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HEADER HYDROLASE 13-OCT-05 2B9V
TITLE ACETOBACTER TURBIDANS ALPHA-AMINO ACID ESTER HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMINO ACID ESTER HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P;
COMPND 4 EC: 3.1.1.43;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACETOBACTER PASTEURIANUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: AEHA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TOP10F;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD
KEYWDS CATALYTIC TRIAD, ALPHA/BETA-HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.R.M.BARENDS
REVDAT 1 27-DEC-05 2B9V 0
JRNL AUTH T.R.M.BARENDS,J.J.POLDERMAN-TIJMES,P.A.JEKEL,
JRNL AUTH 2 G.WYBENGA,C.WILLIAMS,D.B.JANSSEN,B.W.DIJKSTRA
JRNL TITL ACETOBACTER TURBIDANS AEH: HOW A SINGLE MUTATION
JRNL TITL 2 IMPROVES AN ANTIBIOTIC-PRODUCING ENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.4
REMARK 3 NUMBER OF REFLECTIONS : 504379
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, BUT SUCH THAT TWIN
REMARK 3 -RELATED REFLECTIONS ARE
REMARK 3 ALWAYS IN THE SAME SUBSET
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 25420
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 50
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW : 2.02
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8618
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 43.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 467
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 80710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : -0.05000
REMARK 3 B33 (A**2) : -0.04000
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): 0.297
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.210
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 79568 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 58914 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES):108656 ; 1.663 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES):140436 ; 3.386 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 9696 ; 2.715 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 3872 ;32.467 ;23.554
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 11776 ;12.349 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 528 ;14.367 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 11232 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 90000 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 16816 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9456 ; 0.196 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 34971 ; 0.234 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 25478 ; 0.186 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 24687 ; 0.114 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 117 ; 0.153 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 489 ; 0.081 ; 0.500
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): 126 ; 0.300 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 197 ; 0.417 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.123 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): 5 ; 0.296 ; 0.500
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): 48688 ; 1.066 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 19391 ; 0.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 78768 ; 1.646 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 30880 ; 2.501 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 29888 ; 3.664 ; 4.500
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 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L M
REMARK 3 N
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 50 A 666 1
REMARK 3 1 B 50 B 666 1
REMARK 3 1 C 50 C 666 1
REMARK 3 1 D 50 D 666 1
REMARK 3 1 E 50 E 666 1
REMARK 3 1 F 50 F 666 1
REMARK 3 1 G 50 G 666 1
REMARK 3 1 H 50 H 666 1
REMARK 3 1 I 50 I 666 1
REMARK 3 1 J 50 J 666 1
REMARK 3 1 K 50 K 666 1
REMARK 3 1 L 50 L 666 1
REMARK 3 1 M 50 M 666 1
REMARK 3 1 N 50 N 666 1
REMARK 3 1 O 50 O 666 1
REMARK 3 1 P 50 P 666 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 8177 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 8177 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 8177 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 8177 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 8177 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 F (A): 8177 ; 0.12 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 G (A): 8177 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 H (A): 8177 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 I (A): 8177 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 J (A): 8177 ; 0.10 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 K (A): 8177 ; 0.10 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 L (A): 8177 ; 0.10 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 M (A): 8177 ; 0.10 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 N (A): 8177 ; 0.10 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 O (A): 8177 ; 0.11 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 P (A): 8177 ; 0.10 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 8177 ; 0.61 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 8177 ; 0.57 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 8177 ; 0.57 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 8177 ; 0.57 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 8177 ; 0.55 ; 0.50
REMARK 3 TIGHT THERMAL 1 F (A**2): 8177 ; 0.56 ; 0.50
REMARK 3 TIGHT THERMAL 1 G (A**2): 8177 ; 0.56 ; 0.50
REMARK 3 TIGHT THERMAL 1 H (A**2): 8177 ; 0.62 ; 0.50
REMARK 3 TIGHT THERMAL 1 I (A**2): 8177 ; 0.57 ; 0.50
REMARK 3 TIGHT THERMAL 1 J (A**2): 8177 ; 0.58 ; 0.50
REMARK 3 TIGHT THERMAL 1 K (A**2): 8177 ; 0.57 ; 0.50
REMARK 3 TIGHT THERMAL 1 L (A**2): 8177 ; 0.59 ; 0.50
REMARK 3 TIGHT THERMAL 1 M (A**2): 8177 ; 0.57 ; 0.50
REMARK 3 TIGHT THERMAL 1 N (A**2): 8177 ; 0.61 ; 0.50
REMARK 3 TIGHT THERMAL 1 O (A**2): 8177 ; 0.55 ; 0.50
REMARK 3 TIGHT THERMAL 1 P (A**2): 8177 ; 0.65 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 3 RIDING POSITIONS, REFINEMENT AGAINST DETWINNED DATA. THE
REMARK 3 STRUCTURE DATA CONTAINS BOTH DETWINNED AND TWINNED DATA.
REMARK 4
REMARK 4 2B9V COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-2005.
REMARK 100 THE RCSB ID CODE IS RCSB034856.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 598744
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1MPX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-17% PEG 4000, 0.2 M AMMONIUM
REMARK 280 ACETATE, 0.1 M SODIUM ACETATE BUFFER, PH 4.6, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,1/2+Y,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 137.79700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 16CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 4
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 ALA A 44
REMARK 465 ASP A 45
REMARK 465 ALA A 46
REMARK 465 ALA A 47
REMARK 465 GLN A 48
REMARK 465 ALA A 49
REMARK 465 ALA A 63
REMARK 465 SER A 64
REMARK 465 VAL A 65
REMARK 465 HIS A 66
REMARK 465 MET A 67
REMARK 465 PRO A 68
REMARK 465 THR A 69
REMARK 465 ASP A 70
REMARK 465 GLN A 71
REMARK 465 GLN A 667
REMARK 465 LYS A 668
REMARK 465 LEU A 669
REMARK 465 GLY A 670
REMARK 465 PRO A 671
REMARK 465 GLU A 672
REMARK 465 GLN A 673
REMARK 465 LYS A 674
REMARK 465 LEU A 675
REMARK 465 ILE A 676
REMARK 465 SER A 677
REMARK 465 GLU A 678
REMARK 465 GLU A 679
REMARK 465 ASP A 680
REMARK 465 LEU A 681
REMARK 465 ASN A 682
REMARK 465 SER A 683
REMARK 465 ALA A 684
REMARK 465 VAL A 685
REMARK 465 ASP A 686
REMARK 465 HIS A 687
REMARK 465 HIS A 688
REMARK 465 HIS A 689
REMARK 465 HIS A 690
REMARK 465 HIS A 691
REMARK 465 HIS A 692
REMARK 465 ALA B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 ALA B 44
REMARK 465 ASP B 45
REMARK 465 ALA B 46
REMARK 465 ALA B 47
REMARK 465 GLN B 48
REMARK 465 ALA B 49
REMARK 465 ALA B 63
REMARK 465 SER B 64
REMARK 465 VAL B 65
REMARK 465 HIS B 66
REMARK 465 MET B 67
REMARK 465 PRO B 68
REMARK 465 THR B 69
REMARK 465 ASP B 70
REMARK 465 GLN B 71
REMARK 465 GLN B 667
REMARK 465 LYS B 668
REMARK 465 LEU B 669
REMARK 465 GLY B 670
REMARK 465 PRO B 671
REMARK 465 GLU B 672
REMARK 465 GLN B 673
REMARK 465 LYS B 674
REMARK 465 LEU B 675
REMARK 465 ILE B 676
REMARK 465 SER B 677
REMARK 465 GLU B 678
REMARK 465 GLU B 679
REMARK 465 ASP B 680
REMARK 465 LEU B 681
REMARK 465 ASN B 682
REMARK 465 SER B 683
REMARK 465 ALA B 684
REMARK 465 VAL B 685
REMARK 465 ASP B 686
REMARK 465 HIS B 687
REMARK 465 HIS B 688
REMARK 465 HIS B 689
REMARK 465 HIS B 690
REMARK 465 HIS B 691
REMARK 465 HIS B 692
REMARK 465 ALA C 41
REMARK 465 PRO C 42
REMARK 465 ALA C 43
REMARK 465 ALA C 44
REMARK 465 ASP C 45
REMARK 465 ALA C 46
REMARK 465 ALA C 47
REMARK 465 GLN C 48
REMARK 465 ALA C 49
REMARK 465 ALA C 63
REMARK 465 SER C 64
REMARK 465 VAL C 65
REMARK 465 HIS C 66
REMARK 465 MET C 67
REMARK 465 PRO C 68
REMARK 465 THR C 69
REMARK 465 ASP C 70
REMARK 465 GLN C 71
REMARK 465 GLN C 667
REMARK 465 LYS C 668
REMARK 465 LEU C 669
REMARK 465 GLY C 670
REMARK 465 PRO C 671
REMARK 465 GLU C 672
REMARK 465 GLN C 673
REMARK 465 LYS C 674
REMARK 465 LEU C 675
REMARK 465 ILE C 676
REMARK 465 SER C 677
REMARK 465 GLU C 678
REMARK 465 GLU C 679
REMARK 465 ASP C 680
REMARK 465 LEU C 681
REMARK 465 ASN C 682
REMARK 465 SER C 683
REMARK 465 ALA C 684
REMARK 465 VAL C 685
REMARK 465 ASP C 686
REMARK 465 HIS C 687
REMARK 465 HIS C 688
REMARK 465 HIS C 689
REMARK 465 HIS C 690
REMARK 465 HIS C 691
REMARK 465 HIS C 692
REMARK 465 ALA D 41
REMARK 465 PRO D 42
REMARK 465 ALA D 43
REMARK 465 ALA D 44
REMARK 465 ASP D 45
REMARK 465 ALA D 46
REMARK 465 ALA D 47
REMARK 465 GLN D 48
REMARK 465 ALA D 49
REMARK 465 ALA D 63
REMARK 465 SER D 64
REMARK 465 VAL D 65
REMARK 465 HIS D 66
REMARK 465 MET D 67
REMARK 465 PRO D 68
REMARK 465 THR D 69
REMARK 465 ASP D 70
REMARK 465 GLN D 71
REMARK 465 GLN D 667
REMARK 465 LYS D 668
REMARK 465 LEU D 669
REMARK 465 GLY D 670
REMARK 465 PRO D 671
REMARK 465 GLU D 672
REMARK 465 GLN D 673
REMARK 465 LYS D 674
REMARK 465 LEU D 675
REMARK 465 ILE D 676
REMARK 465 SER D 677
REMARK 465 GLU D 678
REMARK 465 GLU D 679
REMARK 465 ASP D 680
REMARK 465 LEU D 681
REMARK 465 ASN D 682
REMARK 465 SER D 683
REMARK 465 ALA D 684
REMARK 465 VAL D 685
REMARK 465 ASP D 686
REMARK 465 HIS D 687
REMARK 465 HIS D 688
REMARK 465 HIS D 689
REMARK 465 HIS D 690
REMARK 465 HIS D 691
REMARK 465 HIS D 692
REMARK 465 ALA E 41
REMARK 465 PRO E 42
REMARK 465 ALA E 43
REMARK 465 ALA E 44
REMARK 465 ASP E 45
REMARK 465 ALA E 46
REMARK 465 ALA E 47
REMARK 465 GLN E 48
REMARK 465 ALA E 49
REMARK 465 ALA E 63
REMARK 465 SER E 64
REMARK 465 VAL E 65
REMARK 465 HIS E 66
REMARK 465 MET E 67
REMARK 465 PRO E 68
REMARK 465 THR E 69
REMARK 465 ASP E 70
REMARK 465 GLN E 71
REMARK 465 GLN E 667
REMARK 465 LYS E 668
REMARK 465 LEU E 669
REMARK 465 GLY E 670
REMARK 465 PRO E 671
REMARK 465 GLU E 672
REMARK 465 GLN E 673
REMARK 465 LYS E 674
REMARK 465 LEU E 675
REMARK 465 ILE E 676
REMARK 465 SER E 677
REMARK 465 GLU E 678
REMARK 465 GLU E 679
REMARK 465 ASP E 680
REMARK 465 LEU E 681
REMARK 465 ASN E 682
REMARK 465 SER E 683
REMARK 465 ALA E 684
REMARK 465 VAL E 685
REMARK 465 ASP E 686
REMARK 465 HIS E 687
REMARK 465 HIS E 688
REMARK 465 HIS E 689
REMARK 465 HIS E 690
REMARK 465 HIS E 691
REMARK 465 HIS E 692
REMARK 465 ALA F 41
REMARK 465 PRO F 42
REMARK 465 ALA F 43
REMARK 465 ALA F 44
REMARK 465 ASP F 45
REMARK 465 ALA F 46
REMARK 465 ALA F 47
REMARK 465 GLN F 48
REMARK 465 ALA F 49
REMARK 465 ALA F 63
REMARK 465 SER F 64
REMARK 465 VAL F 65
REMARK 465 HIS F 66
REMARK 465 MET F 67
REMARK 465 PRO F 68
REMARK 465 THR F 69
REMARK 465 ASP F 70
REMARK 465 GLN F 71
REMARK 465 GLN F 667
REMARK 465 LYS F 668
REMARK 465 LEU F 669
REMARK 465 GLY F 670
REMARK 465 PRO F 671
REMARK 465 GLU F 672
REMARK 465 GLN F 673
REMARK 465 LYS F 674
REMARK 465 LEU F 675
REMARK 465 ILE F 676
REMARK 465 SER F 677
REMARK 465 GLU F 678
REMARK 465 GLU F 679
REMARK 465 ASP F 680
REMARK 465 LEU F 681
REMARK 465 ASN F 682
REMARK 465 SER F 683
REMARK 465 ALA F 684
REMARK 465 VAL F 685
REMARK 465 ASP F 686
REMARK 465 HIS F 687
REMARK 465 HIS F 688
REMARK 465 HIS F 689
REMARK 465 HIS F 690
REMARK 465 HIS F 691
REMARK 465 HIS F 692
REMARK 465 ALA G 41
REMARK 465 PRO G 42
REMARK 465 ALA G 43
REMARK 465 ALA G 44
REMARK 465 ASP G 45
REMARK 465 ALA G 46
REMARK 465 ALA G 47
REMARK 465 GLN G 48
REMARK 465 ALA G 49
REMARK 465 ALA G 63
REMARK 465 SER G 64
REMARK 465 VAL G 65
REMARK 465 HIS G 66
REMARK 465 MET G 67
REMARK 465 PRO G 68
REMARK 465 THR G 69
REMARK 465 ASP G 70
REMARK 465 GLN G 71
REMARK 465 GLN G 667
REMARK 465 LYS G 668
REMARK 465 LEU G 669
REMARK 465 GLY G 670
REMARK 465 PRO G 671
REMARK 465 GLU G 672
REMARK 465 GLN G 673
REMARK 465 LYS G 674
REMARK 465 LEU G 675
REMARK 465 ILE G 676
REMARK 465 SER G 677
REMARK 465 GLU G 678
REMARK 465 GLU G 679
REMARK 465 ASP G 680
REMARK 465 LEU G 681
REMARK 465 ASN G 682
REMARK 465 SER G 683
REMARK 465 ALA G 684
REMARK 465 VAL G 685
REMARK 465 ASP G 686
REMARK 465 HIS G 687
REMARK 465 HIS G 688
REMARK 465 HIS G 689
REMARK 465 HIS G 690
REMARK 465 HIS G 691
REMARK 465 HIS G 692
REMARK 465 ALA H 41
REMARK 465 PRO H 42
REMARK 465 ALA H 43
REMARK 465 ALA H 44
REMARK 465 ASP H 45
REMARK 465 ALA H 46
REMARK 465 ALA H 47
REMARK 465 GLN H 48
REMARK 465 ALA H 49
REMARK 465 ALA H 63
REMARK 465 SER H 64
REMARK 465 VAL H 65
REMARK 465 HIS H 66
REMARK 465 MET H 67
REMARK 465 PRO H 68
REMARK 465 THR H 69
REMARK 465 ASP H 70
REMARK 465 GLN H 71
REMARK 465 GLN H 667
REMARK 465 LYS H 668
REMARK 465 LEU H 669
REMARK 465 GLY H 670
REMARK 465 PRO H 671
REMARK 465 GLU H 672
REMARK 465 GLN H 673
REMARK 465 LYS H 674
REMARK 465 LEU H 675
REMARK 465 ILE H 676
REMARK 465 SER H 677
REMARK 465 GLU H 678
REMARK 465 GLU H 679
REMARK 465 ASP H 680
REMARK 465 LEU H 681
REMARK 465 ASN H 682
REMARK 465 SER H 683
REMARK 465 ALA H 684
REMARK 465 VAL H 685
REMARK 465 ASP H 686
REMARK 465 HIS H 687
REMARK 465 HIS H 688
REMARK 465 HIS H 689
REMARK 465 HIS H 690
REMARK 465 HIS H 691
REMARK 465 HIS H 692
REMARK 465 ALA I 41
REMARK 465 PRO I 42
REMARK 465 ALA I 43
REMARK 465 ALA I 44
REMARK 465 ASP I 45
REMARK 465 ALA I 46
REMARK 465 ALA I 47
REMARK 465 GLN I 48
REMARK 465 ALA I 49
REMARK 465 ALA I 63
REMARK 465 SER I 64
REMARK 465 VAL I 65
REMARK 465 HIS I 66
REMARK 465 MET I 67
REMARK 465 PRO I 68
REMARK 465 THR I 69
REMARK 465 ASP I 70
REMARK 465 GLN I 71
REMARK 465 GLN I 667
REMARK 465 LYS I 668
REMARK 465 LEU I 669
REMARK 465 GLY I 670
REMARK 465 PRO I 671
REMARK 465 GLU I 672
REMARK 465 GLN I 673
REMARK 465 LYS I 674
REMARK 465 LEU I 675
REMARK 465 ILE I 676
REMARK 465 SER I 677
REMARK 465 GLU I 678
REMARK 465 GLU I 679
REMARK 465 ASP I 680
REMARK 465 LEU I 681
REMARK 465 ASN I 682
REMARK 465 SER I 683
REMARK 465 ALA I 684
REMARK 465 VAL I 685
REMARK 465 ASP I 686
REMARK 465 HIS I 687
REMARK 465 HIS I 688
REMARK 465 HIS I 689
REMARK 465 HIS I 690
REMARK 465 HIS I 691
REMARK 465 HIS I 692
REMARK 465 ALA J 41
REMARK 465 PRO J 42
REMARK 465 ALA J 43
REMARK 465 ALA J 44
REMARK 465 ASP J 45
REMARK 465 ALA J 46
REMARK 465 ALA J 47
REMARK 465 GLN J 48
REMARK 465 ALA J 49
REMARK 465 ALA J 63
REMARK 465 SER J 64
REMARK 465 VAL J 65
REMARK 465 HIS J 66
REMARK 465 MET J 67
REMARK 465 PRO J 68
REMARK 465 THR J 69
REMARK 465 ASP J 70
REMARK 465 GLN J 71
REMARK 465 GLN J 667
REMARK 465 LYS J 668
REMARK 465 LEU J 669
REMARK 465 GLY J 670
REMARK 465 PRO J 671
REMARK 465 GLU J 672
REMARK 465 GLN J 673
REMARK 465 LYS J 674
REMARK 465 LEU J 675
REMARK 465 ILE J 676
REMARK 465 SER J 677
REMARK 465 GLU J 678
REMARK 465 GLU J 679
REMARK 465 ASP J 680
REMARK 465 LEU J 681
REMARK 465 ASN J 682
REMARK 465 SER J 683
REMARK 465 ALA J 684
REMARK 465 VAL J 685
REMARK 465 ASP J 686
REMARK 465 HIS J 687
REMARK 465 HIS J 688
REMARK 465 HIS J 689
REMARK 465 HIS J 690
REMARK 465 HIS J 691
REMARK 465 HIS J 692
REMARK 465 ALA K 41
REMARK 465 PRO K 42
REMARK 465 ALA K 43
REMARK 465 ALA K 44
REMARK 465 ASP K 45
REMARK 465 ALA K 46
REMARK 465 ALA K 47
REMARK 465 GLN K 48
REMARK 465 ALA K 49
REMARK 465 ALA K 63
REMARK 465 SER K 64
REMARK 465 VAL K 65
REMARK 465 HIS K 66
REMARK 465 MET K 67
REMARK 465 PRO K 68
REMARK 465 THR K 69
REMARK 465 ASP K 70
REMARK 465 GLN K 71
REMARK 465 GLN K 667
REMARK 465 LYS K 668
REMARK 465 LEU K 669
REMARK 465 GLY K 670
REMARK 465 PRO K 671
REMARK 465 GLU K 672
REMARK 465 GLN K 673
REMARK 465 LYS K 674
REMARK 465 LEU K 675
REMARK 465 ILE K 676
REMARK 465 SER K 677
REMARK 465 GLU K 678
REMARK 465 GLU K 679
REMARK 465 ASP K 680
REMARK 465 LEU K 681
REMARK 465 ASN K 682
REMARK 465 SER K 683
REMARK 465 ALA K 684
REMARK 465 VAL K 685
REMARK 465 ASP K 686
REMARK 465 HIS K 687
REMARK 465 HIS K 688
REMARK 465 HIS K 689
REMARK 465 HIS K 690
REMARK 465 HIS K 691
REMARK 465 HIS K 692
REMARK 465 ALA L 41
REMARK 465 PRO L 42
REMARK 465 ALA L 43
REMARK 465 ALA L 44
REMARK 465 ASP L 45
REMARK 465 ALA L 46
REMARK 465 ALA L 47
REMARK 465 GLN L 48
REMARK 465 ALA L 49
REMARK 465 ALA L 63
REMARK 465 SER L 64
REMARK 465 VAL L 65
REMARK 465 HIS L 66
REMARK 465 MET L 67
REMARK 465 PRO L 68
REMARK 465 THR L 69
REMARK 465 ASP L 70
REMARK 465 GLN L 71
REMARK 465 GLN L 667
REMARK 465 LYS L 668
REMARK 465 LEU L 669
REMARK 465 GLY L 670
REMARK 465 PRO L 671
REMARK 465 GLU L 672
REMARK 465 GLN L 673
REMARK 465 LYS L 674
REMARK 465 LEU L 675
REMARK 465 ILE L 676
REMARK 465 SER L 677
REMARK 465 GLU L 678
REMARK 465 GLU L 679
REMARK 465 ASP L 680
REMARK 465 LEU L 681
REMARK 465 ASN L 682
REMARK 465 SER L 683
REMARK 465 ALA L 684
REMARK 465 VAL L 685
REMARK 465 ASP L 686
REMARK 465 HIS L 687
REMARK 465 HIS L 688
REMARK 465 HIS L 689
REMARK 465 HIS L 690
REMARK 465 HIS L 691
REMARK 465 HIS L 692
REMARK 465 ALA M 41
REMARK 465 PRO M 42
REMARK 465 ALA M 43
REMARK 465 ALA M 44
REMARK 465 ASP M 45
REMARK 465 ALA M 46
REMARK 465 ALA M 47
REMARK 465 GLN M 48
REMARK 465 ALA M 49
REMARK 465 ALA M 63
REMARK 465 SER M 64
REMARK 465 VAL M 65
REMARK 465 HIS M 66
REMARK 465 MET M 67
REMARK 465 PRO M 68
REMARK 465 THR M 69
REMARK 465 ASP M 70
REMARK 465 GLN M 71
REMARK 465 GLN M 667
REMARK 465 LYS M 668
REMARK 465 LEU M 669
REMARK 465 GLY M 670
REMARK 465 PRO M 671
REMARK 465 GLU M 672
REMARK 465 GLN M 673
REMARK 465 LYS M 674
REMARK 465 LEU M 675
REMARK 465 ILE M 676
REMARK 465 SER M 677
REMARK 465 GLU M 678
REMARK 465 GLU M 679
REMARK 465 ASP M 680
REMARK 465 LEU M 681
REMARK 465 ASN M 682
REMARK 465 SER M 683
REMARK 465 ALA M 684
REMARK 465 VAL M 685
REMARK 465 ASP M 686
REMARK 465 HIS M 687
REMARK 465 HIS M 688
REMARK 465 HIS M 689
REMARK 465 HIS M 690
REMARK 465 HIS M 691
REMARK 465 HIS M 692
REMARK 465 ALA N 41
REMARK 465 PRO N 42
REMARK 465 ALA N 43
REMARK 465 ALA N 44
REMARK 465 ASP N 45
REMARK 465 ALA N 46
REMARK 465 ALA N 47
REMARK 465 GLN N 48
REMARK 465 ALA N 49
REMARK 465 ALA N 63
REMARK 465 SER N 64
REMARK 465 VAL N 65
REMARK 465 HIS N 66
REMARK 465 MET N 67
REMARK 465 PRO N 68
REMARK 465 THR N 69
REMARK 465 ASP N 70
REMARK 465 GLN N 71
REMARK 465 GLN N 667
REMARK 465 LYS N 668
REMARK 465 LEU N 669
REMARK 465 GLY N 670
REMARK 465 PRO N 671
REMARK 465 GLU N 672
REMARK 465 GLN N 673
REMARK 465 LYS N 674
REMARK 465 LEU N 675
REMARK 465 ILE N 676
REMARK 465 SER N 677
REMARK 465 GLU N 678
REMARK 465 GLU N 679
REMARK 465 ASP N 680
REMARK 465 LEU N 681
REMARK 465 ASN N 682
REMARK 465 SER N 683
REMARK 465 ALA N 684
REMARK 465 VAL N 685
REMARK 465 ASP N 686
REMARK 465 HIS N 687
REMARK 465 HIS N 688
REMARK 465 HIS N 689
REMARK 465 HIS N 690
REMARK 465 HIS N 691
REMARK 465 HIS N 692
REMARK 465 ALA O 41
REMARK 465 PRO O 42
REMARK 465 ALA O 43
REMARK 465 ALA O 44
REMARK 465 ASP O 45
REMARK 465 ALA O 46
REMARK 465 ALA O 47
REMARK 465 GLN O 48
REMARK 465 ALA O 49
REMARK 465 ALA O 63
REMARK 465 SER O 64
REMARK 465 VAL O 65
REMARK 465 HIS O 66
REMARK 465 MET O 67
REMARK 465 PRO O 68
REMARK 465 THR O 69
REMARK 465 ASP O 70
REMARK 465 GLN O 71
REMARK 465 GLN O 667
REMARK 465 LYS O 668
REMARK 465 LEU O 669
REMARK 465 GLY O 670
REMARK 465 PRO O 671
REMARK 465 GLU O 672
REMARK 465 GLN O 673
REMARK 465 LYS O 674
REMARK 465 LEU O 675
REMARK 465 ILE O 676
REMARK 465 SER O 677
REMARK 465 GLU O 678
REMARK 465 GLU O 679
REMARK 465 ASP O 680
REMARK 465 LEU O 681
REMARK 465 ASN O 682
REMARK 465 SER O 683
REMARK 465 ALA O 684
REMARK 465 VAL O 685
REMARK 465 ASP O 686
REMARK 465 HIS O 687
REMARK 465 HIS O 688
REMARK 465 HIS O 689
REMARK 465 HIS O 690
REMARK 465 HIS O 691
REMARK 465 HIS O 692
REMARK 465 ALA P 41
REMARK 465 PRO P 42
REMARK 465 ALA P 43
REMARK 465 ALA P 44
REMARK 465 ASP P 45
REMARK 465 ALA P 46
REMARK 465 ALA P 47
REMARK 465 GLN P 48
REMARK 465 ALA P 49
REMARK 465 ALA P 63
REMARK 465 SER P 64
REMARK 465 VAL P 65
REMARK 465 HIS P 66
REMARK 465 MET P 67
REMARK 465 PRO P 68
REMARK 465 THR P 69
REMARK 465 ASP P 70
REMARK 465 GLN P 71
REMARK 465 GLN P 667
REMARK 465 LYS P 668
REMARK 465 LEU P 669
REMARK 465 GLY P 670
REMARK 465 PRO P 671
REMARK 465 GLU P 672
REMARK 465 GLN P 673
REMARK 465 LYS P 674
REMARK 465 LEU P 675
REMARK 465 ILE P 676
REMARK 465 SER P 677
REMARK 465 GLU P 678
REMARK 465 GLU P 679
REMARK 465 ASP P 680
REMARK 465 LEU P 681
REMARK 465 ASN P 682
REMARK 465 SER P 683
REMARK 465 ALA P 684
REMARK 465 VAL P 685
REMARK 465 ASP P 686
REMARK 465 HIS P 687
REMARK 465 HIS P 688
REMARK 465 HIS P 689
REMARK 465 HIS P 690
REMARK 465 HIS P 691
REMARK 465 HIS P 692
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
REMARK 500 O ASP K 356 NZ LYS K 358 1.75
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASN D 102 C PRO O 62 2645 1.94
REMARK 500 OD1 ASP M 318 NZ LYS O 655 1455 2.10
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 111 CB PRO A 111 CG -0.056
REMARK 500 PRO A 329 CB PRO A 329 CG -0.049
REMARK 500 PRO A 416 CB PRO A 416 CG -0.064
REMARK 500 PRO A 435 CB PRO A 435 CG -0.048
REMARK 500 PRO A 448 CB PRO A 448 CG -0.053
REMARK 500 PRO A 628 CB PRO A 628 CG -0.059
REMARK 500 PRO B 218 CB PRO B 218 CG -0.052
REMARK 500 PRO B 628 CB PRO B 628 CG -0.060
REMARK 500 PRO C 220 CB PRO C 220 CG -0.049
REMARK 500 PRO D 122 CB PRO D 122 CG -0.049
REMARK 500 PRO D 367 CB PRO D 367 CG -0.056
REMARK 500 PRO D 477 CB PRO D 477 CG -0.051
REMARK 500 PRO D 589 CB PRO D 589 CG -0.071
REMARK 500 PRO E 552 CB PRO E 552 CG -0.060
REMARK 500 PRO E 567 CB PRO E 567 CG -0.056
REMARK 500 PRO F 104 CB PRO F 104 CG -0.050
REMARK 500 PRO F 230 CB PRO F 230 CG -0.058
REMARK 500 PRO G 166 CB PRO G 166 CG -0.048
REMARK 500 PRO G 508 CB PRO G 508 CG -0.051
REMARK 500 PRO G 559 CB PRO G 559 CG -0.059
REMARK 500 PRO G 589 CB PRO G 589 CG -0.075
REMARK 500 PRO H 435 CB PRO H 435 CG -0.052
REMARK 500 PRO I 132 CB PRO I 132 CG -0.058
REMARK 500 PRO I 193 CB PRO I 193 CG -0.057
REMARK 500 PRO I 220 CB PRO I 220 CG -0.051
REMARK 500 PRO I 382 CB PRO I 382 CG -0.051
REMARK 500 PRO I 400 CB PRO I 400 CG -0.049
REMARK 500 PRO I 484 CB PRO I 484 CG -0.054
REMARK 500 PRO J 83 CB PRO J 83 CG -0.052
REMARK 500 PRO J 193 CB PRO J 193 CG -0.052
REMARK 500 PRO J 589 CB PRO J 589 CG -0.050
REMARK 500 PRO K 306 CB PRO K 306 CG -0.048
REMARK 500 PRO K 663 CB PRO K 663 CG 0.068
REMARK 500 PRO L 111 CB PRO L 111 CG -0.061
REMARK 500 PRO L 166 CB PRO L 166 CG -0.053
REMARK 500 PRO L 367 CB PRO L 367 CG -0.054
REMARK 500 THR L 389 CB THR L 389 CG2 -0.054
REMARK 500 PRO L 477 CB PRO L 477 CG -0.049
REMARK 500 PRO L 495 CB PRO L 495 CG 0.048
REMARK 500 PRO L 628 CB PRO L 628 CG -0.065
REMARK 500 PRO M 367 CB PRO M 367 CG -0.061
REMARK 500 SER M 440 C ASN M 441 N 0.050
REMARK 500 ASN M 441 C CYS M 442 N -0.130
REMARK 500 ALA N 181 CA ALA N 181 CB -0.056
REMARK 500 PRO O 329 CB PRO O 329 CG -0.053
REMARK 500 LEU O 446 CG LEU O 446 CD1 -0.048
REMARK 500 PRO O 528 CB PRO O 528 CG -0.050
REMARK 500 PRO O 589 CB PRO O 589 CG -0.065
REMARK 500 ILE O 616 CB ILE O 616 CG2 -0.049
REMARK 500 PRO P 169 CB PRO P 169 CG -0.058
REMARK 500 PRO P 329 CB PRO P 329 CG -0.066
REMARK 500 VAL P 527 CB VAL P 527 CG2 -0.051
REMARK 500 PRO P 622 CB PRO P 622 CG -0.053
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 121 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 GLY A 344 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 ILE A 419 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 ASN A 603 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 ASN A 627 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 VAL B 121 N - CA - C ANGL. DEV. =-13.0 DEGREES
REMARK 500 ASP B 239 N - CA - C ANGL. DEV. = 11.4 DEGREES
REMARK 500 VAL B 517 CB - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 ASP B 531 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 ASN B 603 N - CA - C ANGL. DEV. =-12.7 DEGREES
REMARK 500 ILE B 612 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 LYS B 630 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 GLY C 344 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 LEU C 449 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 ASN C 603 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 PHE C 606 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 LYS C 630 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 VAL D 121 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 ILE D 144 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 ASP D 239 N - CA - C ANGL. DEV. = 10.9 DEGREES
REMARK 500 GLY D 344 N - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 VAL D 517 CB - CA - C ANGL. DEV. = 11.7 DEGREES
REMARK 500 ASN D 603 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 ASN D 627 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 LYS D 630 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 VAL E 121 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 ASP E 239 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 GLY E 344 N - CA - C ANGL. DEV. = 13.3 DEGREES
REMARK 500 VAL E 517 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 ASN E 603 N - CA - C ANGL. DEV. =-12.3 DEGREES
REMARK 500 ILE E 612 N - CA - C ANGL. DEV. =-11.8 DEGREES
REMARK 500 ASN E 627 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 LYS E 630 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 VAL F 121 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 LYS F 325 CD - CE - NZ ANGL. DEV. = 12.0 DEGREES
REMARK 500 GLY F 344 N - CA - C ANGL. DEV. = 11.4 DEGREES
REMARK 500 ILE F 419 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 ASN F 603 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 ASN F 627 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 LYS F 630 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 VAL G 121 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 ILE G 144 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ASP G 239 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 GLY G 344 N - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 LEU G 449 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 VAL G 517 CB - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 ASP G 531 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 PHE G 533 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 ASN G 603 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 PHE G 606 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 ILE G 612 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 VAL H 121 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 ASP H 239 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 GLY H 344 N - CA - C ANGL. DEV. = 13.4 DEGREES
REMARK 500 LEU H 449 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 ASP H 531 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 ASN H 603 N - CA - C ANGL. DEV. =-11.9 DEGREES
REMARK 500 LYS H 630 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ILE H 660 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 VAL I 121 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 ASP I 239 N - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 GLY I 344 N - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 VAL I 517 CB - CA - C ANGL. DEV. = 10.6 DEGREES
REMARK 500 ASN I 603 N - CA - C ANGL. DEV. =-12.3 DEGREES
REMARK 500 PHE I 606 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 LYS I 630 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 ILE I 660 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 ASP J 239 N - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 GLY J 344 N - CA - C ANGL. DEV. = 13.8 DEGREES
REMARK 500 GLY J 381 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 ASN J 603 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 PHE J 606 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 ILE J 612 N - CA - C ANGL. DEV. =-12.7 DEGREES
REMARK 500 LYS J 630 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 VAL K 121 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 GLY K 344 N - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 LEU K 449 N - CA - C ANGL. DEV. =-13.1 DEGREES
REMARK 500 ASP K 531 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 ASN K 603 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 VAL L 121 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 ILE L 419 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 LEU L 449 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 VAL L 517 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 ASN L 603 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 PHE L 606 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 ILE L 612 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 TRP L 620 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 LYS L 630 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 ILE L 660 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 VAL M 121 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 ASP M 239 N - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 GLY M 344 N - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 ILE M 419 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 LEU M 449 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 ASP M 531 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 ASN M 603 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 PHE M 606 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 ILE M 612 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 ASN M 627 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 VAL N 121 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 GLY N 344 N - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 GLY N 575 N - CA - C ANGL. DEV. = 10.7 DEGREES
REMARK 500 PHE N 606 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 ILE N 612 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 GLU O 79 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 VAL O 121 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 ASP O 239 N - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 GLY O 344 N - CA - C ANGL. DEV. = 10.7 DEGREES
REMARK 500 ASP O 531 N - CA - C ANGL. DEV. =-13.9 DEGREES
REMARK 500 ASN O 603 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 PHE O 606 N - CA - C ANGL. DEV. =-12.3 DEGREES
REMARK 500 ILE O 612 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 VAL P 121 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 ASP P 239 N - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 ASN P 603 N - CA - C ANGL. DEV. =-13.9 DEGREES
REMARK 500 ILE P 612 N - CA - C ANGL. DEV. =-11.9 DEGREES
REMARK 500 LYS P 630 N - CA - C ANGL. DEV. =-10.9 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 TYR A 154 -105.67 43.87
REMARK 500 SER A 205 -119.96 60.79
REMARK 500 TYR B 154 -107.71 48.01
REMARK 500 SER B 205 -117.47 60.77
REMARK 500 TYR C 154 -106.57 47.47
REMARK 500 SER C 205 -117.06 65.23
REMARK 500 TYR D 154 -111.25 49.26
REMARK 500 TYR E 154 -110.74 50.85
REMARK 500 TYR F 154 -112.16 46.27
REMARK 500 SER F 205 -117.62 61.99
REMARK 500 TYR G 154 -111.51 49.24
REMARK 500 SER G 205 -116.63 63.44
REMARK 500 TYR H 154 -112.31 41.71
REMARK 500 SER H 205 -119.11 63.67
REMARK 500 TYR I 154 -114.70 44.37
REMARK 500 TYR J 154 -111.47 51.90
REMARK 500 SER J 205 -117.93 58.47
REMARK 500 TYR K 154 -110.54 46.51
REMARK 500 SER K 205 -116.95 64.91
REMARK 500 TYR L 154 -104.89 49.21
REMARK 500 TYR M 154 -111.90 48.05
REMARK 500 TYR N 154 -108.13 41.82
REMARK 500 SER N 205 -118.78 61.99
REMARK 500 TYR O 154 -108.13 44.72
REMARK 500 SER O 205 -118.30 53.79
REMARK 500 TYR P 154 -111.77 45.91
REMARK 500 SER P 205 -115.46 59.22
DBREF 2B9V A 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V B 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V C 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V D 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V E 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V F 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V G 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V H 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V I 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V J 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V K 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V L 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V M 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V N 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V O 41 667 GB 18139885 AAL60195 41 667
DBREF 2B9V P 41 667 GB 18139885 AAL60195 41 667
SEQADV 2B9V LYS A 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU A 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY A 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO A 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU A 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN A 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS A 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU A 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE A 676 GB 18139885 MYC TAG
SEQADV 2B9V SER A 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU A 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU A 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP A 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU A 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN A 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER A 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA A 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL A 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP A 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS A 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS A 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS A 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS A 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS A 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS A 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS B 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU B 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY B 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO B 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU B 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN B 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS B 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU B 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE B 676 GB 18139885 MYC TAG
SEQADV 2B9V SER B 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU B 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU B 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP B 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU B 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN B 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER B 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA B 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL B 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP B 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS B 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS B 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS B 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS B 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS B 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS B 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS C 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU C 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY C 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO C 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU C 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN C 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS C 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU C 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE C 676 GB 18139885 MYC TAG
SEQADV 2B9V SER C 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU C 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU C 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP C 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU C 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN C 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER C 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA C 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL C 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP C 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS C 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS C 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS C 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS C 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS C 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS C 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS D 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU D 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY D 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO D 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU D 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN D 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS D 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU D 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE D 676 GB 18139885 MYC TAG
SEQADV 2B9V SER D 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU D 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU D 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP D 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU D 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN D 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER D 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA D 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL D 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP D 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS D 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS D 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS D 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS D 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS D 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS D 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS E 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU E 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY E 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO E 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU E 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN E 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS E 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU E 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE E 676 GB 18139885 MYC TAG
SEQADV 2B9V SER E 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU E 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU E 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP E 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU E 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN E 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER E 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA E 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL E 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP E 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS E 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS E 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS E 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS E 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS E 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS E 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS F 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU F 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY F 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO F 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU F 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN F 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS F 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU F 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE F 676 GB 18139885 MYC TAG
SEQADV 2B9V SER F 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU F 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU F 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP F 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU F 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN F 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER F 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA F 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL F 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP F 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS F 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS F 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS F 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS F 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS F 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS F 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS G 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU G 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY G 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO G 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU G 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN G 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS G 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU G 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE G 676 GB 18139885 MYC TAG
SEQADV 2B9V SER G 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU G 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU G 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP G 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU G 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN G 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER G 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA G 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL G 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP G 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS G 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS G 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS G 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS G 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS G 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS G 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS H 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU H 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY H 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO H 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU H 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN H 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS H 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU H 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE H 676 GB 18139885 MYC TAG
SEQADV 2B9V SER H 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU H 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU H 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP H 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU H 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN H 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER H 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA H 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL H 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP H 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS H 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS H 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS H 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS H 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS H 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS H 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS I 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU I 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY I 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO I 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU I 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN I 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS I 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU I 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE I 676 GB 18139885 MYC TAG
SEQADV 2B9V SER I 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU I 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU I 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP I 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU I 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN I 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER I 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA I 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL I 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP I 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS I 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS I 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS I 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS I 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS I 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS I 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS J 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU J 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY J 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO J 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU J 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN J 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS J 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU J 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE J 676 GB 18139885 MYC TAG
SEQADV 2B9V SER J 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU J 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU J 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP J 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU J 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN J 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER J 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA J 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL J 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP J 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS J 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS J 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS J 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS J 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS J 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS J 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS K 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU K 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY K 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO K 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU K 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN K 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS K 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU K 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE K 676 GB 18139885 MYC TAG
SEQADV 2B9V SER K 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU K 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU K 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP K 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU K 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN K 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER K 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA K 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL K 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP K 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS K 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS K 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS K 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS K 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS K 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS K 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS L 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU L 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY L 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO L 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU L 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN L 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS L 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU L 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE L 676 GB 18139885 MYC TAG
SEQADV 2B9V SER L 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU L 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU L 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP L 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU L 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN L 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER L 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA L 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL L 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP L 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS L 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS L 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS L 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS L 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS L 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS L 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS M 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU M 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY M 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO M 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU M 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN M 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS M 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU M 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE M 676 GB 18139885 MYC TAG
SEQADV 2B9V SER M 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU M 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU M 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP M 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU M 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN M 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER M 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA M 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL M 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP M 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS M 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS M 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS M 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS M 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS M 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS M 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS N 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU N 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY N 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO N 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU N 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN N 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS N 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU N 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE N 676 GB 18139885 MYC TAG
SEQADV 2B9V SER N 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU N 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU N 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP N 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU N 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN N 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER N 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA N 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL N 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP N 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS N 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS N 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS N 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS N 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS N 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS N 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS O 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU O 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY O 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO O 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU O 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN O 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS O 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU O 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE O 676 GB 18139885 MYC TAG
SEQADV 2B9V SER O 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU O 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU O 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP O 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU O 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN O 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER O 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA O 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL O 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP O 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS O 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS O 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS O 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS O 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS O 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS O 692 GB 18139885 HIS TAG
SEQADV 2B9V LYS P 668 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V LEU P 669 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLY P 670 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V PRO P 671 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V GLU P 672 GB 18139885 MYC TAG
SEQADV 2B9V GLN P 673 GB 18139885 MYC TAG
SEQADV 2B9V LYS P 674 GB 18139885 MYC TAG
SEQADV 2B9V LEU P 675 GB 18139885 MYC TAG
SEQADV 2B9V ILE P 676 GB 18139885 MYC TAG
SEQADV 2B9V SER P 677 GB 18139885 MYC TAG
SEQADV 2B9V GLU P 678 GB 18139885 MYC TAG
SEQADV 2B9V GLU P 679 GB 18139885 MYC TAG
SEQADV 2B9V ASP P 680 GB 18139885 MYC TAG
SEQADV 2B9V LEU P 681 GB 18139885 MYC TAG
SEQADV 2B9V ASN P 682 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V SER P 683 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ALA P 684 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V VAL P 685 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V ASP P 686 GB 18139885 CLONING ARTIFACT
SEQADV 2B9V HIS P 687 GB 18139885 HIS TAG
SEQADV 2B9V HIS P 688 GB 18139885 HIS TAG
SEQADV 2B9V HIS P 689 GB 18139885 HIS TAG
SEQADV 2B9V HIS P 690 GB 18139885 HIS TAG
SEQADV 2B9V HIS P 691 GB 18139885 HIS TAG
SEQADV 2B9V HIS P 692 GB 18139885 HIS TAG
SEQRES 1 A 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 A 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 A 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 A 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 A 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 A 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 A 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 A 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 A 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 A 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 A 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 A 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 A 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 A 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 A 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 A 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 A 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 A 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 A 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 A 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 A 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 A 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 A 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 A 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 A 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 A 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 A 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 A 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 A 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 A 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 A 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 A 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 A 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 A 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 A 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 A 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 A 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 A 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 A 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 A 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 A 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 A 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 A 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 A 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 A 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 A 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 A 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 A 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 A 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 A 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 A 652 HIS HIS
SEQRES 1 B 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 B 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 B 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 B 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 B 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 B 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 B 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 B 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 B 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 B 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 B 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 B 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 B 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 B 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 B 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 B 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 B 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 B 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 B 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 B 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 B 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 B 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 B 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 B 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 B 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 B 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 B 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 B 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 B 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 B 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 B 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 B 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 B 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 B 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 B 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 B 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 B 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 B 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 B 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 B 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 B 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 B 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 B 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 B 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 B 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 B 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 B 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 B 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 B 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 B 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 B 652 HIS HIS
SEQRES 1 C 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 C 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 C 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 C 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 C 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 C 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 C 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 C 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 C 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 C 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 C 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 C 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 C 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 C 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 C 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 C 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 C 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 C 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 C 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 C 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 C 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 C 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 C 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 C 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 C 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 C 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 C 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 C 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 C 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 C 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 C 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 C 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 C 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 C 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 C 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 C 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 C 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 C 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 C 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 C 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 C 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 C 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 C 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 C 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 C 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 C 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 C 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 C 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 C 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 C 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 C 652 HIS HIS
SEQRES 1 D 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 D 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 D 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 D 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 D 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 D 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 D 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 D 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 D 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 D 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 D 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 D 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 D 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 D 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 D 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 D 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 D 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 D 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 D 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 D 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 D 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 D 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 D 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 D 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 D 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 D 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 D 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 D 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 D 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 D 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 D 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 D 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 D 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 D 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 D 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 D 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 D 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 D 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 D 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 D 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 D 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 D 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 D 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 D 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 D 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 D 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 D 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 D 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 D 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 D 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 D 652 HIS HIS
SEQRES 1 E 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 E 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 E 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 E 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 E 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 E 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 E 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 E 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 E 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 E 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 E 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 E 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 E 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 E 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 E 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 E 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 E 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 E 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 E 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 E 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 E 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 E 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 E 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 E 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 E 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 E 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 E 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 E 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 E 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 E 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 E 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 E 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 E 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 E 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 E 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 E 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 E 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 E 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 E 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 E 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 E 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 E 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 E 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 E 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 E 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 E 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 E 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 E 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 E 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 E 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 E 652 HIS HIS
SEQRES 1 F 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 F 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 F 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 F 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 F 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 F 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 F 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 F 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 F 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 F 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 F 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 F 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 F 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 F 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 F 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 F 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 F 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 F 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 F 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 F 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 F 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 F 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 F 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 F 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 F 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 F 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 F 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 F 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 F 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 F 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 F 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 F 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 F 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 F 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 F 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 F 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 F 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 F 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 F 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 F 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 F 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 F 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 F 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 F 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 F 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 F 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 F 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 F 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 F 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 F 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 F 652 HIS HIS
SEQRES 1 G 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 G 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 G 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 G 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 G 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 G 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 G 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 G 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 G 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 G 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 G 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 G 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 G 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 G 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 G 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 G 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 G 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 G 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 G 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 G 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 G 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 G 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 G 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 G 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 G 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 G 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 G 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 G 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 G 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 G 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 G 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 G 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 G 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 G 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 G 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 G 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 G 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 G 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 G 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 G 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 G 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 G 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 G 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 G 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 G 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 G 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 G 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 G 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 G 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 G 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 G 652 HIS HIS
SEQRES 1 H 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 H 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 H 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 H 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 H 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 H 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 H 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 H 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 H 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 H 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 H 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 H 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 H 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 H 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 H 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 H 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 H 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 H 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 H 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 H 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 H 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 H 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 H 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 H 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 H 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 H 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 H 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 H 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 H 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 H 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 H 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 H 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 H 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 H 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 H 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 H 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 H 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 H 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 H 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 H 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 H 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 H 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 H 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 H 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 H 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 H 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 H 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 H 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 H 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 H 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 H 652 HIS HIS
SEQRES 1 I 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 I 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 I 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 I 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 I 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 I 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 I 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 I 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 I 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 I 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 I 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 I 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 I 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 I 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 I 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 I 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 I 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 I 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 I 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 I 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 I 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 I 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 I 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 I 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 I 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 I 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 I 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 I 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 I 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 I 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 I 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 I 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 I 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 I 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 I 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 I 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 I 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 I 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 I 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 I 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 I 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 I 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 I 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 I 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 I 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 I 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 I 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 I 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 I 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 I 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 I 652 HIS HIS
SEQRES 1 J 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 J 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 J 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 J 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 J 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 J 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 J 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 J 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 J 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 J 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 J 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 J 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 J 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 J 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 J 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 J 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 J 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 J 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 J 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 J 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 J 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 J 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 J 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 J 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 J 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 J 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 J 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 J 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 J 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 J 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 J 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 J 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 J 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 J 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 J 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 J 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 J 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 J 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 J 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 J 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 J 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 J 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 J 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 J 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 J 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 J 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 J 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 J 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 J 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 J 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 J 652 HIS HIS
SEQRES 1 K 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 K 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 K 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 K 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 K 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 K 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 K 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 K 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 K 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 K 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 K 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 K 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 K 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 K 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 K 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 K 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 K 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 K 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 K 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 K 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 K 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 K 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 K 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 K 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 K 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 K 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 K 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 K 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 K 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 K 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 K 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 K 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 K 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 K 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 K 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 K 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 K 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 K 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 K 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 K 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 K 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 K 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 K 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 K 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 K 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 K 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 K 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 K 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 K 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 K 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 K 652 HIS HIS
SEQRES 1 L 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 L 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 L 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 L 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 L 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 L 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 L 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 L 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 L 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 L 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 L 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 L 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 L 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 L 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 L 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 L 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 L 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 L 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 L 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 L 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 L 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 L 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 L 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 L 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 L 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 L 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 L 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 L 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 L 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 L 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 L 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 L 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 L 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 L 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 L 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 L 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 L 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 L 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 L 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 L 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 L 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 L 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 L 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 L 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 L 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 L 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 L 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 L 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 L 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 L 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 L 652 HIS HIS
SEQRES 1 M 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 M 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 M 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 M 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 M 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 M 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 M 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 M 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 M 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 M 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 M 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 M 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 M 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 M 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 M 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 M 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 M 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 M 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 M 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 M 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 M 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 M 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 M 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 M 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 M 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 M 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 M 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 M 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 M 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 M 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 M 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 M 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 M 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 M 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 M 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 M 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 M 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 M 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 M 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 M 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 M 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 M 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 M 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 M 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 M 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 M 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 M 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 M 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 M 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 M 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 M 652 HIS HIS
SEQRES 1 N 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 N 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 N 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 N 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 N 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 N 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 N 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 N 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 N 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 N 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 N 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 N 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 N 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 N 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 N 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 N 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 N 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 N 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 N 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 N 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 N 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 N 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 N 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 N 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 N 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 N 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 N 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 N 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 N 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 N 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 N 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 N 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 N 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 N 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 N 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 N 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 N 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 N 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 N 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 N 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 N 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 N 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 N 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 N 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 N 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 N 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 N 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 N 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 N 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 N 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 N 652 HIS HIS
SEQRES 1 O 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 O 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 O 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 O 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 O 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 O 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 O 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 O 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 O 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 O 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 O 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 O 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 O 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 O 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 O 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 O 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 O 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 O 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 O 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 O 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 O 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 O 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 O 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 O 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 O 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 O 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 O 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 O 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 O 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 O 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 O 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 O 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 O 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 O 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 O 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 O 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 O 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 O 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 O 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 O 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 O 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 O 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 O 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 O 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 O 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 O 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 O 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 O 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 O 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 O 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 O 652 HIS HIS
SEQRES 1 P 652 ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU
SEQRES 2 P 652 SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS
SEQRES 3 P 652 MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU
SEQRES 4 P 652 VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR
SEQRES 5 P 652 VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE
SEQRES 6 P 652 LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA
SEQRES 7 P 652 ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU
SEQRES 8 P 652 PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE
SEQRES 9 P 652 ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN
SEQRES 10 P 652 GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU
SEQRES 11 P 652 ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP
SEQRES 12 P 652 THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN
SEQRES 13 P 652 GLY ARG VAL GLY MET THR GLY SER SER TYR GLU GLY PHE
SEQRES 14 P 652 THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU
SEQRES 15 P 652 LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP
SEQRES 16 P 652 MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN
SEQRES 17 P 652 GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG
SEQRES 18 P 652 GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP
SEQRES 19 P 652 TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE
SEQRES 20 P 652 ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN
SEQRES 21 P 652 ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN
SEQRES 22 P 652 GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO
SEQRES 23 P 652 THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN
SEQRES 24 P 652 GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU
SEQRES 25 P 652 LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET
SEQRES 26 P 652 GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER
SEQRES 27 P 652 THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS
SEQRES 28 P 652 GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU
SEQRES 29 P 652 TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP
SEQRES 30 P 652 ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR
SEQRES 31 P 652 TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR
SEQRES 32 P 652 GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY
SEQRES 33 P 652 LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER
SEQRES 34 P 652 TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER
SEQRES 35 P 652 ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO
SEQRES 36 P 652 TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO
SEQRES 37 P 652 ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO
SEQRES 38 P 652 VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA
SEQRES 39 P 652 ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU
SEQRES 40 P 652 ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS
SEQRES 41 P 652 MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE
SEQRES 42 P 652 ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA
SEQRES 43 P 652 LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU
SEQRES 44 P 652 PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE
SEQRES 45 P 652 MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP
SEQRES 46 P 652 ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA
SEQRES 47 P 652 LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS
SEQRES 48 P 652 HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL
SEQRES 49 P 652 VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER
SEQRES 50 P 652 GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS
SEQRES 51 P 652 HIS HIS
FORMUL 17 HOH *3654(H2 O1)
HELIX 1 1 ASN A 113 ALA A 118 1 6
HELIX 2 2 THR A 126 LEU A 131 1 6
HELIX 3 3 PRO A 132 GLY A 134 5 3
HELIX 4 4 ASP A 135 GLY A 141 1 7
HELIX 5 5 ASP A 176 ASN A 191 1 16
HELIX 6 6 TYR A 206 LEU A 216 1 11
HELIX 7 7 GLY A 249 THR A 259 1 11
HELIX 8 8 ASP A 273 GLY A 282 1 10
HELIX 9 9 SER A 283 ALA A 291 1 9
HELIX 10 10 GLY A 292 GLN A 295 5 4
HELIX 11 11 TYR A 296 HIS A 305 1 10
HELIX 12 12 ASP A 309 GLY A 314 1 6
HELIX 13 13 ALA A 316 LYS A 325 1 10
HELIX 14 14 TRP A 343 ALA A 355 1 13
HELIX 15 15 SER A 371 TYR A 375 5 5
HELIX 16 16 ASP A 388 VAL A 397 1 10
HELIX 17 17 VAL A 397 LYS A 407 1 11
HELIX 18 18 ASP A 453 HIS A 455 5 3
HELIX 19 19 GLN A 489 LYS A 494 1 6
HELIX 20 20 PRO A 495 GLN A 499 5 5
HELIX 21 21 GLN A 501 SER A 506 1 6
HELIX 22 22 ASP A 558 GLY A 562 5 5
HELIX 23 23 ARG A 576 ARG A 578 5 3
HELIX 24 24 ASN A 634 ALA A 638 5 5
HELIX 25 25 LYS A 639 TYR A 643 5 5
HELIX 26 26 GLY A 653 ALA A 657 5 5
HELIX 27 27 ASN B 113 ALA B 118 1 6
HELIX 28 28 THR B 126 LEU B 131 1 6
HELIX 29 29 PRO B 132 GLY B 134 5 3
HELIX 30 30 ASP B 135 GLY B 141 1 7
HELIX 31 31 ASP B 176 VAL B 192 1 17
HELIX 32 32 TYR B 206 LEU B 216 1 11
HELIX 33 33 GLY B 249 THR B 259 1 11
HELIX 34 34 ASP B 273 GLY B 282 1 10
HELIX 35 35 SER B 283 ALA B 291 1 9
HELIX 36 36 GLY B 292 GLN B 295 5 4
HELIX 37 37 TYR B 296 ALA B 304 1 9
HELIX 38 38 ASP B 309 GLY B 314 1 6
HELIX 39 39 ALA B 316 LYS B 325 1 10
HELIX 40 40 TRP B 343 ALA B 355 1 13
HELIX 41 41 SER B 371 TYR B 375 5 5
HELIX 42 42 ASP B 388 VAL B 397 1 10
HELIX 43 43 VAL B 397 LYS B 407 1 11
HELIX 44 44 ASP B 453 HIS B 455 5 3
HELIX 45 45 GLN B 489 LYS B 494 1 6
HELIX 46 46 PRO B 495 GLN B 499 5 5
HELIX 47 47 GLN B 501 SER B 506 1 6
HELIX 48 48 ASP B 558 GLY B 562 5 5
HELIX 49 49 ARG B 576 ARG B 578 5 3
HELIX 50 50 ASN B 634 ALA B 638 5 5
HELIX 51 51 LYS B 639 TYR B 643 5 5
HELIX 52 52 GLY B 653 ALA B 657 5 5
HELIX 53 53 ASN C 113 ALA C 118 1 6
HELIX 54 54 THR C 126 LEU C 131 1 6
HELIX 55 55 PRO C 132 GLY C 134 5 3
HELIX 56 56 ASP C 135 GLY C 142 1 8
HELIX 57 57 ASP C 176 VAL C 192 1 17
HELIX 58 58 TYR C 206 LEU C 215 1 10
HELIX 59 59 GLY C 249 THR C 259 1 11
HELIX 60 60 ASP C 273 GLY C 282 1 10
HELIX 61 61 SER C 283 ALA C 291 1 9
HELIX 62 62 GLY C 292 GLN C 295 5 4
HELIX 63 63 TYR C 296 HIS C 305 1 10
HELIX 64 64 ASP C 309 GLY C 314 1 6
HELIX 65 65 ALA C 316 LYS C 325 1 10
HELIX 66 66 TRP C 343 ALA C 355 1 13
HELIX 67 67 SER C 371 TYR C 375 5 5
HELIX 68 68 ASP C 388 VAL C 397 1 10
HELIX 69 69 VAL C 397 LYS C 407 1 11
HELIX 70 70 GLN C 489 LYS C 494 1 6
HELIX 71 71 PRO C 495 GLN C 499 5 5
HELIX 72 72 GLN C 501 SER C 506 1 6
HELIX 73 73 ASP C 558 GLY C 562 5 5
HELIX 74 74 ARG C 576 ARG C 578 5 3
HELIX 75 75 ASN C 634 ALA C 638 5 5
HELIX 76 76 LYS C 639 TYR C 643 5 5
HELIX 77 77 GLY C 653 ALA C 657 5 5
HELIX 78 78 ASN D 113 ALA D 118 1 6
HELIX 79 79 THR D 126 LEU D 131 1 6
HELIX 80 80 PRO D 132 GLY D 134 5 3
HELIX 81 81 ASP D 135 GLY D 142 1 8
HELIX 82 82 ASP D 176 VAL D 192 1 17
HELIX 83 83 SER D 205 LEU D 216 1 12
HELIX 84 84 GLY D 249 THR D 259 1 11
HELIX 85 85 ASP D 273 GLY D 282 1 10
HELIX 86 86 SER D 283 ALA D 291 1 9
HELIX 87 87 GLY D 292 GLN D 295 5 4
HELIX 88 88 TYR D 296 HIS D 305 1 10
HELIX 89 89 ASP D 309 GLY D 314 1 6
HELIX 90 90 ALA D 316 LYS D 325 1 10
HELIX 91 91 TRP D 343 ALA D 355 1 13
HELIX 92 92 SER D 371 TYR D 375 5 5
HELIX 93 93 ASP D 388 VAL D 397 1 10
HELIX 94 94 VAL D 397 LYS D 407 1 11
HELIX 95 95 ASP D 453 HIS D 455 5 3
HELIX 96 96 GLN D 489 LYS D 494 1 6
HELIX 97 97 PRO D 495 GLN D 499 5 5
HELIX 98 98 GLN D 501 SER D 506 1 6
HELIX 99 99 ASP D 558 GLY D 562 5 5
HELIX 100 100 ARG D 576 ARG D 578 5 3
HELIX 101 101 ASN D 634 ALA D 638 5 5
HELIX 102 102 LYS D 639 TYR D 643 5 5
HELIX 103 103 GLY D 653 ALA D 657 5 5
HELIX 104 104 ASN E 113 ALA E 118 1 6
HELIX 105 105 THR E 126 LEU E 131 1 6
HELIX 106 106 PRO E 132 GLY E 134 5 3
HELIX 107 107 ASP E 135 GLY E 141 1 7
HELIX 108 108 ASP E 176 VAL E 192 1 17
HELIX 109 109 SER E 205 LEU E 216 1 12
HELIX 110 110 GLY E 249 THR E 259 1 11
HELIX 111 111 ASP E 273 GLY E 282 1 10
HELIX 112 112 SER E 283 ALA E 291 1 9
HELIX 113 113 GLY E 292 GLN E 295 5 4
HELIX 114 114 TYR E 296 HIS E 305 1 10
HELIX 115 115 ASP E 309 GLY E 314 1 6
HELIX 116 116 ALA E 316 LYS E 325 1 10
HELIX 117 117 TRP E 343 ALA E 355 1 13
HELIX 118 118 SER E 371 TYR E 375 5 5
HELIX 119 119 ASP E 388 VAL E 397 1 10
HELIX 120 120 VAL E 397 LYS E 407 1 11
HELIX 121 121 ASP E 453 HIS E 455 5 3
HELIX 122 122 GLN E 489 LYS E 494 1 6
HELIX 123 123 PRO E 495 GLN E 499 5 5
HELIX 124 124 GLN E 501 SER E 506 1 6
HELIX 125 125 ASP E 558 GLY E 562 5 5
HELIX 126 126 ARG E 576 ARG E 578 5 3
HELIX 127 127 ASN E 634 ALA E 638 5 5
HELIX 128 128 LYS E 639 TYR E 643 5 5
HELIX 129 129 GLY E 653 ALA E 657 5 5
HELIX 130 130 ASN F 113 ALA F 118 1 6
HELIX 131 131 THR F 126 LEU F 131 1 6
HELIX 132 132 PRO F 132 GLY F 134 5 3
HELIX 133 133 ASP F 135 GLY F 141 1 7
HELIX 134 134 ASP F 176 VAL F 192 1 17
HELIX 135 135 TYR F 206 LEU F 215 1 10
HELIX 136 136 GLY F 249 THR F 259 1 11
HELIX 137 137 ASP F 273 GLY F 282 1 10
HELIX 138 138 SER F 283 ALA F 291 1 9
HELIX 139 139 GLY F 292 GLN F 295 5 4
HELIX 140 140 TYR F 296 HIS F 305 1 10
HELIX 141 141 ASP F 309 GLY F 314 1 6
HELIX 142 142 ALA F 316 LYS F 325 1 10
HELIX 143 143 TRP F 343 ALA F 355 1 13
HELIX 144 144 SER F 371 TYR F 375 5 5
HELIX 145 145 ASP F 388 VAL F 397 1 10
HELIX 146 146 VAL F 397 LYS F 407 1 11
HELIX 147 147 GLN F 489 LYS F 494 1 6
HELIX 148 148 PRO F 495 GLN F 499 5 5
HELIX 149 149 GLN F 501 SER F 506 1 6
HELIX 150 150 ASP F 558 GLY F 562 5 5
HELIX 151 151 ARG F 576 ARG F 578 5 3
HELIX 152 152 ASN F 634 ALA F 638 5 5
HELIX 153 153 LYS F 639 TYR F 643 5 5
HELIX 154 154 GLY F 653 ALA F 657 5 5
HELIX 155 155 ASN G 113 ALA G 118 1 6
HELIX 156 156 THR G 126 LEU G 131 1 6
HELIX 157 157 PRO G 132 GLY G 134 5 3
HELIX 158 158 ASP G 135 GLY G 141 1 7
HELIX 159 159 ASP G 176 VAL G 192 1 17
HELIX 160 160 TYR G 206 LEU G 216 1 11
HELIX 161 161 GLY G 249 THR G 259 1 11
HELIX 162 162 ASP G 273 GLY G 282 1 10
HELIX 163 163 SER G 283 GLY G 292 1 10
HELIX 164 164 LEU G 293 GLN G 295 5 3
HELIX 165 165 TYR G 296 HIS G 305 1 10
HELIX 166 166 ASP G 309 GLY G 314 1 6
HELIX 167 167 ALA G 316 LYS G 325 1 10
HELIX 168 168 TRP G 343 ALA G 355 1 13
HELIX 169 169 SER G 371 TYR G 375 5 5
HELIX 170 170 ASP G 388 VAL G 397 1 10
HELIX 171 171 VAL G 397 LYS G 407 1 11
HELIX 172 172 GLN G 489 LYS G 494 1 6
HELIX 173 173 PRO G 495 GLN G 499 5 5
HELIX 174 174 GLN G 501 SER G 506 1 6
HELIX 175 175 ASP G 558 GLY G 562 5 5
HELIX 176 176 ARG G 576 ARG G 578 5 3
HELIX 177 177 ASN G 634 ALA G 638 5 5
HELIX 178 178 LYS G 639 TYR G 643 5 5
HELIX 179 179 GLY G 653 ALA G 657 5 5
HELIX 180 180 ASN H 113 ALA H 118 1 6
HELIX 181 181 THR H 126 LEU H 131 1 6
HELIX 182 182 PRO H 132 GLY H 134 5 3
HELIX 183 183 ASP H 135 GLY H 141 1 7
HELIX 184 184 ASP H 176 VAL H 192 1 17
HELIX 185 185 TYR H 206 LEU H 216 1 11
HELIX 186 186 GLY H 249 THR H 259 1 11
HELIX 187 187 ASP H 273 GLY H 282 1 10
HELIX 188 188 SER H 283 ALA H 291 1 9
HELIX 189 189 GLY H 292 GLN H 295 5 4
HELIX 190 190 TYR H 296 HIS H 305 1 10
HELIX 191 191 ASP H 309 GLY H 314 1 6
HELIX 192 192 ALA H 316 LYS H 325 1 10
HELIX 193 193 TRP H 343 ALA H 355 1 13
HELIX 194 194 SER H 371 TYR H 375 5 5
HELIX 195 195 ASP H 388 VAL H 397 1 10
HELIX 196 196 VAL H 397 LYS H 407 1 11
HELIX 197 197 GLN H 489 LYS H 494 1 6
HELIX 198 198 PRO H 495 GLN H 499 5 5
HELIX 199 199 GLN H 501 SER H 506 1 6
HELIX 200 200 ASP H 558 GLY H 562 5 5
HELIX 201 201 ARG H 576 ARG H 578 5 3
HELIX 202 202 ASN H 634 ALA H 638 5 5
HELIX 203 203 LYS H 639 TYR H 643 5 5
HELIX 204 204 GLY H 653 ALA H 657 5 5
HELIX 205 205 ASN I 113 ALA I 118 1 6
HELIX 206 206 THR I 126 LEU I 131 1 6
HELIX 207 207 PRO I 132 GLY I 134 5 3
HELIX 208 208 ASP I 135 GLY I 141 1 7
HELIX 209 209 ASP I 176 VAL I 192 1 17
HELIX 210 210 SER I 205 LEU I 215 1 11
HELIX 211 211 GLY I 249 THR I 259 1 11
HELIX 212 212 ASP I 273 GLY I 282 1 10
HELIX 213 213 SER I 283 GLY I 292 1 10
HELIX 214 214 LEU I 293 GLN I 295 5 3
HELIX 215 215 TYR I 296 HIS I 305 1 10
HELIX 216 216 ASP I 309 GLY I 314 1 6
HELIX 217 217 ALA I 316 LYS I 325 1 10
HELIX 218 218 TRP I 343 ALA I 355 1 13
HELIX 219 219 SER I 371 TYR I 375 5 5
HELIX 220 220 ASP I 388 VAL I 397 1 10
HELIX 221 221 VAL I 397 LYS I 407 1 11
HELIX 222 222 GLN I 489 LYS I 494 1 6
HELIX 223 223 PRO I 495 GLN I 499 5 5
HELIX 224 224 GLN I 501 SER I 506 1 6
HELIX 225 225 ASP I 558 GLY I 562 5 5
HELIX 226 226 ARG I 576 ARG I 578 5 3
HELIX 227 227 ASN I 634 ALA I 638 5 5
HELIX 228 228 LYS I 639 TYR I 643 5 5
HELIX 229 229 GLY I 653 ALA I 657 5 5
HELIX 230 230 ASN J 113 ALA J 118 1 6
HELIX 231 231 THR J 126 LEU J 131 1 6
HELIX 232 232 PRO J 132 GLY J 134 5 3
HELIX 233 233 ASP J 135 GLY J 141 1 7
HELIX 234 234 ASP J 176 VAL J 192 1 17
HELIX 235 235 SER J 205 LEU J 216 1 12
HELIX 236 236 GLY J 249 THR J 259 1 11
HELIX 237 237 ASP J 273 GLY J 282 1 10
HELIX 238 238 SER J 283 ALA J 291 1 9
HELIX 239 239 GLY J 292 GLN J 295 5 4
HELIX 240 240 TYR J 296 HIS J 305 1 10
HELIX 241 241 ASP J 309 GLY J 314 1 6
HELIX 242 242 ALA J 316 LYS J 325 1 10
HELIX 243 243 TRP J 343 ALA J 355 1 13
HELIX 244 244 SER J 371 TYR J 375 5 5
HELIX 245 245 ASP J 388 VAL J 397 1 10
HELIX 246 246 VAL J 397 LYS J 407 1 11
HELIX 247 247 GLN J 489 LYS J 494 1 6
HELIX 248 248 PRO J 495 GLN J 499 5 5
HELIX 249 249 GLN J 501 SER J 506 1 6
HELIX 250 250 ASP J 558 GLY J 562 5 5
HELIX 251 251 ARG J 576 ARG J 578 5 3
HELIX 252 252 ASN J 634 ALA J 638 5 5
HELIX 253 253 LYS J 639 TYR J 643 5 5
HELIX 254 254 GLY J 653 ALA J 657 5 5
HELIX 255 255 ASN K 113 ALA K 118 1 6
HELIX 256 256 THR K 126 LEU K 131 1 6
HELIX 257 257 PRO K 132 GLY K 134 5 3
HELIX 258 258 ASP K 135 GLY K 141 1 7
HELIX 259 259 ASP K 176 VAL K 192 1 17
HELIX 260 260 SER K 205 LEU K 215 1 11
HELIX 261 261 GLY K 249 THR K 259 1 11
HELIX 262 262 ASP K 273 GLY K 282 1 10
HELIX 263 263 SER K 283 GLY K 292 1 10
HELIX 264 264 LEU K 293 GLN K 295 5 3
HELIX 265 265 TYR K 296 HIS K 305 1 10
HELIX 266 266 ASP K 309 GLY K 314 1 6
HELIX 267 267 ALA K 316 LYS K 325 1 10
HELIX 268 268 TRP K 343 ALA K 355 1 13
HELIX 269 269 SER K 371 TYR K 375 5 5
HELIX 270 270 ASP K 388 VAL K 397 1 10
HELIX 271 271 VAL K 397 LYS K 407 1 11
HELIX 272 272 ASP K 453 HIS K 455 5 3
HELIX 273 273 GLN K 489 LYS K 494 1 6
HELIX 274 274 PRO K 495 GLN K 499 5 5
HELIX 275 275 GLN K 501 SER K 506 1 6
HELIX 276 276 ASP K 558 GLY K 562 5 5
HELIX 277 277 ARG K 576 ARG K 578 5 3
HELIX 278 278 ASN K 634 ALA K 638 5 5
HELIX 279 279 LYS K 639 TYR K 643 5 5
HELIX 280 280 GLY K 653 ALA K 657 5 5
HELIX 281 281 ASN L 113 ALA L 118 1 6
HELIX 282 282 THR L 126 LEU L 131 1 6
HELIX 283 283 PRO L 132 GLY L 134 5 3
HELIX 284 284 ASP L 135 GLU L 140 1 6
HELIX 285 285 ASP L 176 VAL L 192 1 17
HELIX 286 286 SER L 205 LEU L 216 1 12
HELIX 287 287 GLY L 249 THR L 259 1 11
HELIX 288 288 ASP L 273 GLY L 282 1 10
HELIX 289 289 SER L 283 GLY L 292 1 10
HELIX 290 290 LEU L 293 GLN L 295 5 3
HELIX 291 291 TYR L 296 HIS L 305 1 10
HELIX 292 292 ASP L 309 GLY L 314 1 6
HELIX 293 293 ALA L 316 LYS L 325 1 10
HELIX 294 294 TRP L 343 ALA L 355 1 13
HELIX 295 295 SER L 371 TYR L 375 5 5
HELIX 296 296 ASP L 388 VAL L 397 1 10
HELIX 297 297 VAL L 397 LYS L 407 1 11
HELIX 298 298 ASP L 453 HIS L 455 5 3
HELIX 299 299 GLN L 489 LYS L 494 1 6
HELIX 300 300 PRO L 495 GLN L 499 5 5
HELIX 301 301 GLN L 501 SER L 506 1 6
HELIX 302 302 ASP L 558 GLY L 562 5 5
HELIX 303 303 ARG L 576 ARG L 578 5 3
HELIX 304 304 ASN L 634 ALA L 638 5 5
HELIX 305 305 LYS L 639 TYR L 643 5 5
HELIX 306 306 GLY L 653 ALA L 657 5 5
HELIX 307 307 ASN M 113 ALA M 118 1 6
HELIX 308 308 THR M 126 LEU M 131 1 6
HELIX 309 309 PRO M 132 GLY M 134 5 3
HELIX 310 310 ASP M 135 GLY M 142 1 8
HELIX 311 311 ASP M 176 VAL M 192 1 17
HELIX 312 312 SER M 205 LEU M 215 1 11
HELIX 313 313 GLY M 249 THR M 259 1 11
HELIX 314 314 ASP M 273 GLY M 282 1 10
HELIX 315 315 SER M 283 ALA M 291 1 9
HELIX 316 316 GLY M 292 GLN M 295 5 4
HELIX 317 317 TYR M 296 HIS M 305 1 10
HELIX 318 318 ASP M 309 GLY M 314 1 6
HELIX 319 319 ALA M 316 LYS M 325 1 10
HELIX 320 320 TRP M 343 ALA M 355 1 13
HELIX 321 321 SER M 371 TYR M 375 5 5
HELIX 322 322 ASP M 388 VAL M 397 1 10
HELIX 323 323 VAL M 397 LYS M 407 1 11
HELIX 324 324 ASP M 453 HIS M 455 5 3
HELIX 325 325 GLN M 489 LYS M 494 1 6
HELIX 326 326 PRO M 495 GLN M 499 5 5
HELIX 327 327 GLN M 501 SER M 506 1 6
HELIX 328 328 ASP M 558 GLY M 562 5 5
HELIX 329 329 ARG M 576 ARG M 578 5 3
HELIX 330 330 ASN M 634 ALA M 638 5 5
HELIX 331 331 LYS M 639 TYR M 643 5 5
HELIX 332 332 GLY M 653 ALA M 657 5 5
HELIX 333 333 ASN N 113 ALA N 118 1 6
HELIX 334 334 THR N 126 LEU N 131 1 6
HELIX 335 335 PRO N 132 GLY N 134 5 3
HELIX 336 336 ASP N 135 GLY N 141 1 7
HELIX 337 337 ASP N 176 VAL N 192 1 17
HELIX 338 338 TYR N 206 LEU N 215 1 10
HELIX 339 339 GLY N 249 THR N 259 1 11
HELIX 340 340 ASP N 273 GLY N 282 1 10
HELIX 341 341 SER N 283 ALA N 291 1 9
HELIX 342 342 GLY N 292 GLN N 295 5 4
HELIX 343 343 TYR N 296 HIS N 305 1 10
HELIX 344 344 ASP N 309 GLY N 314 1 6
HELIX 345 345 ALA N 316 LYS N 325 1 10
HELIX 346 346 TRP N 343 ALA N 355 1 13
HELIX 347 347 SER N 371 TYR N 375 5 5
HELIX 348 348 ASP N 388 VAL N 397 1 10
HELIX 349 349 VAL N 397 LYS N 407 1 11
HELIX 350 350 ASP N 453 HIS N 455 5 3
HELIX 351 351 GLN N 489 LYS N 494 1 6
HELIX 352 352 PRO N 495 GLN N 499 5 5
HELIX 353 353 GLN N 501 SER N 506 1 6
HELIX 354 354 ASP N 558 GLY N 562 5 5
HELIX 355 355 ARG N 576 ARG N 578 5 3
HELIX 356 356 ASN N 634 ALA N 638 5 5
HELIX 357 357 LYS N 639 TYR N 643 5 5
HELIX 358 358 GLY N 653 ALA N 657 5 5
HELIX 359 359 ASN O 113 ALA O 118 1 6
HELIX 360 360 THR O 126 LEU O 131 1 6
HELIX 361 361 PRO O 132 GLY O 134 5 3
HELIX 362 362 ASP O 135 GLY O 141 1 7
HELIX 363 363 ASP O 176 VAL O 192 1 17
HELIX 364 364 TYR O 206 LEU O 216 1 11
HELIX 365 365 GLY O 249 THR O 259 1 11
HELIX 366 366 ASP O 273 GLY O 282 1 10
HELIX 367 367 SER O 283 ALA O 291 1 9
HELIX 368 368 GLY O 292 GLN O 295 5 4
HELIX 369 369 TYR O 296 HIS O 305 1 10
HELIX 370 370 ASP O 309 GLY O 314 1 6
HELIX 371 371 ALA O 316 LYS O 325 1 10
HELIX 372 372 TRP O 343 ALA O 355 1 13
HELIX 373 373 SER O 371 TYR O 375 5 5
HELIX 374 374 ASP O 388 VAL O 397 1 10
HELIX 375 375 VAL O 397 LYS O 407 1 11
HELIX 376 376 GLN O 489 LYS O 494 1 6
HELIX 377 377 PRO O 495 GLN O 499 5 5
HELIX 378 378 GLN O 501 SER O 506 1 6
HELIX 379 379 ASP O 558 GLY O 562 5 5
HELIX 380 380 ARG O 576 ARG O 578 5 3
HELIX 381 381 ASN O 634 ALA O 638 5 5
HELIX 382 382 LYS O 639 TYR O 643 5 5
HELIX 383 383 GLY O 653 ALA O 657 5 5
HELIX 384 384 ASN P 113 ALA P 118 1 6
HELIX 385 385 THR P 126 LEU P 131 1 6
HELIX 386 386 PRO P 132 GLY P 134 5 3
HELIX 387 387 ASP P 135 GLY P 141 1 7
HELIX 388 388 ASP P 176 ASN P 191 1 16
HELIX 389 389 TYR P 206 LEU P 215 1 10
HELIX 390 390 GLY P 249 THR P 259 1 11
HELIX 391 391 ASP P 273 GLY P 282 1 10
HELIX 392 392 SER P 283 ALA P 291 1 9
HELIX 393 393 GLY P 292 GLN P 295 5 4
HELIX 394 394 TYR P 296 HIS P 305 1 10
HELIX 395 395 ASP P 309 GLY P 314 1 6
HELIX 396 396 ALA P 316 LYS P 325 1 10
HELIX 397 397 TRP P 343 ALA P 355 1 13
HELIX 398 398 SER P 371 TYR P 375 5 5
HELIX 399 399 ASP P 388 VAL P 397 1 10
HELIX 400 400 VAL P 397 LYS P 407 1 11
HELIX 401 401 GLN P 489 LYS P 494 1 6
HELIX 402 402 PRO P 495 GLN P 499 5 5
HELIX 403 403 GLN P 501 SER P 506 1 6
HELIX 404 404 ASP P 558 GLY P 562 5 5
HELIX 405 405 ARG P 576 ARG P 578 5 3
HELIX 406 406 ASN P 634 ALA P 638 5 5
HELIX 407 407 LYS P 639 TYR P 643 5 5
HELIX 408 408 GLY P 653 ALA P 657 5 5
SHEET 1 A 6 TYR A 75 PRO A 83 0
SHEET 2 A 6 LYS A 89 PRO A 97 -1 O THR A 92 N VAL A 80
SHEET 3 A 6 ILE A 144 ASP A 149 -1 O ARG A 145 N VAL A 95
SHEET 4 A 6 ALA A 103 THR A 110 1 N THR A 110 O GLN A 148
SHEET 5 A 6 SER A 195 SER A 205 1 O GLY A 200 N LEU A 107
SHEET 6 A 6 LEU A 222 PRO A 230 1 O GLU A 228 N GLY A 203
SHEET 1 B 2 PHE A 241 HIS A 242 0
SHEET 2 B 2 ALA A 245 PHE A 246 -1 O ALA A 245 N HIS A 242
SHEET 1 C 4 MET A 330 GLY A 335 0
SHEET 2 C 4 ASN A 361 GLY A 366 1 O THR A 362 N TRP A 332
SHEET 3 C 4 ALA A 418 ASN A 422 1 O TYR A 421 N MET A 365
SHEET 4 C 4 LYS A 427 TYR A 431 -1 O LYS A 427 N ASN A 422
SHEET 1 D 2 THR A 379 LEU A 380 0
SHEET 2 D 2 LEU A 383 GLU A 384 -1 O LEU A 383 N LEU A 380
SHEET 1 E 6 GLY A 456 SER A 458 0
SHEET 2 E 6 THR A 447 ALA A 452 -1 N ALA A 452 O GLY A 456
SHEET 3 E 6 SER A 659 LEU A 662 -1 O LEU A 662 N THR A 447
SHEET 4 E 6 VAL A 529 THR A 536 -1 N VAL A 529 O LEU A 661
SHEET 5 E 6 ALA A 646 HIS A 652 -1 O SER A 649 N ALA A 535
SHEET 6 E 6 GLY A 466 SER A 472 -1 N TYR A 470 O GLN A 648
SHEET 1 F 5 GLY A 456 SER A 458 0
SHEET 2 F 5 THR A 447 ALA A 452 -1 N ALA A 452 O GLY A 456
SHEET 3 F 5 SER A 659 LEU A 662 -1 O LEU A 662 N THR A 447
SHEET 4 F 5 VAL A 529 THR A 536 -1 N VAL A 529 O LEU A 661
SHEET 5 F 5 LEU A 593 THR A 598 -1 O TYR A 595 N LEU A 532
SHEET 1 G 4 VAL A 510 GLU A 514 0
SHEET 2 G 4 ARG A 611 GLN A 617 -1 O VAL A 614 N TYR A 513
SHEET 3 G 4 ASP A 542 VAL A 550 -1 N ILE A 548 O MET A 613
SHEET 4 G 4 GLU A 565 ARG A 574 -1 O SER A 569 N LEU A 547
SHEET 1 H 3 VAL A 602 PHE A 606 0
SHEET 2 H 3 VAL A 522 GLY A 526 -1 N VAL A 524 O HIS A 604
SHEET 3 H 3 VAL A 664 VAL A 665 -1 O VAL A 665 N ARG A 523
SHEET 1 I 6 TYR B 75 PRO B 83 0
SHEET 2 I 6 LYS B 89 PRO B 97 -1 O THR B 92 N VAL B 80
SHEET 3 I 6 ILE B 144 ASP B 149 -1 O ARG B 145 N VAL B 95
SHEET 4 I 6 ALA B 103 THR B 110 1 N PRO B 104 O ILE B 144
SHEET 5 I 6 SER B 195 SER B 205 1 O GLY B 200 N LEU B 107
SHEET 6 I 6 LEU B 222 PRO B 230 1 O GLU B 228 N GLY B 203
SHEET 1 J 2 PHE B 241 HIS B 242 0
SHEET 2 J 2 ALA B 245 PHE B 246 -1 O ALA B 245 N HIS B 242
SHEET 1 K 4 MET B 330 GLY B 335 0
SHEET 2 K 4 ASN B 361 GLY B 366 1 O THR B 362 N TRP B 332
SHEET 3 K 4 ALA B 418 ASN B 422 1 O ILE B 419 N LEU B 363
SHEET 4 K 4 LYS B 427 TYR B 431 -1 O TYR B 431 N ALA B 418
SHEET 1 L 2 THR B 379 LEU B 380 0
SHEET 2 L 2 LEU B 383 GLU B 384 -1 O LEU B 383 N LEU B 380
SHEET 1 M 6 GLY B 456 SER B 458 0
SHEET 2 M 6 THR B 447 ALA B 452 -1 N TYR B 450 O SER B 458
SHEET 3 M 6 SER B 659 LEU B 662 -1 O LEU B 662 N THR B 447
SHEET 4 M 6 VAL B 529 THR B 536 -1 N VAL B 529 O LEU B 661
SHEET 5 M 6 ALA B 646 HIS B 652 -1 O SER B 649 N ALA B 535
SHEET 6 M 6 GLY B 466 SER B 472 -1 N SER B 472 O ALA B 646
SHEET 1 N 5 GLY B 456 SER B 458 0
SHEET 2 N 5 THR B 447 ALA B 452 -1 N TYR B 450 O SER B 458
SHEET 3 N 5 SER B 659 LEU B 662 -1 O LEU B 662 N THR B 447
SHEET 4 N 5 VAL B 529 THR B 536 -1 N VAL B 529 O LEU B 661
SHEET 5 N 5 LEU B 593 THR B 598 -1 O TYR B 595 N LEU B 532
SHEET 1 O 4 VAL B 510 GLU B 514 0
SHEET 2 O 4 ARG B 611 GLN B 617 -1 O VAL B 614 N TYR B 513
SHEET 3 O 4 ASP B 542 VAL B 550 -1 N VAL B 544 O GLN B 617
SHEET 4 O 4 GLU B 565 ARG B 574 -1 O SER B 569 N LEU B 547
SHEET 1 P 3 VAL B 602 PHE B 606 0
SHEET 2 P 3 VAL B 522 GLY B 526 -1 N VAL B 524 O HIS B 604
SHEET 3 P 3 VAL B 664 VAL B 665 -1 O VAL B 665 N ARG B 523
SHEET 1 Q 6 TYR C 75 PRO C 83 0
SHEET 2 Q 6 LYS C 89 PRO C 97 -1 O ILE C 94 N ARG C 78
SHEET 3 Q 6 ILE C 144 ASP C 149 -1 O ARG C 145 N VAL C 95
SHEET 4 Q 6 ALA C 103 THR C 110 1 N PRO C 104 O ILE C 144
SHEET 5 Q 6 SER C 195 SER C 205 1 O GLY C 200 N LEU C 107
SHEET 6 Q 6 LEU C 222 PRO C 230 1 O GLU C 228 N GLY C 203
SHEET 1 R 2 PHE C 241 HIS C 242 0
SHEET 2 R 2 ALA C 245 PHE C 246 -1 O ALA C 245 N HIS C 242
SHEET 1 S 4 MET C 330 GLY C 335 0
SHEET 2 S 4 ASN C 361 GLY C 366 1 O THR C 362 N TRP C 332
SHEET 3 S 4 ALA C 418 ASN C 422 1 O ILE C 419 N LEU C 363
SHEET 4 S 4 LYS C 427 TYR C 431 -1 O TYR C 431 N ALA C 418
SHEET 1 T 2 THR C 379 LEU C 380 0
SHEET 2 T 2 LEU C 383 GLU C 384 -1 O LEU C 383 N LEU C 380
SHEET 1 U 6 GLY C 456 SER C 458 0
SHEET 2 U 6 THR C 447 ALA C 452 -1 N ALA C 452 O GLY C 456
SHEET 3 U 6 SER C 659 LEU C 662 -1 O LEU C 662 N THR C 447
SHEET 4 U 6 VAL C 529 THR C 536 -1 N VAL C 529 O LEU C 661
SHEET 5 U 6 ALA C 646 HIS C 652 -1 O SER C 649 N ALA C 535
SHEET 6 U 6 GLY C 466 SER C 472 -1 N TYR C 470 O GLN C 648
SHEET 1 V 5 GLY C 456 SER C 458 0
SHEET 2 V 5 THR C 447 ALA C 452 -1 N ALA C 452 O GLY C 456
SHEET 3 V 5 SER C 659 LEU C 662 -1 O LEU C 662 N THR C 447
SHEET 4 V 5 VAL C 529 THR C 536 -1 N VAL C 529 O LEU C 661
SHEET 5 V 5 LEU C 593 THR C 598 -1 O TYR C 595 N LEU C 532
SHEET 1 W 4 VAL C 510 GLU C 514 0
SHEET 2 W 4 ARG C 611 GLN C 617 -1 O VAL C 614 N TYR C 513
SHEET 3 W 4 ASP C 542 VAL C 550 -1 N VAL C 544 O GLN C 617
SHEET 4 W 4 GLU C 565 ARG C 574 -1 O SER C 569 N LEU C 547
SHEET 1 X 3 VAL C 602 PHE C 606 0
SHEET 2 X 3 VAL C 522 GLY C 526 -1 N VAL C 524 O HIS C 604
SHEET 3 X 3 VAL C 664 VAL C 665 -1 O VAL C 665 N ARG C 523
SHEET 1 Y 6 TYR D 75 PRO D 83 0
SHEET 2 Y 6 LYS D 89 PRO D 97 -1 O THR D 92 N VAL D 80
SHEET 3 Y 6 ILE D 144 ASP D 149 -1 O ARG D 145 N VAL D 95
SHEET 4 Y 6 ALA D 103 THR D 110 1 N THR D 110 O GLN D 148
SHEET 5 Y 6 SER D 195 SER D 204 1 O GLY D 200 N LEU D 107
SHEET 6 Y 6 LEU D 222 GLU D 228 1 O GLU D 228 N GLY D 203
SHEET 1 Z 2 PHE D 241 HIS D 242 0
SHEET 2 Z 2 ALA D 245 PHE D 246 -1 O ALA D 245 N HIS D 242
SHEET 1 AA 4 MET D 330 GLY D 335 0
SHEET 2 AA 4 ASN D 361 GLY D 366 1 O VAL D 364 N TRP D 332
SHEET 3 AA 4 ALA D 418 ASN D 422 1 O TYR D 421 N MET D 365
SHEET 4 AA 4 LYS D 427 TYR D 431 -1 O LYS D 427 N ASN D 422
SHEET 1 AB 2 THR D 379 LEU D 380 0
SHEET 2 AB 2 LEU D 383 GLU D 384 -1 O LEU D 383 N LEU D 380
SHEET 1 AC 6 GLY D 456 SER D 458 0
SHEET 2 AC 6 THR D 447 ALA D 452 -1 N TYR D 450 O SER D 458
SHEET 3 AC 6 SER D 659 LEU D 662 -1 O LEU D 662 N THR D 447
SHEET 4 AC 6 VAL D 529 THR D 536 -1 N VAL D 529 O LEU D 661
SHEET 5 AC 6 ALA D 646 HIS D 652 -1 O SER D 649 N ALA D 535
SHEET 6 AC 6 GLY D 466 SER D 472 -1 N TYR D 470 O GLN D 648
SHEET 1 AD 5 GLY D 456 SER D 458 0
SHEET 2 AD 5 THR D 447 ALA D 452 -1 N TYR D 450 O SER D 458
SHEET 3 AD 5 SER D 659 LEU D 662 -1 O LEU D 662 N THR D 447
SHEET 4 AD 5 VAL D 529 THR D 536 -1 N VAL D 529 O LEU D 661
SHEET 5 AD 5 LEU D 593 THR D 598 -1 O TYR D 595 N LEU D 532
SHEET 1 AE 4 VAL D 510 GLU D 514 0
SHEET 2 AE 4 ARG D 611 GLN D 617 -1 O VAL D 614 N TYR D 513
SHEET 3 AE 4 ASP D 542 VAL D 550 -1 N ILE D 548 O MET D 613
SHEET 4 AE 4 GLU D 565 ARG D 574 -1 O LEU D 566 N ASP D 549
SHEET 1 AF 3 VAL D 602 PHE D 606 0
SHEET 2 AF 3 VAL D 522 GLY D 526 -1 N VAL D 522 O PHE D 606
SHEET 3 AF 3 VAL D 664 VAL D 665 -1 O VAL D 665 N ARG D 523
SHEET 1 AG 6 TYR E 75 PRO E 83 0
SHEET 2 AG 6 LYS E 89 PRO E 97 -1 O ILE E 94 N ARG E 78
SHEET 3 AG 6 ILE E 144 ASP E 149 -1 O ARG E 145 N VAL E 95
SHEET 4 AG 6 ALA E 103 THR E 110 1 N THR E 110 O GLN E 148
SHEET 5 AG 6 SER E 195 SER E 204 1 O GLY E 200 N LEU E 107
SHEET 6 AG 6 LEU E 222 GLU E 228 1 O GLU E 228 N GLY E 203
SHEET 1 AH 2 PHE E 241 HIS E 242 0
SHEET 2 AH 2 ALA E 245 PHE E 246 -1 O ALA E 245 N HIS E 242
SHEET 1 AI 4 MET E 330 GLY E 335 0
SHEET 2 AI 4 ASN E 361 GLY E 366 1 O THR E 362 N TRP E 332
SHEET 3 AI 4 ALA E 418 ASN E 422 1 O TYR E 421 N MET E 365
SHEET 4 AI 4 LYS E 427 TYR E 431 -1 O TYR E 431 N ALA E 418
SHEET 1 AJ 2 THR E 379 LEU E 380 0
SHEET 2 AJ 2 LEU E 383 GLU E 384 -1 O LEU E 383 N LEU E 380
SHEET 1 AK 6 GLY E 456 SER E 458 0
SHEET 2 AK 6 THR E 447 ALA E 452 -1 N ALA E 452 O GLY E 456
SHEET 3 AK 6 SER E 659 LEU E 662 -1 O LEU E 662 N THR E 447
SHEET 4 AK 6 VAL E 529 THR E 536 -1 N VAL E 529 O LEU E 661
SHEET 5 AK 6 ALA E 646 HIS E 652 -1 O SER E 649 N ALA E 535
SHEET 6 AK 6 GLY E 466 SER E 472 -1 N TYR E 470 O GLN E 648
SHEET 1 AL 5 GLY E 456 SER E 458 0
SHEET 2 AL 5 THR E 447 ALA E 452 -1 N ALA E 452 O GLY E 456
SHEET 3 AL 5 SER E 659 LEU E 662 -1 O LEU E 662 N THR E 447
SHEET 4 AL 5 VAL E 529 THR E 536 -1 N VAL E 529 O LEU E 661
SHEET 5 AL 5 LEU E 593 THR E 598 -1 O TYR E 595 N LEU E 532
SHEET 1 AM 4 VAL E 510 GLU E 514 0
SHEET 2 AM 4 ARG E 611 GLN E 617 -1 O VAL E 614 N TYR E 513
SHEET 3 AM 4 ASP E 542 VAL E 550 -1 N ILE E 548 O MET E 613
SHEET 4 AM 4 GLU E 565 ARG E 574 -1 O SER E 569 N LEU E 547
SHEET 1 AN 3 VAL E 602 PHE E 606 0
SHEET 2 AN 3 VAL E 522 GLY E 526 -1 N VAL E 522 O PHE E 606
SHEET 3 AN 3 VAL E 664 VAL E 665 -1 O VAL E 665 N ARG E 523
SHEET 1 AO 6 TYR F 75 PRO F 83 0
SHEET 2 AO 6 LYS F 89 PRO F 97 -1 O ILE F 94 N ARG F 78
SHEET 3 AO 6 ILE F 144 ASP F 149 -1 O ARG F 145 N VAL F 95
SHEET 4 AO 6 ALA F 103 THR F 110 1 N PRO F 104 O ILE F 144
SHEET 5 AO 6 SER F 195 SER F 205 1 O GLY F 200 N LEU F 107
SHEET 6 AO 6 LEU F 222 PRO F 230 1 O GLU F 228 N GLY F 203
SHEET 1 AP 2 PHE F 241 HIS F 242 0
SHEET 2 AP 2 ALA F 245 PHE F 246 -1 O ALA F 245 N HIS F 242
SHEET 1 AQ 4 MET F 330 GLY F 335 0
SHEET 2 AQ 4 ASN F 361 GLY F 366 1 O THR F 362 N TRP F 332
SHEET 3 AQ 4 ALA F 418 ASN F 422 1 O ILE F 419 N LEU F 363
SHEET 4 AQ 4 LYS F 427 TYR F 431 -1 O LYS F 427 N ASN F 422
SHEET 1 AR 2 THR F 379 LEU F 380 0
SHEET 2 AR 2 LEU F 383 GLU F 384 -1 O LEU F 383 N LEU F 380
SHEET 1 AS 6 GLY F 456 SER F 458 0
SHEET 2 AS 6 THR F 447 ALA F 452 -1 N ALA F 452 O GLY F 456
SHEET 3 AS 6 SER F 659 LEU F 662 -1 O LEU F 662 N THR F 447
SHEET 4 AS 6 VAL F 529 THR F 536 -1 N VAL F 529 O LEU F 661
SHEET 5 AS 6 ALA F 646 HIS F 652 -1 O HIS F 651 N PHE F 533
SHEET 6 AS 6 GLY F 466 SER F 472 -1 N TYR F 470 O GLN F 648
SHEET 1 AT 5 GLY F 456 SER F 458 0
SHEET 2 AT 5 THR F 447 ALA F 452 -1 N ALA F 452 O GLY F 456
SHEET 3 AT 5 SER F 659 LEU F 662 -1 O LEU F 662 N THR F 447
SHEET 4 AT 5 VAL F 529 THR F 536 -1 N VAL F 529 O LEU F 661
SHEET 5 AT 5 LEU F 593 THR F 598 -1 O TYR F 595 N LEU F 532
SHEET 1 AU 4 VAL F 510 GLU F 514 0
SHEET 2 AU 4 ARG F 611 GLN F 617 -1 O VAL F 614 N TYR F 513
SHEET 3 AU 4 ASP F 542 VAL F 550 -1 N VAL F 544 O GLN F 617
SHEET 4 AU 4 GLU F 565 ARG F 574 -1 O SER F 569 N LEU F 547
SHEET 1 AV 3 VAL F 602 PHE F 606 0
SHEET 2 AV 3 VAL F 522 GLY F 526 -1 N VAL F 524 O HIS F 604
SHEET 3 AV 3 VAL F 664 VAL F 665 -1 O VAL F 665 N ARG F 523
SHEET 1 AW 6 TYR G 75 PRO G 83 0
SHEET 2 AW 6 LYS G 89 PRO G 97 -1 O THR G 92 N VAL G 80
SHEET 3 AW 6 ILE G 144 ASP G 149 -1 O ARG G 145 N VAL G 95
SHEET 4 AW 6 ALA G 103 THR G 110 1 N THR G 110 O GLN G 148
SHEET 5 AW 6 SER G 195 SER G 205 1 O GLY G 200 N ILE G 105
SHEET 6 AW 6 LEU G 222 PRO G 230 1 O GLU G 228 N GLY G 203
SHEET 1 AX 2 PHE G 241 HIS G 242 0
SHEET 2 AX 2 ALA G 245 PHE G 246 -1 O ALA G 245 N HIS G 242
SHEET 1 AY 4 MET G 330 GLY G 335 0
SHEET 2 AY 4 ASN G 361 GLY G 366 1 O THR G 362 N TRP G 332
SHEET 3 AY 4 ALA G 418 ASN G 422 1 O TYR G 421 N MET G 365
SHEET 4 AY 4 LYS G 427 TYR G 431 -1 O LYS G 427 N ASN G 422
SHEET 1 AZ 2 THR G 379 LEU G 380 0
SHEET 2 AZ 2 LEU G 383 GLU G 384 -1 O LEU G 383 N LEU G 380
SHEET 1 BA 6 GLY G 456 SER G 458 0
SHEET 2 BA 6 THR G 447 ALA G 452 -1 N TYR G 450 O SER G 458
SHEET 3 BA 6 SER G 659 LEU G 662 -1 O LEU G 662 N THR G 447
SHEET 4 BA 6 VAL G 529 THR G 536 -1 N VAL G 529 O LEU G 661
SHEET 5 BA 6 ALA G 646 HIS G 652 -1 O SER G 649 N ALA G 535
SHEET 6 BA 6 GLY G 466 SER G 472 -1 N SER G 472 O ALA G 646
SHEET 1 BB 5 GLY G 456 SER G 458 0
SHEET 2 BB 5 THR G 447 ALA G 452 -1 N TYR G 450 O SER G 458
SHEET 3 BB 5 SER G 659 LEU G 662 -1 O LEU G 662 N THR G 447
SHEET 4 BB 5 VAL G 529 THR G 536 -1 N VAL G 529 O LEU G 661
SHEET 5 BB 5 LEU G 593 THR G 598 -1 O TYR G 595 N LEU G 532
SHEET 1 BC 4 VAL G 511 GLU G 514 0
SHEET 2 BC 4 ARG G 611 GLN G 617 -1 O VAL G 614 N TYR G 513
SHEET 3 BC 4 ASP G 542 VAL G 550 -1 N ILE G 548 O MET G 613
SHEET 4 BC 4 GLU G 565 ARG G 574 -1 O SER G 569 N LEU G 547
SHEET 1 BD 3 VAL G 602 PHE G 606 0
SHEET 2 BD 3 VAL G 522 GLY G 526 -1 N GLY G 526 O VAL G 602
SHEET 3 BD 3 VAL G 664 VAL G 665 -1 O VAL G 665 N ARG G 523
SHEET 1 BE 6 TYR H 75 PRO H 83 0
SHEET 2 BE 6 LYS H 89 PRO H 97 -1 O ILE H 94 N ARG H 78
SHEET 3 BE 6 ILE H 144 ASP H 149 -1 O ARG H 145 N VAL H 95
SHEET 4 BE 6 ALA H 103 THR H 110 1 N THR H 110 O GLN H 148
SHEET 5 BE 6 SER H 195 SER H 205 1 O GLY H 200 N LEU H 107
SHEET 6 BE 6 LEU H 222 PRO H 230 1 O GLU H 228 N GLY H 203
SHEET 1 BF 2 PHE H 241 HIS H 242 0
SHEET 2 BF 2 ALA H 245 PHE H 246 -1 O ALA H 245 N HIS H 242
SHEET 1 BG 4 MET H 330 GLY H 335 0
SHEET 2 BG 4 ASN H 361 GLY H 366 1 O THR H 362 N TRP H 332
SHEET 3 BG 4 ALA H 418 ASN H 422 1 O TYR H 421 N MET H 365
SHEET 4 BG 4 LYS H 427 TYR H 431 -1 O LYS H 427 N ASN H 422
SHEET 1 BH 2 THR H 379 LEU H 380 0
SHEET 2 BH 2 LEU H 383 GLU H 384 -1 O LEU H 383 N LEU H 380
SHEET 1 BI 6 GLY H 456 SER H 458 0
SHEET 2 BI 6 THR H 447 ALA H 452 -1 N TYR H 450 O SER H 458
SHEET 3 BI 6 SER H 659 LEU H 662 -1 O LEU H 662 N THR H 447
SHEET 4 BI 6 VAL H 529 THR H 536 -1 N VAL H 529 O LEU H 661
SHEET 5 BI 6 ALA H 646 HIS H 652 -1 O SER H 649 N ALA H 535
SHEET 6 BI 6 GLY H 466 SER H 472 -1 N TYR H 470 O GLN H 648
SHEET 1 BJ 5 GLY H 456 SER H 458 0
SHEET 2 BJ 5 THR H 447 ALA H 452 -1 N TYR H 450 O SER H 458
SHEET 3 BJ 5 SER H 659 LEU H 662 -1 O LEU H 662 N THR H 447
SHEET 4 BJ 5 VAL H 529 THR H 536 -1 N VAL H 529 O LEU H 661
SHEET 5 BJ 5 LEU H 593 THR H 598 -1 O TYR H 595 N LEU H 532
SHEET 1 BK 4 VAL H 510 GLU H 514 0
SHEET 2 BK 4 ARG H 611 GLN H 617 -1 O VAL H 614 N TYR H 513
SHEET 3 BK 4 ASP H 542 VAL H 550 -1 N VAL H 544 O GLN H 617
SHEET 4 BK 4 GLU H 565 ARG H 574 -1 O SER H 569 N LEU H 547
SHEET 1 BL 3 VAL H 602 PHE H 606 0
SHEET 2 BL 3 VAL H 522 GLY H 526 -1 N VAL H 524 O HIS H 604
SHEET 3 BL 3 VAL H 664 VAL H 665 -1 O VAL H 665 N ARG H 523
SHEET 1 BM 6 TYR I 75 PRO I 83 0
SHEET 2 BM 6 LYS I 89 PRO I 97 -1 O THR I 92 N VAL I 80
SHEET 3 BM 6 ILE I 144 ASP I 149 -1 O ARG I 145 N VAL I 95
SHEET 4 BM 6 ALA I 103 THR I 110 1 N PRO I 104 O ILE I 144
SHEET 5 BM 6 SER I 195 SER I 204 1 O GLY I 200 N LEU I 107
SHEET 6 BM 6 LEU I 222 GLU I 228 1 O GLU I 228 N GLY I 203
SHEET 1 BN 2 PHE I 241 HIS I 242 0
SHEET 2 BN 2 ALA I 245 PHE I 246 -1 O ALA I 245 N HIS I 242
SHEET 1 BO 4 MET I 330 GLY I 335 0
SHEET 2 BO 4 ASN I 361 GLY I 366 1 O VAL I 364 N TRP I 332
SHEET 3 BO 4 ALA I 418 ASN I 422 1 O ILE I 419 N LEU I 363
SHEET 4 BO 4 LYS I 427 TYR I 431 -1 O TYR I 431 N ALA I 418
SHEET 1 BP 2 THR I 379 LEU I 380 0
SHEET 2 BP 2 LEU I 383 GLU I 384 -1 O LEU I 383 N LEU I 380
SHEET 1 BQ 6 GLY I 456 SER I 458 0
SHEET 2 BQ 6 THR I 447 ALA I 452 -1 N TYR I 450 O SER I 458
SHEET 3 BQ 6 SER I 659 LEU I 662 -1 O LEU I 662 N THR I 447
SHEET 4 BQ 6 VAL I 529 THR I 536 -1 N VAL I 529 O LEU I 661
SHEET 5 BQ 6 ALA I 646 HIS I 652 -1 O HIS I 651 N PHE I 533
SHEET 6 BQ 6 GLY I 466 SER I 472 -1 N TYR I 470 O GLN I 648
SHEET 1 BR 5 GLY I 456 SER I 458 0
SHEET 2 BR 5 THR I 447 ALA I 452 -1 N TYR I 450 O SER I 458
SHEET 3 BR 5 SER I 659 LEU I 662 -1 O LEU I 662 N THR I 447
SHEET 4 BR 5 VAL I 529 THR I 536 -1 N VAL I 529 O LEU I 661
SHEET 5 BR 5 LEU I 593 THR I 598 -1 O TYR I 595 N LEU I 532
SHEET 1 BS 4 VAL I 510 GLU I 514 0
SHEET 2 BS 4 ARG I 611 GLN I 617 -1 O VAL I 614 N TYR I 513
SHEET 3 BS 4 ASP I 542 VAL I 550 -1 N ILE I 548 O MET I 613
SHEET 4 BS 4 GLU I 565 ARG I 574 -1 O LEU I 566 N ASP I 549
SHEET 1 BT 3 VAL I 602 PHE I 606 0
SHEET 2 BT 3 VAL I 522 GLY I 526 -1 N VAL I 524 O HIS I 604
SHEET 3 BT 3 VAL I 664 VAL I 665 -1 O VAL I 665 N ARG I 523
SHEET 1 BU 6 TYR J 75 PRO J 83 0
SHEET 2 BU 6 LYS J 89 PRO J 97 -1 O THR J 92 N VAL J 80
SHEET 3 BU 6 ILE J 144 ASP J 149 -1 O ARG J 145 N VAL J 95
SHEET 4 BU 6 ALA J 103 THR J 110 1 N THR J 110 O GLN J 148
SHEET 5 BU 6 SER J 195 SER J 204 1 O GLY J 200 N LEU J 107
SHEET 6 BU 6 LEU J 222 GLU J 228 1 O GLU J 228 N GLY J 203
SHEET 1 BV 2 PHE J 241 HIS J 242 0
SHEET 2 BV 2 ALA J 245 PHE J 246 -1 O ALA J 245 N HIS J 242
SHEET 1 BW 4 MET J 330 GLY J 335 0
SHEET 2 BW 4 ASN J 361 GLY J 366 1 O THR J 362 N TRP J 332
SHEET 3 BW 4 ALA J 418 ASN J 422 1 O TYR J 421 N MET J 365
SHEET 4 BW 4 LYS J 427 TYR J 431 -1 O LYS J 427 N ASN J 422
SHEET 1 BX 2 THR J 379 LEU J 380 0
SHEET 2 BX 2 LEU J 383 GLU J 384 -1 O LEU J 383 N LEU J 380
SHEET 1 BY 6 GLY J 456 SER J 458 0
SHEET 2 BY 6 THR J 447 ALA J 452 -1 N TYR J 450 O SER J 458
SHEET 3 BY 6 SER J 659 LEU J 662 -1 O LEU J 662 N THR J 447
SHEET 4 BY 6 VAL J 529 THR J 536 -1 N VAL J 529 O LEU J 661
SHEET 5 BY 6 ALA J 646 HIS J 652 -1 O SER J 649 N ALA J 535
SHEET 6 BY 6 GLY J 466 SER J 472 -1 N TYR J 470 O GLN J 648
SHEET 1 BZ 5 GLY J 456 SER J 458 0
SHEET 2 BZ 5 THR J 447 ALA J 452 -1 N TYR J 450 O SER J 458
SHEET 3 BZ 5 SER J 659 LEU J 662 -1 O LEU J 662 N THR J 447
SHEET 4 BZ 5 VAL J 529 THR J 536 -1 N VAL J 529 O LEU J 661
SHEET 5 BZ 5 LEU J 593 THR J 598 -1 O TYR J 595 N LEU J 532
SHEET 1 CA 4 VAL J 510 GLU J 514 0
SHEET 2 CA 4 ARG J 611 GLN J 617 -1 O ILE J 616 N VAL J 511
SHEET 3 CA 4 ASP J 542 VAL J 550 -1 N VAL J 544 O GLN J 617
SHEET 4 CA 4 GLU J 565 ARG J 574 -1 O SER J 569 N LEU J 547
SHEET 1 CB 3 VAL J 602 PHE J 606 0
SHEET 2 CB 3 VAL J 522 GLY J 526 -1 N VAL J 522 O PHE J 606
SHEET 3 CB 3 VAL J 664 VAL J 665 -1 O VAL J 665 N ARG J 523
SHEET 1 CC 6 TYR K 75 PRO K 83 0
SHEET 2 CC 6 LYS K 89 PRO K 97 -1 O ILE K 94 N ARG K 78
SHEET 3 CC 6 ILE K 144 ASP K 149 -1 O ARG K 145 N VAL K 95
SHEET 4 CC 6 ALA K 103 THR K 110 1 N THR K 110 O GLN K 148
SHEET 5 CC 6 SER K 195 SER K 204 1 O GLY K 200 N LEU K 107
SHEET 6 CC 6 LEU K 222 GLU K 228 1 O GLU K 228 N GLY K 203
SHEET 1 CD 2 PHE K 241 HIS K 242 0
SHEET 2 CD 2 ALA K 245 PHE K 246 -1 O ALA K 245 N HIS K 242
SHEET 1 CE 4 MET K 330 GLY K 335 0
SHEET 2 CE 4 ASN K 361 GLY K 366 1 O VAL K 364 N TRP K 332
SHEET 3 CE 4 ALA K 418 ASN K 422 1 O TYR K 421 N MET K 365
SHEET 4 CE 4 LYS K 427 TYR K 431 -1 O TYR K 431 N ALA K 418
SHEET 1 CF 2 THR K 379 LEU K 380 0
SHEET 2 CF 2 LEU K 383 GLU K 384 -1 O LEU K 383 N LEU K 380
SHEET 1 CG 6 GLY K 456 SER K 458 0
SHEET 2 CG 6 THR K 447 ALA K 452 -1 N ALA K 452 O GLY K 456
SHEET 3 CG 6 SER K 659 LEU K 662 -1 O LEU K 662 N THR K 447
SHEET 4 CG 6 VAL K 529 THR K 536 -1 N VAL K 529 O LEU K 661
SHEET 5 CG 6 ALA K 646 HIS K 652 -1 O HIS K 651 N PHE K 533
SHEET 6 CG 6 GLY K 466 SER K 472 -1 N SER K 472 O ALA K 646
SHEET 1 CH 5 GLY K 456 SER K 458 0
SHEET 2 CH 5 THR K 447 ALA K 452 -1 N ALA K 452 O GLY K 456
SHEET 3 CH 5 SER K 659 LEU K 662 -1 O LEU K 662 N THR K 447
SHEET 4 CH 5 VAL K 529 THR K 536 -1 N VAL K 529 O LEU K 661
SHEET 5 CH 5 LEU K 593 THR K 598 -1 O TYR K 595 N LEU K 532
SHEET 1 CI 4 VAL K 510 GLU K 514 0
SHEET 2 CI 4 ARG K 611 GLN K 617 -1 O VAL K 614 N TYR K 513
SHEET 3 CI 4 ASP K 542 VAL K 550 -1 N VAL K 544 O GLN K 617
SHEET 4 CI 4 GLU K 565 ARG K 574 -1 O LEU K 566 N ASP K 549
SHEET 1 CJ 3 VAL K 602 PHE K 606 0
SHEET 2 CJ 3 VAL K 522 GLY K 526 -1 N VAL K 524 O HIS K 604
SHEET 3 CJ 3 VAL K 664 VAL K 665 -1 O VAL K 665 N ARG K 523
SHEET 1 CK 6 TYR L 75 PRO L 83 0
SHEET 2 CK 6 LYS L 89 PRO L 97 -1 O THR L 92 N VAL L 80
SHEET 3 CK 6 ILE L 144 ASP L 149 -1 O PHE L 147 N VAL L 93
SHEET 4 CK 6 ALA L 103 THR L 110 1 N THR L 110 O GLN L 148
SHEET 5 CK 6 SER L 195 SER L 204 1 O GLY L 200 N LEU L 107
SHEET 6 CK 6 LEU L 222 GLU L 228 1 O GLU L 228 N GLY L 203
SHEET 1 CL 2 PHE L 241 HIS L 242 0
SHEET 2 CL 2 ALA L 245 PHE L 246 -1 O ALA L 245 N HIS L 242
SHEET 1 CM 4 MET L 330 GLY L 335 0
SHEET 2 CM 4 ASN L 361 GLY L 366 1 O VAL L 364 N TRP L 332
SHEET 3 CM 4 ALA L 418 ASN L 422 1 O ILE L 419 N LEU L 363
SHEET 4 CM 4 LYS L 427 TYR L 431 -1 O LYS L 427 N ASN L 422
SHEET 1 CN 2 THR L 379 LEU L 380 0
SHEET 2 CN 2 LEU L 383 GLU L 384 -1 O LEU L 383 N LEU L 380
SHEET 1 CO 6 GLY L 456 SER L 458 0
SHEET 2 CO 6 THR L 447 ALA L 452 -1 N ALA L 452 O GLY L 456
SHEET 3 CO 6 SER L 659 LEU L 662 -1 O LEU L 662 N THR L 447
SHEET 4 CO 6 VAL L 529 THR L 536 -1 N VAL L 529 O LEU L 661
SHEET 5 CO 6 ALA L 646 HIS L 652 -1 O SER L 649 N ALA L 535
SHEET 6 CO 6 GLY L 466 SER L 472 -1 N TYR L 470 O GLN L 648
SHEET 1 CP 5 GLY L 456 SER L 458 0
SHEET 2 CP 5 THR L 447 ALA L 452 -1 N ALA L 452 O GLY L 456
SHEET 3 CP 5 SER L 659 LEU L 662 -1 O LEU L 662 N THR L 447
SHEET 4 CP 5 VAL L 529 THR L 536 -1 N VAL L 529 O LEU L 661
SHEET 5 CP 5 LEU L 593 THR L 598 -1 O TYR L 595 N LEU L 532
SHEET 1 CQ 4 VAL L 510 GLU L 514 0
SHEET 2 CQ 4 ARG L 611 GLN L 617 -1 O VAL L 614 N TYR L 513
SHEET 3 CQ 4 ASP L 542 VAL L 550 -1 N VAL L 544 O GLN L 617
SHEET 4 CQ 4 GLU L 565 ARG L 574 -1 O LEU L 566 N ASP L 549
SHEET 1 CR 3 VAL L 602 PHE L 606 0
SHEET 2 CR 3 VAL L 522 GLY L 526 -1 N VAL L 524 O HIS L 604
SHEET 3 CR 3 VAL L 664 VAL L 665 -1 O VAL L 665 N ARG L 523
SHEET 1 CS 6 TYR M 75 PRO M 83 0
SHEET 2 CS 6 LYS M 89 PRO M 97 -1 O THR M 92 N VAL M 80
SHEET 3 CS 6 ILE M 144 ASP M 149 -1 O PHE M 147 N VAL M 93
SHEET 4 CS 6 ALA M 103 THR M 110 1 N THR M 110 O GLN M 148
SHEET 5 CS 6 SER M 195 SER M 204 1 O GLY M 200 N ILE M 105
SHEET 6 CS 6 LEU M 222 GLU M 228 1 O GLU M 228 N GLY M 203
SHEET 1 CT 2 PHE M 241 HIS M 242 0
SHEET 2 CT 2 ALA M 245 PHE M 246 -1 O ALA M 245 N HIS M 242
SHEET 1 CU 4 MET M 330 GLY M 335 0
SHEET 2 CU 4 ASN M 361 GLY M 366 1 O VAL M 364 N TRP M 332
SHEET 3 CU 4 ALA M 418 ASN M 422 1 O ILE M 419 N LEU M 363
SHEET 4 CU 4 LYS M 427 TYR M 431 -1 O TYR M 431 N ALA M 418
SHEET 1 CV 2 THR M 379 LEU M 380 0
SHEET 2 CV 2 LEU M 383 GLU M 384 -1 O LEU M 383 N LEU M 380
SHEET 1 CW 6 LEU M 457 SER M 458 0
SHEET 2 CW 6 THR M 447 LEU M 451 -1 N TYR M 450 O SER M 458
SHEET 3 CW 6 SER M 659 LEU M 662 -1 O LEU M 662 N THR M 447
SHEET 4 CW 6 VAL M 529 THR M 536 -1 N VAL M 529 O LEU M 661
SHEET 5 CW 6 ALA M 646 HIS M 652 -1 O SER M 649 N ALA M 535
SHEET 6 CW 6 GLY M 466 SER M 472 -1 N TYR M 470 O GLN M 648
SHEET 1 CX 5 LEU M 457 SER M 458 0
SHEET 2 CX 5 THR M 447 LEU M 451 -1 N TYR M 450 O SER M 458
SHEET 3 CX 5 SER M 659 LEU M 662 -1 O LEU M 662 N THR M 447
SHEET 4 CX 5 VAL M 529 THR M 536 -1 N VAL M 529 O LEU M 661
SHEET 5 CX 5 LEU M 593 THR M 598 -1 O TYR M 595 N LEU M 532
SHEET 1 CY 4 VAL M 510 GLU M 514 0
SHEET 2 CY 4 ARG M 611 GLN M 617 -1 O VAL M 614 N TYR M 513
SHEET 3 CY 4 ASP M 542 VAL M 550 -1 N VAL M 544 O GLN M 617
SHEET 4 CY 4 GLU M 565 ARG M 574 -1 O SER M 569 N LEU M 547
SHEET 1 CZ 3 VAL M 602 PHE M 606 0
SHEET 2 CZ 3 VAL M 522 GLY M 526 -1 N GLY M 526 O VAL M 602
SHEET 3 CZ 3 VAL M 664 VAL M 665 -1 O VAL M 665 N ARG M 523
SHEET 1 DA 6 TYR N 75 PRO N 83 0
SHEET 2 DA 6 LYS N 89 PRO N 97 -1 O THR N 92 N VAL N 80
SHEET 3 DA 6 ILE N 144 ASP N 149 -1 O ARG N 145 N VAL N 95
SHEET 4 DA 6 ALA N 103 THR N 110 1 N THR N 110 O GLN N 148
SHEET 5 DA 6 SER N 195 SER N 205 1 O GLY N 200 N LEU N 107
SHEET 6 DA 6 LEU N 222 PRO N 230 1 O GLU N 228 N GLY N 203
SHEET 1 DB 2 PHE N 241 HIS N 242 0
SHEET 2 DB 2 ALA N 245 PHE N 246 -1 O ALA N 245 N HIS N 242
SHEET 1 DC 4 MET N 330 GLY N 335 0
SHEET 2 DC 4 ASN N 361 GLY N 366 1 O VAL N 364 N TRP N 332
SHEET 3 DC 4 ALA N 418 ASN N 422 1 O ILE N 419 N LEU N 363
SHEET 4 DC 4 LYS N 427 TYR N 431 -1 O TYR N 431 N ALA N 418
SHEET 1 DD 2 THR N 379 LEU N 380 0
SHEET 2 DD 2 LEU N 383 GLU N 384 -1 O LEU N 383 N LEU N 380
SHEET 1 DE 6 GLY N 456 SER N 458 0
SHEET 2 DE 6 THR N 447 ALA N 452 -1 N TYR N 450 O SER N 458
SHEET 3 DE 6 SER N 659 LEU N 662 -1 O LEU N 662 N THR N 447
SHEET 4 DE 6 VAL N 529 THR N 536 -1 N VAL N 529 O LEU N 661
SHEET 5 DE 6 ALA N 646 HIS N 652 -1 O HIS N 651 N PHE N 533
SHEET 6 DE 6 GLY N 466 SER N 472 -1 N TYR N 470 O GLN N 648
SHEET 1 DF 5 GLY N 456 SER N 458 0
SHEET 2 DF 5 THR N 447 ALA N 452 -1 N TYR N 450 O SER N 458
SHEET 3 DF 5 SER N 659 LEU N 662 -1 O LEU N 662 N THR N 447
SHEET 4 DF 5 VAL N 529 THR N 536 -1 N VAL N 529 O LEU N 661
SHEET 5 DF 5 LEU N 593 THR N 598 -1 O TYR N 595 N LEU N 532
SHEET 1 DG 4 VAL N 510 GLU N 514 0
SHEET 2 DG 4 ARG N 611 GLN N 617 -1 O VAL N 614 N TYR N 513
SHEET 3 DG 4 ASP N 542 VAL N 550 -1 N ILE N 548 O MET N 613
SHEET 4 DG 4 GLU N 565 ARG N 574 -1 O SER N 569 N LEU N 547
SHEET 1 DH 3 VAL N 602 PHE N 606 0
SHEET 2 DH 3 VAL N 522 GLY N 526 -1 N VAL N 524 O HIS N 604
SHEET 3 DH 3 VAL N 664 VAL N 665 -1 O VAL N 665 N ARG N 523
SHEET 1 DI 6 TYR O 75 PRO O 83 0
SHEET 2 DI 6 LYS O 89 PRO O 97 -1 O THR O 92 N VAL O 80
SHEET 3 DI 6 ILE O 144 ASP O 149 -1 O ARG O 145 N VAL O 95
SHEET 4 DI 6 ALA O 103 THR O 110 1 N THR O 110 O GLN O 148
SHEET 5 DI 6 SER O 195 SER O 205 1 O GLY O 200 N LEU O 107
SHEET 6 DI 6 LEU O 222 PRO O 230 1 O GLU O 228 N GLY O 203
SHEET 1 DJ 2 PHE O 241 HIS O 242 0
SHEET 2 DJ 2 ALA O 245 PHE O 246 -1 O ALA O 245 N HIS O 242
SHEET 1 DK 4 MET O 330 GLY O 335 0
SHEET 2 DK 4 ASN O 361 GLY O 366 1 O VAL O 364 N TRP O 332
SHEET 3 DK 4 ALA O 418 ASN O 422 1 O ILE O 419 N LEU O 363
SHEET 4 DK 4 LYS O 427 TYR O 431 -1 O LYS O 427 N ASN O 422
SHEET 1 DL 2 THR O 379 LEU O 380 0
SHEET 2 DL 2 LEU O 383 GLU O 384 -1 O LEU O 383 N LEU O 380
SHEET 1 DM 6 GLY O 456 SER O 458 0
SHEET 2 DM 6 THR O 447 ALA O 452 -1 N TYR O 450 O SER O 458
SHEET 3 DM 6 SER O 659 LEU O 662 -1 O LEU O 662 N THR O 447
SHEET 4 DM 6 VAL O 529 THR O 536 -1 N VAL O 529 O LEU O 661
SHEET 5 DM 6 ALA O 646 HIS O 652 -1 O SER O 649 N ALA O 535
SHEET 6 DM 6 GLY O 466 SER O 472 -1 N TYR O 470 O GLN O 648
SHEET 1 DN 5 GLY O 456 SER O 458 0
SHEET 2 DN 5 THR O 447 ALA O 452 -1 N TYR O 450 O SER O 458
SHEET 3 DN 5 SER O 659 LEU O 662 -1 O LEU O 662 N THR O 447
SHEET 4 DN 5 VAL O 529 THR O 536 -1 N VAL O 529 O LEU O 661
SHEET 5 DN 5 LEU O 593 THR O 598 -1 O TYR O 595 N LEU O 532
SHEET 1 DO 4 VAL O 511 GLU O 514 0
SHEET 2 DO 4 ARG O 611 GLN O 617 -1 O VAL O 614 N TYR O 513
SHEET 3 DO 4 ASP O 542 VAL O 550 -1 N ILE O 548 O MET O 613
SHEET 4 DO 4 GLU O 565 ARG O 574 -1 O SER O 569 N LEU O 547
SHEET 1 DP 3 VAL O 602 PHE O 606 0
SHEET 2 DP 3 VAL O 522 GLY O 526 -1 N GLY O 526 O VAL O 602
SHEET 3 DP 3 VAL O 664 VAL O 665 -1 O VAL O 665 N ARG O 523
SHEET 1 DQ 6 TYR P 75 PRO P 83 0
SHEET 2 DQ 6 LYS P 89 PRO P 97 -1 O ILE P 94 N ARG P 78
SHEET 3 DQ 6 ILE P 144 ASP P 149 -1 O PHE P 147 N VAL P 93
SHEET 4 DQ 6 ALA P 103 THR P 110 1 N THR P 110 O GLN P 148
SHEET 5 DQ 6 SER P 195 SER P 205 1 O GLY P 200 N LEU P 107
SHEET 6 DQ 6 LEU P 222 PRO P 230 1 O GLU P 228 N GLY P 203
SHEET 1 DR 2 PHE P 241 HIS P 242 0
SHEET 2 DR 2 ALA P 245 PHE P 246 -1 O ALA P 245 N HIS P 242
SHEET 1 DS 4 MET P 330 GLY P 335 0
SHEET 2 DS 4 ASN P 361 GLY P 366 1 O THR P 362 N TRP P 332
SHEET 3 DS 4 ALA P 418 ASN P 422 1 O ILE P 419 N LEU P 363
SHEET 4 DS 4 LYS P 427 TYR P 431 -1 O TYR P 431 N ALA P 418
SHEET 1 DT 2 THR P 379 LEU P 380 0
SHEET 2 DT 2 LEU P 383 GLU P 384 -1 O LEU P 383 N LEU P 380
SHEET 1 DU 6 GLY P 456 SER P 458 0
SHEET 2 DU 6 THR P 447 ALA P 452 -1 N TYR P 450 O SER P 458
SHEET 3 DU 6 SER P 659 LEU P 662 -1 O LEU P 662 N THR P 447
SHEET 4 DU 6 VAL P 529 THR P 536 -1 N VAL P 529 O LEU P 661
SHEET 5 DU 6 ALA P 646 HIS P 652 -1 O SER P 649 N ALA P 535
SHEET 6 DU 6 GLY P 466 SER P 472 -1 N TYR P 470 O GLN P 648
SHEET 1 DV 5 GLY P 456 SER P 458 0
SHEET 2 DV 5 THR P 447 ALA P 452 -1 N TYR P 450 O SER P 458
SHEET 3 DV 5 SER P 659 LEU P 662 -1 O LEU P 662 N THR P 447
SHEET 4 DV 5 VAL P 529 THR P 536 -1 N VAL P 529 O LEU P 661
SHEET 5 DV 5 LEU P 593 THR P 598 -1 O TYR P 595 N LEU P 532
SHEET 1 DW 4 VAL P 510 GLU P 514 0
SHEET 2 DW 4 ARG P 611 GLN P 617 -1 O VAL P 614 N TYR P 513
SHEET 3 DW 4 ASP P 542 VAL P 550 -1 N ILE P 548 O MET P 613
SHEET 4 DW 4 GLU P 565 ARG P 574 -1 O SER P 569 N LEU P 547
SHEET 1 DX 3 VAL P 602 PHE P 606 0
SHEET 2 DX 3 VAL P 522 GLY P 526 -1 N VAL P 524 O HIS P 604
SHEET 3 DX 3 VAL P 664 VAL P 665 -1 O VAL P 665 N ARG P 523
SSBOND 1 CYS D 438 CYS D 442
SSBOND 2 CYS I 438 CYS I 442
SSBOND 3 CYS K 438 CYS K 442
SSBOND 4 CYS M 438 CYS M 442
SSBOND 5 CYS N 438 CYS N 442
SSBOND 6 CYS O 438 CYS O 442
SSBOND 7 CYS P 438 CYS P 442
CISPEP 1 TRP A 434 PRO A 435 0 -4.65
CISPEP 2 ARG A 483 PRO A 484 0 -0.52
CISPEP 3 PHE A 621 PRO A 622 0 -1.23
CISPEP 4 TRP B 434 PRO B 435 0 -4.53
CISPEP 5 ARG B 483 PRO B 484 0 -0.55
CISPEP 6 PHE B 621 PRO B 622 0 1.36
CISPEP 7 TRP C 434 PRO C 435 0 -1.25
CISPEP 8 ARG C 483 PRO C 484 0 -2.33
CISPEP 9 PHE C 621 PRO C 622 0 -0.40
CISPEP 10 TRP D 434 PRO D 435 0 -4.28
CISPEP 11 ARG D 483 PRO D 484 0 -0.87
CISPEP 12 PHE D 621 PRO D 622 0 -2.10
CISPEP 13 TRP E 434 PRO E 435 0 -1.98
CISPEP 14 ARG E 483 PRO E 484 0 -2.24
CISPEP 15 PHE E 621 PRO E 622 0 -3.09
CISPEP 16 TRP F 434 PRO F 435 0 -2.94
CISPEP 17 ARG F 483 PRO F 484 0 -2.60
CISPEP 18 PHE F 621 PRO F 622 0 -0.93
CISPEP 19 TRP G 434 PRO G 435 0 -4.54
CISPEP 20 ARG G 483 PRO G 484 0 -0.36
CISPEP 21 PHE G 621 PRO G 622 0 -0.99
CISPEP 22 TRP H 434 PRO H 435 0 -1.05
CISPEP 23 ARG H 483 PRO H 484 0 -1.71
CISPEP 24 PHE H 621 PRO H 622 0 -0.64
CISPEP 25 TRP I 434 PRO I 435 0 -1.82
CISPEP 26 ARG I 483 PRO I 484 0 -4.13
CISPEP 27 PHE I 621 PRO I 622 0 -2.59
CISPEP 28 TRP J 434 PRO J 435 0 -0.30
CISPEP 29 ARG J 483 PRO J 484 0 -0.16
CISPEP 30 PHE J 621 PRO J 622 0 -1.31
CISPEP 31 TRP K 434 PRO K 435 0 -0.33
CISPEP 32 ARG K 483 PRO K 484 0 -2.04
CISPEP 33 PHE K 621 PRO K 622 0 -3.24
CISPEP 34 TRP L 434 PRO L 435 0 -0.89
CISPEP 35 ARG L 483 PRO L 484 0 0.17
CISPEP 36 PHE L 621 PRO L 622 0 0.19
CISPEP 37 TRP M 434 PRO M 435 0 -1.66
CISPEP 38 ARG M 483 PRO M 484 0 -3.01
CISPEP 39 PHE M 621 PRO M 622 0 -2.09
CISPEP 40 TRP N 434 PRO N 435 0 -3.85
CISPEP 41 ARG N 483 PRO N 484 0 -2.16
CISPEP 42 PHE N 621 PRO N 622 0 1.55
CISPEP 43 TRP O 434 PRO O 435 0 -2.28
CISPEP 44 ARG O 483 PRO O 484 0 -1.45
CISPEP 45 PHE O 621 PRO O 622 0 0.36
CISPEP 46 TRP P 434 PRO P 435 0 -1.63
CISPEP 47 ARG P 483 PRO P 484 0 -1.68
CISPEP 48 PHE P 621 PRO P 622 0 1.65
CRYST1 98.369 275.594 197.953 90.00 90.11 90.00 P 1 21 1 32
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 0.010166 0.000000 0.000020 0.00000
SCALE2 0.000000 0.003629 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005052 0.00000
TER 4817 LYS A 666
TER 9634 LYS B 666
TER 14451 LYS C 666
TER 19268 LYS D 666
TER 24085 LYS E 666
TER 28902 LYS F 666
TER 33719 LYS G 666
TER 38536 LYS H 666
TER 43353 LYS I 666
TER 48170 LYS J 666
TER 52987 LYS K 666
TER 57804 LYS L 666
TER 62621 LYS M 666
TER 67438 LYS N 666
TER 72255 LYS O 666
TER 77072 LYS P 666
MASTER 1266 0 0 408 512 0 0 680710 16 14 816
END |