HEADER HYDROLASE 10-OCT-17 6EOQ
TITLE DPP9 - APO
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 5 17-JAN-24 6EOQ 1 REMARK
REVDAT 4 16-OCT-19 6EOQ 1 REMARK
REVDAT 3 28-FEB-18 6EOQ 1 JRNL
REVDAT 2 14-FEB-18 6EOQ 1 JRNL
REVDAT 1 07-FEB-18 6EOQ 0
JRNL AUTH B.ROSS,S.KRAPP,M.AUGUSTIN,R.KIERFERSAUER,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. V. 115 E1437 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29382749
JRNL DOI 10.1073/PNAS.1717565115
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 84415
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) : 0.276
REMARK 3 R VALUE (WORKING SET) : 0.273
REMARK 3 FREE R VALUE : 0.334
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4443
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6196
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.3890
REMARK 3 BIN FREE R VALUE SET COUNT : 326
REMARK 3 BIN FREE R VALUE : 0.4290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24880
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.61000
REMARK 3 B22 (A**2) : 6.68000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.81000
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): 0.555
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.549
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.069
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.913
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.870
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25618 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 23735 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34746 ; 1.365 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): 54683 ; 1.999 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3016 ; 6.659 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1248 ;33.472 ;23.598
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4166 ;15.597 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 140 ;13.883 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3656 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 28682 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 6240 ; 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): 12208 ; 2.569 ; 5.380
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 12207 ; 2.569 ; 5.380
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15176 ; 4.296 ; 8.050
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 15177 ; 4.296 ; 8.051
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 13410 ; 2.294 ; 5.583
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 13411 ; 2.294 ; 5.584
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 19571 ; 3.962 ; 8.276
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 26977 ; 6.700 ;59.346
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 26978 ; 6.702 ;59.350
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 6EOQ 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_1200006948.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-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 : 88848
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 49.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.57
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.55000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1ORV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10%PEG 8000, 25% GLYCEROL, 0.16M
REMARK 280 CALCIUM ACETATE, 0.08M CAODILATE PH6.25,, 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 59.01000
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: 4070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 61580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 4150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 61800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 LYS A 43
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 ALA A 52
REMARK 465 ASP A 63
REMARK 465 GLU A 64
REMARK 465 SER A 65
REMARK 465 TYR A 79
REMARK 465 GLY A 80
REMARK 465 SER A 81
REMARK 465 ARG A 82
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 ASP A 110
REMARK 465 HIS A 111
REMARK 465 PHE A 112
REMARK 465 GLN A 113
REMARK 465 ALA A 114
REMARK 465 THR A 115
REMARK 465 PRO A 116
REMARK 465 HIS A 117
REMARK 465 HIS A 118
REMARK 465 GLY A 119
REMARK 465 VAL A 120
REMARK 465 TYR A 121
REMARK 465 SER A 122
REMARK 465 ARG A 123
REMARK 465 GLU A 124
REMARK 465 GLU A 125
REMARK 465 GLU A 126
REMARK 465 LEU A 127
REMARK 465 LEU A 128
REMARK 465 ARG A 129
REMARK 465 GLU A 130
REMARK 465 ARG A 131
REMARK 465 LYS A 132
REMARK 465 ARG A 133
REMARK 465 LEU A 134
REMARK 465 GLY A 135
REMARK 465 VAL A 136
REMARK 465 PHE A 137
REMARK 465 GLY A 138
REMARK 465 GLY A 165
REMARK 465 GLY A 166
REMARK 465 LYS A 167
REMARK 465 ASN A 168
REMARK 465 GLY A 169
REMARK 465 GLY A 228
REMARK 465 LEU A 229
REMARK 465 SER A 230
REMARK 465 ASN A 231
REMARK 465 VAL A 232
REMARK 465 LEU A 233
REMARK 465 GLU A 268
REMARK 465 GLY A 269
REMARK 465 GLN A 432
REMARK 465 SER A 433
REMARK 465 GLU A 434
REMARK 465 GLY A 435
REMARK 465 GLU A 436
REMARK 465 GLY A 475
REMARK 465 GLU A 476
REMARK 465 ASP A 477
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 865
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 LYS B 43
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 LYS B 51
REMARK 465 ASP B 63
REMARK 465 GLU B 64
REMARK 465 SER B 65
REMARK 465 PRO B 78
REMARK 465 TYR B 79
REMARK 465 GLY B 80
REMARK 465 SER B 81
REMARK 465 ARG B 82
REMARK 465 GLU B 83
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 ASP B 110
REMARK 465 HIS B 111
REMARK 465 PHE B 112
REMARK 465 GLN B 113
REMARK 465 ALA B 114
REMARK 465 THR B 115
REMARK 465 PRO B 116
REMARK 465 HIS B 117
REMARK 465 HIS B 118
REMARK 465 GLY B 119
REMARK 465 VAL B 120
REMARK 465 TYR B 121
REMARK 465 SER B 122
REMARK 465 ARG B 123
REMARK 465 GLU B 124
REMARK 465 GLU B 125
REMARK 465 GLU B 126
REMARK 465 LEU B 127
REMARK 465 LEU B 128
REMARK 465 ARG B 129
REMARK 465 GLU B 130
REMARK 465 ARG B 131
REMARK 465 LYS B 132
REMARK 465 ARG B 133
REMARK 465 LEU B 134
REMARK 465 GLY B 135
REMARK 465 VAL B 136
REMARK 465 PHE B 137
REMARK 465 GLY B 138
REMARK 465 GLY B 165
REMARK 465 GLY B 166
REMARK 465 LYS B 167
REMARK 465 ASN B 168
REMARK 465 GLY B 169
REMARK 465 GLY B 228
REMARK 465 LEU B 229
REMARK 465 SER B 230
REMARK 465 ASN B 231
REMARK 465 VAL B 232
REMARK 465 SER B 267
REMARK 465 GLU B 268
REMARK 465 GLY B 269
REMARK 465 GLN B 432
REMARK 465 SER B 433
REMARK 465 GLU B 434
REMARK 465 GLY B 435
REMARK 465 GLU B 436
REMARK 465 GLY B 475
REMARK 465 GLU B 476
REMARK 465 ASP B 477
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 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 LYS C 43
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 ASP C 63
REMARK 465 GLU C 64
REMARK 465 SER C 65
REMARK 465 TYR C 79
REMARK 465 GLY C 80
REMARK 465 SER C 81
REMARK 465 ARG C 82
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 ASP C 110
REMARK 465 HIS C 111
REMARK 465 PHE C 112
REMARK 465 GLN C 113
REMARK 465 ALA C 114
REMARK 465 THR C 115
REMARK 465 PRO C 116
REMARK 465 HIS C 117
REMARK 465 HIS C 118
REMARK 465 GLY C 119
REMARK 465 VAL C 120
REMARK 465 TYR C 121
REMARK 465 SER C 122
REMARK 465 ARG C 123
REMARK 465 GLU C 124
REMARK 465 GLU C 125
REMARK 465 GLU C 126
REMARK 465 LEU C 127
REMARK 465 LEU C 128
REMARK 465 ARG C 129
REMARK 465 GLU C 130
REMARK 465 ARG C 131
REMARK 465 LYS C 132
REMARK 465 ARG C 133
REMARK 465 LEU C 134
REMARK 465 GLY C 135
REMARK 465 VAL C 136
REMARK 465 PHE C 137
REMARK 465 GLY C 138
REMARK 465 GLY C 165
REMARK 465 GLY C 166
REMARK 465 LYS C 167
REMARK 465 ASN C 168
REMARK 465 GLY C 169
REMARK 465 PHE C 170
REMARK 465 MET C 171
REMARK 465 GLY C 228
REMARK 465 LEU C 229
REMARK 465 SER C 230
REMARK 465 ASN C 231
REMARK 465 VAL C 232
REMARK 465 GLU C 265
REMARK 465 GLY C 266
REMARK 465 SER C 267
REMARK 465 GLU C 268
REMARK 465 GLN C 432
REMARK 465 SER C 433
REMARK 465 GLU C 434
REMARK 465 GLY C 435
REMARK 465 GLY C 475
REMARK 465 GLU C 476
REMARK 465 ASP C 477
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 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 LYS D 43
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 ASP D 63
REMARK 465 GLU D 64
REMARK 465 SER D 65
REMARK 465 TYR D 79
REMARK 465 GLY D 80
REMARK 465 SER D 81
REMARK 465 ARG D 82
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 ASP D 110
REMARK 465 HIS D 111
REMARK 465 PHE D 112
REMARK 465 GLN D 113
REMARK 465 ALA D 114
REMARK 465 THR D 115
REMARK 465 PRO D 116
REMARK 465 HIS D 117
REMARK 465 HIS D 118
REMARK 465 GLY D 119
REMARK 465 VAL D 120
REMARK 465 TYR D 121
REMARK 465 SER D 122
REMARK 465 ARG D 123
REMARK 465 GLU D 124
REMARK 465 GLU D 125
REMARK 465 GLU D 126
REMARK 465 LEU D 127
REMARK 465 LEU D 128
REMARK 465 ARG D 129
REMARK 465 GLU D 130
REMARK 465 ARG D 131
REMARK 465 LYS D 132
REMARK 465 ARG D 133
REMARK 465 LEU D 134
REMARK 465 GLY D 135
REMARK 465 VAL D 136
REMARK 465 PHE D 137
REMARK 465 GLY D 138
REMARK 465 GLY D 165
REMARK 465 GLY D 166
REMARK 465 LYS D 167
REMARK 465 ASN D 168
REMARK 465 GLY D 169
REMARK 465 PHE D 170
REMARK 465 GLY D 228
REMARK 465 LEU D 229
REMARK 465 SER D 230
REMARK 465 ASN D 231
REMARK 465 VAL D 232
REMARK 465 GLY D 266
REMARK 465 SER D 267
REMARK 465 GLU D 268
REMARK 465 GLY D 269
REMARK 465 GLN D 432
REMARK 465 SER D 433
REMARK 465 GLU D 434
REMARK 465 GLY D 435
REMARK 465 GLU D 436
REMARK 465 ASP D 437
REMARK 465 GLU D 438
REMARK 465 GLY D 475
REMARK 465 GLU D 476
REMARK 465 ASP D 477
REMARK 465 ALA D 599
REMARK 465 SER D 600
REMARK 465 CYS D 601
REMARK 465 PRO D 602
REMARK 465 PRO D 603
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 ALA A 21 41.21 -142.85
REMARK 500 SER A 156 -125.04 56.92
REMARK 500 SER A 207 40.87 39.59
REMARK 500 ARG A 220 120.74 -173.73
REMARK 500 PHE A 224 46.24 -141.34
REMARK 500 GLU A 282 43.89 -91.52
REMARK 500 VAL A 331 -70.21 -66.64
REMARK 500 GLN A 334 121.18 -171.80
REMARK 500 GLN A 373 63.56 63.21
REMARK 500 GLN A 374 21.33 -144.16
REMARK 500 TRP A 375 42.59 -156.39
REMARK 500 PRO A 388 174.16 -59.17
REMARK 500 VAL A 419 -82.65 -103.20
REMARK 500 CYS A 452 107.45 -59.36
REMARK 500 GLU A 493 41.02 -96.65
REMARK 500 ALA A 498 -40.88 -131.14
REMARK 500 ASP A 618 45.18 76.97
REMARK 500 TYR A 644 -67.86 -129.54
REMARK 500 GLN A 696 52.25 -152.62
REMARK 500 SER A 730 -113.17 51.34
REMARK 500 ASP A 772 -171.87 73.25
REMARK 500 ASN A 777 68.27 -105.61
REMARK 500 ASN A 810 -71.77 -92.88
REMARK 500 PHE A 814 -38.39 -37.69
REMARK 500 ARG A 839 -77.87 -85.49
REMARK 500 SER B 156 -118.27 48.59
REMARK 500 VAL B 172 -51.76 -130.80
REMARK 500 THR B 254 135.82 -172.67
REMARK 500 GLU B 265 -169.61 -126.22
REMARK 500 LYS B 271 131.70 -174.38
REMARK 500 GLU B 391 78.38 -101.88
REMARK 500 ASN B 392 94.50 -169.15
REMARK 500 VAL B 419 -91.66 -110.83
REMARK 500 PHE B 427 96.76 -165.09
REMARK 500 LEU B 461 61.27 -103.56
REMARK 500 GLU B 493 50.00 -96.89
REMARK 500 ALA B 535 89.40 -67.06
REMARK 500 HIS B 586 40.23 -105.66
REMARK 500 TRP B 592 -63.24 -98.16
REMARK 500 TYR B 644 -72.14 -125.95
REMARK 500 ILE B 659 -70.81 -72.91
REMARK 500 PHE B 718 29.66 -147.87
REMARK 500 ARG B 723 75.12 -110.73
REMARK 500 SER B 730 -113.27 57.98
REMARK 500 ALA B 754 49.70 38.63
REMARK 500 ASP B 772 -165.01 71.60
REMARK 500 ASN B 777 71.76 -105.37
REMARK 500 LEU B 800 118.31 -160.42
REMARK 500 LEU B 807 26.70 -75.28
REMARK 500 ASN B 810 -70.07 -98.51
REMARK 500
REMARK 500 THIS ENTRY HAS 101 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6EOQ A 1 863 UNP Q86TI2 DPP9_HUMAN 1 863
DBREF 6EOQ B 1 863 UNP Q86TI2 DPP9_HUMAN 1 863
DBREF 6EOQ C 1 863 UNP Q86TI2 DPP9_HUMAN 1 863
DBREF 6EOQ D 1 863 UNP Q86TI2 DPP9_HUMAN 1 863
SEQADV 6EOQ HIS A 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS A 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS A 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS A 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS A 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS A 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS B 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS B 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS B 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS B 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS B 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS B 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS C 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS C 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS C 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS C 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS C 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS C 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS D 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS D 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS D 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS D 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ HIS D 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6EOQ 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
FORMUL 5 HOH *82(H2 O)
HELIX 1 AA1 SER A 30 ARG A 42 1 13
HELIX 2 AA2 THR A 243 PHE A 250 1 8
HELIX 3 AA3 ALA A 294 ARG A 298 5 5
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 LEU A 670 1 10
HELIX 9 AA9 GLY A 686 GLY A 691 1 6
HELIX 10 AB1 ALA A 692 LYS A 694 5 3
HELIX 11 AB2 VAL A 700 TYR A 716 1 17
HELIX 12 AB3 SER A 730 LYS A 743 1 14
HELIX 13 AB4 VAL A 758 TYR A 762 5 5
HELIX 14 AB5 ASP A 763 ASP A 772 1 10
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 SER B 41 1 12
HELIX 20 AC2 THR B 243 ASP B 251 1 9
HELIX 21 AC3 ALA B 294 ARG B 298 5 5
HELIX 22 AC4 PRO B 341 PHE B 346 1 6
HELIX 23 AC5 PRO B 382 ALA B 384 5 3
HELIX 24 AC6 ASN B 392 VAL B 403 1 12
HELIX 25 AC7 TYR B 661 LEU B 670 1 10
HELIX 26 AC8 GLY B 686 GLY B 691 1 6
HELIX 27 AC9 ALA B 692 LYS B 694 5 3
HELIX 28 AD1 VAL B 700 TYR B 716 1 17
HELIX 29 AD2 SER B 730 LYS B 743 1 14
HELIX 30 AD3 VAL B 758 TYR B 762 5 5
HELIX 31 AD4 ASP B 763 MET B 771 1 9
HELIX 32 AD5 ASN B 777 GLY B 784 1 8
HELIX 33 AD6 SER B 785 LEU B 793 5 9
HELIX 34 AD7 PHE B 813 ALA B 826 1 14
HELIX 35 AD8 CYS B 844 LEU B 863 1 20
HELIX 36 AD9 SER C 30 ARG C 42 1 13
HELIX 37 AE1 THR C 243 PHE C 250 1 8
HELIX 38 AE2 ALA C 294 ARG C 298 5 5
HELIX 39 AE3 PRO C 341 PHE C 346 1 6
HELIX 40 AE4 PRO C 382 ALA C 384 5 3
HELIX 41 AE5 ASN C 392 ALA C 402 1 11
HELIX 42 AE6 TYR C 661 LEU C 670 1 10
HELIX 43 AE7 GLY C 686 GLY C 691 1 6
HELIX 44 AE8 ALA C 692 LYS C 694 5 3
HELIX 45 AE9 VAL C 700 TYR C 716 1 17
HELIX 46 AF1 SER C 730 LYS C 743 1 14
HELIX 47 AF2 VAL C 758 TYR C 762 5 5
HELIX 48 AF3 ASP C 763 ASP C 772 1 10
HELIX 49 AF4 ASN C 777 GLY C 784 1 8
HELIX 50 AF5 SER C 785 LEU C 793 5 9
HELIX 51 AF6 PHE C 813 GLY C 827 1 15
HELIX 52 AF7 CYS C 844 LEU C 863 1 20
HELIX 53 AF8 SER D 30 ARG D 42 1 13
HELIX 54 AF9 THR D 243 PHE D 250 1 8
HELIX 55 AG1 SER D 283 VAL D 285 5 3
HELIX 56 AG2 PRO D 341 PHE D 346 1 6
HELIX 57 AG3 PRO D 382 ALA D 384 5 3
HELIX 58 AG4 ASN D 392 ALA D 402 1 11
HELIX 59 AG5 GLU D 446 GLY D 450 1 5
HELIX 60 AG6 LEU D 662 GLY D 671 1 10
HELIX 61 AG7 GLY D 686 GLY D 691 1 6
HELIX 62 AG8 ALA D 692 LYS D 694 5 3
HELIX 63 AG9 GLN D 699 TYR D 716 1 18
HELIX 64 AH1 SER D 730 LYS D 743 1 14
HELIX 65 AH2 VAL D 758 TYR D 762 5 5
HELIX 66 AH3 ASP D 763 ASP D 772 1 10
HELIX 67 AH4 ASN D 777 GLY D 784 1 8
HELIX 68 AH5 SER D 785 LEU D 793 5 9
HELIX 69 AH6 PHE D 813 GLY D 827 1 15
HELIX 70 AH7 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 68 GLY A 76 -1 O LEU A 75 N HIS A 54
SHEET 3 AA1 4 SER A 85 PRO A 92 -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 TYR A 142 HIS A 145 0
SHEET 2 AA2 4 LEU A 150 ALA A 155 -1 O LEU A 152 N ASP A 143
SHEET 3 AA2 4 SER A 158 ARG A 163 -1 O SER A 158 N ALA A 155
SHEET 4 AA2 4 LEU A 178 ILE A 180 -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 ARG A 220 ARG A 221 -1 O ARG A 220 N VAL A 211
SHEET 1 AA4 4 LYS A 237 ALA A 239 0
SHEET 2 AA4 4 ILE A 275 ASP A 281 -1 O VAL A 280 N SER A 238
SHEET 3 AA4 4 LYS A 314 THR A 324 -1 O ALA A 320 N ILE A 275
SHEET 4 AA4 4 LYS A 271 THR A 272 -1 N LYS A 271 O THR A 324
SHEET 1 AA5 5 TYR A 256 TRP A 258 0
SHEET 2 AA5 5 ILE A 275 ASP A 281 -1 O LEU A 276 N TRP A 257
SHEET 3 AA5 5 LYS A 314 THR A 324 -1 O ALA A 320 N ILE A 275
SHEET 4 AA5 5 ILE A 330 LEU A 338 -1 O GLN A 334 N GLU A 321
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 GLN A 377 LEU A 381 -1 O LEU A 381 N ALA A 364
SHEET 4 AA7 4 TYR A 410 GLU A 414 -1 O TYR A 413 N LEU A 378
SHEET 1 AA8 4 PHE A 427 PRO A 429 0
SHEET 2 AA8 4 LEU A 439 ASN A 445 -1 O LEU A 442 N TYR A 428
SHEET 3 AA8 4 HIS A 453 ALA A 459 -1 O ALA A 459 N LEU A 439
SHEET 4 AA8 4 ILE A 483 ALA A 488 -1 O LYS A 484 N THR A 458
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 HIS A 526 N GLY A 517
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 ALA A 593 N VAL A 574
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 ILE A 677 -1 O VAL A 676 N MET A 624
SHEET 4 AB2 8 HIS A 637 VAL A 643 1 N VAL A 640 O ALA A 673
SHEET 5 AB2 8 ILE A 719 TRP A 729 1 O ALA A 725 N LEU A 641
SHEET 6 AB2 8 VAL A 749 GLY A 753 1 O GLY A 753 N GLY A 728
SHEET 7 AB2 8 LEU A 800 GLY A 805 1 O LEU A 803 N ALA A 752
SHEET 8 AB2 8 GLN A 831 TYR A 835 1 O GLN A 833 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 ARG B 71 N VAL B 59
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 ASP B 143 HIS B 145 0
SHEET 2 AB4 4 LEU B 150 ALA B 155 -1 O LEU B 152 N ASP B 143
SHEET 3 AB4 4 SER B 158 CYS B 162 -1 O SER B 158 N ALA B 155
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 ASN B 205 -1 O SER B 202 N LYS B 192
SHEET 3 AB5 4 ASP B 208 ASN B 213 -1 O ASP B 208 N ASN B 205
SHEET 4 AB5 4 GLU B 219 ARG B 221 -1 O ARG B 220 N VAL B 211
SHEET 1 AB6 4 LYS B 237 ALA B 239 0
SHEET 2 AB6 4 ILE B 275 ASP B 281 -1 O VAL B 280 N SER B 238
SHEET 3 AB6 4 LYS B 314 THR B 324 -1 O LYS B 314 N ASP B 281
SHEET 4 AB6 4 THR B 272 LEU B 273 -1 N LEU B 273 O PHE B 322
SHEET 1 AB7 5 TYR B 256 TRP B 258 0
SHEET 2 AB7 5 ILE B 275 ASP B 281 -1 O LEU B 276 N TRP B 257
SHEET 3 AB7 5 LYS B 314 THR B 324 -1 O LYS B 314 N ASP B 281
SHEET 4 AB7 5 ILE B 330 LEU B 338 -1 O LYS B 336 N LEU B 319
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 TYR B 351 TRP B 357 0
SHEET 2 AB9 4 ALA B 364 LEU B 369 -1 O MET B 367 N ARG B 354
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 TYR B 410 N LEU B 380
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 GLU B 485 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 VAL B 530 N VAL B 513
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 CYS B 571 N TYR B 563
SHEET 4 AC3 4 GLN B 588 MET B 596 -1 O ALA B 593 N VAL B 574
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 ILE B 677 -1 O VAL B 674 N TYR B 626
SHEET 4 AC4 8 HIS B 637 VAL B 643 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 LEU B 641
SHEET 6 AC4 8 VAL B 749 GLY B 753 1 O ILE B 751 N ILE B 726
SHEET 7 AC4 8 LEU B 801 GLY B 805 1 O LEU B 801 N ALA B 750
SHEET 8 AC4 8 LEU B 832 TYR B 835 1 O GLN B 833 N ILE B 802
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 PHE C 153 -1 O LEU C 152 N ASP C 143
SHEET 3 AC6 4 PHE C 160 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 ASN C 205 -1 O SER C 202 N LYS C 192
SHEET 3 AC7 4 ASP C 208 ASN C 213 -1 O TRP C 210 N PHE C 203
SHEET 4 AC7 4 ARG C 220 ARG C 221 -1 O ARG C 220 N VAL C 211
SHEET 1 AC8 3 SER C 238 ALA C 239 0
SHEET 2 AC8 3 ILE C 275 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 SER C 238 ALA C 239 0
SHEET 2 AC9 5 ILE C 275 ASP C 281 -1 O VAL C 280 N SER C 238
SHEET 3 AC9 5 LYS C 314 LEU C 319 -1 O LYS C 314 N ASP C 281
SHEET 4 AC9 5 LYS C 336 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 3 LYS C 271 LEU C 273 0
SHEET 2 AD1 3 PHE C 322 THR C 324 -1 O PHE C 322 N LEU C 273
SHEET 3 AD1 3 ILE C 330 THR C 333 -1 O SER C 332 N GLN C 323
SHEET 1 AD2 2 VAL C 287 PRO C 291 0
SHEET 2 AD2 2 THR C 300 ARG C 304 -1 O ASP C 301 N VAL C 290
SHEET 1 AD3 4 TYR C 351 TRP C 357 0
SHEET 2 AD3 4 ALA C 364 LEU C 369 -1 O TRP C 365 N GLY C 356
SHEET 3 AD3 4 TRP C 375 LEU C 381 -1 O LEU C 381 N ALA C 364
SHEET 4 AD3 4 TYR C 410 VAL C 416 -1 O TYR C 410 N LEU C 380
SHEET 1 AD4 4 PHE C 427 PRO C 429 0
SHEET 2 AD4 4 LEU C 439 ASN C 445 -1 O LEU C 442 N TYR C 428
SHEET 3 AD4 4 HIS C 453 ALA C 459 -1 O ALA C 459 N LEU C 439
SHEET 4 AD4 4 ILE C 483 ALA C 488 -1 O ILE C 487 N LYS C 456
SHEET 1 AD5 4 TRP C 505 ASN C 507 0
SHEET 2 AD5 4 LEU C 512 THR C 521 -1 O TYR C 514 N TRP C 505
SHEET 3 AD5 4 GLU C 524 SER C 531 -1 O VAL C 530 N VAL C 513
SHEET 4 AD5 4 VAL C 539 ARG C 540 -1 O VAL C 539 N VAL C 529
SHEET 1 AD6 4 CYS C 550 MET C 552 0
SHEET 2 AD6 4 MET C 558 TYR C 563 -1 O VAL C 560 N SER C 551
SHEET 3 AD6 4 CYS C 571 SER C 578 -1 O TYR C 575 N PHE C 559
SHEET 4 AD6 4 GLN C 588 MET C 596 -1 O ALA C 593 N VAL C 574
SHEET 1 AD7 8 GLU C 609 HIS C 614 0
SHEET 2 AD7 8 ARG C 620 TYR C 626 -1 O GLY C 623 N PHE C 611
SHEET 3 AD7 8 ALA C 673 ILE C 677 -1 O VAL C 674 N TYR C 626
SHEET 4 AD7 8 HIS C 637 VAL C 643 1 N VAL C 640 O ALA C 673
SHEET 5 AD7 8 ILE C 719 TRP C 729 1 O ALA C 725 N LEU C 641
SHEET 6 AD7 8 VAL C 749 GLY C 753 1 O GLY C 753 N GLY C 728
SHEET 7 AD7 8 LEU C 801 GLY C 805 1 O LEU C 801 N ALA C 750
SHEET 8 AD7 8 GLN C 831 TYR C 835 1 O GLN C 833 N ILE C 802
SHEET 1 AD8 4 HIS D 54 GLN D 60 0
SHEET 2 AD8 4 HIS D 68 GLY D 76 -1 O LEU D 75 N HIS D 54
SHEET 3 AD8 4 SER D 85 PRO D 92 -1 O LEU D 87 N TYR D 74
SHEET 4 AD8 4 LYS D 106 GLN D 107 -1 O LYS D 106 N TYR D 88
SHEET 1 AD9 4 TYR D 142 HIS D 145 0
SHEET 2 AD9 4 LEU D 150 ALA D 155 -1 O LEU D 152 N ASP D 143
SHEET 3 AD9 4 SER D 158 ARG D 163 -1 O PHE D 160 N PHE D 153
SHEET 4 AD9 4 LEU D 178 GLU D 179 -1 O LEU D 178 N HIS D 161
SHEET 1 AE1 4 MET D 189 ILE D 193 0
SHEET 2 AE1 4 PHE D 200 ASN D 205 -1 O ILE D 204 N MET D 189
SHEET 3 AE1 4 ASP D 208 ASN D 213 -1 O ALA D 212 N PHE D 201
SHEET 4 AE1 4 ARG D 220 ARG D 221 -1 O ARG D 220 N VAL D 211
SHEET 1 AE2 3 LYS D 237 ALA D 239 0
SHEET 2 AE2 3 ILE D 275 ASP D 281 -1 O VAL D 280 N SER D 238
SHEET 3 AE2 3 TYR D 256 TRP D 258 -1 N TRP D 257 O LEU D 276
SHEET 1 AE3 5 LYS D 237 ALA D 239 0
SHEET 2 AE3 5 ILE D 275 ASP D 281 -1 O VAL D 280 N SER D 238
SHEET 3 AE3 5 LYS D 314 GLU D 321 -1 O ALA D 320 N ILE D 275
SHEET 4 AE3 5 GLN D 334 LEU D 338 -1 O GLN D 334 N GLU D 321
SHEET 5 AE3 5 PHE D 386 PRO D 388 -1 O ILE D 387 N GLU D 337
SHEET 1 AE4 2 LYS D 271 THR D 272 0
SHEET 2 AE4 2 GLN D 323 THR D 324 -1 O THR D 324 N LYS D 271
SHEET 1 AE5 2 VAL D 287 PRO D 291 0
SHEET 2 AE5 2 THR D 300 ARG D 304 -1 O ASP D 301 N VAL D 290
SHEET 1 AE6 4 TYR D 351 TRP D 357 0
SHEET 2 AE6 4 ALA D 364 LEU D 369 -1 O LEU D 369 N TYR D 351
SHEET 3 AE6 4 TRP D 375 LEU D 381 -1 O GLN D 377 N PHE D 368
SHEET 4 AE6 4 TYR D 410 VAL D 416 -1 O GLU D 415 N LEU D 376
SHEET 1 AE7 4 PHE D 427 PRO D 429 0
SHEET 2 AE7 4 CYS D 440 ASN D 445 -1 O LEU D 442 N TYR D 428
SHEET 3 AE7 4 HIS D 453 ALA D 459 -1 O VAL D 457 N PHE D 441
SHEET 4 AE7 4 ILE D 483 ALA D 488 -1 O GLU D 485 N THR D 458
SHEET 1 AE8 4 TRP D 505 ASN D 507 0
SHEET 2 AE8 4 LEU D 512 GLY D 517 -1 O TYR D 514 N TRP D 505
SHEET 3 AE8 4 HIS D 526 SER D 531 -1 O TYR D 528 N PHE D 515
SHEET 4 AE8 4 VAL D 539 ARG D 540 -1 O VAL D 539 N VAL D 529
SHEET 1 AE9 4 SER D 547 MET D 552 0
SHEET 2 AE9 4 MET D 558 SER D 564 -1 O HIS D 562 N SER D 549
SHEET 3 AE9 4 CYS D 571 SER D 578 -1 O CYS D 571 N TYR D 563
SHEET 4 AE9 4 GLN D 588 MET D 596 -1 O MET D 595 N VAL D 572
SHEET 1 AF1 8 GLU D 609 HIS D 614 0
SHEET 2 AF1 8 ARG D 620 TYR D 626 -1 O GLY D 623 N PHE D 611
SHEET 3 AF1 8 ALA D 673 ILE D 677 -1 O VAL D 674 N TYR D 626
SHEET 4 AF1 8 HIS D 637 PHE D 642 1 N VAL D 640 O ALA D 673
SHEET 5 AF1 8 ILE D 719 TRP D 729 1 O ALA D 725 N LEU D 641
SHEET 6 AF1 8 PHE D 747 GLY D 753 1 O LYS D 748 N VAL D 724
SHEET 7 AF1 8 LEU D 801 GLY D 805 1 O LEU D 801 N ALA D 750
SHEET 8 AF1 8 GLN D 831 TYR D 835 1 O TYR D 835 N HIS D 804
CRYST1 120.370 118.020 164.460 90.00 105.49 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 0.008308 0.000000 0.002302 0.00000
SCALE2 0.000000 0.008473 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006310 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
