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HEADER HYDROLASE 16-JUL-19 6KHM
TITLE LIPASE (OPEN FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE, ALPHA/BETA DOMAIN PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U,
COMPND 4 V, X, Y, W, Z;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CUTIBACTERIUM ACNES HL110PA4;
SOURCE 3 ORGANISM_TAXID: 765080;
SOURCE 4 GENE: HMPREF9578_02569;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.KIM,A.R.KWON
REVDAT 1 22-JUL-20 6KHM 0
JRNL AUTH H.J.KIM,B.J.LEE,A.R.KWON
JRNL TITL CLOSED, BLOCKED, AND OPEN STATES OF LIPASE FROM TYPE II
JRNL TITL 2 CUTIBACTERIUM ACNES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 294293
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 15636
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 21457
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 1170
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 61283
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 204
REMARK 3 SOLVENT ATOMS : 2515
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.03000
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): 0.583
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.291
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.203
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.903
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 62936 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 56744 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 85463 ; 1.686 ; 1.636
REMARK 3 BOND ANGLES OTHERS (DEGREES):130963 ; 1.343 ; 1.584
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 8028 ; 7.260 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 3494 ;33.081 ;22.015
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 9455 ;16.413 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 457 ;19.603 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 8054 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 72690 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 13745 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6KHM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1300013019.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 310189
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
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: PHASER
REMARK 200 STARTING MODEL: 6KHK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)2SO4, 0.2M MGCL2, AND 0.1M BIS
REMARK 280 -TRIS, PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.36633
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 136.73267
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
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
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N
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
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R
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
REMARK 350 BIOMOLECULE: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T
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
REMARK 350 BIOMOLECULE: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V
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
REMARK 350 BIOMOLECULE: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y
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
REMARK 350 BIOMOLECULE: 13
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, Z
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 312
REMARK 465 ILE A 313
REMARK 465 LYS A 314
REMARK 465 ARG A 315
REMARK 465 SER A 316
REMARK 465 ARG A 317
REMARK 465 MET B 1
REMARK 465 ARG B 311
REMARK 465 ARG B 312
REMARK 465 ILE B 313
REMARK 465 LYS B 314
REMARK 465 ARG B 315
REMARK 465 SER B 316
REMARK 465 ARG B 317
REMARK 465 MET C 1
REMARK 465 ARG C 311
REMARK 465 ARG C 312
REMARK 465 ILE C 313
REMARK 465 LYS C 314
REMARK 465 ARG C 315
REMARK 465 SER C 316
REMARK 465 ARG C 317
REMARK 465 MET D 1
REMARK 465 ASN D 310
REMARK 465 ARG D 311
REMARK 465 ARG D 312
REMARK 465 ILE D 313
REMARK 465 LYS D 314
REMARK 465 ARG D 315
REMARK 465 SER D 316
REMARK 465 ARG D 317
REMARK 465 MET E 1
REMARK 465 ILE E 313
REMARK 465 LYS E 314
REMARK 465 ARG E 315
REMARK 465 SER E 316
REMARK 465 ARG E 317
REMARK 465 MET F 1
REMARK 465 ASN F 310
REMARK 465 ARG F 311
REMARK 465 ARG F 312
REMARK 465 ILE F 313
REMARK 465 LYS F 314
REMARK 465 ARG F 315
REMARK 465 SER F 316
REMARK 465 ARG F 317
REMARK 465 MET G 1
REMARK 465 ARG G 312
REMARK 465 ILE G 313
REMARK 465 LYS G 314
REMARK 465 ARG G 315
REMARK 465 SER G 316
REMARK 465 ARG G 317
REMARK 465 MET H 1
REMARK 465 ARG H 311
REMARK 465 ARG H 312
REMARK 465 ILE H 313
REMARK 465 LYS H 314
REMARK 465 ARG H 315
REMARK 465 SER H 316
REMARK 465 ARG H 317
REMARK 465 MET I 1
REMARK 465 ILE I 313
REMARK 465 LYS I 314
REMARK 465 ARG I 315
REMARK 465 SER I 316
REMARK 465 ARG I 317
REMARK 465 MET J 1
REMARK 465 ARG J 312
REMARK 465 ILE J 313
REMARK 465 LYS J 314
REMARK 465 ARG J 315
REMARK 465 SER J 316
REMARK 465 ARG J 317
REMARK 465 MET K 1
REMARK 465 LYS K 314
REMARK 465 ARG K 315
REMARK 465 SER K 316
REMARK 465 ARG K 317
REMARK 465 MET L 1
REMARK 465 LYS L 314
REMARK 465 ARG L 315
REMARK 465 SER L 316
REMARK 465 ARG L 317
REMARK 465 MET M 1
REMARK 465 ARG M 311
REMARK 465 ARG M 312
REMARK 465 ILE M 313
REMARK 465 LYS M 314
REMARK 465 ARG M 315
REMARK 465 SER M 316
REMARK 465 ARG M 317
REMARK 465 MET N 1
REMARK 465 ARG N 312
REMARK 465 ILE N 313
REMARK 465 LYS N 314
REMARK 465 ARG N 315
REMARK 465 SER N 316
REMARK 465 ARG N 317
REMARK 465 MET O 1
REMARK 465 ARG O 312
REMARK 465 ILE O 313
REMARK 465 LYS O 314
REMARK 465 ARG O 315
REMARK 465 SER O 316
REMARK 465 ARG O 317
REMARK 465 MET P 1
REMARK 465 ARG P 312
REMARK 465 ILE P 313
REMARK 465 LYS P 314
REMARK 465 ARG P 315
REMARK 465 SER P 316
REMARK 465 ARG P 317
REMARK 465 MET Q 1
REMARK 465 ILE Q 313
REMARK 465 LYS Q 314
REMARK 465 ARG Q 315
REMARK 465 SER Q 316
REMARK 465 ARG Q 317
REMARK 465 MET R 1
REMARK 465 ARG R 311
REMARK 465 ARG R 312
REMARK 465 ILE R 313
REMARK 465 LYS R 314
REMARK 465 ARG R 315
REMARK 465 SER R 316
REMARK 465 ARG R 317
REMARK 465 MET S 1
REMARK 465 ARG S 312
REMARK 465 ILE S 313
REMARK 465 LYS S 314
REMARK 465 ARG S 315
REMARK 465 SER S 316
REMARK 465 ARG S 317
REMARK 465 MET T 1
REMARK 465 ARG T 311
REMARK 465 ARG T 312
REMARK 465 ILE T 313
REMARK 465 LYS T 314
REMARK 465 ARG T 315
REMARK 465 SER T 316
REMARK 465 ARG T 317
REMARK 465 MET U 1
REMARK 465 ARG U 312
REMARK 465 ILE U 313
REMARK 465 LYS U 314
REMARK 465 ARG U 315
REMARK 465 SER U 316
REMARK 465 ARG U 317
REMARK 465 MET V 1
REMARK 465 ARG V 311
REMARK 465 ARG V 312
REMARK 465 ILE V 313
REMARK 465 LYS V 314
REMARK 465 ARG V 315
REMARK 465 SER V 316
REMARK 465 ARG V 317
REMARK 465 MET X 1
REMARK 465 ARG X 311
REMARK 465 ARG X 312
REMARK 465 ILE X 313
REMARK 465 LYS X 314
REMARK 465 ARG X 315
REMARK 465 SER X 316
REMARK 465 ARG X 317
REMARK 465 MET Y 1
REMARK 465 ARG Y 311
REMARK 465 ARG Y 312
REMARK 465 ILE Y 313
REMARK 465 LYS Y 314
REMARK 465 ARG Y 315
REMARK 465 SER Y 316
REMARK 465 ARG Y 317
REMARK 465 MET W 1
REMARK 465 ARG W 312
REMARK 465 ILE W 313
REMARK 465 LYS W 314
REMARK 465 ARG W 315
REMARK 465 SER W 316
REMARK 465 ARG W 317
REMARK 465 MET Z 1
REMARK 465 ARG Z 311
REMARK 465 ARG Z 312
REMARK 465 ILE Z 313
REMARK 465 LYS Z 314
REMARK 465 ARG Z 315
REMARK 465 SER Z 316
REMARK 465 ARG Z 317
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER N 114 C4 DKO N 900 1.57
REMARK 500 OG SER D 114 C4 DK6 D 900 1.63
REMARK 500 OG SER E 114 C4 DKF E 900 1.67
REMARK 500 OG SER H 114 C4 DK6 H 900 1.68
REMARK 500 OG SER B 114 C4 DKO B 900 1.69
REMARK 500 OG SER K 114 C4 DKF K 900 1.71
REMARK 500 OG SER C 114 C4 DKL C 900 1.73
REMARK 500 OG SER F 114 C4 DK9 F 900 1.74
REMARK 500 OG SER A 114 C4 DKL A 900 1.77
REMARK 500 OG SER R 114 C4 DKO R 900 1.78
REMARK 500 OG SER M 114 C4 DKF M 900 1.79
REMARK 500 OG SER P 114 C4 DK9 P 900 1.81
REMARK 500 OG SER W 114 C4 DKF W 900 1.81
REMARK 500 OG SER G 114 C4 DKF G 900 1.81
REMARK 500 OG SER Q 114 C4 DKL Q 900 1.82
REMARK 500 OG SER O 114 C4 DK9 O 900 1.86
REMARK 500 OG SER V 114 C4 DKF V 900 1.88
REMARK 500 OG SER X 114 C4 DKL X 900 1.90
REMARK 500 OG SER I 114 C4 DKF I 900 1.90
REMARK 500 OG SER T 114 C4 DKL T 900 1.91
REMARK 500 OG SER U 114 C4 DKF U 900 1.96
REMARK 500 OG SER Z 114 C4 DK6 Z 900 2.01
REMARK 500 OG SER Y 114 C4 DKF Y 900 2.03
REMARK 500 OG SER J 114 C4 DKF J 900 2.03
REMARK 500 OG SER S 114 C4 DK6 S 900 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 103 36.81 -144.68
REMARK 500 SER A 114 -117.16 65.55
REMARK 500 LEU A 131 100.55 -167.69
REMARK 500 THR A 148 -35.22 -135.19
REMARK 500 ALA A 162 76.13 -165.25
REMARK 500 ASN A 210 78.19 47.57
REMARK 500 ARG A 284 -144.98 -106.44
REMARK 500 SER B 10 151.91 -49.42
REMARK 500 PHE B 103 32.79 -150.80
REMARK 500 SER B 114 -114.34 61.17
REMARK 500 THR B 148 -57.65 -134.90
REMARK 500 ARG B 284 -138.31 -95.90
REMARK 500 ALA B 309 66.09 -100.11
REMARK 500 PHE C 103 35.44 -145.95
REMARK 500 SER C 114 -118.97 55.98
REMARK 500 THR C 148 -67.41 -130.27
REMARK 500 ALA C 162 66.78 -160.09
REMARK 500 SER C 196 109.15 -58.57
REMARK 500 PHE C 211 137.21 -38.90
REMARK 500 ARG C 284 -143.62 -100.38
REMARK 500 GLU D 40 -159.43 -128.30
REMARK 500 ALA D 65 129.43 -35.76
REMARK 500 SER D 114 -113.51 68.45
REMARK 500 ASP D 187 3.83 -152.85
REMARK 500 PHE D 211 128.76 -36.54
REMARK 500 MET D 239 119.74 -33.56
REMARK 500 ARG D 284 -138.29 -101.14
REMARK 500 PHE E 103 37.15 -140.40
REMARK 500 SER E 114 -116.15 58.78
REMARK 500 THR E 148 -57.98 -130.10
REMARK 500 ALA E 160 43.05 -90.97
REMARK 500 THR E 161 -51.15 -153.75
REMARK 500 ASN E 210 43.15 37.56
REMARK 500 ARG E 284 -139.72 -103.97
REMARK 500 SER F 10 150.86 -49.47
REMARK 500 ARG F 14 -62.35 -105.74
REMARK 500 PHE F 103 34.92 -151.32
REMARK 500 SER F 114 -118.29 58.85
REMARK 500 THR F 148 -34.52 -138.05
REMARK 500 ALA F 162 77.61 -153.83
REMARK 500 ARG F 284 -145.42 -114.27
REMARK 500 GLU G 7 147.28 -38.83
REMARK 500 TYR G 45 33.01 -98.39
REMARK 500 ALA G 65 125.54 -33.18
REMARK 500 PHE G 103 36.39 -146.77
REMARK 500 SER G 114 -118.79 58.78
REMARK 500 LEU G 131 102.55 -164.27
REMARK 500 ALA G 162 77.19 -150.66
REMARK 500 PHE G 211 -70.21 -16.92
REMARK 500 MET G 239 116.42 -39.20
REMARK 500
REMARK 500 THIS ENTRY HAS 189 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKL A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKO B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKL C 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DK6 D 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF E 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DK9 F 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF G 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DK6 H 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF I 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF J 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF K 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF M 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKO N 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DK9 O 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DK9 P 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKL Q 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKO R 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DK6 S 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKL T 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF U 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF V 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKL X 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF Y 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKF W 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DK6 Z 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DKF L 900 and SER L
REMARK 800 114
DBREF 6KHM A 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM B 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM C 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM D 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM E 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM F 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM G 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM H 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM I 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM J 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM K 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM L 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM M 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM N 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM O 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM P 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM Q 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM R 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM S 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM T 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM U 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM V 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM X 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM Y 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM W 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
DBREF 6KHM Z 1 317 UNP E6DAE5 E6DAE5_CUTAC 1 317
SEQRES 1 A 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 A 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 A 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 A 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 A 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 A 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 A 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 A 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 A 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 A 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 A 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 A 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 A 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 A 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 A 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 A 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 A 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 A 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 A 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 A 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 A 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 A 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 A 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 A 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 A 317 ILE LYS ARG SER ARG
SEQRES 1 B 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 B 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 B 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 B 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 B 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 B 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 B 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 B 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 B 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 B 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 B 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 B 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 B 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 B 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 B 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 B 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 B 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 B 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 B 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 B 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 B 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 B 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 B 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 B 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 B 317 ILE LYS ARG SER ARG
SEQRES 1 C 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 C 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 C 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 C 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 C 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 C 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 C 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 C 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 C 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 C 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 C 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 C 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 C 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 C 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 C 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 C 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 C 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 C 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 C 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 C 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 C 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 C 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 C 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 C 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 C 317 ILE LYS ARG SER ARG
SEQRES 1 D 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 D 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 D 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 D 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 D 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 D 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 D 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 D 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 D 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 D 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 D 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 D 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 D 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 D 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 D 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 D 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 D 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 D 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 D 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 D 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 D 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 D 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 D 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 D 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 D 317 ILE LYS ARG SER ARG
SEQRES 1 E 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 E 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 E 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 E 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 E 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 E 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 E 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 E 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 E 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 E 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 E 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 E 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 E 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 E 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 E 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 E 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 E 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 E 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 E 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 E 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 E 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 E 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 E 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 E 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 E 317 ILE LYS ARG SER ARG
SEQRES 1 F 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 F 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 F 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 F 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 F 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 F 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 F 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 F 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 F 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 F 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 F 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 F 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 F 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 F 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 F 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 F 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 F 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 F 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 F 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 F 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 F 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 F 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 F 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 F 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 F 317 ILE LYS ARG SER ARG
SEQRES 1 G 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 G 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 G 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 G 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 G 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 G 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 G 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 G 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 G 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 G 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 G 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 G 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 G 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 G 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 G 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 G 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 G 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 G 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 G 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 G 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 G 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 G 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 G 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 G 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 G 317 ILE LYS ARG SER ARG
SEQRES 1 H 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 H 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 H 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 H 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 H 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 H 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 H 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 H 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 H 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 H 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 H 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 H 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 H 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 H 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 H 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 H 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 H 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 H 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 H 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 H 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 H 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 H 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 H 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 H 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 H 317 ILE LYS ARG SER ARG
SEQRES 1 I 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 I 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 I 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 I 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 I 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 I 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 I 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 I 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 I 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 I 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 I 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 I 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 I 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 I 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 I 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 I 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 I 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 I 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 I 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 I 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 I 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 I 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 I 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 I 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 I 317 ILE LYS ARG SER ARG
SEQRES 1 J 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 J 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 J 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 J 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 J 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 J 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 J 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 J 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 J 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 J 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 J 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 J 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 J 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 J 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 J 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 J 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 J 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 J 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 J 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 J 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 J 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 J 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 J 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 J 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 J 317 ILE LYS ARG SER ARG
SEQRES 1 K 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 K 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 K 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 K 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 K 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 K 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 K 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 K 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 K 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 K 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 K 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 K 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 K 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 K 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 K 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 K 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 K 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 K 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 K 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 K 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 K 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 K 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 K 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 K 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 K 317 ILE LYS ARG SER ARG
SEQRES 1 L 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 L 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 L 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 L 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 L 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 L 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 L 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 L 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 L 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 L 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 L 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 L 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 L 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 L 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 L 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 L 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 L 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 L 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 L 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 L 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 L 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 L 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 L 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 L 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 L 317 ILE LYS ARG SER ARG
SEQRES 1 M 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 M 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 M 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 M 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 M 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 M 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 M 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 M 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 M 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 M 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 M 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 M 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 M 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 M 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 M 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 M 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 M 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 M 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 M 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 M 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 M 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 M 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 M 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 M 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 M 317 ILE LYS ARG SER ARG
SEQRES 1 N 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 N 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 N 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 N 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 N 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 N 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 N 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 N 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 N 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 N 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 N 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 N 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 N 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 N 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 N 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 N 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 N 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 N 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 N 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 N 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 N 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 N 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 N 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 N 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 N 317 ILE LYS ARG SER ARG
SEQRES 1 O 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 O 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 O 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 O 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 O 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 O 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 O 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 O 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 O 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 O 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 O 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 O 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 O 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 O 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 O 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 O 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 O 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 O 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 O 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 O 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 O 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 O 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 O 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 O 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 O 317 ILE LYS ARG SER ARG
SEQRES 1 P 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 P 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 P 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 P 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 P 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 P 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 P 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 P 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 P 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 P 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 P 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 P 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 P 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 P 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 P 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 P 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 P 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 P 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 P 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 P 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 P 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 P 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 P 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 P 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 P 317 ILE LYS ARG SER ARG
SEQRES 1 Q 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 Q 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 Q 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 Q 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 Q 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 Q 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 Q 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 Q 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 Q 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 Q 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 Q 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 Q 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 Q 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 Q 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 Q 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 Q 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 Q 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 Q 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 Q 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 Q 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 Q 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 Q 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 Q 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 Q 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 Q 317 ILE LYS ARG SER ARG
SEQRES 1 R 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 R 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 R 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 R 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 R 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 R 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 R 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 R 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 R 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 R 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 R 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 R 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 R 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 R 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 R 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 R 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 R 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 R 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 R 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 R 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 R 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 R 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 R 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 R 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 R 317 ILE LYS ARG SER ARG
SEQRES 1 S 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 S 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 S 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 S 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 S 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 S 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 S 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 S 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 S 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 S 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 S 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 S 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 S 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 S 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 S 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 S 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 S 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 S 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 S 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 S 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 S 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 S 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 S 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 S 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 S 317 ILE LYS ARG SER ARG
SEQRES 1 T 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 T 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 T 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 T 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 T 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 T 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 T 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 T 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 T 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 T 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 T 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 T 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 T 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 T 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 T 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 T 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 T 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 T 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 T 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 T 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 T 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 T 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 T 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 T 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 T 317 ILE LYS ARG SER ARG
SEQRES 1 U 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 U 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 U 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 U 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 U 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 U 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 U 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 U 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 U 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 U 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 U 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 U 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 U 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 U 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 U 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 U 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 U 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 U 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 U 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 U 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 U 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 U 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 U 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 U 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 U 317 ILE LYS ARG SER ARG
SEQRES 1 V 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 V 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 V 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 V 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 V 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 V 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 V 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 V 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 V 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 V 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 V 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 V 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 V 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 V 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 V 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 V 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 V 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 V 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 V 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 V 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 V 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 V 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 V 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 V 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 V 317 ILE LYS ARG SER ARG
SEQRES 1 X 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 X 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 X 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 X 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 X 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 X 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 X 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 X 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 X 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 X 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 X 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 X 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 X 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 X 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 X 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 X 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 X 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 X 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 X 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 X 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 X 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 X 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 X 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 X 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 X 317 ILE LYS ARG SER ARG
SEQRES 1 Y 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 Y 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 Y 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 Y 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 Y 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 Y 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 Y 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 Y 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 Y 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 Y 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 Y 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 Y 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 Y 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 Y 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 Y 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 Y 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 Y 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 Y 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 Y 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 Y 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 Y 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 Y 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 Y 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 Y 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 Y 317 ILE LYS ARG SER ARG
SEQRES 1 W 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 W 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 W 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 W 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 W 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 W 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 W 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 W 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 W 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 W 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 W 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 W 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 W 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 W 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 W 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 W 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 W 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 W 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 W 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 W 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 W 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 W 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 W 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 W 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 W 317 ILE LYS ARG SER ARG
SEQRES 1 Z 317 MET ALA LEU GLN GLU ILE GLU PHE THR SER HIS ASN GLY
SEQRES 2 Z 317 ARG ASP ALA ILE GLN ALA TRP ALA TYR GLU PRO VAL GLY
SEQRES 3 Z 317 THR PRO THR ALA VAL VAL GLN ILE ILE HIS GLY LEU GLY
SEQRES 4 Z 317 GLU HIS SER ARG ARG TYR LEU HIS MET ILE SER ALA LEU
SEQRES 5 Z 317 LEU ASP ALA GLY PHE VAL VAL ILE ALA ASP ASP HIS ALA
SEQRES 6 Z 317 GLY HIS GLY ARG THR ALA MET GLN SER GLY VAL TRP ALA
SEQRES 7 Z 317 ASP ALA GLY ASP ASN ALA ALA GLU VAL VAL ILE SER ASP
SEQRES 8 Z 317 GLU LEU THR LEU GLN GLN GLN LEU ALA GLY GLN PHE ASP
SEQRES 9 Z 317 ASP LEU PRO TRP VAL VAL PHE GLY HIS SER TRP GLY SER
SEQRES 10 Z 317 MET ILE ALA ARG ALA MET ALA THR ARG PRO GLY THR ARG
SEQRES 11 Z 317 LEU ASP GLY LEU ALA LEU CYS GLY ILE VAL ALA GLN PRO
SEQRES 12 Z 317 ARG GLY PHE GLU THR THR LEU ASP HIS LYS THR LEU ALA
SEQRES 13 Z 317 LYS ALA MET ALA THR ALA PRO THR ASP PRO ALA PRO GLU
SEQRES 14 Z 317 ALA LEU VAL ALA GLN MET PHE ASP GLY PHE ALA ASP ARG
SEQRES 15 Z 317 LEU SER GLU ASP ASP GLY PRO THR GLY TRP VAL ALA ARG
SEQRES 16 Z 317 SER LYS GLU VAL VAL ALA ASP HIS GLY LYS ASP LYS PHE
SEQRES 17 Z 317 ASN ASN PHE GLY ALA PRO MET SER THR ARG PHE LEU GLN
SEQRES 18 Z 317 GLY LEU ALA ASP ILE TYR ALA MET ALA ASN GLY ASP SER
SEQRES 19 Z 317 PHE TYR ALA THR MET PRO ASN ILE PRO ILE VAL LEU PHE
SEQRES 20 Z 317 ALA GLY SER GLU ASP PRO ALA GLY ASP PHE GLY THR GLY
SEQRES 21 Z 317 VAL LYS ALA VAL ALA GLU ARG LEU ARG ARG ASP GLY HIS
SEQRES 22 Z 317 ASN VAL GLU LEU HIS LEU TYR ASP GLY LEU ARG HIS GLU
SEQRES 23 Z 317 VAL HIS ASN GLU PRO GLU SER ARG ALA ASP VAL GLU SER
SEQRES 24 Z 317 SER LEU VAL THR PHE VAL ASP ARG VAL ALA ASN ARG ARG
SEQRES 25 Z 317 ILE LYS ARG SER ARG
HET DKL A 900 9
HET DKO B 900 10
HET DKL C 900 9
HET DK6 D 900 5
HET DKF E 900 8
HET DK9 F 900 7
HET DKF G 900 8
HET DK6 H 900 5
HET DKF I 900 8
HET DKF J 900 8
HET DKF K 900 8
HET DKF L 900 8
HET DKF M 900 8
HET DKO N 900 10
HET DK9 O 900 7
HET DK9 P 900 7
HET DKL Q 900 9
HET DKO R 900 10
HET DK6 S 900 5
HET DKL T 900 9
HET DKF U 900 8
HET DKF V 900 8
HET DKL X 900 9
HET DKF Y 900 8
HET DKF W 900 8
HET DK6 Z 900 5
HETNAM DKL HEPTANE-1,1-DIOL
HETNAM DKO OCTANE-1,1-DIOL
HETNAM DK6 PROPANE-1,1-DIOL
HETNAM DKF HEXANE-1,1-DIOL
HETNAM DK9 PENTANE-1,1-DIOL
FORMUL 27 DKL 5(C7 H16 O2)
FORMUL 28 DKO 3(C8 H18 O2)
FORMUL 30 DK6 4(C3 H8 O2)
FORMUL 31 DKF 11(C6 H14 O2)
FORMUL 32 DK9 3(C5 H12 O2)
FORMUL 53 HOH *2515(H2 O)
HELIX 1 AA1 HIS A 41 ARG A 44 5 4
HELIX 2 AA2 TYR A 45 GLY A 56 1 12
HELIX 3 AA3 HIS A 67 GLY A 75 1 9
HELIX 4 AA4 ASN A 83 GLN A 98 1 16
HELIX 5 AA5 SER A 114 THR A 125 1 12
HELIX 6 AA6 PRO A 143 THR A 148 1 6
HELIX 7 AA7 ASP A 151 ALA A 162 1 12
HELIX 8 AA8 PRO A 168 PHE A 176 1 9
HELIX 9 AA9 THR A 190 ALA A 194 5 5
HELIX 10 AB1 SER A 196 ASP A 206 1 11
HELIX 11 AB2 SER A 216 GLY A 232 1 17
HELIX 12 AB3 GLY A 232 MET A 239 1 8
HELIX 13 AB4 ASP A 252 ASP A 256 5 5
HELIX 14 AB5 GLY A 258 ASP A 271 1 14
HELIX 15 AB6 GLU A 290 ASN A 310 1 21
HELIX 16 AB7 HIS B 41 ARG B 44 5 4
HELIX 17 AB8 TYR B 45 ALA B 55 1 11
HELIX 18 AB9 HIS B 67 GLY B 75 1 9
HELIX 19 AC1 ASN B 83 GLN B 98 1 16
HELIX 20 AC2 SER B 114 THR B 125 1 12
HELIX 21 AC3 PRO B 143 THR B 148 1 6
HELIX 22 AC4 ASP B 151 ALA B 162 1 12
HELIX 23 AC5 PRO B 168 PHE B 176 1 9
HELIX 24 AC6 SER B 184 GLY B 188 5 5
HELIX 25 AC7 THR B 190 ALA B 194 5 5
HELIX 26 AC8 SER B 196 ASP B 206 1 11
HELIX 27 AC9 SER B 216 GLY B 232 1 17
HELIX 28 AD1 GLY B 232 MET B 239 1 8
HELIX 29 AD2 ASP B 252 ASP B 256 5 5
HELIX 30 AD3 GLY B 258 ASP B 271 1 14
HELIX 31 AD4 SER B 293 VAL B 308 1 16
HELIX 32 AD5 HIS C 41 ARG C 44 5 4
HELIX 33 AD6 TYR C 45 ALA C 55 1 11
HELIX 34 AD7 HIS C 67 GLY C 75 1 9
HELIX 35 AD8 ASN C 83 GLN C 98 1 16
HELIX 36 AD9 SER C 114 ARG C 126 1 13
HELIX 37 AE1 PRO C 143 THR C 148 1 6
HELIX 38 AE2 ASP C 151 ALA C 162 1 12
HELIX 39 AE3 PRO C 168 PHE C 176 1 9
HELIX 40 AE4 SER C 184 GLY C 188 5 5
HELIX 41 AE5 THR C 190 ALA C 194 5 5
HELIX 42 AE6 SER C 196 ASP C 206 1 11
HELIX 43 AE7 SER C 216 GLY C 232 1 17
HELIX 44 AE8 GLY C 232 MET C 239 1 8
HELIX 45 AE9 ASP C 252 ASP C 256 5 5
HELIX 46 AF1 GLY C 258 ASP C 271 1 14
HELIX 47 AF2 SER C 293 ASN C 310 1 18
HELIX 48 AF3 HIS D 41 ARG D 44 5 4
HELIX 49 AF4 TYR D 45 ALA D 55 1 11
HELIX 50 AF5 HIS D 67 GLY D 75 1 9
HELIX 51 AF6 ASN D 83 GLN D 98 1 16
HELIX 52 AF7 SER D 114 THR D 125 1 12
HELIX 53 AF8 PRO D 143 THR D 148 1 6
HELIX 54 AF9 ASP D 151 ALA D 162 1 12
HELIX 55 AG1 PRO D 168 PHE D 176 1 9
HELIX 56 AG2 SER D 184 GLY D 188 5 5
HELIX 57 AG3 THR D 190 ALA D 194 5 5
HELIX 58 AG4 SER D 196 ASP D 206 1 11
HELIX 59 AG5 SER D 216 GLY D 232 1 17
HELIX 60 AG6 GLY D 232 MET D 239 1 8
HELIX 61 AG7 ASP D 252 ASP D 256 5 5
HELIX 62 AG8 GLY D 258 ASP D 271 1 14
HELIX 63 AG9 SER D 293 ALA D 309 1 17
HELIX 64 AH1 HIS E 41 ARG E 44 5 4
HELIX 65 AH2 TYR E 45 ALA E 55 1 11
HELIX 66 AH3 HIS E 67 GLY E 75 1 9
HELIX 67 AH4 ASN E 83 GLN E 98 1 16
HELIX 68 AH5 SER E 114 THR E 125 1 12
HELIX 69 AH6 PRO E 143 THR E 148 1 6
HELIX 70 AH7 ASP E 151 ALA E 160 1 10
HELIX 71 AH8 PRO E 168 PHE E 176 1 9
HELIX 72 AH9 THR E 190 ALA E 194 5 5
HELIX 73 AI1 SER E 196 ASP E 206 1 11
HELIX 74 AI2 SER E 216 GLY E 232 1 17
HELIX 75 AI3 GLY E 232 MET E 239 1 8
HELIX 76 AI4 ASP E 252 ASP E 256 5 5
HELIX 77 AI5 GLY E 258 ASP E 271 1 14
HELIX 78 AI6 SER E 293 ARG E 312 1 20
HELIX 79 AI7 HIS F 41 ARG F 44 5 4
HELIX 80 AI8 TYR F 45 ALA F 55 1 11
HELIX 81 AI9 HIS F 67 GLY F 75 1 9
HELIX 82 AJ1 ASN F 83 GLN F 98 1 16
HELIX 83 AJ2 SER F 114 ALA F 124 1 11
HELIX 84 AJ3 PRO F 143 THR F 148 1 6
HELIX 85 AJ4 ASP F 151 ALA F 162 1 12
HELIX 86 AJ5 PRO F 168 PHE F 176 1 9
HELIX 87 AJ6 SER F 184 GLY F 188 5 5
HELIX 88 AJ7 THR F 190 ALA F 194 5 5
HELIX 89 AJ8 SER F 196 ASP F 206 1 11
HELIX 90 AJ9 SER F 216 GLY F 232 1 17
HELIX 91 AK1 GLY F 232 MET F 239 1 8
HELIX 92 AK2 ASP F 252 ASP F 256 5 5
HELIX 93 AK3 GLY F 258 ASP F 271 1 14
HELIX 94 AK4 SER F 293 ALA F 309 1 17
HELIX 95 AK5 HIS G 41 ARG G 44 5 4
HELIX 96 AK6 TYR G 45 ALA G 55 1 11
HELIX 97 AK7 HIS G 67 GLY G 75 1 9
HELIX 98 AK8 ASN G 83 GLN G 98 1 16
HELIX 99 AK9 SER G 114 THR G 125 1 12
HELIX 100 AL1 PRO G 143 THR G 148 1 6
HELIX 101 AL2 ASP G 151 ALA G 162 1 12
HELIX 102 AL3 PRO G 168 PHE G 176 1 9
HELIX 103 AL4 SER G 184 GLY G 188 5 5
HELIX 104 AL5 THR G 190 ALA G 194 5 5
HELIX 105 AL6 SER G 196 ASP G 206 1 11
HELIX 106 AL7 SER G 216 ASN G 231 1 16
HELIX 107 AL8 GLY G 232 MET G 239 1 8
HELIX 108 AL9 ASP G 252 ASP G 256 5 5
HELIX 109 AM1 GLY G 258 ASP G 271 1 14
HELIX 110 AM2 SER G 293 ARG G 311 1 19
HELIX 111 AM3 HIS H 41 ARG H 44 5 4
HELIX 112 AM4 TYR H 45 ALA H 55 1 11
HELIX 113 AM5 HIS H 67 GLY H 75 1 9
HELIX 114 AM6 ASN H 83 GLN H 98 1 16
HELIX 115 AM7 SER H 114 THR H 125 1 12
HELIX 116 AM8 PRO H 143 THR H 148 1 6
HELIX 117 AM9 ASP H 151 ALA H 162 1 12
HELIX 118 AN1 PRO H 168 PHE H 176 1 9
HELIX 119 AN2 SER H 184 GLY H 188 5 5
HELIX 120 AN3 THR H 190 ALA H 194 5 5
HELIX 121 AN4 SER H 196 ASP H 206 1 11
HELIX 122 AN5 SER H 216 ASN H 231 1 16
HELIX 123 AN6 GLY H 232 MET H 239 1 8
HELIX 124 AN7 ASP H 252 ASP H 256 5 5
HELIX 125 AN8 GLY H 258 ASP H 271 1 14
HELIX 126 AN9 SER H 293 ALA H 309 1 17
HELIX 127 AO1 HIS I 41 ARG I 44 5 4
HELIX 128 AO2 TYR I 45 ALA I 55 1 11
HELIX 129 AO3 HIS I 67 GLY I 75 1 9
HELIX 130 AO4 ASN I 83 GLN I 98 1 16
HELIX 131 AO5 SER I 114 THR I 125 1 12
HELIX 132 AO6 PRO I 143 THR I 148 1 6
HELIX 133 AO7 ASP I 151 ALA I 162 1 12
HELIX 134 AO8 PRO I 168 PHE I 176 1 9
HELIX 135 AO9 THR I 190 ALA I 194 5 5
HELIX 136 AP1 SER I 196 ASP I 206 1 11
HELIX 137 AP2 SER I 216 GLY I 232 1 17
HELIX 138 AP3 GLY I 232 MET I 239 1 8
HELIX 139 AP4 ASP I 252 ASP I 256 5 5
HELIX 140 AP5 GLY I 258 ASP I 271 1 14
HELIX 141 AP6 SER I 293 ARG I 312 1 20
HELIX 142 AP7 HIS J 41 ARG J 44 5 4
HELIX 143 AP8 TYR J 45 ALA J 55 1 11
HELIX 144 AP9 HIS J 67 GLY J 75 1 9
HELIX 145 AQ1 ASN J 83 GLN J 98 1 16
HELIX 146 AQ2 SER J 114 THR J 125 1 12
HELIX 147 AQ3 PRO J 143 THR J 148 1 6
HELIX 148 AQ4 ASP J 151 ALA J 162 1 12
HELIX 149 AQ5 PRO J 168 PHE J 176 1 9
HELIX 150 AQ6 SER J 184 GLY J 188 5 5
HELIX 151 AQ7 SER J 196 ASP J 206 1 11
HELIX 152 AQ8 SER J 216 GLY J 232 1 17
HELIX 153 AQ9 GLY J 232 MET J 239 1 8
HELIX 154 AR1 ASP J 252 ASP J 256 5 5
HELIX 155 AR2 GLY J 258 ASP J 271 1 14
HELIX 156 AR3 SER J 293 ASN J 310 1 18
HELIX 157 AR4 HIS K 41 ARG K 44 5 4
HELIX 158 AR5 TYR K 45 ALA K 55 1 11
HELIX 159 AR6 HIS K 67 GLY K 75 1 9
HELIX 160 AR7 ASN K 83 GLN K 98 1 16
HELIX 161 AR8 SER K 114 THR K 125 1 12
HELIX 162 AR9 PRO K 143 THR K 148 1 6
HELIX 163 AS1 ASP K 151 ALA K 162 1 12
HELIX 164 AS2 PRO K 168 PHE K 176 1 9
HELIX 165 AS3 SER K 196 ASP K 206 1 11
HELIX 166 AS4 SER K 216 GLY K 232 1 17
HELIX 167 AS5 GLY K 232 MET K 239 1 8
HELIX 168 AS6 ASP K 252 ASP K 256 5 5
HELIX 169 AS7 GLY K 258 ASP K 271 1 14
HELIX 170 AS8 SER K 293 ARG K 312 1 20
HELIX 171 AS9 HIS L 41 ARG L 44 5 4
HELIX 172 AT1 TYR L 45 ALA L 55 1 11
HELIX 173 AT2 HIS L 67 GLY L 75 1 9
HELIX 174 AT3 ASN L 83 GLN L 97 1 15
HELIX 175 AT4 GLN L 98 ALA L 100 5 3
HELIX 176 AT5 SER L 114 THR L 125 1 12
HELIX 177 AT6 PRO L 143 THR L 148 1 6
HELIX 178 AT7 ASP L 151 ALA L 162 1 12
HELIX 179 AT8 PRO L 168 PHE L 176 1 9
HELIX 180 AT9 SER L 184 GLY L 188 5 5
HELIX 181 AU1 THR L 190 ALA L 194 5 5
HELIX 182 AU2 SER L 196 ASP L 206 1 11
HELIX 183 AU3 SER L 216 GLY L 232 1 17
HELIX 184 AU4 GLY L 232 MET L 239 1 8
HELIX 185 AU5 ASP L 252 ASP L 256 5 5
HELIX 186 AU6 GLY L 258 ASP L 271 1 14
HELIX 187 AU7 SER L 293 ILE L 313 1 21
HELIX 188 AU8 HIS M 41 ARG M 44 5 4
HELIX 189 AU9 TYR M 45 ALA M 55 1 11
HELIX 190 AV1 HIS M 67 GLY M 75 1 9
HELIX 191 AV2 ASN M 83 GLN M 97 1 15
HELIX 192 AV3 GLN M 98 ALA M 100 5 3
HELIX 193 AV4 SER M 114 ARG M 126 1 13
HELIX 194 AV5 PRO M 143 THR M 148 1 6
HELIX 195 AV6 ASP M 151 ALA M 162 1 12
HELIX 196 AV7 PRO M 168 ASP M 177 1 10
HELIX 197 AV8 GLY M 188 ALA M 194 5 7
HELIX 198 AV9 SER M 196 ASP M 206 1 11
HELIX 199 AW1 SER M 216 GLY M 232 1 17
HELIX 200 AW2 GLY M 232 MET M 239 1 8
HELIX 201 AW3 ASP M 252 ASP M 256 5 5
HELIX 202 AW4 GLY M 258 ASP M 271 1 14
HELIX 203 AW5 SER M 293 ASN M 310 1 18
HELIX 204 AW6 HIS N 41 ARG N 44 5 4
HELIX 205 AW7 TYR N 45 ALA N 55 1 11
HELIX 206 AW8 HIS N 67 GLY N 75 1 9
HELIX 207 AW9 ASN N 83 GLN N 98 1 16
HELIX 208 AX1 SER N 114 THR N 125 1 12
HELIX 209 AX2 PRO N 143 THR N 148 1 6
HELIX 210 AX3 ASP N 151 ALA N 162 1 12
HELIX 211 AX4 PRO N 168 ASP N 177 1 10
HELIX 212 AX5 SER N 184 GLY N 188 5 5
HELIX 213 AX6 THR N 190 ALA N 194 5 5
HELIX 214 AX7 SER N 196 ASP N 206 1 11
HELIX 215 AX8 SER N 216 GLY N 232 1 17
HELIX 216 AX9 GLY N 232 MET N 239 1 8
HELIX 217 AY1 ASP N 252 ASP N 256 5 5
HELIX 218 AY2 GLY N 258 ASP N 271 1 14
HELIX 219 AY3 SER N 293 ARG N 311 1 19
HELIX 220 AY4 HIS O 41 ARG O 44 5 4
HELIX 221 AY5 TYR O 45 ALA O 55 1 11
HELIX 222 AY6 HIS O 67 GLY O 75 1 9
HELIX 223 AY7 ASN O 83 GLN O 98 1 16
HELIX 224 AY8 SER O 114 THR O 125 1 12
HELIX 225 AY9 PRO O 143 THR O 148 1 6
HELIX 226 AZ1 ASP O 151 ALA O 162 1 12
HELIX 227 AZ2 PRO O 168 PHE O 176 1 9
HELIX 228 AZ3 SER O 184 GLY O 188 5 5
HELIX 229 AZ4 THR O 190 ALA O 194 5 5
HELIX 230 AZ5 SER O 196 ASP O 206 1 11
HELIX 231 AZ6 SER O 216 GLY O 232 1 17
HELIX 232 AZ7 GLY O 232 MET O 239 1 8
HELIX 233 AZ8 GLY O 258 ASP O 271 1 14
HELIX 234 AZ9 SER O 293 ASN O 310 1 18
HELIX 235 BA1 HIS P 41 ARG P 44 5 4
HELIX 236 BA2 TYR P 45 ALA P 55 1 11
HELIX 237 BA3 HIS P 67 GLY P 75 1 9
HELIX 238 BA4 ASN P 83 GLN P 98 1 16
HELIX 239 BA5 SER P 114 THR P 125 1 12
HELIX 240 BA6 PRO P 143 THR P 148 1 6
HELIX 241 BA7 ASP P 151 ALA P 162 1 12
HELIX 242 BA8 PRO P 168 PHE P 176 1 9
HELIX 243 BA9 THR P 190 ALA P 194 5 5
HELIX 244 BB1 SER P 196 ASP P 206 1 11
HELIX 245 BB2 SER P 216 GLY P 232 1 17
HELIX 246 BB3 GLY P 232 MET P 239 1 8
HELIX 247 BB4 ASP P 252 ASP P 256 5 5
HELIX 248 BB5 GLY P 258 ASP P 271 1 14
HELIX 249 BB6 SER P 293 ALA P 309 1 17
HELIX 250 BB7 HIS Q 41 ARG Q 44 5 4
HELIX 251 BB8 TYR Q 45 ALA Q 55 1 11
HELIX 252 BB9 HIS Q 67 GLY Q 75 1 9
HELIX 253 BC1 ASN Q 83 GLN Q 97 1 15
HELIX 254 BC2 GLN Q 98 ALA Q 100 5 3
HELIX 255 BC3 SER Q 114 THR Q 125 1 12
HELIX 256 BC4 PRO Q 143 THR Q 148 1 6
HELIX 257 BC5 ASP Q 151 ALA Q 162 1 12
HELIX 258 BC6 PRO Q 168 PHE Q 176 1 9
HELIX 259 BC7 THR Q 190 ALA Q 194 5 5
HELIX 260 BC8 SER Q 196 ASP Q 206 1 11
HELIX 261 BC9 SER Q 216 GLY Q 232 1 17
HELIX 262 BD1 GLY Q 232 MET Q 239 1 8
HELIX 263 BD2 GLY Q 258 ASP Q 271 1 14
HELIX 264 BD3 SER Q 293 ARG Q 312 1 20
HELIX 265 BD4 HIS R 41 ARG R 44 5 4
HELIX 266 BD5 TYR R 45 ALA R 55 1 11
HELIX 267 BD6 HIS R 67 GLY R 75 1 9
HELIX 268 BD7 ASN R 83 GLN R 98 1 16
HELIX 269 BD8 SER R 114 THR R 125 1 12
HELIX 270 BD9 PRO R 143 THR R 148 1 6
HELIX 271 BE1 ASP R 151 ALA R 162 1 12
HELIX 272 BE2 PRO R 168 PHE R 176 1 9
HELIX 273 BE3 THR R 190 ALA R 194 5 5
HELIX 274 BE4 SER R 196 ASP R 206 1 11
HELIX 275 BE5 SER R 216 GLY R 232 1 17
HELIX 276 BE6 GLY R 232 MET R 239 1 8
HELIX 277 BE7 GLY R 258 ASP R 271 1 14
HELIX 278 BE8 GLU R 290 ARG R 307 1 18
HELIX 279 BE9 HIS S 41 ARG S 44 5 4
HELIX 280 BF1 TYR S 45 ALA S 55 1 11
HELIX 281 BF2 HIS S 67 GLY S 75 1 9
HELIX 282 BF3 ASN S 83 GLN S 98 1 16
HELIX 283 BF4 SER S 114 THR S 125 1 12
HELIX 284 BF5 PRO S 143 THR S 148 1 6
HELIX 285 BF6 ASP S 151 ALA S 162 1 12
HELIX 286 BF7 PRO S 168 PHE S 176 1 9
HELIX 287 BF8 THR S 190 ALA S 194 5 5
HELIX 288 BF9 SER S 196 ASP S 206 1 11
HELIX 289 BG1 SER S 216 GLY S 232 1 17
HELIX 290 BG2 GLY S 232 MET S 239 1 8
HELIX 291 BG3 ASP S 252 ASP S 256 5 5
HELIX 292 BG4 GLY S 258 ASP S 271 1 14
HELIX 293 BG5 GLU S 290 ASN S 310 1 21
HELIX 294 BG6 HIS T 41 ARG T 44 5 4
HELIX 295 BG7 TYR T 45 ALA T 55 1 11
HELIX 296 BG8 HIS T 67 GLY T 75 1 9
HELIX 297 BG9 ASN T 83 GLN T 98 1 16
HELIX 298 BH1 SER T 114 THR T 125 1 12
HELIX 299 BH2 PRO T 143 THR T 148 1 6
HELIX 300 BH3 ASP T 151 ALA T 162 1 12
HELIX 301 BH4 PRO T 168 PHE T 176 1 9
HELIX 302 BH5 SER T 184 GLY T 188 5 5
HELIX 303 BH6 THR T 190 ALA T 194 5 5
HELIX 304 BH7 SER T 196 ASP T 206 1 11
HELIX 305 BH8 SER T 216 GLY T 232 1 17
HELIX 306 BH9 GLY T 232 MET T 239 1 8
HELIX 307 BI1 ASP T 252 ASP T 256 5 5
HELIX 308 BI2 GLY T 258 ASP T 271 1 14
HELIX 309 BI3 SER T 293 ASN T 310 1 18
HELIX 310 BI4 HIS U 41 ARG U 44 5 4
HELIX 311 BI5 TYR U 45 ALA U 55 1 11
HELIX 312 BI6 HIS U 67 GLY U 75 1 9
HELIX 313 BI7 ASN U 83 GLN U 97 1 15
HELIX 314 BI8 GLN U 98 ALA U 100 5 3
HELIX 315 BI9 SER U 114 ARG U 126 1 13
HELIX 316 BJ1 PRO U 143 THR U 148 1 6
HELIX 317 BJ2 ASP U 151 ALA U 162 1 12
HELIX 318 BJ3 PRO U 168 PHE U 176 1 9
HELIX 319 BJ4 THR U 190 ALA U 194 5 5
HELIX 320 BJ5 SER U 196 ASP U 206 1 11
HELIX 321 BJ6 SER U 216 GLY U 232 1 17
HELIX 322 BJ7 GLY U 232 MET U 239 1 8
HELIX 323 BJ8 ASP U 252 ASP U 256 5 5
HELIX 324 BJ9 GLY U 258 ASP U 271 1 14
HELIX 325 BK1 GLU U 290 ALA U 309 1 20
HELIX 326 BK2 HIS V 41 ARG V 44 5 4
HELIX 327 BK3 TYR V 45 ALA V 55 1 11
HELIX 328 BK4 HIS V 67 GLY V 75 1 9
HELIX 329 BK5 ASN V 83 GLN V 98 1 16
HELIX 330 BK6 SER V 114 ALA V 124 1 11
HELIX 331 BK7 PRO V 143 THR V 148 1 6
HELIX 332 BK8 ASP V 151 ALA V 162 1 12
HELIX 333 BK9 PRO V 168 PHE V 176 1 9
HELIX 334 BL1 SER V 184 GLY V 188 5 5
HELIX 335 BL2 THR V 190 ALA V 194 5 5
HELIX 336 BL3 SER V 196 ASP V 206 1 11
HELIX 337 BL4 SER V 216 ASN V 231 1 16
HELIX 338 BL5 GLY V 232 MET V 239 1 8
HELIX 339 BL6 ASP V 252 ASP V 256 5 5
HELIX 340 BL7 GLY V 258 ASP V 271 1 14
HELIX 341 BL8 GLU V 290 ASN V 310 1 21
HELIX 342 BL9 HIS X 41 ARG X 44 5 4
HELIX 343 BM1 TYR X 45 ALA X 55 1 11
HELIX 344 BM2 HIS X 67 GLY X 75 1 9
HELIX 345 BM3 ASN X 83 GLN X 97 1 15
HELIX 346 BM4 GLN X 98 ALA X 100 5 3
HELIX 347 BM5 SER X 114 ALA X 124 1 11
HELIX 348 BM6 PRO X 143 THR X 148 1 6
HELIX 349 BM7 ASP X 151 ALA X 162 1 12
HELIX 350 BM8 PRO X 168 PHE X 176 1 9
HELIX 351 BM9 SER X 184 GLY X 188 5 5
HELIX 352 BN1 SER X 196 ASP X 206 1 11
HELIX 353 BN2 SER X 216 GLY X 232 1 17
HELIX 354 BN3 GLY X 232 MET X 239 1 8
HELIX 355 BN4 ASP X 252 ASP X 256 5 5
HELIX 356 BN5 GLY X 258 ASP X 271 1 14
HELIX 357 BN6 SER X 293 ALA X 309 1 17
HELIX 358 BN7 HIS Y 41 ARG Y 44 5 4
HELIX 359 BN8 TYR Y 45 GLY Y 56 1 12
HELIX 360 BN9 HIS Y 67 GLY Y 75 1 9
HELIX 361 BO1 ASN Y 83 GLN Y 97 1 15
HELIX 362 BO2 GLN Y 98 ALA Y 100 5 3
HELIX 363 BO3 SER Y 114 THR Y 125 1 12
HELIX 364 BO4 PRO Y 143 THR Y 148 1 6
HELIX 365 BO5 ASP Y 151 ALA Y 162 1 12
HELIX 366 BO6 PRO Y 168 PHE Y 176 1 9
HELIX 367 BO7 THR Y 190 ALA Y 194 5 5
HELIX 368 BO8 SER Y 196 ASP Y 206 1 11
HELIX 369 BO9 SER Y 216 GLY Y 232 1 17
HELIX 370 BP1 GLY Y 232 MET Y 239 1 8
HELIX 371 BP2 ASP Y 252 ASP Y 256 5 5
HELIX 372 BP3 GLY Y 258 ASP Y 271 1 14
HELIX 373 BP4 SER Y 293 ASN Y 310 1 18
HELIX 374 BP5 HIS W 41 ARG W 44 5 4
HELIX 375 BP6 TYR W 45 ALA W 55 1 11
HELIX 376 BP7 HIS W 67 GLY W 75 1 9
HELIX 377 BP8 ASN W 83 GLN W 98 1 16
HELIX 378 BP9 SER W 114 THR W 125 1 12
HELIX 379 BQ1 PRO W 143 THR W 148 1 6
HELIX 380 BQ2 ASP W 151 ALA W 162 1 12
HELIX 381 BQ3 PRO W 168 PHE W 176 1 9
HELIX 382 BQ4 THR W 190 ALA W 194 5 5
HELIX 383 BQ5 SER W 196 ASP W 206 1 11
HELIX 384 BQ6 SER W 216 GLY W 232 1 17
HELIX 385 BQ7 GLY W 232 MET W 239 1 8
HELIX 386 BQ8 ASP W 252 ASP W 256 5 5
HELIX 387 BQ9 GLY W 258 ASP W 271 1 14
HELIX 388 BR1 SER W 293 ASN W 310 1 18
HELIX 389 BR2 HIS Z 41 ARG Z 44 5 4
HELIX 390 BR3 TYR Z 45 ALA Z 55 1 11
HELIX 391 BR4 HIS Z 67 GLY Z 75 1 9
HELIX 392 BR5 ASN Z 83 GLN Z 98 1 16
HELIX 393 BR6 SER Z 114 THR Z 125 1 12
HELIX 394 BR7 PRO Z 143 THR Z 148 1 6
HELIX 395 BR8 ASP Z 151 ALA Z 162 1 12
HELIX 396 BR9 PRO Z 168 PHE Z 176 1 9
HELIX 397 BS1 THR Z 190 ALA Z 194 5 5
HELIX 398 BS2 SER Z 196 ASP Z 206 1 11
HELIX 399 BS3 SER Z 216 GLY Z 232 1 17
HELIX 400 BS4 GLY Z 232 ALA Z 237 1 6
HELIX 401 BS5 ASP Z 252 ASP Z 256 5 5
HELIX 402 BS6 GLY Z 258 GLY Z 272 1 15
HELIX 403 BS7 SER Z 293 ASN Z 310 1 18
SHEET 1 AA1 3 LEU A 3 GLU A 5 0
SHEET 2 AA1 3 ALA A 16 TYR A 22 -1 O ALA A 21 N GLN A 4
SHEET 3 AA1 3 PHE A 8 THR A 9 -1 N PHE A 8 O ILE A 17
SHEET 1 AA2 8 LEU A 3 GLU A 5 0
SHEET 2 AA2 8 ALA A 16 TYR A 22 -1 O ALA A 21 N GLN A 4
SHEET 3 AA2 8 PHE A 57 ASP A 63 -1 O VAL A 59 N TYR A 22
SHEET 4 AA2 8 ALA A 30 ILE A 35 1 N VAL A 32 O VAL A 58
SHEET 5 AA2 8 TRP A 108 HIS A 113 1 O PHE A 111 N GLN A 33
SHEET 6 AA2 8 GLY A 133 CYS A 137 1 O CYS A 137 N GLY A 112
SHEET 7 AA2 8 ILE A 244 GLY A 249 1 O VAL A 245 N LEU A 134
SHEET 8 AA2 8 VAL A 275 TYR A 280 1 O HIS A 278 N LEU A 246
SHEET 1 AA3 8 LEU B 3 THR B 9 0
SHEET 2 AA3 8 ALA B 16 TYR B 22 -1 O ALA B 19 N ILE B 6
SHEET 3 AA3 8 PHE B 57 ASP B 62 -1 O VAL B 59 N TYR B 22
SHEET 4 AA3 8 ALA B 30 ILE B 35 1 N ALA B 30 O VAL B 58
SHEET 5 AA3 8 TRP B 108 HIS B 113 1 O VAL B 109 N VAL B 31
SHEET 6 AA3 8 GLY B 133 CYS B 137 1 O ALA B 135 N VAL B 110
SHEET 7 AA3 8 ILE B 244 GLY B 249 1 O VAL B 245 N LEU B 134
SHEET 8 AA3 8 VAL B 275 TYR B 280 1 O GLU B 276 N LEU B 246
SHEET 1 AA4 8 LEU C 3 THR C 9 0
SHEET 2 AA4 8 ALA C 16 TYR C 22 -1 O ILE C 17 N PHE C 8
SHEET 3 AA4 8 PHE C 57 ASP C 63 -1 O VAL C 59 N TYR C 22
SHEET 4 AA4 8 ALA C 30 ILE C 35 1 N ALA C 30 O VAL C 58
SHEET 5 AA4 8 TRP C 108 HIS C 113 1 O VAL C 109 N VAL C 31
SHEET 6 AA4 8 GLY C 133 CYS C 137 1 O ALA C 135 N VAL C 110
SHEET 7 AA4 8 ILE C 244 GLY C 249 1 O VAL C 245 N LEU C 136
SHEET 8 AA4 8 VAL C 275 TYR C 280 1 O GLU C 276 N LEU C 246
SHEET 1 AA5 8 LEU D 3 THR D 9 0
SHEET 2 AA5 8 ALA D 16 TYR D 22 -1 O ILE D 17 N PHE D 8
SHEET 3 AA5 8 PHE D 57 ASP D 62 -1 O VAL D 59 N TYR D 22
SHEET 4 AA5 8 ALA D 30 ILE D 35 1 N VAL D 32 O VAL D 58
SHEET 5 AA5 8 TRP D 108 HIS D 113 1 O PHE D 111 N GLN D 33
SHEET 6 AA5 8 GLY D 133 CYS D 137 1 O ALA D 135 N VAL D 110
SHEET 7 AA5 8 ILE D 244 GLY D 249 1 O VAL D 245 N LEU D 136
SHEET 8 AA5 8 VAL D 275 TYR D 280 1 O GLU D 276 N LEU D 246
SHEET 1 AA6 8 LEU E 3 THR E 9 0
SHEET 2 AA6 8 ALA E 16 TYR E 22 -1 O ILE E 17 N PHE E 8
SHEET 3 AA6 8 PHE E 57 ASP E 62 -1 O VAL E 59 N TYR E 22
SHEET 4 AA6 8 ALA E 30 ILE E 35 1 N VAL E 32 O VAL E 58
SHEET 5 AA6 8 TRP E 108 HIS E 113 1 O PHE E 111 N GLN E 33
SHEET 6 AA6 8 GLY E 133 CYS E 137 1 O ALA E 135 N VAL E 110
SHEET 7 AA6 8 ILE E 244 GLY E 249 1 O VAL E 245 N LEU E 136
SHEET 8 AA6 8 VAL E 275 TYR E 280 1 O GLU E 276 N LEU E 246
SHEET 1 AA7 8 LEU F 3 THR F 9 0
SHEET 2 AA7 8 ALA F 16 TYR F 22 -1 O ALA F 21 N GLN F 4
SHEET 3 AA7 8 VAL F 58 ASP F 62 -1 O VAL F 59 N TYR F 22
SHEET 4 AA7 8 VAL F 31 ILE F 35 1 N VAL F 32 O VAL F 58
SHEET 5 AA7 8 TRP F 108 HIS F 113 1 O PHE F 111 N GLN F 33
SHEET 6 AA7 8 GLY F 133 CYS F 137 1 O ALA F 135 N VAL F 110
SHEET 7 AA7 8 ILE F 244 GLY F 249 1 O PHE F 247 N LEU F 136
SHEET 8 AA7 8 VAL F 275 TYR F 280 1 O HIS F 278 N LEU F 246
SHEET 1 AA8 3 LEU G 3 GLU G 5 0
SHEET 2 AA8 3 ALA G 16 TYR G 22 -1 O ALA G 21 N GLN G 4
SHEET 3 AA8 3 PHE G 8 THR G 9 -1 N PHE G 8 O ILE G 17
SHEET 1 AA9 8 LEU G 3 GLU G 5 0
SHEET 2 AA9 8 ALA G 16 TYR G 22 -1 O ALA G 21 N GLN G 4
SHEET 3 AA9 8 PHE G 57 ASP G 63 -1 O VAL G 59 N TYR G 22
SHEET 4 AA9 8 ALA G 30 ILE G 35 1 N VAL G 32 O VAL G 58
SHEET 5 AA9 8 TRP G 108 HIS G 113 1 O PHE G 111 N ILE G 35
SHEET 6 AA9 8 GLY G 133 CYS G 137 1 O ALA G 135 N VAL G 110
SHEET 7 AA9 8 ILE G 244 GLY G 249 1 O VAL G 245 N LEU G 136
SHEET 8 AA9 8 VAL G 275 TYR G 280 1 O HIS G 278 N LEU G 246
SHEET 1 AB1 8 LEU H 3 THR H 9 0
SHEET 2 AB1 8 ALA H 16 TYR H 22 -1 O ALA H 19 N ILE H 6
SHEET 3 AB1 8 VAL H 58 ASP H 62 -1 O VAL H 59 N TYR H 22
SHEET 4 AB1 8 VAL H 31 ILE H 35 1 N VAL H 32 O VAL H 58
SHEET 5 AB1 8 TRP H 108 HIS H 113 1 O PHE H 111 N GLN H 33
SHEET 6 AB1 8 GLY H 133 CYS H 137 1 O CYS H 137 N GLY H 112
SHEET 7 AB1 8 ILE H 244 GLY H 249 1 O VAL H 245 N LEU H 134
SHEET 8 AB1 8 VAL H 275 TYR H 280 1 O GLU H 276 N LEU H 246
SHEET 1 AB2 8 LEU I 3 THR I 9 0
SHEET 2 AB2 8 ALA I 16 TYR I 22 -1 O ILE I 17 N PHE I 8
SHEET 3 AB2 8 PHE I 57 ASP I 63 -1 O VAL I 59 N TYR I 22
SHEET 4 AB2 8 ALA I 30 ILE I 35 1 N ALA I 30 O VAL I 58
SHEET 5 AB2 8 TRP I 108 HIS I 113 1 O PHE I 111 N GLN I 33
SHEET 6 AB2 8 GLY I 133 CYS I 137 1 O ALA I 135 N VAL I 110
SHEET 7 AB2 8 ILE I 244 GLY I 249 1 O VAL I 245 N LEU I 136
SHEET 8 AB2 8 VAL I 275 TYR I 280 1 O HIS I 278 N LEU I 246
SHEET 1 AB3 8 LEU J 3 THR J 9 0
SHEET 2 AB3 8 ALA J 16 TYR J 22 -1 O ALA J 19 N ILE J 6
SHEET 3 AB3 8 PHE J 57 ASP J 63 -1 O VAL J 59 N TYR J 22
SHEET 4 AB3 8 ALA J 30 ILE J 35 1 N ALA J 30 O VAL J 58
SHEET 5 AB3 8 TRP J 108 HIS J 113 1 O PHE J 111 N GLN J 33
SHEET 6 AB3 8 GLY J 133 CYS J 137 1 O ALA J 135 N VAL J 110
SHEET 7 AB3 8 ILE J 244 GLY J 249 1 O VAL J 245 N LEU J 136
SHEET 8 AB3 8 VAL J 275 TYR J 280 1 O GLU J 276 N ILE J 244
SHEET 1 AB4 8 LEU K 3 THR K 9 0
SHEET 2 AB4 8 ALA K 16 TYR K 22 -1 O ILE K 17 N PHE K 8
SHEET 3 AB4 8 PHE K 57 ASP K 63 -1 O VAL K 59 N TYR K 22
SHEET 4 AB4 8 ALA K 30 ILE K 35 1 N ALA K 30 O VAL K 58
SHEET 5 AB4 8 TRP K 108 HIS K 113 1 O PHE K 111 N GLN K 33
SHEET 6 AB4 8 GLY K 133 CYS K 137 1 O CYS K 137 N GLY K 112
SHEET 7 AB4 8 ILE K 244 GLY K 249 1 O VAL K 245 N LEU K 134
SHEET 8 AB4 8 VAL K 275 TYR K 280 1 O TYR K 280 N ALA K 248
SHEET 1 AB5 8 LEU L 3 THR L 9 0
SHEET 2 AB5 8 ALA L 16 TYR L 22 -1 O ILE L 17 N PHE L 8
SHEET 3 AB5 8 PHE L 57 ASP L 63 -1 O VAL L 59 N TYR L 22
SHEET 4 AB5 8 ALA L 30 ILE L 35 1 N ALA L 30 O VAL L 58
SHEET 5 AB5 8 TRP L 108 HIS L 113 1 O PHE L 111 N GLN L 33
SHEET 6 AB5 8 GLY L 133 CYS L 137 1 O ALA L 135 N VAL L 110
SHEET 7 AB5 8 ILE L 244 GLY L 249 1 O VAL L 245 N LEU L 136
SHEET 8 AB5 8 VAL L 275 TYR L 280 1 O HIS L 278 N LEU L 246
SHEET 1 AB6 8 LEU M 3 THR M 9 0
SHEET 2 AB6 8 ALA M 16 TYR M 22 -1 O ALA M 19 N ILE M 6
SHEET 3 AB6 8 PHE M 57 ASP M 63 -1 O VAL M 59 N TYR M 22
SHEET 4 AB6 8 ALA M 30 ILE M 35 1 N ALA M 30 O VAL M 58
SHEET 5 AB6 8 TRP M 108 HIS M 113 1 O PHE M 111 N GLN M 33
SHEET 6 AB6 8 GLY M 133 CYS M 137 1 O ALA M 135 N VAL M 110
SHEET 7 AB6 8 ILE M 244 GLY M 249 1 O VAL M 245 N LEU M 134
SHEET 8 AB6 8 VAL M 275 TYR M 280 1 O GLU M 276 N LEU M 246
SHEET 1 AB7 8 LEU N 3 THR N 9 0
SHEET 2 AB7 8 ALA N 16 TYR N 22 -1 O ILE N 17 N PHE N 8
SHEET 3 AB7 8 VAL N 58 ASP N 62 -1 O VAL N 59 N TYR N 22
SHEET 4 AB7 8 VAL N 31 ILE N 35 1 N VAL N 32 O VAL N 58
SHEET 5 AB7 8 TRP N 108 HIS N 113 1 O PHE N 111 N GLN N 33
SHEET 6 AB7 8 GLY N 133 CYS N 137 1 O ALA N 135 N VAL N 110
SHEET 7 AB7 8 ILE N 244 GLY N 249 1 O VAL N 245 N LEU N 136
SHEET 8 AB7 8 VAL N 275 TYR N 280 1 O HIS N 278 N LEU N 246
SHEET 1 AB8 8 LEU O 3 GLU O 5 0
SHEET 2 AB8 8 ALA O 19 TYR O 22 -1 O ALA O 21 N GLN O 4
SHEET 3 AB8 8 PHE O 57 ASP O 62 -1 O VAL O 59 N TYR O 22
SHEET 4 AB8 8 ALA O 30 ILE O 35 1 N VAL O 32 O VAL O 58
SHEET 5 AB8 8 TRP O 108 HIS O 113 1 O PHE O 111 N GLN O 33
SHEET 6 AB8 8 GLY O 133 CYS O 137 1 O ALA O 135 N VAL O 110
SHEET 7 AB8 8 ILE O 244 GLY O 249 1 O VAL O 245 N LEU O 134
SHEET 8 AB8 8 VAL O 275 TYR O 280 1 O HIS O 278 N LEU O 246
SHEET 1 AB9 2 PHE O 8 THR O 9 0
SHEET 2 AB9 2 ALA O 16 ILE O 17 -1 O ILE O 17 N PHE O 8
SHEET 1 AC1 8 LEU P 3 GLU P 5 0
SHEET 2 AC1 8 ALA P 19 TYR P 22 -1 O ALA P 21 N GLN P 4
SHEET 3 AC1 8 PHE P 57 ASP P 62 -1 O VAL P 59 N TYR P 22
SHEET 4 AC1 8 ALA P 30 ILE P 35 1 N ALA P 30 O VAL P 58
SHEET 5 AC1 8 TRP P 108 HIS P 113 1 O PHE P 111 N GLN P 33
SHEET 6 AC1 8 GLY P 133 CYS P 137 1 O ALA P 135 N VAL P 110
SHEET 7 AC1 8 ILE P 244 GLY P 249 1 O VAL P 245 N LEU P 136
SHEET 8 AC1 8 VAL P 275 TYR P 280 1 O HIS P 278 N LEU P 246
SHEET 1 AC2 2 PHE P 8 THR P 9 0
SHEET 2 AC2 2 ALA P 16 ILE P 17 -1 O ILE P 17 N PHE P 8
SHEET 1 AC3 8 LEU Q 3 THR Q 9 0
SHEET 2 AC3 8 ALA Q 16 TYR Q 22 -1 O ALA Q 21 N GLN Q 4
SHEET 3 AC3 8 PHE Q 57 ASP Q 62 -1 O ALA Q 61 N TRP Q 20
SHEET 4 AC3 8 ALA Q 30 ILE Q 35 1 N VAL Q 32 O VAL Q 58
SHEET 5 AC3 8 TRP Q 108 HIS Q 113 1 O PHE Q 111 N GLN Q 33
SHEET 6 AC3 8 GLY Q 133 CYS Q 137 1 O ALA Q 135 N VAL Q 110
SHEET 7 AC3 8 ILE Q 244 GLY Q 249 1 O PHE Q 247 N LEU Q 136
SHEET 8 AC3 8 VAL Q 275 TYR Q 280 1 O HIS Q 278 N LEU Q 246
SHEET 1 AC4 8 LEU R 3 THR R 9 0
SHEET 2 AC4 8 ALA R 16 TYR R 22 -1 O ALA R 19 N ILE R 6
SHEET 3 AC4 8 VAL R 58 ASP R 62 -1 O VAL R 59 N TYR R 22
SHEET 4 AC4 8 VAL R 31 ILE R 35 1 N VAL R 32 O VAL R 58
SHEET 5 AC4 8 TRP R 108 HIS R 113 1 O PHE R 111 N GLN R 33
SHEET 6 AC4 8 GLY R 133 CYS R 137 1 O ALA R 135 N VAL R 110
SHEET 7 AC4 8 ILE R 244 GLY R 249 1 O PHE R 247 N LEU R 136
SHEET 8 AC4 8 VAL R 275 TYR R 280 1 O GLU R 276 N LEU R 246
SHEET 1 AC5 8 LEU S 3 THR S 9 0
SHEET 2 AC5 8 ALA S 16 TYR S 22 -1 O ILE S 17 N PHE S 8
SHEET 3 AC5 8 PHE S 57 ASP S 63 -1 O VAL S 59 N TYR S 22
SHEET 4 AC5 8 ALA S 30 ILE S 35 1 N ALA S 30 O VAL S 58
SHEET 5 AC5 8 TRP S 108 HIS S 113 1 O PHE S 111 N GLN S 33
SHEET 6 AC5 8 GLY S 133 CYS S 137 1 O ALA S 135 N VAL S 110
SHEET 7 AC5 8 ILE S 244 GLY S 249 1 O VAL S 245 N LEU S 134
SHEET 8 AC5 8 VAL S 275 TYR S 280 1 O HIS S 278 N LEU S 246
SHEET 1 AC6 8 LEU T 3 THR T 9 0
SHEET 2 AC6 8 ALA T 16 TYR T 22 -1 O ILE T 17 N PHE T 8
SHEET 3 AC6 8 PHE T 57 ASP T 63 -1 O VAL T 59 N TYR T 22
SHEET 4 AC6 8 ALA T 30 ILE T 35 1 N ALA T 30 O VAL T 58
SHEET 5 AC6 8 TRP T 108 HIS T 113 1 O PHE T 111 N GLN T 33
SHEET 6 AC6 8 GLY T 133 CYS T 137 1 O ALA T 135 N VAL T 110
SHEET 7 AC6 8 ILE T 244 GLY T 249 1 O PHE T 247 N LEU T 136
SHEET 8 AC6 8 VAL T 275 TYR T 280 1 O TYR T 280 N ALA T 248
SHEET 1 AC7 8 LEU U 3 GLU U 5 0
SHEET 2 AC7 8 ALA U 19 TYR U 22 -1 O ALA U 21 N GLN U 4
SHEET 3 AC7 8 PHE U 57 ASP U 62 -1 O VAL U 59 N TYR U 22
SHEET 4 AC7 8 ALA U 30 ILE U 35 1 N VAL U 32 O VAL U 58
SHEET 5 AC7 8 TRP U 108 HIS U 113 1 O PHE U 111 N GLN U 33
SHEET 6 AC7 8 GLY U 133 CYS U 137 1 O ALA U 135 N VAL U 110
SHEET 7 AC7 8 ILE U 244 GLY U 249 1 O PHE U 247 N LEU U 136
SHEET 8 AC7 8 VAL U 275 TYR U 280 1 O HIS U 278 N LEU U 246
SHEET 1 AC8 2 PHE U 8 THR U 9 0
SHEET 2 AC8 2 ALA U 16 ILE U 17 -1 O ILE U 17 N PHE U 8
SHEET 1 AC9 8 LEU V 3 THR V 9 0
SHEET 2 AC9 8 ALA V 16 TYR V 22 -1 O ILE V 17 N PHE V 8
SHEET 3 AC9 8 PHE V 57 ASP V 62 -1 O ALA V 61 N TRP V 20
SHEET 4 AC9 8 ALA V 30 ILE V 35 1 N ILE V 34 O ILE V 60
SHEET 5 AC9 8 TRP V 108 HIS V 113 1 O PHE V 111 N GLN V 33
SHEET 6 AC9 8 GLY V 133 CYS V 137 1 O ALA V 135 N VAL V 110
SHEET 7 AC9 8 ILE V 244 GLY V 249 1 O VAL V 245 N LEU V 134
SHEET 8 AC9 8 VAL V 275 TYR V 280 1 O GLU V 276 N ILE V 244
SHEET 1 AD1 8 LEU X 3 GLU X 5 0
SHEET 2 AD1 8 ALA X 19 TYR X 22 -1 O ALA X 21 N GLN X 4
SHEET 3 AD1 8 VAL X 58 ASP X 62 -1 O VAL X 59 N TYR X 22
SHEET 4 AD1 8 VAL X 31 ILE X 35 1 N VAL X 32 O VAL X 58
SHEET 5 AD1 8 TRP X 108 HIS X 113 1 O PHE X 111 N GLN X 33
SHEET 6 AD1 8 GLY X 133 CYS X 137 1 O ALA X 135 N VAL X 110
SHEET 7 AD1 8 ILE X 244 GLY X 249 1 O PHE X 247 N LEU X 136
SHEET 8 AD1 8 VAL X 275 TYR X 280 1 O HIS X 278 N LEU X 246
SHEET 1 AD2 2 PHE X 8 THR X 9 0
SHEET 2 AD2 2 ALA X 16 ILE X 17 -1 O ILE X 17 N PHE X 8
SHEET 1 AD3 8 LEU Y 3 THR Y 9 0
SHEET 2 AD3 8 ALA Y 16 TYR Y 22 -1 O ALA Y 21 N GLN Y 4
SHEET 3 AD3 8 VAL Y 58 ASP Y 63 -1 O VAL Y 59 N TYR Y 22
SHEET 4 AD3 8 VAL Y 31 ILE Y 35 1 N VAL Y 32 O VAL Y 58
SHEET 5 AD3 8 TRP Y 108 HIS Y 113 1 O VAL Y 109 N VAL Y 31
SHEET 6 AD3 8 GLY Y 133 CYS Y 137 1 O CYS Y 137 N GLY Y 112
SHEET 7 AD3 8 ILE Y 244 GLY Y 249 1 O VAL Y 245 N LEU Y 136
SHEET 8 AD3 8 VAL Y 275 TYR Y 280 1 O GLU Y 276 N LEU Y 246
SHEET 1 AD4 8 LEU W 3 THR W 9 0
SHEET 2 AD4 8 ALA W 16 TYR W 22 -1 O ILE W 17 N PHE W 8
SHEET 3 AD4 8 PHE W 57 ASP W 62 -1 O VAL W 59 N TYR W 22
SHEET 4 AD4 8 ALA W 30 ILE W 35 1 N VAL W 32 O VAL W 58
SHEET 5 AD4 8 TRP W 108 HIS W 113 1 O PHE W 111 N GLN W 33
SHEET 6 AD4 8 GLY W 133 CYS W 137 1 O ALA W 135 N VAL W 110
SHEET 7 AD4 8 ILE W 244 GLY W 249 1 O VAL W 245 N LEU W 136
SHEET 8 AD4 8 VAL W 275 TYR W 280 1 O HIS W 278 N LEU W 246
SHEET 1 AD5 8 LEU Z 3 THR Z 9 0
SHEET 2 AD5 8 ALA Z 16 TYR Z 22 -1 O ILE Z 17 N PHE Z 8
SHEET 3 AD5 8 PHE Z 57 ASP Z 63 -1 O VAL Z 59 N TYR Z 22
SHEET 4 AD5 8 ALA Z 30 ILE Z 35 1 N VAL Z 32 O VAL Z 58
SHEET 5 AD5 8 TRP Z 108 HIS Z 113 1 O PHE Z 111 N GLN Z 33
SHEET 6 AD5 8 GLY Z 133 CYS Z 137 1 O ALA Z 135 N VAL Z 110
SHEET 7 AD5 8 ILE Z 244 GLY Z 249 1 O VAL Z 245 N LEU Z 134
SHEET 8 AD5 8 VAL Z 275 TYR Z 280 1 O TYR Z 280 N ALA Z 248
LINK OG SER L 114 C4 DKF L 900 1555 1555 1.41
SITE 1 AC1 6 GLY A 37 LEU A 38 SER A 114 TRP A 115
SITE 2 AC1 6 PHE A 176 TRP A 192
SITE 1 AC2 6 GLY B 37 LEU B 38 SER B 114 TRP B 115
SITE 2 AC2 6 TRP B 192 HIS B 203
SITE 1 AC3 4 LEU C 38 SER C 114 TRP C 115 TRP C 192
SITE 1 AC4 6 LEU D 38 SER D 114 TRP D 115 TRP D 192
SITE 2 AC4 6 HIS D 285 HOH D1123
SITE 1 AC5 6 LEU E 38 SER E 114 PHE E 176 TRP E 192
SITE 2 AC5 6 PHE E 211 HIS E 285
SITE 1 AC6 6 LEU F 38 SER F 114 TRP F 115 PHE F 176
SITE 2 AC6 6 TRP F 192 HIS F 285
SITE 1 AC7 3 LEU G 38 SER G 114 TRP G 192
SITE 1 AC8 6 GLY H 37 LEU H 38 SER H 114 TRP H 192
SITE 2 AC8 6 HIS H 285 HOH H1095
SITE 1 AC9 6 LEU I 38 SER I 114 TRP I 115 PHE I 176
SITE 2 AC9 6 TRP I 192 HIS I 285
SITE 1 AD1 5 LEU J 38 SER J 114 TRP J 115 PHE J 176
SITE 2 AD1 5 TRP J 192
SITE 1 AD2 6 LEU K 38 SER K 114 TRP K 115 PHE K 176
SITE 2 AD2 6 TRP K 192 PHE K 211
SITE 1 AD3 7 LEU M 38 SER M 114 TRP M 115 PHE M 176
SITE 2 AD3 7 TRP M 192 PHE M 211 HIS M 285
SITE 1 AD4 6 LEU N 38 SER N 114 TRP N 115 PHE N 176
SITE 2 AD4 6 TRP N 192 HIS N 285
SITE 1 AD5 4 LEU O 38 SER O 114 PHE O 176 TRP O 192
SITE 1 AD6 5 LEU P 38 SER P 114 TRP P 115 TRP P 192
SITE 2 AD6 5 HIS P 285
SITE 1 AD7 5 LEU Q 38 SER Q 114 TRP Q 115 PHE Q 176
SITE 2 AD7 5 TRP Q 192
SITE 1 AD8 5 LEU R 38 SER R 114 TRP R 115 TRP R 192
SITE 2 AD8 5 PHE R 211
SITE 1 AD9 3 LEU S 38 SER S 114 HIS S 285
SITE 1 AE1 5 LEU T 38 SER T 114 PHE T 176 TRP T 192
SITE 2 AE1 5 HIS T 285
SITE 1 AE2 3 LEU U 38 SER U 114 TRP U 192
SITE 1 AE3 5 LEU V 38 SER V 114 TRP V 192 PHE V 211
SITE 2 AE3 5 HIS V 285
SITE 1 AE4 6 LEU X 38 SER X 114 TRP X 115 PHE X 176
SITE 2 AE4 6 TRP X 192 HIS X 285
SITE 1 AE5 5 LEU Y 38 SER Y 114 PHE Y 176 TRP Y 192
SITE 2 AE5 5 HIS Y 285
SITE 1 AE6 4 LEU W 38 SER W 114 TRP W 192 HIS W 285
SITE 1 AE7 5 GLY Z 37 LEU Z 38 SER Z 114 TRP Z 192
SITE 2 AE7 5 HIS Z 285
SITE 1 AE8 10 LEU L 38 HIS L 113 TRP L 115 GLY L 116
SITE 2 AE8 10 SER L 117 MET L 118 CYS L 137 GLY L 138
SITE 3 AE8 10 TRP L 192 HIS L 285
CRYST1 185.857 185.857 205.099 90.00 90.00 120.00 P 31 78
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 0.005380 0.003106 0.000000 0.00000
SCALE2 0.000000 0.006213 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004876 0.00000
TER 2361 ARG A 311
TER 4711 ASN B 310
TER 7061 ASN C 310
TER 9403 ALA D 309
TER 11775 ARG E 312
TER 14117 ALA F 309
TER 16478 ARG G 311
TER 18828 ASN H 310
TER 21200 ARG I 312
TER 23561 ARG J 311
TER 25941 ILE K 313
TER 28321 ILE L 313
TER 30671 ASN M 310
TER 33032 ARG N 311
TER 35393 ARG O 311
TER 37754 ARG P 311
TER 40126 ARG Q 312
TER 42476 ASN R 310
TER 44837 ARG S 311
TER 47187 ASN T 310
TER 49548 ARG U 311
TER 51898 ASN V 310
TER 54248 ASN X 310
TER 56598 ASN Y 310
TER 58959 ARG W 311
TER 61309 ASN Z 310
MASTER 784 0 26 403 222 0 47 664002 26 205 650
END |