| 6qzv-pdb | HEADER HYDROLASE 12-MAR-19 6QZV
TITLE DPP9 BOUND TO A DIPEPTIDE (MP) FROM THE N-TERMINUS OF BRCA2
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;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: MET-PRO;
COMPND 11 CHAIN: E, F, G, H;
COMPND 12 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;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS DPP8, DPP9, BRCA2, DIPEPTIDE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.ROSS,R.GEISS-FRIEDLANDER,R.HUBER
REVDAT 1 30-SEP-20 6QZV 0
JRNL AUTH B.H.ROSS,R.HUBER
JRNL TITL DIPEPTIDYL PEPTIDASE 9 ACTIVITY PROMOTES THE REPAIR OF
JRNL TITL 2 MITOMYCIN-C INDUCED DNA DAMAGE BY CLAVING THE N-TERMINUS OF
JRNL TITL 3 BRCA2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0232
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.1
REMARK 3 NUMBER OF REFLECTIONS : 72706
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) : 0.289
REMARK 3 R VALUE (WORKING SET) : 0.286
REMARK 3 FREE R VALUE : 0.345
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3827
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) : 5385
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE SET COUNT : 283
REMARK 3 BIN FREE R VALUE : 0.4150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 26312
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.81000
REMARK 3 B22 (A**2) : 3.79000
REMARK 3 B33 (A**2) : -0.73000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.23000
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): 0.662
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.533
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.275
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.888
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.828
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 27089 ; 0.004 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 24371 ; 0.002 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 36728 ; 1.120 ; 1.644
REMARK 3 BOND ANGLES OTHERS (DEGREES): 56654 ; 0.348 ; 1.571
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3200 ; 7.218 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1496 ;33.113 ;22.092
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4425 ;18.554 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 160 ;18.169 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3305 ; 0.046 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 30132 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5996 ; 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): 12923 ; 1.136 ; 2.741
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 12922 ; 1.136 ; 2.741
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16082 ; 2.036 ; 4.099
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 16083 ; 2.036 ; 4.099
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 14166 ; 0.839 ; 2.803
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 14166 ; 0.838 ; 2.803
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 20646 ; 1.526 ; 4.166
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 29418 ; 3.670 ;30.200
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 29419 ; 3.670 ;30.201
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6QZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101210.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.25
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) : 1.00002
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76534
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 43.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.8
REMARK 200 DATA REDUNDANCY : 2.650
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.000
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: 6EOQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MG/ML OF PROTEIN, 10% PEG 8000, 25%
REMARK 280 GLYCEROL, 0.16 M CALCIUM ACETATE, 0.08 M CACODILATE PH 6.25.
REMARK 280 DROPS ARE SET IN A 1:1 RATIO., VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 58.60950
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -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 PRO A 20
REMARK 465 TYR A 44
REMARK 465 SER A 45
REMARK 465 GLY A 46
REMARK 465 LEU A 47
REMARK 465 ILE A 48
REMARK 465 VAL A 49
REMARK 465 ASN A 50
REMARK 465 LYS A 51
REMARK 465 THR A 62
REMARK 465 ASP A 63
REMARK 465 GLU A 64
REMARK 465 GLY A 80
REMARK 465 SER A 81
REMARK 465 LYS A 94
REMARK 465 VAL A 95
REMARK 465 ARG A 96
REMARK 465 LYS A 97
REMARK 465 GLU A 98
REMARK 465 ALA A 99
REMARK 465 LEU A 100
REMARK 465 GLY A 228
REMARK 465 LEU A 229
REMARK 465 SER A 230
REMARK 465 SER A 267
REMARK 465 GLU A 268
REMARK 465 GLY A 269
REMARK 465 SER A 433
REMARK 465 GLU A 434
REMARK 465 GLY A 435
REMARK 465 GLU A 436
REMARK 465 ASP A 437
REMARK 465 GLU A 438
REMARK 465 ALA A 599
REMARK 465 SER A 600
REMARK 465 CYS A 601
REMARK 465 PRO A 602
REMARK 465 PRO A 603
REMARK 465 HIS A 866
REMARK 465 HIS A 867
REMARK 465 HIS A 868
REMARK 465 HIS A 869
REMARK 465 MET B -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 TYR B 79
REMARK 465 GLY B 80
REMARK 465 SER B 81
REMARK 465 VAL B 95
REMARK 465 ARG B 96
REMARK 465 LYS B 97
REMARK 465 GLU B 98
REMARK 465 ALA B 99
REMARK 465 LEU B 100
REMARK 465 GLY B 165
REMARK 465 GLY B 166
REMARK 465 LYS B 167
REMARK 465 ASN B 168
REMARK 465 GLY B 228
REMARK 465 LEU B 229
REMARK 465 SER B 230
REMARK 465 ASN B 231
REMARK 465 GLU B 265
REMARK 465 GLY B 266
REMARK 465 SER B 267
REMARK 465 GLU B 268
REMARK 465 GLY B 269
REMARK 465 GLY B 435
REMARK 465 GLU B 436
REMARK 465 GLU B 476
REMARK 465 ASP B 477
REMARK 465 GLU B 478
REMARK 465 ALA B 599
REMARK 465 SER B 600
REMARK 465 CYS B 601
REMARK 465 PRO B 602
REMARK 465 PRO B 603
REMARK 465 HIS B 864
REMARK 465 HIS B 865
REMARK 465 HIS B 866
REMARK 465 HIS B 867
REMARK 465 HIS B 868
REMARK 465 HIS B 869
REMARK 465 MET C -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 THR C 17
REMARK 465 ASP C 18
REMARK 465 ASP C 19
REMARK 465 TYR C 44
REMARK 465 SER C 45
REMARK 465 GLY C 46
REMARK 465 LEU C 47
REMARK 465 ILE C 48
REMARK 465 VAL C 49
REMARK 465 ASN C 50
REMARK 465 LYS C 51
REMARK 465 TYR C 79
REMARK 465 GLY C 80
REMARK 465 SER C 81
REMARK 465 VAL C 95
REMARK 465 ARG C 96
REMARK 465 LYS C 97
REMARK 465 GLU C 98
REMARK 465 ALA C 99
REMARK 465 LEU C 100
REMARK 465 GLY C 166
REMARK 465 LYS C 167
REMARK 465 GLY C 228
REMARK 465 LEU C 229
REMARK 465 SER C 230
REMARK 465 ASN C 231
REMARK 465 GLU C 265
REMARK 465 GLY C 266
REMARK 465 SER C 267
REMARK 465 GLU C 268
REMARK 465 GLY C 269
REMARK 465 GLU C 434
REMARK 465 GLY C 435
REMARK 465 GLU C 436
REMARK 465 ALA C 599
REMARK 465 SER C 600
REMARK 465 CYS C 601
REMARK 465 PRO C 602
REMARK 465 PRO C 603
REMARK 465 HIS C 864
REMARK 465 HIS C 865
REMARK 465 HIS C 866
REMARK 465 HIS C 867
REMARK 465 HIS C 868
REMARK 465 HIS C 869
REMARK 465 MET D -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 SER D 65
REMARK 465 TYR D 79
REMARK 465 GLY D 80
REMARK 465 SER D 81
REMARK 465 LYS D 94
REMARK 465 VAL D 95
REMARK 465 ARG D 96
REMARK 465 LYS D 97
REMARK 465 GLU D 98
REMARK 465 ALA D 99
REMARK 465 LEU D 100
REMARK 465 GLY D 228
REMARK 465 LEU D 229
REMARK 465 SER D 230
REMARK 465 ASN D 231
REMARK 465 SER D 267
REMARK 465 GLU D 268
REMARK 465 GLY D 269
REMARK 465 GLU D 434
REMARK 465 GLY D 435
REMARK 465 SER D 600
REMARK 465 CYS D 601
REMARK 465 PRO D 602
REMARK 465 PRO D 603
REMARK 465 HIS D 864
REMARK 465 HIS D 865
REMARK 465 HIS D 866
REMARK 465 HIS D 867
REMARK 465 HIS D 868
REMARK 465 HIS D 869
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 118 -114.57 47.48
REMARK 500 SER A 156 -109.41 42.10
REMARK 500 SER A 158 -161.07 -102.08
REMARK 500 ASP A 190 64.80 64.05
REMARK 500 VAL A 232 -111.59 -76.14
REMARK 500 PRO A 313 124.11 -39.43
REMARK 500 ALA A 316 149.65 -174.93
REMARK 500 ASP A 325 -150.83 -101.17
REMARK 500 VAL A 331 -83.38 -98.74
REMARK 500 LYS A 348 -3.22 79.77
REMARK 500 GLN A 373 51.27 71.25
REMARK 500 VAL A 419 -76.00 -98.84
REMARK 500 TRP A 420 150.43 176.36
REMARK 500 PHE A 427 86.25 -156.24
REMARK 500 GLU A 486 85.46 -158.68
REMARK 500 GLU A 493 43.64 -85.23
REMARK 500 LYS A 511 31.16 70.61
REMARK 500 HIS A 586 42.92 -98.49
REMARK 500 ASP A 618 33.56 74.38
REMARK 500 TYR A 644 -75.41 -122.15
REMARK 500 TYR A 661 56.93 -109.68
REMARK 500 GLN A 696 33.83 -160.09
REMARK 500 SER A 730 -117.59 60.29
REMARK 500 LYS A 743 57.20 -142.90
REMARK 500 ALA A 754 60.63 37.75
REMARK 500 ASP A 772 -167.17 78.48
REMARK 500 ASN A 777 59.79 -146.18
REMARK 500 ASN A 798 4.92 83.73
REMARK 500 ARG A 839 -123.25 -91.63
REMARK 500 LEU A 863 94.56 -67.36
REMARK 500 ARG B 42 57.95 -96.98
REMARK 500 ASP B 55 73.60 60.54
REMARK 500 ASP B 110 84.97 -65.85
REMARK 500 HIS B 111 -101.83 53.89
REMARK 500 PHE B 112 160.65 63.69
REMARK 500 SER B 156 -132.11 41.07
REMARK 500 ASN B 157 50.42 -116.77
REMARK 500 SER B 158 -159.53 -161.40
REMARK 500 VAL B 172 -50.05 -121.01
REMARK 500 LEU B 233 -48.44 73.28
REMARK 500 GLU B 282 32.37 -99.56
REMARK 500 ALA B 294 78.57 -69.89
REMARK 500 LYS B 348 -9.13 82.23
REMARK 500 PRO B 372 8.11 -63.14
REMARK 500 PRO B 383 -8.19 -55.06
REMARK 500 VAL B 419 -85.72 -103.08
REMARK 500 SER B 433 -77.39 -114.53
REMARK 500 LEU B 461 73.50 -112.77
REMARK 500 GLU B 486 84.57 -159.04
REMARK 500 ALA B 498 27.76 -144.50
REMARK 500
REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6QZV A -28 863 UNP Q86TI2 DPP9_HUMAN 1 892
DBREF 6QZV B -28 863 UNP Q86TI2 DPP9_HUMAN 1 892
DBREF 6QZV C -28 863 UNP Q86TI2 DPP9_HUMAN 1 892
DBREF 6QZV D -28 863 UNP Q86TI2 DPP9_HUMAN 1 892
DBREF 6QZV E 232 233 PDB 6QZV 6QZV 232 233
DBREF 6QZV F 232 233 PDB 6QZV 6QZV 232 233
DBREF 6QZV G 232 233 PDB 6QZV 6QZV 232 233
DBREF 6QZV H 232 233 PDB 6QZV 6QZV 232 233
SEQADV 6QZV HIS A 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS A 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS A 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS A 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS A 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS A 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS B 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS B 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS B 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS B 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS B 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS B 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS C 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS C 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS C 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS C 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS C 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS C 869 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS D 864 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS D 865 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS D 866 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS D 867 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS D 868 UNP Q86TI2 EXPRESSION TAG
SEQADV 6QZV HIS D 869 UNP Q86TI2 EXPRESSION TAG
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 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 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
SEQRES 1 E 2 MET PRO
SEQRES 1 F 2 MET PRO
SEQRES 1 G 2 MET PRO
SEQRES 1 H 2 MET PRO
FORMUL 9 HOH *4(H2 O)
HELIX 1 AA1 SER A 30 ARG A 42 1 13
HELIX 2 AA2 SER A 122 LYS A 132 1 11
HELIX 3 AA3 THR A 243 ASP A 251 1 9
HELIX 4 AA4 SER A 283 VAL A 285 5 3
HELIX 5 AA5 PRO A 341 PHE A 346 1 6
HELIX 6 AA6 PRO A 382 ALA A 384 5 3
HELIX 7 AA7 ASN A 392 ALA A 402 1 11
HELIX 8 AA8 LEU A 662 GLY A 671 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 GLY A 717 1 18
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 VAL A 773 ASN A 776 5 4
HELIX 16 AB7 ASN A 777 GLY A 784 1 8
HELIX 17 AB8 SER A 785 LEU A 793 5 9
HELIX 18 AB9 PHE A 813 ALA A 826 1 14
HELIX 19 AC1 CYS A 844 LEU A 863 1 20
HELIX 20 AC2 SER B 30 ARG B 42 1 13
HELIX 21 AC3 PRO B 116 VAL B 120 5 5
HELIX 22 AC4 SER B 122 LYS B 132 1 11
HELIX 23 AC5 THR B 243 ASP B 251 1 9
HELIX 24 AC6 ALA B 294 ARG B 298 5 5
HELIX 25 AC7 PRO B 341 PHE B 346 1 6
HELIX 26 AC8 ASN B 392 VAL B 403 1 12
HELIX 27 AC9 ASP B 583 LYS B 587 5 5
HELIX 28 AD1 TYR B 661 LEU B 670 1 10
HELIX 29 AD2 GLY B 686 GLY B 691 1 6
HELIX 30 AD3 VAL B 700 TYR B 716 1 17
HELIX 31 AD4 SER B 730 LYS B 743 1 14
HELIX 32 AD5 ASP B 763 ASP B 772 1 10
HELIX 33 AD6 VAL B 773 ASN B 776 5 4
HELIX 34 AD7 ASN B 777 GLY B 784 1 8
HELIX 35 AD8 HIS B 789 LEU B 793 5 5
HELIX 36 AD9 PHE B 813 ALA B 826 1 14
HELIX 37 AE1 CYS B 844 LEU B 863 1 20
HELIX 38 AE2 SER C 30 ARG C 42 1 13
HELIX 39 AE3 SER C 122 LYS C 132 1 11
HELIX 40 AE4 THR C 243 ASP C 251 1 9
HELIX 41 AE5 ALA C 294 ARG C 298 5 5
HELIX 42 AE6 PRO C 341 PHE C 346 1 6
HELIX 43 AE7 PRO C 382 ALA C 384 5 3
HELIX 44 AE8 ASN C 392 VAL C 403 1 12
HELIX 45 AE9 TYR C 661 LEU C 670 1 10
HELIX 46 AF1 GLY C 686 GLY C 691 1 6
HELIX 47 AF2 VAL C 700 TYR C 716 1 17
HELIX 48 AF3 SER C 730 LYS C 743 1 14
HELIX 49 AF4 ASP C 763 ASP C 772 1 10
HELIX 50 AF5 ASN C 777 GLY C 784 1 8
HELIX 51 AF6 HIS C 789 LEU C 793 5 5
HELIX 52 AF7 PHE C 813 ALA C 826 1 14
HELIX 53 AF8 CYS C 844 LEU C 863 1 20
HELIX 54 AF9 SER D 30 ARG D 42 1 13
HELIX 55 AG1 PRO D 116 VAL D 120 5 5
HELIX 56 AG2 SER D 122 LYS D 132 1 11
HELIX 57 AG3 THR D 243 PHE D 250 1 8
HELIX 58 AG4 SER D 283 VAL D 285 5 3
HELIX 59 AG5 ALA D 294 ARG D 298 5 5
HELIX 60 AG6 PRO D 341 PHE D 346 1 6
HELIX 61 AG7 PRO D 382 ALA D 384 5 3
HELIX 62 AG8 ASN D 392 ALA D 402 1 11
HELIX 63 AG9 GLU D 446 GLY D 450 1 5
HELIX 64 AH1 ASP D 583 LYS D 587 5 5
HELIX 65 AH2 TYR D 661 LEU D 670 1 10
HELIX 66 AH3 GLY D 686 GLY D 691 1 6
HELIX 67 AH4 ALA D 692 LYS D 694 5 3
HELIX 68 AH5 VAL D 700 GLY D 717 1 18
HELIX 69 AH6 SER D 730 LYS D 743 1 14
HELIX 70 AH7 VAL D 758 TYR D 762 5 5
HELIX 71 AH8 ASP D 763 ASP D 772 1 10
HELIX 72 AH9 ASN D 777 GLY D 784 1 8
HELIX 73 AI1 SER D 785 LEU D 793 5 9
HELIX 74 AI2 PHE D 813 GLY D 827 1 15
HELIX 75 AI3 CYS D 844 LEU D 863 1 20
SHEET 1 AA1 4 HIS A 54 GLN A 60 0
SHEET 2 AA1 4 HIS A 70 GLY A 76 -1 O LEU A 75 N HIS A 54
SHEET 3 AA1 4 SER A 85 SER A 89 -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 GLN A 154 -1 O LEU A 152 N ASP A 143
SHEET 3 AA2 4 LEU A 159 ARG A 163 -1 O PHE A 160 N PHE A 153
SHEET 4 AA2 4 LEU A 178 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 ILE A 204 -1 O SER A 202 N LYS A 192
SHEET 3 AA3 4 LEU A 209 ASN A 213 -1 O TRP A 210 N PHE A 203
SHEET 4 AA3 4 GLU A 219 ARG A 221 -1 O ARG A 220 N VAL A 211
SHEET 1 AA4 3 LYS A 237 ALA A 239 0
SHEET 2 AA4 3 LYS A 271 ASP A 281 -1 O VAL A 280 N SER A 238
SHEET 3 AA4 3 SER A 263 TRP A 264 -1 N SER A 263 O THR A 272
SHEET 1 AA5 5 TYR A 256 TRP A 258 0
SHEET 2 AA5 5 LYS A 271 ASP A 281 -1 O LEU A 276 N TRP A 257
SHEET 3 AA5 5 LEU A 317 THR A 324 -1 O LYS A 318 N TYR A 277
SHEET 4 AA5 5 ILE A 330 LEU A 338 -1 O VAL A 331 N GLN A 323
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 MET A 367 N ARG A 354
SHEET 3 AA7 4 TRP A 375 LEU A 381 -1 O LEU A 381 N ALA A 364
SHEET 4 AA7 4 TYR A 410 VAL A 416 -1 O GLU A 415 N LEU A 376
SHEET 1 AA8 4 PHE A 427 PRO A 429 0
SHEET 2 AA8 4 CYS A 440 ASN A 445 -1 O LEU A 442 N TYR A 428
SHEET 3 AA8 4 HIS A 453 ALA A 459 -1 O VAL A 457 N PHE A 441
SHEET 4 AA8 4 ILE A 483 ALA A 488 -1 O ILE A 487 N LYS A 456
SHEET 1 AA9 4 TRP A 505 ASN A 507 0
SHEET 2 AA9 4 LEU A 512 THR A 521 -1 O TYR A 514 N TRP A 505
SHEET 3 AA9 4 GLU A 524 SER A 531 -1 O TYR A 528 N PHE A 515
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 TYR A 575 N PHE A 559
SHEET 4 AB1 4 GLN A 588 MET A 596 -1 O ARG A 590 N LYS A 576
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 674 N TYR A 626
SHEET 4 AB2 8 HIS A 637 PHE A 642 1 N PRO A 638 O ALA A 673
SHEET 5 AB2 8 ILE A 719 GLY A 728 1 O ALA A 725 N THR A 639
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 801 N ALA A 750
SHEET 8 AB2 8 GLN A 831 TYR A 835 1 O GLN A 833 N HIS A 804
SHEET 1 AB3 4 HIS B 54 GLN B 60 0
SHEET 2 AB3 4 HIS B 68 GLY B 76 -1 O TYR B 73 N GLN B 57
SHEET 3 AB3 4 SER B 85 PRO B 92 -1 O LEU B 87 N TYR B 74
SHEET 4 AB3 4 LYS B 106 GLN B 107 -1 O LYS B 106 N TYR B 88
SHEET 1 AB4 4 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 ARG B 163 -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 ILE B 204 -1 O ILE B 204 N MET B 189
SHEET 3 AB5 4 LEU B 209 ASN B 213 -1 O TRP B 210 N PHE B 203
SHEET 4 AB5 4 GLU B 219 ARG B 221 -1 O ARG B 220 N VAL B 211
SHEET 1 AB6 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 ALA B 316 N GLU B 279
SHEET 4 AB6 4 LYS B 271 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 ALA B 316 N GLU B 279
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 TYR B 303 N ILE B 288
SHEET 1 AB9 4 VAL B 349 TRP B 357 0
SHEET 2 AB9 4 ALA B 364 ASP B 370 -1 O LEU B 369 N GLU B 350
SHEET 3 AB9 4 TRP B 375 LEU B 381 -1 O LEU B 381 N ALA B 364
SHEET 4 AB9 4 TYR B 410 VAL B 416 -1 O GLU B 415 N LEU B 376
SHEET 1 AC1 4 PHE B 427 PRO B 429 0
SHEET 2 AC1 4 CYS B 440 ALA B 444 -1 O LEU B 442 N TYR B 428
SHEET 3 AC1 4 LEU B 454 ALA B 459 -1 O VAL B 457 N PHE B 441
SHEET 4 AC1 4 ILE B 483 ALA B 488 -1 O LYS B 484 N THR B 458
SHEET 1 AC2 4 TRP B 505 ASN B 507 0
SHEET 2 AC2 4 LEU B 512 THR B 521 -1 O TYR B 514 N TRP B 505
SHEET 3 AC2 4 GLU B 524 SER B 531 -1 O TYR B 528 N PHE B 515
SHEET 4 AC2 4 VAL B 539 ARG B 540 -1 O VAL B 539 N VAL B 529
SHEET 1 AC3 4 SER B 547 MET B 552 0
SHEET 2 AC3 4 MET B 558 SER B 565 -1 O HIS B 562 N SER B 549
SHEET 3 AC3 4 THR B 568 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 PHE B 613 0
SHEET 2 AC4 8 LEU B 621 TYR B 626 -1 O LEU B 621 N PHE B 613
SHEET 3 AC4 8 ALA B 673 ILE B 677 -1 O VAL B 676 N MET B 624
SHEET 4 AC4 8 HIS B 637 PHE B 642 1 N VAL B 640 O ALA B 673
SHEET 5 AC4 8 ILE B 719 GLY B 728 1 O ALA B 725 N LEU B 641
SHEET 6 AC4 8 VAL B 749 GLY B 753 1 O GLY B 753 N GLY B 728
SHEET 7 AC4 8 LEU B 800 HIS B 804 1 O LEU B 801 N ALA B 750
SHEET 8 AC4 8 GLN B 831 ILE B 834 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 ALA C 155 -1 O LEU C 152 N ASP C 143
SHEET 3 AC6 4 SER C 158 ARG C 163 -1 O SER C 158 N ALA C 155
SHEET 4 AC6 4 LEU C 178 GLU C 179 -1 O LEU C 178 N HIS C 161
SHEET 1 AC7 4 MET C 189 ILE C 193 0
SHEET 2 AC7 4 PHE C 200 ILE C 204 -1 O ILE C 204 N MET C 189
SHEET 3 AC7 4 LEU C 209 ASN C 213 -1 O TRP C 210 N PHE C 203
SHEET 4 AC7 4 GLU C 219 ARG C 221 -1 O ARG C 220 N VAL C 211
SHEET 1 AC8 4 LYS C 237 ALA C 239 0
SHEET 2 AC8 4 LYS C 271 ASP C 281 -1 O VAL C 280 N SER C 238
SHEET 3 AC8 4 LYS C 314 THR C 324 -1 O THR C 324 N LYS C 271
SHEET 4 AC8 4 ILE C 330 THR C 333 -1 O SER C 332 N GLN C 323
SHEET 1 AC9 5 TYR C 256 TRP C 258 0
SHEET 2 AC9 5 LYS C 271 ASP C 281 -1 O LEU C 276 N TRP C 257
SHEET 3 AC9 5 LYS C 314 THR C 324 -1 O THR C 324 N LYS C 271
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 2 VAL C 287 PRO C 291 0
SHEET 2 AD1 2 THR C 300 ARG C 304 -1 O ASP C 301 N VAL C 290
SHEET 1 AD2 4 TYR C 351 TRP C 357 0
SHEET 2 AD2 4 ALA C 364 LEU C 369 -1 O TRP C 365 N GLY C 356
SHEET 3 AD2 4 TRP C 375 LEU C 381 -1 O LEU C 381 N ALA C 364
SHEET 4 AD2 4 TYR C 410 VAL C 416 -1 O GLU C 415 N LEU C 376
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 THR C 521 -1 O LEU C 512 N ASN C 507
SHEET 3 AD4 4 GLU C 524 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 565 -1 O HIS C 562 N SER C 549
SHEET 3 AD5 4 THR C 568 SER C 578 -1 O TYR C 575 N PHE C 559
SHEET 4 AD5 4 GLN C 588 MET C 596 -1 O ALA C 593 N VAL C 574
SHEET 1 AD6 8 GLU C 609 HIS C 614 0
SHEET 2 AD6 8 ARG C 620 TYR C 626 -1 O GLY C 623 N PHE C 611
SHEET 3 AD6 8 ALA C 673 ILE C 677 -1 O VAL C 676 N MET C 624
SHEET 4 AD6 8 HIS C 637 PHE C 642 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 ILE C 751 N ILE C 726
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 833 N ILE C 802
SHEET 1 AD7 4 HIS D 54 GLN D 60 0
SHEET 2 AD7 4 HIS D 68 GLY D 76 -1 O LEU D 75 N HIS D 54
SHEET 3 AD7 4 SER D 85 PRO D 92 -1 O SER D 85 N GLY D 76
SHEET 4 AD7 4 LYS D 106 GLN D 107 -1 O LYS D 106 N TYR D 88
SHEET 1 AD8 4 TYR D 142 HIS D 145 0
SHEET 2 AD8 4 LEU D 150 ALA D 155 -1 O LEU D 152 N ASP D 143
SHEET 3 AD8 4 SER D 158 ARG D 163 -1 O SER D 158 N ALA D 155
SHEET 4 AD8 4 LEU D 178 ILE D 180 -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 ILE D 204 N MET D 189
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 3 LYS D 237 ALA D 239 0
SHEET 2 AE1 3 LYS D 271 ASP D 281 -1 O VAL D 280 N SER D 238
SHEET 3 AE1 3 TYR D 256 TRP D 258 -1 N TRP D 257 O LEU D 276
SHEET 1 AE2 5 LYS D 237 ALA D 239 0
SHEET 2 AE2 5 LYS D 271 ASP D 281 -1 O VAL D 280 N SER D 238
SHEET 3 AE2 5 LYS D 314 THR D 324 -1 O THR D 324 N LYS D 271
SHEET 4 AE2 5 ILE D 330 LEU D 338 -1 O VAL D 331 N GLN D 323
SHEET 5 AE2 5 PHE D 386 PRO D 388 -1 O ILE D 387 N GLU D 337
SHEET 1 AE3 2 VAL D 287 PRO D 291 0
SHEET 2 AE3 2 THR D 300 ARG D 304 -1 O ASP D 301 N VAL D 290
SHEET 1 AE4 4 TYR D 351 TRP D 357 0
SHEET 2 AE4 4 ALA D 364 LEU D 369 -1 O TRP D 365 N GLY D 356
SHEET 3 AE4 4 TRP D 375 LEU D 381 -1 O LEU D 381 N ALA D 364
SHEET 4 AE4 4 TYR D 410 VAL D 416 -1 O VAL D 412 N LEU D 378
SHEET 1 AE5 4 PHE D 427 PRO D 429 0
SHEET 2 AE5 4 LEU D 439 ASN D 445 -1 O LEU D 442 N TYR D 428
SHEET 3 AE5 4 HIS D 453 ALA D 459 -1 O ALA D 459 N LEU D 439
SHEET 4 AE5 4 ILE D 483 ALA D 488 -1 O LYS D 484 N THR D 458
SHEET 1 AE6 4 TRP D 505 ASN D 507 0
SHEET 2 AE6 4 LEU D 512 THR D 521 -1 O TYR D 514 N TRP D 505
SHEET 3 AE6 4 GLU D 524 SER D 531 -1 O VAL D 530 N VAL D 513
SHEET 4 AE6 4 VAL D 539 ARG D 540 -1 O VAL D 539 N VAL D 529
SHEET 1 AE7 4 SER D 547 MET D 552 0
SHEET 2 AE7 4 MET D 558 SER D 564 -1 O HIS D 562 N SER D 549
SHEET 3 AE7 4 CYS D 571 SER D 578 -1 O TYR D 575 N PHE D 559
SHEET 4 AE7 4 GLN D 588 MET D 596 -1 O ALA D 593 N VAL D 574
SHEET 1 AE8 8 GLU D 609 HIS D 614 0
SHEET 2 AE8 8 ARG D 620 TYR D 626 -1 O LEU D 621 N PHE D 613
SHEET 3 AE8 8 ALA D 673 ILE D 677 -1 O VAL D 676 N MET D 624
SHEET 4 AE8 8 HIS D 637 PHE D 642 1 N VAL D 640 O ALA D 673
SHEET 5 AE8 8 ILE D 719 GLY D 728 1 O ALA D 725 N THR D 639
SHEET 6 AE8 8 PHE D 747 GLY D 753 1 O GLY D 753 N GLY D 728
SHEET 7 AE8 8 LEU D 800 GLY D 805 1 O LEU D 801 N ALA D 750
SHEET 8 AE8 8 GLN D 831 TYR D 835 1 O GLN D 833 N ILE D 802
CRYST1 119.516 117.219 163.401 90.00 105.72 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 0.008367 0.000000 0.002354 0.00000
SCALE2 0.000000 0.008531 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006358 0.00000
TER 6564 HIS A 865
TER 13105 LEU B 863
TER 19666 LEU C 863
TER 26252 LEU D 863
TER 26269 PRO E 233
TER 26286 PRO F 233
TER 26303 PRO G 233
TER 26320 PRO H 233
MASTER 680 0 0 75 186 0 0 626316 8 0 284
END
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