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HEADER HYDROLASE 19-DEC-19 6TRW
TITLE CRYSTAL STRUCTURE OF DPP8 IN COMPLEX WITH THE EIL PEPTIDE
TITLE 2 (SLRFLFEGQRIADNH)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 8;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: DP8,DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 1,DPRP-1,
COMPND 5 DIPEPTIDYL PEPTIDASE VIII,DPP VIII,PROLYL DIPEPTIDASE DPP8;
COMPND 6 EC: 3.4.14.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SER-LEU-ARG-PHE-LEU-PHE-GLU-GLY-GLN-ARG;
COMPND 10 CHAIN: D, E, F;
COMPND 11 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: DPP8, DPRP1, MSTP097, MSTP135, MSTP141;
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 EIL PEPTIDE, DPP8, SUMO1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.ROSS,R.HUBER
REVDAT 1 13-JAN-21 6TRW 0
JRNL AUTH B.ROSS,R.HUBER
JRNL TITL THE AEROSOL-GENERATOR: DIRECT SOAKING OF NAKED PROTEIN
JRNL TITL 2 CRYSTALS FOR PROTEIN-LIGAND COMPLEXATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
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) : 49.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 99257
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5225
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) : 7243
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE SET COUNT : 382
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20694
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 33
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 77.09
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 91.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.07000
REMARK 3 B22 (A**2) : 4.85000
REMARK 3 B33 (A**2) : -2.78000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.658
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.316
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.262
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.252
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 21260 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 19798 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 28818 ; 1.133 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 45639 ; 0.849 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2528 ; 5.946 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1047 ;33.676 ;23.352
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3585 ;13.986 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 150 ;13.949 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3052 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 23857 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5091 ; 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 6TRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292104682.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-FEB-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.75
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) : 0.99989
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104482
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 49.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.427
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.4100
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) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.53
REMARK 200 R MERGE FOR SHELL (I) : 1.27100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.990
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: 6EOO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.46 M NA CITRATE PH 6.75, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 130.71950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 130.71950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 81.52250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 122.64150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 81.52250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 122.64150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 130.71950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 81.52250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 122.64150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 130.71950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 81.52250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 122.64150
REMARK 290 SMTRY3 8 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: 8810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 65230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 522.87800
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: 8640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 64550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 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 GLY A -4
REMARK 465 ALA A -3
REMARK 465 MET A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 TRP A 2
REMARK 465 LYS A 3
REMARK 465 ARG A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 GLN A 7
REMARK 465 MET A 8
REMARK 465 LYS A 9
REMARK 465 ILE A 10
REMARK 465 LYS A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 CYS A 15
REMARK 465 ASN A 16
REMARK 465 MET A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 19
REMARK 465 ALA A 20
REMARK 465 MET A 21
REMARK 465 GLU A 22
REMARK 465 THR A 23
REMARK 465 GLU A 24
REMARK 465 GLN A 25
REMARK 465 LEU A 26
REMARK 465 GLY A 27
REMARK 465 VAL A 28
REMARK 465 GLU A 29
REMARK 465 ILE A 30
REMARK 465 PHE A 31
REMARK 465 GLU A 32
REMARK 465 THR A 33
REMARK 465 ALA A 34
REMARK 465 ASP A 35
REMARK 465 CYS A 36
REMARK 465 GLU A 37
REMARK 465 GLU A 38
REMARK 465 ASN A 39
REMARK 465 ILE A 40
REMARK 465 GLU A 41
REMARK 465 SER A 42
REMARK 465 GLN A 43
REMARK 465 ASP A 44
REMARK 465 ARG A 45
REMARK 465 PRO A 46
REMARK 465 LYS A 47
REMARK 465 GLY A 106
REMARK 465 GLU A 107
REMARK 465 ASN A 108
REMARK 465 GLN A 140
REMARK 465 ALA A 141
REMARK 465 THR A 142
REMARK 465 LEU A 143
REMARK 465 ASP A 144
REMARK 465 TYR A 145
REMARK 465 GLY A 146
REMARK 465 MET A 147
REMARK 465 ILE A 898
REMARK 465 GLY B -4
REMARK 465 ALA B -3
REMARK 465 MET B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 TRP B 2
REMARK 465 LYS B 3
REMARK 465 ARG B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 465 GLN B 7
REMARK 465 MET B 8
REMARK 465 LYS B 9
REMARK 465 ILE B 10
REMARK 465 LYS B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 LYS B 14
REMARK 465 CYS B 15
REMARK 465 ASN B 16
REMARK 465 MET B 17
REMARK 465 ALA B 18
REMARK 465 ALA B 19
REMARK 465 ALA B 20
REMARK 465 MET B 21
REMARK 465 GLU B 22
REMARK 465 THR B 23
REMARK 465 GLU B 24
REMARK 465 GLN B 25
REMARK 465 LEU B 26
REMARK 465 GLY B 27
REMARK 465 VAL B 28
REMARK 465 GLU B 29
REMARK 465 ILE B 30
REMARK 465 PHE B 31
REMARK 465 GLU B 32
REMARK 465 THR B 33
REMARK 465 ALA B 34
REMARK 465 ASP B 35
REMARK 465 CYS B 36
REMARK 465 GLU B 37
REMARK 465 GLU B 38
REMARK 465 ASN B 39
REMARK 465 ILE B 40
REMARK 465 GLU B 41
REMARK 465 SER B 42
REMARK 465 GLN B 43
REMARK 465 ASP B 44
REMARK 465 ARG B 45
REMARK 465 PRO B 46
REMARK 465 LYS B 47
REMARK 465 GLY B 73
REMARK 465 TYR B 74
REMARK 465 MET B 75
REMARK 465 MET B 76
REMARK 465 GLY B 106
REMARK 465 GLU B 107
REMARK 465 ASN B 108
REMARK 465 PHE B 139
REMARK 465 GLN B 140
REMARK 465 ALA B 141
REMARK 465 THR B 142
REMARK 465 LEU B 143
REMARK 465 ASP B 144
REMARK 465 TYR B 145
REMARK 465 GLY B 146
REMARK 465 MET B 147
REMARK 465 ILE B 898
REMARK 465 GLY C -4
REMARK 465 ALA C -3
REMARK 465 MET C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 TRP C 2
REMARK 465 LYS C 3
REMARK 465 ARG C 4
REMARK 465 SER C 5
REMARK 465 GLU C 6
REMARK 465 GLN C 7
REMARK 465 MET C 8
REMARK 465 LYS C 9
REMARK 465 ILE C 10
REMARK 465 LYS C 11
REMARK 465 SER C 12
REMARK 465 GLY C 13
REMARK 465 LYS C 14
REMARK 465 CYS C 15
REMARK 465 ASN C 16
REMARK 465 MET C 17
REMARK 465 ALA C 18
REMARK 465 ALA C 19
REMARK 465 ALA C 20
REMARK 465 MET C 21
REMARK 465 GLU C 22
REMARK 465 THR C 23
REMARK 465 GLU C 24
REMARK 465 GLN C 25
REMARK 465 LEU C 26
REMARK 465 GLY C 27
REMARK 465 VAL C 28
REMARK 465 GLU C 29
REMARK 465 ILE C 30
REMARK 465 PHE C 31
REMARK 465 GLU C 32
REMARK 465 THR C 33
REMARK 465 ALA C 34
REMARK 465 ASP C 35
REMARK 465 CYS C 36
REMARK 465 GLU C 37
REMARK 465 GLU C 38
REMARK 465 ASN C 39
REMARK 465 ILE C 40
REMARK 465 GLU C 41
REMARK 465 SER C 42
REMARK 465 GLN C 43
REMARK 465 ASP C 44
REMARK 465 ARG C 45
REMARK 465 PRO C 46
REMARK 465 LYS C 47
REMARK 465 GLY C 106
REMARK 465 GLU C 107
REMARK 465 ASN C 108
REMARK 465 PHE C 139
REMARK 465 GLN C 140
REMARK 465 ALA C 141
REMARK 465 THR C 142
REMARK 465 LEU C 143
REMARK 465 ASP C 144
REMARK 465 TYR C 145
REMARK 465 GLY C 146
REMARK 465 MET C 147
REMARK 465 ILE C 898
REMARK 465 ILE D 11
REMARK 465 ALA D 12
REMARK 465 ASP D 13
REMARK 465 ASN D 14
REMARK 465 HIS D 15
REMARK 465 ILE E 11
REMARK 465 ALA E 12
REMARK 465 ASP E 13
REMARK 465 ASN E 14
REMARK 465 HIS E 15
REMARK 465 ILE F 11
REMARK 465 ALA F 12
REMARK 465 ASP F 13
REMARK 465 ASN F 14
REMARK 465 HIS F 15
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 ARG A 325 -167.57 -117.85
REMARK 500 PHE A 372 61.97 -108.36
REMARK 500 ILE A 445 -88.36 -93.75
REMARK 500 PHE A 453 102.04 -167.08
REMARK 500 GLU A 462 40.39 -101.06
REMARK 500 ASN A 528 -155.40 -156.11
REMARK 500 SER A 546 146.82 -172.36
REMARK 500 VAL A 558 -61.25 -101.24
REMARK 500 PRO A 594 171.84 -52.31
REMARK 500 TYR A 669 -66.48 -127.54
REMARK 500 VAL A 684 -69.73 -90.81
REMARK 500 TYR A 686 43.27 -106.10
REMARK 500 TYR A 720 -4.39 68.91
REMARK 500 SER A 755 -107.11 65.22
REMARK 500 LEU A 783 105.99 -164.36
REMARK 500 ASN A 802 55.34 -157.69
REMARK 500 SER A 820 33.22 -96.75
REMARK 500 ARG A 864 -140.45 -101.30
REMARK 500 LEU A 888 -63.64 -145.46
REMARK 500 SER B 233 55.86 38.45
REMARK 500 ASP B 418 105.76 -52.86
REMARK 500 ILE B 445 -88.29 -97.15
REMARK 500 PHE B 453 114.97 -170.99
REMARK 500 GLU B 518 55.42 -90.48
REMARK 500 VAL B 558 -61.18 -91.76
REMARK 500 ASP B 655 72.48 64.07
REMARK 500 TYR B 669 -75.50 -115.99
REMARK 500 TYR B 686 44.92 -102.78
REMARK 500 TYR B 720 -0.46 62.78
REMARK 500 SER B 755 -111.08 65.13
REMARK 500 ARG B 768 57.11 -119.89
REMARK 500 LEU B 783 104.68 -164.38
REMARK 500 ASN B 802 56.46 -160.90
REMARK 500 ARG B 864 -137.18 -98.06
REMARK 500 LEU B 888 -66.64 -141.88
REMARK 500 MET C 76 -4.01 96.67
REMARK 500 PRO C 293 48.14 -75.64
REMARK 500 SER C 294 32.76 -156.44
REMARK 500 PRO C 332 88.52 -69.04
REMARK 500 ILE C 445 -87.46 -105.87
REMARK 500 PHE C 453 112.14 -165.24
REMARK 500 SER C 494 44.61 -88.48
REMARK 500 GLU C 511 76.87 -153.77
REMARK 500 GLU C 518 55.27 -93.38
REMARK 500 PRO C 626 118.05 -34.02
REMARK 500 TYR C 669 -74.32 -118.96
REMARK 500 TYR C 686 47.01 -108.30
REMARK 500 ARG C 748 73.33 -113.00
REMARK 500 SER C 755 -113.74 62.99
REMARK 500 LEU C 783 94.44 -161.21
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 901 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 158 O
REMARK 620 2 GLN A 274 O 87.3
REMARK 620 3 ASP A 278 OD1 135.3 90.7
REMARK 620 4 TYR A 280 OH 71.4 80.1 64.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 901 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 158 O
REMARK 620 2 GLN B 274 O 87.4
REMARK 620 3 ASP B 278 OD1 154.9 86.5
REMARK 620 4 TYR B 280 OH 74.0 80.1 81.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 901 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG C 158 O
REMARK 620 2 GLN C 274 O 94.2
REMARK 620 3 ASP C 278 OD1 143.1 79.9
REMARK 620 4 TYR C 280 OH 75.6 73.6 67.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 901
DBREF 6TRW A 1 898 UNP Q6V1X1 DPP8_HUMAN 1 898
DBREF 6TRW B 1 898 UNP Q6V1X1 DPP8_HUMAN 1 898
DBREF 6TRW C 1 898 UNP Q6V1X1 DPP8_HUMAN 1 898
DBREF 6TRW D 1 15 PDB 6TRW 6TRW 1 15
DBREF 6TRW E 1 15 PDB 6TRW 6TRW 1 15
DBREF 6TRW F 1 15 PDB 6TRW 6TRW 1 15
SEQADV 6TRW GLY A -4 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW ALA A -3 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW MET A -2 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW GLY A -1 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW SER A 0 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW GLY B -4 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW ALA B -3 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW MET B -2 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW GLY B -1 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW SER B 0 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW GLY C -4 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW ALA C -3 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW MET C -2 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW GLY C -1 UNP Q6V1X1 EXPRESSION TAG
SEQADV 6TRW SER C 0 UNP Q6V1X1 EXPRESSION TAG
SEQRES 1 A 903 GLY ALA MET GLY SER MET TRP LYS ARG SER GLU GLN MET
SEQRES 2 A 903 LYS ILE LYS SER GLY LYS CYS ASN MET ALA ALA ALA MET
SEQRES 3 A 903 GLU THR GLU GLN LEU GLY VAL GLU ILE PHE GLU THR ALA
SEQRES 4 A 903 ASP CYS GLU GLU ASN ILE GLU SER GLN ASP ARG PRO LYS
SEQRES 5 A 903 LEU GLU PRO PHE TYR VAL GLU ARG TYR SER TRP SER GLN
SEQRES 6 A 903 LEU LYS LYS LEU LEU ALA ASP THR ARG LYS TYR HIS GLY
SEQRES 7 A 903 TYR MET MET ALA LYS ALA PRO HIS ASP PHE MET PHE VAL
SEQRES 8 A 903 LYS ARG ASN ASP PRO ASP GLY PRO HIS SER ASP ARG ILE
SEQRES 9 A 903 TYR TYR LEU ALA MET SER GLY GLU ASN ARG GLU ASN THR
SEQRES 10 A 903 LEU PHE TYR SER GLU ILE PRO LYS THR ILE ASN ARG ALA
SEQRES 11 A 903 ALA VAL LEU MET LEU SER TRP LYS PRO LEU LEU ASP LEU
SEQRES 12 A 903 PHE GLN ALA THR LEU ASP TYR GLY MET TYR SER ARG GLU
SEQRES 13 A 903 GLU GLU LEU LEU ARG GLU ARG LYS ARG ILE GLY THR VAL
SEQRES 14 A 903 GLY ILE ALA SER TYR ASP TYR HIS GLN GLY SER GLY THR
SEQRES 15 A 903 PHE LEU PHE GLN ALA GLY SER GLY ILE TYR HIS VAL LYS
SEQRES 16 A 903 ASP GLY GLY PRO GLN GLY PHE THR GLN GLN PRO LEU ARG
SEQRES 17 A 903 PRO ASN LEU VAL GLU THR SER CYS PRO ASN ILE ARG MET
SEQRES 18 A 903 ASP PRO LYS LEU CYS PRO ALA ASP PRO ASP TRP ILE ALA
SEQRES 19 A 903 PHE ILE HIS SER ASN ASP ILE TRP ILE SER ASN ILE VAL
SEQRES 20 A 903 THR ARG GLU GLU ARG ARG LEU THR TYR VAL HIS ASN GLU
SEQRES 21 A 903 LEU ALA ASN MET GLU GLU ASP ALA ARG SER ALA GLY VAL
SEQRES 22 A 903 ALA THR PHE VAL LEU GLN GLU GLU PHE ASP ARG TYR SER
SEQRES 23 A 903 GLY TYR TRP TRP CYS PRO LYS ALA GLU THR THR PRO SER
SEQRES 24 A 903 GLY GLY LYS ILE LEU ARG ILE LEU TYR GLU GLU ASN ASP
SEQRES 25 A 903 GLU SER GLU VAL GLU ILE ILE HIS VAL THR SER PRO MET
SEQRES 26 A 903 LEU GLU THR ARG ARG ALA ASP SER PHE ARG TYR PRO LYS
SEQRES 27 A 903 THR GLY THR ALA ASN PRO LYS VAL THR PHE LYS MET SER
SEQRES 28 A 903 GLU ILE MET ILE ASP ALA GLU GLY ARG ILE ILE ASP VAL
SEQRES 29 A 903 ILE ASP LYS GLU LEU ILE GLN PRO PHE GLU ILE LEU PHE
SEQRES 30 A 903 GLU GLY VAL GLU TYR ILE ALA ARG ALA GLY TRP THR PRO
SEQRES 31 A 903 GLU GLY LYS TYR ALA TRP SER ILE LEU LEU ASP ARG SER
SEQRES 32 A 903 GLN THR ARG LEU GLN ILE VAL LEU ILE SER PRO GLU LEU
SEQRES 33 A 903 PHE ILE PRO VAL GLU ASP ASP VAL MET GLU ARG GLN ARG
SEQRES 34 A 903 LEU ILE GLU SER VAL PRO ASP SER VAL THR PRO LEU ILE
SEQRES 35 A 903 ILE TYR GLU GLU THR THR ASP ILE TRP ILE ASN ILE HIS
SEQRES 36 A 903 ASP ILE PHE HIS VAL PHE PRO GLN SER HIS GLU GLU GLU
SEQRES 37 A 903 ILE GLU PHE ILE PHE ALA SER GLU CYS LYS THR GLY PHE
SEQRES 38 A 903 ARG HIS LEU TYR LYS ILE THR SER ILE LEU LYS GLU SER
SEQRES 39 A 903 LYS TYR LYS ARG SER SER GLY GLY LEU PRO ALA PRO SER
SEQRES 40 A 903 ASP PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA ILE THR
SEQRES 41 A 903 SER GLY GLU TRP GLU VAL LEU GLY ARG HIS GLY SER ASN
SEQRES 42 A 903 ILE GLN VAL ASP GLU VAL ARG ARG LEU VAL TYR PHE GLU
SEQRES 43 A 903 GLY THR LYS ASP SER PRO LEU GLU HIS HIS LEU TYR VAL
SEQRES 44 A 903 VAL SER TYR VAL ASN PRO GLY GLU VAL THR ARG LEU THR
SEQRES 45 A 903 ASP ARG GLY TYR SER HIS SER CYS CYS ILE SER GLN HIS
SEQRES 46 A 903 CYS ASP PHE PHE ILE SER LYS TYR SER ASN GLN LYS ASN
SEQRES 47 A 903 PRO HIS CYS VAL SER LEU TYR LYS LEU SER SER PRO GLU
SEQRES 48 A 903 ASP ASP PRO THR CYS LYS THR LYS GLU PHE TRP ALA THR
SEQRES 49 A 903 ILE LEU ASP SER ALA GLY PRO LEU PRO ASP TYR THR PRO
SEQRES 50 A 903 PRO GLU ILE PHE SER PHE GLU SER THR THR GLY PHE THR
SEQRES 51 A 903 LEU TYR GLY MET LEU TYR LYS PRO HIS ASP LEU GLN PRO
SEQRES 52 A 903 GLY LYS LYS TYR PRO THR VAL LEU PHE ILE TYR GLY GLY
SEQRES 53 A 903 PRO GLN VAL GLN LEU VAL ASN ASN ARG PHE LYS GLY VAL
SEQRES 54 A 903 LYS TYR PHE ARG LEU ASN THR LEU ALA SER LEU GLY TYR
SEQRES 55 A 903 VAL VAL VAL VAL ILE ASP ASN ARG GLY SER CYS HIS ARG
SEQRES 56 A 903 GLY LEU LYS PHE GLU GLY ALA PHE LYS TYR LYS MET GLY
SEQRES 57 A 903 GLN ILE GLU ILE ASP ASP GLN VAL GLU GLY LEU GLN TYR
SEQRES 58 A 903 LEU ALA SER ARG TYR ASP PHE ILE ASP LEU ASP ARG VAL
SEQRES 59 A 903 GLY ILE HIS GLY TRP SER TYR GLY GLY TYR LEU SER LEU
SEQRES 60 A 903 MET ALA LEU MET GLN ARG SER ASP ILE PHE ARG VAL ALA
SEQRES 61 A 903 ILE ALA GLY ALA PRO VAL THR LEU TRP ILE PHE TYR ASP
SEQRES 62 A 903 THR GLY TYR THR GLU ARG TYR MET GLY HIS PRO ASP GLN
SEQRES 63 A 903 ASN GLU GLN GLY TYR TYR LEU GLY SER VAL ALA MET GLN
SEQRES 64 A 903 ALA GLU LYS PHE PRO SER GLU PRO ASN ARG LEU LEU LEU
SEQRES 65 A 903 LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE ALA HIS
SEQRES 66 A 903 THR SER ILE LEU LEU SER PHE LEU VAL ARG ALA GLY LYS
SEQRES 67 A 903 PRO TYR ASP LEU GLN ILE TYR PRO GLN GLU ARG HIS SER
SEQRES 68 A 903 ILE ARG VAL PRO GLU SER GLY GLU HIS TYR GLU LEU HIS
SEQRES 69 A 903 LEU LEU HIS TYR LEU GLN GLU ASN LEU GLY SER ARG ILE
SEQRES 70 A 903 ALA ALA LEU LYS VAL ILE
SEQRES 1 B 903 GLY ALA MET GLY SER MET TRP LYS ARG SER GLU GLN MET
SEQRES 2 B 903 LYS ILE LYS SER GLY LYS CYS ASN MET ALA ALA ALA MET
SEQRES 3 B 903 GLU THR GLU GLN LEU GLY VAL GLU ILE PHE GLU THR ALA
SEQRES 4 B 903 ASP CYS GLU GLU ASN ILE GLU SER GLN ASP ARG PRO LYS
SEQRES 5 B 903 LEU GLU PRO PHE TYR VAL GLU ARG TYR SER TRP SER GLN
SEQRES 6 B 903 LEU LYS LYS LEU LEU ALA ASP THR ARG LYS TYR HIS GLY
SEQRES 7 B 903 TYR MET MET ALA LYS ALA PRO HIS ASP PHE MET PHE VAL
SEQRES 8 B 903 LYS ARG ASN ASP PRO ASP GLY PRO HIS SER ASP ARG ILE
SEQRES 9 B 903 TYR TYR LEU ALA MET SER GLY GLU ASN ARG GLU ASN THR
SEQRES 10 B 903 LEU PHE TYR SER GLU ILE PRO LYS THR ILE ASN ARG ALA
SEQRES 11 B 903 ALA VAL LEU MET LEU SER TRP LYS PRO LEU LEU ASP LEU
SEQRES 12 B 903 PHE GLN ALA THR LEU ASP TYR GLY MET TYR SER ARG GLU
SEQRES 13 B 903 GLU GLU LEU LEU ARG GLU ARG LYS ARG ILE GLY THR VAL
SEQRES 14 B 903 GLY ILE ALA SER TYR ASP TYR HIS GLN GLY SER GLY THR
SEQRES 15 B 903 PHE LEU PHE GLN ALA GLY SER GLY ILE TYR HIS VAL LYS
SEQRES 16 B 903 ASP GLY GLY PRO GLN GLY PHE THR GLN GLN PRO LEU ARG
SEQRES 17 B 903 PRO ASN LEU VAL GLU THR SER CYS PRO ASN ILE ARG MET
SEQRES 18 B 903 ASP PRO LYS LEU CYS PRO ALA ASP PRO ASP TRP ILE ALA
SEQRES 19 B 903 PHE ILE HIS SER ASN ASP ILE TRP ILE SER ASN ILE VAL
SEQRES 20 B 903 THR ARG GLU GLU ARG ARG LEU THR TYR VAL HIS ASN GLU
SEQRES 21 B 903 LEU ALA ASN MET GLU GLU ASP ALA ARG SER ALA GLY VAL
SEQRES 22 B 903 ALA THR PHE VAL LEU GLN GLU GLU PHE ASP ARG TYR SER
SEQRES 23 B 903 GLY TYR TRP TRP CYS PRO LYS ALA GLU THR THR PRO SER
SEQRES 24 B 903 GLY GLY LYS ILE LEU ARG ILE LEU TYR GLU GLU ASN ASP
SEQRES 25 B 903 GLU SER GLU VAL GLU ILE ILE HIS VAL THR SER PRO MET
SEQRES 26 B 903 LEU GLU THR ARG ARG ALA ASP SER PHE ARG TYR PRO LYS
SEQRES 27 B 903 THR GLY THR ALA ASN PRO LYS VAL THR PHE LYS MET SER
SEQRES 28 B 903 GLU ILE MET ILE ASP ALA GLU GLY ARG ILE ILE ASP VAL
SEQRES 29 B 903 ILE ASP LYS GLU LEU ILE GLN PRO PHE GLU ILE LEU PHE
SEQRES 30 B 903 GLU GLY VAL GLU TYR ILE ALA ARG ALA GLY TRP THR PRO
SEQRES 31 B 903 GLU GLY LYS TYR ALA TRP SER ILE LEU LEU ASP ARG SER
SEQRES 32 B 903 GLN THR ARG LEU GLN ILE VAL LEU ILE SER PRO GLU LEU
SEQRES 33 B 903 PHE ILE PRO VAL GLU ASP ASP VAL MET GLU ARG GLN ARG
SEQRES 34 B 903 LEU ILE GLU SER VAL PRO ASP SER VAL THR PRO LEU ILE
SEQRES 35 B 903 ILE TYR GLU GLU THR THR ASP ILE TRP ILE ASN ILE HIS
SEQRES 36 B 903 ASP ILE PHE HIS VAL PHE PRO GLN SER HIS GLU GLU GLU
SEQRES 37 B 903 ILE GLU PHE ILE PHE ALA SER GLU CYS LYS THR GLY PHE
SEQRES 38 B 903 ARG HIS LEU TYR LYS ILE THR SER ILE LEU LYS GLU SER
SEQRES 39 B 903 LYS TYR LYS ARG SER SER GLY GLY LEU PRO ALA PRO SER
SEQRES 40 B 903 ASP PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA ILE THR
SEQRES 41 B 903 SER GLY GLU TRP GLU VAL LEU GLY ARG HIS GLY SER ASN
SEQRES 42 B 903 ILE GLN VAL ASP GLU VAL ARG ARG LEU VAL TYR PHE GLU
SEQRES 43 B 903 GLY THR LYS ASP SER PRO LEU GLU HIS HIS LEU TYR VAL
SEQRES 44 B 903 VAL SER TYR VAL ASN PRO GLY GLU VAL THR ARG LEU THR
SEQRES 45 B 903 ASP ARG GLY TYR SER HIS SER CYS CYS ILE SER GLN HIS
SEQRES 46 B 903 CYS ASP PHE PHE ILE SER LYS TYR SER ASN GLN LYS ASN
SEQRES 47 B 903 PRO HIS CYS VAL SER LEU TYR LYS LEU SER SER PRO GLU
SEQRES 48 B 903 ASP ASP PRO THR CYS LYS THR LYS GLU PHE TRP ALA THR
SEQRES 49 B 903 ILE LEU ASP SER ALA GLY PRO LEU PRO ASP TYR THR PRO
SEQRES 50 B 903 PRO GLU ILE PHE SER PHE GLU SER THR THR GLY PHE THR
SEQRES 51 B 903 LEU TYR GLY MET LEU TYR LYS PRO HIS ASP LEU GLN PRO
SEQRES 52 B 903 GLY LYS LYS TYR PRO THR VAL LEU PHE ILE TYR GLY GLY
SEQRES 53 B 903 PRO GLN VAL GLN LEU VAL ASN ASN ARG PHE LYS GLY VAL
SEQRES 54 B 903 LYS TYR PHE ARG LEU ASN THR LEU ALA SER LEU GLY TYR
SEQRES 55 B 903 VAL VAL VAL VAL ILE ASP ASN ARG GLY SER CYS HIS ARG
SEQRES 56 B 903 GLY LEU LYS PHE GLU GLY ALA PHE LYS TYR LYS MET GLY
SEQRES 57 B 903 GLN ILE GLU ILE ASP ASP GLN VAL GLU GLY LEU GLN TYR
SEQRES 58 B 903 LEU ALA SER ARG TYR ASP PHE ILE ASP LEU ASP ARG VAL
SEQRES 59 B 903 GLY ILE HIS GLY TRP SER TYR GLY GLY TYR LEU SER LEU
SEQRES 60 B 903 MET ALA LEU MET GLN ARG SER ASP ILE PHE ARG VAL ALA
SEQRES 61 B 903 ILE ALA GLY ALA PRO VAL THR LEU TRP ILE PHE TYR ASP
SEQRES 62 B 903 THR GLY TYR THR GLU ARG TYR MET GLY HIS PRO ASP GLN
SEQRES 63 B 903 ASN GLU GLN GLY TYR TYR LEU GLY SER VAL ALA MET GLN
SEQRES 64 B 903 ALA GLU LYS PHE PRO SER GLU PRO ASN ARG LEU LEU LEU
SEQRES 65 B 903 LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE ALA HIS
SEQRES 66 B 903 THR SER ILE LEU LEU SER PHE LEU VAL ARG ALA GLY LYS
SEQRES 67 B 903 PRO TYR ASP LEU GLN ILE TYR PRO GLN GLU ARG HIS SER
SEQRES 68 B 903 ILE ARG VAL PRO GLU SER GLY GLU HIS TYR GLU LEU HIS
SEQRES 69 B 903 LEU LEU HIS TYR LEU GLN GLU ASN LEU GLY SER ARG ILE
SEQRES 70 B 903 ALA ALA LEU LYS VAL ILE
SEQRES 1 C 903 GLY ALA MET GLY SER MET TRP LYS ARG SER GLU GLN MET
SEQRES 2 C 903 LYS ILE LYS SER GLY LYS CYS ASN MET ALA ALA ALA MET
SEQRES 3 C 903 GLU THR GLU GLN LEU GLY VAL GLU ILE PHE GLU THR ALA
SEQRES 4 C 903 ASP CYS GLU GLU ASN ILE GLU SER GLN ASP ARG PRO LYS
SEQRES 5 C 903 LEU GLU PRO PHE TYR VAL GLU ARG TYR SER TRP SER GLN
SEQRES 6 C 903 LEU LYS LYS LEU LEU ALA ASP THR ARG LYS TYR HIS GLY
SEQRES 7 C 903 TYR MET MET ALA LYS ALA PRO HIS ASP PHE MET PHE VAL
SEQRES 8 C 903 LYS ARG ASN ASP PRO ASP GLY PRO HIS SER ASP ARG ILE
SEQRES 9 C 903 TYR TYR LEU ALA MET SER GLY GLU ASN ARG GLU ASN THR
SEQRES 10 C 903 LEU PHE TYR SER GLU ILE PRO LYS THR ILE ASN ARG ALA
SEQRES 11 C 903 ALA VAL LEU MET LEU SER TRP LYS PRO LEU LEU ASP LEU
SEQRES 12 C 903 PHE GLN ALA THR LEU ASP TYR GLY MET TYR SER ARG GLU
SEQRES 13 C 903 GLU GLU LEU LEU ARG GLU ARG LYS ARG ILE GLY THR VAL
SEQRES 14 C 903 GLY ILE ALA SER TYR ASP TYR HIS GLN GLY SER GLY THR
SEQRES 15 C 903 PHE LEU PHE GLN ALA GLY SER GLY ILE TYR HIS VAL LYS
SEQRES 16 C 903 ASP GLY GLY PRO GLN GLY PHE THR GLN GLN PRO LEU ARG
SEQRES 17 C 903 PRO ASN LEU VAL GLU THR SER CYS PRO ASN ILE ARG MET
SEQRES 18 C 903 ASP PRO LYS LEU CYS PRO ALA ASP PRO ASP TRP ILE ALA
SEQRES 19 C 903 PHE ILE HIS SER ASN ASP ILE TRP ILE SER ASN ILE VAL
SEQRES 20 C 903 THR ARG GLU GLU ARG ARG LEU THR TYR VAL HIS ASN GLU
SEQRES 21 C 903 LEU ALA ASN MET GLU GLU ASP ALA ARG SER ALA GLY VAL
SEQRES 22 C 903 ALA THR PHE VAL LEU GLN GLU GLU PHE ASP ARG TYR SER
SEQRES 23 C 903 GLY TYR TRP TRP CYS PRO LYS ALA GLU THR THR PRO SER
SEQRES 24 C 903 GLY GLY LYS ILE LEU ARG ILE LEU TYR GLU GLU ASN ASP
SEQRES 25 C 903 GLU SER GLU VAL GLU ILE ILE HIS VAL THR SER PRO MET
SEQRES 26 C 903 LEU GLU THR ARG ARG ALA ASP SER PHE ARG TYR PRO LYS
SEQRES 27 C 903 THR GLY THR ALA ASN PRO LYS VAL THR PHE LYS MET SER
SEQRES 28 C 903 GLU ILE MET ILE ASP ALA GLU GLY ARG ILE ILE ASP VAL
SEQRES 29 C 903 ILE ASP LYS GLU LEU ILE GLN PRO PHE GLU ILE LEU PHE
SEQRES 30 C 903 GLU GLY VAL GLU TYR ILE ALA ARG ALA GLY TRP THR PRO
SEQRES 31 C 903 GLU GLY LYS TYR ALA TRP SER ILE LEU LEU ASP ARG SER
SEQRES 32 C 903 GLN THR ARG LEU GLN ILE VAL LEU ILE SER PRO GLU LEU
SEQRES 33 C 903 PHE ILE PRO VAL GLU ASP ASP VAL MET GLU ARG GLN ARG
SEQRES 34 C 903 LEU ILE GLU SER VAL PRO ASP SER VAL THR PRO LEU ILE
SEQRES 35 C 903 ILE TYR GLU GLU THR THR ASP ILE TRP ILE ASN ILE HIS
SEQRES 36 C 903 ASP ILE PHE HIS VAL PHE PRO GLN SER HIS GLU GLU GLU
SEQRES 37 C 903 ILE GLU PHE ILE PHE ALA SER GLU CYS LYS THR GLY PHE
SEQRES 38 C 903 ARG HIS LEU TYR LYS ILE THR SER ILE LEU LYS GLU SER
SEQRES 39 C 903 LYS TYR LYS ARG SER SER GLY GLY LEU PRO ALA PRO SER
SEQRES 40 C 903 ASP PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA ILE THR
SEQRES 41 C 903 SER GLY GLU TRP GLU VAL LEU GLY ARG HIS GLY SER ASN
SEQRES 42 C 903 ILE GLN VAL ASP GLU VAL ARG ARG LEU VAL TYR PHE GLU
SEQRES 43 C 903 GLY THR LYS ASP SER PRO LEU GLU HIS HIS LEU TYR VAL
SEQRES 44 C 903 VAL SER TYR VAL ASN PRO GLY GLU VAL THR ARG LEU THR
SEQRES 45 C 903 ASP ARG GLY TYR SER HIS SER CYS CYS ILE SER GLN HIS
SEQRES 46 C 903 CYS ASP PHE PHE ILE SER LYS TYR SER ASN GLN LYS ASN
SEQRES 47 C 903 PRO HIS CYS VAL SER LEU TYR LYS LEU SER SER PRO GLU
SEQRES 48 C 903 ASP ASP PRO THR CYS LYS THR LYS GLU PHE TRP ALA THR
SEQRES 49 C 903 ILE LEU ASP SER ALA GLY PRO LEU PRO ASP TYR THR PRO
SEQRES 50 C 903 PRO GLU ILE PHE SER PHE GLU SER THR THR GLY PHE THR
SEQRES 51 C 903 LEU TYR GLY MET LEU TYR LYS PRO HIS ASP LEU GLN PRO
SEQRES 52 C 903 GLY LYS LYS TYR PRO THR VAL LEU PHE ILE TYR GLY GLY
SEQRES 53 C 903 PRO GLN VAL GLN LEU VAL ASN ASN ARG PHE LYS GLY VAL
SEQRES 54 C 903 LYS TYR PHE ARG LEU ASN THR LEU ALA SER LEU GLY TYR
SEQRES 55 C 903 VAL VAL VAL VAL ILE ASP ASN ARG GLY SER CYS HIS ARG
SEQRES 56 C 903 GLY LEU LYS PHE GLU GLY ALA PHE LYS TYR LYS MET GLY
SEQRES 57 C 903 GLN ILE GLU ILE ASP ASP GLN VAL GLU GLY LEU GLN TYR
SEQRES 58 C 903 LEU ALA SER ARG TYR ASP PHE ILE ASP LEU ASP ARG VAL
SEQRES 59 C 903 GLY ILE HIS GLY TRP SER TYR GLY GLY TYR LEU SER LEU
SEQRES 60 C 903 MET ALA LEU MET GLN ARG SER ASP ILE PHE ARG VAL ALA
SEQRES 61 C 903 ILE ALA GLY ALA PRO VAL THR LEU TRP ILE PHE TYR ASP
SEQRES 62 C 903 THR GLY TYR THR GLU ARG TYR MET GLY HIS PRO ASP GLN
SEQRES 63 C 903 ASN GLU GLN GLY TYR TYR LEU GLY SER VAL ALA MET GLN
SEQRES 64 C 903 ALA GLU LYS PHE PRO SER GLU PRO ASN ARG LEU LEU LEU
SEQRES 65 C 903 LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE ALA HIS
SEQRES 66 C 903 THR SER ILE LEU LEU SER PHE LEU VAL ARG ALA GLY LYS
SEQRES 67 C 903 PRO TYR ASP LEU GLN ILE TYR PRO GLN GLU ARG HIS SER
SEQRES 68 C 903 ILE ARG VAL PRO GLU SER GLY GLU HIS TYR GLU LEU HIS
SEQRES 69 C 903 LEU LEU HIS TYR LEU GLN GLU ASN LEU GLY SER ARG ILE
SEQRES 70 C 903 ALA ALA LEU LYS VAL ILE
SEQRES 1 D 15 SER LEU ARG PHE LEU PHE GLU GLY GLN ARG ILE ALA ASP
SEQRES 2 D 15 ASN HIS
SEQRES 1 E 15 SER LEU ARG PHE LEU PHE GLU GLY GLN ARG ILE ALA ASP
SEQRES 2 E 15 ASN HIS
SEQRES 1 F 15 SER LEU ARG PHE LEU PHE GLU GLY GLN ARG ILE ALA ASP
SEQRES 2 F 15 ASN HIS
HET NA A 901 1
HET NA B 901 1
HET NA C 901 1
HETNAM NA SODIUM ION
FORMUL 7 NA 3(NA 1+)
FORMUL 10 HOH *33(H2 O)
HELIX 1 AA1 SER A 57 LYS A 70 1 14
HELIX 2 AA2 TYR A 71 GLY A 73 5 3
HELIX 3 AA3 SER A 149 LYS A 159 1 11
HELIX 4 AA4 THR A 270 PHE A 277 1 8
HELIX 5 AA5 MET A 320 ARG A 324 5 5
HELIX 6 AA6 PRO A 367 PHE A 372 1 6
HELIX 7 AA7 SER A 408 GLU A 410 5 3
HELIX 8 AA8 ASP A 418 VAL A 429 1 12
HELIX 9 AA9 TYR A 686 LEU A 695 1 10
HELIX 10 AB1 GLY A 711 GLY A 716 1 6
HELIX 11 AB2 ALA A 717 LYS A 719 5 3
HELIX 12 AB3 ILE A 725 TYR A 741 1 17
HELIX 13 AB4 SER A 755 ARG A 768 1 14
HELIX 14 AB5 ASP A 788 GLY A 797 1 10
HELIX 15 AB6 HIS A 798 GLN A 801 5 4
HELIX 16 AB7 ASN A 802 SER A 810 1 9
HELIX 17 AB8 VAL A 811 PHE A 818 5 8
HELIX 18 AB9 PHE A 838 ALA A 851 1 14
HELIX 19 AC1 VAL A 869 LEU A 888 1 20
HELIX 20 AC2 SER A 890 VAL A 897 1 8
HELIX 21 AC3 SER B 57 TYR B 71 1 15
HELIX 22 AC4 SER B 149 LYS B 159 1 11
HELIX 23 AC5 THR B 270 PHE B 277 1 8
HELIX 24 AC6 MET B 320 ARG B 324 5 5
HELIX 25 AC7 PRO B 367 PHE B 372 1 6
HELIX 26 AC8 SER B 408 GLU B 410 5 3
HELIX 27 AC9 ASP B 418 VAL B 429 1 12
HELIX 28 AD1 TYR B 686 LEU B 695 1 10
HELIX 29 AD2 GLY B 711 GLY B 716 1 6
HELIX 30 AD3 ALA B 717 LYS B 719 5 3
HELIX 31 AD4 ILE B 725 TYR B 741 1 17
HELIX 32 AD5 SER B 755 ARG B 768 1 14
HELIX 33 AD6 LEU B 783 TYR B 787 5 5
HELIX 34 AD7 ASP B 788 MET B 796 1 9
HELIX 35 AD8 HIS B 798 GLN B 801 5 4
HELIX 36 AD9 ASN B 802 GLY B 809 1 8
HELIX 37 AE1 SER B 810 PHE B 818 5 9
HELIX 38 AE2 PHE B 838 ALA B 851 1 14
HELIX 39 AE3 VAL B 869 LEU B 888 1 20
HELIX 40 AE4 SER B 890 VAL B 897 1 8
HELIX 41 AE5 SER C 57 HIS C 72 1 16
HELIX 42 AE6 SER C 149 LYS C 159 1 11
HELIX 43 AE7 THR C 270 PHE C 277 1 8
HELIX 44 AE8 MET C 320 ARG C 324 5 5
HELIX 45 AE9 PRO C 367 PHE C 372 1 6
HELIX 46 AF1 SER C 408 GLU C 410 5 3
HELIX 47 AF2 ASP C 418 VAL C 429 1 12
HELIX 48 AF3 LYS C 492 GLY C 496 5 5
HELIX 49 AF4 ALA C 500 PHE C 504 5 5
HELIX 50 AF5 TYR C 686 GLY C 696 1 11
HELIX 51 AF6 GLY C 711 GLY C 716 1 6
HELIX 52 AF7 ALA C 717 LYS C 719 5 3
HELIX 53 AF8 ILE C 725 TYR C 741 1 17
HELIX 54 AF9 SER C 755 ARG C 768 1 14
HELIX 55 AG1 LEU C 783 TYR C 787 5 5
HELIX 56 AG2 ASP C 788 GLY C 797 1 10
HELIX 57 AG3 ASN C 802 GLY C 809 1 8
HELIX 58 AG4 SER C 810 PHE C 818 5 9
HELIX 59 AG5 PHE C 838 ALA C 851 1 14
HELIX 60 AG6 VAL C 869 LEU C 888 1 20
HELIX 61 AG7 SER C 890 VAL C 897 1 8
SHEET 1 AA1 5 GLU A 49 PRO A 50 0
SHEET 2 AA1 5 LYS A 660 PHE A 667 1 O LYS A 661 N GLU A 49
SHEET 3 AA1 5 VAL A 698 ILE A 702 1 O VAL A 698 N PRO A 663
SHEET 4 AA1 5 THR A 645 TYR A 651 -1 N TYR A 651 O VAL A 699
SHEET 5 AA1 5 GLU A 634 GLU A 639 -1 N PHE A 636 O GLY A 648
SHEET 1 AA2 6 GLU A 49 PRO A 50 0
SHEET 2 AA2 6 LYS A 660 PHE A 667 1 O LYS A 661 N GLU A 49
SHEET 3 AA2 6 ILE A 744 TRP A 754 1 O ARG A 748 N THR A 664
SHEET 4 AA2 6 VAL A 774 GLY A 778 1 O GLY A 778 N GLY A 753
SHEET 5 AA2 6 LEU A 825 GLY A 830 1 O LEU A 826 N ALA A 777
SHEET 6 AA2 6 ASP A 856 TYR A 860 1 O ASP A 856 N LEU A 827
SHEET 1 AA3 4 HIS A 81 LYS A 87 0
SHEET 2 AA3 4 HIS A 95 MET A 104 -1 O LEU A 102 N HIS A 81
SHEET 3 AA3 4 ASN A 111 PRO A 119 -1 O PHE A 114 N TYR A 101
SHEET 4 AA3 4 LYS A 133 PRO A 134 -1 O LYS A 133 N TYR A 115
SHEET 1 AA4 4 ASP A 170 TYR A 171 0
SHEET 2 AA4 4 THR A 177 ALA A 182 -1 O LEU A 179 N ASP A 170
SHEET 3 AA4 4 GLY A 185 LYS A 190 -1 O VAL A 189 N PHE A 178
SHEET 4 AA4 4 ASN A 205 LEU A 206 -1 O ASN A 205 N HIS A 188
SHEET 1 AA5 4 ARG A 215 LEU A 220 0
SHEET 2 AA5 4 TRP A 227 HIS A 232 -1 O ILE A 231 N MET A 216
SHEET 3 AA5 4 ASP A 235 ASN A 240 -1 O TRP A 237 N PHE A 230
SHEET 4 AA5 4 GLU A 246 ARG A 248 -1 O ARG A 247 N ILE A 238
SHEET 1 AA6 3 ARG A 264 ALA A 266 0
SHEET 2 AA6 3 LYS A 297 ASP A 307 -1 O ASN A 306 N SER A 265
SHEET 3 AA6 3 GLU A 290 THR A 291 -1 N GLU A 290 O ILE A 298
SHEET 1 AA7 5 TYR A 283 TRP A 285 0
SHEET 2 AA7 5 LYS A 297 ASP A 307 -1 O LEU A 302 N TRP A 284
SHEET 3 AA7 5 THR A 342 ILE A 350 -1 O ILE A 348 N LEU A 299
SHEET 4 AA7 5 ILE A 356 LEU A 364 -1 O LYS A 362 N MET A 345
SHEET 5 AA7 5 PHE A 412 PRO A 414 -1 O ILE A 413 N GLU A 363
SHEET 1 AA8 2 ILE A 313 THR A 317 0
SHEET 2 AA8 2 ALA A 326 ARG A 330 -1 O ASP A 327 N VAL A 316
SHEET 1 AA9 4 VAL A 375 TRP A 383 0
SHEET 2 AA9 4 ALA A 390 ASP A 396 -1 O ILE A 393 N ARG A 380
SHEET 3 AA9 4 ARG A 401 ILE A 407 -1 O GLN A 403 N LEU A 394
SHEET 4 AA9 4 LEU A 436 THR A 442 -1 O LEU A 436 N LEU A 406
SHEET 1 AB1 4 PHE A 453 VAL A 455 0
SHEET 2 AB1 4 GLU A 463 SER A 470 -1 O ILE A 467 N HIS A 454
SHEET 3 AB1 4 HIS A 478 ILE A 485 -1 O ILE A 482 N PHE A 466
SHEET 4 AB1 4 ILE A 508 ALA A 513 -1 O ILE A 512 N LYS A 481
SHEET 1 AB2 3 VAL A 521 LEU A 522 0
SHEET 2 AB2 3 LEU A 537 GLY A 542 -1 O GLU A 541 N LEU A 522
SHEET 3 AB2 3 ILE A 529 ASP A 532 -1 N GLN A 530 O TYR A 539
SHEET 1 AB3 4 VAL A 521 LEU A 522 0
SHEET 2 AB3 4 LEU A 537 GLY A 542 -1 O GLU A 541 N LEU A 522
SHEET 3 AB3 4 HIS A 551 SER A 556 -1 O TYR A 553 N PHE A 540
SHEET 4 AB3 4 THR A 564 ARG A 565 -1 O THR A 564 N VAL A 554
SHEET 1 AB4 4 SER A 572 ILE A 577 0
SHEET 2 AB4 4 PHE A 583 SER A 589 -1 O LYS A 587 N SER A 574
SHEET 3 AB4 4 CYS A 596 SER A 603 -1 O TYR A 600 N PHE A 584
SHEET 4 AB4 4 THR A 613 LEU A 621 -1 O ALA A 618 N LEU A 599
SHEET 1 AB5 5 GLU B 49 PRO B 50 0
SHEET 2 AB5 5 LYS B 660 PHE B 667 1 O LYS B 661 N GLU B 49
SHEET 3 AB5 5 VAL B 698 ILE B 702 1 O VAL B 698 N VAL B 665
SHEET 4 AB5 5 THR B 645 TYR B 651 -1 N TYR B 651 O VAL B 699
SHEET 5 AB5 5 GLU B 634 GLU B 639 -1 N PHE B 636 O GLY B 648
SHEET 1 AB6 6 GLU B 49 PRO B 50 0
SHEET 2 AB6 6 LYS B 660 PHE B 667 1 O LYS B 661 N GLU B 49
SHEET 3 AB6 6 ILE B 744 TRP B 754 1 O GLY B 750 N LEU B 666
SHEET 4 AB6 6 PHE B 772 GLY B 778 1 O ARG B 773 N VAL B 749
SHEET 5 AB6 6 LEU B 825 GLY B 830 1 O LEU B 826 N ALA B 775
SHEET 6 AB6 6 ASP B 856 TYR B 860 1 O ASP B 856 N LEU B 827
SHEET 1 AB7 4 HIS B 81 LYS B 87 0
SHEET 2 AB7 4 HIS B 95 MET B 104 -1 O ARG B 98 N VAL B 86
SHEET 3 AB7 4 ASN B 111 PRO B 119 -1 O PHE B 114 N TYR B 101
SHEET 4 AB7 4 LYS B 133 PRO B 134 -1 O LYS B 133 N TYR B 115
SHEET 1 AB8 4 ASP B 170 HIS B 172 0
SHEET 2 AB8 4 THR B 177 ALA B 182 -1 O LEU B 179 N ASP B 170
SHEET 3 AB8 4 GLY B 185 LYS B 190 -1 O VAL B 189 N PHE B 178
SHEET 4 AB8 4 ASN B 205 LEU B 206 -1 O ASN B 205 N HIS B 188
SHEET 1 AB9 4 ARG B 215 LEU B 220 0
SHEET 2 AB9 4 TRP B 227 HIS B 232 -1 O ILE B 231 N MET B 216
SHEET 3 AB9 4 ASP B 235 ASN B 240 -1 O TRP B 237 N PHE B 230
SHEET 4 AB9 4 GLU B 246 ARG B 248 -1 O ARG B 247 N ILE B 238
SHEET 1 AC1 3 ARG B 264 ALA B 266 0
SHEET 2 AC1 3 LYS B 297 ASP B 307 -1 O ASN B 306 N SER B 265
SHEET 3 AC1 3 GLU B 290 THR B 291 -1 N GLU B 290 O ILE B 298
SHEET 1 AC2 5 TYR B 283 TRP B 285 0
SHEET 2 AC2 5 LYS B 297 ASP B 307 -1 O LEU B 302 N TRP B 284
SHEET 3 AC2 5 LYS B 340 ILE B 350 -1 O ILE B 350 N LYS B 297
SHEET 4 AC2 5 ILE B 356 LEU B 364 -1 O LYS B 362 N MET B 345
SHEET 5 AC2 5 PHE B 412 PRO B 414 -1 O ILE B 413 N GLU B 363
SHEET 1 AC3 2 ILE B 313 THR B 317 0
SHEET 2 AC3 2 ALA B 326 ARG B 330 -1 O ASP B 327 N VAL B 316
SHEET 1 AC4 4 VAL B 375 TRP B 383 0
SHEET 2 AC4 4 ALA B 390 ASP B 396 -1 O LEU B 395 N GLU B 376
SHEET 3 AC4 4 ARG B 401 ILE B 407 -1 O ILE B 407 N ALA B 390
SHEET 4 AC4 4 LEU B 436 THR B 442 -1 O LEU B 436 N LEU B 406
SHEET 1 AC5 4 PHE B 453 VAL B 455 0
SHEET 2 AC5 4 GLU B 463 SER B 470 -1 O ILE B 467 N HIS B 454
SHEET 3 AC5 4 HIS B 478 ILE B 485 -1 O ILE B 482 N PHE B 466
SHEET 4 AC5 4 ILE B 508 ALA B 513 -1 O ILE B 512 N LYS B 481
SHEET 1 AC6 4 GLN B 530 ASP B 532 0
SHEET 2 AC6 4 LEU B 537 SER B 546 -1 O TYR B 539 N GLN B 530
SHEET 3 AC6 4 GLU B 549 SER B 556 -1 O TYR B 553 N PHE B 540
SHEET 4 AC6 4 THR B 564 ARG B 565 -1 O THR B 564 N VAL B 554
SHEET 1 AC7 4 SER B 572 ILE B 577 0
SHEET 2 AC7 4 PHE B 583 SER B 589 -1 O LYS B 587 N SER B 574
SHEET 3 AC7 4 CYS B 596 SER B 603 -1 O TYR B 600 N PHE B 584
SHEET 4 AC7 4 THR B 613 LEU B 621 -1 O ALA B 618 N LEU B 599
SHEET 1 AC8 5 GLU C 49 PRO C 50 0
SHEET 2 AC8 5 LYS C 660 PHE C 667 1 O LYS C 661 N GLU C 49
SHEET 3 AC8 5 VAL C 698 ILE C 702 1 O VAL C 698 N PRO C 663
SHEET 4 AC8 5 THR C 645 TYR C 651 -1 N TYR C 651 O VAL C 699
SHEET 5 AC8 5 GLU C 634 GLU C 639 -1 N PHE C 638 O LEU C 646
SHEET 1 AC9 6 GLU C 49 PRO C 50 0
SHEET 2 AC9 6 LYS C 660 PHE C 667 1 O LYS C 661 N GLU C 49
SHEET 3 AC9 6 ILE C 744 TRP C 754 1 O GLY C 750 N THR C 664
SHEET 4 AC9 6 PHE C 772 GLY C 778 1 O ILE C 776 N ILE C 751
SHEET 5 AC9 6 LEU C 825 GLY C 830 1 O LEU C 828 N ALA C 777
SHEET 6 AC9 6 ASP C 856 TYR C 860 1 O ASP C 856 N LEU C 827
SHEET 1 AD1 4 HIS C 81 LYS C 87 0
SHEET 2 AD1 4 HIS C 95 MET C 104 -1 O ARG C 98 N VAL C 86
SHEET 3 AD1 4 ASN C 111 PRO C 119 -1 O PHE C 114 N TYR C 101
SHEET 4 AD1 4 LYS C 133 PRO C 134 -1 O LYS C 133 N TYR C 115
SHEET 1 AD2 4 ASP C 170 TYR C 171 0
SHEET 2 AD2 4 THR C 177 ALA C 182 -1 O LEU C 179 N ASP C 170
SHEET 3 AD2 4 GLY C 185 LYS C 190 -1 O VAL C 189 N PHE C 178
SHEET 4 AD2 4 ASN C 205 LEU C 206 -1 O ASN C 205 N HIS C 188
SHEET 1 AD3 4 MET C 216 LEU C 220 0
SHEET 2 AD3 4 TRP C 227 ILE C 231 -1 O ILE C 231 N MET C 216
SHEET 3 AD3 4 ILE C 236 ASN C 240 -1 O TRP C 237 N PHE C 230
SHEET 4 AD3 4 GLU C 246 ARG C 248 -1 O ARG C 247 N ILE C 238
SHEET 1 AD4 3 ARG C 264 ALA C 266 0
SHEET 2 AD4 3 LYS C 297 ASP C 307 -1 O ASN C 306 N SER C 265
SHEET 3 AD4 3 TYR C 283 TRP C 285 -1 N TRP C 284 O LEU C 302
SHEET 1 AD5 5 ARG C 264 ALA C 266 0
SHEET 2 AD5 5 LYS C 297 ASP C 307 -1 O ASN C 306 N SER C 265
SHEET 3 AD5 5 LYS C 340 ILE C 350 -1 O ILE C 348 N LEU C 299
SHEET 4 AD5 5 ILE C 356 LEU C 364 -1 O LYS C 362 N MET C 345
SHEET 5 AD5 5 PHE C 412 PRO C 414 -1 O ILE C 413 N GLU C 363
SHEET 1 AD6 2 ILE C 313 THR C 317 0
SHEET 2 AD6 2 ALA C 326 ARG C 330 -1 O ASP C 327 N VAL C 316
SHEET 1 AD7 4 VAL C 375 TRP C 383 0
SHEET 2 AD7 4 ALA C 390 ASP C 396 -1 O LEU C 395 N TYR C 377
SHEET 3 AD7 4 ARG C 401 ILE C 407 -1 O ILE C 407 N ALA C 390
SHEET 4 AD7 4 LEU C 436 THR C 442 -1 O LEU C 436 N LEU C 406
SHEET 1 AD8 4 PHE C 453 VAL C 455 0
SHEET 2 AD8 4 GLU C 463 SER C 470 -1 O ILE C 467 N HIS C 454
SHEET 3 AD8 4 HIS C 478 ILE C 485 -1 O ILE C 482 N PHE C 466
SHEET 4 AD8 4 ILE C 508 ALA C 513 -1 O ILE C 512 N LYS C 481
SHEET 1 AD9 4 ILE C 529 ASP C 532 0
SHEET 2 AD9 4 LEU C 537 GLY C 542 -1 O TYR C 539 N GLN C 530
SHEET 3 AD9 4 HIS C 551 SER C 556 -1 O TYR C 553 N PHE C 540
SHEET 4 AD9 4 THR C 564 ARG C 565 -1 O THR C 564 N VAL C 554
SHEET 1 AE1 4 SER C 572 ILE C 577 0
SHEET 2 AE1 4 PHE C 583 SER C 589 -1 O LYS C 587 N SER C 574
SHEET 3 AE1 4 CYS C 596 SER C 603 -1 O TYR C 600 N PHE C 584
SHEET 4 AE1 4 THR C 613 LEU C 621 -1 O ALA C 618 N LEU C 599
LINK O ARG A 158 NA NA A 901 1555 1555 2.63
LINK O GLN A 274 NA NA A 901 1555 1555 2.92
LINK OD1 ASP A 278 NA NA A 901 1555 1555 2.69
LINK OH TYR A 280 NA NA A 901 1555 1555 2.99
LINK O ARG B 158 NA NA B 901 1555 1555 2.56
LINK O GLN B 274 NA NA B 901 1555 1555 2.88
LINK OD1 ASP B 278 NA NA B 901 1555 1555 2.81
LINK OH TYR B 280 NA NA B 901 1555 1555 2.76
LINK O ARG C 158 NA NA C 901 1555 1555 2.53
LINK O GLN C 274 NA NA C 901 1555 1555 3.07
LINK OD1 ASP C 278 NA NA C 901 1555 1555 2.71
LINK OH TYR C 280 NA NA C 901 1555 1555 2.84
SITE 1 AC1 5 ARG A 158 GLN A 274 GLU A 275 ASP A 278
SITE 2 AC1 5 TYR A 280
SITE 1 AC2 5 ARG B 158 GLN B 274 GLU B 275 ASP B 278
SITE 2 AC2 5 TYR B 280
SITE 1 AC3 5 ARG C 158 GLN C 274 GLU C 275 ASP C 278
SITE 2 AC3 5 TYR C 280
CRYST1 163.045 245.283 261.439 90.00 90.00 90.00 C 2 2 21 24
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 0.006133 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004077 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003825 0.00000
TER 6829 VAL A 897
TER 13615 VAL B 897
TER 20433 VAL C 897
TER 20522 ARG D 10
TER 20611 ARG E 10
TER 20700 ARG F 10
MASTER 603 0 3 61 150 0 6 620730 6 15 216
END |