ASN VAL GLY GLU LEU ILE GLU LYS
SEQRES 27 H 359 ASN VAL MET GLU SER ILE GLY SER ASP ILE LEU THR ALA
SEQRES 28 H 359 GLU LYS MET ARG GLY ASN GLY ASN
SEQRES 1 I 292 MET ALA CYS ASN PHE GLN PHE PRO GLU ILE ALA TYR PRO
SEQRES 2 I 292 GLY LYS LEU ILE CYS PRO GLN TYR GLY THR GLU ASN LYS
SEQRES 3 I 292 ASP GLY GLU ASP ILE ILE PHE ASN TYR VAL PRO GLY PRO
SEQRES 4 I 292 GLY THR LYS LEU ILE GLN TYR GLU HIS ASN GLY ARG THR
SEQRES 5 I 292 LEU GLU ALA ILE THR ALA THR LEU VAL GLY THR VAL ARG
SEQRES 6 I 292 CYS GLU GLU GLU LYS LYS THR ASP GLN GLU GLU GLU ARG
SEQRES 7 I 292 GLU GLY THR ASP GLN SER THR GLU GLU GLU LYS SER VAL
SEQRES 8 I 292 ASP ALA SER PRO ASN ASP VAL THR ARG ARG THR VAL LYS
SEQRES 9 I 292 ASN ILE LEU VAL SER VAL LEU PRO GLY THR GLU LYS GLY
SEQRES 10 I 292 ARG LYS THR ASN LYS TYR ALA ASN ASN ASP PHE ALA ASN
SEQRES 11 I 292 ASN LEU PRO LYS GLU GLY ASP ILE VAL LEU THR ARG VAL
SEQRES 12 I 292 THR ARG LEU SER LEU GLN ARG ALA ASN VAL GLU ILE LEU
SEQRES 13 I 292 ALA VAL GLU ASP LYS PRO SER PRO ILE ASP SER GLY ILE
SEQRES 14 I 292 GLY SER ASN GLY SER GLY ILE VAL ALA ALA GLY GLY GLY
SEQRES 15 I 292 SER GLY ALA ALA THR PHE SER VAL SER GLN ALA SER SER
SEQRES 16 I 292 ASP LEU GLY GLU THR PHE ARG GLY ILE ILE ARG SER GLN
SEQRES 17 I 292 ASP VAL ARG SER THR ASP ARG ASP ARG VAL LYS VAL ILE
SEQRES 18 I 292 GLU CYS PHE LYS PRO GLY ASP ILE VAL ARG ALA GLN VAL
SEQRES 19 I 292 LEU SER LEU GLY ASP GLY THR ASN TYR TYR LEU THR THR
SEQRES 20 I 292 ALA ARG ASN ASP LEU GLY VAL VAL PHE ALA ARG ALA ALA
SEQRES 21 I 292 ASN GLY ALA GLY GLY LEU MET TYR ALA THR ASP TRP GLN
SEQRES 22 I 292 MET MET THR SER PRO VAL THR GLY ALA THR GLU LYS ARG
SEQRES 23 I 292 LYS CYS ALA LYS PRO PHE
SEQRES 1 J 1001 MET SER VAL PRO ALA ILE ALA PRO ARG ARG LYS ARG LEU
SEQRES 2 J 1001 ALA ASP GLY LEU SER VAL THR GLN LYS VAL PHE VAL ARG
SEQRES 3 J 1001 SER ARG ASN GLY GLY ALA THR LYS ILE VAL ARG GLU HIS
SEQRES 4 J 1001 TYR LEU ARG SER ASP ILE PRO CYS LEU SER ARG SER CYS
SEQRES 5 J 1001 THR LYS CYS PRO GLN ILE VAL VAL PRO ASP ALA GLN ASN
SEQRES 6 J 1001 GLU LEU PRO LYS PHE ILE LEU SER ASP SER PRO LEU GLU
SEQRES 7 J 1001 LEU SER ALA PRO ILE GLY LYS HIS TYR VAL VAL LEU ASP
SEQRES 8 J 1001 THR ASN VAL VAL LEU GLN ALA ILE ASP LEU LEU GLU ASN
SEQRES 9 J 1001 PRO ASN CYS PHE PHE ASP VAL ILE VAL PRO GLN ILE VAL
SEQRES 10 J 1001 LEU ASP GLU VAL ARG ASN LYS SER TYR PRO VAL TYR THR
SEQRES 11 J 1001 ARG LEU ARG THR LEU CYS ARG ASP SER ASP ASP HIS LYS
SEQRES 12 J 1001 ARG PHE ILE VAL PHE HIS ASN GLU PHE SER GLU HIS THR
SEQRES 13 J 1001 PHE VAL GLU ARG LEU PRO ASN GLU THR ILE ASN ASP ARG
SEQRES 14 J 1001 ASN ASN ARG ALA ILE ARG LYS THR CYS GLN TRP TYR SER
SEQRES 15 J 1001 GLU HIS LEU LYS PRO TYR ASP ILE ASN VAL VAL LEU VAL
SEQRES 16 J 1001 THR ASN ASP ARG LEU ASN ARG GLU ALA ALA THR LYS GLU
SEQRES 17 J 1001 VAL GLU SER ASN ILE ILE THR LYS SER LEU VAL GLN TYR
SEQRES 18 J 1001 ILE GLU LEU LEU PRO ASN ALA ASP ASP ILE ARG ASP SER
SEQRES 19 J 1001 ILE PRO GLN MET ASP SER PHE ASP LYS ASP LEU GLU ARG
SEQRES 20 J 1001 ASP THR PHE SER ASP PHE THR PHE PRO GLU TYR TYR SER
SEQRES 21 J 1001 THR ALA ARG VAL MET GLY GLY LEU LYS ASN GLY VAL LEU
SEQRES 22 J 1001 TYR GLN GLY ASN ILE GLN ILE SER GLU TYR ASN PHE LEU
SEQRES 23 J 1001 GLU GLY SER VAL SER LEU PRO ARG PHE SER LYS PRO VAL
SEQRES 24 J 1001 LEU ILE VAL GLY GLN LYS ASN LEU ASN ARG ALA PHE ASN
SEQRES 25 J 1001 GLY ASP GLN VAL ILE VAL GLU LEU LEU PRO GLN SER GLU
SEQRES 26 J 1001 TRP LYS ALA PRO SER SER ILE VAL LEU ASP SER GLU HIS
SEQRES 27 J 1001 PHE ASP VAL ASN ASP ASN PRO ASP ILE GLU ALA GLY ASP
SEQRES 28 J 1001 ASP ASP ASP ASN ASN GLU SER SER SER ASN THR THR VAL
SEQRES 29 J 1001 ILE SER ASP LYS GLN ARG ARG LEU LEU ALA LYS ASP ALA
SEQRES 30 J 1001 MET ILE ALA GLN ARG SER LYS LYS ILE GLN PRO THR ALA
SEQRES 31 J 1001 LYS VAL VAL TYR ILE GLN ARG ARG SER TRP ARG GLN TYR
SEQRES 32 J 1001 VAL GLY GLN LEU ALA PRO SER SER VAL ASP PRO GLN SER
SEQRES 33 J 1001 SER SER THR GLN ASN VAL PHE VAL ILE LEU MET ASP LYS
SEQRES 34 J 1001 CYS LEU PRO LYS VAL ARG ILE ARG THR ARG ARG ALA ALA
SEQRES 35 J 1001 GLU LEU LEU ASP LYS ARG ILE VAL ILE SER ILE ASP SER
SEQRES 36 J 1001 TRP PRO THR THR HIS LYS TYR PRO LEU GLY HIS PHE VAL
SEQRES 37 J 1001 ARG ASP LEU GLY THR ILE GLU SER ALA GLN ALA GLU THR
SEQRES 38 J 1001 GLU ALA LEU LEU LEU GLU HIS ASP VAL GLU TYR ARG PRO
SEQRES 39 J 1001 PHE SER LYS LYS VAL LEU GLU CYS LEU PRO ALA GLU GLY
SEQRES 40 J 1001 HIS ASP TRP LYS ALA PRO THR LYS LEU ASP ASP PRO GLU
SEQRES 41 J 1001 ALA VAL SER LYS ASP PRO LEU LEU THR LYS ARG LYS ASP
SEQRES 42 J 1001 LEU ARG ASP LYS LEU ILE CYS SER ILE ASP PRO PRO GLY
SEQRES 43 J 1001 CYS VAL ASP ILE ASN ASP ALA LEU HIS ALA LYS LYS LEU
SEQRES 44 J 1001 PRO ASN GLY ASN TRP GLU VAL GLY VAL HIS ILE ALA ASP
SEQRES 45 J 1001 VAL THR HIS PHE VAL LYS PRO GLY THR ALA LEU ASP ALA
SEQRES 46 J 1001 GLU GLY ALA ALA ARG GLY THR SER VAL TYR LEU VAL ASP
SEQRES 47 J 1001 LYS ARG ILE ASP MET LEU PRO MET LEU LEU GLY THR ASP
SEQRES 48 J 1001 LEU CYS SER LEU LYS PRO TYR VAL ASP ARG PHE ALA PHE
SEQRES 49 J 1001 SER VAL ILE TRP GLU LEU ASP ASP SER ALA ASN ILE VAL
SEQRES 50 J 1001 ASN VAL ASN PHE MET LYS SER VAL ILE ARG SER ARG GLU
SEQRES 51 J 1001 ALA PHE SER TYR GLU GLN ALA GLN LEU ARG ILE ASP ASP
SEQRES 52 J 1001 LYS THR GLN ASN ASP GLU LEU THR MET GLY MET ARG ALA
SEQRES 53 J 1001 LEU LEU LYS LEU SER VAL LYS LEU LYS GLN LYS ARG LEU
SEQRES 54 J 1001 GLU ALA GLY ALA LEU ASN LEU ALA SER PRO GLU VAL LYS
SEQRES 55 J 1001 VAL HIS MET ASP SER GLU THR SER ASP PRO ASN GLU VAL
SEQRES 56 J 1001 GLU ILE LYS LYS LEU LEU ALA THR ASN SER LEU VAL GLU
SEQRES 57 J 1001 GLU PHE MET LEU LEU ALA ASN ILE SER VAL ALA ARG LYS
SEQRES 58 J 1001 ILE TYR ASP ALA PHE PRO GLN THR ALA MET LEU ARG ARG
SEQRES 59 J 1001 HIS ALA ALA PRO PRO SER THR ASN PHE GLU ILE LEU ASN
SEQRES 60 J 1001 GLU MET LEU ASN THR ARG LYS ASN MET SER ILE SER LEU
SEQRES 61 J 1001 GLU SER SER LYS ALA LEU ALA ASP SER LEU ASP ARG CYS
SEQRES 62 J 1001 VAL ASP PRO GLU ASP PRO TYR PHE ASN THR LEU VAL ARG
SEQRES 63 J 1001 ILE MET SER THR ARG CYS MET MET ALA ALA GLN TYR PHE
SEQRES 64 J 1001 TYR SER GLY ALA TYR SER TYR PRO ASP PHE ARG HIS TYR
SEQRES 65 J 1001 GLY LEU ALA VAL ASP ILE TYR THR HIS PHE THR SER PRO
SEQRES 66 J 1001 ILE ARG ARG TYR CYS ASP VAL VAL ALA HIS ARG GLN LEU
SEQRES 67 J 1001 ALA GLY ALA ILE GLY TYR GLU PRO LEU SER LEU THR HIS
SEQRES 68 J 1001 ARG ASP LYS ASN LYS MET ASP MET ILE CYS ARG ASN ILE
SEQRES 69 J 1001 ASN ARG LYS HIS ARG ASN ALA GLN PHE ALA GLY ARG ALA
SEQRES 70 J 1001 SER ILE GLU TYR TYR VAL GLY GLN VAL MET ARG ASN ASN
SEQRES 71 J 1001 GLU SER THR GLU THR GLY TYR VAL ILE LYS VAL PHE ASN
SEQRES 72 J 1001 ASN GLY ILE VAL VAL LEU VAL PRO LYS PHE GLY VAL GLU
SEQRES 73 J 1001 GLY LEU ILE ARG LEU ASP ASN LEU THR GLU ASP PRO ASN
SEQRES 74 J 1001 SER ALA ALA PHE ASP GLU VAL GLU TYR LYS LEU THR PHE
SEQRES 75 J 1001 VAL PRO THR ASN SER ASP LYS PRO ARG ASP VAL TYR VAL
SEQRES 76 J 1001 PHE ASP LYS VAL GLU VAL GLN VAL ARG SER VAL MET ASP
SEQRES 77 J 1001 PRO ILE THR SER LYS ARG LYS ALA GLU LEU LEU LEU LYS
SEQRES 1 P 747 MET SER LEU LEU GLU GLN LEU ALA ARG LYS ARG ILE GLU
SEQRES 2 P 747 LYS SER LYS GLY LEU LEU SER ALA ASP GLN SER HIS SER
SEQRES 3 P 747 THR SER LYS SER ALA SER LEU LEU GLU ARG LEU HIS LYS
SEQRES 4 P 747 ASN ARG GLU THR LYS ASP ASN ASN ALA GLU THR LYS ARG
SEQRES 5 P 747 LYS ASP LEU LYS THR LEU LEU ALA LYS ASP LYS VAL LYS
SEQRES 6 P 747 ARG SER ASP PHE THR PRO ASN GLN HIS SER VAL SER LEU
SEQRES 7 P 747 SER LEU LYS LEU SER ALA LEU LYS LYS SER ASN SER ASP
SEQRES 8 P 747 LEU GLU LYS GLN GLY LYS SER VAL THR LEU ASP SER LYS
SEQRES 9 P 747 GLU ASN GLU LEU PRO THR LYS ARG LYS SER PRO ASP ASP
SEQRES 10 P 747 LYS LEU ASN LEU GLU GLU SER TRP LYS ALA ILE LYS GLU
SEQRES 11 P 747 MET ASN HIS TYR CYS PHE LEU LYS ASN ASP PRO CYS ILE
SEQRES 12 P 747 ASN GLN THR ASP ASP PHE ALA PHE THR ASN PHE ILE ILE
SEQRES 13 P 747 LYS ASP LYS LYS ASN SER LEU SER THR SER ILE PRO LEU
SEQRES 14 P 747 SER SER GLN ASN SER SER PHE LEU SER LEU LYS LYS HIS
SEQRES 15 P 747 ASN ASN GLU LEU LEU GLY ILE PHE VAL PRO CYS ASN LEU
SEQRES 16 P 747 PRO LYS THR THR ARG LYS VAL ALA ILE GLU ASN PHE ASN
SEQRES 17 P 747 ARG PRO SER PRO ASP ASP ILE ILE GLN SER ALA GLN LEU
SEQRES 18 P 747 ASN ALA PHE ASN GLU LYS LEU GLU ASN LEU ASN ILE LYS
SEQRES 19 P 747 SER VAL PRO LYS ALA GLU LYS LYS GLU PRO ILE ASN LEU
SEQRES 20 P 747 GLN THR PRO PRO THR GLU SER ILE ASP ILE HIS SER PHE
SEQRES 21 P 747 ILE ALA THR HIS PRO LEU ASN LEU THR CYS LEU PHE LEU
SEQRES 22 P 747 GLY ASP THR ASN ALA GLY LYS SER THR LEU LEU GLY HIS
SEQRES 23 P 747 LEU LEU TYR ASP LEU ASN GLU ILE SER MET SER SER MET
SEQRES 24 P 747 ARG GLU LEU GLN LYS LYS SER SER ASN LEU ASP PRO SER
SEQRES 25 P 747 SER SER ASN SER PHE LYS VAL ILE LEU ASP ASN THR LYS
SEQRES 26 P 747 THR GLU ARG GLU ASN GLY PHE SER MET PHE LYS LYS VAL
SEQRES 27 P 747 ILE GLN VAL GLU ASN ASP LEU LEU PRO PRO SER SER THR
SEQRES 28 P 747 LEU THR LEU ILE ASP THR PRO GLY SER ILE LYS TYR PHE
SEQRES 29 P 747 ASN LYS GLU THR LEU ASN SER ILE LEU THR PHE ASP PRO
SEQRES 30 P 747 GLU VAL TYR VAL LEU VAL ILE ASP CYS ASN TYR ASP SER
SEQRES 31 P 747 TRP GLU LYS SER LEU ASP GLY PRO ASN ASN GLN ILE TYR
SEQRES 32 P 747 GLU ILE LEU LYS VAL ILE SER TYR LEU ASN LYS ASN SER
SEQRES 33 P 747 ALA CYS LYS LYS HIS LEU ILE ILE LEU LEU ASN LYS ALA
SEQRES 34 P 747 ASP LEU ILE SER TRP ASP LYS HIS ARG LEU GLU MET ILE
SEQRES 35 P 747 GLN SER GLU LEU ASN TYR VAL LEU LYS GLU ASN PHE GLN
SEQRES 36 P 747 TRP THR ASP ALA GLU PHE GLN PHE ILE PRO CYS SER GLY
SEQRES 37 P 747 LEU LEU GLY SER ASN LEU ASN LYS THR GLU ASN ILE THR
SEQRES 38 P 747 LYS SER LYS TYR LYS SER GLU PHE ASP SER ILE ASN TYR
SEQRES 39 P 747 VAL PRO GLU TRP TYR GLU GLY PRO THR PHE PHE SER GLN
SEQRES 40 P 747 LEU TYR LEU LEU VAL GLU HIS ASN MET ASN LYS ILE GLU
SEQRES 41 P 747 THR THR LEU GLU GLU PRO PHE VAL GLY THR ILE LEU GLN
SEQRES 42 P 747 SER SER VAL LEU GLN PRO ILE ALA GLU ILE ASN TYR VAL
SEQRES 43 P 747 SER LEU LYS VAL LEU ILE ASN SER GLY TYR ILE GLN SER
SEQRES 44 P 747 GLY GLN THR ILE GLU ILE HIS THR GLN TYR GLU ASP PHE
SEQRES 45 P 747 HIS TYR TYR GLY ILE VAL SER ARG MET LYS ASN SER LYS
SEQRES 46 P 747 GLN ILE LEU GLU THR ASN THR LYS ASN ASN ILE SER VAL
SEQRES 47 P 747 GLY LEU ASN PRO ASP ILE LEU GLU VAL LEU VAL LYS ILE
SEQRES 48 P 747 HIS ASN THR GLU ASP PHE THR LYS LYS GLN PHE HIS ILE
SEQRES 49 P 747 ARG LYS GLY ASP ILE ILE ILE HIS SER ARG LYS THR ASN
SEQRES 50 P 747 THR LEU SER PRO ASN LEU PRO ASN THR LEU LYS LEU LEU
SEQRES 51 P 747 ALA LEU ARG LEU ILE LYS LEU SER ILE GLN THR HIS ALA
SEQRES 52 P 747 LEU SER ASP PRO VAL ASP LEU GLY SER GLU LEU LEU LEU
SEQRES 53 P 747 TYR HIS ASN LEU THR HIS ASN ALA VAL LYS LEU VAL LYS
SEQRES 54 P 747 ILE LEU GLY THR ASN ASP ILE SER ILE ASN PRO ASN GLN
SEQRES 55 P 747 SER LEU ILE VAL GLU VAL GLU ILE ILE GLU PRO ASP PHE
SEQRES 56 P 747 ALA LEU ASN VAL ILE ASP SER LYS TYR ILE THR ASN ASN
SEQRES 57 P 747 ILE VAL LEU THR SER ILE ASP HIS LYS VAL ILE ALA VAL
SEQRES 58 P 747 GLY ARG ILE ALA CYS GLN
HELIX 1 1 SER A 8 GLN A 21 1 14
HELIX 2 2 GLY A 98 ARG A 113 1 16
HELIX 3 3 VAL A 120 GLY A 122 5 3
HELIX 4 4 GLY A 146 PHE A 162 1 17
HELIX 5 5 ASP A 205 LYS A 211 1 7
HELIX 6 6 THR A 224 ARG A 231 1 8
HELIX 7 7 ASP A 257 ASN A 291 1 35
HELIX 8 8 LEU B 61 MET B 65 5 5
HELIX 9 9 GLU B 94 VAL B 112 1 19
HELIX 10 10 GLY B 134 GLY B 151 1 18
HELIX 11 11 ASN B 175 ASN B 180 1 6
HELIX 12 12 ARG B 209 ARG B 239 1 31
HELIX 13 13 PRO C 18 SER C 26 1 9
HELIX 14 14 SER C 26 LEU C 37 1 12
HELIX 15 15 SER C 60 ASP C 64 5 5
HELIX 16 16 ILE C 123 ASN C 126 5 4
HELIX 17 17 THR C 145 ARG C 163 1 19
HELIX 18 18 LYS C 167 LEU C 170 5 4
HELIX 19 19 VAL C 226 GLN C 239 1 14
HELIX 20 20 ARG C 251 ASP C 254 5 4
HELIX 21 21 THR C 336 ILE C 343 1 8
HELIX 22 22 THR C 370 PHE C 392 1 23
HELIX 23 23 LYS D 37 GLU D 41 5 5
HELIX 24 24 THR D 61 ILE D 78 1 18
HELIX 25 25 THR D 79 TYR D 83 5 5
HELIX 26 26 SER D 105 GLY D 124 1 20
HELIX 27 27 THR D 150 ILE D 156 1 7
HELIX 28 28 ASN D 187 SER D 218 1 32
HELIX 29 29 SER E 4 SER E 17 1 14
HELIX 30 30 ALA E 89 LEU E 103 1 15
HELIX 31 31 PRO E 137 ASN E 150 1 14
HELIX 32 32 ALA E 202 GLU E 207 1 6
HELIX 33 33 LYS E 240 ASN E 264 1 25
HELIX 34 34 ASN F 106 VAL F 125 1 20
HELIX 35 35 ILE F 165 SER F 167 5 3
HELIX 36 36 LEU F 168 GLY F 184 1 17
HELIX 37 37 ASP F 222 LEU F 245 1 24
HELIX 38 38 ASN G 159 ASN G 169 1 11
HELIX 39 39 PRO G 173 THR G 182 1 10
HELIX 40 40 GLU G 200 ASN G 218 1 19
HELIX 41 41 ALA G 221 ILE G 234 1 14
HELIX 42 42 GLY H 139 VAL H 141 5 3
HELIX 43 43 ASP H 155 LEU H 163 1 9
HELIX 44 44 SER H 237 LEU H 241 5 5
HELIX 45 45 SER H 290 CYS H 310 1 21
HELIX 46 46 THR H 315 SER H 326 1 12
HELIX 47 47 MET H 327 TYR H 329 5 3
HELIX 48 48 ASN H 331 LEU H 335 5 5
HELIX 49 49 GLU H 337 GLY H 356 1 20
HELIX 50 50 GLN I 208 VAL I 210 5 3
HELIX 51 51 LYS I 219 CYS I 223 5 5
HELIX 52 52 ALA I 259 ALA I 263 1 5
HELIX 53 53 LYS J 54 VAL J 59 1 6
HELIX 54 54 ASP J 91 ALA J 98 1 8
HELIX 55 55 ALA J 98 ASN J 104 1 7
HELIX 56 56 GLN J 115 SER J 125 1 11
HELIX 57 57 SER J 125 ASP J 138 1 14
HELIX 58 58 THR J 165 LEU J 185 1 21
HELIX 59 59 LYS J 186 ASP J 189 5 4
HELIX 60 60 ASP J 198 GLU J 208 1 11
HELIX 61 61 LEU J 218 LEU J 225 1 8
HELIX 62 62 SER J 260 ASN J 270 1 11
HELIX 63 63 GLY J 303 ASN J 308 1 6
HELIX 64 64 SER J 366 GLN J 381 1 16
HELIX 65 65 ARG J 440 ASP J 446 1 7
HELIX 66 66 SER J 476 HIS J 488 1 13
HELIX 67 67 SER J 496 CYS J 502 1 7
HELIX 68 68 GLU J 520 ASP J 525 1 6
HELIX 69 69 PRO J 526 ARG J 531 5 6
HELIX 70 70 THR J 581 GLY J 591 1 11
HELIX 71 71 PRO J 605 ASP J 611 1 7
HELIX 72 72 TYR J 654 ASP J 663 1 10
HELIX 73 73 ASP J 668 ALA J 693 1 26
HELIX 74 74 SER J 698 VAL J 703 1 6
HELIX 75 75 LEU J 721 PHE J 746 1 26
HELIX 76 76 PRO J 759 ASN J 775 1 17
HELIX 77 77 SER J 782 ARG J 792 1 11
HELIX 78 78 TYR J 800 MET J 813 1 14
HELIX 79 79 SER J 825 PHE J 829 5 5
HELIX 80 80 ARG J 848 ILE J 862 1 15
HELIX 81 81 SER J 868 ARG J 872 5 5
HELIX 82 82 ASP J 873 GLU J 911 1 39
HELIX 83 83 ARG J 940 LEU J 944 5 5
HELIX 84 84 ASP P 2 THR P 20 1 19
HELIX 85 85 PHE P 31 HIS P 37 1 7
HELIX 86 86 THR P 53 ARG P 64 1 12
HELIX 87 87 ARG P 64 GLN P 72 1 9
HELIX 88 88 LEU P 76 GLU P 95 1 20
SHEET 1 AA 5 VAL A 36 PHE A 40 0
SHEET 2 AA 5 VAL A 47 MET A 51 -1 O SER A 48 N THR A 39
SHEET 3 AA 5 THR A 54 ALA A 65 -1 O THR A 54 N MET A 51
SHEET 4 AA 5 LYS A 130 ASP A 142 -1 O CYS A 131 N ALA A 65
SHEET 5 AA 5 CYS A 124 VAL A 126 1 N ILE A 125 O LYS A 130
SHEET 1 AB 5 VAL A 36 PHE A 40 0
SHEET 2 AB 5 VAL A 47 MET A 51 -1 O SER A 48 N THR A 39
SHEET 3 AB 5 THR A 54 ALA A 65 -1 O THR A 54 N MET A 51
SHEET 4 AB 5 LYS A 130 ASP A 142 -1 O CYS A 131 N ALA A 65
SHEET 5 AB 5 LEU A 76 SER A 80 1 O LEU A 76 N VAL A 134
SHEET 1 AC 2 CYS A 124 VAL A 126 0
SHEET 2 AC 2 LYS A 130 ASP A 142 1 O LYS A 130 N VAL A 126
SHEET 1 AD 2 LYS A 163 LYS A 164 0
SHEET 2 AD 2 VAL A 185 PRO A 186 -1 O VAL A 185 N LYS A 164
SHEET 1 AE 2 ILE A 167 HIS A 170 0
SHEET 2 AE 2 GLN A 173 VAL A 176 -1 O GLN A 173 N HIS A 170
SHEET 1 AF 5 ILE A 218 ILE A 221 0
SHEET 2 AF 5 ILE A 194 PHE A 201 -1 O SER A 199 N ILE A 220
SHEET 3 AF 5 GLY A 233 LEU A 239 -1 O GLY A 233 N PHE A 200
SHEET 4 AF 5 GLU A 244 SER A 249 -1 N VAL A 246 O THR A 238
SHEET 5 AF 5 ILE B 205 PRO B 206 -1 O ILE B 205 N VAL A 245
SHEET 1 AG 3 ASN A 301 ALA A 302 0
SHEET 2 AG 3 LYS J 599 ILE J 601 -1 O ARG J 600 N ASN A 301
SHEET 3 AG 3 VAL J 594 TYR J 595 -1 O VAL J 594 N ILE J 601
SHEET 1 BA 5 PHE B 25 ILE B 29 0
SHEET 2 BA 5 GLY B 38 GLN B 44 -1 O TYR B 41 N SER B 28
SHEET 3 BA 5 ASN B 47 LYS B 57 -1 O ASN B 47 N GLN B 44
SHEET 4 BA 5 VAL B 121 GLU B 130 -1 O VAL B 121 N LYS B 57
SHEET 5 BA 5 LEU B 71 ILE B 78 1 O LEU B 71 N ILE B 122
SHEET 1 BB 4 THR B 169 LEU B 172 0
SHEET 2 BB 4 ILE B 158 TYR B 166 -1 O GLY B 164 N LEU B 171
SHEET 3 BB 4 THR B 184 VAL B 190 -1 O VAL B 185 N VAL B 163
SHEET 4 BB 4 LEU B 196 VAL B 201 -1 N SER B 197 O GLY B 188
SHEET 1 CA 5 ALA C 53 ASN C 56 0
SHEET 2 CA 5 GLY C 76 SER C 82 -1 O VAL C 79 N GLU C 55
SHEET 3 CA 5 THR C 85 GLY C 93 -1 O THR C 85 N SER C 82
SHEET 4 CA 5 LEU C 213 LEU C 220 -1 O TYR C 214 N THR C 92
SHEET 5 CA 5 VAL C 133 VAL C 134 1 O VAL C 133 N ILE C 217
SHEET 1 CB 2 ILE C 96 GLU C 97 0
SHEET 2 CB 2 TRP C 209 SER C 210 -1 O SER C 210 N ILE C 96
SHEET 1 CC 4 PHE C 185 LEU C 188 0
SHEET 2 CC 4 GLY C 175 ALA C 179 -1 O VAL C 176 N LEU C 188
SHEET 3 CC 4 LYS C 242 ILE C 248 1 O ALA C 246 N GLY C 175
SHEET 4 CC 4 CYS C 276 PRO C 283 -1 O ASP C 277 N ARG C 245
SHEET 1 CD 2 LEU C 255 MET C 257 0
SHEET 2 CD 2 ARG C 269 THR C 271 -1 O ARG C 269 N MET C 257
SHEET 1 CE 8 VAL C 329 ALA C 332 0
SHEET 2 CE 8 PHE C 293 VAL C 300 -1 O GLY C 298 N ILE C 331
SHEET 3 CE 8 SER C 345 ALA C 351 -1 O SER C 345 N ILE C 299
SHEET 4 CE 8 TYR C 357 GLY C 364 -1 N LYS C 358 O LEU C 350
SHEET 5 CE 8 VAL D 173 PHE D 186 -1 O LEU D 178 N GLY C 364
SHEET 6 CE 8 SER D 157 VAL D 168 -1 O VAL D 160 N ASN D 183
SHEET 7 CE 8 MET D 130 ILE D 139 -1 O MET D 130 N PHE D 167
SHEET 8 CE 8 ASP D 144 VAL D 147 -1 O ASP D 144 N ILE D 139
SHEET 1 DA 5 VAL D 3 ILE D 7 0
SHEET 2 DA 5 GLY D 15 SER D 21 -1 O GLU D 18 N GLU D 6
SHEET 3 DA 5 THR D 24 ILE D 34 -1 O THR D 24 N SER D 21
SHEET 4 DA 5 LEU D 87 GLU D 96 -1 O LEU D 87 N ILE D 34
SHEET 5 DA 5 ALA D 47 ARG D 53 1 O ALA D 47 N CYS D 88
SHEET 1 EA 2 LEU E 76 ILE E 82 0
SHEET 2 EA 2 TYR E 120 SER E 132 1 O ILE E 124 N GLN E 77
SHEET 1 EB 2 GLN E 115 THR E 117 0
SHEET 2 EB 2 TYR E 120 SER E 132 1 O TYR E 120 N LEU E 116
SHEET 1 HA 6 ILE H 7 LYS H 9 0
SHEET 2 HA 6 ILE E 34 THR E 38 1 O ILE E 34 N THR H 8
SHEET 3 HA 6 GLY E 46 ILE E 51 -1 O ARG E 49 N PHE E 37
SHEET 4 HA 6 GLU E 57 ASP E 68 -1 O CYS E 58 N ILE E 50
SHEET 5 HA 6 TYR E 120 SER E 132 -1 O SER E 121 N VAL E 67
SHEET 6 HA 6 GLN E 115 THR E 117 1 N LEU E 116 O TYR E 120
SHEET 1 HB 6 ILE H 7 LYS H 9 0
SHEET 2 HB 6 ILE E 34 THR E 38 1 O ILE E 34 N THR H 8
SHEET 3 HB 6 GLY E 46 ILE E 51 -1 O ARG E 49 N PHE E 37
SHEET 4 HB 6 GLU E 57 ASP E 68 -1 O CYS E 58 N ILE E 50
SHEET 5 HB 6 TYR E 120 SER E 132 -1 O SER E 121 N VAL E 67
SHEET 6 HB 6 LEU E 76 ILE E 82 1 O GLN E 77 N VAL E 126
SHEET 1 EC 2 TYR E 153 LEU E 157 0
SHEET 2 EC 2 PHE E 172 LYS E 179 -1 N HIS E 173 O LYS E 156
SHEET 1 ED 7 ASN E 196 LEU E 199 0
SHEET 2 ED 7 LEU E 186 VAL E 193 -1 O ALA E 191 N LEU E 198
SHEET 3 ED 7 ASN E 211 TRP E 217 -1 O ASN E 211 N VAL E 192
SHEET 4 ED 7 ILE E 222 VAL E 229 -1 O THR E 223 N SER E 216
SHEET 5 ED 7 GLU F 209 LYS F 215 -1 O PHE F 213 N SER E 228
SHEET 6 ED 7 THR F 199 ILE F 204 -1 O VAL F 200 N TRP F 214
SHEET 7 ED 7 GLY F 192 ALA F 196 -1 O GLY F 192 N PHE F 203
SHEET 1 FA 5 GLU F 45 THR F 50 0
SHEET 2 FA 5 GLY F 58 ARG F 65 -1 O LEU F 61 N HIS F 49
SHEET 3 FA 5 HIS F 69 ARG F 81 -1 O THR F 71 N ALA F 64
SHEET 4 FA 5 GLY F 134 ASP F 146 -1 O GLY F 134 N ARG F 81
SHEET 5 FA 5 THR F 92 LYS F 98 1 O THR F 92 N ILE F 135
SHEET 1 GA 3 SER G 2 ILE G 5 0
SHEET 2 GA 3 GLY G 40 VAL G 44 -1 O GLY G 40 N ILE G 5
SHEET 3 GA 3 ALA G 55 ASP G 58 -1 O TYR G 56 N HIS G 43
SHEET 1 GB 2 ILE G 25 CYS G 27 0
SHEET 2 GB 2 ILE G 34 PRO G 36 -1 O ARG G 35 N TYR G 26
SHEET 1 GC 7 PHE G 71 THR G 79 0
SHEET 2 GC 7 LEU G 118 THR G 125 -1 O VAL G 119 N GLY G 74
SHEET 3 GC 7 ALA G 132 GLU G 135 -1 O GLU G 133 N CYS G 124
SHEET 4 GC 7 VAL G 95 SER G 98 1 O SER G 96 N ILE G 134
SHEET 5 GC 7 SER G 83 SER G 87 -1 O TYR G 84 N LEU G 97
SHEET 6 GC 7 PHE G 71 THR G 79 0
SHEET 1 GD 3 MET G 154 ASP G 157 0
SHEET 2 GD 3 LYS G 193 LYS G 197 -1 O ILE G 194 N ILE G 156
SHEET 3 GD 3 GLU G 185 ILE G 188 -1 O GLU G 185 N LYS G 197
SHEET 1 HC 2 PHE H 75 LEU H 76 0
SHEET 2 HC 2 MET H 79 THR H 80 -1 O MET H 79 N LEU H 76
SHEET 1 HD 2 GLY H 86 VAL H 91 0
SHEET 2 HD 2 LEU H 94 PRO H 99 -1 O LEU H 94 N VAL H 91
SHEET 1 HE 7 HIS H 111 VAL H 119 0
SHEET 2 HE 7 LEU H 168 LEU H 176 -1 O LEU H 169 N GLY H 114
SHEET 3 HE 7 ALA H 182 HIS H 185 1 O SER H 183 N SER H 175
SHEET 4 HE 7 ALA H 134 MET H 137 -1 O VAL H 135 N LEU H 184
SHEET 5 HE 7 ARG H 123 ASP H 127 -1 O TRP H 124 N LEU H 136
SHEET 6 HE 7 HIS H 111 VAL H 119 0
SHEET 1 HF 4 GLY H 197 GLN H 201 0
SHEET 2 HF 4 TYR H 230 LYS H 235 -1 O ILE H 231 N CYS H 200
SHEET 3 HF 4 ILE H 221 LEU H 225 -1 O THR H 222 N ARG H 234
SHEET 4 HF 4 HIS H 215 LEU H 217 -1 O HIS H 215 N VAL H 223
SHEET 1 IA 5 ILE I 10 ALA I 11 0
SHEET 2 IA 5 GLY I 62 GLU I 67 -1 O GLY I 62 N ALA I 11
SHEET 3 IA 5 LYS I 104 LEU I 111 -1 O LEU I 107 N GLU I 67
SHEET 4 IA 5 GLU I 29 PRO I 37 1 O ILE I 32 N LYS I 104
SHEET 5 IA 5 TYR I 21 LYS I 26 -1 O GLY I 22 N PHE I 33
SHEET 1 IB 3 LEU I 16 PRO I 19 0
SHEET 2 IB 3 ARG I 51 ALA I 58 -1 O ILE I 56 N ILE I 17
SHEET 3 IB 3 THR I 41 HIS I 48 -1 O LYS I 42 N THR I 57
SHEET 1 IC 8 ILE I 138 LEU I 146 0
SHEET 2 IC 8 ILE I 229 SER I 236 -1 O VAL I 230 N THR I 141
SHEET 3 IC 8 TYR I 244 THR I 246 1 O TYR I 244 N LEU I 235
SHEET 4 IC 8 ARG I 202 ARG I 206 -1 O ILE I 204 N LEU I 245
SHEET 5 IC 8 ARG I 150 VAL I 158 -1 O ALA I 151 N ILE I 205
SHEET 6 IC 8 ILE I 138 LEU I 146 -1 O VAL I 139 N ALA I 232
SHEET 1 ID 3 ALA I 269 ASP I 271 0
SHEET 2 ID 3 MET I 274 THR I 276 -1 O MET I 274 N THR I 270
SHEET 3 ID 3 THR I 283 LYS I 285 -1 O GLU I 284 N MET I 275
SHEET 1 JA 3 LYS J 11 ALA J 14 0
SHEET 2 JA 3 LEU J 17 ARG J 26 -1 O LEU J 17 N LEU J 13
SHEET 3 JA 3 THR J 33 ARG J 42 -1 O THR J 33 N ARG J 26
SHEET 1 JB 2 GLU J 78 LEU J 79 0
SHEET 2 JB 2 GLY J 84 LEU J 90 1 O GLY J 84 N LEU J 79
SHEET 1 JC 5 ARG J 144 PHE J 148 0
SHEET 2 JC 5 ASP J 110 PRO J 114 1 O VAL J 111 N ILE J 146
SHEET 3 JC 5 GLY J 84 LEU J 90 1 O VAL J 88 N ILE J 112
SHEET 4 JC 5 ASN J 191 THR J 196 1 O ASN J 191 N TYR J 87
SHEET 5 JC 5 ILE J 214 SER J 217 1 O ILE J 214 N LEU J 194
SHEET 1 JD 4 ARG J 144 PHE J 148 0
SHEET 2 JD 4 ASP J 110 PRO J 114 1 O VAL J 111 N ILE J 146
SHEET 3 JD 4 GLY J 84 LEU J 90 1 O VAL J 88 N ILE J 112
SHEET 4 JD 4 GLU J 78 LEU J 79 1 O LEU J 79 N GLY J 84
SHEET 1 JE 6 TYR J 274 ILE J 280 0
SHEET 2 JE 6 GLN J 315 LEU J 320 -1 O VAL J 316 N GLY J 276
SHEET 3 JE 6 THR J 389 ARG J 397 -1 O LYS J 391 N GLU J 319
SHEET 4 JE 6 VAL J 299 VAL J 302 1 O LEU J 300 N ALA J 390
SHEET 5 JE 6 GLU J 287 SER J 291 -1 O GLY J 288 N ILE J 301
SHEET 6 JE 6 TYR J 274 ILE J 280 -1 O ASN J 277 N SER J 291
SHEET 1 JF 6 TYR J 403 LEU J 407 0
SHEET 2 JF 6 LYS J 447 SER J 455 -1 O ILE J 449 N GLY J 405
SHEET 3 JF 6 LEU J 464 THR J 473 -1 O LEU J 464 N ASP J 454
SHEET 4 JF 6 VAL J 434 THR J 438 1 O ARG J 435 N GLY J 465
SHEET 5 JF 6 GLN J 420 LEU J 426 -1 O GLN J 420 N THR J 438
SHEET 6 JF 6 TYR J 403 LEU J 407 -1 O GLN J 406 N ILE J 425
SHEET 1 JG 7 LYS J 532 ASP J 533 0
SHEET 2 JG 7 ILE J 636 SER J 653 1 O LYS J 643 N LYS J 532
SHEET 3 JG 7 VAL J 619 LEU J 630 -1 O VAL J 619 N SER J 648
SHEET 4 JG 7 TRP J 564 ALA J 571 -1 O TRP J 564 N LEU J 630
SHEET 5 JG 7 ASP J 552 LYS J 558 -1 O ALA J 553 N HIS J 569
SHEET 6 JG 7 ILE J 539 ASP J 543 -1 O CYS J 540 N LEU J 554
SHEET 7 JG 7 LYS J 532 ASP J 533 0
SHEET 1 JH 2 MET J 751 ARG J 754 0
SHEET 2 JH 2 GLN J 817 TYR J 820 -1 O GLN J 817 N ARG J 754
SHEET 1 JI 5 GLU J 936 ILE J 939 0
SHEET 2 JI 5 ILE J 926 LEU J 929 -1 O ILE J 926 N ILE J 939
SHEET 3 JI 5 THR J 913 VAL J 921 -1 O TYR J 917 N LEU J 929
SHEET 4 JI 5 LYS J 978 MET J 987 -1 O VAL J 979 N GLY J 916
SHEET 5 JI 5 ARG J 994 LEU J1000 -1 O LYS J 995 N VAL J 986
SHEET 1 JJ 3 ALA J 952 ASP J 954 0
SHEET 2 JJ 3 LYS J 959 PHE J 962 -1 O LYS J 959 N ASP J 954
SHEET 3 JJ 3 ARG J 971 TYR J 974 -1 O ARG J 971 N PHE J 962
SSBOND 1 CYS I 3 CYS I 66 1555 1555 2.04
SSBOND 2 CYS J 52 CYS J 55 1555 1555 2.02
CISPEP 1 GLY B 55 PRO B 56 0 2.88
CISPEP 2 GLY C 263 ARG C 264 0 17.85
CISPEP 3 GLY D 32 PRO D 33 0 -3.59
CISPEP 4 SER E 224 PRO E 225 0 -19.82
CISPEP 5 GLY F 79 PRO F 80 0 2.12
CISPEP 6 ALA J 81 PRO J 82 0 12.19
CISPEP 7 SER P 26 GLN P 27 0 -0.99
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
