HEADER MEMBRANE PROTEIN 16-MAR-17 5NG5
TITLE MULTI-DRUG EFFLUX; MEMBRANE TRANSPORT; RND SUPERFAMILY; DRUG
TITLE 2 RESISTANCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIDRUG EFFLUX PUMP SUBUNIT ACRA;
COMPND 3 CHAIN: E, D, G, H, A, B;
COMPND 4 SYNONYM: ACRAB-TOLC MULTIDRUG EFFLUX PUMP SUBUNIT ACRA,ACRIDINE
COMPND 5 RESISTANCE PROTEIN A;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: OUTER MEMBRANE PROTEIN TOLC;
COMPND 9 CHAIN: F, I, C;
COMPND 10 SYNONYM: MULTIDRUG EFFLUX PUMP SUBUNIT TOLC,OUTER MEMBRANE FACTOR
COMPND 11 TOLC;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: MULTIDRUG EFFLUX PUMP SUBUNIT ACRB;
COMPND 15 CHAIN: K, L, J;
COMPND 16 SYNONYM: ACRAB-TOLC MULTIDRUG EFFLUX PUMP SUBUNIT ACRB,ACRIDINE
COMPND 17 RESISTANCE PROTEIN B;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: MULTIDRUG EFFLUX PUMP ACCESSORY PROTEIN ACRZ;
COMPND 21 CHAIN: M, N, O;
COMPND 22 SYNONYM: ACRAB-TOLC MULTIDRUG EFFLUX PUMP ACCESSORY PROTEIN ACRZ,
COMPND 23 ACRIDINE RESISTANCE PROTEIN Z;
COMPND 24 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ACRA, LIR, MTCA, B0463, JW0452;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 9 ORGANISM_TAXID: 562;
SOURCE 10 GENE: TOLC, COLE1-I, MTCB, MUKA, REFI, TOC, WEEA, B3035, JW5503;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 15 ORGANISM_TAXID: 562;
SOURCE 16 GENE: ACRB, ACRE, B0462, JW0451;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 21 ORGANISM_TAXID: 562;
SOURCE 22 GENE: ACRZ, YBHT, B0762, JW5102;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MULTI-DRUG EFFLUX; MEMBRANE TRANSPORT; RND SUPERFAMILY; DRUG
KEYWDS 2 RESISTANCE, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR Z.WANG,G.FAN,C.F.HRYC,J.N.BLAZA,I.I.SERYSHEVA,M.F.SCHMID,W.CHIU,
AUTHOR 2 B.F.LUISI,D.DU
REVDAT 2 02-AUG-17 5NG5 1
REVDAT 1 19-APR-17 5NG5 0
JRNL AUTH Z.WANG,G.FAN,C.F.HRYC,J.N.BLAZA,I.I.SERYSHEVA,M.F.SCHMID,
JRNL AUTH 2 W.CHIU,B.F.LUISI,D.DU
JRNL TITL AN ALLOSTERIC TRANSPORT MECHANISM FOR THE ACRAB-TOLC
JRNL TITL 2 MULTIDRUG EFFLUX PUMP.
JRNL REF ELIFE V. 6 2017
JRNL REFN ESSN 2050-084X
JRNL PMID 28355133
JRNL DOI 10.7554/ELIFE.24905
REMARK 2
REMARK 2 RESOLUTION. 6.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CTFFIND, UCSF CHIMERA, EMAN, RELION,
REMARK 3 PHENIX, COOT
REMARK 3 RECONSTRUCTION SCHEMA : BACK PROJECTION
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT
REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION COEFFICIENT
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : CRYSTAL STRUCTURES WERE RIGID-BODY FIT INTO
REMARK 3 THE DENSITY MAP AND MODEL OPTIMIZATION WAS THEN CARRIED OUT WITH
REMARK 3 PHENIX REAL-SPACE REFINE. DUE TO THE WEAKER RESOLUTION, STRONGER
REMARK 3 STEREOCHEMICAL AND SECONDARY STRUCTURE RESTRAINTS WERE USED TO
REMARK 3 ENSURE THAT ALPHA-HELICES AND BETA-SHEETS DID NOT DEVIATE FAR
REMARK 3 FROM THEIR EXPECTED GEOMETRY. MANUAL ADJUSTMENTS WERE KEPT TO A
REMARK 3 MINIMUM TO REDUCE HUMAN BIAS IN THE MODELING PROCEDURE, WITH
REMARK 3 COOT ONLY BEING USED TO FIX OBVIOUS ERRORS SUCH AS C-BETA
REMARK 3 DEVIATIONS. A FINAL CHECK OF MOLPROBITY AND CROSS CORRELATION
REMARK 3 WAS DONE TO ENSURE MODEL QUALITY.
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) : 6.500
REMARK 3 NUMBER OF PARTICLES : 13544
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 5NG5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004075.
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 : ACRABTOLC IN APO STATE
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : A 3UL ALIQUOT AT A
REMARK 245 CONCENTRATION OF 2 MG PER ML
REMARK 245 WAS APPLIED ONTO GLOW-
REMARK 245 DISCHARGED HOLEY CARBON GRID
REMARK 245 (QUANTIFOIL AU R1.21.3, 300
REMARK 245 MESH)
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
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) : 1.00
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: PENTADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 88880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 244870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -392.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, D, G, H, A, B, F, I, C, K,
REMARK 350 AND CHAINS: L, M, N, O, J
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 CYS E 25
REMARK 465 ASP E 26
REMARK 465 ASP E 27
REMARK 465 LYS E 28
REMARK 465 GLN E 29
REMARK 465 ALA E 30
REMARK 465 GLN E 31
REMARK 465 GLN E 32
REMARK 465 GLY E 33
REMARK 465 GLY E 34
REMARK 465 GLN E 35
REMARK 465 GLN E 36
REMARK 465 MET E 37
REMARK 465 VAL E 378
REMARK 465 THR E 379
REMARK 465 ALA E 380
REMARK 465 ASP E 381
REMARK 465 ASN E 382
REMARK 465 ASN E 383
REMARK 465 GLN E 384
REMARK 465 GLN E 385
REMARK 465 ALA E 386
REMARK 465 ALA E 387
REMARK 465 SER E 388
REMARK 465 GLY E 389
REMARK 465 ALA E 390
REMARK 465 GLN E 391
REMARK 465 PRO E 392
REMARK 465 GLU E 393
REMARK 465 GLN E 394
REMARK 465 SER E 395
REMARK 465 LYS E 396
REMARK 465 SER E 397
REMARK 465 CYS D 25
REMARK 465 ASP D 26
REMARK 465 ASP D 27
REMARK 465 LYS D 28
REMARK 465 GLN D 29
REMARK 465 ALA D 30
REMARK 465 GLN D 31
REMARK 465 GLN D 32
REMARK 465 GLY D 33
REMARK 465 GLY D 34
REMARK 465 GLN D 35
REMARK 465 GLN D 36
REMARK 465 MET D 37
REMARK 465 VAL D 378
REMARK 465 THR D 379
REMARK 465 ALA D 380
REMARK 465 ASP D 381
REMARK 465 ASN D 382
REMARK 465 ASN D 383
REMARK 465 GLN D 384
REMARK 465 GLN D 385
REMARK 465 ALA D 386
REMARK 465 ALA D 387
REMARK 465 SER D 388
REMARK 465 GLY D 389
REMARK 465 ALA D 390
REMARK 465 GLN D 391
REMARK 465 PRO D 392
REMARK 465 GLU D 393
REMARK 465 GLN D 394
REMARK 465 SER D 395
REMARK 465 LYS D 396
REMARK 465 SER D 397
REMARK 465 CYS G 25
REMARK 465 ASP G 26
REMARK 465 ASP G 27
REMARK 465 LYS G 28
REMARK 465 GLN G 29
REMARK 465 ALA G 30
REMARK 465 GLN G 31
REMARK 465 GLN G 32
REMARK 465 GLY G 33
REMARK 465 GLY G 34
REMARK 465 GLN G 35
REMARK 465 GLN G 36
REMARK 465 MET G 37
REMARK 465 VAL G 378
REMARK 465 THR G 379
REMARK 465 ALA G 380
REMARK 465 ASP G 381
REMARK 465 ASN G 382
REMARK 465 ASN G 383
REMARK 465 GLN G 384
REMARK 465 GLN G 385
REMARK 465 ALA G 386
REMARK 465 ALA G 387
REMARK 465 SER G 388
REMARK 465 GLY G 389
REMARK 465 ALA G 390
REMARK 465 GLN G 391
REMARK 465 PRO G 392
REMARK 465 GLU G 393
REMARK 465 GLN G 394
REMARK 465 SER G 395
REMARK 465 LYS G 396
REMARK 465 SER G 397
REMARK 465 CYS H 25
REMARK 465 ASP H 26
REMARK 465 ASP H 27
REMARK 465 LYS H 28
REMARK 465 GLN H 29
REMARK 465 ALA H 30
REMARK 465 GLN H 31
REMARK 465 GLN H 32
REMARK 465 GLY H 33
REMARK 465 GLY H 34
REMARK 465 GLN H 35
REMARK 465 GLN H 36
REMARK 465 MET H 37
REMARK 465 VAL H 378
REMARK 465 THR H 379
REMARK 465 ALA H 380
REMARK 465 ASP H 381
REMARK 465 ASN H 382
REMARK 465 ASN H 383
REMARK 465 GLN H 384
REMARK 465 GLN H 385
REMARK 465 ALA H 386
REMARK 465 ALA H 387
REMARK 465 SER H 388
REMARK 465 GLY H 389
REMARK 465 ALA H 390
REMARK 465 GLN H 391
REMARK 465 PRO H 392
REMARK 465 GLU H 393
REMARK 465 GLN H 394
REMARK 465 SER H 395
REMARK 465 LYS H 396
REMARK 465 SER H 397
REMARK 465 CYS A 25
REMARK 465 ASP A 26
REMARK 465 ASP A 27
REMARK 465 LYS A 28
REMARK 465 GLN A 29
REMARK 465 ALA A 30
REMARK 465 GLN A 31
REMARK 465 GLN A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 GLN A 35
REMARK 465 GLN A 36
REMARK 465 MET A 37
REMARK 465 VAL A 378
REMARK 465 THR A 379
REMARK 465 ALA A 380
REMARK 465 ASP A 381
REMARK 465 ASN A 382
REMARK 465 ASN A 383
REMARK 465 GLN A 384
REMARK 465 GLN A 385
REMARK 465 ALA A 386
REMARK 465 ALA A 387
REMARK 465 SER A 388
REMARK 465 GLY A 389
REMARK 465 ALA A 390
REMARK 465 GLN A 391
REMARK 465 PRO A 392
REMARK 465 GLU A 393
REMARK 465 GLN A 394
REMARK 465 SER A 395
REMARK 465 LYS A 396
REMARK 465 SER A 397
REMARK 465 CYS B 25
REMARK 465 ASP B 26
REMARK 465 ASP B 27
REMARK 465 LYS B 28
REMARK 465 GLN B 29
REMARK 465 ALA B 30
REMARK 465 GLN B 31
REMARK 465 GLN B 32
REMARK 465 GLY B 33
REMARK 465 GLY B 34
REMARK 465 GLN B 35
REMARK 465 GLN B 36
REMARK 465 MET B 37
REMARK 465 VAL B 378
REMARK 465 THR B 379
REMARK 465 ALA B 380
REMARK 465 ASP B 381
REMARK 465 ASN B 382
REMARK 465 ASN B 383
REMARK 465 GLN B 384
REMARK 465 GLN B 385
REMARK 465 ALA B 386
REMARK 465 ALA B 387
REMARK 465 SER B 388
REMARK 465 GLY B 389
REMARK 465 ALA B 390
REMARK 465 GLN B 391
REMARK 465 PRO B 392
REMARK 465 GLU B 393
REMARK 465 GLN B 394
REMARK 465 SER B 395
REMARK 465 LYS B 396
REMARK 465 SER B 397
REMARK 465 MET F -21
REMARK 465 LYS F -20
REMARK 465 LYS F -19
REMARK 465 LEU F -18
REMARK 465 LEU F -17
REMARK 465 PRO F -16
REMARK 465 ILE F -15
REMARK 465 LEU F -14
REMARK 465 ILE F -13
REMARK 465 GLY F -12
REMARK 465 LEU F -11
REMARK 465 SER F -10
REMARK 465 LEU F -9
REMARK 465 SER F -8
REMARK 465 GLY F -7
REMARK 465 PHE F -6
REMARK 465 SER F -5
REMARK 465 SER F -4
REMARK 465 LEU F -3
REMARK 465 SER F -2
REMARK 465 GLN F -1
REMARK 465 ALA F 0
REMARK 465 ASN F 429
REMARK 465 VAL F 430
REMARK 465 ALA F 431
REMARK 465 PRO F 432
REMARK 465 GLN F 433
REMARK 465 THR F 434
REMARK 465 PRO F 435
REMARK 465 GLU F 436
REMARK 465 GLN F 437
REMARK 465 ASN F 438
REMARK 465 ALA F 439
REMARK 465 ILE F 440
REMARK 465 ALA F 441
REMARK 465 ASP F 442
REMARK 465 GLY F 443
REMARK 465 TYR F 444
REMARK 465 ALA F 445
REMARK 465 PRO F 446
REMARK 465 ASP F 447
REMARK 465 SER F 448
REMARK 465 PRO F 449
REMARK 465 ALA F 450
REMARK 465 PRO F 451
REMARK 465 VAL F 452
REMARK 465 VAL F 453
REMARK 465 GLN F 454
REMARK 465 GLN F 455
REMARK 465 THR F 456
REMARK 465 SER F 457
REMARK 465 ALA F 458
REMARK 465 ARG F 459
REMARK 465 THR F 460
REMARK 465 THR F 461
REMARK 465 THR F 462
REMARK 465 SER F 463
REMARK 465 ASN F 464
REMARK 465 GLY F 465
REMARK 465 HIS F 466
REMARK 465 ASN F 467
REMARK 465 PRO F 468
REMARK 465 PHE F 469
REMARK 465 ARG F 470
REMARK 465 ASN F 471
REMARK 465 MET I -21
REMARK 465 LYS I -20
REMARK 465 LYS I -19
REMARK 465 LEU I -18
REMARK 465 LEU I -17
REMARK 465 PRO I -16
REMARK 465 ILE I -15
REMARK 465 LEU I -14
REMARK 465 ILE I -13
REMARK 465 GLY I -12
REMARK 465 LEU I -11
REMARK 465 SER I -10
REMARK 465 LEU I -9
REMARK 465 SER I -8
REMARK 465 GLY I -7
REMARK 465 PHE I -6
REMARK 465 SER I -5
REMARK 465 SER I -4
REMARK 465 LEU I -3
REMARK 465 SER I -2
REMARK 465 GLN I -1
REMARK 465 ALA I 0
REMARK 465 ASN I 429
REMARK 465 VAL I 430
REMARK 465 ALA I 431
REMARK 465 PRO I 432
REMARK 465 GLN I 433
REMARK 465 THR I 434
REMARK 465 PRO I 435
REMARK 465 GLU I 436
REMARK 465 GLN I 437
REMARK 465 ASN I 438
REMARK 465 ALA I 439
REMARK 465 ILE I 440
REMARK 465 ALA I 441
REMARK 465 ASP I 442
REMARK 465 GLY I 443
REMARK 465 TYR I 444
REMARK 465 ALA I 445
REMARK 465 PRO I 446
REMARK 465 ASP I 447
REMARK 465 SER I 448
REMARK 465 PRO I 449
REMARK 465 ALA I 450
REMARK 465 PRO I 451
REMARK 465 VAL I 452
REMARK 465 VAL I 453
REMARK 465 GLN I 454
REMARK 465 GLN I 455
REMARK 465 THR I 456
REMARK 465 SER I 457
REMARK 465 ALA I 458
REMARK 465 ARG I 459
REMARK 465 THR I 460
REMARK 465 THR I 461
REMARK 465 THR I 462
REMARK 465 SER I 463
REMARK 465 ASN I 464
REMARK 465 GLY I 465
REMARK 465 HIS I 466
REMARK 465 ASN I 467
REMARK 465 PRO I 468
REMARK 465 PHE I 469
REMARK 465 ARG I 470
REMARK 465 ASN I 471
REMARK 465 MET C -21
REMARK 465 LYS C -20
REMARK 465 LYS C -19
REMARK 465 LEU C -18
REMARK 465 LEU C -17
REMARK 465 PRO C -16
REMARK 465 ILE C -15
REMARK 465 LEU C -14
REMARK 465 ILE C -13
REMARK 465 GLY C -12
REMARK 465 LEU C -11
REMARK 465 SER C -10
REMARK 465 LEU C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 PHE C -6
REMARK 465 SER C -5
REMARK 465 SER C -4
REMARK 465 LEU C -3
REMARK 465 SER C -2
REMARK 465 GLN C -1
REMARK 465 ALA C 0
REMARK 465 ASN C 429
REMARK 465 VAL C 430
REMARK 465 ALA C 431
REMARK 465 PRO C 432
REMARK 465 GLN C 433
REMARK 465 THR C 434
REMARK 465 PRO C 435
REMARK 465 GLU C 436
REMARK 465 GLN C 437
REMARK 465 ASN C 438
REMARK 465 ALA C 439
REMARK 465 ILE C 440
REMARK 465 ALA C 441
REMARK 465 ASP C 442
REMARK 465 GLY C 443
REMARK 465 TYR C 444
REMARK 465 ALA C 445
REMARK 465 PRO C 446
REMARK 465 ASP C 447
REMARK 465 SER C 448
REMARK 465 PRO C 449
REMARK 465 ALA C 450
REMARK 465 PRO C 451
REMARK 465 VAL C 452
REMARK 465 VAL C 453
REMARK 465 GLN C 454
REMARK 465 GLN C 455
REMARK 465 THR C 456
REMARK 465 SER C 457
REMARK 465 ALA C 458
REMARK 465 ARG C 459
REMARK 465 THR C 460
REMARK 465 THR C 461
REMARK 465 THR C 462
REMARK 465 SER C 463
REMARK 465 ASN C 464
REMARK 465 GLY C 465
REMARK 465 HIS C 466
REMARK 465 ASN C 467
REMARK 465 PRO C 468
REMARK 465 PHE C 469
REMARK 465 ARG C 470
REMARK 465 ASN C 471
REMARK 465 GLU K 1038
REMARK 465 ASP K 1039
REMARK 465 ILE K 1040
REMARK 465 GLU K 1041
REMARK 465 HIS K 1042
REMARK 465 SER K 1043
REMARK 465 HIS K 1044
REMARK 465 THR K 1045
REMARK 465 VAL K 1046
REMARK 465 ASP K 1047
REMARK 465 HIS K 1048
REMARK 465 HIS K 1049
REMARK 465 GLU L 1038
REMARK 465 ASP L 1039
REMARK 465 ILE L 1040
REMARK 465 GLU L 1041
REMARK 465 HIS L 1042
REMARK 465 SER L 1043
REMARK 465 HIS L 1044
REMARK 465 THR L 1045
REMARK 465 VAL L 1046
REMARK 465 ASP L 1047
REMARK 465 HIS L 1048
REMARK 465 HIS L 1049
REMARK 465 GLN M 47
REMARK 465 ASN M 48
REMARK 465 HIS M 49
REMARK 465 HIS M 50
REMARK 465 HIS M 51
REMARK 465 HIS M 52
REMARK 465 HIS M 53
REMARK 465 HIS M 54
REMARK 465 GLN N 47
REMARK 465 ASN N 48
REMARK 465 HIS N 49
REMARK 465 HIS N 50
REMARK 465 HIS N 51
REMARK 465 HIS N 52
REMARK 465 HIS N 53
REMARK 465 HIS N 54
REMARK 465 GLN O 47
REMARK 465 ASN O 48
REMARK 465 HIS O 49
REMARK 465 HIS O 50
REMARK 465 HIS O 51
REMARK 465 HIS O 52
REMARK 465 HIS O 53
REMARK 465 HIS O 54
REMARK 465 SER J 1034
REMARK 465 ARG J 1035
REMARK 465 LYS J 1036
REMARK 465 ASN J 1037
REMARK 465 GLU J 1038
REMARK 465 ASP J 1039
REMARK 465 ILE J 1040
REMARK 465 GLU J 1041
REMARK 465 HIS J 1042
REMARK 465 SER J 1043
REMARK 465 HIS J 1044
REMARK 465 THR J 1045
REMARK 465 VAL J 1046
REMARK 465 ASP J 1047
REMARK 465 HIS J 1048
REMARK 465 HIS J 1049
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 ASN K 391 CG OD1 ND2
REMARK 470 THR K 392 OG1 CG2
REMARK 470 LEU K 393 CG CD1 CD2
REMARK 470 ARG K 536 CG CD NE CZ NH1 NH2
REMARK 470 LYS K 659 CG CD CE NZ
REMARK 470 ASP K 660 CG OD1 OD2
REMARK 470 THR K 714 OG1 CG2
REMARK 470 VAL K 716 CG1 CG2
REMARK 470 GLU K 866 CG CD OE1 OE2
REMARK 470 ARG K 867 CG CD NE CZ NH1 NH2
REMARK 470 ASN K 871 CG OD1 ND2
REMARK 470 GLU K 893 CG CD OE1 OE2
REMARK 470 ILE K 897 CG1 CG2 CD1
REMARK 470 PHE K 899 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG K1035 CG CD NE CZ NH1 NH2
REMARK 470 LYS K1036 CG CD CE NZ
REMARK 470 ASN K1037 CG OD1 ND2
REMARK 470 ASN L 391 CG OD1 ND2
REMARK 470 THR L 392 OG1 CG2
REMARK 470 LEU L 393 CG CD1 CD2
REMARK 470 ARG L 536 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 659 CG CD CE NZ
REMARK 470 ASP L 660 CG OD1 OD2
REMARK 470 THR L 714 OG1 CG2
REMARK 470 VAL L 716 CG1 CG2
REMARK 470 GLU L 866 CG CD OE1 OE2
REMARK 470 ARG L 867 CG CD NE CZ NH1 NH2
REMARK 470 ASN L 871 CG OD1 ND2
REMARK 470 GLU L 893 CG CD OE1 OE2
REMARK 470 ILE L 897 CG1 CG2 CD1
REMARK 470 PHE L 899 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG L1035 CG CD NE CZ NH1 NH2
REMARK 470 LYS L1036 CG CD CE NZ
REMARK 470 ASN L1037 CG OD1 ND2
REMARK 470 PHE M 36 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS M 41 CG CD CE NZ
REMARK 470 LYS M 42 CG CD CE NZ
REMARK 470 GLN M 44 CG CD OE1 NE2
REMARK 470 PHE N 36 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS N 41 CG CD CE NZ
REMARK 470 LYS N 42 CG CD CE NZ
REMARK 470 GLN N 44 CG CD OE1 NE2
REMARK 470 PHE O 36 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS O 41 CG CD CE NZ
REMARK 470 LYS O 42 CG CD CE NZ
REMARK 470 GLN O 44 CG CD OE1 NE2
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 CD1 PHE K 628 H30 5QF K 1101 0.88
REMARK 500 CE1 PHE K 628 H30 5QF K 1101 0.93
REMARK 500 CE1 PHE K 628 C32 5QF K 1101 1.03
REMARK 500 CD2 PHE L 178 H4 5QF L 1101 1.34
REMARK 500 CZ PHE K 615 H20 5QF K 1101 1.40
REMARK 500 O PHE L 178 H12 5QF L 1101 1.52
REMARK 500 CG2 ILE J 277 O19 5QF J 1101 1.56
REMARK 500 CE2 PHE L 178 H3 5QF L 1101 1.58
REMARK 500 CG PHE L 178 C12 5QF L 1101 1.68
REMARK 500 CG2 ILE L 277 O19 5QF L 1101 1.70
REMARK 500 CZ PHE K 628 C32 5QF K 1101 1.71
REMARK 500 CD2 PHE L 628 C6 5QF L 1101 1.72
REMARK 500 CE2 PHE L 628 C5 5QF L 1101 1.76
REMARK 500 CE2 PHE K 628 C1 5QF K 1101 1.78
REMARK 500 CB PHE L 178 C13 5QF L 1101 1.79
REMARK 500 CZ PHE K 628 C35 5QF K 1101 1.80
REMARK 500 CG2 ILE K 277 O18 5QF K 1101 1.81
REMARK 500 CZ PHE L 628 C1 5QF L 1101 1.82
REMARK 500 CD1 PHE K 628 C32 5QF K 1101 1.82
REMARK 500 CE2 PHE J 628 C5 5QF J 1101 1.84
REMARK 500 CE1 PHE K 628 O34 5QF K 1101 1.88
REMARK 500 CD2 PHE L 628 C7 5QF L 1101 1.88
REMARK 500 CD1 PHE L 178 C17 5QF L 1101 1.89
REMARK 500 CG PHE L 178 C17 5QF L 1101 1.93
REMARK 500 CE2 PHE L 628 C2 5QF L 1101 1.93
REMARK 500 CE1 PHE K 628 C1 5QF K 1101 1.94
REMARK 500 CE2 PHE K 628 C2 5QF K 1101 1.95
REMARK 500 CE2 PHE L 610 C10 5QF L 1101 1.96
REMARK 500 CE2 PHE J 628 N4 5QF J 1101 1.96
REMARK 500 CB PHE L 178 C12 5QF L 1101 1.97
REMARK 500 CB PHE L 178 C14 5QF L 1101 2.00
REMARK 500 CB ILE K 277 O18 5QF K 1101 2.00
REMARK 500 CG2 ILE K 277 C16 5QF K 1101 2.05
REMARK 500 CZ PHE K 628 O34 5QF K 1101 2.08
REMARK 500 CE2 PHE J 628 C6 5QF J 1101 2.08
REMARK 500 CD2 PHE J 628 C6 5QF J 1101 2.09
REMARK 500 O PHE L 178 C21 5QF L 1101 2.10
REMARK 500 CG2 ILE J 277 C21 5QF J 1101 2.15
REMARK 500 CE2 PHE L 178 C11 5QF L 1101 2.15
REMARK 500 CD2 PHE L 178 C12 5QF L 1101 2.16
REMARK 500 CE1 PHE K 628 C36 5QF K 1101 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL E 68 C ARG E 69 N -0.181
REMARK 500 SER K 805 CA SER K 805 CB -0.107
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 E 64 C - N - CA ANGL. DEV. = 16.7 DEGREES
REMARK 500 ARG D 64 C - N - CA ANGL. DEV. = 16.1 DEGREES
REMARK 500 ARG G 64 C - N - CA ANGL. DEV. = 15.9 DEGREES
REMARK 500 LEU H 56 CB - CG - CD1 ANGL. DEV. = -14.0 DEGREES
REMARK 500 LEU A 56 CB - CG - CD1 ANGL. DEV. = -12.4 DEGREES
REMARK 500 LEU B 56 CB - CG - CD1 ANGL. DEV. = -11.5 DEGREES
REMARK 500 ILE K 38 CG1 - CB - CG2 ANGL. DEV. = -13.3 DEGREES
REMARK 500 LEU K 425 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 LEU K1017 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 LEU L 425 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 LEU J 75 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU J 113 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 ASP J 256 CB - CG - OD1 ANGL. DEV. = 11.3 DEGREES
REMARK 500 ASP J 256 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 SER J 258 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 LEU J 344 CA - CB - CG ANGL. DEV. = 14.6 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 ARG E 64 67.57 61.67
REMARK 500 THR E 135 -162.49 -75.10
REMARK 500 SER E 139 76.32 55.78
REMARK 500 LYS E 140 -34.30 -30.52
REMARK 500 LYS E 175 -56.08 -120.43
REMARK 500 PRO E 179 12.29 -60.36
REMARK 500 LYS E 186 -166.05 -78.53
REMARK 500 THR E 286 48.88 -94.23
REMARK 500 MET E 287 -37.36 -130.66
REMARK 500 MET E 288 82.77 51.21
REMARK 500 ASP E 330 -6.60 66.06
REMARK 500 SER E 340 -60.61 -98.67
REMARK 500 GLU E 351 116.16 -162.36
REMARK 500 ILE E 361 -63.03 -106.68
REMARK 500 ARG D 64 66.92 61.07
REMARK 500 THR D 135 -163.03 -75.28
REMARK 500 SER D 139 77.42 58.09
REMARK 500 LYS D 140 -35.75 -29.36
REMARK 500 LYS D 175 -54.37 -120.53
REMARK 500 PRO D 179 11.76 -59.05
REMARK 500 LYS D 186 -164.66 -78.72
REMARK 500 THR D 201 -168.25 -78.24
REMARK 500 THR D 286 50.11 -92.52
REMARK 500 MET D 288 81.91 52.30
REMARK 500 ASP D 330 -5.86 66.33
REMARK 500 GLU D 351 111.11 -160.56
REMARK 500 SER G 92 96.10 -67.49
REMARK 500 THR G 135 -165.33 -76.46
REMARK 500 GLN G 136 -71.39 -85.56
REMARK 500 SER G 139 76.80 54.68
REMARK 500 LYS G 140 -35.06 -28.21
REMARK 500 LYS G 175 -55.39 -122.27
REMARK 500 PRO G 179 11.50 -61.27
REMARK 500 LYS G 186 -163.19 -78.84
REMARK 500 ASP G 257 -169.27 -78.62
REMARK 500 THR G 286 50.26 -92.87
REMARK 500 MET G 287 -35.38 -132.02
REMARK 500 MET G 288 82.97 48.30
REMARK 500 VAL G 293 133.80 -37.72
REMARK 500 ASP G 330 -6.27 66.42
REMARK 500 GLU G 351 115.14 -160.43
REMARK 500 ALA H 66 70.14 58.73
REMARK 500 ASN H 197 97.36 -69.13
REMARK 500 LYS H 236 172.70 179.67
REMARK 500 ASN H 239 -10.54 74.52
REMARK 500 MET H 291 -52.97 -122.36
REMARK 500 LEU H 301 73.96 50.67
REMARK 500 ASN H 302 107.97 -50.80
REMARK 500 PRO H 317 -151.27 -74.63
REMARK 500 LEU H 324 54.00 -115.65
REMARK 500
REMARK 500 THIS ENTRY HAS 178 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 ALA E 62 TYR E 63 -148.98
REMARK 500 LEU E 93 TYR E 94 147.23
REMARK 500 THR E 135 GLN E 136 -137.43
REMARK 500 THR E 174 LYS E 175 -38.95
REMARK 500 THR E 177 SER E 178 149.99
REMARK 500 MET E 223 MET E 224 138.61
REMARK 500 GLU E 238 ASN E 239 41.94
REMARK 500 LYS E 241 ALA E 242 -149.35
REMARK 500 MET E 291 PHE E 292 -144.92
REMARK 500 PHE E 292 VAL E 293 -147.20
REMARK 500 ALA D 62 TYR D 63 -139.97
REMARK 500 LEU D 93 TYR D 94 149.73
REMARK 500 THR D 135 GLN D 136 -134.00
REMARK 500 THR D 174 LYS D 175 -40.58
REMARK 500 MET D 223 MET D 224 138.97
REMARK 500 GLU D 238 ASN D 239 39.99
REMARK 500 LYS D 241 ALA D 242 -149.63
REMARK 500 MET D 291 PHE D 292 -149.98
REMARK 500 PHE D 292 VAL D 293 -148.71
REMARK 500 ILE D 306 LEU D 307 149.24
REMARK 500 ALA G 62 TYR G 63 -144.99
REMARK 500 THR G 135 GLN G 136 -134.35
REMARK 500 THR G 174 LYS G 175 -36.42
REMARK 500 MET G 223 MET G 224 144.50
REMARK 500 GLU G 238 ASN G 239 42.18
REMARK 500 PHE G 292 VAL G 293 -144.83
REMARK 500 THR H 47 GLU H 48 -142.77
REMARK 500 TYR H 173 THR H 174 147.64
REMARK 500 ASP H 210 PRO H 211 148.21
REMARK 500 LEU H 235 LYS H 236 141.39
REMARK 500 GLY H 300 LEU H 301 145.41
REMARK 500 LYS A 46 THR A 47 -148.88
REMARK 500 THR A 47 GLU A 48 -141.81
REMARK 500 TYR A 173 THR A 174 149.43
REMARK 500 ASP A 210 PRO A 211 148.72
REMARK 500 LEU A 235 LYS A 236 140.52
REMARK 500 GLY A 300 LEU A 301 145.25
REMARK 500 THR B 47 GLU B 48 -140.18
REMARK 500 ASP B 210 PRO B 211 148.88
REMARK 500 LEU B 235 LYS B 236 138.57
REMARK 500 GLY B 300 LEU B 301 146.11
REMARK 500 ILE K 38 ALA K 39 146.54
REMARK 500 SER K 80 ASN K 81 149.00
REMARK 500 LEU K 903 VAL K 904 149.11
REMARK 500 VAL K 1024 PHE K 1025 146.93
REMARK 500 SER L 80 ASN L 81 149.84
REMARK 500 LYS L 110 LEU L 111 147.88
REMARK 500 ILE L 879 SER L 880 144.97
REMARK 500 GLN J 108 ASN J 109 149.77
REMARK 500 GLN J 112 LEU J 113 146.82
REMARK 500
REMARK 500 THIS ENTRY HAS 57 NON CIS, NON-TRANS OMEGA OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5QF J 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5QF K 1101 and PHE K
REMARK 800 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5QF K 1101 and PHE K
REMARK 800 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5QF K 1101 and PHE K
REMARK 800 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5QF L 1101 and PHE L
REMARK 800 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5QF L 1101 and PHE L
REMARK 800 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5QF L 1101 and PHE L
REMARK 800 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5QF L 1101 and PHE L
REMARK 800 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 5QF L 1101 and PHE L
REMARK 800 178
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-3636 RELATED DB: EMDB
REMARK 900 MULTI-DRUG EFFLUX; MEMBRANE TRANSPORT; RND SUPERFAMILY; DRUG
REMARK 900 RESISTANCE
DBREF 5NG5 E 25 397 UNP P0AE06 ACRA_ECOLI 25 397
DBREF 5NG5 D 25 397 UNP P0AE06 ACRA_ECOLI 25 397
DBREF 5NG5 G 25 397 UNP P0AE06 ACRA_ECOLI 25 397
DBREF 5NG5 H 25 397 UNP P0AE06 ACRA_ECOLI 25 397
DBREF 5NG5 A 25 397 UNP P0AE06 ACRA_ECOLI 25 397
DBREF 5NG5 B 25 397 UNP P0AE06 ACRA_ECOLI 25 397
DBREF 5NG5 F -21 471 UNP P02930 TOLC_ECOLI 1 493
DBREF 5NG5 I -21 471 UNP P02930 TOLC_ECOLI 1 493
DBREF 5NG5 C -21 471 UNP P02930 TOLC_ECOLI 1 493
DBREF 5NG5 K 1 1049 UNP P31224 ACRB_ECOLI 1 1049
DBREF 5NG5 L 1 1049 UNP P31224 ACRB_ECOLI 1 1049
DBREF 5NG5 M 1 49 UNP P0AAW9 ACRZ_ECOLI 1 49
DBREF 5NG5 N 1 49 UNP P0AAW9 ACRZ_ECOLI 1 49
DBREF 5NG5 O 1 49 UNP P0AAW9 ACRZ_ECOLI 1 49
DBREF 5NG5 J 1 1049 UNP P31224 ACRB_ECOLI 1 1049
SEQADV 5NG5 MET E 223 UNP P0AE06 PHE 223 CONFLICT
SEQADV 5NG5 MET E 224 UNP P0AE06 LEU 224 CONFLICT
SEQADV 5NG5 MET E 287 UNP P0AE06 LEU 287 CONFLICT
SEQADV 5NG5 MET E 288 UNP P0AE06 LEU 288 CONFLICT
SEQADV 5NG5 MET D 223 UNP P0AE06 PHE 223 CONFLICT
SEQADV 5NG5 MET D 224 UNP P0AE06 LEU 224 CONFLICT
SEQADV 5NG5 MET D 287 UNP P0AE06 LEU 287 CONFLICT
SEQADV 5NG5 MET D 288 UNP P0AE06 LEU 288 CONFLICT
SEQADV 5NG5 MET G 223 UNP P0AE06 PHE 223 CONFLICT
SEQADV 5NG5 MET G 224 UNP P0AE06 LEU 224 CONFLICT
SEQADV 5NG5 MET G 287 UNP P0AE06 LEU 287 CONFLICT
SEQADV 5NG5 MET G 288 UNP P0AE06 LEU 288 CONFLICT
SEQADV 5NG5 MET H 223 UNP P0AE06 PHE 223 CONFLICT
SEQADV 5NG5 MET H 224 UNP P0AE06 LEU 224 CONFLICT
SEQADV 5NG5 MET H 287 UNP P0AE06 LEU 287 CONFLICT
SEQADV 5NG5 MET H 288 UNP P0AE06 LEU 288 CONFLICT
SEQADV 5NG5 MET A 223 UNP P0AE06 PHE 223 CONFLICT
SEQADV 5NG5 MET A 224 UNP P0AE06 LEU 224 CONFLICT
SEQADV 5NG5 MET A 287 UNP P0AE06 LEU 287 CONFLICT
SEQADV 5NG5 MET A 288 UNP P0AE06 LEU 288 CONFLICT
SEQADV 5NG5 MET B 223 UNP P0AE06 PHE 223 CONFLICT
SEQADV 5NG5 MET B 224 UNP P0AE06 LEU 224 CONFLICT
SEQADV 5NG5 MET B 287 UNP P0AE06 LEU 287 CONFLICT
SEQADV 5NG5 MET B 288 UNP P0AE06 LEU 288 CONFLICT
SEQADV 5NG5 HIS M 50 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS M 51 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS M 52 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS M 53 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS M 54 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS N 50 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS N 51 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS N 52 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS N 53 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS N 54 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS O 50 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS O 51 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS O 52 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS O 53 UNP P0AAW9 EXPRESSION TAG
SEQADV 5NG5 HIS O 54 UNP P0AAW9 EXPRESSION TAG
SEQRES 1 E 373 CYS ASP ASP LYS GLN ALA GLN GLN GLY GLY GLN GLN MET
SEQRES 2 E 373 PRO ALA VAL GLY VAL VAL THR VAL LYS THR GLU PRO LEU
SEQRES 3 E 373 GLN ILE THR THR GLU LEU PRO GLY ARG THR SER ALA TYR
SEQRES 4 E 373 ARG ILE ALA GLU VAL ARG PRO GLN VAL SER GLY ILE ILE
SEQRES 5 E 373 LEU LYS ARG ASN PHE LYS GLU GLY SER ASP ILE GLU ALA
SEQRES 6 E 373 GLY VAL SER LEU TYR GLN ILE ASP PRO ALA THR TYR GLN
SEQRES 7 E 373 ALA THR TYR ASP SER ALA LYS GLY ASP LEU ALA LYS ALA
SEQRES 8 E 373 GLN ALA ALA ALA ASN ILE ALA GLN LEU THR VAL ASN ARG
SEQRES 9 E 373 TYR GLN LYS LEU LEU GLY THR GLN TYR ILE SER LYS GLN
SEQRES 10 E 373 GLU TYR ASP GLN ALA LEU ALA ASP ALA GLN GLN ALA ASN
SEQRES 11 E 373 ALA ALA VAL THR ALA ALA LYS ALA ALA VAL GLU THR ALA
SEQRES 12 E 373 ARG ILE ASN LEU ALA TYR THR LYS VAL THR SER PRO ILE
SEQRES 13 E 373 SER GLY ARG ILE GLY LYS SER ASN VAL THR GLU GLY ALA
SEQRES 14 E 373 LEU VAL GLN ASN GLY GLN ALA THR ALA LEU ALA THR VAL
SEQRES 15 E 373 GLN GLN LEU ASP PRO ILE TYR VAL ASP VAL THR GLN SER
SEQRES 16 E 373 SER ASN ASP MET MET ARG LEU LYS GLN GLU LEU ALA ASN
SEQRES 17 E 373 GLY THR LEU LYS GLN GLU ASN GLY LYS ALA LYS VAL SER
SEQRES 18 E 373 LEU ILE THR SER ASP GLY ILE LYS PHE PRO GLN ASP GLY
SEQRES 19 E 373 THR LEU GLU PHE SER ASP VAL THR VAL ASP GLN THR THR
SEQRES 20 E 373 GLY SER ILE THR LEU ARG ALA ILE PHE PRO ASN PRO ASP
SEQRES 21 E 373 HIS THR MET MET PRO GLY MET PHE VAL ARG ALA ARG LEU
SEQRES 22 E 373 GLU GLU GLY LEU ASN PRO ASN ALA ILE LEU VAL PRO GLN
SEQRES 23 E 373 GLN GLY VAL THR ARG THR PRO ARG GLY ASP ALA THR VAL
SEQRES 24 E 373 LEU VAL VAL GLY ALA ASP ASP LYS VAL GLU THR ARG PRO
SEQRES 25 E 373 ILE VAL ALA SER GLN ALA ILE GLY ASP LYS TRP LEU VAL
SEQRES 26 E 373 THR GLU GLY LEU LYS ALA GLY ASP ARG VAL VAL ILE SER
SEQRES 27 E 373 GLY LEU GLN LYS VAL ARG PRO GLY VAL GLN VAL LYS ALA
SEQRES 28 E 373 GLN GLU VAL THR ALA ASP ASN ASN GLN GLN ALA ALA SER
SEQRES 29 E 373 GLY ALA GLN PRO GLU GLN SER LYS SER
SEQRES 1 D 373 CYS ASP ASP LYS GLN ALA GLN GLN GLY GLY GLN GLN MET
SEQRES 2 D 373 PRO ALA VAL GLY VAL VAL THR VAL LYS THR GLU PRO LEU
SEQRES 3 D 373 GLN ILE THR THR GLU LEU PRO GLY ARG THR SER ALA TYR
SEQRES 4 D 373 ARG ILE ALA GLU VAL ARG PRO GLN VAL SER GLY ILE ILE
SEQRES 5 D 373 LEU LYS ARG ASN PHE LYS GLU GLY SER ASP ILE GLU ALA
SEQRES 6 D 373 GLY VAL SER LEU TYR GLN ILE ASP PRO ALA THR TYR GLN
SEQRES 7 D 373 ALA THR TYR ASP SER ALA LYS GLY ASP LEU ALA LYS ALA
SEQRES 8 D 373 GLN ALA ALA ALA ASN ILE ALA GLN LEU THR VAL ASN ARG
SEQRES 9 D 373 TYR GLN LYS LEU LEU GLY THR GLN TYR ILE SER LYS GLN
SEQRES 10 D 373 GLU TYR ASP GLN ALA LEU ALA ASP ALA GLN GLN ALA ASN
SEQRES 11 D 373 ALA ALA VAL THR ALA ALA LYS ALA ALA VAL GLU THR ALA
SEQRES 12 D 373 ARG ILE ASN LEU ALA TYR THR LYS VAL THR SER PRO ILE
SEQRES 13 D 373 SER GLY ARG ILE GLY LYS SER ASN VAL THR GLU GLY ALA
SEQRES 14 D 373 LEU VAL GLN ASN GLY GLN ALA THR ALA LEU ALA THR VAL
SEQRES 15 D 373 GLN GLN LEU ASP PRO ILE TYR VAL ASP VAL THR GLN SER
SEQRES 16 D 373 SER ASN ASP MET MET ARG LEU LYS GLN GLU LEU ALA ASN
SEQRES 17 D 373 GLY THR LEU LYS GLN GLU ASN GLY LYS ALA LYS VAL SER
SEQRES 18 D 373 LEU ILE THR SER ASP GLY ILE LYS PHE PRO GLN ASP GLY
SEQRES 19 D 373 THR LEU GLU PHE SER ASP VAL THR VAL ASP GLN THR THR
SEQRES 20 D 373 GLY SER ILE THR LEU ARG ALA ILE PHE PRO ASN PRO ASP
SEQRES 21 D 373 HIS THR MET MET PRO GLY MET PHE VAL ARG ALA ARG LEU
SEQRES 22 D 373 GLU GLU GLY LEU ASN PRO ASN ALA ILE LEU VAL PRO GLN
SEQRES 23 D 373 GLN GLY VAL THR ARG THR PRO ARG GLY ASP ALA THR VAL
SEQRES 24 D 373 LEU VAL VAL GLY ALA ASP ASP LYS VAL GLU THR ARG PRO
SEQRES 25 D 373 ILE VAL ALA SER GLN ALA ILE GLY ASP LYS TRP LEU VAL
SEQRES 26 D 373 THR GLU GLY LEU LYS ALA GLY ASP ARG VAL VAL ILE SER
SEQRES 27 D 373 GLY LEU GLN LYS VAL ARG PRO GLY VAL GLN VAL LYS ALA
SEQRES 28 D 373 GLN GLU VAL THR ALA ASP ASN ASN GLN GLN ALA ALA SER
SEQRES 29 D 373 GLY ALA GLN PRO GLU GLN SER LYS SER
SEQRES 1 G 373 CYS ASP ASP LYS GLN ALA GLN GLN GLY GLY GLN GLN MET
SEQRES 2 G 373 PRO ALA VAL GLY VAL VAL THR VAL LYS THR GLU PRO LEU
SEQRES 3 G 373 GLN ILE THR THR GLU LEU PRO GLY ARG THR SER ALA TYR
SEQRES 4 G 373 ARG ILE ALA GLU VAL ARG PRO GLN VAL SER GLY ILE ILE
SEQRES 5 G 373 LEU LYS ARG ASN PHE LYS GLU GLY SER ASP ILE GLU ALA
SEQRES 6 G 373 GLY VAL SER LEU TYR GLN ILE ASP PRO ALA THR TYR GLN
SEQRES 7 G 373 ALA THR TYR ASP SER ALA LYS GLY ASP LEU ALA LYS ALA
SEQRES 8 G 373 GLN ALA ALA ALA ASN ILE ALA GLN LEU THR VAL ASN ARG
SEQRES 9 G 373 TYR GLN LYS LEU LEU GLY THR GLN TYR ILE SER LYS GLN
SEQRES 10 G 373 GLU TYR ASP GLN ALA LEU ALA ASP ALA GLN GLN ALA ASN
SEQRES 11 G 373 ALA ALA VAL THR ALA ALA LYS ALA ALA VAL GLU THR ALA
SEQRES 12 G 373 ARG ILE ASN LEU ALA TYR THR LYS VAL THR SER PRO ILE
SEQRES 13 G 373 SER GLY ARG ILE GLY LYS SER ASN VAL THR GLU GLY ALA
SEQRES 14 G 373 LEU VAL GLN ASN GLY GLN ALA THR ALA LEU ALA THR VAL
SEQRES 15 G 373 GLN GLN LEU ASP PRO ILE TYR VAL ASP VAL THR GLN SER
SEQRES 16 G 373 SER ASN ASP MET MET ARG LEU LYS GLN GLU LEU ALA ASN
SEQRES 17 G 373 GLY THR LEU LYS GLN GLU ASN GLY LYS ALA LYS VAL SER
SEQRES 18 G 373 LEU ILE THR SER ASP GLY ILE LYS PHE PRO GLN ASP GLY
SEQRES 19 G 373 THR LEU GLU PHE SER ASP VAL THR VAL ASP GLN THR THR
SEQRES 20 G 373 GLY SER ILE THR LEU ARG ALA ILE PHE PRO ASN PRO ASP
SEQRES 21 G 373 HIS THR MET MET PRO GLY MET PHE VAL ARG ALA ARG LEU
SEQRES 22 G 373 GLU GLU GLY LEU ASN PRO ASN ALA ILE LEU VAL PRO GLN
SEQRES 23 G 373 GLN GLY VAL THR ARG THR PRO ARG GLY ASP ALA THR VAL
SEQRES 24 G 373 LEU VAL VAL GLY ALA ASP ASP LYS VAL GLU THR ARG PRO
SEQRES 25 G 373 ILE VAL ALA SER GLN ALA ILE GLY ASP LYS TRP LEU VAL
SEQRES 26 G 373 THR GLU GLY LEU LYS ALA GLY ASP ARG VAL VAL ILE SER
SEQRES 27 G 373 GLY LEU GLN LYS VAL ARG PRO GLY VAL GLN VAL LYS ALA
SEQRES 28 G 373 GLN GLU VAL THR ALA ASP ASN ASN GLN GLN ALA ALA SER
SEQRES 29 G 373 GLY ALA GLN PRO GLU GLN SER LYS SER
SEQRES 1 H 373 CYS ASP ASP LYS GLN ALA GLN GLN GLY GLY GLN GLN MET
SEQRES 2 H 373 PRO ALA VAL GLY VAL VAL THR VAL LYS THR GLU PRO LEU
SEQRES 3 H 373 GLN ILE THR THR GLU LEU PRO GLY ARG THR SER ALA TYR
SEQRES 4 H 373 ARG ILE ALA GLU VAL ARG PRO GLN VAL SER GLY ILE ILE
SEQRES 5 H 373 LEU LYS ARG ASN PHE LYS GLU GLY SER ASP ILE GLU ALA
SEQRES 6 H 373 GLY VAL SER LEU TYR GLN ILE ASP PRO ALA THR TYR GLN
SEQRES 7 H 373 ALA THR TYR ASP SER ALA LYS GLY ASP LEU ALA LYS ALA
SEQRES 8 H 373 GLN ALA ALA ALA ASN ILE ALA GLN LEU THR VAL ASN ARG
SEQRES 9 H 373 TYR GLN LYS LEU LEU GLY THR GLN TYR ILE SER LYS GLN
SEQRES 10 H 373 GLU TYR ASP GLN ALA LEU ALA ASP ALA GLN GLN ALA ASN
SEQRES 11 H 373 ALA ALA VAL THR ALA ALA LYS ALA ALA VAL GLU THR ALA
SEQRES 12 H 373 ARG ILE ASN LEU ALA TYR THR LYS VAL THR SER PRO ILE
SEQRES 13 H 373 SER GLY ARG ILE GLY LYS SER ASN VAL THR GLU GLY ALA
SEQRES 14 H 373 LEU VAL GLN ASN GLY GLN ALA THR ALA LEU ALA THR VAL
SEQRES 15 H 373 GLN GLN LEU ASP PRO ILE TYR VAL ASP VAL THR GLN SER
SEQRES 16 H 373 SER ASN ASP MET MET ARG LEU LYS GLN GLU LEU ALA ASN
SEQRES 17 H 373 GLY THR LEU LYS GLN GLU ASN GLY LYS ALA LYS VAL SER
SEQRES 18 H 373 LEU ILE THR SER ASP GLY ILE LYS PHE PRO GLN ASP GLY
SEQRES 19 H 373 THR LEU GLU PHE SER ASP VAL THR VAL ASP GLN THR THR
SEQRES 20 H 373 GLY SER ILE THR LEU ARG ALA ILE PHE PRO ASN PRO ASP
SEQRES 21 H 373 HIS THR MET MET PRO GLY MET PHE VAL ARG ALA ARG LEU
SEQRES 22 H 373 GLU GLU GLY LEU ASN PRO ASN ALA ILE LEU VAL PRO GLN
SEQRES 23 H 373 GLN GLY VAL THR ARG THR PRO ARG GLY ASP ALA THR VAL
SEQRES 24 H 373 LEU VAL VAL GLY ALA ASP ASP LYS VAL GLU THR ARG PRO
SEQRES 25 H 373 ILE VAL ALA SER GLN ALA ILE GLY ASP LYS TRP LEU VAL
SEQRES 26 H 373 THR GLU GLY LEU LYS ALA GLY ASP ARG VAL VAL ILE SER
SEQRES 27 H 373 GLY LEU GLN LYS VAL ARG PRO GLY VAL GLN VAL LYS ALA
SEQRES 28 H 373 GLN GLU VAL THR ALA ASP ASN ASN GLN GLN ALA ALA SER
SEQRES 29 H 373 GLY ALA GLN PRO GLU GLN SER LYS SER
SEQRES 1 A 373 CYS ASP ASP LYS GLN ALA GLN GLN GLY GLY GLN GLN MET
SEQRES 2 A 373 PRO ALA VAL GLY VAL VAL THR VAL LYS THR GLU PRO LEU
SEQRES 3 A 373 GLN ILE THR THR GLU LEU PRO GLY ARG THR SER ALA TYR
SEQRES 4 A 373 ARG ILE ALA GLU VAL ARG PRO GLN VAL SER GLY ILE ILE
SEQRES 5 A 373 LEU LYS ARG ASN PHE LYS GLU GLY SER ASP ILE GLU ALA
SEQRES 6 A 373 GLY VAL SER LEU TYR GLN ILE ASP PRO ALA THR TYR GLN
SEQRES 7 A 373 ALA THR TYR ASP SER ALA LYS GLY ASP LEU ALA LYS ALA
SEQRES 8 A 373 GLN ALA ALA ALA ASN ILE ALA GLN LEU THR VAL ASN ARG
SEQRES 9 A 373 TYR GLN LYS LEU LEU GLY THR GLN TYR ILE SER LYS GLN
SEQRES 10 A 373 GLU TYR ASP GLN ALA LEU ALA ASP ALA GLN GLN ALA ASN
SEQRES 11 A 373 ALA ALA VAL THR ALA ALA LYS ALA ALA VAL GLU THR ALA
SEQRES 12 A 373 ARG ILE ASN LEU ALA TYR THR LYS VAL THR SER PRO ILE
SEQRES 13 A 373 SER GLY ARG ILE GLY LYS SER ASN VAL THR GLU GLY ALA
SEQRES 14 A 373 LEU VAL GLN ASN GLY GLN ALA THR ALA LEU ALA THR VAL
SEQRES 15 A 373 GLN GLN LEU ASP PRO ILE TYR VAL ASP VAL THR GLN SER
SEQRES 16 A 373 SER ASN ASP MET MET ARG LEU LYS GLN GLU LEU ALA ASN
SEQRES 17 A 373 GLY THR LEU LYS GLN GLU ASN GLY LYS ALA LYS VAL SER
SEQRES 18 A 373 LEU ILE THR SER ASP GLY ILE LYS PHE PRO GLN ASP GLY
SEQRES 19 A 373 THR LEU GLU PHE SER ASP VAL THR VAL ASP GLN THR THR
SEQRES 20 A 373 GLY SER ILE THR LEU ARG ALA ILE PHE PRO ASN PRO ASP
SEQRES 21 A 373 HIS THR MET MET PRO GLY MET PHE VAL ARG ALA ARG LEU
SEQRES 22 A 373 GLU GLU GLY LEU ASN PRO ASN ALA ILE LEU VAL PRO GLN
SEQRES 23 A 373 GLN GLY VAL THR ARG THR PRO ARG GLY ASP ALA THR VAL
SEQRES 24 A 373 LEU VAL VAL GLY ALA ASP ASP LYS VAL GLU THR ARG PRO
SEQRES 25 A 373 ILE VAL ALA SER GLN ALA ILE GLY ASP LYS TRP LEU VAL
SEQRES 26 A 373 THR GLU GLY LEU LYS ALA GLY ASP ARG VAL VAL ILE SER
SEQRES 27 A 373 GLY LEU GLN LYS VAL ARG PRO GLY VAL GLN VAL LYS ALA
SEQRES 28 A 373 GLN GLU VAL THR ALA ASP ASN ASN GLN GLN ALA ALA SER
SEQRES 29 A 373 GLY ALA GLN PRO GLU GLN SER LYS SER
SEQRES 1 B 373 CYS ASP ASP LYS GLN ALA GLN GLN GLY GLY GLN GLN MET
SEQRES 2 B 373 PRO ALA VAL GLY VAL VAL THR VAL LYS THR GLU PRO LEU
SEQRES 3 B 373 GLN ILE THR THR GLU LEU PRO GLY ARG THR SER ALA TYR
SEQRES 4 B 373 ARG ILE ALA GLU VAL ARG PRO GLN VAL SER GLY ILE ILE
SEQRES 5 B 373 LEU LYS ARG ASN PHE LYS GLU GLY SER ASP ILE GLU ALA
SEQRES 6 B 373 GLY VAL SER LEU TYR GLN ILE ASP PRO ALA THR TYR GLN
SEQRES 7 B 373 ALA THR TYR ASP SER ALA LYS GLY ASP LEU ALA LYS ALA
SEQRES 8 B 373 GLN ALA ALA ALA ASN ILE ALA GLN LEU THR VAL ASN ARG
SEQRES 9 B 373 TYR GLN LYS LEU LEU GLY THR GLN TYR ILE SER LYS GLN
SEQRES 10 B 373 GLU TYR ASP GLN ALA LEU ALA ASP ALA GLN GLN ALA ASN
SEQRES 11 B 373 ALA ALA VAL THR ALA ALA LYS ALA ALA VAL GLU THR ALA
SEQRES 12 B 373 ARG ILE ASN LEU ALA TYR THR LYS VAL THR SER PRO ILE
SEQRES 13 B 373 SER GLY ARG ILE GLY LYS SER ASN VAL THR GLU GLY ALA
SEQRES 14 B 373 LEU VAL GLN ASN GLY GLN ALA THR ALA LEU ALA THR VAL
SEQRES 15 B 373 GLN GLN LEU ASP PRO ILE TYR VAL ASP VAL THR GLN SER
SEQRES 16 B 373 SER ASN ASP MET MET ARG LEU LYS GLN GLU LEU ALA ASN
SEQRES 17 B 373 GLY THR LEU LYS GLN GLU ASN GLY LYS ALA LYS VAL SER
SEQRES 18 B 373 LEU ILE THR SER ASP GLY ILE LYS PHE PRO GLN ASP GLY
SEQRES 19 B 373 THR LEU GLU PHE SER ASP VAL THR VAL ASP GLN THR THR
SEQRES 20 B 373 GLY SER ILE THR LEU ARG ALA ILE PHE PRO ASN PRO ASP
SEQRES 21 B 373 HIS THR MET MET PRO GLY MET PHE VAL ARG ALA ARG LEU
SEQRES 22 B 373 GLU GLU GLY LEU ASN PRO ASN ALA ILE LEU VAL PRO GLN
SEQRES 23 B 373 GLN GLY VAL THR ARG THR PRO ARG GLY ASP ALA THR VAL
SEQRES 24 B 373 LEU VAL VAL GLY ALA ASP ASP LYS VAL GLU THR ARG PRO
SEQRES 25 B 373 ILE VAL ALA SER GLN ALA ILE GLY ASP LYS TRP LEU VAL
SEQRES 26 B 373 THR GLU GLY LEU LYS ALA GLY ASP ARG VAL VAL ILE SER
SEQRES 27 B 373 GLY LEU GLN LYS VAL ARG PRO GLY VAL GLN VAL LYS ALA
SEQRES 28 B 373 GLN GLU VAL THR ALA ASP ASN ASN GLN GLN ALA ALA SER
SEQRES 29 B 373 GLY ALA GLN PRO GLU GLN SER LYS SER
SEQRES 1 F 493 MET LYS LYS LEU LEU PRO ILE LEU ILE GLY LEU SER LEU
SEQRES 2 F 493 SER GLY PHE SER SER LEU SER GLN ALA GLU ASN LEU MET
SEQRES 3 F 493 GLN VAL TYR GLN GLN ALA ARG LEU SER ASN PRO GLU LEU
SEQRES 4 F 493 ARG LYS SER ALA ALA ASP ARG ASP ALA ALA PHE GLU LYS
SEQRES 5 F 493 ILE ASN GLU ALA ARG SER PRO LEU LEU PRO GLN LEU GLY
SEQRES 6 F 493 LEU GLY ALA ASP TYR THR TYR SER ASN GLY TYR ARG ASP
SEQRES 7 F 493 ALA ASN GLY ILE ASN SER ASN ALA THR SER ALA SER LEU
SEQRES 8 F 493 GLN LEU THR GLN SER ILE PHE ASP MET SER LYS TRP ARG
SEQRES 9 F 493 ALA LEU THR LEU GLN GLU LYS ALA ALA GLY ILE GLN ASP
SEQRES 10 F 493 VAL THR TYR GLN THR ASP GLN GLN THR LEU ILE LEU ASN
SEQRES 11 F 493 THR ALA THR ALA TYR PHE ASN VAL LEU ASN ALA ILE ASP
SEQRES 12 F 493 VAL LEU SER TYR THR GLN ALA GLN LYS GLU ALA ILE TYR
SEQRES 13 F 493 ARG GLN LEU ASP GLN THR THR GLN ARG PHE ASN VAL GLY
SEQRES 14 F 493 LEU VAL ALA ILE THR ASP VAL GLN ASN ALA ARG ALA GLN
SEQRES 15 F 493 TYR ASP THR VAL LEU ALA ASN GLU VAL THR ALA ARG ASN
SEQRES 16 F 493 ASN LEU ASP ASN ALA VAL GLU GLN LEU ARG GLN ILE THR
SEQRES 17 F 493 GLY ASN TYR TYR PRO GLU LEU ALA ALA LEU ASN VAL GLU
SEQRES 18 F 493 ASN PHE LYS THR ASP LYS PRO GLN PRO VAL ASN ALA LEU
SEQRES 19 F 493 LEU LYS GLU ALA GLU LYS ARG ASN LEU SER LEU LEU GLN
SEQRES 20 F 493 ALA ARG LEU SER GLN ASP LEU ALA ARG GLU GLN ILE ARG
SEQRES 21 F 493 GLN ALA GLN ASP GLY HIS LEU PRO THR LEU ASP LEU THR
SEQRES 22 F 493 ALA SER THR GLY ILE SER ASP THR SER TYR SER GLY SER
SEQRES 23 F 493 LYS THR ARG GLY ALA ALA GLY THR GLN TYR ASP ASP SER
SEQRES 24 F 493 ASN MET GLY GLN ASN LYS VAL GLY LEU SER PHE SER LEU
SEQRES 25 F 493 PRO ILE TYR GLN GLY GLY MET VAL ASN SER GLN VAL LYS
SEQRES 26 F 493 GLN ALA GLN TYR ASN PHE VAL GLY ALA SER GLU GLN LEU
SEQRES 27 F 493 GLU SER ALA HIS ARG SER VAL VAL GLN THR VAL ARG SER
SEQRES 28 F 493 SER PHE ASN ASN ILE ASN ALA SER ILE SER SER ILE ASN
SEQRES 29 F 493 ALA TYR LYS GLN ALA VAL VAL SER ALA GLN SER SER LEU
SEQRES 30 F 493 ASP ALA MET GLU ALA GLY TYR SER VAL GLY THR ARG THR
SEQRES 31 F 493 ILE VAL ASP VAL LEU ASP ALA THR THR THR LEU TYR ASN
SEQRES 32 F 493 ALA LYS GLN GLU LEU ALA ASN ALA ARG TYR ASN TYR LEU
SEQRES 33 F 493 ILE ASN GLN LEU ASN ILE LYS SER ALA LEU GLY THR LEU
SEQRES 34 F 493 ASN GLU GLN ASP LEU LEU ALA LEU ASN ASN ALA LEU SER
SEQRES 35 F 493 LYS PRO VAL SER THR ASN PRO GLU ASN VAL ALA PRO GLN
SEQRES 36 F 493 THR PRO GLU GLN ASN ALA ILE ALA ASP GLY TYR ALA PRO
SEQRES 37 F 493 ASP SER PRO ALA PRO VAL VAL GLN GLN THR SER ALA ARG
SEQRES 38 F 493 THR THR THR SER ASN GLY HIS ASN PRO PHE ARG ASN
SEQRES 1 I 493 MET LYS LYS LEU LEU PRO ILE LEU ILE GLY LEU SER LEU
SEQRES 2 I 493 SER GLY PHE SER SER LEU SER GLN ALA GLU ASN LEU MET
SEQRES 3 I 493 GLN VAL TYR GLN GLN ALA ARG LEU SER ASN PRO GLU LEU
SEQRES 4 I 493 ARG LYS SER ALA ALA ASP ARG ASP ALA ALA PHE GLU LYS
SEQRES 5 I 493 ILE ASN GLU ALA ARG SER PRO LEU LEU PRO GLN LEU GLY
SEQRES 6 I 493 LEU GLY ALA ASP TYR THR TYR SER ASN GLY TYR ARG ASP
SEQRES 7 I 493 ALA ASN GLY ILE ASN SER ASN ALA THR SER ALA SER LEU
SEQRES 8 I 493 GLN LEU THR GLN SER ILE PHE ASP MET SER LYS TRP ARG
SEQRES 9 I 493 ALA LEU THR LEU GLN GLU LYS ALA ALA GLY ILE GLN ASP
SEQRES 10 I 493 VAL THR TYR GLN THR ASP GLN GLN THR LEU ILE LEU ASN
SEQRES 11 I 493 THR ALA THR ALA TYR PHE ASN VAL LEU ASN ALA ILE ASP
SEQRES 12 I 493 VAL LEU SER TYR THR GLN ALA GLN LYS GLU ALA ILE TYR
SEQRES 13 I 493 ARG GLN LEU ASP GLN THR THR GLN ARG PHE ASN VAL GLY
SEQRES 14 I 493 LEU VAL ALA ILE THR ASP VAL GLN ASN ALA ARG ALA GLN
SEQRES 15 I 493 TYR ASP THR VAL LEU ALA ASN GLU VAL THR ALA ARG ASN
SEQRES 16 I 493 ASN LEU ASP ASN ALA VAL GLU GLN LEU ARG GLN ILE THR
SEQRES 17 I 493 GLY ASN TYR TYR PRO GLU LEU ALA ALA LEU ASN VAL GLU
SEQRES 18 I 493 ASN PHE LYS THR ASP LYS PRO GLN PRO VAL ASN ALA LEU
SEQRES 19 I 493 LEU LYS GLU ALA GLU LYS ARG ASN LEU SER LEU LEU GLN
SEQRES 20 I 493 ALA ARG LEU SER GLN ASP LEU ALA ARG GLU GLN ILE ARG
SEQRES 21 I 493 GLN ALA GLN ASP GLY HIS LEU PRO THR LEU ASP LEU THR
SEQRES 22 I 493 ALA SER THR GLY ILE SER ASP THR SER TYR SER GLY SER
SEQRES 23 I 493 LYS THR ARG GLY ALA ALA GLY THR GLN TYR ASP ASP SER
SEQRES 24 I 493 ASN MET GLY GLN ASN LYS VAL GLY LEU SER PHE SER LEU
SEQRES 25 I 493 PRO ILE TYR GLN GLY GLY MET VAL ASN SER GLN VAL LYS
SEQRES 26 I 493 GLN ALA GLN TYR ASN PHE VAL GLY ALA SER GLU GLN LEU
SEQRES 27 I 493 GLU SER ALA HIS ARG SER VAL VAL GLN THR VAL ARG SER
SEQRES 28 I 493 SER PHE ASN ASN ILE ASN ALA SER ILE SER SER ILE ASN
SEQRES 29 I 493 ALA TYR LYS GLN ALA VAL VAL SER ALA GLN SER SER LEU
SEQRES 30 I 493 ASP ALA MET GLU ALA GLY TYR SER VAL GLY THR ARG THR
SEQRES 31 I 493 ILE VAL ASP VAL LEU ASP ALA THR THR THR LEU TYR ASN
SEQRES 32 I 493 ALA LYS GLN GLU LEU ALA ASN ALA ARG TYR ASN TYR LEU
SEQRES 33 I 493 ILE ASN GLN LEU ASN ILE LYS SER ALA LEU GLY THR LEU
SEQRES 34 I 493 ASN GLU GLN ASP LEU LEU ALA LEU ASN ASN ALA LEU SER
SEQRES 35 I 493 LYS PRO VAL SER THR ASN PRO GLU ASN VAL ALA PRO GLN
SEQRES 36 I 493 THR PRO GLU GLN ASN ALA ILE ALA ASP GLY TYR ALA PRO
SEQRES 37 I 493 ASP SER PRO ALA PRO VAL VAL GLN GLN THR SER ALA ARG
SEQRES 38 I 493 THR THR THR SER ASN GLY HIS ASN PRO PHE ARG ASN
SEQRES 1 C 493 MET LYS LYS LEU LEU PRO ILE LEU ILE GLY LEU SER LEU
SEQRES 2 C 493 SER GLY PHE SER SER LEU SER GLN ALA GLU ASN LEU MET
SEQRES 3 C 493 GLN VAL TYR GLN GLN ALA ARG LEU SER ASN PRO GLU LEU
SEQRES 4 C 493 ARG LYS SER ALA ALA ASP ARG ASP ALA ALA PHE GLU LYS
SEQRES 5 C 493 ILE ASN GLU ALA ARG SER PRO LEU LEU PRO GLN LEU GLY
SEQRES 6 C 493 LEU GLY ALA ASP TYR THR TYR SER ASN GLY TYR ARG ASP
SEQRES 7 C 493 ALA ASN GLY ILE ASN SER ASN ALA THR SER ALA SER LEU
SEQRES 8 C 493 GLN LEU THR GLN SER ILE PHE ASP MET SER LYS TRP ARG
SEQRES 9 C 493 ALA LEU THR LEU GLN GLU LYS ALA ALA GLY ILE GLN ASP
SEQRES 10 C 493 VAL THR TYR GLN THR ASP GLN GLN THR LEU ILE LEU ASN
SEQRES 11 C 493 THR ALA THR ALA TYR PHE ASN VAL LEU ASN ALA ILE ASP
SEQRES 12 C 493 VAL LEU SER TYR THR GLN ALA GLN LYS GLU ALA ILE TYR
SEQRES 13 C 493 ARG GLN LEU ASP GLN THR THR GLN ARG PHE ASN VAL GLY
SEQRES 14 C 493 LEU VAL ALA ILE THR ASP VAL GLN ASN ALA ARG ALA GLN
SEQRES 15 C 493 TYR ASP THR VAL LEU ALA ASN GLU VAL THR ALA ARG ASN
SEQRES 16 C 493 ASN LEU ASP ASN ALA VAL GLU GLN LEU ARG GLN ILE THR
SEQRES 17 C 493 GLY ASN TYR TYR PRO GLU LEU ALA ALA LEU ASN VAL GLU
SEQRES 18 C 493 ASN PHE LYS THR ASP LYS PRO GLN PRO VAL ASN ALA LEU
SEQRES 19 C 493 LEU LYS GLU ALA GLU LYS ARG ASN LEU SER LEU LEU GLN
SEQRES 20 C 493 ALA ARG LEU SER GLN ASP LEU ALA ARG GLU GLN ILE ARG
SEQRES 21 C 493 GLN ALA GLN ASP GLY HIS LEU PRO THR LEU ASP LEU THR
SEQRES 22 C 493 ALA SER THR GLY ILE SER ASP THR SER TYR SER GLY SER
SEQRES 23 C 493 LYS THR ARG GLY ALA ALA GLY THR GLN TYR ASP ASP SER
SEQRES 24 C 493 ASN MET GLY GLN ASN LYS VAL GLY LEU SER PHE SER LEU
SEQRES 25 C 493 PRO ILE TYR GLN GLY GLY MET VAL ASN SER GLN VAL LYS
SEQRES 26 C 493 GLN ALA GLN TYR ASN PHE VAL GLY ALA SER GLU GLN LEU
SEQRES 27 C 493 GLU SER ALA HIS ARG SER VAL VAL GLN THR VAL ARG SER
SEQRES 28 C 493 SER PHE ASN ASN ILE ASN ALA SER ILE SER SER ILE ASN
SEQRES 29 C 493 ALA TYR LYS GLN ALA VAL VAL SER ALA GLN SER SER LEU
SEQRES 30 C 493 ASP ALA MET GLU ALA GLY TYR SER VAL GLY THR ARG THR
SEQRES 31 C 493 ILE VAL ASP VAL LEU ASP ALA THR THR THR LEU TYR ASN
SEQRES 32 C 493 ALA LYS GLN GLU LEU ALA ASN ALA ARG TYR ASN TYR LEU
SEQRES 33 C 493 ILE ASN GLN LEU ASN ILE LYS SER ALA LEU GLY THR LEU
SEQRES 34 C 493 ASN GLU GLN ASP LEU LEU ALA LEU ASN ASN ALA LEU SER
SEQRES 35 C 493 LYS PRO VAL SER THR ASN PRO GLU ASN VAL ALA PRO GLN
SEQRES 36 C 493 THR PRO GLU GLN ASN ALA ILE ALA ASP GLY TYR ALA PRO
SEQRES 37 C 493 ASP SER PRO ALA PRO VAL VAL GLN GLN THR SER ALA ARG
SEQRES 38 C 493 THR THR THR SER ASN GLY HIS ASN PRO PHE ARG ASN
SEQRES 1 K 1049 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 K 1049 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 K 1049 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 K 1049 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 K 1049 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 K 1049 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 K 1049 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 K 1049 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 K 1049 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 K 1049 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 K 1049 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 K 1049 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 K 1049 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 K 1049 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 K 1049 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 K 1049 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 K 1049 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 K 1049 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 K 1049 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 K 1049 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 K 1049 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 K 1049 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 K 1049 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 K 1049 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 K 1049 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 K 1049 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 K 1049 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 K 1049 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 K 1049 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 K 1049 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 K 1049 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 K 1049 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 K 1049 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 K 1049 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 K 1049 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 K 1049 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 K 1049 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 K 1049 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 K 1049 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 K 1049 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 K 1049 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 K 1049 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 K 1049 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 K 1049 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 K 1049 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 K 1049 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 K 1049 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 K 1049 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 K 1049 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 K 1049 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 K 1049 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 K 1049 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 K 1049 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 K 1049 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 K 1049 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 K 1049 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 K 1049 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 K 1049 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 K 1049 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 K 1049 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 K 1049 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 K 1049 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 K 1049 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 K 1049 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 K 1049 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 K 1049 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 K 1049 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 K 1049 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 K 1049 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 K 1049 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 K 1049 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 K 1049 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 K 1049 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 K 1049 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 K 1049 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 K 1049 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 K 1049 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 K 1049 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 K 1049 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 K 1049 VAL VAL ARG ARG ARG PHE SER ARG LYS ASN GLU ASP ILE
SEQRES 81 K 1049 GLU HIS SER HIS THR VAL ASP HIS HIS
SEQRES 1 L 1049 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 L 1049 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 L 1049 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 L 1049 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 L 1049 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 L 1049 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 L 1049 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 L 1049 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 L 1049 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 L 1049 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 L 1049 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 L 1049 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 L 1049 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 L 1049 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 L 1049 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 L 1049 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 L 1049 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 L 1049 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 L 1049 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 L 1049 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 L 1049 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 L 1049 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 L 1049 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 L 1049 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 L 1049 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 L 1049 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 L 1049 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 L 1049 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 L 1049 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 L 1049 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 L 1049 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 L 1049 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 L 1049 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 L 1049 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 L 1049 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 L 1049 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 L 1049 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 L 1049 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 L 1049 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 L 1049 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 L 1049 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 L 1049 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 L 1049 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 L 1049 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 L 1049 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 L 1049 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 L 1049 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 L 1049 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 L 1049 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 L 1049 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 L 1049 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 L 1049 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 L 1049 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 L 1049 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 L 1049 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 L 1049 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 L 1049 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 L 1049 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 L 1049 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 L 1049 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 L 1049 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 L 1049 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 L 1049 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 L 1049 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 L 1049 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 L 1049 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 L 1049 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 L 1049 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 L 1049 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 L 1049 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 L 1049 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 L 1049 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 L 1049 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 L 1049 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 L 1049 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 L 1049 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 L 1049 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 L 1049 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 L 1049 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 L 1049 VAL VAL ARG ARG ARG PHE SER ARG LYS ASN GLU ASP ILE
SEQRES 81 L 1049 GLU HIS SER HIS THR VAL ASP HIS HIS
SEQRES 1 M 54 MET LEU GLU LEU LEU LYS SER LEU VAL PHE ALA VAL ILE
SEQRES 2 M 54 MET VAL PRO VAL VAL MET ALA ILE ILE LEU GLY LEU ILE
SEQRES 3 M 54 TYR GLY LEU GLY GLU VAL PHE ASN ILE PHE SER GLY VAL
SEQRES 4 M 54 GLY LYS LYS ASP GLN PRO GLY GLN ASN HIS HIS HIS HIS
SEQRES 5 M 54 HIS HIS
SEQRES 1 N 54 MET LEU GLU LEU LEU LYS SER LEU VAL PHE ALA VAL ILE
SEQRES 2 N 54 MET VAL PRO VAL VAL MET ALA ILE ILE LEU GLY LEU ILE
SEQRES 3 N 54 TYR GLY LEU GLY GLU VAL PHE ASN ILE PHE SER GLY VAL
SEQRES 4 N 54 GLY LYS LYS ASP GLN PRO GLY GLN ASN HIS HIS HIS HIS
SEQRES 5 N 54 HIS HIS
SEQRES 1 O 54 MET LEU GLU LEU LEU LYS SER LEU VAL PHE ALA VAL ILE
SEQRES 2 O 54 MET VAL PRO VAL VAL MET ALA ILE ILE LEU GLY LEU ILE
SEQRES 3 O 54 TYR GLY LEU GLY GLU VAL PHE ASN ILE PHE SER GLY VAL
SEQRES 4 O 54 GLY LYS LYS ASP GLN PRO GLY GLN ASN HIS HIS HIS HIS
SEQRES 5 O 54 HIS HIS
SEQRES 1 J 1049 MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES 2 J 1049 VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES 3 J 1049 ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES 4 J 1049 PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES 5 J 1049 ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES 6 J 1049 GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES 7 J 1049 SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES 8 J 1049 LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES 9 J 1049 VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES 10 J 1049 LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES 11 J 1049 LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES 12 J 1049 ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES 13 J 1049 TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES 14 J 1049 SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES 15 J 1049 ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES 16 J 1049 PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES 17 J 1049 ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES 18 J 1049 THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES 19 J 1049 ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES 20 J 1049 LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES 21 J 1049 LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES 22 J 1049 ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES 23 J 1049 SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES 24 J 1049 LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES 25 J 1049 MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES 26 J 1049 PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES 27 J 1049 GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES 28 J 1049 PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES 29 J 1049 THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES 30 J 1049 GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES 31 J 1049 ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES 32 J 1049 LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES 33 J 1049 GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES 34 J 1049 ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES 35 J 1049 VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES 36 J 1049 MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES 37 J 1049 GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES 38 J 1049 VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES 39 J 1049 THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES 40 J 1049 GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES 41 J 1049 GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES 42 J 1049 ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES 43 J 1049 ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES 44 J 1049 PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES 45 J 1049 MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES 46 J 1049 ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES 47 J 1049 LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES 48 J 1049 VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES 49 J 1049 GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES 50 J 1049 PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES 51 J 1049 ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES 52 J 1049 PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES 53 J 1049 ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES 54 J 1049 LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES 55 J 1049 LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES 56 J 1049 VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES 57 J 1049 ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES 58 J 1049 SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES 59 J 1049 GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES 60 J 1049 VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES 61 J 1049 MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES 62 J 1049 ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES 63 J 1049 SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES 64 J 1049 ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES 65 J 1049 PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES 66 J 1049 GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES 67 J 1049 TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES 68 J 1049 GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES 69 J 1049 PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES 70 J 1049 PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES 71 J 1049 GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES 72 J 1049 ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES 73 J 1049 LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES 74 J 1049 LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES 75 J 1049 ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES 76 J 1049 LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES 77 J 1049 LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES 78 J 1049 ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES 79 J 1049 THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES 80 J 1049 VAL VAL ARG ARG ARG PHE SER ARG LYS ASN GLU ASP ILE
SEQRES 81 J 1049 GLU HIS SER HIS THR VAL ASP HIS HIS
HET 5QF K1101 75
HET 5QF L1101 75
HET 5QF J1101 75
HETNAM 5QF 6-[2-(3,4-DIMETHOXYPHENYL)ETHYLSULFANYL]-8-[4-(2-
HETNAM 2 5QF METHOXYETHYL)PIPERAZIN-1-YL]-3,3-DIMETHYL-1,4-
HETNAM 3 5QF DIHYDROPYRANO[3,4-C]PYRIDINE-5-CARBONITRILE
FORMUL 16 5QF 3(C28 H38 N4 O4 S)
HELIX 1 AA1 PRO E 98 ARG E 128 1 31
HELIX 2 AA2 TYR E 129 LEU E 133 5 5
HELIX 3 AA3 LYS E 140 ILE E 169 1 30
HELIX 4 AA4 ASN E 221 LEU E 226 1 6
HELIX 5 AA5 GLY E 363 VAL E 367 5 5
HELIX 6 AA6 PRO D 98 LYS D 131 1 34
HELIX 7 AA7 LYS D 140 ILE D 169 1 30
HELIX 8 AA8 ASN D 221 GLU D 229 1 9
HELIX 9 AA9 ASP G 97 ARG G 128 1 32
HELIX 10 AB1 TYR G 129 LEU G 133 5 5
HELIX 11 AB2 LYS G 140 ILE G 169 1 30
HELIX 12 AB3 SER G 219 LEU G 226 1 8
HELIX 13 AB4 GLY G 363 VAL G 367 5 5
HELIX 14 AB5 TYR H 101 LYS H 131 1 31
HELIX 15 AB6 SER H 139 THR H 174 1 36
HELIX 16 AB7 SER H 220 GLY H 233 1 14
HELIX 17 AB8 TYR A 101 ALA A 117 1 17
HELIX 18 AB9 ALA A 117 LYS A 131 1 15
HELIX 19 AC1 SER A 139 THR A 174 1 36
HELIX 20 AC2 SER A 220 GLY A 233 1 14
HELIX 21 AC3 PRO B 98 THR B 100 5 3
HELIX 22 AC4 TYR B 101 LYS B 131 1 31
HELIX 23 AC5 SER B 139 THR B 174 1 36
HELIX 24 AC6 SER B 220 GLY B 233 1 14
HELIX 25 AC7 ASN F 2 SER F 13 1 12
HELIX 26 AC8 ASN F 14 SER F 36 1 23
HELIX 27 AC9 ASP F 77 ASN F 145 1 69
HELIX 28 AD1 ALA F 150 THR F 186 1 37
HELIX 29 AD2 PRO F 208 ASN F 220 1 13
HELIX 30 AD3 ASN F 220 GLN F 241 1 22
HELIX 31 AD4 ASP F 242 HIS F 244 5 3
HELIX 32 AD5 GLY F 296 VAL F 364 1 69
HELIX 33 AD6 THR F 368 GLY F 405 1 38
HELIX 34 AD7 GLN F 410 ASN F 417 1 8
HELIX 35 AD8 ASN I 2 SER I 13 1 12
HELIX 36 AD9 ASN I 14 SER I 36 1 23
HELIX 37 AE1 ASP I 77 ASN I 145 1 69
HELIX 38 AE2 ALA I 150 THR I 186 1 37
HELIX 39 AE3 PRO I 208 ASN I 220 1 13
HELIX 40 AE4 ASN I 220 GLN I 241 1 22
HELIX 41 AE5 ASP I 242 HIS I 244 5 3
HELIX 42 AE6 GLY I 296 GLY I 365 1 70
HELIX 43 AE7 THR I 368 GLY I 405 1 38
HELIX 44 AE8 GLN I 410 ASN I 417 1 8
HELIX 45 AE9 ASN C 2 SER C 13 1 12
HELIX 46 AF1 ASN C 14 SER C 36 1 23
HELIX 47 AF2 ASP C 77 ASN C 145 1 69
HELIX 48 AF3 ALA C 150 THR C 186 1 37
HELIX 49 AF4 PRO C 208 ASN C 220 1 13
HELIX 50 AF5 ASN C 220 GLN C 241 1 22
HELIX 51 AF6 ASP C 242 HIS C 244 5 3
HELIX 52 AF7 GLY C 296 VAL C 364 1 69
HELIX 53 AF8 THR C 368 GLY C 405 1 38
HELIX 54 AF9 GLN C 410 ASN C 417 1 8
HELIX 55 AG1 PRO K 2 ASP K 7 1 6
HELIX 56 AG2 ILE K 10 ILE K 27 1 18
HELIX 57 AG3 ASP K 53 THR K 60 1 8
HELIX 58 AG4 VAL K 61 GLN K 67 1 7
HELIX 59 AG5 ALA K 100 LYS K 110 1 11
HELIX 60 AG6 THR K 150 ASN K 161 1 12
HELIX 61 AG7 MET K 162 SER K 167 1 6
HELIX 62 AG8 ASN K 189 GLN K 197 1 9
HELIX 63 AG9 THR K 199 ASN K 211 1 13
HELIX 64 AH1 SER K 242 LYS K 248 1 7
HELIX 65 AH2 ALA K 299 ALA K 311 1 13
HELIX 66 AH3 THR K 329 TYR K 356 1 28
HELIX 67 AH4 ILE K 367 GLY K 387 1 21
HELIX 68 AH5 THR K 394 VAL K 399 1 6
HELIX 69 AH6 VAL K 406 ILE K 410 5 5
HELIX 70 AH7 VAL K 411 GLY K 424 1 14
HELIX 71 AH8 PRO K 426 GLN K 439 1 14
HELIX 72 AH9 MET K 447 VAL K 452 1 6
HELIX 73 AI1 PHE K 453 PHE K 459 5 7
HELIX 74 AI2 GLY K 461 LEU K 486 1 26
HELIX 75 AI3 ILE K 487 CYS K 493 1 7
HELIX 76 AI4 PHE K 512 ASN K 517 1 6
HELIX 77 AI5 GLU K 521 GLY K 532 1 12
HELIX 78 AI6 ARG K 536 ARG K 540 5 5
HELIX 79 AI7 TYR K 541 VAL K 549 1 9
HELIX 80 AI8 VAL K 549 LEU K 559 1 11
HELIX 81 AI9 THR K 583 LYS K 601 1 19
HELIX 82 AJ1 GLY K 639 ASN K 642 5 4
HELIX 83 AJ2 LYS K 643 SER K 656 1 14
HELIX 84 AJ3 HIS K 692 LYS K 708 1 17
HELIX 85 AJ4 ASP K 732 GLY K 740 1 9
HELIX 86 AJ5 SER K 742 TRP K 754 1 13
HELIX 87 AJ6 ALA K 777 ARG K 780 5 4
HELIX 88 AJ7 LEU K 782 GLY K 787 5 6
HELIX 89 AJ8 SER K 836 LEU K 847 1 12
HELIX 90 AJ9 TYR K 864 SER K 869 1 6
HELIX 91 AK1 GLN K 872 TYR K 877 1 6
HELIX 92 AK2 ALA K 878 GLU K 893 1 16
HELIX 93 AK3 SER K 896 VAL K 904 5 9
HELIX 94 AK4 VAL K 905 PHE K 918 1 14
HELIX 95 AK5 ASP K 924 THR K 933 1 10
HELIX 96 AK6 THR K 934 LYS K 955 1 22
HELIX 97 AK7 ILE K 961 ASP K 966 1 6
HELIX 98 AK8 ASP K 966 ARG K 971 1 6
HELIX 99 AK9 ARG K 971 LEU K 976 1 6
HELIX 100 AL1 SER K 979 LEU K 984 1 6
HELIX 101 AL2 GLN K 1000 VAL K 1016 1 17
HELIX 102 AL3 LEU K 1017 PHE K 1021 5 5
HELIX 103 AL4 VAL K 1022 VAL K 1027 1 6
HELIX 104 AL5 VAL K 1028 PHE K 1033 1 6
HELIX 105 AL6 MET L 1 PHE L 5 5 5
HELIX 106 AL7 PRO L 9 GLY L 23 1 15
HELIX 107 AL8 GLY L 23 LEU L 30 1 8
HELIX 108 AL9 ASP L 53 THR L 60 1 8
HELIX 109 AM1 VAL L 61 MET L 69 1 9
HELIX 110 AM2 ALA L 100 GLN L 106 1 7
HELIX 111 AM3 GLU L 121 GLY L 126 1 6
HELIX 112 AM4 THR L 150 MET L 162 1 13
HELIX 113 AM5 MET L 162 THR L 169 1 8
HELIX 114 AM6 ASN L 189 GLN L 197 1 9
HELIX 115 AM7 THR L 199 ASN L 211 1 13
HELIX 116 AM8 LEU L 261 VAL L 265 5 5
HELIX 117 AM9 ALA L 299 ALA L 311 1 13
HELIX 118 AN1 THR L 329 TYR L 356 1 28
HELIX 119 AN2 THR L 365 GLY L 387 1 23
HELIX 120 AN3 THR L 394 LEU L 400 1 7
HELIX 121 AN4 LEU L 400 LEU L 405 1 6
HELIX 122 AN5 ASP L 408 MET L 420 1 13
HELIX 123 AN6 PRO L 426 SER L 434 1 9
HELIX 124 AN7 THR L 463 ILE L 472 1 10
HELIX 125 AN8 ILE L 472 LEU L 483 1 12
HELIX 126 AN9 ILE L 487 LEU L 492 1 6
HELIX 127 AO1 GLY L 511 ASN L 517 1 7
HELIX 128 AO2 GLU L 521 SER L 537 1 17
HELIX 129 AO3 TYR L 541 LEU L 546 1 6
HELIX 130 AO4 VAL L 549 LEU L 559 1 11
HELIX 131 AO5 THR L 583 LYS L 601 1 19
HELIX 132 AO6 GLY L 639 ASN L 642 5 4
HELIX 133 AO7 LYS L 643 PHE L 655 1 13
HELIX 134 AO8 HIS L 692 ALA L 707 1 16
HELIX 135 AO9 ASP L 732 GLY L 740 1 9
HELIX 136 AP1 SER L 742 TRP L 754 1 13
HELIX 137 AP2 GLU L 776 ARG L 780 5 5
HELIX 138 AP3 PRO L 783 GLY L 787 5 5
HELIX 139 AP4 SER L 836 SER L 849 1 14
HELIX 140 AP5 MET L 862 SER L 869 1 8
HELIX 141 AP6 TYR L 877 SER L 880 5 4
HELIX 142 AP7 LEU L 881 GLU L 893 1 13
HELIX 143 AP8 SER L 896 VAL L 901 5 6
HELIX 144 AP9 VAL L 905 ALA L 915 1 11
HELIX 145 AQ1 ASP L 924 ILE L 945 1 22
HELIX 146 AQ2 GLU L 947 LYS L 955 1 9
HELIX 147 AQ3 GLY L 959 ALA L 967 1 9
HELIX 148 AQ4 ARG L 971 LEU L 976 1 6
HELIX 149 AQ5 THR L 978 LEU L 984 1 7
HELIX 150 AQ6 GLY L 985 MET L 987 5 3
HELIX 151 AQ7 MET L 1011 VAL L 1016 1 6
HELIX 152 AQ8 PHE L 1021 ARG L 1030 1 10
HELIX 153 AQ9 LEU M 2 PHE M 10 1 9
HELIX 154 AR1 VAL M 15 TYR M 27 1 13
HELIX 155 AR2 TYR M 27 PHE M 33 1 7
HELIX 156 AR3 ILE N 13 PHE N 33 1 21
HELIX 157 AR4 LEU O 2 PHE O 10 1 9
HELIX 158 AR5 ILE O 13 TYR O 27 1 15
HELIX 159 AR6 TYR O 27 PHE O 36 1 10
HELIX 160 AR7 ARG J 8 ILE J 27 1 20
HELIX 161 AR8 VAL J 61 GLN J 67 1 7
HELIX 162 AR9 ASP J 99 GLN J 108 1 10
HELIX 163 AS1 ALA J 114 PRO J 119 5 6
HELIX 164 AS2 GLN J 120 GLN J 125 1 6
HELIX 165 AS3 THR J 150 MET J 162 1 13
HELIX 166 AS4 MET J 162 SER J 167 1 6
HELIX 167 AS5 ASN J 189 ASN J 194 1 6
HELIX 168 AS6 LYS J 195 GLN J 197 5 3
HELIX 169 AS7 THR J 199 ASN J 211 1 13
HELIX 170 AS8 THR J 243 LYS J 248 1 6
HELIX 171 AS9 LEU J 261 ASP J 264 5 4
HELIX 172 AT1 ASN J 298 GLU J 314 1 17
HELIX 173 AT2 THR J 329 LEU J 353 1 25
HELIX 174 AT3 VAL J 354 LEU J 359 1 6
HELIX 175 AT4 LEU J 366 GLY J 387 1 22
HELIX 176 AT5 MET J 395 LEU J 400 1 6
HELIX 177 AT6 ALA J 401 VAL J 406 1 6
HELIX 178 AT7 ASP J 408 ALA J 421 1 14
HELIX 179 AT8 PRO J 426 ARG J 432 1 7
HELIX 180 AT9 ARG J 432 GLY J 440 1 9
HELIX 181 AU1 GLY J 440 VAL J 452 1 13
HELIX 182 AU2 PHE J 453 PHE J 458 5 6
HELIX 183 AU3 GLY J 460 LEU J 486 1 27
HELIX 184 AU4 ILE J 487 CYS J 493 1 7
HELIX 185 AU5 GLY J 511 TYR J 527 1 17
HELIX 186 AU6 TYR J 527 ARG J 536 1 10
HELIX 187 AU7 GLY J 539 ARG J 558 1 20
HELIX 188 AU8 THR J 583 TYR J 598 1 16
HELIX 189 AU9 GLY J 639 ASN J 642 5 4
HELIX 190 AV1 LYS J 643 GLN J 657 1 15
HELIX 191 AV2 HIS J 692 ALA J 706 1 15
HELIX 192 AV3 GLU J 734 LEU J 739 1 6
HELIX 193 AV4 ILE J 743 ALA J 753 1 11
HELIX 194 AV5 ALA J 777 ARG J 780 5 4
HELIX 195 AV6 LEU J 782 ILE J 786 5 5
HELIX 196 AV7 SER J 802 PHE J 804 5 3
HELIX 197 AV8 THR J 837 ALA J 848 1 12
HELIX 198 AV9 GLY J 861 ALA J 873 1 13
HELIX 199 AW1 SER J 875 GLU J 893 1 19
HELIX 200 AW2 SER J 896 LEU J 903 5 8
HELIX 201 AW3 VAL J 904 PHE J 918 1 15
HELIX 202 AW4 ASP J 924 LEU J 944 1 21
HELIX 203 AW5 ILE J 945 GLU J 956 1 12
HELIX 204 AW6 LEU J 960 ARG J 971 1 12
HELIX 205 AW7 LEU J 972 ILE J 983 1 12
HELIX 206 AW8 VAL J 986 ILE J 991 1 6
HELIX 207 AW9 SER J 997 VAL J 1016 1 20
HELIX 208 AX1 PHE J 1020 VAL J 1028 1 9
HELIX 209 AX2 VAL J 1028 PHE J 1033 1 6
SHEET 1 AA1 2 ALA E 39 GLY E 41 0
SHEET 2 AA1 2 LYS E 374 GLN E 376 1 N GLN E 376 O VAL E 40
SHEET 1 AA2 2 VAL E 43 THR E 44 0
SHEET 2 AA2 2 ARG E 358 VAL E 359 -1 O VAL E 359 N VAL E 43
SHEET 1 AA3 7 GLU E 55 LEU E 56 0
SHEET 2 AA3 7 ARG E 294 GLU E 298 -1 O ALA E 295 N LEU E 56
SHEET 3 AA3 7 LYS E 243 ILE E 247 -1 N LYS E 243 O GLU E 298
SHEET 4 AA3 7 GLY E 258 SER E 263 -1 O GLY E 258 N VAL E 244
SHEET 5 AA3 7 LEU E 276 PRO E 281 -1 O ARG E 277 N GLU E 261
SHEET 6 AA3 7 PRO E 211 VAL E 214 -1 N ILE E 212 O PHE E 280
SHEET 7 AA3 7 THR E 60 SER E 61 -1 N SER E 61 O TYR E 213
SHEET 1 AA4 3 TYR E 94 ILE E 96 0
SHEET 2 AA4 3 GLY E 74 ARG E 79 -1 N LEU E 77 O GLN E 95
SHEET 3 AA4 3 LEU E 194 VAL E 195 -1 O VAL E 195 N GLY E 74
SHEET 1 AA5 2 ASP E 86 ILE E 87 0
SHEET 2 AA5 2 GLY E 182 ARG E 183 -1 O GLY E 182 N ILE E 87
SHEET 1 AA6 2 VAL E 308 PRO E 309 0
SHEET 2 AA6 2 LYS E 346 TRP E 347 -1 O TRP E 347 N VAL E 308
SHEET 1 AA7 3 VAL E 313 THR E 314 0
SHEET 2 AA7 3 THR E 322 VAL E 323 -1 O THR E 322 N THR E 314
SHEET 3 AA7 3 ARG E 335 PRO E 336 -1 O ARG E 335 N VAL E 323
SHEET 1 AA8 2 ALA D 39 GLY D 41 0
SHEET 2 AA8 2 LYS D 374 GLN D 376 1 O LYS D 374 N VAL D 40
SHEET 1 AA9 2 VAL D 43 THR D 44 0
SHEET 2 AA9 2 ARG D 358 VAL D 359 -1 O VAL D 359 N VAL D 43
SHEET 1 AB1 6 THR D 60 SER D 61 0
SHEET 2 AB1 6 PRO D 211 VAL D 214 -1 O TYR D 213 N SER D 61
SHEET 3 AB1 6 ALA D 278 PRO D 281 -1 O PHE D 280 N ILE D 212
SHEET 4 AB1 6 GLY D 258 LEU D 260 -1 N THR D 259 O ILE D 279
SHEET 5 AB1 6 LYS D 243 ILE D 247 -1 N VAL D 244 O GLY D 258
SHEET 6 AB1 6 ARG D 294 GLU D 298 -1 O ARG D 294 N ILE D 247
SHEET 1 AB2 3 TYR D 94 ILE D 96 0
SHEET 2 AB2 3 GLY D 74 ARG D 79 -1 N LEU D 77 O GLN D 95
SHEET 3 AB2 3 LEU D 194 VAL D 195 -1 O VAL D 195 N GLY D 74
SHEET 1 AB3 3 ASP D 86 ILE D 87 0
SHEET 2 AB3 3 GLY D 182 ILE D 184 -1 O GLY D 182 N ILE D 87
SHEET 3 AB3 3 VAL D 206 GLN D 207 -1 O GLN D 207 N ARG D 183
SHEET 1 AB4 2 THR D 217 GLN D 218 0
SHEET 2 AB4 2 ILE D 274 THR D 275 -1 O ILE D 274 N GLN D 218
SHEET 1 AB5 2 VAL D 308 PRO D 309 0
SHEET 2 AB5 2 LYS D 346 TRP D 347 -1 O TRP D 347 N VAL D 308
SHEET 1 AB6 3 VAL D 313 THR D 314 0
SHEET 2 AB6 3 THR D 322 VAL D 323 -1 O THR D 322 N THR D 314
SHEET 3 AB6 3 ARG D 335 PRO D 336 -1 O ARG D 335 N VAL D 323
SHEET 1 AB7 2 ALA G 39 GLY G 41 0
SHEET 2 AB7 2 LYS G 374 GLN G 376 1 O LYS G 374 N VAL G 40
SHEET 1 AB8 2 VAL G 43 THR G 44 0
SHEET 2 AB8 2 ARG G 358 VAL G 359 -1 O VAL G 359 N VAL G 43
SHEET 1 AB9 4 THR G 60 SER G 61 0
SHEET 2 AB9 4 PRO G 211 VAL G 214 -1 O TYR G 213 N SER G 61
SHEET 3 AB9 4 ILE G 274 PRO G 281 -1 O PHE G 280 N ILE G 212
SHEET 4 AB9 4 THR G 217 GLN G 218 -1 N GLN G 218 O ILE G 274
SHEET 1 AC1 6 THR G 60 SER G 61 0
SHEET 2 AC1 6 PRO G 211 VAL G 214 -1 O TYR G 213 N SER G 61
SHEET 3 AC1 6 ILE G 274 PRO G 281 -1 O PHE G 280 N ILE G 212
SHEET 4 AC1 6 GLY G 258 SER G 263 -1 N GLU G 261 O ARG G 277
SHEET 5 AC1 6 LYS G 243 ILE G 247 -1 N VAL G 244 O GLY G 258
SHEET 6 AC1 6 ARG G 294 LEU G 297 -1 O ARG G 296 N SER G 245
SHEET 1 AC2 2 GLY G 74 ILE G 75 0
SHEET 2 AC2 2 LEU G 194 VAL G 195 -1 O VAL G 195 N GLY G 74
SHEET 1 AC3 2 ASP G 86 ILE G 87 0
SHEET 2 AC3 2 GLY G 182 ARG G 183 -1 O GLY G 182 N ILE G 87
SHEET 1 AC4 2 VAL G 308 PRO G 309 0
SHEET 2 AC4 2 LYS G 346 TRP G 347 -1 O TRP G 347 N VAL G 308
SHEET 1 AC5 3 VAL G 313 THR G 314 0
SHEET 2 AC5 3 THR G 322 VAL G 323 -1 O THR G 322 N THR G 314
SHEET 3 AC5 3 ARG G 335 PRO G 336 -1 O ARG G 335 N VAL G 323
SHEET 1 AC6 3 ARG H 358 VAL H 360 0
SHEET 2 AC6 3 ALA H 39 THR H 44 -1 N VAL H 43 O VAL H 359
SHEET 3 AC6 3 LYS H 374 GLN H 376 1 O GLN H 376 N VAL H 42
SHEET 1 AC7 6 VAL H 244 LEU H 246 0
SHEET 2 AC7 6 ARG H 294 GLU H 298 -1 O ARG H 296 N SER H 245
SHEET 3 AC7 6 THR H 53 SER H 61 -1 N THR H 54 O LEU H 297
SHEET 4 AC7 6 PRO H 211 SER H 219 -1 O ASP H 215 N ARG H 59
SHEET 5 AC7 6 SER H 273 PRO H 281 -1 O LEU H 276 N VAL H 216
SHEET 6 AC7 6 LEU H 260 SER H 263 -1 N GLU H 261 O ARG H 277
SHEET 1 AC8 4 GLU H 67 VAL H 68 0
SHEET 2 AC8 4 ALA H 204 GLN H 207 -1 O ALA H 204 N VAL H 68
SHEET 3 AC8 4 GLY H 182 ILE H 184 -1 N ARG H 183 O GLN H 207
SHEET 4 AC8 4 ASP H 86 ILE H 87 -1 N ILE H 87 O GLY H 182
SHEET 1 AC9 3 TYR H 94 ILE H 96 0
SHEET 2 AC9 3 GLY H 74 ARG H 79 -1 N LYS H 78 O GLN H 95
SHEET 3 AC9 3 LEU H 194 VAL H 195 -1 O VAL H 195 N GLY H 74
SHEET 1 AD1 3 ILE H 306 PRO H 309 0
SHEET 2 AD1 3 LYS H 346 VAL H 349 -1 O TRP H 347 N VAL H 308
SHEET 3 AD1 3 ALA H 339 ILE H 343 -1 N SER H 340 O LEU H 348
SHEET 1 AD2 2 THR H 314 ARG H 315 0
SHEET 2 AD2 2 ALA H 321 THR H 322 -1 O THR H 322 N THR H 314
SHEET 1 AD3 4 VAL A 325 VAL A 326 0
SHEET 2 AD3 4 ARG A 358 SER A 362 -1 O ARG A 358 N VAL A 326
SHEET 3 AD3 4 ALA A 39 THR A 44 -1 N VAL A 43 O VAL A 359
SHEET 4 AD3 4 LYS A 374 GLN A 376 1 O GLN A 376 N VAL A 42
SHEET 1 AD4 6 VAL A 244 LEU A 246 0
SHEET 2 AD4 6 ARG A 294 GLU A 299 -1 O ARG A 296 N SER A 245
SHEET 3 AD4 6 ILE A 52 SER A 61 -1 N THR A 54 O LEU A 297
SHEET 4 AD4 6 PRO A 211 SER A 219 -1 O ASP A 215 N ARG A 59
SHEET 5 AD4 6 SER A 273 PRO A 281 -1 O PHE A 280 N ILE A 212
SHEET 6 AD4 6 THR A 259 SER A 263 -1 N GLU A 261 O ARG A 277
SHEET 1 AD5 4 GLU A 67 VAL A 68 0
SHEET 2 AD5 4 ALA A 204 GLN A 207 -1 O ALA A 204 N VAL A 68
SHEET 3 AD5 4 GLY A 182 ILE A 184 -1 N ARG A 183 O GLN A 207
SHEET 4 AD5 4 ASP A 86 ILE A 87 -1 N ILE A 87 O GLY A 182
SHEET 1 AD6 3 TYR A 94 ILE A 96 0
SHEET 2 AD6 3 GLY A 74 ARG A 79 -1 N LYS A 78 O GLN A 95
SHEET 3 AD6 3 LEU A 194 VAL A 195 -1 O VAL A 195 N GLY A 74
SHEET 1 AD7 2 THR A 314 ARG A 315 0
SHEET 2 AD7 2 ALA A 321 THR A 322 -1 O THR A 322 N THR A 314
SHEET 1 AD8 3 ARG B 358 VAL B 360 0
SHEET 2 AD8 3 ALA B 39 THR B 44 -1 N VAL B 43 O VAL B 359
SHEET 3 AD8 3 LYS B 374 GLN B 376 1 O GLN B 376 N VAL B 42
SHEET 1 AD9 5 GLU B 67 VAL B 68 0
SHEET 2 AD9 5 ALA B 204 SER B 219 -1 O ALA B 204 N VAL B 68
SHEET 3 AD9 5 ILE B 52 ARG B 64 -1 N ARG B 59 O ASP B 215
SHEET 4 AD9 5 ARG B 294 GLU B 299 -1 O GLU B 299 N ILE B 52
SHEET 5 AD9 5 LYS B 243 ILE B 247 -1 N SER B 245 O ARG B 296
SHEET 1 AE1 5 ASP B 86 ILE B 87 0
SHEET 2 AE1 5 GLY B 182 ILE B 184 -1 O GLY B 182 N ILE B 87
SHEET 3 AE1 5 ALA B 204 SER B 219 -1 O GLN B 207 N ARG B 183
SHEET 4 AE1 5 SER B 273 PRO B 281 -1 O PHE B 280 N ILE B 212
SHEET 5 AE1 5 THR B 259 SER B 263 -1 N THR B 259 O ILE B 279
SHEET 1 AE2 3 TYR B 94 ILE B 96 0
SHEET 2 AE2 3 GLY B 74 ARG B 79 -1 N LYS B 78 O GLN B 95
SHEET 3 AE2 3 LEU B 194 VAL B 195 -1 O VAL B 195 N GLY B 74
SHEET 1 AE3 2 THR B 314 ARG B 315 0
SHEET 2 AE3 2 ALA B 321 THR B 322 -1 O THR B 322 N THR B 314
SHEET 1 AE413 GLN F 41 GLY F 53 0
SHEET 2 AE413 ASN F 61 PHE F 76 -1 O SER F 66 N ASP F 47
SHEET 3 AE413 THR F 247 SER F 262 -1 O THR F 254 N LEU F 69
SHEET 4 AE413 SER F 277 TYR F 293 -1 O SER F 277 N THR F 259
SHEET 5 AE413 GLN C 41 GLY C 53 -1 O TYR C 50 N VAL F 284
SHEET 6 AE413 ASN C 61 PHE C 76 -1 O SER C 68 N GLY C 45
SHEET 7 AE413 THR C 247 SER C 262 -1 O THR C 254 N LEU C 69
SHEET 8 AE413 SER C 277 TYR C 293 -1 O SER C 277 N THR C 259
SHEET 9 AE413 GLN I 41 SER I 51 -1 N LEU I 44 O LEU C 290
SHEET 10 AE413 ASN I 61 PHE I 76 -1 O SER I 66 N ASP I 47
SHEET 11 AE413 THR I 247 SER I 262 -1 O THR I 254 N LEU I 69
SHEET 12 AE413 SER I 277 TYR I 293 -1 O SER I 277 N THR I 259
SHEET 13 AE413 GLN F 41 GLY F 53 -1 N LEU F 44 O LEU I 290
SHEET 1 AE5 2 GLU F 192 LEU F 196 0
SHEET 2 AE5 2 LEU F 419 SER F 424 -1 O VAL F 423 N LEU F 193
SHEET 1 AE6 2 GLU I 192 LEU I 196 0
SHEET 2 AE6 2 LEU I 419 SER I 424 -1 O VAL I 423 N LEU I 193
SHEET 1 AE7 2 GLU C 192 LEU C 196 0
SHEET 2 AE7 2 LEU C 419 SER C 424 -1 O VAL C 423 N LEU C 193
SHEET 1 AE8 4 LEU K 75 MET K 78 0
SHEET 2 AE8 4 THR K 87 PHE K 94 -1 O THR K 93 N MET K 76
SHEET 3 AE8 4 ALA K 42 SER K 48 -1 N ILE K 45 O ILE K 90
SHEET 4 AE8 4 VAL K 127 GLU K 130 -1 O GLU K 130 N THR K 44
SHEET 1 AE9 2 SER K 82 ASP K 83 0
SHEET 2 AE9 2 ARG K 815 LEU K 816 -1 O LEU K 816 N SER K 82
SHEET 1 AF1 4 VAL K 172 LEU K 177 0
SHEET 2 AF1 4 LEU K 289 LEU K 293 -1 O GLY K 290 N GLN K 176
SHEET 3 AF1 4 MET K 138 ASN K 144 -1 N MET K 138 O ILE K 291
SHEET 4 AF1 4 LEU K 321 TYR K 327 -1 O LYS K 322 N ILE K 143
SHEET 1 AF2 9 VAL K 172 LEU K 177 0
SHEET 2 AF2 9 LEU K 289 LEU K 293 -1 O GLY K 290 N GLN K 176
SHEET 3 AF2 9 MET K 138 ASN K 144 -1 N MET K 138 O ILE K 291
SHEET 4 AF2 9 GLN K 284 SER K 287 -1 O SER K 287 N VAL K 142
SHEET 5 AF2 9 ILE K 278 PHE K 281 -1 N ALA K 279 O ALA K 286
SHEET 6 AF2 9 VAL K 606 ASN K 613 -1 O ASN K 613 N ILE K 278
SHEET 7 AF2 9 THR K 624 LEU K 631 -1 O ILE K 626 N VAL K 612
SHEET 8 AF2 9 VAL K 571 GLN K 577 -1 N THR K 574 O ALA K 627
SHEET 9 AF2 9 PHE K 664 PHE K 666 -1 O PHE K 666 N MET K 573
SHEET 1 AF3 4 ALA K 266 LEU K 270 0
SHEET 2 AF3 4 MET K 184 MET K 188 -1 N TRP K 187 O LYS K 267
SHEET 3 AF3 4 ARG K 767 SER K 775 1 O MET K 774 N MET K 188
SHEET 4 AF3 4 TYR K 758 ASP K 764 -1 N PHE K 762 O LYS K 769
SHEET 1 AF4 3 ILE K 234 ILE K 235 0
SHEET 2 AF4 3 GLN L 726 ILE L 731 1 O ILE L 729 N ILE K 235
SHEET 3 AF4 3 SER L 805 GLU L 810 -1 O SER L 806 N ASP L 730
SHEET 1 AF5 2 LEU K 250 VAL K 253 0
SHEET 2 AF5 2 ARG K 259 LEU K 261 -1 O VAL K 260 N LEU K 251
SHEET 1 AF6 2 PHE K 680 PHE K 682 0
SHEET 2 AF6 2 ILE K 827 GLY K 829 -1 O ILE K 827 N PHE K 682
SHEET 1 AF7 2 ILE K 685 ASP K 686 0
SHEET 2 AF7 2 VAL K 855 GLY K 856 -1 O GLY K 856 N ILE K 685
SHEET 1 AF8 2 THR K 724 PHE K 727 0
SHEET 2 AF8 2 TRP K 809 GLY K 812 -1 O GLU K 810 N GLN K 726
SHEET 1 AF9 2 ASP K 730 ILE K 731 0
SHEET 2 AF9 2 SER K 805 SER K 806 -1 O SER K 806 N ASP K 730
SHEET 1 AG1 2 VAL K 791 ARG K 792 0
SHEET 2 AG1 2 MET K 798 VAL K 799 -1 O VAL K 799 N VAL K 791
SHEET 1 AG2 2 ARG K 818 TYR K 819 0
SHEET 2 AG2 2 LEU K 822 PRO K 823 -1 O LEU K 822 N TYR K 819
SHEET 1 AG3 4 LEU L 75 SER L 79 0
SHEET 2 AG3 4 ILE L 90 PHE L 94 -1 O THR L 91 N SER L 79
SHEET 3 AG3 4 THR L 44 ALA L 47 -1 N ILE L 45 O ILE L 90
SHEET 4 AG3 4 VAL L 127 GLU L 130 -1 O SER L 128 N SER L 46
SHEET 1 AG4 4 VAL L 172 LEU L 177 0
SHEET 2 AG4 4 ALA L 286 LEU L 293 -1 O LYS L 292 N GLY L 173
SHEET 3 AG4 4 PHE L 136 ASN L 144 -1 N LEU L 137 O ILE L 291
SHEET 4 AG4 4 LEU L 321 ASP L 328 -1 O LYS L 322 N ILE L 143
SHEET 1 AG5 4 GLU L 269 GLY L 271 0
SHEET 2 AG5 4 ALA L 183 ILE L 186 -1 N ALA L 183 O GLY L 271
SHEET 3 AG5 4 ARG L 767 VAL L 773 1 O LYS L 770 N MET L 184
SHEET 4 AG5 4 SER L 757 ASP L 764 -1 N PHE L 762 O LYS L 769
SHEET 1 AG6 3 SER L 233 ILE L 235 0
SHEET 2 AG6 3 GLN J 726 ASP J 730 1 O PHE J 727 N SER L 233
SHEET 3 AG6 3 SER J 806 SER J 807 -1 O SER J 806 N ASP J 730
SHEET 1 AG7 5 ILE L 278 PHE L 281 0
SHEET 2 AG7 5 SER L 608 ASN L 613 -1 O ASN L 613 N ILE L 278
SHEET 3 AG7 5 THR L 624 SER L 630 -1 O PHE L 628 N PHE L 610
SHEET 4 AG7 5 VAL L 571 GLN L 577 -1 N VAL L 576 O GLY L 625
SHEET 5 AG7 5 PHE L 664 PHE L 666 -1 O PHE L 664 N MET L 575
SHEET 1 AG8 4 GLU L 817 TYR L 819 0
SHEET 2 AG8 4 LEU L 822 ILE L 827 -1 O LEU L 822 N TYR L 819
SHEET 3 AG8 4 PHE L 682 ILE L 685 -1 N PHE L 682 O ILE L 827
SHEET 4 AG8 4 TYR L 857 TRP L 859 -1 O ASP L 858 N GLU L 683
SHEET 1 AG9 2 TYR L 790 ARG L 792 0
SHEET 2 AG9 2 MET L 798 PRO L 800 -1 O VAL L 799 N VAL L 791
SHEET 1 AH1 6 SER J 128 GLU J 130 0
SHEET 2 AH1 6 ALA J 42 SER J 46 -1 N THR J 44 O GLU J 130
SHEET 3 AH1 6 GLN J 89 PHE J 94 -1 O ILE J 90 N ILE J 45
SHEET 4 AH1 6 LEU J 75 SER J 82 -1 N SER J 79 O THR J 91
SHEET 5 AH1 6 LEU J 816 TYR J 819 -1 O ARG J 818 N SER J 80
SHEET 6 AH1 6 LEU J 822 PRO J 823 -1 O LEU J 822 N TYR J 819
SHEET 1 AH2 4 VAL J 172 PHE J 178 0
SHEET 2 AH2 4 GLN J 284 LEU J 293 -1 O LYS J 292 N ASP J 174
SHEET 3 AH2 4 GLY J 141 ASN J 144 -1 N VAL J 142 O SER J 287
SHEET 4 AH2 4 LEU J 321 VAL J 324 -1 O LYS J 322 N ILE J 143
SHEET 1 AH3 6 VAL J 172 PHE J 178 0
SHEET 2 AH3 6 GLN J 284 LEU J 293 -1 O LYS J 292 N ASP J 174
SHEET 3 AH3 6 ILE J 278 PHE J 281 -1 N PHE J 281 O GLN J 284
SHEET 4 AH3 6 SER J 608 ASN J 613 -1 O ASN J 613 N ILE J 278
SHEET 5 AH3 6 ILE J 626 SER J 630 -1 O PHE J 628 N PHE J 610
SHEET 6 AH3 6 VAL J 571 MET J 575 -1 N THR J 574 O ALA J 627
SHEET 1 AH4 4 ALA J 266 GLY J 272 0
SHEET 2 AH4 4 TYR J 182 MET J 188 -1 N TRP J 187 O LYS J 267
SHEET 3 AH4 4 ARG J 767 SER J 775 1 O TYR J 772 N ILE J 186
SHEET 4 AH4 4 SER J 757 ASP J 764 -1 N ASP J 764 O ARG J 767
SHEET 1 AH5 4 ARG J 717 PRO J 718 0
SHEET 2 AH5 4 ILE J 827 GLY J 829 -1 O LEU J 828 N ARG J 717
SHEET 3 AH5 4 PHE J 680 LEU J 684 -1 N PHE J 682 O ILE J 827
SHEET 4 AH5 4 TYR J 857 TRP J 859 -1 O ASP J 858 N GLU J 683
SHEET 1 AH6 2 TYR J 790 ARG J 792 0
SHEET 2 AH6 2 MET J 798 PRO J 800 -1 O VAL J 799 N VAL J 791
LINK CE1 PHE K 628 C33 5QF K1101 1555 1555 1.42
LINK CZ PHE K 628 C1 5QF K1101 1555 1555 1.26
LINK CZ PHE K 628 C2 5QF K1101 1555 1555 1.28
LINK CD2 PHE L 178 C11 5QF L1101 1555 1555 1.65
LINK CE2 PHE L 610 S9 5QF L1101 1555 1555 1.86
LINK CE2 PHE L 628 C1 5QF L1101 1555 1555 1.36
LINK CE2 PHE L 628 C6 5QF L1101 1555 1555 1.20
LINK CZ PHE L 628 C2 5QF L1101 1555 1555 1.61
CISPEP 1 TYR E 63 ARG E 64 0 3.30
CISPEP 2 VAL E 176 THR E 177 0 -16.94
CISPEP 3 GLY E 233 THR E 234 0 -5.94
CISPEP 4 THR E 234 LEU E 235 0 -6.20
CISPEP 5 GLN E 237 GLU E 238 0 3.93
CISPEP 6 THR E 316 PRO E 317 0 -3.12
CISPEP 7 TYR D 63 ARG D 64 0 -0.12
CISPEP 8 VAL D 176 THR D 177 0 -24.52
CISPEP 9 GLY D 233 THR D 234 0 -4.32
CISPEP 10 THR D 234 LEU D 235 0 -3.11
CISPEP 11 GLN D 237 GLU D 238 0 0.65
CISPEP 12 THR D 316 PRO D 317 0 -6.03
CISPEP 13 TYR G 63 ARG G 64 0 2.82
CISPEP 14 VAL G 176 THR G 177 0 -20.67
CISPEP 15 GLY G 233 THR G 234 0 -3.19
CISPEP 16 THR G 234 LEU G 235 0 -7.19
CISPEP 17 GLN G 237 GLU G 238 0 4.82
CISPEP 18 THR G 316 PRO G 317 0 -3.74
CISPEP 19 ASN H 232 GLY H 233 0 8.84
CISPEP 20 GLY H 233 THR H 234 0 -4.76
CISPEP 21 THR H 234 LEU H 235 0 -18.09
CISPEP 22 LYS H 241 ALA H 242 0 -6.99
CISPEP 23 MET H 291 PHE H 292 0 -0.29
CISPEP 24 THR H 316 PRO H 317 0 -4.84
CISPEP 25 ASN A 232 GLY A 233 0 9.67
CISPEP 26 GLY A 233 THR A 234 0 -4.36
CISPEP 27 THR A 234 LEU A 235 0 -17.75
CISPEP 28 LYS A 241 ALA A 242 0 -2.29
CISPEP 29 MET A 291 PHE A 292 0 -0.30
CISPEP 30 THR A 316 PRO A 317 0 4.90
CISPEP 31 ASN B 232 GLY B 233 0 6.96
CISPEP 32 GLY B 233 THR B 234 0 -7.53
CISPEP 33 THR B 234 LEU B 235 0 -17.94
CISPEP 34 LYS B 241 ALA B 242 0 -2.84
CISPEP 35 MET B 291 PHE B 292 0 -4.00
CISPEP 36 THR B 316 PRO B 317 0 -5.84
CISPEP 37 THR K 222 PRO K 223 0 5.51
CISPEP 38 GLY L 179 SER L 180 0 4.82
CISPEP 39 THR L 222 PRO L 223 0 1.96
CISPEP 40 PHE J 178 GLY J 179 0 -14.04
CISPEP 41 THR J 222 PRO J 223 0 3.31
SITE 1 AC1 20 PHE J 136 VAL J 139 GLN J 151 PHE J 178
SITE 2 AC1 20 GLY J 179 ILE J 277 ALA J 279 ALA J 286
SITE 3 AC1 20 SER J 287 GLY J 288 PRO J 326 TYR J 327
SITE 4 AC1 20 VAL J 571 MET J 573 PHE J 610 VAL J 612
SITE 5 AC1 20 PHE J 615 PHE J 617 PHE J 628 LEU J 668
SITE 1 AC2 16 PHE K 136 VAL K 139 GLN K 176 PHE K 178
SITE 2 AC2 16 GLY K 179 ILE K 277 ALA K 279 PRO K 326
SITE 3 AC2 16 MET K 573 VAL K 609 PHE K 610 VAL K 612
SITE 4 AC2 16 PHE K 615 ALA K 627 VAL K 629 LEU K 668
SITE 1 AC3 16 PHE K 136 VAL K 139 GLN K 176 PHE K 178
SITE 2 AC3 16 GLY K 179 ILE K 277 ALA K 279 PRO K 326
SITE 3 AC3 16 MET K 573 VAL K 609 PHE K 610 VAL K 612
SITE 4 AC3 16 PHE K 615 ALA K 627 VAL K 629 LEU K 668
SITE 1 AC4 16 PHE K 136 VAL K 139 GLN K 176 PHE K 178
SITE 2 AC4 16 GLY K 179 ILE K 277 ALA K 279 PRO K 326
SITE 3 AC4 16 MET K 573 VAL K 609 PHE K 610 VAL K 612
SITE 4 AC4 16 PHE K 615 ALA K 627 VAL K 629 LEU K 668
SITE 1 AC5 14 PHE L 136 VAL L 139 PHE L 178 GLY L 179
SITE 2 AC5 14 ILE L 277 PRO L 326 MET L 573 VAL L 609
SITE 3 AC5 14 PHE L 610 PHE L 615 ARG L 620 ALA L 627
SITE 4 AC5 14 VAL L 629 LEU L 668
SITE 1 AC6 16 PHE L 136 VAL L 139 PHE L 178 GLY L 179
SITE 2 AC6 16 ILE L 277 GLU L 280 PHE L 281 PRO L 326
SITE 3 AC6 16 MET L 573 VAL L 609 ALA L 611 PHE L 615
SITE 4 AC6 16 ARG L 620 ALA L 627 PHE L 628 LEU L 668
SITE 1 AC7 14 PHE L 136 VAL L 139 PHE L 178 GLY L 179
SITE 2 AC7 14 ILE L 277 PRO L 326 MET L 573 VAL L 609
SITE 3 AC7 14 PHE L 610 PHE L 615 ARG L 620 ALA L 627
SITE 4 AC7 14 VAL L 629 LEU L 668
SITE 1 AC8 14 PHE L 136 VAL L 139 PHE L 178 GLY L 179
SITE 2 AC8 14 ILE L 277 PRO L 326 MET L 573 VAL L 609
SITE 3 AC8 14 PHE L 610 PHE L 615 ARG L 620 ALA L 627
SITE 4 AC8 14 VAL L 629 LEU L 668
SITE 1 AC9 14 PHE L 136 VAL L 139 LEU L 177 GLY L 179
SITE 2 AC9 14 ILE L 277 GLY L 288 LEU L 289 PRO L 326
SITE 3 AC9 14 MET L 573 PHE L 610 PHE L 615 ARG L 620
SITE 4 AC9 14 PHE L 628 LEU L 668
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
