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HEADER HYDROLASE 19-SEP-18 6HP8
TITLE CRYSTAL STRUCTURE OF DPP8 IN COMPLEX WITH VAL-BOROPRO
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
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
KEYWDS VAL-BOROPRO, DPP8, PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.H.ROSS,R.HUBER
REVDAT 1 31-JUL-19 6HP8 0
JRNL AUTH B.H.ROSS
JRNL TITL IMPROVEMENT OF PROTEIN CRYSTAL DIFFRACTION USING
JRNL TITL 2 POST-CRYSTALLIZATION METHODS: INFRARED LASER RADIATION
JRNL TITL 3 CONTROLS CRYSTAL ORDER
JRNL REF THESIS 2019
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 7.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 170840
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8992
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12436
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.4060
REMARK 3 BIN FREE R VALUE SET COUNT : 655
REMARK 3 BIN FREE R VALUE : 0.4020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20379
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 138
REMARK 3 SOLVENT ATOMS : 715
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.62000
REMARK 3 B22 (A**2) : 1.12000
REMARK 3 B33 (A**2) : -0.49000
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): 0.258
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.205
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.165
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.978
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 21095 ; 0.002 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 19187 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 28598 ; 0.916 ; 1.649
REMARK 3 BOND ANGLES OTHERS (DEGREES): 44563 ; 0.261 ; 1.576
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2505 ; 6.496 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1174 ;30.022 ;21.814
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3530 ;14.195 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 144 ;15.584 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2664 ; 0.037 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 23437 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4655 ; 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): 10038 ; 1.388 ; 5.189
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 10037 ; 1.388 ; 5.189
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12537 ; 2.492 ; 7.777
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 12538 ; 2.492 ; 7.777
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11056 ; 1.159 ; 5.287
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 11057 ; 1.159 ; 5.287
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 16062 ; 2.085 ; 7.870
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 22590 ; 4.086 ;57.210
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 22591 ; 4.086 ;57.212
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 6HP8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1200011967.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-17
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) : 0.99992
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 : 179844
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 44.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.6400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.46 M NA-CITRATE, PH 6.75,
REMARK 280 EVAPORATION, TEMPERATURE 293K
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 130.79400
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 130.79400
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 81.58150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 122.65850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 81.58150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 122.65850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 130.79400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 81.58150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 122.65850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 130.79400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 81.58150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 122.65850
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 65080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 490.63400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 523.17600
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 64550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1179 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 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 TYR A 71
REMARK 465 HIS A 72
REMARK 465 GLY A 73
REMARK 465 TYR A 74
REMARK 465 MET A 75
REMARK 465 MET A 76
REMARK 465 PHE A 139
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 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 TYR B 71
REMARK 465 HIS B 72
REMARK 465 GLY B 73
REMARK 465 TYR B 74
REMARK 465 MET B 75
REMARK 465 MET B 76
REMARK 465 LEU B 138
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 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 TYR C 71
REMARK 465 HIS C 72
REMARK 465 GLY C 73
REMARK 465 TYR C 74
REMARK 465 MET C 75
REMARK 465 MET C 76
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 418 105.62 -55.84
REMARK 500 ILE A 445 -86.74 -105.20
REMARK 500 PHE A 453 108.95 -166.34
REMARK 500 GLU A 462 47.58 -106.33
REMARK 500 VAL A 558 -63.83 -93.32
REMARK 500 ASN A 559 74.73 -118.87
REMARK 500 PRO A 594 170.28 -58.21
REMARK 500 VAL A 684 -76.06 -98.67
REMARK 500 TYR A 720 -8.14 73.10
REMARK 500 LYS A 721 46.57 -140.10
REMARK 500 SER A 755 -121.17 64.56
REMARK 500 ALA A 779 57.39 37.45
REMARK 500 ASN A 802 56.16 -156.90
REMARK 500 SER A 820 46.82 -88.00
REMARK 500 ASN A 835 -74.09 -90.83
REMARK 500 ARG A 864 -130.17 -95.88
REMARK 500 LEU A 888 -57.06 -142.48
REMARK 500 SER B 294 -18.67 178.29
REMARK 500 ILE B 445 -87.83 -102.29
REMARK 500 PHE B 453 114.21 -162.18
REMARK 500 VAL B 558 -65.16 -92.90
REMARK 500 ASN B 559 77.86 -115.71
REMARK 500 PRO B 626 117.91 -35.48
REMARK 500 VAL B 684 -74.89 -94.34
REMARK 500 TYR B 720 -2.30 71.46
REMARK 500 SER B 755 -116.14 62.17
REMARK 500 ASN B 802 57.82 -159.20
REMARK 500 ASN B 835 -71.94 -96.49
REMARK 500 ARG B 864 -127.52 -95.38
REMARK 500 LEU B 888 -51.51 -147.37
REMARK 500 ASP C 224 101.57 -160.61
REMARK 500 ILE C 445 -84.75 -105.37
REMARK 500 PHE C 453 113.42 -161.43
REMARK 500 VAL C 558 -65.06 -95.40
REMARK 500 ASN C 559 79.44 -117.01
REMARK 500 ASP C 655 61.51 64.59
REMARK 500 TYR C 669 -72.34 -111.44
REMARK 500 VAL C 684 -78.94 -103.77
REMARK 500 TYR C 720 -5.61 74.63
REMARK 500 SER C 755 -118.22 63.17
REMARK 500 ASN C 802 55.30 -158.60
REMARK 500 SER C 820 33.62 -93.15
REMARK 500 ASN C 835 -68.49 -90.76
REMARK 500 ARG C 864 -132.58 -97.43
REMARK 500 LEU C 888 -57.62 -147.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 GOL A 906
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 902 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 158 O
REMARK 620 2 GLN A 274 O 96.4
REMARK 620 3 ASP A 278 OD1 140.0 89.6
REMARK 620 4 TYR A 280 OH 75.0 79.8 67.3
REMARK 620 5 HOH A1234 O 89.2 148.2 67.1 71.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 902 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 158 O
REMARK 620 2 GLN B 274 O 102.1
REMARK 620 3 ASP B 278 OD1 150.2 97.5
REMARK 620 4 TYR B 280 OH 82.6 91.2 74.7
REMARK 620 5 HOH B1131 O 93.7 110.9 100.0 157.8
REMARK 620 6 HOH B1192 O 80.7 158.1 72.9 67.4 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 902 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG C 158 O
REMARK 620 2 GLN C 274 O 98.5
REMARK 620 3 ASP C 278 OD1 154.7 94.3
REMARK 620 4 TYR C 280 OH 83.4 91.1 74.6
REMARK 620 5 HOH C1007 O 93.3 100.0 105.9 168.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GK2 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GK2 B 901 and SER B
REMARK 800 755
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GK2 C 901 and SER C
REMARK 800 755
DBREF 6HP8 A 1 898 UNP Q6V1X1 DPP8_HUMAN 1 898
DBREF 6HP8 B 1 898 UNP Q6V1X1 DPP8_HUMAN 1 898
DBREF 6HP8 C 1 898 UNP Q6V1X1 DPP8_HUMAN 1 898
SEQRES 1 A 898 MET TRP LYS ARG SER GLU GLN MET LYS ILE LYS SER GLY
SEQRES 2 A 898 LYS CYS ASN MET ALA ALA ALA MET GLU THR GLU GLN LEU
SEQRES 3 A 898 GLY VAL GLU ILE PHE GLU THR ALA ASP CYS GLU GLU ASN
SEQRES 4 A 898 ILE GLU SER GLN ASP ARG PRO LYS LEU GLU PRO PHE TYR
SEQRES 5 A 898 VAL GLU ARG TYR SER TRP SER GLN LEU LYS LYS LEU LEU
SEQRES 6 A 898 ALA ASP THR ARG LYS TYR HIS GLY TYR MET MET ALA LYS
SEQRES 7 A 898 ALA PRO HIS ASP PHE MET PHE VAL LYS ARG ASN ASP PRO
SEQRES 8 A 898 ASP GLY PRO HIS SER ASP ARG ILE TYR TYR LEU ALA MET
SEQRES 9 A 898 SER GLY GLU ASN ARG GLU ASN THR LEU PHE TYR SER GLU
SEQRES 10 A 898 ILE PRO LYS THR ILE ASN ARG ALA ALA VAL LEU MET LEU
SEQRES 11 A 898 SER TRP LYS PRO LEU LEU ASP LEU PHE GLN ALA THR LEU
SEQRES 12 A 898 ASP TYR GLY MET TYR SER ARG GLU GLU GLU LEU LEU ARG
SEQRES 13 A 898 GLU ARG LYS ARG ILE GLY THR VAL GLY ILE ALA SER TYR
SEQRES 14 A 898 ASP TYR HIS GLN GLY SER GLY THR PHE LEU PHE GLN ALA
SEQRES 15 A 898 GLY SER GLY ILE TYR HIS VAL LYS ASP GLY GLY PRO GLN
SEQRES 16 A 898 GLY PHE THR GLN GLN PRO LEU ARG PRO ASN LEU VAL GLU
SEQRES 17 A 898 THR SER CYS PRO ASN ILE ARG MET ASP PRO LYS LEU CYS
SEQRES 18 A 898 PRO ALA ASP PRO ASP TRP ILE ALA PHE ILE HIS SER ASN
SEQRES 19 A 898 ASP ILE TRP ILE SER ASN ILE VAL THR ARG GLU GLU ARG
SEQRES 20 A 898 ARG LEU THR TYR VAL HIS ASN GLU LEU ALA ASN MET GLU
SEQRES 21 A 898 GLU ASP ALA ARG SER ALA GLY VAL ALA THR PHE VAL LEU
SEQRES 22 A 898 GLN GLU GLU PHE ASP ARG TYR SER GLY TYR TRP TRP CYS
SEQRES 23 A 898 PRO LYS ALA GLU THR THR PRO SER GLY GLY LYS ILE LEU
SEQRES 24 A 898 ARG ILE LEU TYR GLU GLU ASN ASP GLU SER GLU VAL GLU
SEQRES 25 A 898 ILE ILE HIS VAL THR SER PRO MET LEU GLU THR ARG ARG
SEQRES 26 A 898 ALA ASP SER PHE ARG TYR PRO LYS THR GLY THR ALA ASN
SEQRES 27 A 898 PRO LYS VAL THR PHE LYS MET SER GLU ILE MET ILE ASP
SEQRES 28 A 898 ALA GLU GLY ARG ILE ILE ASP VAL ILE ASP LYS GLU LEU
SEQRES 29 A 898 ILE GLN PRO PHE GLU ILE LEU PHE GLU GLY VAL GLU TYR
SEQRES 30 A 898 ILE ALA ARG ALA GLY TRP THR PRO GLU GLY LYS TYR ALA
SEQRES 31 A 898 TRP SER ILE LEU LEU ASP ARG SER GLN THR ARG LEU GLN
SEQRES 32 A 898 ILE VAL LEU ILE SER PRO GLU LEU PHE ILE PRO VAL GLU
SEQRES 33 A 898 ASP ASP VAL MET GLU ARG GLN ARG LEU ILE GLU SER VAL
SEQRES 34 A 898 PRO ASP SER VAL THR PRO LEU ILE ILE TYR GLU GLU THR
SEQRES 35 A 898 THR ASP ILE TRP ILE ASN ILE HIS ASP ILE PHE HIS VAL
SEQRES 36 A 898 PHE PRO GLN SER HIS GLU GLU GLU ILE GLU PHE ILE PHE
SEQRES 37 A 898 ALA SER GLU CYS LYS THR GLY PHE ARG HIS LEU TYR LYS
SEQRES 38 A 898 ILE THR SER ILE LEU LYS GLU SER LYS TYR LYS ARG SER
SEQRES 39 A 898 SER GLY GLY LEU PRO ALA PRO SER ASP PHE LYS CYS PRO
SEQRES 40 A 898 ILE LYS GLU GLU ILE ALA ILE THR SER GLY GLU TRP GLU
SEQRES 41 A 898 VAL LEU GLY ARG HIS GLY SER ASN ILE GLN VAL ASP GLU
SEQRES 42 A 898 VAL ARG ARG LEU VAL TYR PHE GLU GLY THR LYS ASP SER
SEQRES 43 A 898 PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR VAL ASN
SEQRES 44 A 898 PRO GLY GLU VAL THR ARG LEU THR ASP ARG GLY TYR SER
SEQRES 45 A 898 HIS SER CYS CYS ILE SER GLN HIS CYS ASP PHE PHE ILE
SEQRES 46 A 898 SER LYS TYR SER ASN GLN LYS ASN PRO HIS CYS VAL SER
SEQRES 47 A 898 LEU TYR LYS LEU SER SER PRO GLU ASP ASP PRO THR CYS
SEQRES 48 A 898 LYS THR LYS GLU PHE TRP ALA THR ILE LEU ASP SER ALA
SEQRES 49 A 898 GLY PRO LEU PRO ASP TYR THR PRO PRO GLU ILE PHE SER
SEQRES 50 A 898 PHE GLU SER THR THR GLY PHE THR LEU TYR GLY MET LEU
SEQRES 51 A 898 TYR LYS PRO HIS ASP LEU GLN PRO GLY LYS LYS TYR PRO
SEQRES 52 A 898 THR VAL LEU PHE ILE TYR GLY GLY PRO GLN VAL GLN LEU
SEQRES 53 A 898 VAL ASN ASN ARG PHE LYS GLY VAL LYS TYR PHE ARG LEU
SEQRES 54 A 898 ASN THR LEU ALA SER LEU GLY TYR VAL VAL VAL VAL ILE
SEQRES 55 A 898 ASP ASN ARG GLY SER CYS HIS ARG GLY LEU LYS PHE GLU
SEQRES 56 A 898 GLY ALA PHE LYS TYR LYS MET GLY GLN ILE GLU ILE ASP
SEQRES 57 A 898 ASP GLN VAL GLU GLY LEU GLN TYR LEU ALA SER ARG TYR
SEQRES 58 A 898 ASP PHE ILE ASP LEU ASP ARG VAL GLY ILE HIS GLY TRP
SEQRES 59 A 898 SER TYR GLY GLY TYR LEU SER LEU MET ALA LEU MET GLN
SEQRES 60 A 898 ARG SER ASP ILE PHE ARG VAL ALA ILE ALA GLY ALA PRO
SEQRES 61 A 898 VAL THR LEU TRP ILE PHE TYR ASP THR GLY TYR THR GLU
SEQRES 62 A 898 ARG TYR MET GLY HIS PRO ASP GLN ASN GLU GLN GLY TYR
SEQRES 63 A 898 TYR LEU GLY SER VAL ALA MET GLN ALA GLU LYS PHE PRO
SEQRES 64 A 898 SER GLU PRO ASN ARG LEU LEU LEU LEU HIS GLY PHE LEU
SEQRES 65 A 898 ASP GLU ASN VAL HIS PHE ALA HIS THR SER ILE LEU LEU
SEQRES 66 A 898 SER PHE LEU VAL ARG ALA GLY LYS PRO TYR ASP LEU GLN
SEQRES 67 A 898 ILE TYR PRO GLN GLU ARG HIS SER ILE ARG VAL PRO GLU
SEQRES 68 A 898 SER GLY GLU HIS TYR GLU LEU HIS LEU LEU HIS TYR LEU
SEQRES 69 A 898 GLN GLU ASN LEU GLY SER ARG ILE ALA ALA LEU LYS VAL
SEQRES 70 A 898 ILE
SEQRES 1 B 898 MET TRP LYS ARG SER GLU GLN MET LYS ILE LYS SER GLY
SEQRES 2 B 898 LYS CYS ASN MET ALA ALA ALA MET GLU THR GLU GLN LEU
SEQRES 3 B 898 GLY VAL GLU ILE PHE GLU THR ALA ASP CYS GLU GLU ASN
SEQRES 4 B 898 ILE GLU SER GLN ASP ARG PRO LYS LEU GLU PRO PHE TYR
SEQRES 5 B 898 VAL GLU ARG TYR SER TRP SER GLN LEU LYS LYS LEU LEU
SEQRES 6 B 898 ALA ASP THR ARG LYS TYR HIS GLY TYR MET MET ALA LYS
SEQRES 7 B 898 ALA PRO HIS ASP PHE MET PHE VAL LYS ARG ASN ASP PRO
SEQRES 8 B 898 ASP GLY PRO HIS SER ASP ARG ILE TYR TYR LEU ALA MET
SEQRES 9 B 898 SER GLY GLU ASN ARG GLU ASN THR LEU PHE TYR SER GLU
SEQRES 10 B 898 ILE PRO LYS THR ILE ASN ARG ALA ALA VAL LEU MET LEU
SEQRES 11 B 898 SER TRP LYS PRO LEU LEU ASP LEU PHE GLN ALA THR LEU
SEQRES 12 B 898 ASP TYR GLY MET TYR SER ARG GLU GLU GLU LEU LEU ARG
SEQRES 13 B 898 GLU ARG LYS ARG ILE GLY THR VAL GLY ILE ALA SER TYR
SEQRES 14 B 898 ASP TYR HIS GLN GLY SER GLY THR PHE LEU PHE GLN ALA
SEQRES 15 B 898 GLY SER GLY ILE TYR HIS VAL LYS ASP GLY GLY PRO GLN
SEQRES 16 B 898 GLY PHE THR GLN GLN PRO LEU ARG PRO ASN LEU VAL GLU
SEQRES 17 B 898 THR SER CYS PRO ASN ILE ARG MET ASP PRO LYS LEU CYS
SEQRES 18 B 898 PRO ALA ASP PRO ASP TRP ILE ALA PHE ILE HIS SER ASN
SEQRES 19 B 898 ASP ILE TRP ILE SER ASN ILE VAL THR ARG GLU GLU ARG
SEQRES 20 B 898 ARG LEU THR TYR VAL HIS ASN GLU LEU ALA ASN MET GLU
SEQRES 21 B 898 GLU ASP ALA ARG SER ALA GLY VAL ALA THR PHE VAL LEU
SEQRES 22 B 898 GLN GLU GLU PHE ASP ARG TYR SER GLY TYR TRP TRP CYS
SEQRES 23 B 898 PRO LYS ALA GLU THR THR PRO SER GLY GLY LYS ILE LEU
SEQRES 24 B 898 ARG ILE LEU TYR GLU GLU ASN ASP GLU SER GLU VAL GLU
SEQRES 25 B 898 ILE ILE HIS VAL THR SER PRO MET LEU GLU THR ARG ARG
SEQRES 26 B 898 ALA ASP SER PHE ARG TYR PRO LYS THR GLY THR ALA ASN
SEQRES 27 B 898 PRO LYS VAL THR PHE LYS MET SER GLU ILE MET ILE ASP
SEQRES 28 B 898 ALA GLU GLY ARG ILE ILE ASP VAL ILE ASP LYS GLU LEU
SEQRES 29 B 898 ILE GLN PRO PHE GLU ILE LEU PHE GLU GLY VAL GLU TYR
SEQRES 30 B 898 ILE ALA ARG ALA GLY TRP THR PRO GLU GLY LYS TYR ALA
SEQRES 31 B 898 TRP SER ILE LEU LEU ASP ARG SER GLN THR ARG LEU GLN
SEQRES 32 B 898 ILE VAL LEU ILE SER PRO GLU LEU PHE ILE PRO VAL GLU
SEQRES 33 B 898 ASP ASP VAL MET GLU ARG GLN ARG LEU ILE GLU SER VAL
SEQRES 34 B 898 PRO ASP SER VAL THR PRO LEU ILE ILE TYR GLU GLU THR
SEQRES 35 B 898 THR ASP ILE TRP ILE ASN ILE HIS ASP ILE PHE HIS VAL
SEQRES 36 B 898 PHE PRO GLN SER HIS GLU GLU GLU ILE GLU PHE ILE PHE
SEQRES 37 B 898 ALA SER GLU CYS LYS THR GLY PHE ARG HIS LEU TYR LYS
SEQRES 38 B 898 ILE THR SER ILE LEU LYS GLU SER LYS TYR LYS ARG SER
SEQRES 39 B 898 SER GLY GLY LEU PRO ALA PRO SER ASP PHE LYS CYS PRO
SEQRES 40 B 898 ILE LYS GLU GLU ILE ALA ILE THR SER GLY GLU TRP GLU
SEQRES 41 B 898 VAL LEU GLY ARG HIS GLY SER ASN ILE GLN VAL ASP GLU
SEQRES 42 B 898 VAL ARG ARG LEU VAL TYR PHE GLU GLY THR LYS ASP SER
SEQRES 43 B 898 PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR VAL ASN
SEQRES 44 B 898 PRO GLY GLU VAL THR ARG LEU THR ASP ARG GLY TYR SER
SEQRES 45 B 898 HIS SER CYS CYS ILE SER GLN HIS CYS ASP PHE PHE ILE
SEQRES 46 B 898 SER LYS TYR SER ASN GLN LYS ASN PRO HIS CYS VAL SER
SEQRES 47 B 898 LEU TYR LYS LEU SER SER PRO GLU ASP ASP PRO THR CYS
SEQRES 48 B 898 LYS THR LYS GLU PHE TRP ALA THR ILE LEU ASP SER ALA
SEQRES 49 B 898 GLY PRO LEU PRO ASP TYR THR PRO PRO GLU ILE PHE SER
SEQRES 50 B 898 PHE GLU SER THR THR GLY PHE THR LEU TYR GLY MET LEU
SEQRES 51 B 898 TYR LYS PRO HIS ASP LEU GLN PRO GLY LYS LYS TYR PRO
SEQRES 52 B 898 THR VAL LEU PHE ILE TYR GLY GLY PRO GLN VAL GLN LEU
SEQRES 53 B 898 VAL ASN ASN ARG PHE LYS GLY VAL LYS TYR PHE ARG LEU
SEQRES 54 B 898 ASN THR LEU ALA SER LEU GLY TYR VAL VAL VAL VAL ILE
SEQRES 55 B 898 ASP ASN ARG GLY SER CYS HIS ARG GLY LEU LYS PHE GLU
SEQRES 56 B 898 GLY ALA PHE LYS TYR LYS MET GLY GLN ILE GLU ILE ASP
SEQRES 57 B 898 ASP GLN VAL GLU GLY LEU GLN TYR LEU ALA SER ARG TYR
SEQRES 58 B 898 ASP PHE ILE ASP LEU ASP ARG VAL GLY ILE HIS GLY TRP
SEQRES 59 B 898 SER TYR GLY GLY TYR LEU SER LEU MET ALA LEU MET GLN
SEQRES 60 B 898 ARG SER ASP ILE PHE ARG VAL ALA ILE ALA GLY ALA PRO
SEQRES 61 B 898 VAL THR LEU TRP ILE PHE TYR ASP THR GLY TYR THR GLU
SEQRES 62 B 898 ARG TYR MET GLY HIS PRO ASP GLN ASN GLU GLN GLY TYR
SEQRES 63 B 898 TYR LEU GLY SER VAL ALA MET GLN ALA GLU LYS PHE PRO
SEQRES 64 B 898 SER GLU PRO ASN ARG LEU LEU LEU LEU HIS GLY PHE LEU
SEQRES 65 B 898 ASP GLU ASN VAL HIS PHE ALA HIS THR SER ILE LEU LEU
SEQRES 66 B 898 SER PHE LEU VAL ARG ALA GLY LYS PRO TYR ASP LEU GLN
SEQRES 67 B 898 ILE TYR PRO GLN GLU ARG HIS SER ILE ARG VAL PRO GLU
SEQRES 68 B 898 SER GLY GLU HIS TYR GLU LEU HIS LEU LEU HIS TYR LEU
SEQRES 69 B 898 GLN GLU ASN LEU GLY SER ARG ILE ALA ALA LEU LYS VAL
SEQRES 70 B 898 ILE
SEQRES 1 C 898 MET TRP LYS ARG SER GLU GLN MET LYS ILE LYS SER GLY
SEQRES 2 C 898 LYS CYS ASN MET ALA ALA ALA MET GLU THR GLU GLN LEU
SEQRES 3 C 898 GLY VAL GLU ILE PHE GLU THR ALA ASP CYS GLU GLU ASN
SEQRES 4 C 898 ILE GLU SER GLN ASP ARG PRO LYS LEU GLU PRO PHE TYR
SEQRES 5 C 898 VAL GLU ARG TYR SER TRP SER GLN LEU LYS LYS LEU LEU
SEQRES 6 C 898 ALA ASP THR ARG LYS TYR HIS GLY TYR MET MET ALA LYS
SEQRES 7 C 898 ALA PRO HIS ASP PHE MET PHE VAL LYS ARG ASN ASP PRO
SEQRES 8 C 898 ASP GLY PRO HIS SER ASP ARG ILE TYR TYR LEU ALA MET
SEQRES 9 C 898 SER GLY GLU ASN ARG GLU ASN THR LEU PHE TYR SER GLU
SEQRES 10 C 898 ILE PRO LYS THR ILE ASN ARG ALA ALA VAL LEU MET LEU
SEQRES 11 C 898 SER TRP LYS PRO LEU LEU ASP LEU PHE GLN ALA THR LEU
SEQRES 12 C 898 ASP TYR GLY MET TYR SER ARG GLU GLU GLU LEU LEU ARG
SEQRES 13 C 898 GLU ARG LYS ARG ILE GLY THR VAL GLY ILE ALA SER TYR
SEQRES 14 C 898 ASP TYR HIS GLN GLY SER GLY THR PHE LEU PHE GLN ALA
SEQRES 15 C 898 GLY SER GLY ILE TYR HIS VAL LYS ASP GLY GLY PRO GLN
SEQRES 16 C 898 GLY PHE THR GLN GLN PRO LEU ARG PRO ASN LEU VAL GLU
SEQRES 17 C 898 THR SER CYS PRO ASN ILE ARG MET ASP PRO LYS LEU CYS
SEQRES 18 C 898 PRO ALA ASP PRO ASP TRP ILE ALA PHE ILE HIS SER ASN
SEQRES 19 C 898 ASP ILE TRP ILE SER ASN ILE VAL THR ARG GLU GLU ARG
SEQRES 20 C 898 ARG LEU THR TYR VAL HIS ASN GLU LEU ALA ASN MET GLU
SEQRES 21 C 898 GLU ASP ALA ARG SER ALA GLY VAL ALA THR PHE VAL LEU
SEQRES 22 C 898 GLN GLU GLU PHE ASP ARG TYR SER GLY TYR TRP TRP CYS
SEQRES 23 C 898 PRO LYS ALA GLU THR THR PRO SER GLY GLY LYS ILE LEU
SEQRES 24 C 898 ARG ILE LEU TYR GLU GLU ASN ASP GLU SER GLU VAL GLU
SEQRES 25 C 898 ILE ILE HIS VAL THR SER PRO MET LEU GLU THR ARG ARG
SEQRES 26 C 898 ALA ASP SER PHE ARG TYR PRO LYS THR GLY THR ALA ASN
SEQRES 27 C 898 PRO LYS VAL THR PHE LYS MET SER GLU ILE MET ILE ASP
SEQRES 28 C 898 ALA GLU GLY ARG ILE ILE ASP VAL ILE ASP LYS GLU LEU
SEQRES 29 C 898 ILE GLN PRO PHE GLU ILE LEU PHE GLU GLY VAL GLU TYR
SEQRES 30 C 898 ILE ALA ARG ALA GLY TRP THR PRO GLU GLY LYS TYR ALA
SEQRES 31 C 898 TRP SER ILE LEU LEU ASP ARG SER GLN THR ARG LEU GLN
SEQRES 32 C 898 ILE VAL LEU ILE SER PRO GLU LEU PHE ILE PRO VAL GLU
SEQRES 33 C 898 ASP ASP VAL MET GLU ARG GLN ARG LEU ILE GLU SER VAL
SEQRES 34 C 898 PRO ASP SER VAL THR PRO LEU ILE ILE TYR GLU GLU THR
SEQRES 35 C 898 THR ASP ILE TRP ILE ASN ILE HIS ASP ILE PHE HIS VAL
SEQRES 36 C 898 PHE PRO GLN SER HIS GLU GLU GLU ILE GLU PHE ILE PHE
SEQRES 37 C 898 ALA SER GLU CYS LYS THR GLY PHE ARG HIS LEU TYR LYS
SEQRES 38 C 898 ILE THR SER ILE LEU LYS GLU SER LYS TYR LYS ARG SER
SEQRES 39 C 898 SER GLY GLY LEU PRO ALA PRO SER ASP PHE LYS CYS PRO
SEQRES 40 C 898 ILE LYS GLU GLU ILE ALA ILE THR SER GLY GLU TRP GLU
SEQRES 41 C 898 VAL LEU GLY ARG HIS GLY SER ASN ILE GLN VAL ASP GLU
SEQRES 42 C 898 VAL ARG ARG LEU VAL TYR PHE GLU GLY THR LYS ASP SER
SEQRES 43 C 898 PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR VAL ASN
SEQRES 44 C 898 PRO GLY GLU VAL THR ARG LEU THR ASP ARG GLY TYR SER
SEQRES 45 C 898 HIS SER CYS CYS ILE SER GLN HIS CYS ASP PHE PHE ILE
SEQRES 46 C 898 SER LYS TYR SER ASN GLN LYS ASN PRO HIS CYS VAL SER
SEQRES 47 C 898 LEU TYR LYS LEU SER SER PRO GLU ASP ASP PRO THR CYS
SEQRES 48 C 898 LYS THR LYS GLU PHE TRP ALA THR ILE LEU ASP SER ALA
SEQRES 49 C 898 GLY PRO LEU PRO ASP TYR THR PRO PRO GLU ILE PHE SER
SEQRES 50 C 898 PHE GLU SER THR THR GLY PHE THR LEU TYR GLY MET LEU
SEQRES 51 C 898 TYR LYS PRO HIS ASP LEU GLN PRO GLY LYS LYS TYR PRO
SEQRES 52 C 898 THR VAL LEU PHE ILE TYR GLY GLY PRO GLN VAL GLN LEU
SEQRES 53 C 898 VAL ASN ASN ARG PHE LYS GLY VAL LYS TYR PHE ARG LEU
SEQRES 54 C 898 ASN THR LEU ALA SER LEU GLY TYR VAL VAL VAL VAL ILE
SEQRES 55 C 898 ASP ASN ARG GLY SER CYS HIS ARG GLY LEU LYS PHE GLU
SEQRES 56 C 898 GLY ALA PHE LYS TYR LYS MET GLY GLN ILE GLU ILE ASP
SEQRES 57 C 898 ASP GLN VAL GLU GLY LEU GLN TYR LEU ALA SER ARG TYR
SEQRES 58 C 898 ASP PHE ILE ASP LEU ASP ARG VAL GLY ILE HIS GLY TRP
SEQRES 59 C 898 SER TYR GLY GLY TYR LEU SER LEU MET ALA LEU MET GLN
SEQRES 60 C 898 ARG SER ASP ILE PHE ARG VAL ALA ILE ALA GLY ALA PRO
SEQRES 61 C 898 VAL THR LEU TRP ILE PHE TYR ASP THR GLY TYR THR GLU
SEQRES 62 C 898 ARG TYR MET GLY HIS PRO ASP GLN ASN GLU GLN GLY TYR
SEQRES 63 C 898 TYR LEU GLY SER VAL ALA MET GLN ALA GLU LYS PHE PRO
SEQRES 64 C 898 SER GLU PRO ASN ARG LEU LEU LEU LEU HIS GLY PHE LEU
SEQRES 65 C 898 ASP GLU ASN VAL HIS PHE ALA HIS THR SER ILE LEU LEU
SEQRES 66 C 898 SER PHE LEU VAL ARG ALA GLY LYS PRO TYR ASP LEU GLN
SEQRES 67 C 898 ILE TYR PRO GLN GLU ARG HIS SER ILE ARG VAL PRO GLU
SEQRES 68 C 898 SER GLY GLU HIS TYR GLU LEU HIS LEU LEU HIS TYR LEU
SEQRES 69 C 898 GLN GLU ASN LEU GLY SER ARG ILE ALA ALA LEU LYS VAL
SEQRES 70 C 898 ILE
HET GK2 A 901 15
HET NA A 902 1
HET GOL A 903 6
HET GOL A 904 6
HET GOL A 905 6
HET GOL A 906 6
HET GOL A 907 6
HET GK2 B 901 15
HET NA B 902 1
HET GOL B 903 6
HET GOL B 904 6
HET GOL B 905 6
HET GOL B 906 6
HET GOL B 907 6
HET GK2 C 901 15
HET NA C 902 1
HET GOL C 903 6
HET GOL C 904 6
HET GOL C 905 6
HET GOL C 906 6
HET GOL C 907 6
HETNAM GK2 [(2~{R})-1-[(2~{R})-2-AZANYL-3-METHYL-
HETNAM 2 GK2 BUTANOYL]PYRROLIDIN-2-YL]BORONIC ACID
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 GK2 3(C9 H19 B N2 O3)
FORMUL 5 NA 3(NA 1+)
FORMUL 6 GOL 15(C3 H8 O3)
FORMUL 25 HOH *715(H2 O)
HELIX 1 AA1 SER A 57 LYS A 70 1 14
HELIX 2 AA2 SER A 149 ARG A 160 1 12
HELIX 3 AA3 THR A 270 PHE A 277 1 8
HELIX 4 AA4 MET A 320 ARG A 324 5 5
HELIX 5 AA5 PRO A 367 PHE A 372 1 6
HELIX 6 AA6 SER A 408 GLU A 410 5 3
HELIX 7 AA7 ASP A 418 SER A 428 1 11
HELIX 8 AA8 LYS A 492 GLY A 496 5 5
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 LEU A 783 TYR A 787 5 5
HELIX 15 AB6 ASP A 788 GLY A 797 1 10
HELIX 16 AB7 HIS A 798 GLN A 801 5 4
HELIX 17 AB8 ASN A 802 SER A 810 1 9
HELIX 18 AB9 VAL A 811 PHE A 818 5 8
HELIX 19 AC1 PHE A 838 ALA A 851 1 14
HELIX 20 AC2 VAL A 869 LEU A 888 1 20
HELIX 21 AC3 SER A 890 VAL A 897 1 8
HELIX 22 AC4 SER B 57 LYS B 70 1 14
HELIX 23 AC5 SER B 149 ARG B 160 1 12
HELIX 24 AC6 THR B 270 PHE B 277 1 8
HELIX 25 AC7 MET B 320 ARG B 324 5 5
HELIX 26 AC8 PRO B 367 PHE B 372 1 6
HELIX 27 AC9 SER B 408 GLU B 410 5 3
HELIX 28 AD1 ASP B 418 SER B 428 1 11
HELIX 29 AD2 LYS B 492 GLY B 496 5 5
HELIX 30 AD3 TYR B 686 LEU B 695 1 10
HELIX 31 AD4 GLY B 711 GLY B 716 1 6
HELIX 32 AD5 ALA B 717 LYS B 719 5 3
HELIX 33 AD6 ILE B 725 TYR B 741 1 17
HELIX 34 AD7 SER B 755 ARG B 768 1 14
HELIX 35 AD8 LEU B 783 TYR B 787 5 5
HELIX 36 AD9 ASP B 788 GLY B 797 1 10
HELIX 37 AE1 HIS B 798 GLN B 801 5 4
HELIX 38 AE2 ASN B 802 GLY B 809 1 8
HELIX 39 AE3 SER B 810 PHE B 818 5 9
HELIX 40 AE4 PHE B 838 ALA B 851 1 14
HELIX 41 AE5 VAL B 869 LEU B 888 1 20
HELIX 42 AE6 SER B 890 VAL B 897 1 8
HELIX 43 AE7 SER C 57 LYS C 70 1 14
HELIX 44 AE8 SER C 149 ARG C 160 1 12
HELIX 45 AE9 THR C 270 PHE C 277 1 8
HELIX 46 AF1 MET C 320 ARG C 324 5 5
HELIX 47 AF2 PRO C 367 PHE C 372 1 6
HELIX 48 AF3 SER C 408 GLU C 410 5 3
HELIX 49 AF4 ASP C 418 VAL C 429 1 12
HELIX 50 AF5 LYS C 492 GLY C 496 5 5
HELIX 51 AF6 TYR C 686 LEU C 695 1 10
HELIX 52 AF7 GLY C 711 GLY C 716 1 6
HELIX 53 AF8 ALA C 717 LYS C 719 5 3
HELIX 54 AF9 ILE C 725 TYR C 741 1 17
HELIX 55 AG1 SER C 755 ARG C 768 1 14
HELIX 56 AG2 LEU C 783 TYR C 787 5 5
HELIX 57 AG3 ASP C 788 GLY C 797 1 10
HELIX 58 AG4 HIS C 798 GLN C 801 5 4
HELIX 59 AG5 ASN C 802 GLY C 809 1 8
HELIX 60 AG6 SER C 810 PHE C 818 5 9
HELIX 61 AG7 PHE C 838 ALA C 851 1 14
HELIX 62 AG8 VAL C 869 LEU C 888 1 20
HELIX 63 AG9 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 VAL A 665
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 GLY A 750 N LEU A 666
SHEET 4 AA2 6 VAL A 774 GLY A 778 1 O ILE A 776 N ILE A 751
SHEET 5 AA2 6 LEU A 825 GLY A 830 1 O LEU A 828 N ALA A 777
SHEET 6 AA2 6 ASP A 856 TYR A 860 1 O GLN A 858 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 ARG A 98 N VAL A 86
SHEET 3 AA3 4 ASN A 111 PRO A 119 -1 O ILE A 118 N ASP A 97
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 HIS A 172 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 CYS A 221 0
SHEET 2 AA5 4 ASP A 224 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 LYS A 340 ILE A 350 -1 O ILE A 348 N LEU A 299
SHEET 4 AA7 5 ILE A 356 LEU A 364 -1 O ILE A 357 N MET A 349
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 LEU A 395 N TYR A 377
SHEET 3 AA9 4 ARG A 401 ILE A 407 -1 O ILE A 407 N ALA A 390
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 GLN A 530 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 ILE A 585 N CYS A 576
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 GLU B 634 O LEU B 650
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 THR B 664
SHEET 4 AB6 6 VAL B 774 GLY B 778 1 O ILE B 776 N ILE B 751
SHEET 5 AB6 6 LEU B 825 GLY B 830 1 O LEU B 828 N ALA B 777
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 ALA B 103 -1 O ARG B 98 N VAL B 86
SHEET 3 AB7 4 THR B 112 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 TYR B 171 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 CYS B 221 0
SHEET 2 AB9 4 ASP B 224 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 348 N LEU B 299
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 TRP B 391 N GLY B 382
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 ILE B 529 ASP B 532 0
SHEET 2 AC6 4 LEU B 537 GLY B 542 -1 O TYR B 539 N GLN B 530
SHEET 3 AC6 4 HIS B 551 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 CYS B 596 N TYR B 588
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 VAL C 665
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 636 O GLY C 648
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 LEU C 666
SHEET 4 AC9 6 VAL C 774 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 GLN C 858 N LEU C 827
SHEET 1 AD1 4 HIS C 81 LYS C 87 0
SHEET 2 AD1 4 HIS C 95 ALA C 103 -1 O ARG C 98 N VAL C 86
SHEET 3 AD1 4 THR C 112 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 HIS C 172 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 ARG C 215 CYS C 221 0
SHEET 2 AD3 4 ASP C 224 HIS C 232 -1 O ILE C 231 N MET C 216
SHEET 3 AD3 4 ASP C 235 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 GLU C 290 THR C 291 -1 N GLU C 290 O ILE C 298
SHEET 1 AD5 5 TYR C 283 TRP C 285 0
SHEET 2 AD5 5 LYS C 297 ASP C 307 -1 O LEU C 302 N TRP C 284
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 ILE C 360 N GLU C 347
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 ILE C 393 N ARG C 380
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 GLN C 530 ASP C 532 0
SHEET 2 AD9 4 LEU C 537 SER C 546 -1 O TYR C 539 N GLN C 530
SHEET 3 AD9 4 GLU C 549 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 ASN C 590 -1 O LYS C 587 N SER C 574
SHEET 3 AE1 4 ASN C 593 SER C 603 -1 O CYS C 596 N TYR C 588
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 902 1555 1555 2.46
LINK O GLN A 274 NA NA A 902 1555 1555 2.78
LINK OD1 ASP A 278 NA NA A 902 1555 1555 2.48
LINK OH TYR A 280 NA NA A 902 1555 1555 2.86
LINK OG SER A 755 B15 GK2 A 901 1555 1555 1.43
LINK O ARG B 158 NA NA B 902 1555 1555 2.40
LINK O GLN B 274 NA NA B 902 1555 1555 2.60
LINK OD1 ASP B 278 NA NA B 902 1555 1555 2.38
LINK OH TYR B 280 NA NA B 902 1555 1555 2.56
LINK OG SER B 755 B15 GK2 B 901 1555 1555 1.44
LINK O ARG C 158 NA NA C 902 1555 1555 2.32
LINK O GLN C 274 NA NA C 902 1555 1555 2.64
LINK OD1 ASP C 278 NA NA C 902 1555 1555 2.32
LINK OH TYR C 280 NA NA C 902 1555 1555 2.71
LINK OG SER C 755 B15 GK2 C 901 1555 1555 1.43
LINK NA NA A 902 O HOH A1234 1555 1555 3.15
LINK NA NA B 902 O HOH B1131 1555 1555 2.43
LINK NA NA B 902 O HOH B1192 1555 1555 3.13
LINK NA NA C 902 O HOH C1007 1555 1555 2.33
SITE 1 AC1 11 ARG A 160 GLU A 275 GLU A 276 TYR A 669
SITE 2 AC1 11 GLN A 673 SER A 755 TYR A 756 TYR A 787
SITE 3 AC1 11 TYR A 791 ASN A 835 HIS A 865
SITE 1 AC2 5 ARG A 158 GLN A 274 GLU A 275 ASP A 278
SITE 2 AC2 5 TYR A 280
SITE 1 AC3 7 HIS A 315 THR A 317 ARG A 324 ALA A 326
SITE 2 AC3 7 PHE A 831 HIS A 837 HOH A1083
SITE 1 AC4 5 HIS A 188 LEU A 206 GLU A 208 ILE A 241
SITE 2 AC4 5 HOH A1003
SITE 1 AC5 9 GLY A 526 SER A 527 ASN A 528 ILE A 529
SITE 2 AC5 9 GLN A 530 GLU A 541 CYS A 575 ILE A 577
SITE 3 AC5 9 HOH A1014
SITE 1 AC6 7 ASN A 448 HIS A 525 GLN A 673 HOH A1031
SITE 2 AC6 7 HOH A1102 HOH A1166 HOH A1201
SITE 1 AC7 6 TRP A 383 THR A 384 PRO A 385 TRP A 391
SITE 2 AC7 6 PHE A 453 VAL A 455
SITE 1 AC8 5 ARG B 158 GLN B 274 ASP B 278 TYR B 280
SITE 2 AC8 5 HOH B1131
SITE 1 AC9 6 THR B 317 ARG B 324 ARG B 325 HIS C 315
SITE 2 AC9 6 HIS C 837 GOL C 903
SITE 1 AD1 6 HOH A1011 HIS B 188 LEU B 206 GLU B 208
SITE 2 AD1 6 ILE B 241 ARG B 244
SITE 1 AD2 6 TRP B 383 TRP B 391 PHE B 453 HIS B 454
SITE 2 AD2 6 VAL B 455 HOH B1002
SITE 1 AD3 7 ASN B 448 ILE B 449 ARG B 524 GLN B 673
SITE 2 AD3 7 ARG B 794 HOH B1025 HOH B1051
SITE 1 AD4 8 GLY B 526 SER B 527 ASN B 528 GLN B 530
SITE 2 AD4 8 GLU B 541 CYS B 575 ILE B 577 HOH B1174
SITE 1 AD5 5 ARG C 158 GLN C 274 ASP C 278 TYR C 280
SITE 2 AD5 5 HOH C1007
SITE 1 AD6 8 HIS B 315 HIS B 837 GOL B 903 HOH B1115
SITE 2 AD6 8 THR C 317 ARG C 324 ALA C 326 PHE C 831
SITE 1 AD7 5 TRP C 383 TRP C 391 PHE C 453 HIS C 454
SITE 2 AD7 5 VAL C 455
SITE 1 AD8 10 ASN C 448 ARG C 524 HIS C 525 GLN C 673
SITE 2 AD8 10 ARG C 794 HOH C1004 HOH C1030 HOH C1067
SITE 3 AD8 10 HOH C1123 HOH C1166
SITE 1 AD9 6 GLY C 526 SER C 527 ASN C 528 GLU C 541
SITE 2 AD9 6 CYS C 575 ILE C 577
SITE 1 AE1 2 HIS C 595 LYS C 682
SITE 1 AE2 17 ARG B 160 GLU B 275 GLU B 276 TYR B 669
SITE 2 AE2 17 GLN B 673 TRP B 754 TYR B 756 GLY B 757
SITE 3 AE2 17 GLY B 758 TYR B 759 GLY B 778 ALA B 779
SITE 4 AE2 17 PRO B 780 TYR B 787 TYR B 791 ASN B 835
SITE 5 AE2 17 HIS B 865
SITE 1 AE3 17 ARG C 160 GLU C 275 GLU C 276 TYR C 669
SITE 2 AE3 17 GLN C 673 TRP C 754 TYR C 756 GLY C 757
SITE 3 AE3 17 GLY C 758 TYR C 759 GLY C 778 ALA C 779
SITE 4 AE3 17 TYR C 787 TYR C 791 ASN C 835 HIS C 865
SITE 5 AE3 17 HOH C1150
CRYST1 163.163 245.317 261.588 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 0.006129 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004076 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003823 0.00000
TER 6804 ILE A 898
TER 13600 ILE B 898
TER 20415 ILE C 898
MASTER 663 0 21 63 150 0 50 621232 3 160 210
END |