HEADER PROTEIN TRANSPORT 14-NOV-18 6N38
TITLE STRUCTURE OF THE TYPE VI SECRETION SYSTEM TSSK-TSSF-TSSG BASEPLATE
TITLE 2 SUBCOMPLEX REVEALED BY CRYO-ELECTRON MICROSCOPY - FULL MAP SHARPENED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE TYPE VI SECRETION PROTEIN;
COMPND 3 CHAIN: I, H;
COMPND 4 SYNONYM: TSSF;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PUTATIVE TYPE VI SECRETION PROTEIN;
COMPND 8 CHAIN: G;
COMPND 9 FRAGMENT: UNP RESIDUES 31-333;
COMPND 10 SYNONYM: TSSG;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: UNASSIGNED PROTEIN;
COMPND 14 CHAIN: K, L;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: PUTATIVE TYPE VI SECRETION PROTEIN;
COMPND 18 CHAIN: A, D, B, E, C, F;
COMPND 19 FRAGMENT: NECK AND SHOULDER DOMAINS (UNP RESIDUES 1-316);
COMPND 20 SYNONYM: TSSK;
COMPND 21 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O44:H18 (STRAIN 042 / EAEC);
SOURCE 3 ORGANISM_TAXID: 216592;
SOURCE 4 STRAIN: 042 / EAEC;
SOURCE 5 GENE: EC042_4542;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O44:H18 (STRAIN 042 / EAEC);
SOURCE 10 ORGANISM_TAXID: 216592;
SOURCE 11 STRAIN: 042 / EAEC;
SOURCE 12 GENE: EC042_4543;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O44:H18 (STRAIN 042 / EAEC);
SOURCE 17 ORGANISM_TAXID: 216592;
SOURCE 18 STRAIN: STRAIN 042 / EAEC;
SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 21 MOL_ID: 4;
SOURCE 22 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O44:H18 (STRAIN 042 / EAEC);
SOURCE 23 ORGANISM_TAXID: 216592;
SOURCE 24 STRAIN: 042 / EAEC;
SOURCE 25 GENE: EC042_4526;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TYPE VI SECRETION SYSTEM, ENTEROAGGREGATIVE E. COLI, PROTEIN
KEYWDS 2 SECRETION, BASEPLATE, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL
KEYWDS 3 GENOMICS CENTER FOR INFECTIOUS DISEASE, SSGCID, PROTEIN TRANSPORT
EXPDTA ELECTRON MICROSCOPY
AUTHOR Y.J.PARK,K.D.LACOURSE,C.CAMBILLAU,SEATTLE STRUCTURAL GENOMICS CENTER
AUTHOR 2 FOR INFECTIOUS DISEASE (SSGCID),F.DIMAIO,J.D.MOUGOUS,D.VEESLER
REVDAT 3 18-DEC-19 6N38 1 REMARK
REVDAT 2 02-JAN-19 6N38 1 JRNL
REVDAT 1 26-DEC-18 6N38 0
JRNL AUTH Y.J.PARK,K.D.LACOURSE,C.CAMBILLAU,F.DIMAIO,J.D.MOUGOUS,
JRNL AUTH 2 D.VEESLER
JRNL TITL STRUCTURE OF THE TYPE VI SECRETION SYSTEM TSSK-TSSF-TSSG
JRNL TITL 2 BASEPLATE SUBCOMPLEX REVEALED BY CRYO-ELECTRON MICROSCOPY.
JRNL REF NAT COMMUN V. 9 5385 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 30568167
JRNL DOI 10.1038/S41467-018-07796-5
REMARK 2
REMARK 2 RESOLUTION. 3.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : LEGINON, GCTF, 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) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.700
REMARK 3 NUMBER OF PARTICLES : 36496
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6N38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1000238029.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : TSSK-TSSF-TSSG T6SS BASEPLATE
REMARK 245 SUBCOMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.12
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.80
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
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) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
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 : NULL
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: I, G, H, K, L, A, D, B, E, C,
REMARK 350 AND CHAINS: F
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 I 1
REMARK 465 ASP I 2
REMARK 465 ASP I 3
REMARK 465 LEU I 4
REMARK 465 THR I 5
REMARK 465 LEU I 6
REMARK 465 ARG I 7
REMARK 465 TYR I 8
REMARK 465 PHE I 9
REMARK 465 ASP I 10
REMARK 465 ALA I 11
REMARK 465 GLU I 12
REMARK 465 MET I 13
REMARK 465 ARG I 14
REMARK 465 TYR I 15
REMARK 465 LEU I 16
REMARK 465 ARG I 17
REMARK 465 GLU I 18
REMARK 465 ALA I 19
REMARK 465 GLY I 20
REMARK 465 LYS I 21
REMARK 465 ALA I 22
REMARK 465 PHE I 23
REMARK 465 ALA I 24
REMARK 465 GLN I 25
REMARK 465 ALA I 26
REMARK 465 HIS I 27
REMARK 465 PRO I 28
REMARK 465 ASP I 29
REMARK 465 ARG I 30
REMARK 465 ALA I 31
REMARK 465 ALA I 32
REMARK 465 MET I 33
REMARK 465 LEU I 34
REMARK 465 ASP I 35
REMARK 465 LEU I 36
REMARK 465 ASP I 37
REMARK 465 LYS I 38
REMARK 465 ALA I 39
REMARK 465 GLY I 40
REMARK 465 THR I 41
REMARK 465 PRO I 42
REMARK 465 ASP I 43
REMARK 465 PRO I 44
REMARK 465 CYS I 45
REMARK 465 VAL I 46
REMARK 465 GLY I 393
REMARK 465 GLY I 394
REMARK 465 GLN I 395
REMARK 465 ARG I 396
REMARK 465 TRP I 397
REMARK 465 GLU I 398
REMARK 465 ALA I 399
REMARK 465 ASP I 400
REMARK 465 ARG I 401
REMARK 465 MET I 402
REMARK 465 PRO I 403
REMARK 465 GLU I 404
REMARK 465 ARG I 405
REMARK 465 MET G 64
REMARK 465 GLY G 65
REMARK 465 PHE G 66
REMARK 465 PRO G 67
REMARK 465 ALA G 68
REMARK 465 SER G 69
REMARK 465 GLU G 70
REMARK 465 ILE G 71
REMARK 465 LYS G 72
REMARK 465 ASP G 73
REMARK 465 ALA G 74
REMARK 465 VAL G 75
REMARK 465 ILE G 76
REMARK 465 PRO G 77
REMARK 465 GLU G 78
REMARK 465 GLU G 79
REMARK 465 SER G 80
REMARK 465 HIS G 81
REMARK 465 LEU G 82
REMARK 465 PRO G 83
REMARK 465 PRO G 84
REMARK 465 ILE G 85
REMARK 465 VAL G 86
REMARK 465 HIS G 87
REMARK 465 VAL G 88
REMARK 465 THR G 89
REMARK 465 PHE G 90
REMARK 465 MET G 91
REMARK 465 GLY G 92
REMARK 465 LEU G 93
REMARK 465 TYR G 94
REMARK 465 GLY G 95
REMARK 465 VAL G 96
REMARK 465 THR G 97
REMARK 465 SER G 98
REMARK 465 PRO G 99
REMARK 465 LEU G 100
REMARK 465 PRO G 101
REMARK 465 ALA G 102
REMARK 465 HIS G 103
REMARK 465 TYR G 104
REMARK 465 ILE G 105
REMARK 465 SER G 106
REMARK 465 ASP G 107
REMARK 465 ILE G 108
REMARK 465 ALA G 109
REMARK 465 GLN G 110
REMARK 465 GLN G 111
REMARK 465 ARG G 112
REMARK 465 GLU G 113
REMARK 465 GLY G 114
REMARK 465 HIS G 115
REMARK 465 GLU G 116
REMARK 465 ALA G 117
REMARK 465 ALA G 118
REMARK 465 ALA G 119
REMARK 465 ASP G 120
REMARK 465 PHE G 121
REMARK 465 ILE G 331
REMARK 465 ALA G 332
REMARK 465 THR G 333
REMARK 465 SER G 334
REMARK 465 ALA G 335
REMARK 465 MET H 1
REMARK 465 ASP H 2
REMARK 465 ASP H 3
REMARK 465 LEU H 4
REMARK 465 THR H 5
REMARK 465 LEU H 6
REMARK 465 ARG H 7
REMARK 465 TYR H 8
REMARK 465 PHE H 9
REMARK 465 ASP H 10
REMARK 465 ALA H 11
REMARK 465 GLU H 12
REMARK 465 MET H 13
REMARK 465 ARG H 14
REMARK 465 TYR H 15
REMARK 465 LEU H 16
REMARK 465 ARG H 17
REMARK 465 GLU H 18
REMARK 465 ALA H 19
REMARK 465 GLY H 20
REMARK 465 LYS H 21
REMARK 465 ALA H 22
REMARK 465 PHE H 23
REMARK 465 ALA H 24
REMARK 465 GLN H 25
REMARK 465 ALA H 26
REMARK 465 HIS H 27
REMARK 465 PRO H 28
REMARK 465 ASP H 29
REMARK 465 ARG H 30
REMARK 465 ALA H 31
REMARK 465 ALA H 32
REMARK 465 MET H 33
REMARK 465 LEU H 34
REMARK 465 ASP H 35
REMARK 465 LEU H 36
REMARK 465 ASP H 37
REMARK 465 LYS H 38
REMARK 465 ALA H 39
REMARK 465 GLY H 40
REMARK 465 THR H 41
REMARK 465 PRO H 42
REMARK 465 ASP H 43
REMARK 465 PRO H 44
REMARK 465 GLY H 393
REMARK 465 GLY H 394
REMARK 465 GLN H 395
REMARK 465 ARG H 396
REMARK 465 TRP H 397
REMARK 465 GLU H 398
REMARK 465 ALA H 399
REMARK 465 ASP H 400
REMARK 465 ARG H 401
REMARK 465 MET H 402
REMARK 465 PRO H 403
REMARK 465 UNK L 19
REMARK 465 UNK L 20
REMARK 465 UNK L 21
REMARK 465 MET A 1
REMARK 465 ARG A 220
REMARK 465 GLU A 221
REMARK 465 ASN A 222
REMARK 465 ASN A 223
REMARK 465 ALA A 224
REMARK 465 ARG A 225
REMARK 465 LEU A 226
REMARK 465 ALA A 227
REMARK 465 ASP A 228
REMARK 465 PHE A 229
REMARK 465 ALA A 230
REMARK 465 VAL A 231
REMARK 465 SER A 313
REMARK 465 LEU A 314
REMARK 465 PRO A 315
REMARK 465 SER A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 MET D 1
REMARK 465 ARG D 220
REMARK 465 GLU D 221
REMARK 465 ASN D 222
REMARK 465 ASN D 223
REMARK 465 ALA D 224
REMARK 465 ARG D 225
REMARK 465 LEU D 226
REMARK 465 ALA D 227
REMARK 465 ASP D 228
REMARK 465 PHE D 229
REMARK 465 ALA D 230
REMARK 465 VAL D 231
REMARK 465 SER D 313
REMARK 465 LEU D 314
REMARK 465 PRO D 315
REMARK 465 SER D 316
REMARK 465 HIS D 317
REMARK 465 HIS D 318
REMARK 465 HIS D 319
REMARK 465 HIS D 320
REMARK 465 HIS D 321
REMARK 465 HIS D 322
REMARK 465 ARG B 220
REMARK 465 GLU B 221
REMARK 465 ASN B 222
REMARK 465 ASN B 223
REMARK 465 ALA B 224
REMARK 465 ARG B 225
REMARK 465 LEU B 226
REMARK 465 ALA B 227
REMARK 465 ASP B 228
REMARK 465 PHE B 229
REMARK 465 ALA B 230
REMARK 465 VAL B 231
REMARK 465 ALA B 232
REMARK 465 LEU B 314
REMARK 465 PRO B 315
REMARK 465 SER B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 ARG E 220
REMARK 465 GLU E 221
REMARK 465 ASN E 222
REMARK 465 ASN E 223
REMARK 465 ALA E 224
REMARK 465 ARG E 225
REMARK 465 LEU E 226
REMARK 465 ALA E 227
REMARK 465 ASP E 228
REMARK 465 PHE E 229
REMARK 465 ALA E 230
REMARK 465 VAL E 231
REMARK 465 LEU E 314
REMARK 465 PRO E 315
REMARK 465 SER E 316
REMARK 465 HIS E 317
REMARK 465 HIS E 318
REMARK 465 HIS E 319
REMARK 465 HIS E 320
REMARK 465 HIS E 321
REMARK 465 HIS E 322
REMARK 465 MET C 1
REMARK 465 ARG C 220
REMARK 465 GLU C 221
REMARK 465 ASN C 222
REMARK 465 ASN C 223
REMARK 465 ALA C 224
REMARK 465 ARG C 225
REMARK 465 LEU C 226
REMARK 465 ALA C 227
REMARK 465 ASP C 228
REMARK 465 PHE C 229
REMARK 465 ALA C 230
REMARK 465 VAL C 231
REMARK 465 SER C 313
REMARK 465 LEU C 314
REMARK 465 PRO C 315
REMARK 465 SER C 316
REMARK 465 HIS C 317
REMARK 465 HIS C 318
REMARK 465 HIS C 319
REMARK 465 HIS C 320
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 MET F 1
REMARK 465 ARG F 220
REMARK 465 GLU F 221
REMARK 465 ASN F 222
REMARK 465 ASN F 223
REMARK 465 ALA F 224
REMARK 465 ARG F 225
REMARK 465 LEU F 226
REMARK 465 ALA F 227
REMARK 465 ASP F 228
REMARK 465 PHE F 229
REMARK 465 ALA F 230
REMARK 465 VAL F 231
REMARK 465 LEU F 314
REMARK 465 PRO F 315
REMARK 465 SER F 316
REMARK 465 HIS F 317
REMARK 465 HIS F 318
REMARK 465 HIS F 319
REMARK 465 HIS F 320
REMARK 465 HIS F 321
REMARK 465 HIS F 322
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU I 47 CG CD OE1 OE2
REMARK 470 ARG I 48 CG CD NE CZ NH1 NH2
REMARK 470 LEU I 49 CG CD1 CD2
REMARK 470 PHE I 50 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU I 51 CG CD OE1 OE2
REMARK 470 GLU I 70 CG CD OE1 OE2
REMARK 470 LYS I 103 CG CD CE NZ
REMARK 470 GLU I 106 CG CD OE1 OE2
REMARK 470 GLU I 164 CG CD OE1 OE2
REMARK 470 GLU I 210 CG CD OE1 OE2
REMARK 470 GLU I 225 CG CD OE1 OE2
REMARK 470 GLU I 226 CG CD OE1 OE2
REMARK 470 ASP I 234 CG OD1 OD2
REMARK 470 GLU I 251 CG CD OE1 OE2
REMARK 470 ASP I 274 CG OD1 OD2
REMARK 470 ASP I 292 CG OD1 OD2
REMARK 470 LEU I 312 CG CD1 CD2
REMARK 470 ILE I 313 CG1 CG2 CD1
REMARK 470 ILE I 314 CG1 CG2 CD1
REMARK 470 ASN I 315 CG OD1 ND2
REMARK 470 LEU I 317 CG CD1 CD2
REMARK 470 GLU I 320 CG CD OE1 OE2
REMARK 470 GLN I 329 CG CD OE1 NE2
REMARK 470 GLU I 334 CG CD OE1 OE2
REMARK 470 ARG I 346 CG CD NE CZ NH1 NH2
REMARK 470 THR I 347 OG1 CG2
REMARK 470 ARG I 366 CG CD NE CZ NH1 NH2
REMARK 470 GLU I 371 CG CD OE1 OE2
REMARK 470 LYS I 379 CG CD CE NZ
REMARK 470 ARG I 380 CG CD NE CZ NH1 NH2
REMARK 470 MET I 385 CG SD CE
REMARK 470 LEU I 392 CG CD1 CD2
REMARK 470 GLU I 406 CG CD OE1 OE2
REMARK 470 THR I 407 OG1 CG2
REMARK 470 LEU I 408 CG CD1 CD2
REMARK 470 LEU I 424 CG CD1 CD2
REMARK 470 ARG I 431 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 447 CG CD CE NZ
REMARK 470 GLU I 480 CG CD OE1 OE2
REMARK 470 GLU I 495 CG CD OE1 OE2
REMARK 470 GLU I 516 CG CD OE1 OE2
REMARK 470 ASP I 531 CG OD1 OD2
REMARK 470 CYS H 45 SG
REMARK 470 VAL H 46 CG1 CG2
REMARK 470 GLU H 47 CG CD OE1 OE2
REMARK 470 ARG H 48 CG CD NE CZ NH1 NH2
REMARK 470 LEU H 49 CG CD1 CD2
REMARK 470 PHE H 50 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU H 51 CG CD OE1 OE2
REMARK 470 LYS H 103 CG CD CE NZ
REMARK 470 GLU H 106 CG CD OE1 OE2
REMARK 470 GLU H 164 CG CD OE1 OE2
REMARK 470 ARG H 204 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 210 CG CD OE1 OE2
REMARK 470 GLU H 225 CG CD OE1 OE2
REMARK 470 GLU H 226 CG CD OE1 OE2
REMARK 470 ASP H 234 CG OD1 OD2
REMARK 470 GLU H 251 CG CD OE1 OE2
REMARK 470 GLU H 262 CG CD OE1 OE2
REMARK 470 ASP H 274 CG OD1 OD2
REMARK 470 GLU H 276 CG CD OE1 OE2
REMARK 470 ASP H 286 CG OD1 OD2
REMARK 470 ASP H 292 CG OD1 OD2
REMARK 470 ASP H 310 CG OD1 OD2
REMARK 470 GLU H 320 CG CD OE1 OE2
REMARK 470 ARG H 327 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 334 CG CD OE1 OE2
REMARK 470 ARG H 346 CG CD NE CZ NH1 NH2
REMARK 470 THR H 347 OG1 CG2
REMARK 470 SER H 349 OG
REMARK 470 GLU H 351 CG CD OE1 OE2
REMARK 470 ASP H 368 CG OD1 OD2
REMARK 470 GLU H 371 CG CD OE1 OE2
REMARK 470 MET H 385 CG SD CE
REMARK 470 LEU H 392 CG CD1 CD2
REMARK 470 GLU H 404 CG CD OE1 OE2
REMARK 470 ARG H 405 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 406 CG CD OE1 OE2
REMARK 470 ARG H 431 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 457 CG CD OE1 OE2
REMARK 470 ASP H 458 CG OD1 OD2
REMARK 470 ASP H 493 CG OD1 OD2
REMARK 470 GLU H 495 CG CD OE1 OE2
REMARK 470 GLU A 139 CG CD OE1 OE2
REMARK 470 GLU A 281 CG CD OE1 OE2
REMARK 470 GLU D 120 CG CD OE1 OE2
REMARK 470 ASP D 233 CG OD1 OD2
REMARK 470 ASP B 10 CG OD1 OD2
REMARK 470 GLU B 120 CG CD OE1 OE2
REMARK 470 ASP B 233 CG OD1 OD2
REMARK 470 GLU B 293 CG CD OE1 OE2
REMARK 470 GLU E 118 CG CD OE1 OE2
REMARK 470 GLU E 120 CG CD OE1 OE2
REMARK 470 GLU E 139 CG CD OE1 OE2
REMARK 470 ASP E 233 CG OD1 OD2
REMARK 470 GLU E 281 CG CD OE1 OE2
REMARK 470 GLU E 311 CG CD OE1 OE2
REMARK 470 GLU C 118 CG CD OE1 OE2
REMARK 470 GLU C 120 CG CD OE1 OE2
REMARK 470 GLU C 139 CG CD OE1 OE2
REMARK 470 GLN C 175 CG CD OE1 NE2
REMARK 470 GLN C 177 CG CD OE1 NE2
REMARK 470 ASP C 233 CG OD1 OD2
REMARK 470 GLU C 311 CG CD OE1 OE2
REMARK 470 ASP F 10 CG OD1 OD2
REMARK 470 GLU F 118 CG CD OE1 OE2
REMARK 470 GLU F 120 CG CD OE1 OE2
REMARK 470 GLU F 139 CG CD OE1 OE2
REMARK 470 GLU F 200 CG CD OE1 OE2
REMARK 470 ASP F 233 CG OD1 OD2
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 VAL I 101 CA - CB - CG2 ANGL. DEV. = 16.6 DEGREES
REMARK 500 LEU I 165 CD1 - CG - CD2 ANGL. DEV. = 22.0 DEGREES
REMARK 500 VAL I 186 CG1 - CB - CG2 ANGL. DEV. = 20.1 DEGREES
REMARK 500 LEU I 192 CD1 - CG - CD2 ANGL. DEV. = 21.1 DEGREES
REMARK 500 LEU I 287 CD1 - CG - CD2 ANGL. DEV. = 21.3 DEGREES
REMARK 500 LEU I 328 CD1 - CG - CD2 ANGL. DEV. = 20.4 DEGREES
REMARK 500 LEU I 365 CD1 - CG - CD2 ANGL. DEV. = 22.5 DEGREES
REMARK 500 LEU H 287 CD1 - CG - CD2 ANGL. DEV. = 21.2 DEGREES
REMARK 500 VAL D 234 CA - CB - CG2 ANGL. DEV. = 15.8 DEGREES
REMARK 500 LEU B 239 CD1 - CG - CD2 ANGL. DEV. = 21.1 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 ASP I 67 74.40 52.54
REMARK 500 LEU I 68 30.83 78.81
REMARK 500 ARG I 228 -14.18 67.29
REMARK 500 LEU I 229 -7.29 58.25
REMARK 500 PRO I 231 63.40 -66.15
REMARK 500 THR I 248 -96.22 -105.93
REMARK 500 SER I 271 -142.48 72.20
REMARK 500 SER I 319 -116.19 57.37
REMARK 500 PRO I 439 73.69 -69.05
REMARK 500 ASP I 458 -129.15 50.49
REMARK 500 GLN I 560 141.85 -179.46
REMARK 500 PRO G 176 82.31 -66.67
REMARK 500 GLN G 354 39.33 -146.25
REMARK 500 GLU G 357 -107.34 10.10
REMARK 500 ASP G 363 21.84 -140.04
REMARK 500 LYS H 103 -54.41 -127.57
REMARK 500 ARG H 228 -19.87 75.27
REMARK 500 LEU H 229 8.04 58.60
REMARK 500 SER H 271 -123.34 63.22
REMARK 500 PHE H 273 114.25 -179.21
REMARK 500 SER H 319 -129.96 68.09
REMARK 500 GLU H 457 -59.64 -124.82
REMARK 500 ARG H 459 -15.34 79.74
REMARK 500 PHE H 460 74.99 54.84
REMARK 500 ALA A 47 63.62 -151.55
REMARK 500 ALA A 79 39.05 -154.01
REMARK 500 ASP D 285 32.88 -94.91
REMARK 500 VAL D 298 -64.08 -122.82
REMARK 500 PRO B 69 -14.52 -48.84
REMARK 500 ALA B 79 38.25 -153.93
REMARK 500 MET B 256 74.20 -113.08
REMARK 500 ALA E 47 62.55 -152.57
REMARK 500 ASP E 70 21.31 -154.47
REMARK 500 ALA C 79 45.23 -156.17
REMARK 500 MET C 256 78.35 -113.73
REMARK 500 ASP F 10 -129.43 46.02
REMARK 500 ALA F 47 67.01 -154.27
REMARK 500 ALA F 79 -27.75 -142.60
REMARK 500 MET F 256 71.83 -117.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-9341 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9342 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9343 RELATED DB: EMDB
DBREF 6N38 I 1 587 UNP D3GUX3 D3GUX3_ECO44 1 587
DBREF 6N38 G 64 366 UNP D3GUX4 D3GUX4_ECO44 31 333
DBREF 6N38 H 1 587 UNP D3GUX3 D3GUX3_ECO44 1 587
DBREF 6N38 K 1 21 PDB 6N38 6N38 1 21
DBREF 6N38 L 1 21 PDB 6N38 6N38 1 21
DBREF 6N38 A 1 316 UNP D3GU39 D3GU39_ECO44 1 316
DBREF 6N38 D 1 316 UNP D3GU39 D3GU39_ECO44 1 316
DBREF 6N38 B 1 316 UNP D3GU39 D3GU39_ECO44 1 316
DBREF 6N38 E 1 316 UNP D3GU39 D3GU39_ECO44 1 316
DBREF 6N38 C 1 316 UNP D3GU39 D3GU39_ECO44 1 316
DBREF 6N38 F 1 316 UNP D3GU39 D3GU39_ECO44 1 316
SEQADV 6N38 HIS A 317 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS A 318 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS A 319 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS A 320 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS A 321 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS A 322 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS D 317 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS D 318 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS D 319 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS D 320 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS D 321 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS D 322 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS B 317 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS B 318 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS B 319 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS B 320 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS B 321 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS B 322 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS E 317 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS E 318 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS E 319 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS E 320 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS E 321 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS E 322 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS C 317 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS C 318 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS C 319 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS C 320 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS C 321 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS C 322 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS F 317 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS F 318 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS F 319 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS F 320 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS F 321 UNP D3GU39 EXPRESSION TAG
SEQADV 6N38 HIS F 322 UNP D3GU39 EXPRESSION TAG
SEQRES 1 I 587 MET ASP ASP LEU THR LEU ARG TYR PHE ASP ALA GLU MET
SEQRES 2 I 587 ARG TYR LEU ARG GLU ALA GLY LYS ALA PHE ALA GLN ALA
SEQRES 3 I 587 HIS PRO ASP ARG ALA ALA MET LEU ASP LEU ASP LYS ALA
SEQRES 4 I 587 GLY THR PRO ASP PRO CYS VAL GLU ARG LEU PHE GLU GLY
SEQRES 5 I 587 PHE ALA PHE SER MET GLY ARG LEU ARG GLN LYS ILE ASP
SEQRES 6 I 587 ASP ASP LEU PRO GLU LEU THR GLU SER LEU VAL SER MET
SEQRES 7 I 587 LEU TRP PRO HIS TYR LEU ARG THR ILE PRO SER LEU SER
SEQRES 8 I 587 VAL VAL ALA LEU THR PRO ARG LEU SER VAL MET LYS MET
SEQRES 9 I 587 ALA GLU THR VAL PRO ALA GLY LEU GLU VAL THR SER ARG
SEQRES 10 I 587 PRO VAL GLY PRO GLY ASN THR VAL CYS ARG TYR ARG THR
SEQRES 11 I 587 THR ARG ALA ILE PRO LEU ASN PRO LEU ALA VAL GLU LYS
SEQRES 12 I 587 VAL VAL MET THR THR GLU PRO ASP GLY ARG SER VAL LEU
SEQRES 13 I 587 LYS ILE GLY PHE ALA CYS SER GLU LEU ALA ASP TRP SER
SEQRES 14 I 587 GLN VAL ASP LEU HIS ARG LEU SER LEU TYR LEU ALA ALA
SEQRES 15 I 587 GLU ALA PRO VAL SER SER THR LEU HIS LEU MET MET THR
SEQRES 16 I 587 LYS ARG LEU ALA ALA LEU TYR LEU ARG LEU PRO GLY ASN
SEQRES 17 I 587 ASP GLU ARG ILE ARG ILE ASP GLY TRP PHE SER PRO GLY
SEQRES 18 I 587 GLY PHE ALA GLU GLU ASP ARG LEU TRP PRO LYS GLY ASP
SEQRES 19 I 587 SER ALA PHE SER GLY TYR GLN LEU LEU LEU GLU TYR PHE
SEQRES 20 I 587 THR PHE ARG GLU LYS PHE MET PHE VAL HIS LEU ASN GLY
SEQRES 21 I 587 LEU GLU ASN VAL SER LEU PRO ALA GLY ILE SER GLY PHE
SEQRES 22 I 587 ASP LEU GLU VAL VAL LEU SER GLN PRO TRP PRO ALA ASP
SEQRES 23 I 587 LEU PRO VAL THR ASP ASP ALA LEU CYS LEU HIS CYS VAL
SEQRES 24 I 587 PRO VAL ILE ASN LEU PHE THR LEU GLU ALA ASP PRO LEU
SEQRES 25 I 587 ILE ILE ASN GLY LEU GLU SER GLU TYR LEU LEU ARG PRO
SEQRES 26 I 587 LYS ARG LEU GLN ASP GLY TYR THR GLU ILE TYR SER VAL
SEQRES 27 I 587 ASP ALA VAL THR GLY SER GLY ARG THR GLY SER ALA GLU
SEQRES 28 I 587 TYR VAL PRO PHE THR SER PHE ARG HIS ARG GLY GLY MET
SEQRES 29 I 587 LEU ARG HIS ASP ALA PRO GLU ARG TYR TYR HIS THR ARG
SEQRES 30 I 587 VAL LYS ARG GLY VAL THR GLY MET TYR ASP THR TRP LEU
SEQRES 31 I 587 ILE LEU GLY GLY GLN ARG TRP GLU ALA ASP ARG MET PRO
SEQRES 32 I 587 GLU ARG GLU THR LEU SER LEU ARG ILE THR GLY THR ASN
SEQRES 33 I 587 GLY GLN LEU PRO ARG ARG ALA LEU GLN SER THR LEU LEU
SEQRES 34 I 587 ASP ARG CYS GLU GLN VAL LEU GLN ALA PRO VAL SER VAL
SEQRES 35 I 587 ARG ASN LEU CYS LYS PRO THR LEU PRO VAL TYR PRO PRO
SEQRES 36 I 587 THR GLU ASP ARG PHE HIS TRP ARG VAL MET SER HIS LEU
SEQRES 37 I 587 GLY THR GLY PHE LEU ASN MET LEU SER SER ALA GLU VAL
SEQRES 38 I 587 LEU ARG GLY THR LEU ALA LEU TYR ASN TRP ARG ASP ASP
SEQRES 39 I 587 GLU LEU ASN HIS ARG ARG LEU ASP ALA ILE LEU ALA VAL
SEQRES 40 I 587 GLN HIS HIS ARG ILE GLN ARG PHE GLU LYS GLY PHE LEU
SEQRES 41 I 587 LEU ARG GLY LEU ASP VAL GLU VAL THR LEU ASP GLY ASN
SEQRES 42 I 587 GLY PHE ALA GLY GLU GLY ASP ILE HIS LEU PHE GLY GLU
SEQRES 43 I 587 MET LEU ASN ARG PHE LEU ALA LEU TYR ALA ASP MET ASN
SEQRES 44 I 587 GLN PHE ASN GLN LEU THR LEU ILE VAL GLN PRO GLU GLY
SEQRES 45 I 587 LYS CYS ILE ARG TRP LYS GLU ASN HIS ASN PRO ARG LEU
SEQRES 46 I 587 PRO GLY
SEQRES 1 G 303 MET GLY PHE PRO ALA SER GLU ILE LYS ASP ALA VAL ILE
SEQRES 2 G 303 PRO GLU GLU SER HIS LEU PRO PRO ILE VAL HIS VAL THR
SEQRES 3 G 303 PHE MET GLY LEU TYR GLY VAL THR SER PRO LEU PRO ALA
SEQRES 4 G 303 HIS TYR ILE SER ASP ILE ALA GLN GLN ARG GLU GLY HIS
SEQRES 5 G 303 GLU ALA ALA ALA ASP PHE LEU ASP ILE PHE SER HIS ARG
SEQRES 6 G 303 LEU ILE THR GLN TYR TYR ARG ILE TRP ARG LYS TYR SER
SEQRES 7 G 303 TYR PRO ALA THR PHE GLU ALA GLY GLY GLN ASP LYS THR
SEQRES 8 G 303 SER GLN TYR LEU LEU GLY LEU ALA ARG LEU GLY ILE PRO
SEQRES 9 G 303 GLY CYS ALA GLN ASN ILE ALA THR PRO VAL SER ARG PHE
SEQRES 10 G 303 LEU ALA LEU LEU PRO LEU MET LEU LEU PRO GLY ARG THR
SEQRES 11 G 303 ALA GLU GLY LEU THR SER LEU VAL THR LEU LEU ALA PRO
SEQRES 12 G 303 GLY THR GLN ALA ARG VAL TRP HIS HIS ASP ARG ARG ARG
SEQRES 13 G 303 ILE PRO LEU LYS THR PRO LEU THR MET ARG VAL HIS HIS
SEQRES 14 G 303 PRO VAL SER LEU LYS SER ARG PRO VAL MET GLY ASP HIS
SEQRES 15 G 303 ALA THR ASP VAL ASN GLY GLN VAL LEU LEU GLN LEU SER
SEQRES 16 G 303 THR GLN THR GLY SER GLU VAL GLN GLY TRP LEU PRO GLY
SEQRES 17 G 303 GLY HIS LEU TYR SER ASP LEU LEU ALA LEU LEU HIS VAL
SEQRES 18 G 303 TYR LEU GLY SER ARG LEU ASP VAL ARG LEU GLN LEU CYS
SEQRES 19 G 303 VAL GLU ARG SER LEU LEU PRO ASP ALA ARG LEU SER CYS
SEQRES 20 G 303 ARG PRO ALA ALA GLY SER PRO GLN LEU GLY ARG THR ALA
SEQRES 21 G 303 VAL MET ARG THR GLN ALA LYS ILE ALA THR SER ALA ALA
SEQRES 22 G 303 ARG VAL MET THR ILE SER LEU GLY ARG TYR GLN ARG VAL
SEQRES 23 G 303 GLN GLU HIS TYR GLN ARG LYS GLU THR GLN GLU ASN GLY
SEQRES 24 G 303 ASP TYR ARG TRP
SEQRES 1 H 587 MET ASP ASP LEU THR LEU ARG TYR PHE ASP ALA GLU MET
SEQRES 2 H 587 ARG TYR LEU ARG GLU ALA GLY LYS ALA PHE ALA GLN ALA
SEQRES 3 H 587 HIS PRO ASP ARG ALA ALA MET LEU ASP LEU ASP LYS ALA
SEQRES 4 H 587 GLY THR PRO ASP PRO CYS VAL GLU ARG LEU PHE GLU GLY
SEQRES 5 H 587 PHE ALA PHE SER MET GLY ARG LEU ARG GLN LYS ILE ASP
SEQRES 6 H 587 ASP ASP LEU PRO GLU LEU THR GLU SER LEU VAL SER MET
SEQRES 7 H 587 LEU TRP PRO HIS TYR LEU ARG THR ILE PRO SER LEU SER
SEQRES 8 H 587 VAL VAL ALA LEU THR PRO ARG LEU SER VAL MET LYS MET
SEQRES 9 H 587 ALA GLU THR VAL PRO ALA GLY LEU GLU VAL THR SER ARG
SEQRES 10 H 587 PRO VAL GLY PRO GLY ASN THR VAL CYS ARG TYR ARG THR
SEQRES 11 H 587 THR ARG ALA ILE PRO LEU ASN PRO LEU ALA VAL GLU LYS
SEQRES 12 H 587 VAL VAL MET THR THR GLU PRO ASP GLY ARG SER VAL LEU
SEQRES 13 H 587 LYS ILE GLY PHE ALA CYS SER GLU LEU ALA ASP TRP SER
SEQRES 14 H 587 GLN VAL ASP LEU HIS ARG LEU SER LEU TYR LEU ALA ALA
SEQRES 15 H 587 GLU ALA PRO VAL SER SER THR LEU HIS LEU MET MET THR
SEQRES 16 H 587 LYS ARG LEU ALA ALA LEU TYR LEU ARG LEU PRO GLY ASN
SEQRES 17 H 587 ASP GLU ARG ILE ARG ILE ASP GLY TRP PHE SER PRO GLY
SEQRES 18 H 587 GLY PHE ALA GLU GLU ASP ARG LEU TRP PRO LYS GLY ASP
SEQRES 19 H 587 SER ALA PHE SER GLY TYR GLN LEU LEU LEU GLU TYR PHE
SEQRES 20 H 587 THR PHE ARG GLU LYS PHE MET PHE VAL HIS LEU ASN GLY
SEQRES 21 H 587 LEU GLU ASN VAL SER LEU PRO ALA GLY ILE SER GLY PHE
SEQRES 22 H 587 ASP LEU GLU VAL VAL LEU SER GLN PRO TRP PRO ALA ASP
SEQRES 23 H 587 LEU PRO VAL THR ASP ASP ALA LEU CYS LEU HIS CYS VAL
SEQRES 24 H 587 PRO VAL ILE ASN LEU PHE THR LEU GLU ALA ASP PRO LEU
SEQRES 25 H 587 ILE ILE ASN GLY LEU GLU SER GLU TYR LEU LEU ARG PRO
SEQRES 26 H 587 LYS ARG LEU GLN ASP GLY TYR THR GLU ILE TYR SER VAL
SEQRES 27 H 587 ASP ALA VAL THR GLY SER GLY ARG THR GLY SER ALA GLU
SEQRES 28 H 587 TYR VAL PRO PHE THR SER PHE ARG HIS ARG GLY GLY MET
SEQRES 29 H 587 LEU ARG HIS ASP ALA PRO GLU ARG TYR TYR HIS THR ARG
SEQRES 30 H 587 VAL LYS ARG GLY VAL THR GLY MET TYR ASP THR TRP LEU
SEQRES 31 H 587 ILE LEU GLY GLY GLN ARG TRP GLU ALA ASP ARG MET PRO
SEQRES 32 H 587 GLU ARG GLU THR LEU SER LEU ARG ILE THR GLY THR ASN
SEQRES 33 H 587 GLY GLN LEU PRO ARG ARG ALA LEU GLN SER THR LEU LEU
SEQRES 34 H 587 ASP ARG CYS GLU GLN VAL LEU GLN ALA PRO VAL SER VAL
SEQRES 35 H 587 ARG ASN LEU CYS LYS PRO THR LEU PRO VAL TYR PRO PRO
SEQRES 36 H 587 THR GLU ASP ARG PHE HIS TRP ARG VAL MET SER HIS LEU
SEQRES 37 H 587 GLY THR GLY PHE LEU ASN MET LEU SER SER ALA GLU VAL
SEQRES 38 H 587 LEU ARG GLY THR LEU ALA LEU TYR ASN TRP ARG ASP ASP
SEQRES 39 H 587 GLU LEU ASN HIS ARG ARG LEU ASP ALA ILE LEU ALA VAL
SEQRES 40 H 587 GLN HIS HIS ARG ILE GLN ARG PHE GLU LYS GLY PHE LEU
SEQRES 41 H 587 LEU ARG GLY LEU ASP VAL GLU VAL THR LEU ASP GLY ASN
SEQRES 42 H 587 GLY PHE ALA GLY GLU GLY ASP ILE HIS LEU PHE GLY GLU
SEQRES 43 H 587 MET LEU ASN ARG PHE LEU ALA LEU TYR ALA ASP MET ASN
SEQRES 44 H 587 GLN PHE ASN GLN LEU THR LEU ILE VAL GLN PRO GLU GLY
SEQRES 45 H 587 LYS CYS ILE ARG TRP LYS GLU ASN HIS ASN PRO ARG LEU
SEQRES 46 H 587 PRO GLY
SEQRES 1 K 21 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 K 21 UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 L 21 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 L 21 UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 A 322 MET LYS ILE TYR ARG PRO LEU TRP GLU ASP GLY ALA PHE
SEQRES 2 A 322 LEU MET PRO GLN GLN PHE GLN GLN GLN ALA ALA TRP ASP
SEQRES 3 A 322 VAL HIS LEU ALA ASP SER VAL ALA ARG MET GLY LEU ALA
SEQRES 4 A 322 HIS PRO TRP GLY VAL VAL ALA ALA GLU PHE ASP ASP SER
SEQRES 5 A 322 LEU LEU PRO LEU SER ARG LEU ASN ALA THR ARG LEU ILE
SEQRES 6 A 322 VAL ARG PHE PRO ASP GLY THR LEU ILE ASP THR GLU ARG
SEQRES 7 A 322 ALA ASP ASN LEU PRO PRO VAL CYS ASP LEU SER THR VAL
SEQRES 8 A 322 SER ASP ARG SER LEU VAL ASP ILE VAL LEU ALA LEU PRO
SEQRES 9 A 322 LEU LEU ASN ALA ASN GLY GLY ASN LEU ASP ASN GLY SER
SEQRES 10 A 322 GLU SER GLU ARG PRO ARG ARG TRP LYS SER GLU ARG VAL
SEQRES 11 A 322 ASN VAL GLN GLU LEU ALA GLY HIS GLU GLN SER GLU VAL
SEQRES 12 A 322 ALA VAL LEU ARG HIS ASN LEU THR LEU ARG MET ALA HIS
SEQRES 13 A 322 GLN GLU ASN ALA ALA TRP LEU THR CYS PRO VAL THR ARG
SEQRES 14 A 322 LEU VAL ARG ASP ALA GLN GLY GLN TRP CYS ARG ASP PRO
SEQRES 15 A 322 ARG PHE ILE PRO PRO LEU LEU THR LEU SER ALA SER PRO
SEQRES 16 A 322 SER LEU MET THR GLU LEU ALA GLU LEU LEU HIS HIS LEU
SEQRES 17 A 322 GLN ALA ARG ARG GLN ARG LEU MET SER MET ARG ARG GLU
SEQRES 18 A 322 ASN ASN ALA ARG LEU ALA ASP PHE ALA VAL ALA ASP VAL
SEQRES 19 A 322 SER LEU PHE TRP LEU LEU ASN ALA LEU ASN SER ALA GLU
SEQRES 20 A 322 PRO VAL LEU LYS GLU LEU LEU ASP MET PRO TYR ARG HIS
SEQRES 21 A 322 PRO GLU LEU LEU TYR ARG GLU LEU ALA ARG LEU ALA GLY
SEQRES 22 A 322 SER LEU LEU THR PHE SER LEU GLU HIS ASN VAL ASP ALA
SEQRES 23 A 322 VAL PRO ALA TYR HIS HIS GLU THR PRO GLU ASN VAL PHE
SEQRES 24 A 322 PRO PRO LEU LEU SER LEU LEU ASN ARG LEU LEU GLU ALA
SEQRES 25 A 322 SER LEU PRO SER HIS HIS HIS HIS HIS HIS
SEQRES 1 D 322 MET LYS ILE TYR ARG PRO LEU TRP GLU ASP GLY ALA PHE
SEQRES 2 D 322 LEU MET PRO GLN GLN PHE GLN GLN GLN ALA ALA TRP ASP
SEQRES 3 D 322 VAL HIS LEU ALA ASP SER VAL ALA ARG MET GLY LEU ALA
SEQRES 4 D 322 HIS PRO TRP GLY VAL VAL ALA ALA GLU PHE ASP ASP SER
SEQRES 5 D 322 LEU LEU PRO LEU SER ARG LEU ASN ALA THR ARG LEU ILE
SEQRES 6 D 322 VAL ARG PHE PRO ASP GLY THR LEU ILE ASP THR GLU ARG
SEQRES 7 D 322 ALA ASP ASN LEU PRO PRO VAL CYS ASP LEU SER THR VAL
SEQRES 8 D 322 SER ASP ARG SER LEU VAL ASP ILE VAL LEU ALA LEU PRO
SEQRES 9 D 322 LEU LEU ASN ALA ASN GLY GLY ASN LEU ASP ASN GLY SER
SEQRES 10 D 322 GLU SER GLU ARG PRO ARG ARG TRP LYS SER GLU ARG VAL
SEQRES 11 D 322 ASN VAL GLN GLU LEU ALA GLY HIS GLU GLN SER GLU VAL
SEQRES 12 D 322 ALA VAL LEU ARG HIS ASN LEU THR LEU ARG MET ALA HIS
SEQRES 13 D 322 GLN GLU ASN ALA ALA TRP LEU THR CYS PRO VAL THR ARG
SEQRES 14 D 322 LEU VAL ARG ASP ALA GLN GLY GLN TRP CYS ARG ASP PRO
SEQRES 15 D 322 ARG PHE ILE PRO PRO LEU LEU THR LEU SER ALA SER PRO
SEQRES 16 D 322 SER LEU MET THR GLU LEU ALA GLU LEU LEU HIS HIS LEU
SEQRES 17 D 322 GLN ALA ARG ARG GLN ARG LEU MET SER MET ARG ARG GLU
SEQRES 18 D 322 ASN ASN ALA ARG LEU ALA ASP PHE ALA VAL ALA ASP VAL
SEQRES 19 D 322 SER LEU PHE TRP LEU LEU ASN ALA LEU ASN SER ALA GLU
SEQRES 20 D 322 PRO VAL LEU LYS GLU LEU LEU ASP MET PRO TYR ARG HIS
SEQRES 21 D 322 PRO GLU LEU LEU TYR ARG GLU LEU ALA ARG LEU ALA GLY
SEQRES 22 D 322 SER LEU LEU THR PHE SER LEU GLU HIS ASN VAL ASP ALA
SEQRES 23 D 322 VAL PRO ALA TYR HIS HIS GLU THR PRO GLU ASN VAL PHE
SEQRES 24 D 322 PRO PRO LEU LEU SER LEU LEU ASN ARG LEU LEU GLU ALA
SEQRES 25 D 322 SER LEU PRO SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 322 MET LYS ILE TYR ARG PRO LEU TRP GLU ASP GLY ALA PHE
SEQRES 2 B 322 LEU MET PRO GLN GLN PHE GLN GLN GLN ALA ALA TRP ASP
SEQRES 3 B 322 VAL HIS LEU ALA ASP SER VAL ALA ARG MET GLY LEU ALA
SEQRES 4 B 322 HIS PRO TRP GLY VAL VAL ALA ALA GLU PHE ASP ASP SER
SEQRES 5 B 322 LEU LEU PRO LEU SER ARG LEU ASN ALA THR ARG LEU ILE
SEQRES 6 B 322 VAL ARG PHE PRO ASP GLY THR LEU ILE ASP THR GLU ARG
SEQRES 7 B 322 ALA ASP ASN LEU PRO PRO VAL CYS ASP LEU SER THR VAL
SEQRES 8 B 322 SER ASP ARG SER LEU VAL ASP ILE VAL LEU ALA LEU PRO
SEQRES 9 B 322 LEU LEU ASN ALA ASN GLY GLY ASN LEU ASP ASN GLY SER
SEQRES 10 B 322 GLU SER GLU ARG PRO ARG ARG TRP LYS SER GLU ARG VAL
SEQRES 11 B 322 ASN VAL GLN GLU LEU ALA GLY HIS GLU GLN SER GLU VAL
SEQRES 12 B 322 ALA VAL LEU ARG HIS ASN LEU THR LEU ARG MET ALA HIS
SEQRES 13 B 322 GLN GLU ASN ALA ALA TRP LEU THR CYS PRO VAL THR ARG
SEQRES 14 B 322 LEU VAL ARG ASP ALA GLN GLY GLN TRP CYS ARG ASP PRO
SEQRES 15 B 322 ARG PHE ILE PRO PRO LEU LEU THR LEU SER ALA SER PRO
SEQRES 16 B 322 SER LEU MET THR GLU LEU ALA GLU LEU LEU HIS HIS LEU
SEQRES 17 B 322 GLN ALA ARG ARG GLN ARG LEU MET SER MET ARG ARG GLU
SEQRES 18 B 322 ASN ASN ALA ARG LEU ALA ASP PHE ALA VAL ALA ASP VAL
SEQRES 19 B 322 SER LEU PHE TRP LEU LEU ASN ALA LEU ASN SER ALA GLU
SEQRES 20 B 322 PRO VAL LEU LYS GLU LEU LEU ASP MET PRO TYR ARG HIS
SEQRES 21 B 322 PRO GLU LEU LEU TYR ARG GLU LEU ALA ARG LEU ALA GLY
SEQRES 22 B 322 SER LEU LEU THR PHE SER LEU GLU HIS ASN VAL ASP ALA
SEQRES 23 B 322 VAL PRO ALA TYR HIS HIS GLU THR PRO GLU ASN VAL PHE
SEQRES 24 B 322 PRO PRO LEU LEU SER LEU LEU ASN ARG LEU LEU GLU ALA
SEQRES 25 B 322 SER LEU PRO SER HIS HIS HIS HIS HIS HIS
SEQRES 1 E 322 MET LYS ILE TYR ARG PRO LEU TRP GLU ASP GLY ALA PHE
SEQRES 2 E 322 LEU MET PRO GLN GLN PHE GLN GLN GLN ALA ALA TRP ASP
SEQRES 3 E 322 VAL HIS LEU ALA ASP SER VAL ALA ARG MET GLY LEU ALA
SEQRES 4 E 322 HIS PRO TRP GLY VAL VAL ALA ALA GLU PHE ASP ASP SER
SEQRES 5 E 322 LEU LEU PRO LEU SER ARG LEU ASN ALA THR ARG LEU ILE
SEQRES 6 E 322 VAL ARG PHE PRO ASP GLY THR LEU ILE ASP THR GLU ARG
SEQRES 7 E 322 ALA ASP ASN LEU PRO PRO VAL CYS ASP LEU SER THR VAL
SEQRES 8 E 322 SER ASP ARG SER LEU VAL ASP ILE VAL LEU ALA LEU PRO
SEQRES 9 E 322 LEU LEU ASN ALA ASN GLY GLY ASN LEU ASP ASN GLY SER
SEQRES 10 E 322 GLU SER GLU ARG PRO ARG ARG TRP LYS SER GLU ARG VAL
SEQRES 11 E 322 ASN VAL GLN GLU LEU ALA GLY HIS GLU GLN SER GLU VAL
SEQRES 12 E 322 ALA VAL LEU ARG HIS ASN LEU THR LEU ARG MET ALA HIS
SEQRES 13 E 322 GLN GLU ASN ALA ALA TRP LEU THR CYS PRO VAL THR ARG
SEQRES 14 E 322 LEU VAL ARG ASP ALA GLN GLY GLN TRP CYS ARG ASP PRO
SEQRES 15 E 322 ARG PHE ILE PRO PRO LEU LEU THR LEU SER ALA SER PRO
SEQRES 16 E 322 SER LEU MET THR GLU LEU ALA GLU LEU LEU HIS HIS LEU
SEQRES 17 E 322 GLN ALA ARG ARG GLN ARG LEU MET SER MET ARG ARG GLU
SEQRES 18 E 322 ASN ASN ALA ARG LEU ALA ASP PHE ALA VAL ALA ASP VAL
SEQRES 19 E 322 SER LEU PHE TRP LEU LEU ASN ALA LEU ASN SER ALA GLU
SEQRES 20 E 322 PRO VAL LEU LYS GLU LEU LEU ASP MET PRO TYR ARG HIS
SEQRES 21 E 322 PRO GLU LEU LEU TYR ARG GLU LEU ALA ARG LEU ALA GLY
SEQRES 22 E 322 SER LEU LEU THR PHE SER LEU GLU HIS ASN VAL ASP ALA
SEQRES 23 E 322 VAL PRO ALA TYR HIS HIS GLU THR PRO GLU ASN VAL PHE
SEQRES 24 E 322 PRO PRO LEU LEU SER LEU LEU ASN ARG LEU LEU GLU ALA
SEQRES 25 E 322 SER LEU PRO SER HIS HIS HIS HIS HIS HIS
SEQRES 1 C 322 MET LYS ILE TYR ARG PRO LEU TRP GLU ASP GLY ALA PHE
SEQRES 2 C 322 LEU MET PRO GLN GLN PHE GLN GLN GLN ALA ALA TRP ASP
SEQRES 3 C 322 VAL HIS LEU ALA ASP SER VAL ALA ARG MET GLY LEU ALA
SEQRES 4 C 322 HIS PRO TRP GLY VAL VAL ALA ALA GLU PHE ASP ASP SER
SEQRES 5 C 322 LEU LEU PRO LEU SER ARG LEU ASN ALA THR ARG LEU ILE
SEQRES 6 C 322 VAL ARG PHE PRO ASP GLY THR LEU ILE ASP THR GLU ARG
SEQRES 7 C 322 ALA ASP ASN LEU PRO PRO VAL CYS ASP LEU SER THR VAL
SEQRES 8 C 322 SER ASP ARG SER LEU VAL ASP ILE VAL LEU ALA LEU PRO
SEQRES 9 C 322 LEU LEU ASN ALA ASN GLY GLY ASN LEU ASP ASN GLY SER
SEQRES 10 C 322 GLU SER GLU ARG PRO ARG ARG TRP LYS SER GLU ARG VAL
SEQRES 11 C 322 ASN VAL GLN GLU LEU ALA GLY HIS GLU GLN SER GLU VAL
SEQRES 12 C 322 ALA VAL LEU ARG HIS ASN LEU THR LEU ARG MET ALA HIS
SEQRES 13 C 322 GLN GLU ASN ALA ALA TRP LEU THR CYS PRO VAL THR ARG
SEQRES 14 C 322 LEU VAL ARG ASP ALA GLN GLY GLN TRP CYS ARG ASP PRO
SEQRES 15 C 322 ARG PHE ILE PRO PRO LEU LEU THR LEU SER ALA SER PRO
SEQRES 16 C 322 SER LEU MET THR GLU LEU ALA GLU LEU LEU HIS HIS LEU
SEQRES 17 C 322 GLN ALA ARG ARG GLN ARG LEU MET SER MET ARG ARG GLU
SEQRES 18 C 322 ASN ASN ALA ARG LEU ALA ASP PHE ALA VAL ALA ASP VAL
SEQRES 19 C 322 SER LEU PHE TRP LEU LEU ASN ALA LEU ASN SER ALA GLU
SEQRES 20 C 322 PRO VAL LEU LYS GLU LEU LEU ASP MET PRO TYR ARG HIS
SEQRES 21 C 322 PRO GLU LEU LEU TYR ARG GLU LEU ALA ARG LEU ALA GLY
SEQRES 22 C 322 SER LEU LEU THR PHE SER LEU GLU HIS ASN VAL ASP ALA
SEQRES 23 C 322 VAL PRO ALA TYR HIS HIS GLU THR PRO GLU ASN VAL PHE
SEQRES 24 C 322 PRO PRO LEU LEU SER LEU LEU ASN ARG LEU LEU GLU ALA
SEQRES 25 C 322 SER LEU PRO SER HIS HIS HIS HIS HIS HIS
SEQRES 1 F 322 MET LYS ILE TYR ARG PRO LEU TRP GLU ASP GLY ALA PHE
SEQRES 2 F 322 LEU MET PRO GLN GLN PHE GLN GLN GLN ALA ALA TRP ASP
SEQRES 3 F 322 VAL HIS LEU ALA ASP SER VAL ALA ARG MET GLY LEU ALA
SEQRES 4 F 322 HIS PRO TRP GLY VAL VAL ALA ALA GLU PHE ASP ASP SER
SEQRES 5 F 322 LEU LEU PRO LEU SER ARG LEU ASN ALA THR ARG LEU ILE
SEQRES 6 F 322 VAL ARG PHE PRO ASP GLY THR LEU ILE ASP THR GLU ARG
SEQRES 7 F 322 ALA ASP ASN LEU PRO PRO VAL CYS ASP LEU SER THR VAL
SEQRES 8 F 322 SER ASP ARG SER LEU VAL ASP ILE VAL LEU ALA LEU PRO
SEQRES 9 F 322 LEU LEU ASN ALA ASN GLY GLY ASN LEU ASP ASN GLY SER
SEQRES 10 F 322 GLU SER GLU ARG PRO ARG ARG TRP LYS SER GLU ARG VAL
SEQRES 11 F 322 ASN VAL GLN GLU LEU ALA GLY HIS GLU GLN SER GLU VAL
SEQRES 12 F 322 ALA VAL LEU ARG HIS ASN LEU THR LEU ARG MET ALA HIS
SEQRES 13 F 322 GLN GLU ASN ALA ALA TRP LEU THR CYS PRO VAL THR ARG
SEQRES 14 F 322 LEU VAL ARG ASP ALA GLN GLY GLN TRP CYS ARG ASP PRO
SEQRES 15 F 322 ARG PHE ILE PRO PRO LEU LEU THR LEU SER ALA SER PRO
SEQRES 16 F 322 SER LEU MET THR GLU LEU ALA GLU LEU LEU HIS HIS LEU
SEQRES 17 F 322 GLN ALA ARG ARG GLN ARG LEU MET SER MET ARG ARG GLU
SEQRES 18 F 322 ASN ASN ALA ARG LEU ALA ASP PHE ALA VAL ALA ASP VAL
SEQRES 19 F 322 SER LEU PHE TRP LEU LEU ASN ALA LEU ASN SER ALA GLU
SEQRES 20 F 322 PRO VAL LEU LYS GLU LEU LEU ASP MET PRO TYR ARG HIS
SEQRES 21 F 322 PRO GLU LEU LEU TYR ARG GLU LEU ALA ARG LEU ALA GLY
SEQRES 22 F 322 SER LEU LEU THR PHE SER LEU GLU HIS ASN VAL ASP ALA
SEQRES 23 F 322 VAL PRO ALA TYR HIS HIS GLU THR PRO GLU ASN VAL PHE
SEQRES 24 F 322 PRO PRO LEU LEU SER LEU LEU ASN ARG LEU LEU GLU ALA
SEQRES 25 F 322 SER LEU PRO SER HIS HIS HIS HIS HIS HIS
HELIX 1 AA1 GLU I 47 ASP I 67 1 21
HELIX 2 AA2 LEU I 68 SER I 77 1 10
HELIX 3 AA3 GLU I 183 LYS I 196 1 14
HELIX 4 AA4 PHE I 237 THR I 248 1 12
HELIX 5 AA5 PHE I 249 PHE I 253 5 5
HELIX 6 AA6 LEU I 261 VAL I 264 5 4
HELIX 7 AA7 THR I 290 ASP I 292 5 3
HELIX 8 AA8 ARG I 327 GLY I 331 5 5
HELIX 9 AA9 PHE I 355 HIS I 360 1 6
HELIX 10 AB1 MET I 364 ALA I 369 1 6
HELIX 11 AB2 PRO I 420 SER I 426 1 7
HELIX 12 AB3 ARG I 459 GLY I 469 1 11
HELIX 13 AB4 THR I 470 LEU I 476 5 7
HELIX 14 AB5 SER I 478 ALA I 487 1 10
HELIX 15 AB6 LEU I 488 ASN I 490 5 3
HELIX 16 AB7 ASP I 494 ASP I 502 1 9
HELIX 17 AB8 GLY I 532 PHE I 535 5 4
HELIX 18 AB9 ALA I 536 ALA I 553 1 18
HELIX 19 AC1 LEU I 554 ALA I 556 5 3
HELIX 20 AC2 ASP G 123 TYR G 140 1 18
HELIX 21 AC3 SER G 141 PHE G 146 5 6
HELIX 22 AC4 ASP G 152 ALA G 162 1 11
HELIX 23 AC5 CYS G 169 ILE G 173 5 5
HELIX 24 AC6 PRO G 176 MET G 187 5 12
HELIX 25 AC7 THR G 193 ALA G 205 1 13
HELIX 26 AC8 SER G 235 ARG G 239 5 5
HELIX 27 AC9 THR G 261 LEU G 269 1 9
HELIX 28 AD1 GLY G 272 LEU G 286 1 15
HELIX 29 AD2 SER G 301 LEU G 303 5 3
HELIX 30 AD3 VAL H 46 ASP H 65 1 20
HELIX 31 AD4 ASP H 67 TRP H 80 1 14
HELIX 32 AD5 GLY H 120 THR H 124 5 5
HELIX 33 AD6 GLU H 183 ARG H 197 1 15
HELIX 34 AD7 PHE H 237 PHE H 249 1 13
HELIX 35 AD8 ARG H 250 PHE H 253 5 4
HELIX 36 AD9 LEU H 261 VAL H 264 5 4
HELIX 37 AE1 THR H 290 ASP H 292 5 3
HELIX 38 AE2 ARG H 359 MET H 364 1 6
HELIX 39 AE3 PRO H 420 GLN H 425 1 6
HELIX 40 AE4 PHE H 460 GLY H 471 1 12
HELIX 41 AE5 SER H 478 LEU H 488 1 11
HELIX 42 AE6 ASP H 494 ASP H 502 1 9
HELIX 43 AE7 GLY H 532 PHE H 535 5 4
HELIX 44 AE8 ALA H 536 LEU H 554 1 19
HELIX 45 AE9 UNK K 2 UNK K 20 1 19
HELIX 46 AF1 UNK L 2 UNK L 18 1 17
HELIX 47 AF2 MET A 15 ARG A 35 1 21
HELIX 48 AF3 ASP A 51 LEU A 56 5 6
HELIX 49 AF4 SER A 89 SER A 92 5 4
HELIX 50 AF5 THR A 190 ALA A 193 5 4
HELIX 51 AF6 SER A 194 ARG A 219 1 26
HELIX 52 AF7 ASP A 233 MET A 256 1 24
HELIX 53 AF8 HIS A 260 LEU A 276 1 17
HELIX 54 AF9 ASN A 283 VAL A 287 5 5
HELIX 55 AG1 THR A 294 ASN A 297 5 4
HELIX 56 AG2 VAL A 298 ALA A 312 1 15
HELIX 57 AG3 MET D 15 ARG D 35 1 21
HELIX 58 AG4 ASP D 51 LEU D 56 5 6
HELIX 59 AG5 SER D 89 SER D 92 5 4
HELIX 60 AG6 THR D 190 ALA D 193 5 4
HELIX 61 AG7 SER D 194 SER D 217 1 24
HELIX 62 AG8 ASP D 233 MET D 256 1 24
HELIX 63 AG9 PRO D 261 LEU D 276 1 16
HELIX 64 AH1 THR D 294 ASN D 297 5 4
HELIX 65 AH2 VAL D 298 ALA D 312 1 15
HELIX 66 AH3 MET B 15 ARG B 35 1 21
HELIX 67 AH4 ASP B 51 LEU B 56 5 6
HELIX 68 AH5 SER B 89 SER B 92 5 4
HELIX 69 AH6 THR B 190 ALA B 193 5 4
HELIX 70 AH7 SER B 194 MET B 218 1 25
HELIX 71 AH8 VAL B 234 MET B 256 1 23
HELIX 72 AH9 HIS B 260 LEU B 276 1 17
HELIX 73 AI1 THR B 294 ASN B 297 5 4
HELIX 74 AI2 VAL B 298 ALA B 312 1 15
HELIX 75 AI3 MET E 15 ARG E 35 1 21
HELIX 76 AI4 LEU E 53 LEU E 56 5 4
HELIX 77 AI5 SER E 89 VAL E 91 5 3
HELIX 78 AI6 THR E 190 ALA E 193 5 4
HELIX 79 AI7 SER E 194 MET E 218 1 25
HELIX 80 AI8 ASP E 233 MET E 256 1 24
HELIX 81 AI9 HIS E 260 LEU E 276 1 17
HELIX 82 AJ1 ASN E 283 VAL E 287 5 5
HELIX 83 AJ2 THR E 294 ASN E 297 5 4
HELIX 84 AJ3 VAL E 298 GLU E 311 1 14
HELIX 85 AJ4 MET C 15 ARG C 35 1 21
HELIX 86 AJ5 ASP C 51 LEU C 56 5 6
HELIX 87 AJ6 SER C 89 SER C 92 5 4
HELIX 88 AJ7 THR C 190 ALA C 193 5 4
HELIX 89 AJ8 SER C 194 MET C 218 1 25
HELIX 90 AJ9 ASP C 233 MET C 256 1 24
HELIX 91 AK1 HIS C 260 LEU C 276 1 17
HELIX 92 AK2 ASN C 283 VAL C 287 5 5
HELIX 93 AK3 THR C 294 ASN C 297 5 4
HELIX 94 AK4 VAL C 298 ALA C 312 1 15
HELIX 95 AK5 MET F 15 ARG F 35 1 21
HELIX 96 AK6 ASP F 51 LEU F 56 5 6
HELIX 97 AK7 SER F 89 SER F 92 5 4
HELIX 98 AK8 THR F 190 ALA F 193 5 4
HELIX 99 AK9 SER F 194 ARG F 219 1 26
HELIX 100 AL1 ASP F 233 MET F 256 1 24
HELIX 101 AL2 HIS F 260 LEU F 276 1 17
HELIX 102 AL3 THR F 294 ASN F 297 5 4
HELIX 103 AL4 VAL F 298 SER F 313 1 16
SHEET 1 AA1 6 LEU I 429 CYS I 432 0
SHEET 2 AA1 6 GLU I 113 SER I 116 -1 N THR I 115 O ASP I 430
SHEET 3 AA1 6 ARG I 127 THR I 130 -1 O TYR I 128 N VAL I 114
SHEET 4 AA1 6 CYS I 298 ILE I 302 -1 O ILE I 302 N ARG I 129
SHEET 5 AA1 6 LEU I 90 THR I 96 -1 N SER I 91 O VAL I 301
SHEET 6 AA1 6 SER I 441 ASN I 444 -1 O ARG I 443 N ALA I 94
SHEET 1 AA2 2 GLU I 106 VAL I 108 0
SHEET 2 AA2 2 ILE I 134 LEU I 136 -1 O ILE I 134 N VAL I 108
SHEET 1 AA3 4 LEU I 139 THR I 148 0
SHEET 2 AA3 4 SER I 154 CYS I 162 -1 O LYS I 157 N VAL I 145
SHEET 3 AA3 4 SER I 271 LEU I 279 -1 O PHE I 273 N PHE I 160
SHEET 4 AA3 4 LEU I 198 ARG I 204 -1 N ARG I 204 O ASP I 274
SHEET 1 AA4 4 TRP I 217 PRO I 220 0
SHEET 2 AA4 4 PHE I 255 ASN I 259 -1 O HIS I 257 N SER I 219
SHEET 3 AA4 4 ARG I 175 LEU I 180 -1 N LEU I 178 O VAL I 256
SHEET 4 AA4 4 LEU I 294 CYS I 295 -1 O CYS I 295 N TYR I 179
SHEET 1 AA5 3 PHE I 305 LEU I 307 0
SHEET 2 AA5 3 THR I 407 ASN I 416 -1 O GLY I 414 N PHE I 305
SHEET 3 AA5 3 PRO I 311 ILE I 313 -1 N LEU I 312 O LEU I 408
SHEET 1 AA6 4 PHE I 305 LEU I 307 0
SHEET 2 AA6 4 THR I 407 ASN I 416 -1 O GLY I 414 N PHE I 305
SHEET 3 AA6 4 THR I 333 GLY I 345 -1 N ASP I 339 O ARG I 411
SHEET 4 AA6 4 GLY I 348 GLU I 351 -1 O GLY I 348 N GLY I 345
SHEET 1 AA7 4 TYR I 321 LEU I 323 0
SHEET 2 AA7 4 TYR I 386 ILE I 391 -1 O THR I 388 N LEU I 323
SHEET 3 AA7 4 TYR I 373 ARG I 380 -1 N HIS I 375 O ILE I 391
SHEET 4 AA7 4 VAL I 353 PRO I 354 1 N VAL I 353 O TYR I 374
SHEET 1 AA8 5 ILE I 504 GLU I 516 0
SHEET 2 AA8 5 PHE I 519 LEU I 530 -1 O LEU I 521 N ARG I 514
SHEET 3 AA8 5 PHE I 561 VAL I 568 1 O ILE I 567 N LEU I 530
SHEET 4 AA8 5 LYS I 573 ARG I 576 -1 O ILE I 575 N LEU I 566
SHEET 5 AA8 5 GLU G 360 ASN G 361 1 O GLU G 360 N ARG I 576
SHEET 1 AA9 4 GLN G 209 PRO G 221 0
SHEET 2 AA9 4 HIS G 245 SER G 258 -1 O ALA G 246 N ILE G 220
SHEET 3 AA9 4 ASP G 291 GLU G 299 1 O CYS G 297 N LEU G 257
SHEET 4 AA9 4 VAL G 338 TYR G 346 -1 O MET G 339 N VAL G 298
SHEET 1 AB1 6 LEU H 429 CYS H 432 0
SHEET 2 AB1 6 GLU H 113 SER H 116 -1 N THR H 115 O ASP H 430
SHEET 3 AB1 6 ARG H 127 THR H 130 -1 O TYR H 128 N VAL H 114
SHEET 4 AB1 6 CYS H 298 ILE H 302 -1 O ILE H 302 N ARG H 129
SHEET 5 AB1 6 LEU H 90 PRO H 97 -1 N SER H 91 O VAL H 301
SHEET 6 AB1 6 VAL H 440 ASN H 444 -1 O ARG H 443 N ALA H 94
SHEET 1 AB2 2 GLU H 106 VAL H 108 0
SHEET 2 AB2 2 ILE H 134 LEU H 136 -1 O LEU H 136 N GLU H 106
SHEET 1 AB3 5 LEU H 139 THR H 148 0
SHEET 2 AB3 5 SER H 154 CYS H 162 -1 O LYS H 157 N VAL H 145
SHEET 3 AB3 5 ASP H 274 LEU H 279 -1 O VAL H 277 N LEU H 156
SHEET 4 AB3 5 LEU H 198 ARG H 204 -1 N ARG H 204 O ASP H 274
SHEET 5 AB3 5 ARG H 213 ILE H 214 -1 O ILE H 214 N LEU H 201
SHEET 1 AB4 4 TRP H 217 PRO H 220 0
SHEET 2 AB4 4 PHE H 255 ASN H 259 -1 O HIS H 257 N SER H 219
SHEET 3 AB4 4 ARG H 175 LEU H 180 -1 N LEU H 178 O VAL H 256
SHEET 4 AB4 4 LEU H 294 CYS H 295 -1 O CYS H 295 N TYR H 179
SHEET 1 AB5 3 PHE H 305 THR H 306 0
SHEET 2 AB5 3 THR H 407 ASN H 416 -1 O GLY H 414 N PHE H 305
SHEET 3 AB5 3 LEU H 312 ILE H 313 -1 N LEU H 312 O LEU H 408
SHEET 1 AB6 4 PHE H 305 THR H 306 0
SHEET 2 AB6 4 THR H 407 ASN H 416 -1 O GLY H 414 N PHE H 305
SHEET 3 AB6 4 THR H 333 GLY H 345 -1 N GLU H 334 O THR H 415
SHEET 4 AB6 4 GLY H 348 GLU H 351 -1 O ALA H 350 N GLY H 343
SHEET 1 AB7 4 GLU H 320 LEU H 322 0
SHEET 2 AB7 4 TYR H 386 ILE H 391 -1 O LEU H 390 N TYR H 321
SHEET 3 AB7 4 TYR H 373 ARG H 380 -1 N ARG H 377 O TRP H 389
SHEET 4 AB7 4 VAL H 353 PRO H 354 1 N VAL H 353 O TYR H 374
SHEET 1 AB8 4 ILE H 504 GLU H 516 0
SHEET 2 AB8 4 PHE H 519 LEU H 530 -1 O ASP H 525 N HIS H 510
SHEET 3 AB8 4 PHE H 561 VAL H 568 1 O ILE H 567 N LEU H 530
SHEET 4 AB8 4 CYS H 574 TRP H 577 -1 O TRP H 577 N LEU H 564
SHEET 1 AB9 3 GLY A 43 PHE A 49 0
SHEET 2 AB9 3 ALA A 61 ARG A 67 -1 O THR A 62 N GLU A 48
SHEET 3 AB9 3 LEU A 73 ASP A 75 -1 O ILE A 74 N VAL A 66
SHEET 1 AC1 2 ARG A 58 LEU A 59 0
SHEET 2 AC1 2 CYS A 86 ASP A 87 -1 O CYS A 86 N LEU A 59
SHEET 1 AC2 4 THR A 151 MET A 154 0
SHEET 2 AC2 4 LEU A 96 PRO A 104 -1 N ALA A 102 O THR A 151
SHEET 3 AC2 4 TRP A 162 ARG A 172 -1 O LEU A 163 N LEU A 103
SHEET 4 AC2 4 TRP A 178 ARG A 180 -1 O CYS A 179 N VAL A 171
SHEET 1 AC3 2 TRP A 125 GLN A 133 0
SHEET 2 AC3 2 GLN A 140 HIS A 148 -1 O VAL A 145 N GLU A 128
SHEET 1 AC4 3 GLY D 43 ASP D 50 0
SHEET 2 AC4 3 ARG D 58 ARG D 67 -1 O THR D 62 N GLU D 48
SHEET 3 AC4 3 LEU D 73 ASP D 75 -1 O ILE D 74 N VAL D 66
SHEET 1 AC5 3 GLY D 43 ASP D 50 0
SHEET 2 AC5 3 ARG D 58 ARG D 67 -1 O THR D 62 N GLU D 48
SHEET 3 AC5 3 CYS D 86 ASP D 87 -1 O CYS D 86 N LEU D 59
SHEET 1 AC6 4 THR D 151 MET D 154 0
SHEET 2 AC6 4 LEU D 96 PRO D 104 -1 N ALA D 102 O THR D 151
SHEET 3 AC6 4 TRP D 162 ARG D 172 -1 O LEU D 163 N LEU D 103
SHEET 4 AC6 4 TRP D 178 ARG D 180 -1 O CYS D 179 N VAL D 171
SHEET 1 AC7 2 TRP D 125 GLN D 133 0
SHEET 2 AC7 2 GLN D 140 HIS D 148 -1 O SER D 141 N VAL D 132
SHEET 1 AC8 3 GLY B 43 ASP B 50 0
SHEET 2 AC8 3 ARG B 58 ARG B 67 -1 O ASN B 60 N ASP B 50
SHEET 3 AC8 3 LEU B 73 ASP B 75 -1 O ILE B 74 N VAL B 66
SHEET 1 AC9 3 GLY B 43 ASP B 50 0
SHEET 2 AC9 3 ARG B 58 ARG B 67 -1 O ASN B 60 N ASP B 50
SHEET 3 AC9 3 CYS B 86 ASP B 87 -1 O CYS B 86 N LEU B 59
SHEET 1 AD1 4 THR B 151 MET B 154 0
SHEET 2 AD1 4 LEU B 96 PRO B 104 -1 N ALA B 102 O THR B 151
SHEET 3 AD1 4 TRP B 162 ARG B 172 -1 O LEU B 163 N LEU B 103
SHEET 4 AD1 4 TRP B 178 ARG B 180 -1 O CYS B 179 N VAL B 171
SHEET 1 AD2 2 TRP B 125 GLN B 133 0
SHEET 2 AD2 2 GLN B 140 HIS B 148 -1 O SER B 141 N VAL B 132
SHEET 1 AD3 3 GLY E 43 ASP E 50 0
SHEET 2 AD3 3 ARG E 58 ARG E 67 -1 O THR E 62 N GLU E 48
SHEET 3 AD3 3 LEU E 73 ASP E 75 -1 O ILE E 74 N VAL E 66
SHEET 1 AD4 3 GLY E 43 ASP E 50 0
SHEET 2 AD4 3 ARG E 58 ARG E 67 -1 O THR E 62 N GLU E 48
SHEET 3 AD4 3 CYS E 86 ASP E 87 -1 O CYS E 86 N LEU E 59
SHEET 1 AD5 4 THR E 151 MET E 154 0
SHEET 2 AD5 4 LEU E 96 PRO E 104 -1 N ALA E 102 O THR E 151
SHEET 3 AD5 4 TRP E 162 ARG E 172 -1 O LEU E 163 N LEU E 103
SHEET 4 AD5 4 TRP E 178 ARG E 180 -1 O CYS E 179 N VAL E 171
SHEET 1 AD6 2 TRP E 125 GLN E 133 0
SHEET 2 AD6 2 GLN E 140 HIS E 148 -1 O VAL E 145 N GLU E 128
SHEET 1 AD7 3 GLY C 43 ASP C 50 0
SHEET 2 AD7 3 ARG C 58 ARG C 67 -1 O ILE C 65 N VAL C 45
SHEET 3 AD7 3 LEU C 73 ASP C 75 -1 O ILE C 74 N VAL C 66
SHEET 1 AD8 3 GLY C 43 ASP C 50 0
SHEET 2 AD8 3 ARG C 58 ARG C 67 -1 O ILE C 65 N VAL C 45
SHEET 3 AD8 3 CYS C 86 ASP C 87 -1 O CYS C 86 N LEU C 59
SHEET 1 AD9 4 THR C 151 MET C 154 0
SHEET 2 AD9 4 LEU C 96 PRO C 104 -1 N ALA C 102 O THR C 151
SHEET 3 AD9 4 TRP C 162 ARG C 172 -1 O LEU C 163 N LEU C 103
SHEET 4 AD9 4 TRP C 178 ARG C 180 -1 O CYS C 179 N VAL C 171
SHEET 1 AE1 2 TRP C 125 GLN C 133 0
SHEET 2 AE1 2 GLN C 140 HIS C 148 -1 O VAL C 145 N GLU C 128
SHEET 1 AE2 3 GLY F 43 ASP F 50 0
SHEET 2 AE2 3 ARG F 58 ARG F 67 -1 O THR F 62 N GLU F 48
SHEET 3 AE2 3 LEU F 73 ASP F 75 -1 O ILE F 74 N VAL F 66
SHEET 1 AE3 3 GLY F 43 ASP F 50 0
SHEET 2 AE3 3 ARG F 58 ARG F 67 -1 O THR F 62 N GLU F 48
SHEET 3 AE3 3 CYS F 86 ASP F 87 -1 O CYS F 86 N LEU F 59
SHEET 1 AE4 4 THR F 151 MET F 154 0
SHEET 2 AE4 4 LEU F 96 PRO F 104 -1 N ALA F 102 O THR F 151
SHEET 3 AE4 4 TRP F 162 ARG F 172 -1 O LEU F 163 N LEU F 103
SHEET 4 AE4 4 TRP F 178 ARG F 180 -1 O CYS F 179 N VAL F 171
SHEET 1 AE5 2 TRP F 125 GLN F 133 0
SHEET 2 AE5 2 GLN F 140 HIS F 148 -1 O VAL F 145 N GLU F 128
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
