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HEADER HYDROLASE 10-OCT-17 6EOR
TITLE DPP9 - 1G244
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 9;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DP9,DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 2,DPRP-2,
COMPND 5 DIPEPTIDYL PEPTIDASE IX,DPP IX,DIPEPTIDYL PEPTIDASE-LIKE PROTEIN 9,
COMPND 6 DPLP9;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP9, DPRP2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS DPP9, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.ROSS,R.HUBER
REVDAT 1 07-FEB-18 6EOR 0
JRNL AUTH B.H.ROSS,S.KRAPP,M.AUGUSTIN,R.KIEFERSAUER,M.ARCINIEGA,
JRNL AUTH 2 R.GEISS-FRIEDLANDER,R.HUBER
JRNL TITL STRUCTURES AND MECHANISM OF DIPEPTIDYL PEPTIDASES 8 AND 9,
JRNL TITL 2 IMPORTANT PLAYERS IN CELLULAR HOMEOSTASIS AND CANCER
JRNL REF PROC.NATL.ACAD.SCI.USA 2018
JRNL REFN ESSN 1091-6490
JRNL DOI 10.1073/PNAS.1717565115
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 90340
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) : 0.269
REMARK 3 R VALUE (WORKING SET) : 0.265
REMARK 3 FREE R VALUE : 0.332
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4755
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6560
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.3540
REMARK 3 BIN FREE R VALUE SET COUNT : 345
REMARK 3 BIN FREE R VALUE : 0.4050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 26248
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 148
REMARK 3 SOLVENT ATOMS : 231
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.15000
REMARK 3 B22 (A**2) : 3.76000
REMARK 3 B33 (A**2) : -0.50000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.07000
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): 0.534
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.445
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.591
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.910
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.842
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 27189 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 25138 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 36876 ; 1.335 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 57907 ; 1.985 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3196 ; 6.538 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1336 ;34.439 ;23.540
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4413 ;15.440 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 160 ;15.501 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3841 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 30572 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 6672 ; 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): 12895 ; 1.531 ; 3.827
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 12894 ; 1.531 ; 3.827
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16054 ; 2.705 ; 5.727
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 16055 ; 2.705 ; 5.727
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 14294 ; 1.273 ; 3.964
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 14295 ; 1.273 ; 3.964
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 20823 ; 2.272 ; 5.883
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 28925 ; 4.858 ;42.137
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 28926 ; 4.858 ;42.138
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6EOR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200006949.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-17
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99997
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95096
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 43.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.280
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.16000
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.38
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.980
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: 1ORV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 25% GLYCEROL, 0.16M
REMARK 280 CALCIUM ACETATE, 0.08M CACODILATE PH 6.25, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 58.60600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 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 ALA A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 GLY A 5
REMARK 465 THR A 6
REMARK 465 PRO A 7
REMARK 465 THR A 8
REMARK 465 ALA A 9
REMARK 465 ASP A 10
REMARK 465 ARG A 11
REMARK 465 GLY A 12
REMARK 465 ASP A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 THR A 17
REMARK 465 ASP A 18
REMARK 465 ASP A 19
REMARK 465 PRO A 20
REMARK 465 TYR A 44
REMARK 465 SER A 45
REMARK 465 GLY A 46
REMARK 465 LEU A 47
REMARK 465 ILE A 48
REMARK 465 VAL A 49
REMARK 465 ASN A 50
REMARK 465 LYS A 51
REMARK 465 THR A 62
REMARK 465 ASP A 63
REMARK 465 GLU A 64
REMARK 465 GLY A 80
REMARK 465 SER A 81
REMARK 465 LYS A 94
REMARK 465 VAL A 95
REMARK 465 ARG A 96
REMARK 465 LYS A 97
REMARK 465 GLU A 98
REMARK 465 ALA A 99
REMARK 465 LEU A 100
REMARK 465 GLY A 228
REMARK 465 LEU A 229
REMARK 465 SER A 230
REMARK 465 SER A 267
REMARK 465 GLU A 268
REMARK 465 GLY A 269
REMARK 465 SER A 433
REMARK 465 GLU A 434
REMARK 465 GLY A 435
REMARK 465 GLU A 436
REMARK 465 ASP A 437
REMARK 465 GLU A 438
REMARK 465 ALA A 599
REMARK 465 SER A 600
REMARK 465 CYS A 601
REMARK 465 PRO A 602
REMARK 465 PRO A 603
REMARK 465 HIS A 866
REMARK 465 HIS A 867
REMARK 465 HIS A 868
REMARK 465 HIS A 869
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 THR B 4
REMARK 465 GLY B 5
REMARK 465 THR B 6
REMARK 465 PRO B 7
REMARK 465 THR B 8
REMARK 465 ALA B 9
REMARK 465 ASP B 10
REMARK 465 ARG B 11
REMARK 465 GLY B 12
REMARK 465 ASP B 13
REMARK 465 ALA B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 THR B 17
REMARK 465 ASP B 18
REMARK 465 ASP B 19
REMARK 465 TYR B 44
REMARK 465 SER B 45
REMARK 465 GLY B 46
REMARK 465 LEU B 47
REMARK 465 ILE B 48
REMARK 465 VAL B 49
REMARK 465 ASN B 50
REMARK 465 TYR B 79
REMARK 465 GLY B 80
REMARK 465 SER B 81
REMARK 465 VAL B 95
REMARK 465 ARG B 96
REMARK 465 LYS B 97
REMARK 465 GLU B 98
REMARK 465 ALA B 99
REMARK 465 LEU B 100
REMARK 465 GLY B 165
REMARK 465 GLY B 166
REMARK 465 LYS B 167
REMARK 465 ASN B 168
REMARK 465 GLY B 228
REMARK 465 LEU B 229
REMARK 465 SER B 230
REMARK 465 ASN B 231
REMARK 465 GLU B 265
REMARK 465 GLY B 266
REMARK 465 SER B 267
REMARK 465 GLU B 268
REMARK 465 GLY B 269
REMARK 465 GLY B 435
REMARK 465 GLU B 436
REMARK 465 GLU B 476
REMARK 465 ASP B 477
REMARK 465 GLU B 478
REMARK 465 ALA B 599
REMARK 465 SER B 600
REMARK 465 CYS B 601
REMARK 465 PRO B 602
REMARK 465 PRO B 603
REMARK 465 HIS B 864
REMARK 465 HIS B 865
REMARK 465 HIS B 866
REMARK 465 HIS B 867
REMARK 465 HIS B 868
REMARK 465 HIS B 869
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 THR C 3
REMARK 465 THR C 4
REMARK 465 GLY C 5
REMARK 465 THR C 6
REMARK 465 PRO C 7
REMARK 465 THR C 8
REMARK 465 ALA C 9
REMARK 465 ASP C 10
REMARK 465 ARG C 11
REMARK 465 GLY C 12
REMARK 465 ASP C 13
REMARK 465 ALA C 14
REMARK 465 ALA C 15
REMARK 465 ALA C 16
REMARK 465 THR C 17
REMARK 465 ASP C 18
REMARK 465 ASP C 19
REMARK 465 TYR C 44
REMARK 465 SER C 45
REMARK 465 GLY C 46
REMARK 465 LEU C 47
REMARK 465 ILE C 48
REMARK 465 VAL C 49
REMARK 465 ASN C 50
REMARK 465 LYS C 51
REMARK 465 TYR C 79
REMARK 465 GLY C 80
REMARK 465 SER C 81
REMARK 465 VAL C 95
REMARK 465 ARG C 96
REMARK 465 LYS C 97
REMARK 465 GLU C 98
REMARK 465 ALA C 99
REMARK 465 LEU C 100
REMARK 465 GLY C 166
REMARK 465 LYS C 167
REMARK 465 GLY C 228
REMARK 465 LEU C 229
REMARK 465 SER C 230
REMARK 465 ASN C 231
REMARK 465 GLU C 265
REMARK 465 GLY C 266
REMARK 465 SER C 267
REMARK 465 GLU C 268
REMARK 465 GLY C 269
REMARK 465 GLU C 434
REMARK 465 GLY C 435
REMARK 465 GLU C 436
REMARK 465 ALA C 599
REMARK 465 SER C 600
REMARK 465 CYS C 601
REMARK 465 PRO C 602
REMARK 465 PRO C 603
REMARK 465 HIS C 864
REMARK 465 HIS C 865
REMARK 465 HIS C 866
REMARK 465 HIS C 867
REMARK 465 HIS C 868
REMARK 465 HIS C 869
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 THR D 3
REMARK 465 THR D 4
REMARK 465 GLY D 5
REMARK 465 THR D 6
REMARK 465 PRO D 7
REMARK 465 THR D 8
REMARK 465 ALA D 9
REMARK 465 ASP D 10
REMARK 465 ARG D 11
REMARK 465 GLY D 12
REMARK 465 ASP D 13
REMARK 465 ALA D 14
REMARK 465 ALA D 15
REMARK 465 ALA D 16
REMARK 465 THR D 17
REMARK 465 ASP D 18
REMARK 465 ASP D 19
REMARK 465 TYR D 44
REMARK 465 SER D 45
REMARK 465 GLY D 46
REMARK 465 LEU D 47
REMARK 465 ILE D 48
REMARK 465 VAL D 49
REMARK 465 ASN D 50
REMARK 465 LYS D 51
REMARK 465 SER D 65
REMARK 465 TYR D 79
REMARK 465 GLY D 80
REMARK 465 SER D 81
REMARK 465 LYS D 94
REMARK 465 VAL D 95
REMARK 465 ARG D 96
REMARK 465 LYS D 97
REMARK 465 GLU D 98
REMARK 465 ALA D 99
REMARK 465 LEU D 100
REMARK 465 GLY D 228
REMARK 465 LEU D 229
REMARK 465 SER D 230
REMARK 465 ASN D 231
REMARK 465 SER D 267
REMARK 465 GLU D 268
REMARK 465 GLY D 269
REMARK 465 GLU D 434
REMARK 465 GLY D 435
REMARK 465 SER D 600
REMARK 465 CYS D 601
REMARK 465 PRO D 602
REMARK 465 PRO D 603
REMARK 465 HIS D 864
REMARK 465 HIS D 865
REMARK 465 HIS D 866
REMARK 465 HIS D 867
REMARK 465 HIS D 868
REMARK 465 HIS D 869
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 ASP A 55 62.46 60.01
REMARK 500 PRO A 116 -166.93 -70.39
REMARK 500 HIS A 118 -84.77 56.42
REMARK 500 SER A 156 -131.37 54.65
REMARK 500 VAL A 232 -72.75 -48.42
REMARK 500 ALA A 294 80.68 -69.59
REMARK 500 VAL A 419 -80.80 -94.52
REMARK 500 ASP A 477 51.16 -117.36
REMARK 500 THR A 521 143.30 -174.46
REMARK 500 ALA A 535 94.88 -67.58
REMARK 500 HIS A 586 40.29 -103.91
REMARK 500 TRP A 592 -64.87 -102.26
REMARK 500 ASP A 618 64.54 63.93
REMARK 500 TYR A 644 -66.73 -133.94
REMARK 500 TYR A 661 53.45 -103.23
REMARK 500 SER A 682 148.71 -39.86
REMARK 500 GLN A 684 -5.27 74.07
REMARK 500 GLN A 696 34.56 -148.18
REMARK 500 GLN A 699 -57.75 -133.73
REMARK 500 SER A 730 -118.55 59.93
REMARK 500 ALA A 754 48.70 37.18
REMARK 500 ASP A 772 -175.39 69.57
REMARK 500 ASN A 810 -67.38 -101.13
REMARK 500 ARG A 839 -138.48 -100.68
REMARK 500 ASP B 55 65.16 60.89
REMARK 500 HIS B 111 -85.23 54.16
REMARK 500 PHE B 112 146.51 67.78
REMARK 500 SER B 156 -138.08 60.47
REMARK 500 ASN B 157 51.26 -113.79
REMARK 500 SER B 158 -155.84 -162.13
REMARK 500 VAL B 172 -62.27 -108.95
REMARK 500 LEU B 233 -47.16 56.77
REMARK 500 THR B 308 128.21 -31.95
REMARK 500 PHE B 346 65.81 -118.30
REMARK 500 VAL B 412 -70.36 -75.60
REMARK 500 VAL B 419 -82.64 -103.56
REMARK 500 SER B 433 -78.03 -127.92
REMARK 500 LYS B 480 105.97 -52.57
REMARK 500 GLU B 486 87.77 -152.71
REMARK 500 GLU B 493 36.80 -85.31
REMARK 500 ALA B 498 -9.73 -142.60
REMARK 500 TYR B 644 -66.37 -127.88
REMARK 500 GLN B 696 36.99 -144.12
REMARK 500 SER B 730 -119.35 61.99
REMARK 500 ASP B 772 176.76 66.60
REMARK 500 ASN B 777 47.64 -147.25
REMARK 500 ASN B 810 -77.16 -91.97
REMARK 500 ARG B 839 -131.91 -94.79
REMARK 500 ASP C 55 66.60 61.86
REMARK 500 LYS C 93 -64.21 -100.65
REMARK 500
REMARK 500 THIS ENTRY HAS 94 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D1059 DISTANCE = 5.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9XH A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9XH B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9XH C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9XH D 901
DBREF 6EOR A 1 863 UNP Q86TI2 DPP9_HUMAN 1 863
DBREF 6EOR B 1 863 UNP Q86TI2 DPP9_HUMAN 1 863
DBREF 6EOR C 1 863 UNP Q86TI2 DPP9_HUMAN 1 863
DBREF 6EOR D 1 863 UNP Q86TI2 DPP9_HUMAN 1 863
SEQADV 6EOR HIS A 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS A 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS A 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS A 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS A 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS A 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS B 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS B 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS B 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS B 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS B 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS B 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS C 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS C 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS C 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS C 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS C 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS C 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS D 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS D 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS D 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS D 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS D 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOR HIS D 869 UNP Q86TI2 EXPRESSION TAG
SEQRES 1 A 869 MET ALA THR THR GLY THR PRO THR ALA ASP ARG GLY ASP
SEQRES 2 A 869 ALA ALA ALA THR ASP ASP PRO ALA ALA ARG PHE GLN VAL
SEQRES 3 A 869 GLN LYS HIS SER TRP ASP GLY LEU ARG SER ILE ILE HIS
SEQRES 4 A 869 GLY SER ARG LYS TYR SER GLY LEU ILE VAL ASN LYS ALA
SEQRES 5 A 869 PRO HIS ASP PHE GLN PHE VAL GLN LYS THR ASP GLU SER
SEQRES 6 A 869 GLY PRO HIS SER HIS ARG LEU TYR TYR LEU GLY MET PRO
SEQRES 7 A 869 TYR GLY SER ARG GLU ASN SER LEU LEU TYR SER GLU ILE
SEQRES 8 A 869 PRO LYS LYS VAL ARG LYS GLU ALA LEU LEU LEU LEU SER
SEQRES 9 A 869 TRP LYS GLN MET LEU ASP HIS PHE GLN ALA THR PRO HIS
SEQRES 10 A 869 HIS GLY VAL TYR SER ARG GLU GLU GLU LEU LEU ARG GLU
SEQRES 11 A 869 ARG LYS ARG LEU GLY VAL PHE GLY ILE THR SER TYR ASP
SEQRES 12 A 869 PHE HIS SER GLU SER GLY LEU PHE LEU PHE GLN ALA SER
SEQRES 13 A 869 ASN SER LEU PHE HIS CYS ARG ASP GLY GLY LYS ASN GLY
SEQRES 14 A 869 PHE MET VAL SER PRO MET LYS PRO LEU GLU ILE LYS THR
SEQRES 15 A 869 GLN CYS SER GLY PRO ARG MET ASP PRO LYS ILE CYS PRO
SEQRES 16 A 869 ALA ASP PRO ALA PHE PHE SER PHE ILE ASN ASN SER ASP
SEQRES 17 A 869 LEU TRP VAL ALA ASN ILE GLU THR GLY GLU GLU ARG ARG
SEQRES 18 A 869 LEU THR PHE CYS HIS GLN GLY LEU SER ASN VAL LEU ASP
SEQRES 19 A 869 ASP PRO LYS SER ALA GLY VAL ALA THR PHE VAL ILE GLN
SEQRES 20 A 869 GLU GLU PHE ASP ARG PHE THR GLY TYR TRP TRP CYS PRO
SEQRES 21 A 869 THR ALA SER TRP GLU GLY SER GLU GLY LEU LYS THR LEU
SEQRES 22 A 869 ARG ILE LEU TYR GLU GLU VAL ASP GLU SER GLU VAL GLU
SEQRES 23 A 869 VAL ILE HIS VAL PRO SER PRO ALA LEU GLU GLU ARG LYS
SEQRES 24 A 869 THR ASP SER TYR ARG TYR PRO ARG THR GLY SER LYS ASN
SEQRES 25 A 869 PRO LYS ILE ALA LEU LYS LEU ALA GLU PHE GLN THR ASP
SEQRES 26 A 869 SER GLN GLY LYS ILE VAL SER THR GLN GLU LYS GLU LEU
SEQRES 27 A 869 VAL GLN PRO PHE SER SER LEU PHE PRO LYS VAL GLU TYR
SEQRES 28 A 869 ILE ALA ARG ALA GLY TRP THR ARG ASP GLY LYS TYR ALA
SEQRES 29 A 869 TRP ALA MET PHE LEU ASP ARG PRO GLN GLN TRP LEU GLN
SEQRES 30 A 869 LEU VAL LEU LEU PRO PRO ALA LEU PHE ILE PRO SER THR
SEQRES 31 A 869 GLU ASN GLU GLU GLN ARG LEU ALA SER ALA ARG ALA VAL
SEQRES 32 A 869 PRO ARG ASN VAL GLN PRO TYR VAL VAL TYR GLU GLU VAL
SEQRES 33 A 869 THR ASN VAL TRP ILE ASN VAL HIS ASP ILE PHE TYR PRO
SEQRES 34 A 869 PHE PRO GLN SER GLU GLY GLU ASP GLU LEU CYS PHE LEU
SEQRES 35 A 869 ARG ALA ASN GLU CYS LYS THR GLY PHE CYS HIS LEU TYR
SEQRES 36 A 869 LYS VAL THR ALA VAL LEU LYS SER GLN GLY TYR ASP TRP
SEQRES 37 A 869 SER GLU PRO PHE SER PRO GLY GLU ASP GLU PHE LYS CYS
SEQRES 38 A 869 PRO ILE LYS GLU GLU ILE ALA LEU THR SER GLY GLU TRP
SEQRES 39 A 869 GLU VAL LEU ALA ARG HIS GLY SER LYS ILE TRP VAL ASN
SEQRES 40 A 869 GLU GLU THR LYS LEU VAL TYR PHE GLN GLY THR LYS ASP
SEQRES 41 A 869 THR PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR GLU
SEQRES 42 A 869 ALA ALA GLY GLU ILE VAL ARG LEU THR THR PRO GLY PHE
SEQRES 43 A 869 SER HIS SER CYS SER MET SER GLN ASN PHE ASP MET PHE
SEQRES 44 A 869 VAL SER HIS TYR SER SER VAL SER THR PRO PRO CYS VAL
SEQRES 45 A 869 HIS VAL TYR LYS LEU SER GLY PRO ASP ASP ASP PRO LEU
SEQRES 46 A 869 HIS LYS GLN PRO ARG PHE TRP ALA SER MET MET GLU ALA
SEQRES 47 A 869 ALA SER CYS PRO PRO ASP TYR VAL PRO PRO GLU ILE PHE
SEQRES 48 A 869 HIS PHE HIS THR ARG SER ASP VAL ARG LEU TYR GLY MET
SEQRES 49 A 869 ILE TYR LYS PRO HIS ALA LEU GLN PRO GLY LYS LYS HIS
SEQRES 50 A 869 PRO THR VAL LEU PHE VAL TYR GLY GLY PRO GLN VAL GLN
SEQRES 51 A 869 LEU VAL ASN ASN SER PHE LYS GLY ILE LYS TYR LEU ARG
SEQRES 52 A 869 LEU ASN THR LEU ALA SER LEU GLY TYR ALA VAL VAL VAL
SEQRES 53 A 869 ILE ASP GLY ARG GLY SER CYS GLN ARG GLY LEU ARG PHE
SEQRES 54 A 869 GLU GLY ALA LEU LYS ASN GLN MET GLY GLN VAL GLU ILE
SEQRES 55 A 869 GLU ASP GLN VAL GLU GLY LEU GLN PHE VAL ALA GLU LYS
SEQRES 56 A 869 TYR GLY PHE ILE ASP LEU SER ARG VAL ALA ILE HIS GLY
SEQRES 57 A 869 TRP SER TYR GLY GLY PHE LEU SER LEU MET GLY LEU ILE
SEQRES 58 A 869 HIS LYS PRO GLN VAL PHE LYS VAL ALA ILE ALA GLY ALA
SEQRES 59 A 869 PRO VAL THR VAL TRP MET ALA TYR ASP THR GLY TYR THR
SEQRES 60 A 869 GLU ARG TYR MET ASP VAL PRO GLU ASN ASN GLN HIS GLY
SEQRES 61 A 869 TYR GLU ALA GLY SER VAL ALA LEU HIS VAL GLU LYS LEU
SEQRES 62 A 869 PRO ASN GLU PRO ASN ARG LEU LEU ILE LEU HIS GLY PHE
SEQRES 63 A 869 LEU ASP GLU ASN VAL HIS PHE PHE HIS THR ASN PHE LEU
SEQRES 64 A 869 VAL SER GLN LEU ILE ARG ALA GLY LYS PRO TYR GLN LEU
SEQRES 65 A 869 GLN ILE TYR PRO ASN GLU ARG HIS SER ILE ARG CYS PRO
SEQRES 66 A 869 GLU SER GLY GLU HIS TYR GLU VAL THR LEU LEU HIS PHE
SEQRES 67 A 869 LEU GLN GLU TYR LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 869 MET ALA THR THR GLY THR PRO THR ALA ASP ARG GLY ASP
SEQRES 2 B 869 ALA ALA ALA THR ASP ASP PRO ALA ALA ARG PHE GLN VAL
SEQRES 3 B 869 GLN LYS HIS SER TRP ASP GLY LEU ARG SER ILE ILE HIS
SEQRES 4 B 869 GLY SER ARG LYS TYR SER GLY LEU ILE VAL ASN LYS ALA
SEQRES 5 B 869 PRO HIS ASP PHE GLN PHE VAL GLN LYS THR ASP GLU SER
SEQRES 6 B 869 GLY PRO HIS SER HIS ARG LEU TYR TYR LEU GLY MET PRO
SEQRES 7 B 869 TYR GLY SER ARG GLU ASN SER LEU LEU TYR SER GLU ILE
SEQRES 8 B 869 PRO LYS LYS VAL ARG LYS GLU ALA LEU LEU LEU LEU SER
SEQRES 9 B 869 TRP LYS GLN MET LEU ASP HIS PHE GLN ALA THR PRO HIS
SEQRES 10 B 869 HIS GLY VAL TYR SER ARG GLU GLU GLU LEU LEU ARG GLU
SEQRES 11 B 869 ARG LYS ARG LEU GLY VAL PHE GLY ILE THR SER TYR ASP
SEQRES 12 B 869 PHE HIS SER GLU SER GLY LEU PHE LEU PHE GLN ALA SER
SEQRES 13 B 869 ASN SER LEU PHE HIS CYS ARG ASP GLY GLY LYS ASN GLY
SEQRES 14 B 869 PHE MET VAL SER PRO MET LYS PRO LEU GLU ILE LYS THR
SEQRES 15 B 869 GLN CYS SER GLY PRO ARG MET ASP PRO LYS ILE CYS PRO
SEQRES 16 B 869 ALA ASP PRO ALA PHE PHE SER PHE ILE ASN ASN SER ASP
SEQRES 17 B 869 LEU TRP VAL ALA ASN ILE GLU THR GLY GLU GLU ARG ARG
SEQRES 18 B 869 LEU THR PHE CYS HIS GLN GLY LEU SER ASN VAL LEU ASP
SEQRES 19 B 869 ASP PRO LYS SER ALA GLY VAL ALA THR PHE VAL ILE GLN
SEQRES 20 B 869 GLU GLU PHE ASP ARG PHE THR GLY TYR TRP TRP CYS PRO
SEQRES 21 B 869 THR ALA SER TRP GLU GLY SER GLU GLY LEU LYS THR LEU
SEQRES 22 B 869 ARG ILE LEU TYR GLU GLU VAL ASP GLU SER GLU VAL GLU
SEQRES 23 B 869 VAL ILE HIS VAL PRO SER PRO ALA LEU GLU GLU ARG LYS
SEQRES 24 B 869 THR ASP SER TYR ARG TYR PRO ARG THR GLY SER LYS ASN
SEQRES 25 B 869 PRO LYS ILE ALA LEU LYS LEU ALA GLU PHE GLN THR ASP
SEQRES 26 B 869 SER GLN GLY LYS ILE VAL SER THR GLN GLU LYS GLU LEU
SEQRES 27 B 869 VAL GLN PRO PHE SER SER LEU PHE PRO LYS VAL GLU TYR
SEQRES 28 B 869 ILE ALA ARG ALA GLY TRP THR ARG ASP GLY LYS TYR ALA
SEQRES 29 B 869 TRP ALA MET PHE LEU ASP ARG PRO GLN GLN TRP LEU GLN
SEQRES 30 B 869 LEU VAL LEU LEU PRO PRO ALA LEU PHE ILE PRO SER THR
SEQRES 31 B 869 GLU ASN GLU GLU GLN ARG LEU ALA SER ALA ARG ALA VAL
SEQRES 32 B 869 PRO ARG ASN VAL GLN PRO TYR VAL VAL TYR GLU GLU VAL
SEQRES 33 B 869 THR ASN VAL TRP ILE ASN VAL HIS ASP ILE PHE TYR PRO
SEQRES 34 B 869 PHE PRO GLN SER GLU GLY GLU ASP GLU LEU CYS PHE LEU
SEQRES 35 B 869 ARG ALA ASN GLU CYS LYS THR GLY PHE CYS HIS LEU TYR
SEQRES 36 B 869 LYS VAL THR ALA VAL LEU LYS SER GLN GLY TYR ASP TRP
SEQRES 37 B 869 SER GLU PRO PHE SER PRO GLY GLU ASP GLU PHE LYS CYS
SEQRES 38 B 869 PRO ILE LYS GLU GLU ILE ALA LEU THR SER GLY GLU TRP
SEQRES 39 B 869 GLU VAL LEU ALA ARG HIS GLY SER LYS ILE TRP VAL ASN
SEQRES 40 B 869 GLU GLU THR LYS LEU VAL TYR PHE GLN GLY THR LYS ASP
SEQRES 41 B 869 THR PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR GLU
SEQRES 42 B 869 ALA ALA GLY GLU ILE VAL ARG LEU THR THR PRO GLY PHE
SEQRES 43 B 869 SER HIS SER CYS SER MET SER GLN ASN PHE ASP MET PHE
SEQRES 44 B 869 VAL SER HIS TYR SER SER VAL SER THR PRO PRO CYS VAL
SEQRES 45 B 869 HIS VAL TYR LYS LEU SER GLY PRO ASP ASP ASP PRO LEU
SEQRES 46 B 869 HIS LYS GLN PRO ARG PHE TRP ALA SER MET MET GLU ALA
SEQRES 47 B 869 ALA SER CYS PRO PRO ASP TYR VAL PRO PRO GLU ILE PHE
SEQRES 48 B 869 HIS PHE HIS THR ARG SER ASP VAL ARG LEU TYR GLY MET
SEQRES 49 B 869 ILE TYR LYS PRO HIS ALA LEU GLN PRO GLY LYS LYS HIS
SEQRES 50 B 869 PRO THR VAL LEU PHE VAL TYR GLY GLY PRO GLN VAL GLN
SEQRES 51 B 869 LEU VAL ASN ASN SER PHE LYS GLY ILE LYS TYR LEU ARG
SEQRES 52 B 869 LEU ASN THR LEU ALA SER LEU GLY TYR ALA VAL VAL VAL
SEQRES 53 B 869 ILE ASP GLY ARG GLY SER CYS GLN ARG GLY LEU ARG PHE
SEQRES 54 B 869 GLU GLY ALA LEU LYS ASN GLN MET GLY GLN VAL GLU ILE
SEQRES 55 B 869 GLU ASP GLN VAL GLU GLY LEU GLN PHE VAL ALA GLU LYS
SEQRES 56 B 869 TYR GLY PHE ILE ASP LEU SER ARG VAL ALA ILE HIS GLY
SEQRES 57 B 869 TRP SER TYR GLY GLY PHE LEU SER LEU MET GLY LEU ILE
SEQRES 58 B 869 HIS LYS PRO GLN VAL PHE LYS VAL ALA ILE ALA GLY ALA
SEQRES 59 B 869 PRO VAL THR VAL TRP MET ALA TYR ASP THR GLY TYR THR
SEQRES 60 B 869 GLU ARG TYR MET ASP VAL PRO GLU ASN ASN GLN HIS GLY
SEQRES 61 B 869 TYR GLU ALA GLY SER VAL ALA LEU HIS VAL GLU LYS LEU
SEQRES 62 B 869 PRO ASN GLU PRO ASN ARG LEU LEU ILE LEU HIS GLY PHE
SEQRES 63 B 869 LEU ASP GLU ASN VAL HIS PHE PHE HIS THR ASN PHE LEU
SEQRES 64 B 869 VAL SER GLN LEU ILE ARG ALA GLY LYS PRO TYR GLN LEU
SEQRES 65 B 869 GLN ILE TYR PRO ASN GLU ARG HIS SER ILE ARG CYS PRO
SEQRES 66 B 869 GLU SER GLY GLU HIS TYR GLU VAL THR LEU LEU HIS PHE
SEQRES 67 B 869 LEU GLN GLU TYR LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 869 MET ALA THR THR GLY THR PRO THR ALA ASP ARG GLY ASP
SEQRES 2 C 869 ALA ALA ALA THR ASP ASP PRO ALA ALA ARG PHE GLN VAL
SEQRES 3 C 869 GLN LYS HIS SER TRP ASP GLY LEU ARG SER ILE ILE HIS
SEQRES 4 C 869 GLY SER ARG LYS TYR SER GLY LEU ILE VAL ASN LYS ALA
SEQRES 5 C 869 PRO HIS ASP PHE GLN PHE VAL GLN LYS THR ASP GLU SER
SEQRES 6 C 869 GLY PRO HIS SER HIS ARG LEU TYR TYR LEU GLY MET PRO
SEQRES 7 C 869 TYR GLY SER ARG GLU ASN SER LEU LEU TYR SER GLU ILE
SEQRES 8 C 869 PRO LYS LYS VAL ARG LYS GLU ALA LEU LEU LEU LEU SER
SEQRES 9 C 869 TRP LYS GLN MET LEU ASP HIS PHE GLN ALA THR PRO HIS
SEQRES 10 C 869 HIS GLY VAL TYR SER ARG GLU GLU GLU LEU LEU ARG GLU
SEQRES 11 C 869 ARG LYS ARG LEU GLY VAL PHE GLY ILE THR SER TYR ASP
SEQRES 12 C 869 PHE HIS SER GLU SER GLY LEU PHE LEU PHE GLN ALA SER
SEQRES 13 C 869 ASN SER LEU PHE HIS CYS ARG ASP GLY GLY LYS ASN GLY
SEQRES 14 C 869 PHE MET VAL SER PRO MET LYS PRO LEU GLU ILE LYS THR
SEQRES 15 C 869 GLN CYS SER GLY PRO ARG MET ASP PRO LYS ILE CYS PRO
SEQRES 16 C 869 ALA ASP PRO ALA PHE PHE SER PHE ILE ASN ASN SER ASP
SEQRES 17 C 869 LEU TRP VAL ALA ASN ILE GLU THR GLY GLU GLU ARG ARG
SEQRES 18 C 869 LEU THR PHE CYS HIS GLN GLY LEU SER ASN VAL LEU ASP
SEQRES 19 C 869 ASP PRO LYS SER ALA GLY VAL ALA THR PHE VAL ILE GLN
SEQRES 20 C 869 GLU GLU PHE ASP ARG PHE THR GLY TYR TRP TRP CYS PRO
SEQRES 21 C 869 THR ALA SER TRP GLU GLY SER GLU GLY LEU LYS THR LEU
SEQRES 22 C 869 ARG ILE LEU TYR GLU GLU VAL ASP GLU SER GLU VAL GLU
SEQRES 23 C 869 VAL ILE HIS VAL PRO SER PRO ALA LEU GLU GLU ARG LYS
SEQRES 24 C 869 THR ASP SER TYR ARG TYR PRO ARG THR GLY SER LYS ASN
SEQRES 25 C 869 PRO LYS ILE ALA LEU LYS LEU ALA GLU PHE GLN THR ASP
SEQRES 26 C 869 SER GLN GLY LYS ILE VAL SER THR GLN GLU LYS GLU LEU
SEQRES 27 C 869 VAL GLN PRO PHE SER SER LEU PHE PRO LYS VAL GLU TYR
SEQRES 28 C 869 ILE ALA ARG ALA GLY TRP THR ARG ASP GLY LYS TYR ALA
SEQRES 29 C 869 TRP ALA MET PHE LEU ASP ARG PRO GLN GLN TRP LEU GLN
SEQRES 30 C 869 LEU VAL LEU LEU PRO PRO ALA LEU PHE ILE PRO SER THR
SEQRES 31 C 869 GLU ASN GLU GLU GLN ARG LEU ALA SER ALA ARG ALA VAL
SEQRES 32 C 869 PRO ARG ASN VAL GLN PRO TYR VAL VAL TYR GLU GLU VAL
SEQRES 33 C 869 THR ASN VAL TRP ILE ASN VAL HIS ASP ILE PHE TYR PRO
SEQRES 34 C 869 PHE PRO GLN SER GLU GLY GLU ASP GLU LEU CYS PHE LEU
SEQRES 35 C 869 ARG ALA ASN GLU CYS LYS THR GLY PHE CYS HIS LEU TYR
SEQRES 36 C 869 LYS VAL THR ALA VAL LEU LYS SER GLN GLY TYR ASP TRP
SEQRES 37 C 869 SER GLU PRO PHE SER PRO GLY GLU ASP GLU PHE LYS CYS
SEQRES 38 C 869 PRO ILE LYS GLU GLU ILE ALA LEU THR SER GLY GLU TRP
SEQRES 39 C 869 GLU VAL LEU ALA ARG HIS GLY SER LYS ILE TRP VAL ASN
SEQRES 40 C 869 GLU GLU THR LYS LEU VAL TYR PHE GLN GLY THR LYS ASP
SEQRES 41 C 869 THR PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR GLU
SEQRES 42 C 869 ALA ALA GLY GLU ILE VAL ARG LEU THR THR PRO GLY PHE
SEQRES 43 C 869 SER HIS SER CYS SER MET SER GLN ASN PHE ASP MET PHE
SEQRES 44 C 869 VAL SER HIS TYR SER SER VAL SER THR PRO PRO CYS VAL
SEQRES 45 C 869 HIS VAL TYR LYS LEU SER GLY PRO ASP ASP ASP PRO LEU
SEQRES 46 C 869 HIS LYS GLN PRO ARG PHE TRP ALA SER MET MET GLU ALA
SEQRES 47 C 869 ALA SER CYS PRO PRO ASP TYR VAL PRO PRO GLU ILE PHE
SEQRES 48 C 869 HIS PHE HIS THR ARG SER ASP VAL ARG LEU TYR GLY MET
SEQRES 49 C 869 ILE TYR LYS PRO HIS ALA LEU GLN PRO GLY LYS LYS HIS
SEQRES 50 C 869 PRO THR VAL LEU PHE VAL TYR GLY GLY PRO GLN VAL GLN
SEQRES 51 C 869 LEU VAL ASN ASN SER PHE LYS GLY ILE LYS TYR LEU ARG
SEQRES 52 C 869 LEU ASN THR LEU ALA SER LEU GLY TYR ALA VAL VAL VAL
SEQRES 53 C 869 ILE ASP GLY ARG GLY SER CYS GLN ARG GLY LEU ARG PHE
SEQRES 54 C 869 GLU GLY ALA LEU LYS ASN GLN MET GLY GLN VAL GLU ILE
SEQRES 55 C 869 GLU ASP GLN VAL GLU GLY LEU GLN PHE VAL ALA GLU LYS
SEQRES 56 C 869 TYR GLY PHE ILE ASP LEU SER ARG VAL ALA ILE HIS GLY
SEQRES 57 C 869 TRP SER TYR GLY GLY PHE LEU SER LEU MET GLY LEU ILE
SEQRES 58 C 869 HIS LYS PRO GLN VAL PHE LYS VAL ALA ILE ALA GLY ALA
SEQRES 59 C 869 PRO VAL THR VAL TRP MET ALA TYR ASP THR GLY TYR THR
SEQRES 60 C 869 GLU ARG TYR MET ASP VAL PRO GLU ASN ASN GLN HIS GLY
SEQRES 61 C 869 TYR GLU ALA GLY SER VAL ALA LEU HIS VAL GLU LYS LEU
SEQRES 62 C 869 PRO ASN GLU PRO ASN ARG LEU LEU ILE LEU HIS GLY PHE
SEQRES 63 C 869 LEU ASP GLU ASN VAL HIS PHE PHE HIS THR ASN PHE LEU
SEQRES 64 C 869 VAL SER GLN LEU ILE ARG ALA GLY LYS PRO TYR GLN LEU
SEQRES 65 C 869 GLN ILE TYR PRO ASN GLU ARG HIS SER ILE ARG CYS PRO
SEQRES 66 C 869 GLU SER GLY GLU HIS TYR GLU VAL THR LEU LEU HIS PHE
SEQRES 67 C 869 LEU GLN GLU TYR LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 869 MET ALA THR THR GLY THR PRO THR ALA ASP ARG GLY ASP
SEQRES 2 D 869 ALA ALA ALA THR ASP ASP PRO ALA ALA ARG PHE GLN VAL
SEQRES 3 D 869 GLN LYS HIS SER TRP ASP GLY LEU ARG SER ILE ILE HIS
SEQRES 4 D 869 GLY SER ARG LYS TYR SER GLY LEU ILE VAL ASN LYS ALA
SEQRES 5 D 869 PRO HIS ASP PHE GLN PHE VAL GLN LYS THR ASP GLU SER
SEQRES 6 D 869 GLY PRO HIS SER HIS ARG LEU TYR TYR LEU GLY MET PRO
SEQRES 7 D 869 TYR GLY SER ARG GLU ASN SER LEU LEU TYR SER GLU ILE
SEQRES 8 D 869 PRO LYS LYS VAL ARG LYS GLU ALA LEU LEU LEU LEU SER
SEQRES 9 D 869 TRP LYS GLN MET LEU ASP HIS PHE GLN ALA THR PRO HIS
SEQRES 10 D 869 HIS GLY VAL TYR SER ARG GLU GLU GLU LEU LEU ARG GLU
SEQRES 11 D 869 ARG LYS ARG LEU GLY VAL PHE GLY ILE THR SER TYR ASP
SEQRES 12 D 869 PHE HIS SER GLU SER GLY LEU PHE LEU PHE GLN ALA SER
SEQRES 13 D 869 ASN SER LEU PHE HIS CYS ARG ASP GLY GLY LYS ASN GLY
SEQRES 14 D 869 PHE MET VAL SER PRO MET LYS PRO LEU GLU ILE LYS THR
SEQRES 15 D 869 GLN CYS SER GLY PRO ARG MET ASP PRO LYS ILE CYS PRO
SEQRES 16 D 869 ALA ASP PRO ALA PHE PHE SER PHE ILE ASN ASN SER ASP
SEQRES 17 D 869 LEU TRP VAL ALA ASN ILE GLU THR GLY GLU GLU ARG ARG
SEQRES 18 D 869 LEU THR PHE CYS HIS GLN GLY LEU SER ASN VAL LEU ASP
SEQRES 19 D 869 ASP PRO LYS SER ALA GLY VAL ALA THR PHE VAL ILE GLN
SEQRES 20 D 869 GLU GLU PHE ASP ARG PHE THR GLY TYR TRP TRP CYS PRO
SEQRES 21 D 869 THR ALA SER TRP GLU GLY SER GLU GLY LEU LYS THR LEU
SEQRES 22 D 869 ARG ILE LEU TYR GLU GLU VAL ASP GLU SER GLU VAL GLU
SEQRES 23 D 869 VAL ILE HIS VAL PRO SER PRO ALA LEU GLU GLU ARG LYS
SEQRES 24 D 869 THR ASP SER TYR ARG TYR PRO ARG THR GLY SER LYS ASN
SEQRES 25 D 869 PRO LYS ILE ALA LEU LYS LEU ALA GLU PHE GLN THR ASP
SEQRES 26 D 869 SER GLN GLY LYS ILE VAL SER THR GLN GLU LYS GLU LEU
SEQRES 27 D 869 VAL GLN PRO PHE SER SER LEU PHE PRO LYS VAL GLU TYR
SEQRES 28 D 869 ILE ALA ARG ALA GLY TRP THR ARG ASP GLY LYS TYR ALA
SEQRES 29 D 869 TRP ALA MET PHE LEU ASP ARG PRO GLN GLN TRP LEU GLN
SEQRES 30 D 869 LEU VAL LEU LEU PRO PRO ALA LEU PHE ILE PRO SER THR
SEQRES 31 D 869 GLU ASN GLU GLU GLN ARG LEU ALA SER ALA ARG ALA VAL
SEQRES 32 D 869 PRO ARG ASN VAL GLN PRO TYR VAL VAL TYR GLU GLU VAL
SEQRES 33 D 869 THR ASN VAL TRP ILE ASN VAL HIS ASP ILE PHE TYR PRO
SEQRES 34 D 869 PHE PRO GLN SER GLU GLY GLU ASP GLU LEU CYS PHE LEU
SEQRES 35 D 869 ARG ALA ASN GLU CYS LYS THR GLY PHE CYS HIS LEU TYR
SEQRES 36 D 869 LYS VAL THR ALA VAL LEU LYS SER GLN GLY TYR ASP TRP
SEQRES 37 D 869 SER GLU PRO PHE SER PRO GLY GLU ASP GLU PHE LYS CYS
SEQRES 38 D 869 PRO ILE LYS GLU GLU ILE ALA LEU THR SER GLY GLU TRP
SEQRES 39 D 869 GLU VAL LEU ALA ARG HIS GLY SER LYS ILE TRP VAL ASN
SEQRES 40 D 869 GLU GLU THR LYS LEU VAL TYR PHE GLN GLY THR LYS ASP
SEQRES 41 D 869 THR PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR GLU
SEQRES 42 D 869 ALA ALA GLY GLU ILE VAL ARG LEU THR THR PRO GLY PHE
SEQRES 43 D 869 SER HIS SER CYS SER MET SER GLN ASN PHE ASP MET PHE
SEQRES 44 D 869 VAL SER HIS TYR SER SER VAL SER THR PRO PRO CYS VAL
SEQRES 45 D 869 HIS VAL TYR LYS LEU SER GLY PRO ASP ASP ASP PRO LEU
SEQRES 46 D 869 HIS LYS GLN PRO ARG PHE TRP ALA SER MET MET GLU ALA
SEQRES 47 D 869 ALA SER CYS PRO PRO ASP TYR VAL PRO PRO GLU ILE PHE
SEQRES 48 D 869 HIS PHE HIS THR ARG SER ASP VAL ARG LEU TYR GLY MET
SEQRES 49 D 869 ILE TYR LYS PRO HIS ALA LEU GLN PRO GLY LYS LYS HIS
SEQRES 50 D 869 PRO THR VAL LEU PHE VAL TYR GLY GLY PRO GLN VAL GLN
SEQRES 51 D 869 LEU VAL ASN ASN SER PHE LYS GLY ILE LYS TYR LEU ARG
SEQRES 52 D 869 LEU ASN THR LEU ALA SER LEU GLY TYR ALA VAL VAL VAL
SEQRES 53 D 869 ILE ASP GLY ARG GLY SER CYS GLN ARG GLY LEU ARG PHE
SEQRES 54 D 869 GLU GLY ALA LEU LYS ASN GLN MET GLY GLN VAL GLU ILE
SEQRES 55 D 869 GLU ASP GLN VAL GLU GLY LEU GLN PHE VAL ALA GLU LYS
SEQRES 56 D 869 TYR GLY PHE ILE ASP LEU SER ARG VAL ALA ILE HIS GLY
SEQRES 57 D 869 TRP SER TYR GLY GLY PHE LEU SER LEU MET GLY LEU ILE
SEQRES 58 D 869 HIS LYS PRO GLN VAL PHE LYS VAL ALA ILE ALA GLY ALA
SEQRES 59 D 869 PRO VAL THR VAL TRP MET ALA TYR ASP THR GLY TYR THR
SEQRES 60 D 869 GLU ARG TYR MET ASP VAL PRO GLU ASN ASN GLN HIS GLY
SEQRES 61 D 869 TYR GLU ALA GLY SER VAL ALA LEU HIS VAL GLU LYS LEU
SEQRES 62 D 869 PRO ASN GLU PRO ASN ARG LEU LEU ILE LEU HIS GLY PHE
SEQRES 63 D 869 LEU ASP GLU ASN VAL HIS PHE PHE HIS THR ASN PHE LEU
SEQRES 64 D 869 VAL SER GLN LEU ILE ARG ALA GLY LYS PRO TYR GLN LEU
SEQRES 65 D 869 GLN ILE TYR PRO ASN GLU ARG HIS SER ILE ARG CYS PRO
SEQRES 66 D 869 GLU SER GLY GLU HIS TYR GLU VAL THR LEU LEU HIS PHE
SEQRES 67 D 869 LEU GLN GLU TYR LEU HIS HIS HIS HIS HIS HIS
HET 9XH A 901 37
HET 9XH B 901 37
HET 9XH C 901 37
HET 9XH D 901 37
HETNAM 9XH (2~{S})-2-AZANYL-4-[4-[BIS(4-FLUOROPHENYL)
HETNAM 2 9XH METHYL]PIPERAZIN-1-YL]-1-(1,3-DIHYDROISOINDOL-2-YL)
HETNAM 3 9XH BUTANE-1,4-DIONE
FORMUL 5 9XH 4(C29 H30 F2 N4 O2)
FORMUL 9 HOH *231(H2 O)
HELIX 1 AA1 SER A 30 ARG A 42 1 13
HELIX 2 AA2 SER A 122 LYS A 132 1 11
HELIX 3 AA3 THR A 243 ASP A 251 1 9
HELIX 4 AA4 PRO A 341 PHE A 346 1 6
HELIX 5 AA5 PRO A 382 ALA A 384 5 3
HELIX 6 AA6 ASN A 392 VAL A 403 1 12
HELIX 7 AA7 ASP A 583 LYS A 587 5 5
HELIX 8 AA8 TYR A 661 GLY A 671 1 11
HELIX 9 AA9 GLY A 686 ALA A 692 1 7
HELIX 10 AB1 GLN A 699 TYR A 716 1 18
HELIX 11 AB2 SER A 730 LYS A 743 1 14
HELIX 12 AB3 VAL A 758 TYR A 762 5 5
HELIX 13 AB4 ASP A 763 ASP A 772 1 10
HELIX 14 AB5 VAL A 773 ASN A 776 5 4
HELIX 15 AB6 ASN A 777 GLY A 784 1 8
HELIX 16 AB7 SER A 785 LEU A 793 5 9
HELIX 17 AB8 PHE A 813 GLY A 827 1 15
HELIX 18 AB9 CYS A 844 LEU A 863 1 20
HELIX 19 AC1 SER B 30 ARG B 42 1 13
HELIX 20 AC2 PRO B 116 VAL B 120 5 5
HELIX 21 AC3 SER B 122 GLU B 130 1 9
HELIX 22 AC4 THR B 243 ASP B 251 1 9
HELIX 23 AC5 ALA B 294 ARG B 298 5 5
HELIX 24 AC6 PRO B 341 PHE B 346 1 6
HELIX 25 AC7 PRO B 382 ALA B 384 5 3
HELIX 26 AC8 ASN B 392 VAL B 403 1 12
HELIX 27 AC9 TYR B 661 LEU B 670 1 10
HELIX 28 AD1 GLY B 686 ALA B 692 1 7
HELIX 29 AD2 VAL B 700 TYR B 716 1 17
HELIX 30 AD3 SER B 730 LYS B 743 1 14
HELIX 31 AD4 VAL B 758 TYR B 762 5 5
HELIX 32 AD5 ASP B 763 ASP B 772 1 10
HELIX 33 AD6 VAL B 773 ASN B 776 5 4
HELIX 34 AD7 ASN B 777 GLY B 784 1 8
HELIX 35 AD8 SER B 785 LEU B 793 5 9
HELIX 36 AD9 PHE B 813 GLY B 827 1 15
HELIX 37 AE1 CYS B 844 LEU B 863 1 20
HELIX 38 AE2 SER C 30 ARG C 42 1 13
HELIX 39 AE3 SER C 122 LYS C 132 1 11
HELIX 40 AE4 THR C 243 ASP C 251 1 9
HELIX 41 AE5 PRO C 341 PHE C 346 1 6
HELIX 42 AE6 PRO C 382 ALA C 384 5 3
HELIX 43 AE7 ASN C 392 VAL C 403 1 12
HELIX 44 AE8 TYR C 661 LEU C 670 1 10
HELIX 45 AE9 GLY C 686 GLY C 691 1 6
HELIX 46 AF1 ALA C 692 LYS C 694 5 3
HELIX 47 AF2 VAL C 700 TYR C 716 1 17
HELIX 48 AF3 SER C 730 LYS C 743 1 14
HELIX 49 AF4 VAL C 758 TYR C 762 5 5
HELIX 50 AF5 ASP C 763 ASP C 772 1 10
HELIX 51 AF6 VAL C 773 ASN C 776 5 4
HELIX 52 AF7 ASN C 777 GLY C 784 1 8
HELIX 53 AF8 SER C 785 LEU C 793 5 9
HELIX 54 AF9 PHE C 813 ALA C 826 1 14
HELIX 55 AG1 CYS C 844 LEU C 863 1 20
HELIX 56 AG2 SER D 30 ARG D 42 1 13
HELIX 57 AG3 PRO D 116 VAL D 120 5 5
HELIX 58 AG4 SER D 122 LYS D 132 1 11
HELIX 59 AG5 THR D 243 PHE D 250 1 8
HELIX 60 AG6 ALA D 294 ARG D 298 5 5
HELIX 61 AG7 PRO D 341 PHE D 346 1 6
HELIX 62 AG8 PRO D 382 ALA D 384 5 3
HELIX 63 AG9 ASN D 392 ALA D 402 1 11
HELIX 64 AH1 ASP D 583 LYS D 587 5 5
HELIX 65 AH2 TYR D 661 LEU D 670 1 10
HELIX 66 AH3 GLY D 686 GLY D 691 1 6
HELIX 67 AH4 ALA D 692 LYS D 694 5 3
HELIX 68 AH5 VAL D 700 TYR D 716 1 17
HELIX 69 AH6 SER D 730 LYS D 743 1 14
HELIX 70 AH7 VAL D 758 TYR D 762 5 5
HELIX 71 AH8 ASP D 763 ASP D 772 1 10
HELIX 72 AH9 VAL D 773 ASN D 776 5 4
HELIX 73 AI1 ASN D 777 GLY D 784 1 8
HELIX 74 AI2 SER D 785 LEU D 793 5 9
HELIX 75 AI3 PHE D 813 ALA D 826 1 14
HELIX 76 AI4 CYS D 844 LEU D 863 1 20
SHEET 1 AA1 4 HIS A 54 GLN A 60 0
SHEET 2 AA1 4 HIS A 70 GLY A 76 -1 O LEU A 75 N HIS A 54
SHEET 3 AA1 4 SER A 85 ILE A 91 -1 O LEU A 87 N TYR A 74
SHEET 4 AA1 4 LYS A 106 GLN A 107 -1 O LYS A 106 N TYR A 88
SHEET 1 AA2 4 ASP A 143 HIS A 145 0
SHEET 2 AA2 4 LEU A 150 GLN A 154 -1 O LEU A 152 N ASP A 143
SHEET 3 AA2 4 LEU A 159 ARG A 163 -1 O PHE A 160 N PHE A 153
SHEET 4 AA2 4 LEU A 178 GLU A 179 -1 O LEU A 178 N HIS A 161
SHEET 1 AA3 4 MET A 189 ILE A 193 0
SHEET 2 AA3 4 PHE A 200 ASN A 205 -1 O ILE A 204 N MET A 189
SHEET 3 AA3 4 ASP A 208 ASN A 213 -1 O TRP A 210 N PHE A 203
SHEET 4 AA3 4 GLU A 219 ARG A 221 -1 O ARG A 220 N VAL A 211
SHEET 1 AA4 3 LYS A 237 ALA A 239 0
SHEET 2 AA4 3 LYS A 271 ASP A 281 -1 O VAL A 280 N SER A 238
SHEET 3 AA4 3 TYR A 256 TRP A 258 -1 N TRP A 257 O LEU A 276
SHEET 1 AA5 5 LYS A 237 ALA A 239 0
SHEET 2 AA5 5 LYS A 271 ASP A 281 -1 O VAL A 280 N SER A 238
SHEET 3 AA5 5 LYS A 314 THR A 324 -1 O ALA A 316 N GLU A 279
SHEET 4 AA5 5 ILE A 330 LEU A 338 -1 O LYS A 336 N LEU A 319
SHEET 5 AA5 5 PHE A 386 PRO A 388 -1 O ILE A 387 N GLU A 337
SHEET 1 AA6 2 VAL A 287 PRO A 291 0
SHEET 2 AA6 2 THR A 300 ARG A 304 -1 O ASP A 301 N VAL A 290
SHEET 1 AA7 4 TYR A 351 TRP A 357 0
SHEET 2 AA7 4 ALA A 364 LEU A 369 -1 O TRP A 365 N GLY A 356
SHEET 3 AA7 4 TRP A 375 LEU A 381 -1 O GLN A 377 N PHE A 368
SHEET 4 AA7 4 TYR A 410 VAL A 416 -1 O TYR A 413 N LEU A 378
SHEET 1 AA8 4 PHE A 427 PRO A 429 0
SHEET 2 AA8 4 CYS A 440 ASN A 445 -1 O LEU A 442 N TYR A 428
SHEET 3 AA8 4 HIS A 453 ALA A 459 -1 O TYR A 455 N ARG A 443
SHEET 4 AA8 4 ILE A 483 ALA A 488 -1 O ILE A 487 N LYS A 456
SHEET 1 AA9 4 TRP A 505 ASN A 507 0
SHEET 2 AA9 4 LEU A 512 GLY A 517 -1 O TYR A 514 N TRP A 505
SHEET 3 AA9 4 HIS A 526 SER A 531 -1 O VAL A 530 N VAL A 513
SHEET 4 AA9 4 VAL A 539 ARG A 540 -1 O VAL A 539 N VAL A 529
SHEET 1 AB1 4 SER A 547 MET A 552 0
SHEET 2 AB1 4 MET A 558 SER A 564 -1 O HIS A 562 N SER A 549
SHEET 3 AB1 4 CYS A 571 SER A 578 -1 O CYS A 571 N TYR A 563
SHEET 4 AB1 4 GLN A 588 MET A 596 -1 O MET A 595 N VAL A 572
SHEET 1 AB2 8 GLU A 609 HIS A 614 0
SHEET 2 AB2 8 ARG A 620 TYR A 626 -1 O LEU A 621 N PHE A 613
SHEET 3 AB2 8 ALA A 673 ASP A 678 -1 O VAL A 674 N TYR A 626
SHEET 4 AB2 8 HIS A 637 PHE A 642 1 N VAL A 640 O ALA A 673
SHEET 5 AB2 8 ILE A 719 TRP A 729 1 O ARG A 723 N THR A 639
SHEET 6 AB2 8 VAL A 749 GLY A 753 1 O ILE A 751 N ILE A 726
SHEET 7 AB2 8 LEU A 800 GLY A 805 1 O LEU A 801 N ALA A 750
SHEET 8 AB2 8 GLN A 831 TYR A 835 1 O GLN A 831 N ILE A 802
SHEET 1 AB3 4 HIS B 54 GLN B 60 0
SHEET 2 AB3 4 HIS B 68 GLY B 76 -1 O TYR B 73 N GLN B 57
SHEET 3 AB3 4 SER B 85 PRO B 92 -1 O LEU B 87 N TYR B 74
SHEET 4 AB3 4 LYS B 106 GLN B 107 -1 O LYS B 106 N TYR B 88
SHEET 1 AB4 4 TYR B 142 HIS B 145 0
SHEET 2 AB4 4 LEU B 150 PHE B 153 -1 O LEU B 152 N ASP B 143
SHEET 3 AB4 4 PHE B 160 ARG B 163 -1 O CYS B 162 N PHE B 151
SHEET 4 AB4 4 LEU B 178 GLU B 179 -1 O LEU B 178 N HIS B 161
SHEET 1 AB5 4 MET B 189 ILE B 193 0
SHEET 2 AB5 4 PHE B 200 ILE B 204 -1 O ILE B 204 N MET B 189
SHEET 3 AB5 4 LEU B 209 ASN B 213 -1 O TRP B 210 N PHE B 203
SHEET 4 AB5 4 GLU B 219 ARG B 221 -1 O ARG B 220 N VAL B 211
SHEET 1 AB6 3 LYS B 237 ALA B 239 0
SHEET 2 AB6 3 LYS B 271 ASP B 281 -1 O VAL B 280 N SER B 238
SHEET 3 AB6 3 TYR B 256 TRP B 258 -1 N TRP B 257 O LEU B 276
SHEET 1 AB7 5 LYS B 237 ALA B 239 0
SHEET 2 AB7 5 LYS B 271 ASP B 281 -1 O VAL B 280 N SER B 238
SHEET 3 AB7 5 LYS B 314 THR B 324 -1 O ALA B 316 N GLU B 279
SHEET 4 AB7 5 ILE B 330 LEU B 338 -1 O GLN B 334 N GLU B 321
SHEET 5 AB7 5 PHE B 386 PRO B 388 -1 O ILE B 387 N GLU B 337
SHEET 1 AB8 2 VAL B 287 PRO B 291 0
SHEET 2 AB8 2 THR B 300 ARG B 304 -1 O ASP B 301 N VAL B 290
SHEET 1 AB9 4 VAL B 349 TRP B 357 0
SHEET 2 AB9 4 ALA B 364 ASP B 370 -1 O LEU B 369 N GLU B 350
SHEET 3 AB9 4 TRP B 375 LEU B 381 -1 O LEU B 381 N ALA B 364
SHEET 4 AB9 4 TYR B 410 VAL B 416 -1 O GLU B 415 N LEU B 376
SHEET 1 AC1 4 PHE B 427 PRO B 429 0
SHEET 2 AC1 4 GLU B 438 ASN B 445 -1 O LEU B 442 N TYR B 428
SHEET 3 AC1 4 HIS B 453 VAL B 460 -1 O VAL B 457 N PHE B 441
SHEET 4 AC1 4 ILE B 483 ALA B 488 -1 O LYS B 484 N THR B 458
SHEET 1 AC2 4 TRP B 505 ASN B 507 0
SHEET 2 AC2 4 LEU B 512 GLY B 517 -1 O TYR B 514 N TRP B 505
SHEET 3 AC2 4 HIS B 526 SER B 531 -1 O TYR B 528 N PHE B 515
SHEET 4 AC2 4 VAL B 539 ARG B 540 -1 O VAL B 539 N VAL B 529
SHEET 1 AC3 4 SER B 547 MET B 552 0
SHEET 2 AC3 4 MET B 558 SER B 564 -1 O HIS B 562 N SER B 549
SHEET 3 AC3 4 CYS B 571 SER B 578 -1 O TYR B 575 N PHE B 559
SHEET 4 AC3 4 GLN B 588 MET B 596 -1 O MET B 595 N VAL B 572
SHEET 1 AC4 8 GLU B 609 HIS B 614 0
SHEET 2 AC4 8 ARG B 620 TYR B 626 -1 O GLY B 623 N PHE B 611
SHEET 3 AC4 8 ALA B 673 ASP B 678 -1 O VAL B 674 N TYR B 626
SHEET 4 AC4 8 HIS B 637 PHE B 642 1 N VAL B 640 O ALA B 673
SHEET 5 AC4 8 ILE B 719 TRP B 729 1 O ALA B 725 N THR B 639
SHEET 6 AC4 8 VAL B 749 GLY B 753 1 O GLY B 753 N GLY B 728
SHEET 7 AC4 8 LEU B 800 GLY B 805 1 O LEU B 801 N ALA B 750
SHEET 8 AC4 8 GLN B 831 TYR B 835 1 O GLN B 833 N HIS B 804
SHEET 1 AC5 4 HIS C 54 GLN C 60 0
SHEET 2 AC5 4 HIS C 68 GLY C 76 -1 O LEU C 75 N HIS C 54
SHEET 3 AC5 4 SER C 85 PRO C 92 -1 O LEU C 87 N TYR C 74
SHEET 4 AC5 4 LYS C 106 GLN C 107 -1 O LYS C 106 N TYR C 88
SHEET 1 AC6 4 ASP C 143 HIS C 145 0
SHEET 2 AC6 4 LEU C 150 ALA C 155 -1 O LEU C 152 N ASP C 143
SHEET 3 AC6 4 SER C 158 ARG C 163 -1 O PHE C 160 N PHE C 153
SHEET 4 AC6 4 LEU C 178 GLU C 179 -1 O LEU C 178 N HIS C 161
SHEET 1 AC7 4 MET C 189 ILE C 193 0
SHEET 2 AC7 4 PHE C 200 ILE C 204 -1 O ILE C 204 N MET C 189
SHEET 3 AC7 4 LEU C 209 ASN C 213 -1 O TRP C 210 N PHE C 203
SHEET 4 AC7 4 GLU C 219 ARG C 221 -1 O ARG C 220 N VAL C 211
SHEET 1 AC8 3 LYS C 237 ALA C 239 0
SHEET 2 AC8 3 LYS C 271 ASP C 281 -1 O VAL C 280 N SER C 238
SHEET 3 AC8 3 TYR C 256 TRP C 258 -1 N TRP C 257 O LEU C 276
SHEET 1 AC9 5 LYS C 237 ALA C 239 0
SHEET 2 AC9 5 LYS C 271 ASP C 281 -1 O VAL C 280 N SER C 238
SHEET 3 AC9 5 LYS C 314 THR C 324 -1 O THR C 324 N LYS C 271
SHEET 4 AC9 5 ILE C 330 LEU C 338 -1 O LYS C 336 N LEU C 319
SHEET 5 AC9 5 PHE C 386 PRO C 388 -1 O ILE C 387 N GLU C 337
SHEET 1 AD1 2 VAL C 287 PRO C 291 0
SHEET 2 AD1 2 THR C 300 ARG C 304 -1 O ASP C 301 N VAL C 290
SHEET 1 AD2 4 TYR C 351 TRP C 357 0
SHEET 2 AD2 4 ALA C 364 LEU C 369 -1 O TRP C 365 N GLY C 356
SHEET 3 AD2 4 TRP C 375 LEU C 381 -1 O LEU C 381 N ALA C 364
SHEET 4 AD2 4 TYR C 410 VAL C 416 -1 O TYR C 410 N LEU C 380
SHEET 1 AD3 4 PHE C 427 PRO C 429 0
SHEET 2 AD3 4 LEU C 439 ASN C 445 -1 O LEU C 442 N TYR C 428
SHEET 3 AD3 4 HIS C 453 ALA C 459 -1 O VAL C 457 N PHE C 441
SHEET 4 AD3 4 ILE C 483 ALA C 488 -1 O ILE C 487 N LYS C 456
SHEET 1 AD4 4 TRP C 505 ASN C 507 0
SHEET 2 AD4 4 LEU C 512 GLY C 517 -1 O LEU C 512 N ASN C 507
SHEET 3 AD4 4 HIS C 526 SER C 531 -1 O TYR C 528 N PHE C 515
SHEET 4 AD4 4 VAL C 539 ARG C 540 -1 O VAL C 539 N VAL C 529
SHEET 1 AD5 4 SER C 547 MET C 552 0
SHEET 2 AD5 4 MET C 558 SER C 564 -1 O HIS C 562 N SER C 549
SHEET 3 AD5 4 CYS C 571 SER C 578 -1 O TYR C 575 N PHE C 559
SHEET 4 AD5 4 GLN C 588 MET C 596 -1 O ALA C 593 N VAL C 574
SHEET 1 AD6 8 GLU C 609 HIS C 614 0
SHEET 2 AD6 8 ARG C 620 TYR C 626 -1 O GLY C 623 N PHE C 611
SHEET 3 AD6 8 ALA C 673 ASP C 678 -1 O VAL C 676 N MET C 624
SHEET 4 AD6 8 HIS C 637 VAL C 643 1 N VAL C 640 O ALA C 673
SHEET 5 AD6 8 ILE C 719 TRP C 729 1 O ALA C 725 N LEU C 641
SHEET 6 AD6 8 PHE C 747 GLY C 753 1 O LYS C 748 N VAL C 724
SHEET 7 AD6 8 LEU C 800 GLY C 805 1 O LEU C 803 N ALA C 752
SHEET 8 AD6 8 GLN C 831 TYR C 835 1 O GLN C 833 N ILE C 802
SHEET 1 AD7 4 HIS D 54 GLN D 60 0
SHEET 2 AD7 4 HIS D 68 GLY D 76 -1 O LEU D 75 N HIS D 54
SHEET 3 AD7 4 SER D 85 PRO D 92 -1 O LEU D 87 N TYR D 74
SHEET 4 AD7 4 LYS D 106 GLN D 107 -1 O LYS D 106 N TYR D 88
SHEET 1 AD8 4 TYR D 142 HIS D 145 0
SHEET 2 AD8 4 LEU D 150 ALA D 155 -1 O LEU D 152 N ASP D 143
SHEET 3 AD8 4 SER D 158 ARG D 163 -1 O CYS D 162 N PHE D 151
SHEET 4 AD8 4 LEU D 178 GLU D 179 -1 O LEU D 178 N HIS D 161
SHEET 1 AD9 4 MET D 189 ILE D 193 0
SHEET 2 AD9 4 PHE D 200 ASN D 205 -1 O ILE D 204 N MET D 189
SHEET 3 AD9 4 ASP D 208 ASN D 213 -1 O TRP D 210 N PHE D 203
SHEET 4 AD9 4 GLU D 219 ARG D 221 -1 O ARG D 220 N VAL D 211
SHEET 1 AE1 3 LYS D 237 ALA D 239 0
SHEET 2 AE1 3 LYS D 271 ASP D 281 -1 O VAL D 280 N SER D 238
SHEET 3 AE1 3 TYR D 256 TRP D 258 -1 N TRP D 257 O LEU D 276
SHEET 1 AE2 5 LYS D 237 ALA D 239 0
SHEET 2 AE2 5 LYS D 271 ASP D 281 -1 O VAL D 280 N SER D 238
SHEET 3 AE2 5 LYS D 314 THR D 324 -1 O THR D 324 N LYS D 271
SHEET 4 AE2 5 ILE D 330 LEU D 338 -1 O GLN D 334 N GLU D 321
SHEET 5 AE2 5 PHE D 386 PRO D 388 -1 O ILE D 387 N GLU D 337
SHEET 1 AE3 2 VAL D 287 PRO D 291 0
SHEET 2 AE3 2 THR D 300 ARG D 304 -1 O ASP D 301 N VAL D 290
SHEET 1 AE4 4 TYR D 351 TRP D 357 0
SHEET 2 AE4 4 ALA D 364 LEU D 369 -1 O TRP D 365 N GLY D 356
SHEET 3 AE4 4 TRP D 375 LEU D 381 -1 O LEU D 381 N ALA D 364
SHEET 4 AE4 4 TYR D 410 VAL D 416 -1 O GLU D 415 N LEU D 376
SHEET 1 AE5 4 PHE D 427 PRO D 429 0
SHEET 2 AE5 4 LEU D 439 ASN D 445 -1 O LEU D 442 N TYR D 428
SHEET 3 AE5 4 HIS D 453 ALA D 459 -1 O ALA D 459 N LEU D 439
SHEET 4 AE5 4 ILE D 483 ALA D 488 -1 O ILE D 487 N LYS D 456
SHEET 1 AE6 4 ILE D 504 ASN D 507 0
SHEET 2 AE6 4 LEU D 512 THR D 521 -1 O TYR D 514 N TRP D 505
SHEET 3 AE6 4 GLU D 524 SER D 531 -1 O TYR D 528 N PHE D 515
SHEET 4 AE6 4 VAL D 539 ARG D 540 -1 O VAL D 539 N VAL D 529
SHEET 1 AE7 4 SER D 547 MET D 552 0
SHEET 2 AE7 4 MET D 558 SER D 564 -1 O HIS D 562 N SER D 549
SHEET 3 AE7 4 CYS D 571 SER D 578 -1 O TYR D 575 N PHE D 559
SHEET 4 AE7 4 GLN D 588 MET D 596 -1 O ALA D 593 N VAL D 574
SHEET 1 AE8 8 GLU D 609 HIS D 614 0
SHEET 2 AE8 8 ARG D 620 TYR D 626 -1 O LEU D 621 N PHE D 613
SHEET 3 AE8 8 ALA D 673 ASP D 678 -1 O VAL D 676 N MET D 624
SHEET 4 AE8 8 HIS D 637 VAL D 643 1 N VAL D 640 O ALA D 673
SHEET 5 AE8 8 ILE D 719 TRP D 729 1 O ARG D 723 N THR D 639
SHEET 6 AE8 8 VAL D 749 GLY D 753 1 O GLY D 753 N GLY D 728
SHEET 7 AE8 8 LEU D 800 GLY D 805 1 O LEU D 803 N ALA D 752
SHEET 8 AE8 8 GLN D 831 TYR D 835 1 O GLN D 831 N ILE D 802
SITE 1 AC1 16 ARG A 133 GLU A 248 GLU A 249 TYR A 644
SITE 2 AC1 16 GLN A 648 SER A 730 TYR A 731 VAL A 756
SITE 3 AC1 16 TYR A 762 TYR A 766 ASN A 810 VAL A 811
SITE 4 AC1 16 HIS A 840 HOH A1029 HOH A1036 HOH A1056
SITE 1 AC2 15 ARG B 133 GLU B 248 GLU B 249 TYR B 644
SITE 2 AC2 15 GLN B 648 SER B 730 TYR B 731 VAL B 756
SITE 3 AC2 15 TRP B 759 TYR B 762 TYR B 766 ASN B 810
SITE 4 AC2 15 VAL B 811 HOH B1019 HOH B1027
SITE 1 AC3 12 ARG C 133 GLU C 248 GLU C 249 TYR C 644
SITE 2 AC3 12 GLN C 648 SER C 730 TYR C 731 VAL C 756
SITE 3 AC3 12 TRP C 759 TYR C 762 TYR C 766 ASN C 810
SITE 1 AC4 16 ARG D 133 GLU D 248 GLU D 249 TYR D 644
SITE 2 AC4 16 GLN D 648 VAL D 649 SER D 730 TYR D 731
SITE 3 AC4 16 VAL D 756 TRP D 759 TYR D 762 TYR D 766
SITE 4 AC4 16 ASN D 810 VAL D 811 HIS D 840 SER D 841
CRYST1 119.357 117.212 163.396 90.00 105.57 90.00 P 1 21 1 8
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 0.008378 0.000000 0.002334 0.00000
SCALE2 0.000000 0.008532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006353 0.00000
TER 6564 HIS A 865
TER 13105 LEU B 863
TER 19666 LEU C 863
TER 26252 LEU D 863
MASTER 592 0 4 76 184 0 15 626627 4 148 268
END |