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HEADER HYDROLASE 18-AUG-20 7A3F
TITLE CRYSTAL STRUCTURE OF APO DPP9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 9;
COMPND 3 CHAIN: B, A, 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, PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.H.ROSS,R.HUBER
REVDAT 1 30-JUN-21 7A3F 0
JRNL AUTH L.FEHR,L.A.R.CARVALHO,B.H.ROSS,K.LUM,A.C.VIEIRA,
JRNL AUTH 2 R.KIEFERSAUER,R.GEISS-FRIEDLANDER,M.KAISER,T.RODRIGUES,
JRNL AUTH 3 S.D.LUCAS,B.F.CRAVATT,R.HUBER,R.MOREIRA
JRNL TITL DISCOVERY AND DEVELOPMENT OF 4-OXO-BETA-LACTAMS AS NOVEL
JRNL TITL 2 INHIBITORS OF DIPEPTIDYL PEPTIDASES 8 AND 9
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 88289
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4647
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) : 6523
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.3950
REMARK 3 BIN FREE R VALUE SET COUNT : 343
REMARK 3 BIN FREE R VALUE : 0.4350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 25524
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 129
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.12000
REMARK 3 B22 (A**2) : -0.99000
REMARK 3 B33 (A**2) : 2.13000
REMARK 3 B12 (A**2) : -5.08000
REMARK 3 B13 (A**2) : 5.61000
REMARK 3 B23 (A**2) : -5.08000
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): 0.464
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.448
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.629
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
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): 26315 ; 0.003 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 23620 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 35712 ; 1.272 ; 1.643
REMARK 3 BOND ANGLES OTHERS (DEGREES): 54952 ; 1.061 ; 1.569
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3121 ; 7.403 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1421 ;32.805 ;22.294
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4266 ;17.669 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 143 ;16.715 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3228 ; 0.045 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 29226 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5759 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7A3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1292108108.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-19
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 : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92941
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 46.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 2.235
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.2400
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) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.49100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.060
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: 6EOR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.08 M NA-CACODILATE PH 5.25, 0.16 M
REMARK 280 CA-ACETATE, 30 % GLYCEROL, 10 % PEG 8K, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
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: 5120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 B -28
REMARK 465 ARG B -27
REMARK 465 LYS B -26
REMARK 465 VAL B -25
REMARK 465 LYS B -24
REMARK 465 LYS B -23
REMARK 465 LEU B -22
REMARK 465 ARG B -21
REMARK 465 LEU B -20
REMARK 465 ASP B -19
REMARK 465 LYS B -18
REMARK 465 GLU B -17
REMARK 465 ASN B -16
REMARK 465 THR B -15
REMARK 465 GLY B -14
REMARK 465 SER B -13
REMARK 465 TRP B -12
REMARK 465 ARG B -11
REMARK 465 SER B -10
REMARK 465 PHE B -9
REMARK 465 SER B -8
REMARK 465 LEU B -7
REMARK 465 ASN B -6
REMARK 465 SER B -5
REMARK 465 GLU B -4
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 GLU B -1
REMARK 465 ARG B 0
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 LYS B 51
REMARK 465 GLU B 64
REMARK 465 SER B 65
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 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 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 GLU B 434
REMARK 465 GLY B 435
REMARK 465 GLU B 436
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 A -28
REMARK 465 ARG A -27
REMARK 465 LYS A -26
REMARK 465 VAL A -25
REMARK 465 LYS A -24
REMARK 465 LYS A -23
REMARK 465 LEU A -22
REMARK 465 ARG A -21
REMARK 465 LEU A -20
REMARK 465 ASP A -19
REMARK 465 LYS A -18
REMARK 465 GLU A -17
REMARK 465 ASN A -16
REMARK 465 THR A -15
REMARK 465 GLY A -14
REMARK 465 SER A -13
REMARK 465 TRP A -12
REMARK 465 ARG A -11
REMARK 465 SER A -10
REMARK 465 PHE A -9
REMARK 465 SER A -8
REMARK 465 LEU A -7
REMARK 465 ASN A -6
REMARK 465 SER A -5
REMARK 465 GLU A -4
REMARK 465 GLY A -3
REMARK 465 ALA A -2
REMARK 465 GLU A -1
REMARK 465 ARG A 0
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 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 TYR A 79
REMARK 465 GLY A 80
REMARK 465 SER A 81
REMARK 465 LEU A 109
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 228
REMARK 465 LEU A 229
REMARK 465 SER A 230
REMARK 465 ASN A 231
REMARK 465 GLU A 434
REMARK 465 GLY A 435
REMARK 465 GLU A 436
REMARK 465 HIS A 866
REMARK 465 HIS A 867
REMARK 465 HIS A 868
REMARK 465 HIS A 869
REMARK 465 MET C -28
REMARK 465 ARG C -27
REMARK 465 LYS C -26
REMARK 465 VAL C -25
REMARK 465 LYS C -24
REMARK 465 LYS C -23
REMARK 465 LEU C -22
REMARK 465 ARG C -21
REMARK 465 LEU C -20
REMARK 465 ASP C -19
REMARK 465 LYS C -18
REMARK 465 GLU C -17
REMARK 465 ASN C -16
REMARK 465 THR C -15
REMARK 465 GLY C -14
REMARK 465 SER C -13
REMARK 465 TRP C -12
REMARK 465 ARG C -11
REMARK 465 SER C -10
REMARK 465 PHE C -9
REMARK 465 SER C -8
REMARK 465 LEU C -7
REMARK 465 ASN C -6
REMARK 465 SER C -5
REMARK 465 GLU C -4
REMARK 465 GLY C -3
REMARK 465 ALA C -2
REMARK 465 GLU C -1
REMARK 465 ARG C 0
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 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 ARG C 82
REMARK 465 GLU C 83
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 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 228
REMARK 465 LEU C 229
REMARK 465 SER C 230
REMARK 465 ASN C 231
REMARK 465 GLU C 434
REMARK 465 GLY C 435
REMARK 465 GLU C 436
REMARK 465 HIS C 866
REMARK 465 HIS C 867
REMARK 465 HIS C 868
REMARK 465 HIS C 869
REMARK 465 MET D -28
REMARK 465 ARG D -27
REMARK 465 LYS D -26
REMARK 465 VAL D -25
REMARK 465 LYS D -24
REMARK 465 LYS D -23
REMARK 465 LEU D -22
REMARK 465 ARG D -21
REMARK 465 LEU D -20
REMARK 465 ASP D -19
REMARK 465 LYS D -18
REMARK 465 GLU D -17
REMARK 465 ASN D -16
REMARK 465 THR D -15
REMARK 465 GLY D -14
REMARK 465 SER D -13
REMARK 465 TRP D -12
REMARK 465 ARG D -11
REMARK 465 SER D -10
REMARK 465 PHE D -9
REMARK 465 SER D -8
REMARK 465 LEU D -7
REMARK 465 ASN D -6
REMARK 465 SER D -5
REMARK 465 GLU D -4
REMARK 465 GLY D -3
REMARK 465 ALA D -2
REMARK 465 GLU D -1
REMARK 465 ARG D 0
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 GLY D 80
REMARK 465 SER D 81
REMARK 465 ARG D 82
REMARK 465 GLU D 83
REMARK 465 GLU D 98
REMARK 465 ALA D 99
REMARK 465 LEU D 100
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 165
REMARK 465 GLY D 166
REMARK 465 LYS D 167
REMARK 465 ASN D 168
REMARK 465 LEU D 229
REMARK 465 SER D 230
REMARK 465 ASN D 231
REMARK 465 GLU D 265
REMARK 465 GLY D 266
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 GLU D 436
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR C 17 OG1 CG2
REMARK 470 ASP C 18 CG OD1 OD2
REMARK 470 ASP C 19 CG OD1 OD2
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 B 21 37.95 -83.06
REMARK 500 ASP B 55 74.60 60.47
REMARK 500 SER B 69 -70.10 -105.62
REMARK 500 SER B 156 -139.76 59.71
REMARK 500 CYS B 162 150.33 179.57
REMARK 500 PHE B 201 138.91 -173.53
REMARK 500 ASN B 205 119.80 -160.76
REMARK 500 SER B 207 53.90 31.33
REMARK 500 GLN B 227 -152.70 -101.24
REMARK 500 LEU B 233 -19.88 72.00
REMARK 500 ASP B 235 70.37 -117.21
REMARK 500 SER B 238 146.87 -178.94
REMARK 500 THR B 243 -178.94 -66.88
REMARK 500 GLU B 249 -6.50 -140.18
REMARK 500 THR B 308 118.33 -36.58
REMARK 500 LYS B 348 -8.43 78.92
REMARK 500 GLN B 373 30.19 70.82
REMARK 500 ASN B 406 -71.60 -54.73
REMARK 500 VAL B 419 -93.69 -102.72
REMARK 500 GLN B 432 -165.34 -101.71
REMARK 500 GLU B 476 -96.69 58.57
REMARK 500 GLU B 493 58.51 -62.90
REMARK 500 ALA B 498 7.54 -154.10
REMARK 500 ALA B 535 76.44 -62.45
REMARK 500 PHE B 556 40.09 39.23
REMARK 500 PRO B 603 -21.09 -36.16
REMARK 500 ALA B 630 72.01 45.35
REMARK 500 PRO B 633 139.03 -39.34
REMARK 500 TYR B 644 -74.79 -112.86
REMARK 500 GLN B 684 15.63 81.11
REMARK 500 LYS B 694 115.44 -39.68
REMARK 500 SER B 730 -113.06 67.43
REMARK 500 ASP B 772 -152.98 62.32
REMARK 500 ASN B 777 52.67 -103.90
REMARK 500 ASN B 810 -73.44 -76.39
REMARK 500 ARG B 839 -132.31 -91.57
REMARK 500 ALA A 21 28.21 -79.80
REMARK 500 GLN A 27 105.63 -43.25
REMARK 500 ASP A 55 54.07 70.65
REMARK 500 GLU A 64 34.73 -90.25
REMARK 500 LYS A 97 -123.49 52.20
REMARK 500 ALA A 99 127.94 -177.19
REMARK 500 SER A 156 -120.38 54.20
REMARK 500 SER A 158 -163.17 -126.92
REMARK 500 VAL A 172 -70.05 -82.00
REMARK 500 SER A 185 -72.02 -85.14
REMARK 500 LEU A 233 -13.12 80.73
REMARK 500 ASP A 235 53.11 -142.04
REMARK 500 SER A 238 145.72 -173.00
REMARK 500 LEU A 270 153.18 78.83
REMARK 500
REMARK 500 THIS ENTRY HAS 154 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6EOR RELATED DB: PDB
REMARK 900 A DIFFERENT SPACE GROUP
DBREF 7A3F B -28 863 UNP Q86TI2 DPP9_HUMAN 1 892
DBREF 7A3F A -28 863 UNP Q86TI2 DPP9_HUMAN 1 892
DBREF 7A3F C -28 863 UNP Q86TI2 DPP9_HUMAN 1 892
DBREF 7A3F D -28 863 UNP Q86TI2 DPP9_HUMAN 1 892
SEQADV 7A3F HIS B 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS B 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS B 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS B 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS B 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS B 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS A 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS A 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS A 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS A 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS A 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS A 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS C 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS C 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS C 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS C 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS C 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS C 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS D 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS D 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS D 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS D 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS D 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 7A3F HIS D 869 UNP Q86TI2 EXPRESSION TAG
SEQRES 1 B 898 MET ARG LYS VAL LYS LYS LEU ARG LEU ASP LYS GLU ASN
SEQRES 2 B 898 THR GLY SER TRP ARG SER PHE SER LEU ASN SER GLU GLY
SEQRES 3 B 898 ALA GLU ARG MET ALA THR THR GLY THR PRO THR ALA ASP
SEQRES 4 B 898 ARG GLY ASP ALA ALA ALA THR ASP ASP PRO ALA ALA ARG
SEQRES 5 B 898 PHE GLN VAL GLN LYS HIS SER TRP ASP GLY LEU ARG SER
SEQRES 6 B 898 ILE ILE HIS GLY SER ARG LYS TYR SER GLY LEU ILE VAL
SEQRES 7 B 898 ASN LYS ALA PRO HIS ASP PHE GLN PHE VAL GLN LYS THR
SEQRES 8 B 898 ASP GLU SER GLY PRO HIS SER HIS ARG LEU TYR TYR LEU
SEQRES 9 B 898 GLY MET PRO TYR GLY SER ARG GLU ASN SER LEU LEU TYR
SEQRES 10 B 898 SER GLU ILE PRO LYS LYS VAL ARG LYS GLU ALA LEU LEU
SEQRES 11 B 898 LEU LEU SER TRP LYS GLN MET LEU ASP HIS PHE GLN ALA
SEQRES 12 B 898 THR PRO HIS HIS GLY VAL TYR SER ARG GLU GLU GLU LEU
SEQRES 13 B 898 LEU ARG GLU ARG LYS ARG LEU GLY VAL PHE GLY ILE THR
SEQRES 14 B 898 SER TYR ASP PHE HIS SER GLU SER GLY LEU PHE LEU PHE
SEQRES 15 B 898 GLN ALA SER ASN SER LEU PHE HIS CYS ARG ASP GLY GLY
SEQRES 16 B 898 LYS ASN GLY PHE MET VAL SER PRO MET LYS PRO LEU GLU
SEQRES 17 B 898 ILE LYS THR GLN CYS SER GLY PRO ARG MET ASP PRO LYS
SEQRES 18 B 898 ILE CYS PRO ALA ASP PRO ALA PHE PHE SER PHE ILE ASN
SEQRES 19 B 898 ASN SER ASP LEU TRP VAL ALA ASN ILE GLU THR GLY GLU
SEQRES 20 B 898 GLU ARG ARG LEU THR PHE CYS HIS GLN GLY LEU SER ASN
SEQRES 21 B 898 VAL LEU ASP ASP PRO LYS SER ALA GLY VAL ALA THR PHE
SEQRES 22 B 898 VAL ILE GLN GLU GLU PHE ASP ARG PHE THR GLY TYR TRP
SEQRES 23 B 898 TRP CYS PRO THR ALA SER TRP GLU GLY SER GLU GLY LEU
SEQRES 24 B 898 LYS THR LEU ARG ILE LEU TYR GLU GLU VAL ASP GLU SER
SEQRES 25 B 898 GLU VAL GLU VAL ILE HIS VAL PRO SER PRO ALA LEU GLU
SEQRES 26 B 898 GLU ARG LYS THR ASP SER TYR ARG TYR PRO ARG THR GLY
SEQRES 27 B 898 SER LYS ASN PRO LYS ILE ALA LEU LYS LEU ALA GLU PHE
SEQRES 28 B 898 GLN THR ASP SER GLN GLY LYS ILE VAL SER THR GLN GLU
SEQRES 29 B 898 LYS GLU LEU VAL GLN PRO PHE SER SER LEU PHE PRO LYS
SEQRES 30 B 898 VAL GLU TYR ILE ALA ARG ALA GLY TRP THR ARG ASP GLY
SEQRES 31 B 898 LYS TYR ALA TRP ALA MET PHE LEU ASP ARG PRO GLN GLN
SEQRES 32 B 898 TRP LEU GLN LEU VAL LEU LEU PRO PRO ALA LEU PHE ILE
SEQRES 33 B 898 PRO SER THR GLU ASN GLU GLU GLN ARG LEU ALA SER ALA
SEQRES 34 B 898 ARG ALA VAL PRO ARG ASN VAL GLN PRO TYR VAL VAL TYR
SEQRES 35 B 898 GLU GLU VAL THR ASN VAL TRP ILE ASN VAL HIS ASP ILE
SEQRES 36 B 898 PHE TYR PRO PHE PRO GLN SER GLU GLY GLU ASP GLU LEU
SEQRES 37 B 898 CYS PHE LEU ARG ALA ASN GLU CYS LYS THR GLY PHE CYS
SEQRES 38 B 898 HIS LEU TYR LYS VAL THR ALA VAL LEU LYS SER GLN GLY
SEQRES 39 B 898 TYR ASP TRP SER GLU PRO PHE SER PRO GLY GLU ASP GLU
SEQRES 40 B 898 PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA LEU THR SER
SEQRES 41 B 898 GLY GLU TRP GLU VAL LEU ALA ARG HIS GLY SER LYS ILE
SEQRES 42 B 898 TRP VAL ASN GLU GLU THR LYS LEU VAL TYR PHE GLN GLY
SEQRES 43 B 898 THR LYS ASP THR PRO LEU GLU HIS HIS LEU TYR VAL VAL
SEQRES 44 B 898 SER TYR GLU ALA ALA GLY GLU ILE VAL ARG LEU THR THR
SEQRES 45 B 898 PRO GLY PHE SER HIS SER CYS SER MET SER GLN ASN PHE
SEQRES 46 B 898 ASP MET PHE VAL SER HIS TYR SER SER VAL SER THR PRO
SEQRES 47 B 898 PRO CYS VAL HIS VAL TYR LYS LEU SER GLY PRO ASP ASP
SEQRES 48 B 898 ASP PRO LEU HIS LYS GLN PRO ARG PHE TRP ALA SER MET
SEQRES 49 B 898 MET GLU ALA ALA SER CYS PRO PRO ASP TYR VAL PRO PRO
SEQRES 50 B 898 GLU ILE PHE HIS PHE HIS THR ARG SER ASP VAL ARG LEU
SEQRES 51 B 898 TYR GLY MET ILE TYR LYS PRO HIS ALA LEU GLN PRO GLY
SEQRES 52 B 898 LYS LYS HIS PRO THR VAL LEU PHE VAL TYR GLY GLY PRO
SEQRES 53 B 898 GLN VAL GLN LEU VAL ASN ASN SER PHE LYS GLY ILE LYS
SEQRES 54 B 898 TYR LEU ARG LEU ASN THR LEU ALA SER LEU GLY TYR ALA
SEQRES 55 B 898 VAL VAL VAL ILE ASP GLY ARG GLY SER CYS GLN ARG GLY
SEQRES 56 B 898 LEU ARG PHE GLU GLY ALA LEU LYS ASN GLN MET GLY GLN
SEQRES 57 B 898 VAL GLU ILE GLU ASP GLN VAL GLU GLY LEU GLN PHE VAL
SEQRES 58 B 898 ALA GLU LYS TYR GLY PHE ILE ASP LEU SER ARG VAL ALA
SEQRES 59 B 898 ILE HIS GLY TRP SER TYR GLY GLY PHE LEU SER LEU MET
SEQRES 60 B 898 GLY LEU ILE HIS LYS PRO GLN VAL PHE LYS VAL ALA ILE
SEQRES 61 B 898 ALA GLY ALA PRO VAL THR VAL TRP MET ALA TYR ASP THR
SEQRES 62 B 898 GLY TYR THR GLU ARG TYR MET ASP VAL PRO GLU ASN ASN
SEQRES 63 B 898 GLN HIS GLY TYR GLU ALA GLY SER VAL ALA LEU HIS VAL
SEQRES 64 B 898 GLU LYS LEU PRO ASN GLU PRO ASN ARG LEU LEU ILE LEU
SEQRES 65 B 898 HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE PHE HIS THR
SEQRES 66 B 898 ASN PHE LEU VAL SER GLN LEU ILE ARG ALA GLY LYS PRO
SEQRES 67 B 898 TYR GLN LEU GLN ILE TYR PRO ASN GLU ARG HIS SER ILE
SEQRES 68 B 898 ARG CYS PRO GLU SER GLY GLU HIS TYR GLU VAL THR LEU
SEQRES 69 B 898 LEU HIS PHE LEU GLN GLU TYR LEU HIS HIS HIS HIS HIS
SEQRES 70 B 898 HIS
SEQRES 1 A 898 MET ARG LYS VAL LYS LYS LEU ARG LEU ASP LYS GLU ASN
SEQRES 2 A 898 THR GLY SER TRP ARG SER PHE SER LEU ASN SER GLU GLY
SEQRES 3 A 898 ALA GLU ARG MET ALA THR THR GLY THR PRO THR ALA ASP
SEQRES 4 A 898 ARG GLY ASP ALA ALA ALA THR ASP ASP PRO ALA ALA ARG
SEQRES 5 A 898 PHE GLN VAL GLN LYS HIS SER TRP ASP GLY LEU ARG SER
SEQRES 6 A 898 ILE ILE HIS GLY SER ARG LYS TYR SER GLY LEU ILE VAL
SEQRES 7 A 898 ASN LYS ALA PRO HIS ASP PHE GLN PHE VAL GLN LYS THR
SEQRES 8 A 898 ASP GLU SER GLY PRO HIS SER HIS ARG LEU TYR TYR LEU
SEQRES 9 A 898 GLY MET PRO TYR GLY SER ARG GLU ASN SER LEU LEU TYR
SEQRES 10 A 898 SER GLU ILE PRO LYS LYS VAL ARG LYS GLU ALA LEU LEU
SEQRES 11 A 898 LEU LEU SER TRP LYS GLN MET LEU ASP HIS PHE GLN ALA
SEQRES 12 A 898 THR PRO HIS HIS GLY VAL TYR SER ARG GLU GLU GLU LEU
SEQRES 13 A 898 LEU ARG GLU ARG LYS ARG LEU GLY VAL PHE GLY ILE THR
SEQRES 14 A 898 SER TYR ASP PHE HIS SER GLU SER GLY LEU PHE LEU PHE
SEQRES 15 A 898 GLN ALA SER ASN SER LEU PHE HIS CYS ARG ASP GLY GLY
SEQRES 16 A 898 LYS ASN GLY PHE MET VAL SER PRO MET LYS PRO LEU GLU
SEQRES 17 A 898 ILE LYS THR GLN CYS SER GLY PRO ARG MET ASP PRO LYS
SEQRES 18 A 898 ILE CYS PRO ALA ASP PRO ALA PHE PHE SER PHE ILE ASN
SEQRES 19 A 898 ASN SER ASP LEU TRP VAL ALA ASN ILE GLU THR GLY GLU
SEQRES 20 A 898 GLU ARG ARG LEU THR PHE CYS HIS GLN GLY LEU SER ASN
SEQRES 21 A 898 VAL LEU ASP ASP PRO LYS SER ALA GLY VAL ALA THR PHE
SEQRES 22 A 898 VAL ILE GLN GLU GLU PHE ASP ARG PHE THR GLY TYR TRP
SEQRES 23 A 898 TRP CYS PRO THR ALA SER TRP GLU GLY SER GLU GLY LEU
SEQRES 24 A 898 LYS THR LEU ARG ILE LEU TYR GLU GLU VAL ASP GLU SER
SEQRES 25 A 898 GLU VAL GLU VAL ILE HIS VAL PRO SER PRO ALA LEU GLU
SEQRES 26 A 898 GLU ARG LYS THR ASP SER TYR ARG TYR PRO ARG THR GLY
SEQRES 27 A 898 SER LYS ASN PRO LYS ILE ALA LEU LYS LEU ALA GLU PHE
SEQRES 28 A 898 GLN THR ASP SER GLN GLY LYS ILE VAL SER THR GLN GLU
SEQRES 29 A 898 LYS GLU LEU VAL GLN PRO PHE SER SER LEU PHE PRO LYS
SEQRES 30 A 898 VAL GLU TYR ILE ALA ARG ALA GLY TRP THR ARG ASP GLY
SEQRES 31 A 898 LYS TYR ALA TRP ALA MET PHE LEU ASP ARG PRO GLN GLN
SEQRES 32 A 898 TRP LEU GLN LEU VAL LEU LEU PRO PRO ALA LEU PHE ILE
SEQRES 33 A 898 PRO SER THR GLU ASN GLU GLU GLN ARG LEU ALA SER ALA
SEQRES 34 A 898 ARG ALA VAL PRO ARG ASN VAL GLN PRO TYR VAL VAL TYR
SEQRES 35 A 898 GLU GLU VAL THR ASN VAL TRP ILE ASN VAL HIS ASP ILE
SEQRES 36 A 898 PHE TYR PRO PHE PRO GLN SER GLU GLY GLU ASP GLU LEU
SEQRES 37 A 898 CYS PHE LEU ARG ALA ASN GLU CYS LYS THR GLY PHE CYS
SEQRES 38 A 898 HIS LEU TYR LYS VAL THR ALA VAL LEU LYS SER GLN GLY
SEQRES 39 A 898 TYR ASP TRP SER GLU PRO PHE SER PRO GLY GLU ASP GLU
SEQRES 40 A 898 PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA LEU THR SER
SEQRES 41 A 898 GLY GLU TRP GLU VAL LEU ALA ARG HIS GLY SER LYS ILE
SEQRES 42 A 898 TRP VAL ASN GLU GLU THR LYS LEU VAL TYR PHE GLN GLY
SEQRES 43 A 898 THR LYS ASP THR PRO LEU GLU HIS HIS LEU TYR VAL VAL
SEQRES 44 A 898 SER TYR GLU ALA ALA GLY GLU ILE VAL ARG LEU THR THR
SEQRES 45 A 898 PRO GLY PHE SER HIS SER CYS SER MET SER GLN ASN PHE
SEQRES 46 A 898 ASP MET PHE VAL SER HIS TYR SER SER VAL SER THR PRO
SEQRES 47 A 898 PRO CYS VAL HIS VAL TYR LYS LEU SER GLY PRO ASP ASP
SEQRES 48 A 898 ASP PRO LEU HIS LYS GLN PRO ARG PHE TRP ALA SER MET
SEQRES 49 A 898 MET GLU ALA ALA SER CYS PRO PRO ASP TYR VAL PRO PRO
SEQRES 50 A 898 GLU ILE PHE HIS PHE HIS THR ARG SER ASP VAL ARG LEU
SEQRES 51 A 898 TYR GLY MET ILE TYR LYS PRO HIS ALA LEU GLN PRO GLY
SEQRES 52 A 898 LYS LYS HIS PRO THR VAL LEU PHE VAL TYR GLY GLY PRO
SEQRES 53 A 898 GLN VAL GLN LEU VAL ASN ASN SER PHE LYS GLY ILE LYS
SEQRES 54 A 898 TYR LEU ARG LEU ASN THR LEU ALA SER LEU GLY TYR ALA
SEQRES 55 A 898 VAL VAL VAL ILE ASP GLY ARG GLY SER CYS GLN ARG GLY
SEQRES 56 A 898 LEU ARG PHE GLU GLY ALA LEU LYS ASN GLN MET GLY GLN
SEQRES 57 A 898 VAL GLU ILE GLU ASP GLN VAL GLU GLY LEU GLN PHE VAL
SEQRES 58 A 898 ALA GLU LYS TYR GLY PHE ILE ASP LEU SER ARG VAL ALA
SEQRES 59 A 898 ILE HIS GLY TRP SER TYR GLY GLY PHE LEU SER LEU MET
SEQRES 60 A 898 GLY LEU ILE HIS LYS PRO GLN VAL PHE LYS VAL ALA ILE
SEQRES 61 A 898 ALA GLY ALA PRO VAL THR VAL TRP MET ALA TYR ASP THR
SEQRES 62 A 898 GLY TYR THR GLU ARG TYR MET ASP VAL PRO GLU ASN ASN
SEQRES 63 A 898 GLN HIS GLY TYR GLU ALA GLY SER VAL ALA LEU HIS VAL
SEQRES 64 A 898 GLU LYS LEU PRO ASN GLU PRO ASN ARG LEU LEU ILE LEU
SEQRES 65 A 898 HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE PHE HIS THR
SEQRES 66 A 898 ASN PHE LEU VAL SER GLN LEU ILE ARG ALA GLY LYS PRO
SEQRES 67 A 898 TYR GLN LEU GLN ILE TYR PRO ASN GLU ARG HIS SER ILE
SEQRES 68 A 898 ARG CYS PRO GLU SER GLY GLU HIS TYR GLU VAL THR LEU
SEQRES 69 A 898 LEU HIS PHE LEU GLN GLU TYR LEU HIS HIS HIS HIS HIS
SEQRES 70 A 898 HIS
SEQRES 1 C 898 MET ARG LYS VAL LYS LYS LEU ARG LEU ASP LYS GLU ASN
SEQRES 2 C 898 THR GLY SER TRP ARG SER PHE SER LEU ASN SER GLU GLY
SEQRES 3 C 898 ALA GLU ARG MET ALA THR THR GLY THR PRO THR ALA ASP
SEQRES 4 C 898 ARG GLY ASP ALA ALA ALA THR ASP ASP PRO ALA ALA ARG
SEQRES 5 C 898 PHE GLN VAL GLN LYS HIS SER TRP ASP GLY LEU ARG SER
SEQRES 6 C 898 ILE ILE HIS GLY SER ARG LYS TYR SER GLY LEU ILE VAL
SEQRES 7 C 898 ASN LYS ALA PRO HIS ASP PHE GLN PHE VAL GLN LYS THR
SEQRES 8 C 898 ASP GLU SER GLY PRO HIS SER HIS ARG LEU TYR TYR LEU
SEQRES 9 C 898 GLY MET PRO TYR GLY SER ARG GLU ASN SER LEU LEU TYR
SEQRES 10 C 898 SER GLU ILE PRO LYS LYS VAL ARG LYS GLU ALA LEU LEU
SEQRES 11 C 898 LEU LEU SER TRP LYS GLN MET LEU ASP HIS PHE GLN ALA
SEQRES 12 C 898 THR PRO HIS HIS GLY VAL TYR SER ARG GLU GLU GLU LEU
SEQRES 13 C 898 LEU ARG GLU ARG LYS ARG LEU GLY VAL PHE GLY ILE THR
SEQRES 14 C 898 SER TYR ASP PHE HIS SER GLU SER GLY LEU PHE LEU PHE
SEQRES 15 C 898 GLN ALA SER ASN SER LEU PHE HIS CYS ARG ASP GLY GLY
SEQRES 16 C 898 LYS ASN GLY PHE MET VAL SER PRO MET LYS PRO LEU GLU
SEQRES 17 C 898 ILE LYS THR GLN CYS SER GLY PRO ARG MET ASP PRO LYS
SEQRES 18 C 898 ILE CYS PRO ALA ASP PRO ALA PHE PHE SER PHE ILE ASN
SEQRES 19 C 898 ASN SER ASP LEU TRP VAL ALA ASN ILE GLU THR GLY GLU
SEQRES 20 C 898 GLU ARG ARG LEU THR PHE CYS HIS GLN GLY LEU SER ASN
SEQRES 21 C 898 VAL LEU ASP ASP PRO LYS SER ALA GLY VAL ALA THR PHE
SEQRES 22 C 898 VAL ILE GLN GLU GLU PHE ASP ARG PHE THR GLY TYR TRP
SEQRES 23 C 898 TRP CYS PRO THR ALA SER TRP GLU GLY SER GLU GLY LEU
SEQRES 24 C 898 LYS THR LEU ARG ILE LEU TYR GLU GLU VAL ASP GLU SER
SEQRES 25 C 898 GLU VAL GLU VAL ILE HIS VAL PRO SER PRO ALA LEU GLU
SEQRES 26 C 898 GLU ARG LYS THR ASP SER TYR ARG TYR PRO ARG THR GLY
SEQRES 27 C 898 SER LYS ASN PRO LYS ILE ALA LEU LYS LEU ALA GLU PHE
SEQRES 28 C 898 GLN THR ASP SER GLN GLY LYS ILE VAL SER THR GLN GLU
SEQRES 29 C 898 LYS GLU LEU VAL GLN PRO PHE SER SER LEU PHE PRO LYS
SEQRES 30 C 898 VAL GLU TYR ILE ALA ARG ALA GLY TRP THR ARG ASP GLY
SEQRES 31 C 898 LYS TYR ALA TRP ALA MET PHE LEU ASP ARG PRO GLN GLN
SEQRES 32 C 898 TRP LEU GLN LEU VAL LEU LEU PRO PRO ALA LEU PHE ILE
SEQRES 33 C 898 PRO SER THR GLU ASN GLU GLU GLN ARG LEU ALA SER ALA
SEQRES 34 C 898 ARG ALA VAL PRO ARG ASN VAL GLN PRO TYR VAL VAL TYR
SEQRES 35 C 898 GLU GLU VAL THR ASN VAL TRP ILE ASN VAL HIS ASP ILE
SEQRES 36 C 898 PHE TYR PRO PHE PRO GLN SER GLU GLY GLU ASP GLU LEU
SEQRES 37 C 898 CYS PHE LEU ARG ALA ASN GLU CYS LYS THR GLY PHE CYS
SEQRES 38 C 898 HIS LEU TYR LYS VAL THR ALA VAL LEU LYS SER GLN GLY
SEQRES 39 C 898 TYR ASP TRP SER GLU PRO PHE SER PRO GLY GLU ASP GLU
SEQRES 40 C 898 PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA LEU THR SER
SEQRES 41 C 898 GLY GLU TRP GLU VAL LEU ALA ARG HIS GLY SER LYS ILE
SEQRES 42 C 898 TRP VAL ASN GLU GLU THR LYS LEU VAL TYR PHE GLN GLY
SEQRES 43 C 898 THR LYS ASP THR PRO LEU GLU HIS HIS LEU TYR VAL VAL
SEQRES 44 C 898 SER TYR GLU ALA ALA GLY GLU ILE VAL ARG LEU THR THR
SEQRES 45 C 898 PRO GLY PHE SER HIS SER CYS SER MET SER GLN ASN PHE
SEQRES 46 C 898 ASP MET PHE VAL SER HIS TYR SER SER VAL SER THR PRO
SEQRES 47 C 898 PRO CYS VAL HIS VAL TYR LYS LEU SER GLY PRO ASP ASP
SEQRES 48 C 898 ASP PRO LEU HIS LYS GLN PRO ARG PHE TRP ALA SER MET
SEQRES 49 C 898 MET GLU ALA ALA SER CYS PRO PRO ASP TYR VAL PRO PRO
SEQRES 50 C 898 GLU ILE PHE HIS PHE HIS THR ARG SER ASP VAL ARG LEU
SEQRES 51 C 898 TYR GLY MET ILE TYR LYS PRO HIS ALA LEU GLN PRO GLY
SEQRES 52 C 898 LYS LYS HIS PRO THR VAL LEU PHE VAL TYR GLY GLY PRO
SEQRES 53 C 898 GLN VAL GLN LEU VAL ASN ASN SER PHE LYS GLY ILE LYS
SEQRES 54 C 898 TYR LEU ARG LEU ASN THR LEU ALA SER LEU GLY TYR ALA
SEQRES 55 C 898 VAL VAL VAL ILE ASP GLY ARG GLY SER CYS GLN ARG GLY
SEQRES 56 C 898 LEU ARG PHE GLU GLY ALA LEU LYS ASN GLN MET GLY GLN
SEQRES 57 C 898 VAL GLU ILE GLU ASP GLN VAL GLU GLY LEU GLN PHE VAL
SEQRES 58 C 898 ALA GLU LYS TYR GLY PHE ILE ASP LEU SER ARG VAL ALA
SEQRES 59 C 898 ILE HIS GLY TRP SER TYR GLY GLY PHE LEU SER LEU MET
SEQRES 60 C 898 GLY LEU ILE HIS LYS PRO GLN VAL PHE LYS VAL ALA ILE
SEQRES 61 C 898 ALA GLY ALA PRO VAL THR VAL TRP MET ALA TYR ASP THR
SEQRES 62 C 898 GLY TYR THR GLU ARG TYR MET ASP VAL PRO GLU ASN ASN
SEQRES 63 C 898 GLN HIS GLY TYR GLU ALA GLY SER VAL ALA LEU HIS VAL
SEQRES 64 C 898 GLU LYS LEU PRO ASN GLU PRO ASN ARG LEU LEU ILE LEU
SEQRES 65 C 898 HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE PHE HIS THR
SEQRES 66 C 898 ASN PHE LEU VAL SER GLN LEU ILE ARG ALA GLY LYS PRO
SEQRES 67 C 898 TYR GLN LEU GLN ILE TYR PRO ASN GLU ARG HIS SER ILE
SEQRES 68 C 898 ARG CYS PRO GLU SER GLY GLU HIS TYR GLU VAL THR LEU
SEQRES 69 C 898 LEU HIS PHE LEU GLN GLU TYR LEU HIS HIS HIS HIS HIS
SEQRES 70 C 898 HIS
SEQRES 1 D 898 MET ARG LYS VAL LYS LYS LEU ARG LEU ASP LYS GLU ASN
SEQRES 2 D 898 THR GLY SER TRP ARG SER PHE SER LEU ASN SER GLU GLY
SEQRES 3 D 898 ALA GLU ARG MET ALA THR THR GLY THR PRO THR ALA ASP
SEQRES 4 D 898 ARG GLY ASP ALA ALA ALA THR ASP ASP PRO ALA ALA ARG
SEQRES 5 D 898 PHE GLN VAL GLN LYS HIS SER TRP ASP GLY LEU ARG SER
SEQRES 6 D 898 ILE ILE HIS GLY SER ARG LYS TYR SER GLY LEU ILE VAL
SEQRES 7 D 898 ASN LYS ALA PRO HIS ASP PHE GLN PHE VAL GLN LYS THR
SEQRES 8 D 898 ASP GLU SER GLY PRO HIS SER HIS ARG LEU TYR TYR LEU
SEQRES 9 D 898 GLY MET PRO TYR GLY SER ARG GLU ASN SER LEU LEU TYR
SEQRES 10 D 898 SER GLU ILE PRO LYS LYS VAL ARG LYS GLU ALA LEU LEU
SEQRES 11 D 898 LEU LEU SER TRP LYS GLN MET LEU ASP HIS PHE GLN ALA
SEQRES 12 D 898 THR PRO HIS HIS GLY VAL TYR SER ARG GLU GLU GLU LEU
SEQRES 13 D 898 LEU ARG GLU ARG LYS ARG LEU GLY VAL PHE GLY ILE THR
SEQRES 14 D 898 SER TYR ASP PHE HIS SER GLU SER GLY LEU PHE LEU PHE
SEQRES 15 D 898 GLN ALA SER ASN SER LEU PHE HIS CYS ARG ASP GLY GLY
SEQRES 16 D 898 LYS ASN GLY PHE MET VAL SER PRO MET LYS PRO LEU GLU
SEQRES 17 D 898 ILE LYS THR GLN CYS SER GLY PRO ARG MET ASP PRO LYS
SEQRES 18 D 898 ILE CYS PRO ALA ASP PRO ALA PHE PHE SER PHE ILE ASN
SEQRES 19 D 898 ASN SER ASP LEU TRP VAL ALA ASN ILE GLU THR GLY GLU
SEQRES 20 D 898 GLU ARG ARG LEU THR PHE CYS HIS GLN GLY LEU SER ASN
SEQRES 21 D 898 VAL LEU ASP ASP PRO LYS SER ALA GLY VAL ALA THR PHE
SEQRES 22 D 898 VAL ILE GLN GLU GLU PHE ASP ARG PHE THR GLY TYR TRP
SEQRES 23 D 898 TRP CYS PRO THR ALA SER TRP GLU GLY SER GLU GLY LEU
SEQRES 24 D 898 LYS THR LEU ARG ILE LEU TYR GLU GLU VAL ASP GLU SER
SEQRES 25 D 898 GLU VAL GLU VAL ILE HIS VAL PRO SER PRO ALA LEU GLU
SEQRES 26 D 898 GLU ARG LYS THR ASP SER TYR ARG TYR PRO ARG THR GLY
SEQRES 27 D 898 SER LYS ASN PRO LYS ILE ALA LEU LYS LEU ALA GLU PHE
SEQRES 28 D 898 GLN THR ASP SER GLN GLY LYS ILE VAL SER THR GLN GLU
SEQRES 29 D 898 LYS GLU LEU VAL GLN PRO PHE SER SER LEU PHE PRO LYS
SEQRES 30 D 898 VAL GLU TYR ILE ALA ARG ALA GLY TRP THR ARG ASP GLY
SEQRES 31 D 898 LYS TYR ALA TRP ALA MET PHE LEU ASP ARG PRO GLN GLN
SEQRES 32 D 898 TRP LEU GLN LEU VAL LEU LEU PRO PRO ALA LEU PHE ILE
SEQRES 33 D 898 PRO SER THR GLU ASN GLU GLU GLN ARG LEU ALA SER ALA
SEQRES 34 D 898 ARG ALA VAL PRO ARG ASN VAL GLN PRO TYR VAL VAL TYR
SEQRES 35 D 898 GLU GLU VAL THR ASN VAL TRP ILE ASN VAL HIS ASP ILE
SEQRES 36 D 898 PHE TYR PRO PHE PRO GLN SER GLU GLY GLU ASP GLU LEU
SEQRES 37 D 898 CYS PHE LEU ARG ALA ASN GLU CYS LYS THR GLY PHE CYS
SEQRES 38 D 898 HIS LEU TYR LYS VAL THR ALA VAL LEU LYS SER GLN GLY
SEQRES 39 D 898 TYR ASP TRP SER GLU PRO PHE SER PRO GLY GLU ASP GLU
SEQRES 40 D 898 PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA LEU THR SER
SEQRES 41 D 898 GLY GLU TRP GLU VAL LEU ALA ARG HIS GLY SER LYS ILE
SEQRES 42 D 898 TRP VAL ASN GLU GLU THR LYS LEU VAL TYR PHE GLN GLY
SEQRES 43 D 898 THR LYS ASP THR PRO LEU GLU HIS HIS LEU TYR VAL VAL
SEQRES 44 D 898 SER TYR GLU ALA ALA GLY GLU ILE VAL ARG LEU THR THR
SEQRES 45 D 898 PRO GLY PHE SER HIS SER CYS SER MET SER GLN ASN PHE
SEQRES 46 D 898 ASP MET PHE VAL SER HIS TYR SER SER VAL SER THR PRO
SEQRES 47 D 898 PRO CYS VAL HIS VAL TYR LYS LEU SER GLY PRO ASP ASP
SEQRES 48 D 898 ASP PRO LEU HIS LYS GLN PRO ARG PHE TRP ALA SER MET
SEQRES 49 D 898 MET GLU ALA ALA SER CYS PRO PRO ASP TYR VAL PRO PRO
SEQRES 50 D 898 GLU ILE PHE HIS PHE HIS THR ARG SER ASP VAL ARG LEU
SEQRES 51 D 898 TYR GLY MET ILE TYR LYS PRO HIS ALA LEU GLN PRO GLY
SEQRES 52 D 898 LYS LYS HIS PRO THR VAL LEU PHE VAL TYR GLY GLY PRO
SEQRES 53 D 898 GLN VAL GLN LEU VAL ASN ASN SER PHE LYS GLY ILE LYS
SEQRES 54 D 898 TYR LEU ARG LEU ASN THR LEU ALA SER LEU GLY TYR ALA
SEQRES 55 D 898 VAL VAL VAL ILE ASP GLY ARG GLY SER CYS GLN ARG GLY
SEQRES 56 D 898 LEU ARG PHE GLU GLY ALA LEU LYS ASN GLN MET GLY GLN
SEQRES 57 D 898 VAL GLU ILE GLU ASP GLN VAL GLU GLY LEU GLN PHE VAL
SEQRES 58 D 898 ALA GLU LYS TYR GLY PHE ILE ASP LEU SER ARG VAL ALA
SEQRES 59 D 898 ILE HIS GLY TRP SER TYR GLY GLY PHE LEU SER LEU MET
SEQRES 60 D 898 GLY LEU ILE HIS LYS PRO GLN VAL PHE LYS VAL ALA ILE
SEQRES 61 D 898 ALA GLY ALA PRO VAL THR VAL TRP MET ALA TYR ASP THR
SEQRES 62 D 898 GLY TYR THR GLU ARG TYR MET ASP VAL PRO GLU ASN ASN
SEQRES 63 D 898 GLN HIS GLY TYR GLU ALA GLY SER VAL ALA LEU HIS VAL
SEQRES 64 D 898 GLU LYS LEU PRO ASN GLU PRO ASN ARG LEU LEU ILE LEU
SEQRES 65 D 898 HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE PHE HIS THR
SEQRES 66 D 898 ASN PHE LEU VAL SER GLN LEU ILE ARG ALA GLY LYS PRO
SEQRES 67 D 898 TYR GLN LEU GLN ILE TYR PRO ASN GLU ARG HIS SER ILE
SEQRES 68 D 898 ARG CYS PRO GLU SER GLY GLU HIS TYR GLU VAL THR LEU
SEQRES 69 D 898 LEU HIS PHE LEU GLN GLU TYR LEU HIS HIS HIS HIS HIS
SEQRES 70 D 898 HIS
HET PO4 B 901 5
HET GOL B 902 6
HET PO4 A 901 5
HET GOL A 902 6
HET PO4 C 901 5
HET PO4 D 901 5
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 PO4 4(O4 P 3-)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 11 HOH *129(H2 O)
HELIX 1 AA1 SER B 30 ARG B 42 1 13
HELIX 2 AA2 THR B 243 PHE B 250 1 8
HELIX 3 AA3 PRO B 341 PHE B 346 1 6
HELIX 4 AA4 PRO B 382 ALA B 384 5 3
HELIX 5 AA5 ASN B 392 VAL B 403 1 12
HELIX 6 AA6 TYR B 661 LEU B 670 1 10
HELIX 7 AA7 GLY B 686 GLY B 691 1 6
HELIX 8 AA8 ALA B 692 LYS B 694 5 3
HELIX 9 AA9 GLY B 698 TYR B 716 1 19
HELIX 10 AB1 SER B 730 LYS B 743 1 14
HELIX 11 AB2 VAL B 758 TYR B 762 5 5
HELIX 12 AB3 ASP B 763 ASP B 772 1 10
HELIX 13 AB4 ASN B 777 SER B 785 1 9
HELIX 14 AB5 HIS B 789 LEU B 793 5 5
HELIX 15 AB6 PHE B 813 ALA B 826 1 14
HELIX 16 AB7 CYS B 844 LEU B 863 1 20
HELIX 17 AB8 SER A 30 SER A 41 1 12
HELIX 18 AB9 THR A 243 PHE A 250 1 8
HELIX 19 AC1 ALA A 294 ARG A 298 5 5
HELIX 20 AC2 PRO A 341 PHE A 346 1 6
HELIX 21 AC3 PRO A 382 ALA A 384 5 3
HELIX 22 AC4 ASN A 392 VAL A 403 1 12
HELIX 23 AC5 LEU A 662 LEU A 670 1 9
HELIX 24 AC6 GLY A 686 GLY A 691 1 6
HELIX 25 AC7 VAL A 700 TYR A 716 1 17
HELIX 26 AC8 SER A 730 LYS A 743 1 14
HELIX 27 AC9 VAL A 758 TYR A 762 5 5
HELIX 28 AD1 ASP A 763 ASP A 772 1 10
HELIX 29 AD2 ASN A 777 GLY A 784 1 8
HELIX 30 AD3 SER A 785 LEU A 793 5 9
HELIX 31 AD4 PHE A 813 ALA A 826 1 14
HELIX 32 AD5 CYS A 844 LEU A 863 1 20
HELIX 33 AD6 ASP C 18 ARG C 23 1 6
HELIX 34 AD7 SER C 30 ARG C 42 1 13
HELIX 35 AD8 THR C 243 PHE C 250 1 8
HELIX 36 AD9 PRO C 341 PHE C 346 1 6
HELIX 37 AE1 PRO C 382 ALA C 384 5 3
HELIX 38 AE2 ASN C 392 ALA C 402 1 11
HELIX 39 AE3 TYR C 661 LEU C 670 1 10
HELIX 40 AE4 GLY C 686 GLY C 691 1 6
HELIX 41 AE5 ALA C 692 LYS C 694 5 3
HELIX 42 AE6 GLN C 699 TYR C 716 1 18
HELIX 43 AE7 SER C 730 LYS C 743 1 14
HELIX 44 AE8 VAL C 758 TYR C 762 5 5
HELIX 45 AE9 ASP C 763 ASP C 772 1 10
HELIX 46 AF1 ASN C 777 GLY C 784 1 8
HELIX 47 AF2 HIS C 789 LEU C 793 5 5
HELIX 48 AF3 PHE C 813 ALA C 826 1 14
HELIX 49 AF4 CYS C 844 LEU C 863 1 20
HELIX 50 AF5 SER D 30 ARG D 42 1 13
HELIX 51 AF6 THR D 243 ASP D 251 1 9
HELIX 52 AF7 PRO D 341 PHE D 346 1 6
HELIX 53 AF8 PRO D 382 ALA D 384 5 3
HELIX 54 AF9 ASN D 392 ARG D 401 1 10
HELIX 55 AG1 TYR D 661 LEU D 670 1 10
HELIX 56 AG2 GLY D 686 GLY D 691 1 6
HELIX 57 AG3 ALA D 692 LYS D 694 5 3
HELIX 58 AG4 VAL D 700 TYR D 716 1 17
HELIX 59 AG5 SER D 730 LYS D 743 1 14
HELIX 60 AG6 VAL D 758 TYR D 762 5 5
HELIX 61 AG7 ASP D 763 ASP D 772 1 10
HELIX 62 AG8 ASN D 777 SER D 785 1 9
HELIX 63 AG9 VAL D 786 LEU D 793 5 8
HELIX 64 AH1 PHE D 813 GLY D 827 1 15
HELIX 65 AH2 CYS D 844 LEU D 863 1 20
SHEET 1 AA1 4 GLN B 57 GLN B 60 0
SHEET 2 AA1 4 HIS B 68 GLY B 76 -1 O TYR B 73 N GLN B 57
SHEET 3 AA1 4 SER B 85 PRO B 92 -1 O ILE B 91 N SER B 69
SHEET 4 AA1 4 LYS B 106 GLN B 107 -1 O LYS B 106 N TYR B 88
SHEET 1 AA2 4 TYR B 142 HIS B 145 0
SHEET 2 AA2 4 LEU B 150 PHE B 153 -1 O LEU B 152 N ASP B 143
SHEET 3 AA2 4 PHE B 160 ARG B 163 -1 O CYS B 162 N PHE B 151
SHEET 4 AA2 4 LEU B 178 GLU B 179 -1 O LEU B 178 N HIS B 161
SHEET 1 AA3 4 MET B 189 ILE B 193 0
SHEET 2 AA3 4 PHE B 200 ILE B 204 -1 O ILE B 204 N MET B 189
SHEET 3 AA3 4 LEU B 209 ASN B 213 -1 O TRP B 210 N PHE B 203
SHEET 4 AA3 4 ARG B 220 ARG B 221 -1 O ARG B 220 N VAL B 211
SHEET 1 AA4 4 LYS B 237 ALA B 239 0
SHEET 2 AA4 4 ILE B 275 ASP B 281 -1 O VAL B 280 N SER B 238
SHEET 3 AA4 4 LYS B 314 THR B 324 -1 O ALA B 320 N ILE B 275
SHEET 4 AA4 4 LYS B 271 LEU B 273 -1 N LEU B 273 O PHE B 322
SHEET 1 AA5 5 TYR B 256 TRP B 258 0
SHEET 2 AA5 5 ILE B 275 ASP B 281 -1 O LEU B 276 N TRP B 257
SHEET 3 AA5 5 LYS B 314 THR B 324 -1 O ALA B 320 N ILE B 275
SHEET 4 AA5 5 ILE B 330 LEU B 338 -1 O LYS B 336 N LEU B 319
SHEET 5 AA5 5 PHE B 386 PRO B 388 -1 O ILE B 387 N GLU B 337
SHEET 1 AA6 2 VAL B 287 PRO B 291 0
SHEET 2 AA6 2 THR B 300 ARG B 304 -1 O ASP B 301 N VAL B 290
SHEET 1 AA7 4 TYR B 351 TRP B 357 0
SHEET 2 AA7 4 ALA B 364 LEU B 369 -1 O MET B 367 N ARG B 354
SHEET 3 AA7 4 TRP B 375 LEU B 381 -1 O VAL B 379 N ALA B 366
SHEET 4 AA7 4 TYR B 410 VAL B 416 -1 O GLU B 415 N LEU B 376
SHEET 1 AA8 4 PHE B 427 PRO B 429 0
SHEET 2 AA8 4 CYS B 440 ASN B 445 -1 O LEU B 442 N TYR B 428
SHEET 3 AA8 4 HIS B 453 ALA B 459 -1 O VAL B 457 N PHE B 441
SHEET 4 AA8 4 ILE B 483 ALA B 488 -1 O ILE B 487 N LYS B 456
SHEET 1 AA9 4 TRP B 505 ASN B 507 0
SHEET 2 AA9 4 LEU B 512 GLY B 517 -1 O TYR B 514 N TRP B 505
SHEET 3 AA9 4 HIS B 526 SER B 531 -1 O VAL B 530 N VAL B 513
SHEET 4 AA9 4 VAL B 539 ARG B 540 -1 O VAL B 539 N VAL B 529
SHEET 1 AB1 4 SER B 547 MET B 552 0
SHEET 2 AB1 4 MET B 558 SER B 564 -1 O HIS B 562 N SER B 549
SHEET 3 AB1 4 CYS B 571 SER B 578 -1 O TYR B 575 N PHE B 559
SHEET 4 AB1 4 GLN B 588 MET B 596 -1 O ALA B 593 N VAL B 574
SHEET 1 AB2 8 GLU B 609 HIS B 614 0
SHEET 2 AB2 8 ARG B 620 TYR B 626 -1 O LEU B 621 N PHE B 613
SHEET 3 AB2 8 ALA B 673 ILE B 677 -1 O VAL B 674 N TYR B 626
SHEET 4 AB2 8 HIS B 637 PHE B 642 1 N VAL B 640 O ALA B 673
SHEET 5 AB2 8 ILE B 719 TRP B 729 1 O ALA B 725 N LEU B 641
SHEET 6 AB2 8 PHE B 747 GLY B 753 1 O GLY B 753 N GLY B 728
SHEET 7 AB2 8 LEU B 800 GLY B 805 1 O LEU B 801 N ALA B 750
SHEET 8 AB2 8 LEU B 832 TYR B 835 1 O GLN B 833 N ILE B 802
SHEET 1 AB3 4 HIS A 54 GLN A 60 0
SHEET 2 AB3 4 HIS A 68 GLY A 76 -1 O LEU A 75 N HIS A 54
SHEET 3 AB3 4 SER A 85 PRO A 92 -1 O SER A 89 N LEU A 72
SHEET 4 AB3 4 LYS A 106 GLN A 107 -1 O LYS A 106 N TYR A 88
SHEET 1 AB4 4 ASP A 143 PHE A 144 0
SHEET 2 AB4 4 LEU A 150 ALA A 155 -1 O LEU A 152 N ASP A 143
SHEET 3 AB4 4 SER A 158 ARG A 163 -1 O CYS A 162 N PHE A 151
SHEET 4 AB4 4 LEU A 178 ILE A 180 -1 O LEU A 178 N HIS A 161
SHEET 1 AB5 4 MET A 189 ILE A 193 0
SHEET 2 AB5 4 PHE A 200 ILE A 204 -1 O SER A 202 N LYS A 192
SHEET 3 AB5 4 LEU A 209 ASN A 213 -1 O TRP A 210 N PHE A 203
SHEET 4 AB5 4 GLU A 219 ARG A 221 -1 O ARG A 220 N VAL A 211
SHEET 1 AB6 4 LYS A 237 ALA A 239 0
SHEET 2 AB6 4 ILE A 275 ASP A 281 -1 O VAL A 280 N SER A 238
SHEET 3 AB6 4 LYS A 314 THR A 324 -1 O LYS A 318 N TYR A 277
SHEET 4 AB6 4 LYS A 271 LEU A 273 -1 N LYS A 271 O THR A 324
SHEET 1 AB7 5 TYR A 256 TRP A 258 0
SHEET 2 AB7 5 ILE A 275 ASP A 281 -1 O LEU A 276 N TRP A 257
SHEET 3 AB7 5 LYS A 314 THR A 324 -1 O LYS A 318 N TYR A 277
SHEET 4 AB7 5 ILE A 330 LEU A 338 -1 O LYS A 336 N LEU A 319
SHEET 5 AB7 5 PHE A 386 PRO A 388 -1 O ILE A 387 N GLU A 337
SHEET 1 AB8 2 VAL A 287 PRO A 291 0
SHEET 2 AB8 2 THR A 300 ARG A 304 -1 O ASP A 301 N VAL A 290
SHEET 1 AB9 4 TYR A 351 TRP A 357 0
SHEET 2 AB9 4 ALA A 364 LEU A 369 -1 O MET A 367 N ALA A 353
SHEET 3 AB9 4 TRP A 375 LEU A 381 -1 O LEU A 381 N ALA A 364
SHEET 4 AB9 4 TYR A 410 VAL A 416 -1 O TYR A 410 N LEU A 380
SHEET 1 AC1 4 PHE A 427 PRO A 429 0
SHEET 2 AC1 4 GLU A 438 ASN A 445 -1 O LEU A 442 N TYR A 428
SHEET 3 AC1 4 HIS A 453 VAL A 460 -1 O VAL A 457 N PHE A 441
SHEET 4 AC1 4 ILE A 483 ALA A 488 -1 O ILE A 487 N LYS A 456
SHEET 1 AC2 4 TRP A 505 ASN A 507 0
SHEET 2 AC2 4 LEU A 512 THR A 521 -1 O TYR A 514 N TRP A 505
SHEET 3 AC2 4 GLU A 524 SER A 531 -1 O VAL A 530 N VAL A 513
SHEET 4 AC2 4 VAL A 539 ARG A 540 -1 O VAL A 539 N VAL A 529
SHEET 1 AC3 4 SER A 547 MET A 552 0
SHEET 2 AC3 4 MET A 558 SER A 564 -1 O HIS A 562 N SER A 549
SHEET 3 AC3 4 CYS A 571 SER A 578 -1 O TYR A 575 N PHE A 559
SHEET 4 AC3 4 GLN A 588 MET A 596 -1 O ALA A 593 N VAL A 574
SHEET 1 AC4 8 PHE A 611 HIS A 614 0
SHEET 2 AC4 8 ARG A 620 TYR A 626 -1 O GLY A 623 N PHE A 611
SHEET 3 AC4 8 ALA A 673 ILE A 677 -1 O VAL A 674 N TYR A 626
SHEET 4 AC4 8 HIS A 637 VAL A 643 1 N PHE A 642 O VAL A 675
SHEET 5 AC4 8 ILE A 719 TRP A 729 1 O ASP A 720 N HIS A 637
SHEET 6 AC4 8 VAL A 749 GLY A 753 1 O GLY A 753 N GLY A 728
SHEET 7 AC4 8 LEU A 800 GLY A 805 1 O LEU A 803 N ALA A 752
SHEET 8 AC4 8 GLN A 831 TYR A 835 1 O GLN A 833 N ILE A 802
SHEET 1 AC5 4 HIS C 54 GLN C 60 0
SHEET 2 AC5 4 HIS C 70 GLY C 76 -1 O TYR C 73 N GLN C 57
SHEET 3 AC5 4 SER C 85 SER C 89 -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 TYR C 142 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 LEU C 159 ARG C 163 -1 O PHE C 160 N PHE C 153
SHEET 4 AC6 4 LEU C 178 ILE C 180 -1 O ILE C 180 N LEU C 159
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 PHE C 322 N LEU C 273
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 MET C 367 N ALA C 353
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 413 N LEU C 378
SHEET 1 AD3 4 PHE C 427 PRO C 429 0
SHEET 2 AD3 4 GLU C 438 ASN C 445 -1 O LEU C 442 N TYR C 428
SHEET 3 AD3 4 HIS C 453 VAL C 460 -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 VAL C 530 N VAL C 513
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 MET C 595 N VAL C 572
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 VAL C 749 GLY C 753 1 O GLY C 753 N GLY C 728
SHEET 7 AD6 8 LEU C 800 GLY C 805 1 O LEU C 801 N ALA C 750
SHEET 8 AD6 8 GLN C 831 TYR C 835 1 O GLN C 831 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 TYR D 73 N GLN D 57
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 ASP D 143 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 ILE D 204 -1 O SER D 202 N LYS D 192
SHEET 3 AD9 4 LEU D 209 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 4 LYS D 237 ALA D 239 0
SHEET 2 AE1 4 ILE D 275 ASP D 281 -1 O VAL D 280 N SER D 238
SHEET 3 AE1 4 LYS D 314 THR D 324 -1 O LYS D 314 N ASP D 281
SHEET 4 AE1 4 LYS D 271 LEU D 273 -1 N LEU D 273 O PHE D 322
SHEET 1 AE2 5 TYR D 256 TRP D 258 0
SHEET 2 AE2 5 ILE D 275 ASP D 281 -1 O LEU D 276 N TRP D 257
SHEET 3 AE2 5 LYS D 314 THR D 324 -1 O LYS D 314 N ASP D 281
SHEET 4 AE2 5 SER D 332 LEU D 338 -1 O LYS D 336 N LEU D 319
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 MET D 367 N ARG D 354
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 411 -1 O TYR D 410 N LEU D 380
SHEET 1 AE5 4 TYR D 351 TRP D 357 0
SHEET 2 AE5 4 ALA D 364 LEU D 369 -1 O MET D 367 N ARG D 354
SHEET 3 AE5 4 TRP D 375 LEU D 381 -1 O LEU D 381 N ALA D 364
SHEET 4 AE5 4 GLU D 415 VAL D 416 -1 O GLU D 415 N LEU D 376
SHEET 1 AE6 4 PHE D 427 PRO D 429 0
SHEET 2 AE6 4 GLU D 438 ASN D 445 -1 O LEU D 442 N TYR D 428
SHEET 3 AE6 4 HIS D 453 VAL D 460 -1 O ALA D 459 N LEU D 439
SHEET 4 AE6 4 ILE D 483 ALA D 488 -1 O LYS D 484 N THR D 458
SHEET 1 AE7 4 TRP D 505 ASN D 507 0
SHEET 2 AE7 4 LEU D 512 THR D 521 -1 O TYR D 514 N TRP D 505
SHEET 3 AE7 4 GLU D 524 SER D 531 -1 O VAL D 530 N VAL D 513
SHEET 4 AE7 4 VAL D 539 ARG D 540 -1 O VAL D 539 N VAL D 529
SHEET 1 AE8 4 SER D 547 MET D 552 0
SHEET 2 AE8 4 MET D 558 SER D 565 -1 O HIS D 562 N SER D 549
SHEET 3 AE8 4 THR D 568 SER D 578 -1 O TYR D 575 N PHE D 559
SHEET 4 AE8 4 GLN D 588 MET D 596 -1 O ARG D 590 N LYS D 576
SHEET 1 AE9 8 GLU D 609 HIS D 614 0
SHEET 2 AE9 8 ARG D 620 TYR D 626 -1 O GLY D 623 N PHE D 611
SHEET 3 AE9 8 ALA D 673 ILE D 677 -1 O VAL D 676 N MET D 624
SHEET 4 AE9 8 HIS D 637 VAL D 643 1 N VAL D 640 O ALA D 673
SHEET 5 AE9 8 ILE D 719 TRP D 729 1 O ALA D 725 N LEU D 641
SHEET 6 AE9 8 VAL D 749 GLY D 753 1 O GLY D 753 N GLY D 728
SHEET 7 AE9 8 LEU D 800 GLY D 805 1 O LEU D 803 N ALA D 752
SHEET 8 AE9 8 GLN D 831 TYR D 835 1 O GLN D 833 N ILE D 802
SITE 1 AC1 6 TYR B 644 SER B 730 TYR B 731 VAL B 756
SITE 2 AC1 6 TYR B 762 TYR B 766
SITE 1 AC2 5 TYR B 413 GLU B 414 ASN B 445 LYS B 480
SITE 2 AC2 5 GLU B 486
SITE 1 AC3 5 TYR A 644 SER A 730 TYR A 731 TYR A 762
SITE 2 AC3 5 TYR A 766
SITE 1 AC4 4 ASN A 312 PRO A 313 ILE A 315 GLU A 350
SITE 1 AC5 4 TYR C 644 SER C 730 TYR C 762 TYR C 766
SITE 1 AC6 5 TYR D 644 SER D 730 TYR D 731 TYR D 762
SITE 2 AC6 5 TYR D 766
CRYST1 95.170 95.310 127.196 86.56 102.54 102.44 P 1 4
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 0.010508 0.002319 0.002304 0.00000
SCALE2 0.000000 0.010744 -0.000150 0.00000
SCALE3 0.000000 0.000000 0.008055 0.00000
TER 6330 HIS B 864
TER 12758 HIS A 865
TER 19148 HIS C 865
TER 25528 HIS D 864
MASTER 791 0 6 65 191 0 10 625685 4 32 280
END |