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HEADER OXIDOREDUCTASE, VIRAL PROTEIN 20-MAY-14 4QFF
TITLE STRUCTURE OF A 16 NM PROTEIN CAGE DESIGNED BY FUSING SYMMETRIC
TITLE 2 OLIGOMERIC DOMAINS, QUADRUPLE MUTANT, P212121 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-HAEM BROMOPEROXIDASE BPO-A2, MATRIX PROTEIN 1 CHIMERA;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 FRAGMENT: SEE REMARK 999;
COMPND 5 SYNONYM: DESIGNED 16NM TETRAHEDRAL PROTEIN CAGE, BPO2, BROMIDE
COMPND 6 PEROXIDASE, M1;
COMPND 7 EC: 1.11.1.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS, INFLUENZA A VIRUS;
SOURCE 3 ORGANISM_TAXID: 1894, 11320;
SOURCE 4 GENE: BPOA2, M;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PROTEIN DESIGN, BIONANOTECHNOLOGY, PROTEIN ASSEMBLY, SYMMETRY,
KEYWDS 2 BIOMATERIALS, OXIDOREDUCTASE, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-T.LAI,T.O.YEATES
REVDAT 1 20-MAY-15 4QFF 0
JRNL AUTH Y.-T.LAI,T.O.YEATES
JRNL TITL STRUCTURAL TRANSITION OF A PROTEIN NANOCAGE AS A FUNCTION OF
JRNL TITL 2 PH AND SALT CONCENTRATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 7.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 7.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 8723
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.290
REMARK 3 R VALUE (WORKING SET) : 0.288
REMARK 3 FREE R VALUE : 0.339
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 437
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 7.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 8.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 484
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 26
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 40512
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 127.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 241.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -13.46000
REMARK 3 B22 (A**2) : -9.11000
REMARK 3 B33 (A**2) : 22.57000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 6.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 4.205
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 560.278
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.704
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.602
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 41436 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 38664 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 56448 ; 1.437 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 88596 ; 1.421 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 5280 ; 4.143 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1860 ;34.023 ;23.742
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 6300 ;15.718 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 264 ;20.390 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 6420 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 47784 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 9744 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 21156 ; 5.873 ;24.360
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 21155 ; 5.873 ;24.360
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 26424 ;10.827 ;36.532
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 66
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 441 B 1 441 25960 0.090 0.050
REMARK 3 2 A 1 441 C 1 441 25974 0.090 0.050
REMARK 3 3 A 1 441 D 1 441 27329 0.050 0.050
REMARK 3 4 A 1 441 E 1 441 27435 0.020 0.050
REMARK 3 5 A 1 441 F 1 441 27414 0.020 0.050
REMARK 3 6 A 1 441 G 1 441 27339 0.030 0.050
REMARK 3 7 A 1 441 H 1 441 26024 0.090 0.050
REMARK 3 8 A 1 441 I 1 441 25959 0.090 0.050
REMARK 3 9 A 1 441 J 1 441 27387 0.020 0.050
REMARK 3 10 A 1 441 K 1 441 25710 0.110 0.050
REMARK 3 11 A 1 441 L 1 441 25937 0.090 0.050
REMARK 3 12 B 1 441 C 1 441 27274 0.030 0.050
REMARK 3 13 B 1 441 D 1 441 25838 0.100 0.050
REMARK 3 14 B 1 441 E 1 441 25943 0.090 0.050
REMARK 3 15 B 1 441 F 1 441 25936 0.090 0.050
REMARK 3 16 B 1 441 G 1 441 25914 0.090 0.050
REMARK 3 17 B 1 441 H 1 441 27306 0.040 0.050
REMARK 3 18 B 1 441 I 1 441 27332 0.030 0.050
REMARK 3 19 B 1 441 J 1 441 25906 0.090 0.050
REMARK 3 20 B 1 441 K 1 441 27051 0.060 0.050
REMARK 3 21 B 1 441 L 1 441 27196 0.040 0.050
REMARK 3 22 C 1 441 D 1 441 25896 0.090 0.050
REMARK 3 23 C 1 441 E 1 441 25983 0.090 0.050
REMARK 3 24 C 1 441 F 1 441 25958 0.090 0.050
REMARK 3 25 C 1 441 G 1 441 25852 0.090 0.050
REMARK 3 26 C 1 441 H 1 441 27346 0.020 0.050
REMARK 3 27 C 1 441 I 1 441 27286 0.030 0.050
REMARK 3 28 C 1 441 J 1 441 25937 0.090 0.050
REMARK 3 29 C 1 441 K 1 441 27056 0.060 0.050
REMARK 3 30 C 1 441 L 1 441 27259 0.030 0.050
REMARK 3 31 D 1 441 E 1 441 27332 0.040 0.050
REMARK 3 32 D 1 441 F 1 441 27294 0.040 0.050
REMARK 3 33 D 1 441 G 1 441 27207 0.050 0.050
REMARK 3 34 D 1 441 H 1 441 25915 0.090 0.050
REMARK 3 35 D 1 441 I 1 441 25847 0.100 0.050
REMARK 3 36 D 1 441 J 1 441 27294 0.040 0.050
REMARK 3 37 D 1 441 K 1 441 25624 0.110 0.050
REMARK 3 38 D 1 441 L 1 441 25861 0.100 0.050
REMARK 3 39 E 1 441 F 1 441 27416 0.020 0.050
REMARK 3 40 E 1 441 G 1 441 27316 0.030 0.050
REMARK 3 41 E 1 441 H 1 441 26009 0.090 0.050
REMARK 3 42 E 1 441 I 1 441 25942 0.090 0.050
REMARK 3 43 E 1 441 J 1 441 27386 0.020 0.050
REMARK 3 44 E 1 441 K 1 441 25696 0.110 0.050
REMARK 3 45 E 1 441 L 1 441 25938 0.090 0.050
REMARK 3 46 F 1 441 G 1 441 27323 0.030 0.050
REMARK 3 47 F 1 441 H 1 441 25986 0.090 0.050
REMARK 3 48 F 1 441 I 1 441 25943 0.090 0.050
REMARK 3 49 F 1 441 J 1 441 27346 0.030 0.050
REMARK 3 50 F 1 441 K 1 441 25718 0.110 0.050
REMARK 3 51 F 1 441 L 1 441 25924 0.090 0.050
REMARK 3 52 G 1 441 H 1 441 25890 0.090 0.050
REMARK 3 53 G 1 441 I 1 441 25916 0.090 0.050
REMARK 3 54 G 1 441 J 1 441 27276 0.030 0.050
REMARK 3 55 G 1 441 K 1 441 25654 0.110 0.050
REMARK 3 56 G 1 441 L 1 441 25820 0.100 0.050
REMARK 3 57 H 1 441 I 1 441 27330 0.030 0.050
REMARK 3 58 H 1 441 J 1 441 25956 0.090 0.050
REMARK 3 59 H 1 441 K 1 441 27078 0.060 0.050
REMARK 3 60 H 1 441 L 1 441 27269 0.040 0.050
REMARK 3 61 I 1 441 J 1 441 25920 0.090 0.050
REMARK 3 62 I 1 441 K 1 441 27050 0.060 0.050
REMARK 3 63 I 1 441 L 1 441 27205 0.040 0.050
REMARK 3 64 J 1 441 K 1 441 25670 0.110 0.050
REMARK 3 65 J 1 441 L 1 441 25888 0.090 0.050
REMARK 3 66 K 1 441 L 1 441 26980 0.060 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4QFF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-14.
REMARK 100 THE RCSB ID CODE IS RCSB085986.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : VARIMAX HR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8723
REMARK 200 RESOLUTION RANGE HIGH (A) : 7.810
REMARK 200 RESOLUTION RANGE LOW (A) : 91.273
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.14200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 7.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 8.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.59700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.350
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM/POTASSIUM PHOSPHATE, PH
REMARK 280 5.8, 10% PEG8000, 0.2 M SODIUM CHLORIDE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 77.75000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 162.51500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.26000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 162.51500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 77.75000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 78.26000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 32320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 190580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, C, E, F, L, G, K, I,
REMARK 350 AND CHAINS: D, B, 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 MET A 0
REMARK 465 HIS A 442
REMARK 465 ARG A 443
REMARK 465 SER A 444
REMARK 465 HIS A 445
REMARK 465 ARG A 446
REMARK 465 GLN A 447
REMARK 465 LEU A 448
REMARK 465 GLU A 449
REMARK 465 HIS A 450
REMARK 465 HIS A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 MET B 0
REMARK 465 HIS B 442
REMARK 465 ARG B 443
REMARK 465 SER B 444
REMARK 465 HIS B 445
REMARK 465 ARG B 446
REMARK 465 GLN B 447
REMARK 465 LEU B 448
REMARK 465 GLU B 449
REMARK 465 HIS B 450
REMARK 465 HIS B 451
REMARK 465 HIS B 452
REMARK 465 HIS B 453
REMARK 465 HIS B 454
REMARK 465 HIS B 455
REMARK 465 MET C 0
REMARK 465 HIS C 442
REMARK 465 ARG C 443
REMARK 465 SER C 444
REMARK 465 HIS C 445
REMARK 465 ARG C 446
REMARK 465 GLN C 447
REMARK 465 LEU C 448
REMARK 465 GLU C 449
REMARK 465 HIS C 450
REMARK 465 HIS C 451
REMARK 465 HIS C 452
REMARK 465 HIS C 453
REMARK 465 HIS C 454
REMARK 465 HIS C 455
REMARK 465 MET D 0
REMARK 465 HIS D 442
REMARK 465 ARG D 443
REMARK 465 SER D 444
REMARK 465 HIS D 445
REMARK 465 ARG D 446
REMARK 465 GLN D 447
REMARK 465 LEU D 448
REMARK 465 GLU D 449
REMARK 465 HIS D 450
REMARK 465 HIS D 451
REMARK 465 HIS D 452
REMARK 465 HIS D 453
REMARK 465 HIS D 454
REMARK 465 HIS D 455
REMARK 465 MET E 0
REMARK 465 HIS E 442
REMARK 465 ARG E 443
REMARK 465 SER E 444
REMARK 465 HIS E 445
REMARK 465 ARG E 446
REMARK 465 GLN E 447
REMARK 465 LEU E 448
REMARK 465 GLU E 449
REMARK 465 HIS E 450
REMARK 465 HIS E 451
REMARK 465 HIS E 452
REMARK 465 HIS E 453
REMARK 465 HIS E 454
REMARK 465 HIS E 455
REMARK 465 MET F 0
REMARK 465 HIS F 442
REMARK 465 ARG F 443
REMARK 465 SER F 444
REMARK 465 HIS F 445
REMARK 465 ARG F 446
REMARK 465 GLN F 447
REMARK 465 LEU F 448
REMARK 465 GLU F 449
REMARK 465 HIS F 450
REMARK 465 HIS F 451
REMARK 465 HIS F 452
REMARK 465 HIS F 453
REMARK 465 HIS F 454
REMARK 465 HIS F 455
REMARK 465 MET G 0
REMARK 465 HIS G 442
REMARK 465 ARG G 443
REMARK 465 SER G 444
REMARK 465 HIS G 445
REMARK 465 ARG G 446
REMARK 465 GLN G 447
REMARK 465 LEU G 448
REMARK 465 GLU G 449
REMARK 465 HIS G 450
REMARK 465 HIS G 451
REMARK 465 HIS G 452
REMARK 465 HIS G 453
REMARK 465 HIS G 454
REMARK 465 HIS G 455
REMARK 465 MET H 0
REMARK 465 HIS H 442
REMARK 465 ARG H 443
REMARK 465 SER H 444
REMARK 465 HIS H 445
REMARK 465 ARG H 446
REMARK 465 GLN H 447
REMARK 465 LEU H 448
REMARK 465 GLU H 449
REMARK 465 HIS H 450
REMARK 465 HIS H 451
REMARK 465 HIS H 452
REMARK 465 HIS H 453
REMARK 465 HIS H 454
REMARK 465 HIS H 455
REMARK 465 MET I 0
REMARK 465 HIS I 442
REMARK 465 ARG I 443
REMARK 465 SER I 444
REMARK 465 HIS I 445
REMARK 465 ARG I 446
REMARK 465 GLN I 447
REMARK 465 LEU I 448
REMARK 465 GLU I 449
REMARK 465 HIS I 450
REMARK 465 HIS I 451
REMARK 465 HIS I 452
REMARK 465 HIS I 453
REMARK 465 HIS I 454
REMARK 465 HIS I 455
REMARK 465 MET J 0
REMARK 465 HIS J 442
REMARK 465 ARG J 443
REMARK 465 SER J 444
REMARK 465 HIS J 445
REMARK 465 ARG J 446
REMARK 465 GLN J 447
REMARK 465 LEU J 448
REMARK 465 GLU J 449
REMARK 465 HIS J 450
REMARK 465 HIS J 451
REMARK 465 HIS J 452
REMARK 465 HIS J 453
REMARK 465 HIS J 454
REMARK 465 HIS J 455
REMARK 465 MET K 0
REMARK 465 HIS K 442
REMARK 465 ARG K 443
REMARK 465 SER K 444
REMARK 465 HIS K 445
REMARK 465 ARG K 446
REMARK 465 GLN K 447
REMARK 465 LEU K 448
REMARK 465 GLU K 449
REMARK 465 HIS K 450
REMARK 465 HIS K 451
REMARK 465 HIS K 452
REMARK 465 HIS K 453
REMARK 465 HIS K 454
REMARK 465 HIS K 455
REMARK 465 MET L 0
REMARK 465 HIS L 442
REMARK 465 ARG L 443
REMARK 465 SER L 444
REMARK 465 HIS L 445
REMARK 465 ARG L 446
REMARK 465 GLN L 447
REMARK 465 LEU L 448
REMARK 465 GLU L 449
REMARK 465 HIS L 450
REMARK 465 HIS L 451
REMARK 465 HIS L 452
REMARK 465 HIS L 453
REMARK 465 HIS L 454
REMARK 465 HIS L 455
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 GLN A 279 CG CD OE1 NE2
REMARK 470 GLU A 280 CG CD OE1 OE2
REMARK 470 GLN A 282 CG CD OE1 NE2
REMARK 470 LYS A 283 CG CD CE NZ
REMARK 470 GLN A 284 CG CD OE1 NE2
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 GLN B 279 CG CD OE1 NE2
REMARK 470 GLU B 280 CG CD OE1 OE2
REMARK 470 GLN B 282 CG CD OE1 NE2
REMARK 470 LYS B 283 CG CD CE NZ
REMARK 470 GLN B 284 CG CD OE1 NE2
REMARK 470 LYS B 285 CG CD CE NZ
REMARK 470 GLN C 279 CG CD OE1 NE2
REMARK 470 GLU C 280 CG CD OE1 OE2
REMARK 470 GLN C 282 CG CD OE1 NE2
REMARK 470 LYS C 283 CG CD CE NZ
REMARK 470 GLN C 284 CG CD OE1 NE2
REMARK 470 LYS C 285 CG CD CE NZ
REMARK 470 GLN D 279 CG CD OE1 NE2
REMARK 470 GLU D 280 CG CD OE1 OE2
REMARK 470 GLN D 282 CG CD OE1 NE2
REMARK 470 LYS D 283 CG CD CE NZ
REMARK 470 GLN D 284 CG CD OE1 NE2
REMARK 470 LYS D 285 CG CD CE NZ
REMARK 470 GLN E 279 CG CD OE1 NE2
REMARK 470 GLU E 280 CG CD OE1 OE2
REMARK 470 GLN E 282 CG CD OE1 NE2
REMARK 470 LYS E 283 CG CD CE NZ
REMARK 470 GLN E 284 CG CD OE1 NE2
REMARK 470 LYS E 285 CG CD CE NZ
REMARK 470 GLN F 279 CG CD OE1 NE2
REMARK 470 GLU F 280 CG CD OE1 OE2
REMARK 470 GLN F 282 CG CD OE1 NE2
REMARK 470 LYS F 283 CG CD CE NZ
REMARK 470 GLN F 284 CG CD OE1 NE2
REMARK 470 LYS F 285 CG CD CE NZ
REMARK 470 GLN G 279 CG CD OE1 NE2
REMARK 470 GLU G 280 CG CD OE1 OE2
REMARK 470 GLN G 282 CG CD OE1 NE2
REMARK 470 LYS G 283 CG CD CE NZ
REMARK 470 GLN G 284 CG CD OE1 NE2
REMARK 470 LYS G 285 CG CD CE NZ
REMARK 470 GLN H 279 CG CD OE1 NE2
REMARK 470 GLU H 280 CG CD OE1 OE2
REMARK 470 GLN H 282 CG CD OE1 NE2
REMARK 470 LYS H 283 CG CD CE NZ
REMARK 470 GLN H 284 CG CD OE1 NE2
REMARK 470 LYS H 285 CG CD CE NZ
REMARK 470 GLN I 279 CG CD OE1 NE2
REMARK 470 GLU I 280 CG CD OE1 OE2
REMARK 470 GLN I 282 CG CD OE1 NE2
REMARK 470 LYS I 283 CG CD CE NZ
REMARK 470 GLN I 284 CG CD OE1 NE2
REMARK 470 LYS I 285 CG CD CE NZ
REMARK 470 GLN J 279 CG CD OE1 NE2
REMARK 470 GLU J 280 CG CD OE1 OE2
REMARK 470 GLN J 282 CG CD OE1 NE2
REMARK 470 LYS J 283 CG CD CE NZ
REMARK 470 GLN J 284 CG CD OE1 NE2
REMARK 470 LYS J 285 CG CD CE NZ
REMARK 470 GLN K 279 CG CD OE1 NE2
REMARK 470 GLU K 280 CG CD OE1 OE2
REMARK 470 GLN K 282 CG CD OE1 NE2
REMARK 470 LYS K 283 CG CD CE NZ
REMARK 470 GLN K 284 CG CD OE1 NE2
REMARK 470 LYS K 285 CG CD CE NZ
REMARK 470 GLN L 279 CG CD OE1 NE2
REMARK 470 GLU L 280 CG CD OE1 OE2
REMARK 470 GLN L 282 CG CD OE1 NE2
REMARK 470 LYS L 283 CG CD CE NZ
REMARK 470 GLN L 284 CG CD OE1 NE2
REMARK 470 LYS L 285 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 9 -122.51 50.97
REMARK 500 SER A 98 -118.31 55.05
REMARK 500 PHE A 128 103.80 -174.61
REMARK 500 ASP A 155 93.11 -172.26
REMARK 500 THR A 176 -83.86 -129.00
REMARK 500 TYR A 206 33.32 -97.90
REMARK 500 THR A 236 -102.85 -125.13
REMARK 500 TRP A 261 -60.17 -92.44
REMARK 500 ASP A 321 97.71 -67.27
REMARK 500 ILE A 334 -38.00 64.20
REMARK 500 ASN B 9 -122.41 50.92
REMARK 500 SER B 98 -118.39 54.99
REMARK 500 PHE B 128 103.82 -174.61
REMARK 500 ASP B 155 93.07 -172.19
REMARK 500 THR B 176 -83.84 -128.88
REMARK 500 TYR B 206 33.44 -97.84
REMARK 500 THR B 236 -102.91 -125.16
REMARK 500 TRP B 261 -60.30 -92.41
REMARK 500 THR B 320 -15.95 -155.62
REMARK 500 ILE B 334 -37.97 64.18
REMARK 500 ARG B 355 -126.62 67.12
REMARK 500 ASN B 370 -4.65 79.98
REMARK 500 ASN C 9 -122.51 50.93
REMARK 500 SER C 98 -118.47 55.02
REMARK 500 PHE C 128 103.70 -174.54
REMARK 500 ASP C 155 93.17 -172.07
REMARK 500 THR C 176 -83.98 -128.75
REMARK 500 TYR C 206 33.46 -97.85
REMARK 500 THR C 236 -102.91 -125.08
REMARK 500 TRP C 261 -60.27 -92.41
REMARK 500 THR C 320 -16.00 -155.74
REMARK 500 ILE C 334 -38.48 64.40
REMARK 500 ARG C 355 -126.55 67.14
REMARK 500 ASN C 370 -4.62 79.93
REMARK 500 ASN D 9 -122.28 50.93
REMARK 500 SER D 98 -118.37 55.02
REMARK 500 PHE D 128 103.90 -174.52
REMARK 500 ASP D 155 93.14 -172.28
REMARK 500 THR D 176 -83.88 -128.89
REMARK 500 TYR D 206 33.48 -97.91
REMARK 500 THR D 236 -102.89 -125.14
REMARK 500 TRP D 261 -60.23 -92.42
REMARK 500 ASP D 321 97.74 -67.25
REMARK 500 ILE D 334 -38.00 64.22
REMARK 500 ASN E 9 -122.46 50.93
REMARK 500 SER E 98 -118.41 55.06
REMARK 500 PHE E 128 103.80 -174.57
REMARK 500 ASP E 155 93.10 -172.14
REMARK 500 THR E 176 -83.98 -128.74
REMARK 500 TYR E 206 33.46 -97.73
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QES RELATED DB: PDB
REMARK 900 RELATED ID: 4QF0 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE DESIGNED PROTEIN CONSTRUCT IS A CHIMERA COMPRISING BPO2 (UNP
REMARK 999 P29715) AND RESIDUES 2-164 (UNP P03485) OF M1, SEPARATED BY A
REMARK 999 LINKER.
DBREF 4QFF A 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF A 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF B 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF B 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF C 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF C 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF D 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF D 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF E 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF E 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF F 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF F 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF G 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF G 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF H 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF H 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF I 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF I 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF J 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF J 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF K 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF K 286 447 UNP P03485 M1_I34A1 3 164
DBREF 4QFF L 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4QFF L 286 447 UNP P03485 M1_I34A1 3 164
SEQADV 4QFF THR A 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA A 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA A 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA A 278 UNP P03485 LINKER
SEQADV 4QFF GLN A 279 UNP P03485 LINKER
SEQADV 4QFF GLU A 280 UNP P03485 LINKER
SEQADV 4QFF ALA A 281 UNP P03485 LINKER
SEQADV 4QFF GLN A 282 UNP P03485 LINKER
SEQADV 4QFF LYS A 283 UNP P03485 LINKER
SEQADV 4QFF GLN A 284 UNP P03485 LINKER
SEQADV 4QFF LYS A 285 UNP P03485 LINKER
SEQADV 4QFF LEU A 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU A 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS A 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS A 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS A 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS A 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS A 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS A 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR B 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA B 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA B 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA B 278 UNP P03485 LINKER
SEQADV 4QFF GLN B 279 UNP P03485 LINKER
SEQADV 4QFF GLU B 280 UNP P03485 LINKER
SEQADV 4QFF ALA B 281 UNP P03485 LINKER
SEQADV 4QFF GLN B 282 UNP P03485 LINKER
SEQADV 4QFF LYS B 283 UNP P03485 LINKER
SEQADV 4QFF GLN B 284 UNP P03485 LINKER
SEQADV 4QFF LYS B 285 UNP P03485 LINKER
SEQADV 4QFF LEU B 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU B 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS B 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS B 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS B 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS B 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS B 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS B 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR C 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA C 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA C 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA C 278 UNP P03485 LINKER
SEQADV 4QFF GLN C 279 UNP P03485 LINKER
SEQADV 4QFF GLU C 280 UNP P03485 LINKER
SEQADV 4QFF ALA C 281 UNP P03485 LINKER
SEQADV 4QFF GLN C 282 UNP P03485 LINKER
SEQADV 4QFF LYS C 283 UNP P03485 LINKER
SEQADV 4QFF GLN C 284 UNP P03485 LINKER
SEQADV 4QFF LYS C 285 UNP P03485 LINKER
SEQADV 4QFF LEU C 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU C 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS C 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS C 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS C 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS C 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS C 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS C 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR D 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA D 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA D 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA D 278 UNP P03485 LINKER
SEQADV 4QFF GLN D 279 UNP P03485 LINKER
SEQADV 4QFF GLU D 280 UNP P03485 LINKER
SEQADV 4QFF ALA D 281 UNP P03485 LINKER
SEQADV 4QFF GLN D 282 UNP P03485 LINKER
SEQADV 4QFF LYS D 283 UNP P03485 LINKER
SEQADV 4QFF GLN D 284 UNP P03485 LINKER
SEQADV 4QFF LYS D 285 UNP P03485 LINKER
SEQADV 4QFF LEU D 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU D 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS D 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS D 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS D 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS D 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS D 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS D 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR E 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA E 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA E 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA E 278 UNP P03485 LINKER
SEQADV 4QFF GLN E 279 UNP P03485 LINKER
SEQADV 4QFF GLU E 280 UNP P03485 LINKER
SEQADV 4QFF ALA E 281 UNP P03485 LINKER
SEQADV 4QFF GLN E 282 UNP P03485 LINKER
SEQADV 4QFF LYS E 283 UNP P03485 LINKER
SEQADV 4QFF GLN E 284 UNP P03485 LINKER
SEQADV 4QFF LYS E 285 UNP P03485 LINKER
SEQADV 4QFF LEU E 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU E 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS E 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS E 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS E 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS E 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS E 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS E 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR F 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA F 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA F 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA F 278 UNP P03485 LINKER
SEQADV 4QFF GLN F 279 UNP P03485 LINKER
SEQADV 4QFF GLU F 280 UNP P03485 LINKER
SEQADV 4QFF ALA F 281 UNP P03485 LINKER
SEQADV 4QFF GLN F 282 UNP P03485 LINKER
SEQADV 4QFF LYS F 283 UNP P03485 LINKER
SEQADV 4QFF GLN F 284 UNP P03485 LINKER
SEQADV 4QFF LYS F 285 UNP P03485 LINKER
SEQADV 4QFF LEU F 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU F 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS F 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS F 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS F 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS F 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS F 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS F 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR G 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA G 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA G 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA G 278 UNP P03485 LINKER
SEQADV 4QFF GLN G 279 UNP P03485 LINKER
SEQADV 4QFF GLU G 280 UNP P03485 LINKER
SEQADV 4QFF ALA G 281 UNP P03485 LINKER
SEQADV 4QFF GLN G 282 UNP P03485 LINKER
SEQADV 4QFF LYS G 283 UNP P03485 LINKER
SEQADV 4QFF GLN G 284 UNP P03485 LINKER
SEQADV 4QFF LYS G 285 UNP P03485 LINKER
SEQADV 4QFF LEU G 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU G 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS G 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS G 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS G 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS G 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS G 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS G 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR H 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA H 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA H 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA H 278 UNP P03485 LINKER
SEQADV 4QFF GLN H 279 UNP P03485 LINKER
SEQADV 4QFF GLU H 280 UNP P03485 LINKER
SEQADV 4QFF ALA H 281 UNP P03485 LINKER
SEQADV 4QFF GLN H 282 UNP P03485 LINKER
SEQADV 4QFF LYS H 283 UNP P03485 LINKER
SEQADV 4QFF GLN H 284 UNP P03485 LINKER
SEQADV 4QFF LYS H 285 UNP P03485 LINKER
SEQADV 4QFF LEU H 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU H 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS H 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS H 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS H 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS H 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS H 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS H 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR I 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA I 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA I 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA I 278 UNP P03485 LINKER
SEQADV 4QFF GLN I 279 UNP P03485 LINKER
SEQADV 4QFF GLU I 280 UNP P03485 LINKER
SEQADV 4QFF ALA I 281 UNP P03485 LINKER
SEQADV 4QFF GLN I 282 UNP P03485 LINKER
SEQADV 4QFF LYS I 283 UNP P03485 LINKER
SEQADV 4QFF GLN I 284 UNP P03485 LINKER
SEQADV 4QFF LYS I 285 UNP P03485 LINKER
SEQADV 4QFF LEU I 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU I 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS I 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS I 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS I 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS I 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS I 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS I 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR J 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA J 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA J 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA J 278 UNP P03485 LINKER
SEQADV 4QFF GLN J 279 UNP P03485 LINKER
SEQADV 4QFF GLU J 280 UNP P03485 LINKER
SEQADV 4QFF ALA J 281 UNP P03485 LINKER
SEQADV 4QFF GLN J 282 UNP P03485 LINKER
SEQADV 4QFF LYS J 283 UNP P03485 LINKER
SEQADV 4QFF GLN J 284 UNP P03485 LINKER
SEQADV 4QFF LYS J 285 UNP P03485 LINKER
SEQADV 4QFF LEU J 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU J 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS J 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS J 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS J 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS J 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS J 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS J 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR K 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA K 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA K 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA K 278 UNP P03485 LINKER
SEQADV 4QFF GLN K 279 UNP P03485 LINKER
SEQADV 4QFF GLU K 280 UNP P03485 LINKER
SEQADV 4QFF ALA K 281 UNP P03485 LINKER
SEQADV 4QFF GLN K 282 UNP P03485 LINKER
SEQADV 4QFF LYS K 283 UNP P03485 LINKER
SEQADV 4QFF GLN K 284 UNP P03485 LINKER
SEQADV 4QFF LYS K 285 UNP P03485 LINKER
SEQADV 4QFF LEU K 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU K 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS K 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS K 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS K 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS K 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS K 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS K 455 UNP P03485 EXPRESSION TAG
SEQADV 4QFF THR L 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4QFF ALA L 51 UNP P29715 TYR 52 ENGINEERED MUTATION
SEQADV 4QFF ALA L 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4QFF ALA L 278 UNP P03485 LINKER
SEQADV 4QFF GLN L 279 UNP P03485 LINKER
SEQADV 4QFF GLU L 280 UNP P03485 LINKER
SEQADV 4QFF ALA L 281 UNP P03485 LINKER
SEQADV 4QFF GLN L 282 UNP P03485 LINKER
SEQADV 4QFF LYS L 283 UNP P03485 LINKER
SEQADV 4QFF GLN L 284 UNP P03485 LINKER
SEQADV 4QFF LYS L 285 UNP P03485 LINKER
SEQADV 4QFF LEU L 448 UNP P03485 EXPRESSION TAG
SEQADV 4QFF GLU L 449 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS L 450 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS L 451 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS L 452 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS L 453 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS L 454 UNP P03485 EXPRESSION TAG
SEQADV 4QFF HIS L 455 UNP P03485 EXPRESSION TAG
SEQRES 1 A 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 A 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 A 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 A 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 A 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 A 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 A 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 A 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 A 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 A 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 A 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 A 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 A 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 A 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 A 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 A 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 A 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 A 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 A 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 A 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 A 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 A 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 A 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 A 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 A 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 A 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 A 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 A 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 A 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 A 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 A 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 A 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 A 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 A 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 A 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 A 456 HIS
SEQRES 1 B 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 B 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 B 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 B 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 B 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 B 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 B 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 B 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 B 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 B 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 B 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 B 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 B 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 B 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 B 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 B 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 B 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 B 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 B 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 B 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 B 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 B 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 B 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 B 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 B 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 B 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 B 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 B 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 B 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 B 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 B 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 B 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 B 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 B 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 B 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 B 456 HIS
SEQRES 1 C 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 C 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 C 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 C 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 C 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 C 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 C 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 C 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 C 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 C 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 C 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 C 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 C 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 C 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 C 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 C 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 C 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 C 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 C 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 C 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 C 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 C 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 C 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 C 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 C 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 C 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 C 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 C 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 C 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 C 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 C 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 C 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 C 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 C 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 C 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 C 456 HIS
SEQRES 1 D 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 D 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 D 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 D 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 D 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 D 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 D 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 D 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 D 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 D 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 D 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 D 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 D 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 D 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 D 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 D 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 D 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 D 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 D 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 D 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 D 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 D 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 D 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 D 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 D 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 D 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 D 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 D 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 D 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 D 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 D 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 D 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 D 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 D 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 D 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 D 456 HIS
SEQRES 1 E 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 E 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 E 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 E 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 E 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 E 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 E 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 E 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 E 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 E 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 E 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 E 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 E 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 E 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 E 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 E 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 E 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 E 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 E 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 E 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 E 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 E 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 E 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 E 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 E 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 E 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 E 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 E 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 E 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 E 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 E 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 E 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 E 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 E 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 E 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 E 456 HIS
SEQRES 1 F 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 F 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 F 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 F 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 F 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 F 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 F 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 F 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 F 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 F 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 F 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 F 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 F 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 F 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 F 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 F 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 F 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 F 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 F 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 F 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 F 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 F 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 F 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 F 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 F 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 F 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 F 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 F 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 F 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 F 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 F 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 F 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 F 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 F 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 F 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 F 456 HIS
SEQRES 1 G 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 G 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 G 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 G 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 G 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 G 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 G 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 G 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 G 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 G 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 G 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 G 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 G 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 G 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 G 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 G 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 G 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 G 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 G 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 G 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 G 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 G 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 G 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 G 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 G 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 G 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 G 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 G 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 G 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 G 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 G 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 G 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 G 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 G 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 G 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 G 456 HIS
SEQRES 1 H 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 H 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 H 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 H 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 H 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 H 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 H 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 H 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 H 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 H 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 H 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 H 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 H 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 H 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 H 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 H 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 H 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 H 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 H 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 H 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 H 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 H 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 H 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 H 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 H 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 H 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 H 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 H 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 H 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 H 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 H 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 H 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 H 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 H 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 H 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 H 456 HIS
SEQRES 1 I 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 I 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 I 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 I 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 I 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 I 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 I 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 I 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 I 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 I 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 I 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 I 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 I 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 I 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 I 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 I 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 I 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 I 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 I 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 I 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 I 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 I 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 I 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 I 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 I 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 I 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 I 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 I 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 I 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 I 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 I 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 I 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 I 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 I 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 I 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 I 456 HIS
SEQRES 1 J 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 J 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 J 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 J 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 J 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 J 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 J 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 J 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 J 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 J 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 J 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 J 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 J 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 J 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 J 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 J 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 J 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 J 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 J 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 J 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 J 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 J 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 J 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 J 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 J 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 J 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 J 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 J 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 J 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 J 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 J 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 J 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 J 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 J 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 J 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 J 456 HIS
SEQRES 1 K 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 K 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 K 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 K 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 K 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 K 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 K 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 K 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 K 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 K 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 K 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 K 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 K 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 K 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 K 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 K 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 K 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 K 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 K 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 K 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 K 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 K 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 K 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 K 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 K 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 K 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 K 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 K 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 K 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 K 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 K 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 K 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 K 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 K 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 K 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 K 456 HIS
SEQRES 1 L 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 L 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 L 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 L 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY ALA
SEQRES 5 L 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 L 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 L 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 L 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 L 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 L 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 L 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 L 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 L 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 L 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 L 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 L 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 L 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 L 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 L 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 L 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 L 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 L 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 L 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 L 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 L 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 L 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 L 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 L 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 L 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 L 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 L 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 L 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 L 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 L 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 L 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 L 456 HIS
HELIX 1 1 SER A 35 SER A 38 5 4
HELIX 2 2 TRP A 39 GLY A 50 1 12
HELIX 3 3 ASP A 72 ASP A 88 1 17
HELIX 4 4 MET A 99 GLY A 112 1 14
HELIX 5 5 PRO A 141 ASP A 155 1 15
HELIX 6 6 ASP A 155 ASN A 169 1 15
HELIX 7 7 ASN A 169 LEU A 174 1 6
HELIX 8 8 SER A 179 SER A 192 1 14
HELIX 9 9 GLY A 194 TRP A 205 1 12
HELIX 10 10 ASP A 212 ILE A 216 5 5
HELIX 11 11 THR A 236 LEU A 244 1 9
HELIX 12 12 GLY A 258 HIS A 263 1 6
HELIX 13 13 HIS A 263 SER A 296 1 34
HELIX 14 14 GLY A 301 ALA A 316 1 16
HELIX 15 15 ASP A 321 THR A 331 1 11
HELIX 16 16 SER A 336 VAL A 351 1 16
HELIX 17 17 ARG A 360 LEU A 367 1 8
HELIX 18 18 ASN A 368 GLY A 371 5 4
HELIX 19 19 ASP A 372 LYS A 387 1 16
HELIX 20 20 THR A 391 LEU A 400 1 10
HELIX 21 21 SER A 403 ASN A 416 1 14
HELIX 22 22 THR A 422 GLN A 441 1 20
HELIX 23 23 SER B 35 SER B 38 5 4
HELIX 24 24 TRP B 39 GLY B 50 1 12
HELIX 25 25 ASP B 72 ASP B 88 1 17
HELIX 26 26 MET B 99 GLY B 112 1 14
HELIX 27 27 PRO B 141 ASP B 155 1 15
HELIX 28 28 ASP B 155 ASN B 169 1 15
HELIX 29 29 ASN B 169 LEU B 174 1 6
HELIX 30 30 SER B 179 SER B 192 1 14
HELIX 31 31 GLY B 194 TRP B 205 1 12
HELIX 32 32 ASP B 212 ILE B 216 5 5
HELIX 33 33 THR B 236 LEU B 244 1 9
HELIX 34 34 GLY B 258 HIS B 263 1 6
HELIX 35 35 HIS B 263 SER B 296 1 34
HELIX 36 36 GLY B 301 ALA B 316 1 16
HELIX 37 37 ASP B 321 THR B 331 1 11
HELIX 38 38 SER B 336 VAL B 351 1 16
HELIX 39 39 ARG B 360 ASN B 368 1 9
HELIX 40 40 ASP B 372 LYS B 387 1 16
HELIX 41 41 THR B 391 LEU B 400 1 10
HELIX 42 42 SER B 403 ASN B 416 1 14
HELIX 43 43 THR B 422 GLN B 441 1 20
HELIX 44 44 SER C 35 SER C 38 5 4
HELIX 45 45 TRP C 39 GLY C 50 1 12
HELIX 46 46 ASP C 72 ASP C 88 1 17
HELIX 47 47 MET C 99 GLY C 112 1 14
HELIX 48 48 PRO C 141 ASP C 155 1 15
HELIX 49 49 ASP C 155 ASN C 169 1 15
HELIX 50 50 ASN C 169 LEU C 174 1 6
HELIX 51 51 SER C 179 SER C 192 1 14
HELIX 52 52 GLY C 194 TRP C 205 1 12
HELIX 53 53 ASP C 212 ILE C 216 5 5
HELIX 54 54 THR C 236 LEU C 244 1 9
HELIX 55 55 GLY C 258 HIS C 263 1 6
HELIX 56 56 HIS C 263 SER C 296 1 34
HELIX 57 57 GLY C 301 ALA C 316 1 16
HELIX 58 58 ASP C 321 THR C 331 1 11
HELIX 59 59 SER C 336 VAL C 351 1 16
HELIX 60 60 ARG C 360 ASN C 368 1 9
HELIX 61 61 ASP C 372 LYS C 387 1 16
HELIX 62 62 THR C 391 LEU C 400 1 10
HELIX 63 63 SER C 403 ASN C 416 1 14
HELIX 64 64 THR C 422 GLN C 441 1 20
HELIX 65 65 SER D 35 SER D 38 5 4
HELIX 66 66 TRP D 39 GLY D 50 1 12
HELIX 67 67 ASP D 72 ASP D 88 1 17
HELIX 68 68 MET D 99 GLY D 112 1 14
HELIX 69 69 PRO D 141 ASP D 155 1 15
HELIX 70 70 ASP D 155 ASN D 169 1 15
HELIX 71 71 ASN D 169 LEU D 174 1 6
HELIX 72 72 SER D 179 SER D 192 1 14
HELIX 73 73 GLY D 194 TRP D 205 1 12
HELIX 74 74 ASP D 212 ILE D 216 5 5
HELIX 75 75 THR D 236 LEU D 244 1 9
HELIX 76 76 GLY D 258 HIS D 263 1 6
HELIX 77 77 HIS D 263 SER D 296 1 34
HELIX 78 78 GLY D 301 ALA D 316 1 16
HELIX 79 79 ASP D 321 THR D 331 1 11
HELIX 80 80 SER D 336 VAL D 351 1 16
HELIX 81 81 ARG D 360 LEU D 367 1 8
HELIX 82 82 ASN D 368 GLY D 371 5 4
HELIX 83 83 ASP D 372 LYS D 387 1 16
HELIX 84 84 THR D 391 LEU D 400 1 10
HELIX 85 85 SER D 403 ASN D 416 1 14
HELIX 86 86 THR D 422 GLN D 441 1 20
HELIX 87 87 SER E 35 SER E 38 5 4
HELIX 88 88 TRP E 39 GLY E 50 1 12
HELIX 89 89 ASP E 72 ASP E 88 1 17
HELIX 90 90 MET E 99 GLY E 112 1 14
HELIX 91 91 PRO E 141 ASP E 155 1 15
HELIX 92 92 ASP E 155 ASN E 169 1 15
HELIX 93 93 ASN E 169 LEU E 174 1 6
HELIX 94 94 SER E 179 SER E 192 1 14
HELIX 95 95 GLY E 194 TRP E 205 1 12
HELIX 96 96 ASP E 212 ILE E 216 5 5
HELIX 97 97 THR E 236 LEU E 244 1 9
HELIX 98 98 GLY E 258 HIS E 263 1 6
HELIX 99 99 HIS E 263 SER E 296 1 34
HELIX 100 100 GLY E 301 ALA E 316 1 16
HELIX 101 101 ASP E 321 THR E 331 1 11
HELIX 102 102 SER E 336 VAL E 351 1 16
HELIX 103 103 ARG E 360 LEU E 367 1 8
HELIX 104 104 ASN E 368 GLY E 371 5 4
HELIX 105 105 ASP E 372 LYS E 387 1 16
HELIX 106 106 THR E 391 LEU E 400 1 10
HELIX 107 107 SER E 403 ASN E 416 1 14
HELIX 108 108 THR E 422 GLN E 441 1 20
HELIX 109 109 SER F 35 SER F 38 5 4
HELIX 110 110 TRP F 39 GLY F 50 1 12
HELIX 111 111 ASP F 72 ASP F 88 1 17
HELIX 112 112 MET F 99 GLY F 112 1 14
HELIX 113 113 PRO F 141 ASP F 155 1 15
HELIX 114 114 ASP F 155 ASN F 169 1 15
HELIX 115 115 ASN F 169 LEU F 174 1 6
HELIX 116 116 SER F 179 SER F 192 1 14
HELIX 117 117 GLY F 194 TRP F 205 1 12
HELIX 118 118 ASP F 212 ILE F 216 5 5
HELIX 119 119 THR F 236 LEU F 244 1 9
HELIX 120 120 GLY F 258 HIS F 263 1 6
HELIX 121 121 HIS F 263 SER F 296 1 34
HELIX 122 122 GLY F 301 ALA F 316 1 16
HELIX 123 123 ASP F 321 THR F 331 1 11
HELIX 124 124 SER F 336 VAL F 351 1 16
HELIX 125 125 ARG F 360 LEU F 367 1 8
HELIX 126 126 ASN F 368 GLY F 371 5 4
HELIX 127 127 ASP F 372 LYS F 387 1 16
HELIX 128 128 THR F 391 LEU F 400 1 10
HELIX 129 129 SER F 403 ASN F 416 1 14
HELIX 130 130 THR F 422 GLN F 441 1 20
HELIX 131 131 SER G 35 SER G 38 5 4
HELIX 132 132 TRP G 39 GLY G 50 1 12
HELIX 133 133 ASP G 72 ASP G 88 1 17
HELIX 134 134 MET G 99 GLY G 112 1 14
HELIX 135 135 PRO G 141 ASP G 155 1 15
HELIX 136 136 ASP G 155 ASN G 169 1 15
HELIX 137 137 ASN G 169 LEU G 174 1 6
HELIX 138 138 SER G 179 SER G 192 1 14
HELIX 139 139 GLY G 194 TRP G 205 1 12
HELIX 140 140 ASP G 212 ILE G 216 5 5
HELIX 141 141 THR G 236 LEU G 244 1 9
HELIX 142 142 GLY G 258 HIS G 263 1 6
HELIX 143 143 HIS G 263 SER G 296 1 34
HELIX 144 144 GLY G 301 ALA G 316 1 16
HELIX 145 145 ASP G 321 THR G 331 1 11
HELIX 146 146 SER G 336 VAL G 351 1 16
HELIX 147 147 ARG G 360 LEU G 367 1 8
HELIX 148 148 ASN G 368 GLY G 371 5 4
HELIX 149 149 ASP G 372 LYS G 387 1 16
HELIX 150 150 THR G 391 LEU G 400 1 10
HELIX 151 151 SER G 403 ASN G 416 1 14
HELIX 152 152 THR G 422 GLN G 441 1 20
HELIX 153 153 SER H 35 SER H 38 5 4
HELIX 154 154 TRP H 39 GLY H 50 1 12
HELIX 155 155 ASP H 72 ASP H 88 1 17
HELIX 156 156 MET H 99 GLY H 112 1 14
HELIX 157 157 PRO H 141 ASP H 155 1 15
HELIX 158 158 ASP H 155 ASN H 169 1 15
HELIX 159 159 ASN H 169 LEU H 174 1 6
HELIX 160 160 SER H 179 SER H 192 1 14
HELIX 161 161 GLY H 194 TRP H 205 1 12
HELIX 162 162 ASP H 212 ILE H 216 5 5
HELIX 163 163 THR H 236 LEU H 244 1 9
HELIX 164 164 GLY H 258 HIS H 263 1 6
HELIX 165 165 HIS H 263 SER H 296 1 34
HELIX 166 166 GLY H 301 ALA H 316 1 16
HELIX 167 167 ASP H 321 THR H 331 1 11
HELIX 168 168 SER H 336 VAL H 351 1 16
HELIX 169 169 ARG H 360 ASN H 368 1 9
HELIX 170 170 ASP H 372 LYS H 387 1 16
HELIX 171 171 THR H 391 LEU H 400 1 10
HELIX 172 172 SER H 403 ASN H 416 1 14
HELIX 173 173 THR H 422 GLN H 441 1 20
HELIX 174 174 SER I 35 SER I 38 5 4
HELIX 175 175 TRP I 39 GLY I 50 1 12
HELIX 176 176 ASP I 72 ASP I 88 1 17
HELIX 177 177 MET I 99 GLY I 112 1 14
HELIX 178 178 PRO I 141 ASP I 155 1 15
HELIX 179 179 ASP I 155 ASN I 169 1 15
HELIX 180 180 ASN I 169 LEU I 174 1 6
HELIX 181 181 SER I 179 SER I 192 1 14
HELIX 182 182 GLY I 194 TRP I 205 1 12
HELIX 183 183 ASP I 212 ILE I 216 5 5
HELIX 184 184 THR I 236 LEU I 244 1 9
HELIX 185 185 GLY I 258 HIS I 263 1 6
HELIX 186 186 HIS I 263 SER I 296 1 34
HELIX 187 187 GLY I 301 ALA I 316 1 16
HELIX 188 188 ASP I 321 THR I 331 1 11
HELIX 189 189 SER I 336 VAL I 351 1 16
HELIX 190 190 ARG I 360 ASN I 368 1 9
HELIX 191 191 ASP I 372 LYS I 387 1 16
HELIX 192 192 THR I 391 LEU I 400 1 10
HELIX 193 193 SER I 403 ASN I 416 1 14
HELIX 194 194 THR I 422 GLN I 441 1 20
HELIX 195 195 SER J 35 SER J 38 5 4
HELIX 196 196 TRP J 39 GLY J 50 1 12
HELIX 197 197 ASP J 72 ASP J 88 1 17
HELIX 198 198 MET J 99 GLY J 112 1 14
HELIX 199 199 PRO J 141 ASP J 155 1 15
HELIX 200 200 ASP J 155 ASN J 169 1 15
HELIX 201 201 ASN J 169 LEU J 174 1 6
HELIX 202 202 SER J 179 SER J 192 1 14
HELIX 203 203 GLY J 194 TRP J 205 1 12
HELIX 204 204 ASP J 212 ILE J 216 5 5
HELIX 205 205 THR J 236 LEU J 244 1 9
HELIX 206 206 GLY J 258 HIS J 263 1 6
HELIX 207 207 HIS J 263 SER J 296 1 34
HELIX 208 208 GLY J 301 ALA J 316 1 16
HELIX 209 209 ASP J 321 THR J 331 1 11
HELIX 210 210 SER J 336 VAL J 351 1 16
HELIX 211 211 ARG J 360 LEU J 367 1 8
HELIX 212 212 ASN J 368 GLY J 371 5 4
HELIX 213 213 ASP J 372 LYS J 387 1 16
HELIX 214 214 THR J 391 LEU J 400 1 10
HELIX 215 215 SER J 403 ASN J 416 1 14
HELIX 216 216 THR J 422 GLN J 441 1 20
HELIX 217 217 SER K 35 SER K 38 5 4
HELIX 218 218 TRP K 39 GLY K 50 1 12
HELIX 219 219 ASP K 72 ASP K 88 1 17
HELIX 220 220 MET K 99 GLY K 112 1 14
HELIX 221 221 PRO K 141 ASP K 155 1 15
HELIX 222 222 ASP K 155 ASN K 169 1 15
HELIX 223 223 ASN K 169 LEU K 174 1 6
HELIX 224 224 SER K 179 SER K 192 1 14
HELIX 225 225 GLY K 194 TRP K 205 1 12
HELIX 226 226 ASP K 212 ILE K 216 5 5
HELIX 227 227 THR K 236 LEU K 244 1 9
HELIX 228 228 GLY K 258 HIS K 263 1 6
HELIX 229 229 HIS K 263 SER K 296 1 34
HELIX 230 230 GLY K 301 ALA K 316 1 16
HELIX 231 231 ASP K 321 THR K 331 1 11
HELIX 232 232 SER K 336 VAL K 351 1 16
HELIX 233 233 ARG K 360 ASN K 368 1 9
HELIX 234 234 ASP K 372 LYS K 387 1 16
HELIX 235 235 THR K 391 LEU K 400 1 10
HELIX 236 236 SER K 403 ASN K 416 1 14
HELIX 237 237 THR K 422 GLN K 441 1 20
HELIX 238 238 SER L 35 SER L 38 5 4
HELIX 239 239 TRP L 39 GLY L 50 1 12
HELIX 240 240 ASP L 72 ASP L 88 1 17
HELIX 241 241 MET L 99 GLY L 112 1 14
HELIX 242 242 PRO L 141 ASP L 155 1 15
HELIX 243 243 ASP L 155 ASN L 169 1 15
HELIX 244 244 ASN L 169 LEU L 174 1 6
HELIX 245 245 SER L 179 SER L 192 1 14
HELIX 246 246 GLY L 194 TRP L 205 1 12
HELIX 247 247 ASP L 212 ILE L 216 5 5
HELIX 248 248 THR L 236 LEU L 244 1 9
HELIX 249 249 GLY L 258 HIS L 263 1 6
HELIX 250 250 HIS L 263 SER L 296 1 34
HELIX 251 251 GLY L 301 ALA L 316 1 16
HELIX 252 252 ASP L 321 THR L 331 1 11
HELIX 253 253 SER L 336 VAL L 351 1 16
HELIX 254 254 ARG L 360 ASN L 368 1 9
HELIX 255 255 ASP L 372 LYS L 387 1 16
HELIX 256 256 THR L 391 LEU L 400 1 10
HELIX 257 257 SER L 403 ASN L 416 1 14
HELIX 258 258 THR L 422 GLN L 441 1 20
SHEET 1 A 8 PHE A 2 GLU A 8 0
SHEET 2 A 8 THR A 11 HIS A 20 -1 O LEU A 15 N ILE A 3
SHEET 3 A 8 ARG A 52 TYR A 56 -1 O VAL A 53 N HIS A 20
SHEET 4 A 8 PRO A 25 ILE A 29 1 N VAL A 26 O ARG A 52
SHEET 5 A 8 ALA A 92 PHE A 97 1 O VAL A 93 N VAL A 27
SHEET 6 A 8 ILE A 116 LEU A 122 1 O ALA A 117 N ALA A 92
SHEET 7 A 8 ALA A 220 GLY A 225 1 O LEU A 223 N PHE A 121
SHEET 8 A 8 GLU A 248 VAL A 252 1 O VAL A 252 N HIS A 224
SHEET 1 B 8 PHE B 2 GLU B 8 0
SHEET 2 B 8 THR B 11 HIS B 20 -1 O LEU B 15 N ILE B 3
SHEET 3 B 8 ARG B 52 TYR B 56 -1 O VAL B 53 N HIS B 20
SHEET 4 B 8 PRO B 25 ILE B 29 1 N VAL B 26 O ARG B 52
SHEET 5 B 8 ALA B 92 PHE B 97 1 O VAL B 93 N VAL B 27
SHEET 6 B 8 ILE B 116 LEU B 122 1 O ALA B 117 N ALA B 92
SHEET 7 B 8 ALA B 220 GLY B 225 1 O LEU B 223 N PHE B 121
SHEET 8 B 8 GLU B 248 VAL B 252 1 O VAL B 252 N HIS B 224
SHEET 1 C 8 PHE C 2 GLU C 8 0
SHEET 2 C 8 THR C 11 HIS C 20 -1 O LEU C 15 N ILE C 3
SHEET 3 C 8 ARG C 52 TYR C 56 -1 O VAL C 53 N HIS C 20
SHEET 4 C 8 PRO C 25 ILE C 29 1 N VAL C 26 O ARG C 52
SHEET 5 C 8 ALA C 92 PHE C 97 1 O VAL C 93 N VAL C 27
SHEET 6 C 8 ILE C 116 LEU C 122 1 O ALA C 117 N ALA C 92
SHEET 7 C 8 ALA C 220 GLY C 225 1 O LEU C 223 N PHE C 121
SHEET 8 C 8 GLU C 248 VAL C 252 1 O VAL C 252 N HIS C 224
SHEET 1 D 8 PHE D 2 GLU D 8 0
SHEET 2 D 8 THR D 11 HIS D 20 -1 O LEU D 15 N ILE D 3
SHEET 3 D 8 ARG D 52 TYR D 56 -1 O VAL D 53 N HIS D 20
SHEET 4 D 8 PRO D 25 ILE D 29 1 N VAL D 26 O ARG D 52
SHEET 5 D 8 ALA D 92 PHE D 97 1 O VAL D 93 N VAL D 27
SHEET 6 D 8 ILE D 116 LEU D 122 1 O ALA D 117 N ALA D 92
SHEET 7 D 8 ALA D 220 GLY D 225 1 O LEU D 223 N PHE D 121
SHEET 8 D 8 GLU D 248 VAL D 252 1 O VAL D 252 N HIS D 224
SHEET 1 E 8 PHE E 2 GLU E 8 0
SHEET 2 E 8 THR E 11 HIS E 20 -1 O LEU E 15 N ILE E 3
SHEET 3 E 8 ARG E 52 TYR E 56 -1 O VAL E 53 N HIS E 20
SHEET 4 E 8 PRO E 25 ILE E 29 1 N VAL E 26 O ARG E 52
SHEET 5 E 8 ALA E 92 PHE E 97 1 O VAL E 93 N VAL E 27
SHEET 6 E 8 ILE E 116 LEU E 122 1 O ALA E 117 N ALA E 92
SHEET 7 E 8 ALA E 220 GLY E 225 1 O LEU E 223 N PHE E 121
SHEET 8 E 8 GLU E 248 VAL E 252 1 O VAL E 252 N HIS E 224
SHEET 1 F 8 PHE F 2 GLU F 8 0
SHEET 2 F 8 THR F 11 HIS F 20 -1 O LEU F 15 N ILE F 3
SHEET 3 F 8 ARG F 52 TYR F 56 -1 O VAL F 53 N HIS F 20
SHEET 4 F 8 PRO F 25 ILE F 29 1 N VAL F 26 O ARG F 52
SHEET 5 F 8 ALA F 92 PHE F 97 1 O VAL F 93 N VAL F 27
SHEET 6 F 8 ILE F 116 LEU F 122 1 O ALA F 117 N ALA F 92
SHEET 7 F 8 ALA F 220 GLY F 225 1 O LEU F 223 N PHE F 121
SHEET 8 F 8 GLU F 248 VAL F 252 1 O VAL F 252 N HIS F 224
SHEET 1 G 8 PHE G 2 GLU G 8 0
SHEET 2 G 8 THR G 11 HIS G 20 -1 O LEU G 15 N ILE G 3
SHEET 3 G 8 ARG G 52 TYR G 56 -1 O VAL G 53 N HIS G 20
SHEET 4 G 8 PRO G 25 ILE G 29 1 N VAL G 26 O ARG G 52
SHEET 5 G 8 ALA G 92 PHE G 97 1 O VAL G 93 N VAL G 27
SHEET 6 G 8 ILE G 116 LEU G 122 1 O ALA G 117 N ALA G 92
SHEET 7 G 8 ALA G 220 GLY G 225 1 O LEU G 223 N PHE G 121
SHEET 8 G 8 GLU G 248 VAL G 252 1 O VAL G 252 N HIS G 224
SHEET 1 H 8 PHE H 2 GLU H 8 0
SHEET 2 H 8 THR H 11 HIS H 20 -1 O LEU H 15 N ILE H 3
SHEET 3 H 8 ARG H 52 TYR H 56 -1 O VAL H 53 N HIS H 20
SHEET 4 H 8 PRO H 25 ILE H 29 1 N VAL H 26 O ARG H 52
SHEET 5 H 8 ALA H 92 PHE H 97 1 O VAL H 93 N VAL H 27
SHEET 6 H 8 ILE H 116 LEU H 122 1 O ALA H 117 N ALA H 92
SHEET 7 H 8 ALA H 220 GLY H 225 1 O LEU H 223 N PHE H 121
SHEET 8 H 8 GLU H 248 VAL H 252 1 O VAL H 252 N HIS H 224
SHEET 1 I 8 PHE I 2 GLU I 8 0
SHEET 2 I 8 THR I 11 HIS I 20 -1 O LEU I 15 N ILE I 3
SHEET 3 I 8 ARG I 52 TYR I 56 -1 O VAL I 53 N HIS I 20
SHEET 4 I 8 PRO I 25 ILE I 29 1 N VAL I 26 O ARG I 52
SHEET 5 I 8 ALA I 92 PHE I 97 1 O VAL I 93 N VAL I 27
SHEET 6 I 8 ILE I 116 LEU I 122 1 O ALA I 117 N ALA I 92
SHEET 7 I 8 ALA I 220 GLY I 225 1 O LEU I 223 N PHE I 121
SHEET 8 I 8 GLU I 248 VAL I 252 1 O VAL I 252 N HIS I 224
SHEET 1 J 8 PHE J 2 GLU J 8 0
SHEET 2 J 8 THR J 11 HIS J 20 -1 O LEU J 15 N ILE J 3
SHEET 3 J 8 ARG J 52 TYR J 56 -1 O VAL J 53 N HIS J 20
SHEET 4 J 8 PRO J 25 ILE J 29 1 N VAL J 26 O ARG J 52
SHEET 5 J 8 ALA J 92 PHE J 97 1 O VAL J 93 N VAL J 27
SHEET 6 J 8 ILE J 116 LEU J 122 1 O ALA J 117 N ALA J 92
SHEET 7 J 8 ALA J 220 GLY J 225 1 O LEU J 223 N PHE J 121
SHEET 8 J 8 GLU J 248 VAL J 252 1 O VAL J 252 N HIS J 224
SHEET 1 K 8 PHE K 2 GLU K 8 0
SHEET 2 K 8 THR K 11 HIS K 20 -1 O LEU K 15 N ILE K 3
SHEET 3 K 8 ARG K 52 TYR K 56 -1 O VAL K 53 N HIS K 20
SHEET 4 K 8 PRO K 25 ILE K 29 1 N VAL K 26 O ARG K 52
SHEET 5 K 8 ALA K 92 PHE K 97 1 O VAL K 93 N VAL K 27
SHEET 6 K 8 ILE K 116 LEU K 122 1 O ALA K 117 N ALA K 92
SHEET 7 K 8 ALA K 220 GLY K 225 1 O LEU K 223 N PHE K 121
SHEET 8 K 8 GLU K 248 VAL K 252 1 O VAL K 252 N HIS K 224
SHEET 1 L 8 PHE L 2 GLU L 8 0
SHEET 2 L 8 THR L 11 HIS L 20 -1 O LEU L 15 N ILE L 3
SHEET 3 L 8 ARG L 52 TYR L 56 -1 O VAL L 53 N HIS L 20
SHEET 4 L 8 PRO L 25 ILE L 29 1 N VAL L 26 O ARG L 52
SHEET 5 L 8 ALA L 92 PHE L 97 1 O VAL L 93 N VAL L 27
SHEET 6 L 8 ILE L 116 LEU L 122 1 O ALA L 117 N ALA L 92
SHEET 7 L 8 ALA L 220 GLY L 225 1 O LEU L 223 N PHE L 121
SHEET 8 L 8 GLU L 248 VAL L 252 1 O VAL L 252 N HIS L 224
CISPEP 1 PHE A 32 PRO A 33 0 -1.51
CISPEP 2 GLU A 126 PRO A 127 0 5.62
CISPEP 3 PHE B 32 PRO B 33 0 -1.54
CISPEP 4 GLU B 126 PRO B 127 0 5.59
CISPEP 5 PHE C 32 PRO C 33 0 -1.48
CISPEP 6 GLU C 126 PRO C 127 0 5.53
CISPEP 7 PHE D 32 PRO D 33 0 -1.69
CISPEP 8 GLU D 126 PRO D 127 0 5.70
CISPEP 9 PHE E 32 PRO E 33 0 -1.70
CISPEP 10 GLU E 126 PRO E 127 0 5.52
CISPEP 11 PHE F 32 PRO F 33 0 -1.66
CISPEP 12 GLU F 126 PRO F 127 0 5.61
CISPEP 13 PHE G 32 PRO G 33 0 -1.71
CISPEP 14 GLU G 126 PRO G 127 0 5.63
CISPEP 15 PHE H 32 PRO H 33 0 -1.62
CISPEP 16 GLU H 126 PRO H 127 0 5.47
CISPEP 17 PHE I 32 PRO I 33 0 -1.60
CISPEP 18 GLU I 126 PRO I 127 0 5.63
CISPEP 19 PHE J 32 PRO J 33 0 -1.84
CISPEP 20 GLU J 126 PRO J 127 0 5.61
CISPEP 21 PHE K 32 PRO K 33 0 -1.69
CISPEP 22 GLU K 126 PRO K 127 0 5.62
CISPEP 23 PHE L 32 PRO L 33 0 -1.63
CISPEP 24 GLU L 126 PRO L 127 0 5.54
CRYST1 155.500 156.520 325.030 90.00 90.00 90.00 P 21 21 21 48
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 0.006431 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006389 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003077 0.00000
TER 3377 GLN A 441
TER 6754 GLN B 441
TER 10131 GLN C 441
TER 13508 GLN D 441
TER 16885 GLN E 441
TER 20262 GLN F 441
TER 23639 GLN G 441
TER 27016 GLN H 441
TER 30393 GLN I 441
TER 33770 GLN J 441
TER 37147 GLN K 441
TER 40524 GLN L 441
MASTER 651 0 0 258 96 0 0 640512 12 0 432
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