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HEADER TOXIN 03-OCT-18 6II2
TITLE CRYSTAL STRUCTURE OF ALPHA-BETA HYDROLASE (ABH) AND MAKES CATERPILLARS
TITLE 2 FLOPPY (MCF)-LIKE EFFECTORS OF VIBRIO VULNIFICUS MO6-24/O
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE RTX-TOXIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: ABH-MCF;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO VULNIFICUS;
SOURCE 3 ORGANISM_TAXID: 672;
SOURCE 4 GENE: RTXA1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ABH-MCF, MARTX TOXIN, EFFECTOR DOMAIN, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LEE,B.S.KIM,S.CHOI,E.Y.LEE,S.PARK,J.HWANG,Y.KWON,J.HYUNG,C.LEE,
AUTHOR 2 S.H.EOM,M.H.KIM
REVDAT 1 07-AUG-19 6II2 0
JRNL AUTH Y.LEE,B.S.KIM,S.CHOI,E.Y.LEE,S.PARK,J.HWANG,Y.KWON,J.HYUNG,
JRNL AUTH 2 C.LEE,S.H.EOM,M.H.KIM
JRNL TITL CRYSTAL STRUCTURE OF PATHOGENIC BACTERIAL TOXIN AB
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 77.5
REMARK 3 NUMBER OF REFLECTIONS : 29984
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) : 0.287
REMARK 3 R VALUE (WORKING SET) : 0.285
REMARK 3 FREE R VALUE : 0.327
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1514
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 435
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 15.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.3700
REMARK 3 BIN FREE R VALUE SET COUNT : 18
REMARK 3 BIN FREE R VALUE : 0.4120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17825
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.60000
REMARK 3 B22 (A**2) : 0.84000
REMARK 3 B33 (A**2) : -0.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.978
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.746
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.181
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.785
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.752
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 18098 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 16905 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24375 ; 1.195 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 39307 ; 0.808 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2299 ; 8.166 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 821 ;37.085 ;25.323
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3184 ;16.164 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;16.598 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2697 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20262 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3442 ; 0.002 ; 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): 9298 ; 3.067 ; 6.026
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 9297 ; 3.066 ; 6.026
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11563 ; 5.344 ; 9.018
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 11564 ; 5.344 ; 9.019
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8800 ; 2.395 ; 6.155
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 8801 ; 2.395 ; 6.156
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 12813 ; 4.413 ; 9.198
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 20196 ; 9.652 ;71.467
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 20197 ; 9.651 ;71.466
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
REMARK 4
REMARK 4 6II2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1300009234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34303
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
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 (%) : 89.9
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 6II6 AND 6IMP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 4000, 0.1M TRIS-HCL (PH 8.5),
REMARK 280 0.2M LI2SO4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 43.10750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 167.36850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.29650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 167.36850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.10750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.29650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 2901
REMARK 465 SER A 2902
REMARK 465 GLY A 2903
REMARK 465 ASN A 2904
REMARK 465 GLU A 2905
REMARK 465 LYS A 2906
REMARK 465 HIS A 2907
REMARK 465 LYS A 2908
REMARK 465 ASN A 2961
REMARK 465 GLY A 2962
REMARK 465 GLU A 2963
REMARK 465 SER A 2987
REMARK 465 GLU A 2988
REMARK 465 GLY A 2989
REMARK 465 GLU A 2990
REMARK 465 THR A 2991
REMARK 465 SER A 2992
REMARK 465 ALA A 2993
REMARK 465 THR A 2994
REMARK 465 ARG A 3226
REMARK 465 TYR A 3227
REMARK 465 GLY A 3228
REMARK 465 ASP A 3229
REMARK 465 ALA A 3230
REMARK 465 LEU A 3231
REMARK 465 LYS A 3232
REMARK 465 PRO A 3233
REMARK 465 ASP A 3234
REMARK 465 THR A 3235
REMARK 465 SER A 3236
REMARK 465 VAL A 3237
REMARK 465 PRO A 3238
REMARK 465 GLY A 3239
REMARK 465 LYS A 3240
REMARK 465 SER A 3241
REMARK 465 LYS A 3242
REMARK 465 ASP A 3243
REMARK 465 LEU A 3340
REMARK 465 ASN A 3341
REMARK 465 LEU A 3342
REMARK 465 SER A 3343
REMARK 465 ASN A 3344
REMARK 465 ASP A 3345
REMARK 465 GLY A 3346
REMARK 465 PHE A 3347
REMARK 465 GLY A 3348
REMARK 465 GLY A 3349
REMARK 465 ARG A 3350
REMARK 465 THR A 3563
REMARK 465 PRO A 3564
REMARK 465 MET A 3565
REMARK 465 LYS A 3566
REMARK 465 LYS A 3567
REMARK 465 PRO A 3568
REMARK 465 GLY A 3569
REMARK 465 THR A 3570
REMARK 465 SER A 3571
REMARK 465 ASP A 3572
REMARK 465 VAL A 3573
REMARK 465 ASP A 3574
REMARK 465 GLY A 3575
REMARK 465 ASN A 3576
REMARK 465 ALA A 3577
REMARK 465 LYS A 3578
REMARK 465 ALA A 3579
REMARK 465 VAL A 3580
REMARK 465 ASP A 3581
REMARK 465 ASP A 3582
REMARK 465 THR A 3583
REMARK 465 LYS A 3584
REMARK 465 GLU A 3585
REMARK 465 ALA A 3586
REMARK 465 LEU A 3587
REMARK 465 GLU A 3588
REMARK 465 HIS A 3589
REMARK 465 HIS A 3590
REMARK 465 HIS A 3591
REMARK 465 HIS A 3592
REMARK 465 HIS A 3593
REMARK 465 HIS A 3594
REMARK 465 MET B 2901
REMARK 465 SER B 2902
REMARK 465 GLY B 2903
REMARK 465 ASN B 2904
REMARK 465 GLU B 2905
REMARK 465 LYS B 2906
REMARK 465 HIS B 2907
REMARK 465 LYS B 2908
REMARK 465 GLU B 2960
REMARK 465 ASN B 2961
REMARK 465 GLY B 2962
REMARK 465 GLU B 2963
REMARK 465 GLU B 2988
REMARK 465 GLY B 2989
REMARK 465 GLU B 2990
REMARK 465 THR B 2991
REMARK 465 SER B 2992
REMARK 465 ALA B 2993
REMARK 465 THR B 2994
REMARK 465 VAL B 3116
REMARK 465 ALA B 3117
REMARK 465 ASN B 3118
REMARK 465 PRO B 3119
REMARK 465 ALA B 3120
REMARK 465 TYR B 3227
REMARK 465 GLY B 3228
REMARK 465 ASP B 3229
REMARK 465 ALA B 3230
REMARK 465 LEU B 3231
REMARK 465 LYS B 3232
REMARK 465 PRO B 3233
REMARK 465 ASP B 3234
REMARK 465 THR B 3235
REMARK 465 SER B 3236
REMARK 465 VAL B 3237
REMARK 465 PRO B 3238
REMARK 465 GLY B 3239
REMARK 465 LYS B 3240
REMARK 465 SER B 3241
REMARK 465 LYS B 3242
REMARK 465 ASN B 3341
REMARK 465 LEU B 3342
REMARK 465 SER B 3343
REMARK 465 ASN B 3344
REMARK 465 ASP B 3345
REMARK 465 GLY B 3346
REMARK 465 PHE B 3347
REMARK 465 GLY B 3348
REMARK 465 GLY B 3349
REMARK 465 ARG B 3350
REMARK 465 THR B 3563
REMARK 465 PRO B 3564
REMARK 465 MET B 3565
REMARK 465 LYS B 3566
REMARK 465 LYS B 3567
REMARK 465 PRO B 3568
REMARK 465 GLY B 3569
REMARK 465 THR B 3570
REMARK 465 SER B 3571
REMARK 465 ASP B 3572
REMARK 465 VAL B 3573
REMARK 465 ASP B 3574
REMARK 465 GLY B 3575
REMARK 465 ASN B 3576
REMARK 465 ALA B 3577
REMARK 465 LYS B 3578
REMARK 465 ALA B 3579
REMARK 465 VAL B 3580
REMARK 465 ASP B 3581
REMARK 465 ASP B 3582
REMARK 465 THR B 3583
REMARK 465 LYS B 3584
REMARK 465 GLU B 3585
REMARK 465 ALA B 3586
REMARK 465 LEU B 3587
REMARK 465 GLU B 3588
REMARK 465 HIS B 3589
REMARK 465 HIS B 3590
REMARK 465 HIS B 3591
REMARK 465 HIS B 3592
REMARK 465 HIS B 3593
REMARK 465 HIS B 3594
REMARK 465 MET C 2901
REMARK 465 SER C 2902
REMARK 465 GLY C 2903
REMARK 465 ASN C 2904
REMARK 465 GLU C 2905
REMARK 465 LYS C 2906
REMARK 465 HIS C 2907
REMARK 465 LYS C 2908
REMARK 465 GLU C 2909
REMARK 465 GLU C 2960
REMARK 465 ASN C 2961
REMARK 465 GLY C 2962
REMARK 465 GLU C 2963
REMARK 465 SER C 2964
REMARK 465 GLU C 2988
REMARK 465 GLY C 2989
REMARK 465 GLU C 2990
REMARK 465 THR C 2991
REMARK 465 SER C 2992
REMARK 465 ALA C 2993
REMARK 465 THR C 2994
REMARK 465 SER C 2995
REMARK 465 ASP C 3223
REMARK 465 PHE C 3224
REMARK 465 LYS C 3225
REMARK 465 ARG C 3226
REMARK 465 TYR C 3227
REMARK 465 GLY C 3228
REMARK 465 ASP C 3229
REMARK 465 ALA C 3230
REMARK 465 LEU C 3231
REMARK 465 LYS C 3232
REMARK 465 PRO C 3233
REMARK 465 ASP C 3234
REMARK 465 THR C 3235
REMARK 465 SER C 3236
REMARK 465 VAL C 3237
REMARK 465 PRO C 3238
REMARK 465 GLY C 3239
REMARK 465 LYS C 3240
REMARK 465 SER C 3241
REMARK 465 LYS C 3242
REMARK 465 ASP C 3243
REMARK 465 ILE C 3244
REMARK 465 ARG C 3245
REMARK 465 THR C 3246
REMARK 465 THR C 3247
REMARK 465 ASP C 3264
REMARK 465 GLY C 3265
REMARK 465 PHE C 3266
REMARK 465 ARG C 3267
REMARK 465 SER C 3268
REMARK 465 ASP C 3269
REMARK 465 MET C 3270
REMARK 465 VAL C 3280
REMARK 465 LYS C 3281
REMARK 465 GLY C 3282
REMARK 465 SER C 3283
REMARK 465 TRP C 3284
REMARK 465 SER C 3321
REMARK 465 ALA C 3322
REMARK 465 GLY C 3323
REMARK 465 VAL C 3324
REMARK 465 VAL C 3325
REMARK 465 ASP C 3326
REMARK 465 MET C 3338
REMARK 465 LEU C 3339
REMARK 465 LEU C 3340
REMARK 465 ASN C 3341
REMARK 465 LEU C 3342
REMARK 465 SER C 3343
REMARK 465 ASN C 3344
REMARK 465 ASP C 3345
REMARK 465 GLY C 3346
REMARK 465 PHE C 3347
REMARK 465 GLY C 3348
REMARK 465 GLY C 3349
REMARK 465 ARG C 3350
REMARK 465 MET C 3417
REMARK 465 HIS C 3418
REMARK 465 ASP C 3419
REMARK 465 THR C 3420
REMARK 465 SER C 3421
REMARK 465 MET C 3422
REMARK 465 LYS C 3423
REMARK 465 ALA C 3447
REMARK 465 SER C 3448
REMARK 465 ALA C 3449
REMARK 465 ASN C 3450
REMARK 465 GLY C 3451
REMARK 465 ASN C 3520
REMARK 465 ASP C 3521
REMARK 465 ALA C 3522
REMARK 465 GLY C 3523
REMARK 465 THR C 3563
REMARK 465 PRO C 3564
REMARK 465 MET C 3565
REMARK 465 LYS C 3566
REMARK 465 LYS C 3567
REMARK 465 PRO C 3568
REMARK 465 GLY C 3569
REMARK 465 THR C 3570
REMARK 465 SER C 3571
REMARK 465 ASP C 3572
REMARK 465 VAL C 3573
REMARK 465 ASP C 3574
REMARK 465 GLY C 3575
REMARK 465 ASN C 3576
REMARK 465 ALA C 3577
REMARK 465 LYS C 3578
REMARK 465 ALA C 3579
REMARK 465 VAL C 3580
REMARK 465 ASP C 3581
REMARK 465 ASP C 3582
REMARK 465 THR C 3583
REMARK 465 LYS C 3584
REMARK 465 GLU C 3585
REMARK 465 ALA C 3586
REMARK 465 LEU C 3587
REMARK 465 GLU C 3588
REMARK 465 HIS C 3589
REMARK 465 HIS C 3590
REMARK 465 HIS C 3591
REMARK 465 HIS C 3592
REMARK 465 HIS C 3593
REMARK 465 HIS C 3594
REMARK 465 MET D 2901
REMARK 465 SER D 2902
REMARK 465 GLY D 2903
REMARK 465 ASN D 2904
REMARK 465 GLU D 2905
REMARK 465 LYS D 2906
REMARK 465 HIS D 2907
REMARK 465 LYS D 2908
REMARK 465 GLU D 2960
REMARK 465 ASN D 2961
REMARK 465 GLY D 2962
REMARK 465 GLU D 2963
REMARK 465 ALA D 2985
REMARK 465 SER D 2986
REMARK 465 SER D 2987
REMARK 465 GLU D 2988
REMARK 465 GLY D 2989
REMARK 465 GLU D 2990
REMARK 465 THR D 2991
REMARK 465 SER D 2992
REMARK 465 ALA D 2993
REMARK 465 THR D 2994
REMARK 465 GLY D 3228
REMARK 465 ASP D 3229
REMARK 465 ALA D 3230
REMARK 465 LEU D 3231
REMARK 465 LYS D 3232
REMARK 465 PRO D 3233
REMARK 465 ASP D 3234
REMARK 465 THR D 3235
REMARK 465 SER D 3236
REMARK 465 VAL D 3237
REMARK 465 PRO D 3238
REMARK 465 GLY D 3239
REMARK 465 LYS D 3240
REMARK 465 SER D 3241
REMARK 465 LYS D 3242
REMARK 465 ASP D 3243
REMARK 465 LEU D 3339
REMARK 465 LEU D 3340
REMARK 465 ASN D 3341
REMARK 465 LEU D 3342
REMARK 465 SER D 3343
REMARK 465 ASN D 3344
REMARK 465 ASP D 3345
REMARK 465 GLY D 3346
REMARK 465 PHE D 3347
REMARK 465 GLY D 3348
REMARK 465 GLY D 3349
REMARK 465 ARG D 3350
REMARK 465 ASP D 3367
REMARK 465 GLY D 3368
REMARK 465 GLN D 3369
REMARK 465 VAL D 3370
REMARK 465 ASN D 3389
REMARK 465 PRO D 3390
REMARK 465 THR D 3391
REMARK 465 LEU D 3392
REMARK 465 MET D 3417
REMARK 465 HIS D 3418
REMARK 465 ASP D 3419
REMARK 465 THR D 3420
REMARK 465 SER D 3421
REMARK 465 MET D 3422
REMARK 465 LYS D 3423
REMARK 465 VAL D 3424
REMARK 465 TRP D 3425
REMARK 465 GLN D 3426
REMARK 465 GLU D 3427
REMARK 465 LYS D 3428
REMARK 465 LEU D 3429
REMARK 465 GLU D 3430
REMARK 465 GLY D 3431
REMARK 465 LYS D 3432
REMARK 465 GLN D 3433
REMARK 465 ALA D 3434
REMARK 465 LEU D 3435
REMARK 465 THR D 3436
REMARK 465 ILE D 3444
REMARK 465 THR D 3445
REMARK 465 ASP D 3446
REMARK 465 ALA D 3447
REMARK 465 SER D 3448
REMARK 465 ALA D 3449
REMARK 465 ASN D 3450
REMARK 465 GLY D 3451
REMARK 465 LYS D 3470
REMARK 465 GLY D 3471
REMARK 465 SER D 3472
REMARK 465 GLY D 3473
REMARK 465 ASP D 3474
REMARK 465 LYS D 3506
REMARK 465 SER D 3507
REMARK 465 ASP D 3508
REMARK 465 LEU D 3509
REMARK 465 ASN D 3510
REMARK 465 MET D 3511
REMARK 465 ALA D 3512
REMARK 465 GLN D 3513
REMARK 465 SER D 3514
REMARK 465 TYR D 3515
REMARK 465 LYS D 3516
REMARK 465 LEU D 3517
REMARK 465 GLY D 3518
REMARK 465 LYS D 3519
REMARK 465 ASN D 3520
REMARK 465 ASP D 3521
REMARK 465 ALA D 3522
REMARK 465 GLY D 3523
REMARK 465 GLU D 3524
REMARK 465 ALA D 3525
REMARK 465 ILE D 3526
REMARK 465 PHE D 3527
REMARK 465 PRO D 3543
REMARK 465 THR D 3544
REMARK 465 PHE D 3545
REMARK 465 GLY D 3546
REMARK 465 ASP D 3547
REMARK 465 LYS D 3548
REMARK 465 THR D 3549
REMARK 465 THR D 3550
REMARK 465 ASP D 3561
REMARK 465 ALA D 3562
REMARK 465 THR D 3563
REMARK 465 PRO D 3564
REMARK 465 MET D 3565
REMARK 465 LYS D 3566
REMARK 465 LYS D 3567
REMARK 465 PRO D 3568
REMARK 465 GLY D 3569
REMARK 465 THR D 3570
REMARK 465 SER D 3571
REMARK 465 ASP D 3572
REMARK 465 VAL D 3573
REMARK 465 ASP D 3574
REMARK 465 GLY D 3575
REMARK 465 ASN D 3576
REMARK 465 ALA D 3577
REMARK 465 LYS D 3578
REMARK 465 ALA D 3579
REMARK 465 VAL D 3580
REMARK 465 ASP D 3581
REMARK 465 ASP D 3582
REMARK 465 THR D 3583
REMARK 465 LYS D 3584
REMARK 465 GLU D 3585
REMARK 465 ALA D 3586
REMARK 465 LEU D 3587
REMARK 465 GLU D 3588
REMARK 465 HIS D 3589
REMARK 465 HIS D 3590
REMARK 465 HIS D 3591
REMARK 465 HIS D 3592
REMARK 465 HIS D 3593
REMARK 465 HIS D 3594
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A2926 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 ARG A2945 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 GLY A3073 N - CA - C ANGL. DEV. = -18.7 DEGREES
REMARK 500 TYR A3074 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 MET A3338 N - CA - C ANGL. DEV. = -19.0 DEGREES
REMARK 500 ARG B3017 CB - CA - C ANGL. DEV. = -13.8 DEGREES
REMARK 500 PRO C2919 C - N - CD ANGL. DEV. = -12.9 DEGREES
REMARK 500 ASP C3065 N - CA - C ANGL. DEV. = 22.9 DEGREES
REMARK 500 GLU C3115 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 LYS C3516 N - CA - C ANGL. DEV. = -23.4 DEGREES
REMARK 500 ILE D3064 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 ARG D3102 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG D3102 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A2918 34.09 -144.05
REMARK 500 PRO A2919 -175.83 -67.47
REMARK 500 LEU A2926 -81.99 -123.73
REMARK 500 SER A3067 98.44 -164.32
REMARK 500 HIS A3072 72.68 42.70
REMARK 500 MET A3076 -52.30 71.38
REMARK 500 ALA A3117 -112.03 59.66
REMARK 500 ASN A3118 51.50 -153.66
REMARK 500 ALA A3206 66.78 -153.03
REMARK 500 GLU A3207 -120.88 60.94
REMARK 500 LYS A3281 -76.63 -92.66
REMARK 500 LEU A3337 66.43 33.83
REMARK 500 ALA A3485 22.07 -150.08
REMARK 500 ASP A3508 -73.68 -134.56
REMARK 500 VAL A3559 -56.11 -125.86
REMARK 500 PRO B2919 -178.89 -64.34
REMARK 500 SER B2925 -32.71 -133.82
REMARK 500 LEU B2926 -134.01 60.05
REMARK 500 PRO B3066 -141.34 24.07
REMARK 500 SER B3075 -123.45 55.03
REMARK 500 PHE B3204 -161.70 -175.51
REMARK 500 ALA B3206 80.04 -157.93
REMARK 500 GLU B3207 -126.71 62.43
REMARK 500 LEU B3339 -133.33 57.86
REMARK 500 ASN B3389 73.08 -151.80
REMARK 500 ASP B3419 146.93 -171.60
REMARK 500 THR B3420 33.97 -144.90
REMARK 500 ASP B3508 -75.86 -134.87
REMARK 500 VAL B3559 -62.66 -121.26
REMARK 500 LEU C2926 -128.98 64.14
REMARK 500 SER C3075 -122.83 52.62
REMARK 500 ALA C3117 -51.49 73.76
REMARK 500 ASN C3118 20.72 -154.50
REMARK 500 ALA C3206 71.55 -157.68
REMARK 500 GLU C3207 -120.87 58.73
REMARK 500 LYS C3328 41.94 -108.56
REMARK 500 ASP C3352 12.37 -142.69
REMARK 500 ALA C3485 29.76 -151.10
REMARK 500 ASP C3508 -75.81 -136.33
REMARK 500 VAL C3559 -67.24 -125.30
REMARK 500 ASN D2910 88.18 -157.07
REMARK 500 VAL D2911 -71.27 -141.20
REMARK 500 ILE D2913 -77.20 -132.50
REMARK 500 PRO D2919 -166.34 -66.35
REMARK 500 LEU D2926 -78.83 -114.47
REMARK 500 PRO D3066 -78.67 -133.71
REMARK 500 VAL D3116 50.29 39.86
REMARK 500 ALA D3206 73.08 -157.20
REMARK 500 GLU D3207 -122.16 57.13
REMARK 500 PHE D3224 -39.69 -39.02
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 3283 TRP A 3284 -147.98
REMARK 500 SER B 2927 PRO B 2928 -142.44
REMARK 500 SER B 3201 GLY B 3202 -62.81
REMARK 500 LEU B 3337 MET B 3338 61.87
REMARK 500 MET B 3338 LEU B 3339 -134.81
REMARK 500 SER C 2927 PRO C 2928 -146.77
REMARK 500 GLU C 3115 VAL C 3116 -144.28
REMARK 500 PHE C 3204 ASN C 3205 -148.40
REMARK 500 SER D 2927 PRO D 2928 -138.73
REMARK 500 GLY D 3077 GLY D 3078 129.20
REMARK 500 GLU D 3115 VAL D 3116 46.90
REMARK 500 TYR D 3393 SER D 3394 -33.82
REMARK 500 LEU D 3500 THR D 3501 148.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG D3102 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE HAS BEEN DEPOSITED TO DATABASE WITH THE NCBI ACCESSION
REMARK 999 ID WP_015728045.1. N-TERMIANL M IS THE INITIAL METHIONINE. RESIDUE
REMARK 999 C3351S REPRESENT MUTATION.
DBREF 6II2 A 2901 3594 PDB 6II2 6II2 2901 3594
DBREF 6II2 B 2901 3594 PDB 6II2 6II2 2901 3594
DBREF 6II2 C 2901 3594 PDB 6II2 6II2 2901 3594
DBREF 6II2 D 2901 3594 PDB 6II2 6II2 2901 3594
SEQRES 1 A 694 MET SER GLY ASN GLU LYS HIS LYS GLU ASN VAL ALA ILE
SEQRES 2 A 694 GLU ASN ASP GLY THR PRO PRO ARG ASP LYS GLU SER LEU
SEQRES 3 A 694 SER PRO LEU THR ARG PHE LEU ASN ASN GLU LEU TYR GLY
SEQRES 4 A 694 GLU LYS ASP ALA ARG ARG LYS ILE GLY GLU ILE THR GLN
SEQRES 5 A 694 THR LEU LEU ASP HIS ALA VAL GLU ASN GLY GLU SER GLN
SEQRES 6 A 694 LYS VAL THR LEU LYS GLY GLU VAL GLY ARG LEU THR GLY
SEQRES 7 A 694 TYR TYR HIS GLN GLY ALA ALA SER SER GLU GLY GLU THR
SEQRES 8 A 694 SER ALA THR SER GLY LYS VAL VAL LEU PHE LEU HIS GLY
SEQRES 9 A 694 SER GLY SER SER ALA GLU GLU GLN ALA SER GLU ILE ARG
SEQRES 10 A 694 ASN HIS TYR GLN LYS GLN GLY ILE ASP MET LEU ALA VAL
SEQRES 11 A 694 ASN LEU ARG GLY TYR GLY GLU SER ASP GLY GLY PRO SER
SEQRES 12 A 694 GLU LYS GLY LEU TYR GLN ASP ALA ARG THR MET PHE ASN
SEQRES 13 A 694 TYR LEU VAL ASN ASP LYS GLY ILE ASP PRO SER ASN ILE
SEQRES 14 A 694 ILE ILE HIS GLY TYR SER MET GLY GLY PRO ILE ALA ALA
SEQRES 15 A 694 ASP LEU ALA ARG TYR ALA ALA GLN ASN GLY GLN ALA VAL
SEQRES 16 A 694 SER GLY LEU LEU LEU ASP ARG PRO MET PRO SER MET THR
SEQRES 17 A 694 LYS ALA ILE THR ALA HIS GLU VAL ALA ASN PRO ALA GLY
SEQRES 18 A 694 ILE VAL GLY ALA ILE ALA LYS ALA VAL ASN GLY GLN PHE
SEQRES 19 A 694 SER VAL GLU LYS ASN LEU LYS GLY LEU PRO LYS GLU THR
SEQRES 20 A 694 PRO ILE LEU LEU LEU THR ASP ASN GLU GLY LEU GLY GLU
SEQRES 21 A 694 GLU GLY GLU LYS LEU ARG ALA LYS LEU ALA ILE ALA GLY
SEQRES 22 A 694 TYR ASN VAL THR GLY GLU GLN THR PHE TYR GLY HIS GLU
SEQRES 23 A 694 ALA SER ASN ARG LEU MET GLY GLN TYR ALA ASP GLN ILE
SEQRES 24 A 694 VAL SER GLY LEU PHE ASN ALA GLU GLN ALA ALA VAL GLU
SEQRES 25 A 694 ALA GLY GLU VAL LEU LYS GLY LEU GLU LYS ASP PHE LYS
SEQRES 26 A 694 ARG TYR GLY ASP ALA LEU LYS PRO ASP THR SER VAL PRO
SEQRES 27 A 694 GLY LYS SER LYS ASP ILE ARG THR THR LYS ASP PHE LEU
SEQRES 28 A 694 ASN GLY TYR LYS ASN ASP HIS ALA LYS GLU ILE VAL ASP
SEQRES 29 A 694 GLY PHE ARG SER ASP MET SER ILE LYS GLN LEU VAL ASP
SEQRES 30 A 694 LEU PHE VAL LYS GLY SER TRP SER ALA GLU GLN LYS GLY
SEQRES 31 A 694 ALA LEU ALA TRP GLU ILE GLU SER ARG ALA LEU LYS VAL
SEQRES 32 A 694 THR PHE GLN ASN LYS SER GLU LYS TYR ASN ARG LEU PHE
SEQRES 33 A 694 ARG GLU ILE ALA SER ALA GLY VAL VAL ASP ALA LYS ALA
SEQRES 34 A 694 THR GLU GLN LEU ALA PRO GLN LEU MET LEU LEU ASN LEU
SEQRES 35 A 694 SER ASN ASP GLY PHE GLY GLY ARG SER ASP PRO LEU SER
SEQRES 36 A 694 LYS LEU VAL LEU VAL ALA LYS GLN LEU GLU ASN ASP GLY
SEQRES 37 A 694 GLN VAL GLY VAL ALA ARG GLN LEU LEU GLU LYS MET TYR
SEQRES 38 A 694 SER ALA ALA ALA VAL LEU SER ASN PRO THR LEU TYR SER
SEQRES 39 A 694 ASP SER GLU ASN ALA ASN ALA SER LYS LEU LEU SER SER
SEQRES 40 A 694 LEU ALA ALA ILE HIS ALA LYS ASN PRO MET HIS ASP THR
SEQRES 41 A 694 SER MET LYS VAL TRP GLN GLU LYS LEU GLU GLY LYS GLN
SEQRES 42 A 694 ALA LEU THR VAL ASN GLY VAL VAL GLU LYS ILE THR ASP
SEQRES 43 A 694 ALA SER ALA ASN GLY LYS PRO VAL LEU LEU GLU LEU ASP
SEQRES 44 A 694 ALA PRO GLY HIS ALA MET ALA ALA TRP ALA LYS GLY SER
SEQRES 45 A 694 GLY ASP ASP ARG VAL TYR GLY PHE TYR ASP PRO ASN ALA
SEQRES 46 A 694 GLY ILE VAL GLU PHE SER SER ALA GLU LYS PHE GLY ASP
SEQRES 47 A 694 TYR LEU THR ARG PHE PHE GLY LYS SER ASP LEU ASN MET
SEQRES 48 A 694 ALA GLN SER TYR LYS LEU GLY LYS ASN ASP ALA GLY GLU
SEQRES 49 A 694 ALA ILE PHE ASN ARG VAL VAL VAL MET ASP GLY ASN THR
SEQRES 50 A 694 LEU ALA SER TYR LYS PRO THR PHE GLY ASP LYS THR THR
SEQRES 51 A 694 MET GLN GLY ILE LEU ASP LEU PRO VAL PHE ASP ALA THR
SEQRES 52 A 694 PRO MET LYS LYS PRO GLY THR SER ASP VAL ASP GLY ASN
SEQRES 53 A 694 ALA LYS ALA VAL ASP ASP THR LYS GLU ALA LEU GLU HIS
SEQRES 54 A 694 HIS HIS HIS HIS HIS
SEQRES 1 B 694 MET SER GLY ASN GLU LYS HIS LYS GLU ASN VAL ALA ILE
SEQRES 2 B 694 GLU ASN ASP GLY THR PRO PRO ARG ASP LYS GLU SER LEU
SEQRES 3 B 694 SER PRO LEU THR ARG PHE LEU ASN ASN GLU LEU TYR GLY
SEQRES 4 B 694 GLU LYS ASP ALA ARG ARG LYS ILE GLY GLU ILE THR GLN
SEQRES 5 B 694 THR LEU LEU ASP HIS ALA VAL GLU ASN GLY GLU SER GLN
SEQRES 6 B 694 LYS VAL THR LEU LYS GLY GLU VAL GLY ARG LEU THR GLY
SEQRES 7 B 694 TYR TYR HIS GLN GLY ALA ALA SER SER GLU GLY GLU THR
SEQRES 8 B 694 SER ALA THR SER GLY LYS VAL VAL LEU PHE LEU HIS GLY
SEQRES 9 B 694 SER GLY SER SER ALA GLU GLU GLN ALA SER GLU ILE ARG
SEQRES 10 B 694 ASN HIS TYR GLN LYS GLN GLY ILE ASP MET LEU ALA VAL
SEQRES 11 B 694 ASN LEU ARG GLY TYR GLY GLU SER ASP GLY GLY PRO SER
SEQRES 12 B 694 GLU LYS GLY LEU TYR GLN ASP ALA ARG THR MET PHE ASN
SEQRES 13 B 694 TYR LEU VAL ASN ASP LYS GLY ILE ASP PRO SER ASN ILE
SEQRES 14 B 694 ILE ILE HIS GLY TYR SER MET GLY GLY PRO ILE ALA ALA
SEQRES 15 B 694 ASP LEU ALA ARG TYR ALA ALA GLN ASN GLY GLN ALA VAL
SEQRES 16 B 694 SER GLY LEU LEU LEU ASP ARG PRO MET PRO SER MET THR
SEQRES 17 B 694 LYS ALA ILE THR ALA HIS GLU VAL ALA ASN PRO ALA GLY
SEQRES 18 B 694 ILE VAL GLY ALA ILE ALA LYS ALA VAL ASN GLY GLN PHE
SEQRES 19 B 694 SER VAL GLU LYS ASN LEU LYS GLY LEU PRO LYS GLU THR
SEQRES 20 B 694 PRO ILE LEU LEU LEU THR ASP ASN GLU GLY LEU GLY GLU
SEQRES 21 B 694 GLU GLY GLU LYS LEU ARG ALA LYS LEU ALA ILE ALA GLY
SEQRES 22 B 694 TYR ASN VAL THR GLY GLU GLN THR PHE TYR GLY HIS GLU
SEQRES 23 B 694 ALA SER ASN ARG LEU MET GLY GLN TYR ALA ASP GLN ILE
SEQRES 24 B 694 VAL SER GLY LEU PHE ASN ALA GLU GLN ALA ALA VAL GLU
SEQRES 25 B 694 ALA GLY GLU VAL LEU LYS GLY LEU GLU LYS ASP PHE LYS
SEQRES 26 B 694 ARG TYR GLY ASP ALA LEU LYS PRO ASP THR SER VAL PRO
SEQRES 27 B 694 GLY LYS SER LYS ASP ILE ARG THR THR LYS ASP PHE LEU
SEQRES 28 B 694 ASN GLY TYR LYS ASN ASP HIS ALA LYS GLU ILE VAL ASP
SEQRES 29 B 694 GLY PHE ARG SER ASP MET SER ILE LYS GLN LEU VAL ASP
SEQRES 30 B 694 LEU PHE VAL LYS GLY SER TRP SER ALA GLU GLN LYS GLY
SEQRES 31 B 694 ALA LEU ALA TRP GLU ILE GLU SER ARG ALA LEU LYS VAL
SEQRES 32 B 694 THR PHE GLN ASN LYS SER GLU LYS TYR ASN ARG LEU PHE
SEQRES 33 B 694 ARG GLU ILE ALA SER ALA GLY VAL VAL ASP ALA LYS ALA
SEQRES 34 B 694 THR GLU GLN LEU ALA PRO GLN LEU MET LEU LEU ASN LEU
SEQRES 35 B 694 SER ASN ASP GLY PHE GLY GLY ARG SER ASP PRO LEU SER
SEQRES 36 B 694 LYS LEU VAL LEU VAL ALA LYS GLN LEU GLU ASN ASP GLY
SEQRES 37 B 694 GLN VAL GLY VAL ALA ARG GLN LEU LEU GLU LYS MET TYR
SEQRES 38 B 694 SER ALA ALA ALA VAL LEU SER ASN PRO THR LEU TYR SER
SEQRES 39 B 694 ASP SER GLU ASN ALA ASN ALA SER LYS LEU LEU SER SER
SEQRES 40 B 694 LEU ALA ALA ILE HIS ALA LYS ASN PRO MET HIS ASP THR
SEQRES 41 B 694 SER MET LYS VAL TRP GLN GLU LYS LEU GLU GLY LYS GLN
SEQRES 42 B 694 ALA LEU THR VAL ASN GLY VAL VAL GLU LYS ILE THR ASP
SEQRES 43 B 694 ALA SER ALA ASN GLY LYS PRO VAL LEU LEU GLU LEU ASP
SEQRES 44 B 694 ALA PRO GLY HIS ALA MET ALA ALA TRP ALA LYS GLY SER
SEQRES 45 B 694 GLY ASP ASP ARG VAL TYR GLY PHE TYR ASP PRO ASN ALA
SEQRES 46 B 694 GLY ILE VAL GLU PHE SER SER ALA GLU LYS PHE GLY ASP
SEQRES 47 B 694 TYR LEU THR ARG PHE PHE GLY LYS SER ASP LEU ASN MET
SEQRES 48 B 694 ALA GLN SER TYR LYS LEU GLY LYS ASN ASP ALA GLY GLU
SEQRES 49 B 694 ALA ILE PHE ASN ARG VAL VAL VAL MET ASP GLY ASN THR
SEQRES 50 B 694 LEU ALA SER TYR LYS PRO THR PHE GLY ASP LYS THR THR
SEQRES 51 B 694 MET GLN GLY ILE LEU ASP LEU PRO VAL PHE ASP ALA THR
SEQRES 52 B 694 PRO MET LYS LYS PRO GLY THR SER ASP VAL ASP GLY ASN
SEQRES 53 B 694 ALA LYS ALA VAL ASP ASP THR LYS GLU ALA LEU GLU HIS
SEQRES 54 B 694 HIS HIS HIS HIS HIS
SEQRES 1 C 694 MET SER GLY ASN GLU LYS HIS LYS GLU ASN VAL ALA ILE
SEQRES 2 C 694 GLU ASN ASP GLY THR PRO PRO ARG ASP LYS GLU SER LEU
SEQRES 3 C 694 SER PRO LEU THR ARG PHE LEU ASN ASN GLU LEU TYR GLY
SEQRES 4 C 694 GLU LYS ASP ALA ARG ARG LYS ILE GLY GLU ILE THR GLN
SEQRES 5 C 694 THR LEU LEU ASP HIS ALA VAL GLU ASN GLY GLU SER GLN
SEQRES 6 C 694 LYS VAL THR LEU LYS GLY GLU VAL GLY ARG LEU THR GLY
SEQRES 7 C 694 TYR TYR HIS GLN GLY ALA ALA SER SER GLU GLY GLU THR
SEQRES 8 C 694 SER ALA THR SER GLY LYS VAL VAL LEU PHE LEU HIS GLY
SEQRES 9 C 694 SER GLY SER SER ALA GLU GLU GLN ALA SER GLU ILE ARG
SEQRES 10 C 694 ASN HIS TYR GLN LYS GLN GLY ILE ASP MET LEU ALA VAL
SEQRES 11 C 694 ASN LEU ARG GLY TYR GLY GLU SER ASP GLY GLY PRO SER
SEQRES 12 C 694 GLU LYS GLY LEU TYR GLN ASP ALA ARG THR MET PHE ASN
SEQRES 13 C 694 TYR LEU VAL ASN ASP LYS GLY ILE ASP PRO SER ASN ILE
SEQRES 14 C 694 ILE ILE HIS GLY TYR SER MET GLY GLY PRO ILE ALA ALA
SEQRES 15 C 694 ASP LEU ALA ARG TYR ALA ALA GLN ASN GLY GLN ALA VAL
SEQRES 16 C 694 SER GLY LEU LEU LEU ASP ARG PRO MET PRO SER MET THR
SEQRES 17 C 694 LYS ALA ILE THR ALA HIS GLU VAL ALA ASN PRO ALA GLY
SEQRES 18 C 694 ILE VAL GLY ALA ILE ALA LYS ALA VAL ASN GLY GLN PHE
SEQRES 19 C 694 SER VAL GLU LYS ASN LEU LYS GLY LEU PRO LYS GLU THR
SEQRES 20 C 694 PRO ILE LEU LEU LEU THR ASP ASN GLU GLY LEU GLY GLU
SEQRES 21 C 694 GLU GLY GLU LYS LEU ARG ALA LYS LEU ALA ILE ALA GLY
SEQRES 22 C 694 TYR ASN VAL THR GLY GLU GLN THR PHE TYR GLY HIS GLU
SEQRES 23 C 694 ALA SER ASN ARG LEU MET GLY GLN TYR ALA ASP GLN ILE
SEQRES 24 C 694 VAL SER GLY LEU PHE ASN ALA GLU GLN ALA ALA VAL GLU
SEQRES 25 C 694 ALA GLY GLU VAL LEU LYS GLY LEU GLU LYS ASP PHE LYS
SEQRES 26 C 694 ARG TYR GLY ASP ALA LEU LYS PRO ASP THR SER VAL PRO
SEQRES 27 C 694 GLY LYS SER LYS ASP ILE ARG THR THR LYS ASP PHE LEU
SEQRES 28 C 694 ASN GLY TYR LYS ASN ASP HIS ALA LYS GLU ILE VAL ASP
SEQRES 29 C 694 GLY PHE ARG SER ASP MET SER ILE LYS GLN LEU VAL ASP
SEQRES 30 C 694 LEU PHE VAL LYS GLY SER TRP SER ALA GLU GLN LYS GLY
SEQRES 31 C 694 ALA LEU ALA TRP GLU ILE GLU SER ARG ALA LEU LYS VAL
SEQRES 32 C 694 THR PHE GLN ASN LYS SER GLU LYS TYR ASN ARG LEU PHE
SEQRES 33 C 694 ARG GLU ILE ALA SER ALA GLY VAL VAL ASP ALA LYS ALA
SEQRES 34 C 694 THR GLU GLN LEU ALA PRO GLN LEU MET LEU LEU ASN LEU
SEQRES 35 C 694 SER ASN ASP GLY PHE GLY GLY ARG SER ASP PRO LEU SER
SEQRES 36 C 694 LYS LEU VAL LEU VAL ALA LYS GLN LEU GLU ASN ASP GLY
SEQRES 37 C 694 GLN VAL GLY VAL ALA ARG GLN LEU LEU GLU LYS MET TYR
SEQRES 38 C 694 SER ALA ALA ALA VAL LEU SER ASN PRO THR LEU TYR SER
SEQRES 39 C 694 ASP SER GLU ASN ALA ASN ALA SER LYS LEU LEU SER SER
SEQRES 40 C 694 LEU ALA ALA ILE HIS ALA LYS ASN PRO MET HIS ASP THR
SEQRES 41 C 694 SER MET LYS VAL TRP GLN GLU LYS LEU GLU GLY LYS GLN
SEQRES 42 C 694 ALA LEU THR VAL ASN GLY VAL VAL GLU LYS ILE THR ASP
SEQRES 43 C 694 ALA SER ALA ASN GLY LYS PRO VAL LEU LEU GLU LEU ASP
SEQRES 44 C 694 ALA PRO GLY HIS ALA MET ALA ALA TRP ALA LYS GLY SER
SEQRES 45 C 694 GLY ASP ASP ARG VAL TYR GLY PHE TYR ASP PRO ASN ALA
SEQRES 46 C 694 GLY ILE VAL GLU PHE SER SER ALA GLU LYS PHE GLY ASP
SEQRES 47 C 694 TYR LEU THR ARG PHE PHE GLY LYS SER ASP LEU ASN MET
SEQRES 48 C 694 ALA GLN SER TYR LYS LEU GLY LYS ASN ASP ALA GLY GLU
SEQRES 49 C 694 ALA ILE PHE ASN ARG VAL VAL VAL MET ASP GLY ASN THR
SEQRES 50 C 694 LEU ALA SER TYR LYS PRO THR PHE GLY ASP LYS THR THR
SEQRES 51 C 694 MET GLN GLY ILE LEU ASP LEU PRO VAL PHE ASP ALA THR
SEQRES 52 C 694 PRO MET LYS LYS PRO GLY THR SER ASP VAL ASP GLY ASN
SEQRES 53 C 694 ALA LYS ALA VAL ASP ASP THR LYS GLU ALA LEU GLU HIS
SEQRES 54 C 694 HIS HIS HIS HIS HIS
SEQRES 1 D 694 MET SER GLY ASN GLU LYS HIS LYS GLU ASN VAL ALA ILE
SEQRES 2 D 694 GLU ASN ASP GLY THR PRO PRO ARG ASP LYS GLU SER LEU
SEQRES 3 D 694 SER PRO LEU THR ARG PHE LEU ASN ASN GLU LEU TYR GLY
SEQRES 4 D 694 GLU LYS ASP ALA ARG ARG LYS ILE GLY GLU ILE THR GLN
SEQRES 5 D 694 THR LEU LEU ASP HIS ALA VAL GLU ASN GLY GLU SER GLN
SEQRES 6 D 694 LYS VAL THR LEU LYS GLY GLU VAL GLY ARG LEU THR GLY
SEQRES 7 D 694 TYR TYR HIS GLN GLY ALA ALA SER SER GLU GLY GLU THR
SEQRES 8 D 694 SER ALA THR SER GLY LYS VAL VAL LEU PHE LEU HIS GLY
SEQRES 9 D 694 SER GLY SER SER ALA GLU GLU GLN ALA SER GLU ILE ARG
SEQRES 10 D 694 ASN HIS TYR GLN LYS GLN GLY ILE ASP MET LEU ALA VAL
SEQRES 11 D 694 ASN LEU ARG GLY TYR GLY GLU SER ASP GLY GLY PRO SER
SEQRES 12 D 694 GLU LYS GLY LEU TYR GLN ASP ALA ARG THR MET PHE ASN
SEQRES 13 D 694 TYR LEU VAL ASN ASP LYS GLY ILE ASP PRO SER ASN ILE
SEQRES 14 D 694 ILE ILE HIS GLY TYR SER MET GLY GLY PRO ILE ALA ALA
SEQRES 15 D 694 ASP LEU ALA ARG TYR ALA ALA GLN ASN GLY GLN ALA VAL
SEQRES 16 D 694 SER GLY LEU LEU LEU ASP ARG PRO MET PRO SER MET THR
SEQRES 17 D 694 LYS ALA ILE THR ALA HIS GLU VAL ALA ASN PRO ALA GLY
SEQRES 18 D 694 ILE VAL GLY ALA ILE ALA LYS ALA VAL ASN GLY GLN PHE
SEQRES 19 D 694 SER VAL GLU LYS ASN LEU LYS GLY LEU PRO LYS GLU THR
SEQRES 20 D 694 PRO ILE LEU LEU LEU THR ASP ASN GLU GLY LEU GLY GLU
SEQRES 21 D 694 GLU GLY GLU LYS LEU ARG ALA LYS LEU ALA ILE ALA GLY
SEQRES 22 D 694 TYR ASN VAL THR GLY GLU GLN THR PHE TYR GLY HIS GLU
SEQRES 23 D 694 ALA SER ASN ARG LEU MET GLY GLN TYR ALA ASP GLN ILE
SEQRES 24 D 694 VAL SER GLY LEU PHE ASN ALA GLU GLN ALA ALA VAL GLU
SEQRES 25 D 694 ALA GLY GLU VAL LEU LYS GLY LEU GLU LYS ASP PHE LYS
SEQRES 26 D 694 ARG TYR GLY ASP ALA LEU LYS PRO ASP THR SER VAL PRO
SEQRES 27 D 694 GLY LYS SER LYS ASP ILE ARG THR THR LYS ASP PHE LEU
SEQRES 28 D 694 ASN GLY TYR LYS ASN ASP HIS ALA LYS GLU ILE VAL ASP
SEQRES 29 D 694 GLY PHE ARG SER ASP MET SER ILE LYS GLN LEU VAL ASP
SEQRES 30 D 694 LEU PHE VAL LYS GLY SER TRP SER ALA GLU GLN LYS GLY
SEQRES 31 D 694 ALA LEU ALA TRP GLU ILE GLU SER ARG ALA LEU LYS VAL
SEQRES 32 D 694 THR PHE GLN ASN LYS SER GLU LYS TYR ASN ARG LEU PHE
SEQRES 33 D 694 ARG GLU ILE ALA SER ALA GLY VAL VAL ASP ALA LYS ALA
SEQRES 34 D 694 THR GLU GLN LEU ALA PRO GLN LEU MET LEU LEU ASN LEU
SEQRES 35 D 694 SER ASN ASP GLY PHE GLY GLY ARG SER ASP PRO LEU SER
SEQRES 36 D 694 LYS LEU VAL LEU VAL ALA LYS GLN LEU GLU ASN ASP GLY
SEQRES 37 D 694 GLN VAL GLY VAL ALA ARG GLN LEU LEU GLU LYS MET TYR
SEQRES 38 D 694 SER ALA ALA ALA VAL LEU SER ASN PRO THR LEU TYR SER
SEQRES 39 D 694 ASP SER GLU ASN ALA ASN ALA SER LYS LEU LEU SER SER
SEQRES 40 D 694 LEU ALA ALA ILE HIS ALA LYS ASN PRO MET HIS ASP THR
SEQRES 41 D 694 SER MET LYS VAL TRP GLN GLU LYS LEU GLU GLY LYS GLN
SEQRES 42 D 694 ALA LEU THR VAL ASN GLY VAL VAL GLU LYS ILE THR ASP
SEQRES 43 D 694 ALA SER ALA ASN GLY LYS PRO VAL LEU LEU GLU LEU ASP
SEQRES 44 D 694 ALA PRO GLY HIS ALA MET ALA ALA TRP ALA LYS GLY SER
SEQRES 45 D 694 GLY ASP ASP ARG VAL TYR GLY PHE TYR ASP PRO ASN ALA
SEQRES 46 D 694 GLY ILE VAL GLU PHE SER SER ALA GLU LYS PHE GLY ASP
SEQRES 47 D 694 TYR LEU THR ARG PHE PHE GLY LYS SER ASP LEU ASN MET
SEQRES 48 D 694 ALA GLN SER TYR LYS LEU GLY LYS ASN ASP ALA GLY GLU
SEQRES 49 D 694 ALA ILE PHE ASN ARG VAL VAL VAL MET ASP GLY ASN THR
SEQRES 50 D 694 LEU ALA SER TYR LYS PRO THR PHE GLY ASP LYS THR THR
SEQRES 51 D 694 MET GLN GLY ILE LEU ASP LEU PRO VAL PHE ASP ALA THR
SEQRES 52 D 694 PRO MET LYS LYS PRO GLY THR SER ASP VAL ASP GLY ASN
SEQRES 53 D 694 ALA LYS ALA VAL ASP ASP THR LYS GLU ALA LEU GLU HIS
SEQRES 54 D 694 HIS HIS HIS HIS HIS
HELIX 1 AA1 SER A 2927 GLY A 2939 1 13
HELIX 2 AA2 GLU A 2940 LYS A 2946 1 7
HELIX 3 AA3 GLY A 2948 ASP A 2956 1 9
HELIX 4 AA4 SER A 3008 LYS A 3022 1 15
HELIX 5 AA5 SER A 3043 ASN A 3060 1 18
HELIX 6 AA6 MET A 3076 ASN A 3091 1 16
HELIX 7 AA7 SER A 3106 GLU A 3115 1 10
HELIX 8 AA8 GLY A 3121 VAL A 3130 1 10
HELIX 9 AA9 SER A 3135 LYS A 3141 1 7
HELIX 10 AB1 GLU A 3156 GLY A 3173 1 18
HELIX 11 AB2 ALA A 3187 SER A 3201 1 15
HELIX 12 AB3 GLU A 3207 LYS A 3225 1 19
HELIX 13 AB4 THR A 3247 TYR A 3254 1 8
HELIX 14 AB5 HIS A 3258 VAL A 3263 1 6
HELIX 15 AB6 SER A 3271 VAL A 3280 1 10
HELIX 16 AB7 SER A 3285 THR A 3304 1 20
HELIX 17 AB8 SER A 3309 ALA A 3322 1 14
HELIX 18 AB9 PRO A 3353 ASP A 3367 1 15
HELIX 19 AC1 GLY A 3371 ASN A 3389 1 19
HELIX 20 AC2 SER A 3394 LYS A 3414 1 21
HELIX 21 AC3 LYS A 3432 ALA A 3434 5 3
HELIX 22 AC4 THR A 3436 ASP A 3446 1 11
HELIX 23 AC5 SER A 3492 GLY A 3505 1 14
HELIX 24 AC6 ASN A 3510 TYR A 3515 1 6
HELIX 25 AC7 ASP A 3534 TYR A 3541 1 8
HELIX 26 AC8 THR A 3550 ASP A 3556 1 7
HELIX 27 AC9 SER B 2927 GLY B 2939 1 13
HELIX 28 AD1 GLU B 2940 LYS B 2946 1 7
HELIX 29 AD2 GLY B 2948 ASP B 2956 1 9
HELIX 30 AD3 SER B 3008 LYS B 3022 1 15
HELIX 31 AD4 SER B 3043 ASN B 3060 1 18
HELIX 32 AD5 MET B 3076 ASN B 3091 1 16
HELIX 33 AD6 SER B 3106 GLU B 3115 1 10
HELIX 34 AD7 ILE B 3122 VAL B 3130 1 9
HELIX 35 AD8 SER B 3135 LYS B 3141 1 7
HELIX 36 AD9 GLU B 3156 GLY B 3173 1 18
HELIX 37 AE1 ALA B 3187 VAL B 3200 1 14
HELIX 38 AE2 GLU B 3207 LYS B 3225 1 19
HELIX 39 AE3 THR B 3247 TYR B 3254 1 8
HELIX 40 AE4 HIS B 3258 VAL B 3263 1 6
HELIX 41 AE5 SER B 3271 GLY B 3282 1 12
HELIX 42 AE6 SER B 3285 VAL B 3303 1 19
HELIX 43 AE7 SER B 3309 ALA B 3322 1 14
HELIX 44 AE8 ASP B 3352 ASP B 3367 1 16
HELIX 45 AE9 GLY B 3371 SER B 3388 1 18
HELIX 46 AF1 SER B 3394 LYS B 3414 1 21
HELIX 47 AF2 THR B 3436 ASP B 3446 1 11
HELIX 48 AF3 PRO B 3483 ALA B 3485 5 3
HELIX 49 AF4 SER B 3492 GLY B 3505 1 14
HELIX 50 AF5 ASN B 3510 TYR B 3515 1 6
HELIX 51 AF6 ASP B 3534 TYR B 3541 1 8
HELIX 52 AF7 THR B 3550 ASP B 3556 1 7
HELIX 53 AF8 SER C 2927 GLY C 2939 1 13
HELIX 54 AF9 GLU C 2940 LYS C 2946 1 7
HELIX 55 AG1 GLY C 2948 ASP C 2956 1 9
HELIX 56 AG2 SER C 3008 LYS C 3022 1 15
HELIX 57 AG3 SER C 3043 ASN C 3060 1 18
HELIX 58 AG4 MET C 3076 ASN C 3091 1 16
HELIX 59 AG5 SER C 3106 GLU C 3115 1 10
HELIX 60 AG6 GLY C 3121 VAL C 3130 1 10
HELIX 61 AG7 SER C 3135 LYS C 3141 1 7
HELIX 62 AG8 GLU C 3156 GLY C 3173 1 18
HELIX 63 AG9 ALA C 3187 SER C 3201 1 15
HELIX 64 AH1 GLU C 3207 LYS C 3222 1 16
HELIX 65 AH2 ASP C 3249 TYR C 3254 1 6
HELIX 66 AH3 HIS C 3258 VAL C 3263 1 6
HELIX 67 AH4 ILE C 3272 PHE C 3279 1 8
HELIX 68 AH5 GLU C 3287 ALA C 3300 1 14
HELIX 69 AH6 LEU C 3301 PHE C 3305 5 5
HELIX 70 AH7 SER C 3309 ALA C 3320 1 12
HELIX 71 AH8 ASP C 3352 ASP C 3367 1 16
HELIX 72 AH9 GLY C 3371 SER C 3388 1 18
HELIX 73 AI1 SER C 3396 LYS C 3414 1 19
HELIX 74 AI2 GLU C 3430 ALA C 3434 5 5
HELIX 75 AI3 THR C 3436 ASP C 3446 1 11
HELIX 76 AI4 SER C 3492 GLY C 3505 1 14
HELIX 77 AI5 ASN C 3510 LYS C 3516 1 7
HELIX 78 AI6 ASP C 3534 TYR C 3541 1 8
HELIX 79 AI7 THR C 3550 ASP C 3556 1 7
HELIX 80 AI8 SER D 2927 GLY D 2939 1 13
HELIX 81 AI9 GLU D 2940 LYS D 2946 1 7
HELIX 82 AJ1 GLY D 2948 ASP D 2956 1 9
HELIX 83 AJ2 SER D 3008 LYS D 3022 1 15
HELIX 84 AJ3 SER D 3043 ASN D 3060 1 18
HELIX 85 AJ4 PRO D 3079 ASN D 3091 1 13
HELIX 86 AJ5 SER D 3106 HIS D 3114 1 9
HELIX 87 AJ6 GLY D 3121 VAL D 3130 1 10
HELIX 88 AJ7 SER D 3135 LYS D 3141 1 7
HELIX 89 AJ8 GLU D 3156 GLY D 3173 1 18
HELIX 90 AJ9 ALA D 3187 SER D 3201 1 15
HELIX 91 AK1 GLU D 3207 ARG D 3226 1 20
HELIX 92 AK2 THR D 3247 TYR D 3254 1 8
HELIX 93 AK3 HIS D 3258 VAL D 3263 1 6
HELIX 94 AK4 SER D 3271 LYS D 3281 1 11
HELIX 95 AK5 SER D 3285 VAL D 3303 1 19
HELIX 96 AK6 SER D 3309 ALA D 3322 1 14
HELIX 97 AK7 ASP D 3352 ASN D 3366 1 15
HELIX 98 AK8 VAL D 3372 SER D 3388 1 17
HELIX 99 AK9 GLU D 3397 LYS D 3414 1 18
HELIX 100 AL1 ASN D 3438 LYS D 3443 1 6
HELIX 101 AL2 SER D 3492 LEU D 3500 1 9
HELIX 102 AL3 ASP D 3534 TYR D 3541 1 8
HELIX 103 AL4 GLN D 3552 ASP D 3556 1 5
SHEET 1 AA1 5 LYS A2966 LYS A2970 0
SHEET 2 AA1 5 ARG A2975 HIS A2981 -1 O GLY A2978 N VAL A2967
SHEET 3 AA1 5 ASP A3026 VAL A3030 -1 O MET A3027 N HIS A2981
SHEET 4 AA1 5 VAL A2998 PHE A3001 1 N VAL A2999 O LEU A3028
SHEET 5 AA1 5 ILE A3069 ILE A3070 1 O ILE A3070 N LEU A3000
SHEET 1 AA2 3 LEU A3098 ASP A3101 0
SHEET 2 AA2 3 PRO A3148 LEU A3152 1 O LEU A3150 N LEU A3100
SHEET 3 AA2 3 ASN A3175 THR A3177 1 O THR A3177 N ILE A3149
SHEET 1 AA3 7 THR A3330 GLN A3332 0
SHEET 2 AA3 7 ILE A3487 PHE A3490 -1 O ILE A3487 N GLN A3332
SHEET 3 AA3 7 VAL A3477 TYR A3481 -1 N TYR A3478 O PHE A3490
SHEET 4 AA3 7 ALA A3464 LYS A3470 -1 N ALA A3466 O TYR A3481
SHEET 5 AA3 7 VAL A3454 ASP A3459 -1 N LEU A3458 O MET A3465
SHEET 6 AA3 7 ARG A3529 MET A3533 -1 O MET A3533 N LEU A3455
SHEET 7 AA3 7 TRP A3425 GLU A3430 -1 N GLN A3426 O VAL A3532
SHEET 1 AA4 8 LYS B2966 LYS B2970 0
SHEET 2 AA4 8 ARG B2975 HIS B2981 -1 O GLY B2978 N VAL B2967
SHEET 3 AA4 8 ASP B3026 VAL B3030 -1 O MET B3027 N HIS B2981
SHEET 4 AA4 8 VAL B2998 LEU B3002 1 N VAL B2999 O LEU B3028
SHEET 5 AA4 8 ILE B3069 TYR B3074 1 O HIS B3072 N LEU B3002
SHEET 6 AA4 8 GLY B3097 ASP B3101 1 O LEU B3099 N GLY B3073
SHEET 7 AA4 8 PRO B3148 LEU B3152 1 O LEU B3150 N LEU B3100
SHEET 8 AA4 8 ASN B3175 THR B3177 1 O THR B3177 N ILE B3149
SHEET 1 AA5 7 THR B3330 GLN B3332 0
SHEET 2 AA5 7 GLY B3486 PHE B3490 -1 O ILE B3487 N GLN B3332
SHEET 3 AA5 7 VAL B3477 ASP B3482 -1 N TYR B3478 O PHE B3490
SHEET 4 AA5 7 ALA B3464 LYS B3470 -1 N ALA B3466 O TYR B3481
SHEET 5 AA5 7 VAL B3454 ASP B3459 -1 N LEU B3458 O MET B3465
SHEET 6 AA5 7 ARG B3529 MET B3533 -1 O MET B3533 N LEU B3455
SHEET 7 AA5 7 TRP B3425 LEU B3429 -1 N GLN B3426 O VAL B3532
SHEET 1 AA6 8 LYS C2966 LYS C2970 0
SHEET 2 AA6 8 ARG C2975 HIS C2981 -1 O GLY C2978 N VAL C2967
SHEET 3 AA6 8 ASP C3026 VAL C3030 -1 O MET C3027 N HIS C2981
SHEET 4 AA6 8 VAL C2998 LEU C3002 1 N VAL C2999 O LEU C3028
SHEET 5 AA6 8 ILE C3069 TYR C3074 1 O HIS C3072 N LEU C3002
SHEET 6 AA6 8 GLY C3097 ASP C3101 1 O LEU C3099 N GLY C3073
SHEET 7 AA6 8 PRO C3148 LEU C3152 1 O LEU C3150 N LEU C3100
SHEET 8 AA6 8 ASN C3175 THR C3177 1 O THR C3177 N ILE C3149
SHEET 1 AA7 7 THR C3330 GLN C3332 0
SHEET 2 AA7 7 ILE C3487 PHE C3490 -1 O ILE C3487 N GLN C3332
SHEET 3 AA7 7 VAL C3477 TYR C3481 -1 N TYR C3478 O PHE C3490
SHEET 4 AA7 7 ALA C3464 LYS C3470 -1 N TRP C3468 O GLY C3479
SHEET 5 AA7 7 VAL C3454 ASP C3459 -1 N LEU C3458 O MET C3465
SHEET 6 AA7 7 ARG C3529 MET C3533 -1 O MET C3533 N LEU C3455
SHEET 7 AA7 7 TRP C3425 LYS C3428 -1 N GLN C3426 O VAL C3532
SHEET 1 AA8 5 LYS D2966 LYS D2970 0
SHEET 2 AA8 5 ARG D2975 HIS D2981 -1 O GLY D2978 N VAL D2967
SHEET 3 AA8 5 ASP D3026 VAL D3030 -1 O MET D3027 N HIS D2981
SHEET 4 AA8 5 VAL D2998 LEU D3002 1 N VAL D2999 O LEU D3028
SHEET 5 AA8 5 ILE D3069 GLY D3073 1 O ILE D3070 N LEU D3000
SHEET 1 AA9 3 LEU D3098 ASP D3101 0
SHEET 2 AA9 3 PRO D3148 LEU D3152 1 O PRO D3148 N LEU D3098
SHEET 3 AA9 3 ASN D3175 THR D3177 1 O THR D3177 N ILE D3149
SHEET 1 AB1 6 GLU D3331 GLN D3332 0
SHEET 2 AB1 6 ILE D3487 PHE D3490 -1 N ILE D3487 O GLN D3332
SHEET 3 AB1 6 TYR D3478 TYR D3481 -1 N PHE D3480 O VAL D3488
SHEET 4 AB1 6 ALA D3466 ALA D3469 -1 N ALA D3466 O TYR D3481
SHEET 5 AB1 6 VAL D3454 GLU D3457 -1 N VAL D3454 O ALA D3469
SHEET 6 AB1 6 VAL D3531 VAL D3532 -1 O VAL D3531 N GLU D3457
CISPEP 1 HIS A 3072 GLY A 3073 0 26.93
CISPEP 2 ALA A 3206 GLU A 3207 0 6.08
CISPEP 3 GLN A 3306 ASN A 3307 0 -3.59
CISPEP 4 ALA B 3206 GLU B 3207 0 -8.15
CISPEP 5 GLN B 3306 ASN B 3307 0 -11.55
CISPEP 6 HIS C 2957 ALA C 2958 0 8.92
CISPEP 7 ASP C 3065 PRO C 3066 0 -9.16
CISPEP 8 ALA C 3120 GLY C 3121 0 1.95
CISPEP 9 ALA C 3206 GLU C 3207 0 0.26
CISPEP 10 GLN C 3306 ASN C 3307 0 -4.16
CISPEP 11 TYR C 3515 LYS C 3516 0 -2.97
CISPEP 12 LYS C 3516 LEU C 3517 0 0.25
CISPEP 13 ILE D 3064 ASP D 3065 0 3.22
CISPEP 14 ASP D 3065 PRO D 3066 0 -9.26
CISPEP 15 GLY D 3078 PRO D 3079 0 16.10
CISPEP 16 ALA D 3120 GLY D 3121 0 -5.44
CISPEP 17 ALA D 3206 GLU D 3207 0 0.55
CISPEP 18 GLN D 3306 ASN D 3307 0 -2.19
CISPEP 19 ASN D 3528 ARG D 3529 0 -25.16
CRYST1 86.215 108.593 334.737 90.00 90.00 90.00 P 21 21 21 16
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 0.011599 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009209 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002987 0.00000
TER 4682 ALA A3562
TER 9356 ALA B3562
TER 13695 ALA C3562
TER 17829 PHE D3560
MASTER 850 0 0 103 59 0 0 617825 4 0 216
END |