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HEADER HYDROLASE 10-OCT-17 6EOP
TITLE DPP8 - SLRFLYEG, SPACE GROUP 20
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-TYR-GLU-GLY;
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_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606
KEYWDS DPP8, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.ROSS,R.HUBER
REVDAT 1 07-FEB-18 6EOP 0
JRNL AUTH B.H.ROSS,S.KRAPP,M.AUGUSTIN,R.KIEFERSAUER,M.ARCINIEGA,
JRNL AUTH 2 R.GEISS-FRIEDLANDER,R.HUBER
JRNL TITL STRUCTURES AND MECHANISM OF DIPEPTIDYL PEPTIDASES 8 AND 9,
JRNL TITL 2 IMPORTANT PLAYERS IN CELLULAR HOMEOSTASIS AND CANCER
JRNL REF PROC.NATL.ACAD.SCI.USA 2018
JRNL REFN ESSN 1091-6490
JRNL DOI 10.1073/PNAS.1717565115
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
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 : 193059
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10161
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14110
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.4960
REMARK 3 BIN FREE R VALUE SET COUNT : 742
REMARK 3 BIN FREE R VALUE : 0.5310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 592
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.29000
REMARK 3 B22 (A**2) : 2.84000
REMARK 3 B33 (A**2) : -1.55000
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): 0.232
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.192
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.191
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.091
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 21320 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 19874 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 28884 ; 1.145 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 45837 ; 0.853 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2528 ; 6.092 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1044 ;34.140 ;23.381
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3576 ;13.280 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 147 ;15.479 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3051 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 23871 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5078 ; 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): 10148 ; 1.884 ; 6.422
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 10147 ; 1.884 ; 6.422
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12664 ; 3.282 ; 9.627
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 12665 ; 3.282 ; 9.627
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11172 ; 1.677 ; 6.601
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 11170 ; 1.677 ; 6.600
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 16220 ; 2.934 ; 9.810
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 22532 ; 5.262 ;71.028
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 22532 ; 5.262 ;71.027
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6EOP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200006947.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-SEP-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99992
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 : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 203220
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.440
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.17000
REMARK 200 FOR THE DATA SET : 22.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
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 : 2.090
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1ORV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA CITRATE 0.46M, VAPOR DIFFUSION,
REMARK 280 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 130.59550
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 130.59550
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 81.41500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 123.18550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 81.41500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 123.18550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 130.59550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 81.41500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 123.18550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 130.59550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 81.41500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 123.18550
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: 10360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 64420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 522.38200
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: 9860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 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 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 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 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 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 SER C 105
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 72 33.77 -141.56
REMARK 500 ASP A 262 74.39 -156.04
REMARK 500 ILE A 445 -81.58 -110.05
REMARK 500 PHE A 453 107.97 -165.72
REMARK 500 GLU A 462 35.02 -99.38
REMARK 500 ASN A 559 78.01 -118.92
REMARK 500 VAL A 684 -73.76 -98.22
REMARK 500 TYR A 720 -1.39 65.44
REMARK 500 SER A 755 -115.77 57.11
REMARK 500 ALA A 779 56.33 39.45
REMARK 500 LEU A 783 108.25 -163.42
REMARK 500 ASN A 802 58.68 -156.83
REMARK 500 ASN A 835 -71.49 -95.14
REMARK 500 ARG A 864 -143.39 -108.01
REMARK 500 SER A 866 158.66 179.88
REMARK 500 LEU A 888 -60.27 -141.52
REMARK 500 TYR B 74 46.19 -102.85
REMARK 500 ASP B 137 -68.32 -92.80
REMARK 500 ASP B 224 104.18 -161.16
REMARK 500 ASP B 418 104.08 -57.69
REMARK 500 ILE B 445 -81.34 -109.59
REMARK 500 PHE B 453 115.03 -162.34
REMARK 500 ASP B 655 67.49 60.75
REMARK 500 TYR B 669 -74.65 -111.69
REMARK 500 VAL B 684 -74.23 -94.48
REMARK 500 TYR B 720 -1.75 66.48
REMARK 500 SER B 755 -116.41 59.32
REMARK 500 ASN B 802 54.82 -155.26
REMARK 500 ASN B 835 -67.24 -93.32
REMARK 500 ARG B 864 -145.33 -111.58
REMARK 500 LEU B 888 -57.92 -139.72
REMARK 500 TYR C 71 49.04 -100.34
REMARK 500 ILE C 445 -80.24 -107.42
REMARK 500 PHE C 453 113.44 -162.70
REMARK 500 GLU C 518 58.63 -94.16
REMARK 500 VAL C 558 -60.11 -90.24
REMARK 500 VAL C 684 -72.17 -98.00
REMARK 500 TYR C 720 -3.64 66.73
REMARK 500 ARG C 748 65.19 -119.96
REMARK 500 SER C 755 -115.76 58.66
REMARK 500 ALA C 779 55.58 37.54
REMARK 500 ASN C 802 59.44 -149.77
REMARK 500 ASN C 835 -70.55 -102.76
REMARK 500 ARG C 864 -143.70 -109.69
REMARK 500 SER C 866 155.75 177.44
REMARK 500 LEU C 888 -60.56 -138.30
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 CA A 902 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 158 O
REMARK 620 2 GLN A 274 O 96.1
REMARK 620 3 ASP A 278 OD1 154.2 99.5
REMARK 620 4 TYR A 280 OH 78.5 91.5 80.7
REMARK 620 5 HOH A1019 O 89.3 104.5 106.3 160.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 901 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 158 O
REMARK 620 2 GLN B 274 O 87.0
REMARK 620 3 ASP B 278 OD1 162.6 87.6
REMARK 620 4 TYR B 280 OH 80.3 83.8 82.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 901 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG C 158 O
REMARK 620 2 GLN C 274 O 97.9
REMARK 620 3 ASP C 278 OD1 160.6 89.5
REMARK 620 4 TYR C 280 OH 82.7 86.4 79.9
REMARK 620 5 HOH C1042 O 90.7 106.8 104.4 166.0
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 FLC A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F15 D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F15 E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F15 F 101
DBREF 6EOP A 1 898 UNP Q6V1X1 DPP8_HUMAN 1 898
DBREF 6EOP B 1 898 UNP Q6V1X1 DPP8_HUMAN 1 898
DBREF 6EOP C 1 898 UNP Q6V1X1 DPP8_HUMAN 1 898
DBREF 6EOP D 10 17 PDB 6EOP 6EOP 10 17
DBREF 6EOP E 10 17 PDB 6EOP 6EOP 10 17
DBREF 6EOP F 10 17 PDB 6EOP 6EOP 10 17
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 CME 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 CME 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 CME 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
SEQRES 1 D 8 SER LEU ARG PHE LEU TYR GLU GLY
SEQRES 1 E 8 SER LEU ARG PHE LEU TYR GLU GLY
SEQRES 1 F 8 SER LEU ARG PHE LEU TYR GLU GLY
MODRES 6EOP CME A 708 CYS MODIFIED RESIDUE
MODRES 6EOP CME B 708 CYS MODIFIED RESIDUE
MODRES 6EOP CME C 708 CYS MODIFIED RESIDUE
HET CME A 708 10
HET CME B 708 10
HET CME C 708 10
HET FLC A 901 13
HET CA A 902 1
HET CA B 901 1
HET CA C 901 1
HET F15 D 101 17
HET F15 E 101 17
HET F15 F 101 17
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM FLC CITRATE ANION
HETNAM CA CALCIUM ION
HETNAM F15 PENTADECANOIC ACID
FORMUL 1 CME 3(C5 H11 N O3 S2)
FORMUL 7 FLC C6 H5 O7 3-
FORMUL 8 CA 3(CA 2+)
FORMUL 11 F15 3(C15 H30 O2)
FORMUL 14 HOH *592(H2 O)
HELIX 1 AA1 SER A 57 LYS A 70 1 14
HELIX 2 AA2 SER A 149 LYS A 159 1 11
HELIX 3 AA3 ASN A 258 ASP A 262 5 5
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 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 GLY A 809 1 8
HELIX 18 AB9 SER A 810 PHE A 818 5 9
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 LYS A 896 1 7
HELIX 22 AC4 SER B 57 TYR B 71 1 15
HELIX 23 AC5 HIS B 72 MET B 76 5 5
HELIX 24 AC6 SER B 149 LYS B 159 1 11
HELIX 25 AC7 THR B 270 PHE B 277 1 8
HELIX 26 AC8 MET B 320 ARG B 324 5 5
HELIX 27 AC9 PRO B 367 PHE B 372 1 6
HELIX 28 AD1 SER B 408 GLU B 410 5 3
HELIX 29 AD2 ASP B 418 VAL B 429 1 12
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 TYR C 71 1 15
HELIX 44 AE8 SER C 149 LYS C 159 1 11
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 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 HIS C 798 GLN C 801 5 4
HELIX 58 AG4 ASN C 802 SER C 810 1 9
HELIX 59 AG5 VAL C 811 PHE C 818 5 8
HELIX 60 AG6 PHE C 838 ALA C 851 1 14
HELIX 61 AG7 VAL C 869 LEU C 888 1 20
HELIX 62 AG8 SER C 890 LYS C 896 1 7
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 PHE A 772 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 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 ALA A 103 -1 O LEU A 102 N HIS A 81
SHEET 3 AA3 4 THR A 112 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 8 GLU A 290 THR A 291 0
SHEET 2 AA6 8 PHE A 412 PRO A 414 0
SHEET 3 AA6 8 ARG A 264 VAL A 268 0
SHEET 4 AA6 8 SER A 281 TRP A 285 -1 O GLY A 282 N GLY A 267
SHEET 5 AA6 8 LYS A 297 ASP A 307 -1 O GLU A 304 N GLY A 282
SHEET 6 AA6 8 LYS A 340 ILE A 350 -1 O ILE A 350 N LYS A 297
SHEET 7 AA6 8 ILE A 356 LEU A 364 -1 O ILE A 357 N MET A 349
SHEET 8 AA6 8 PHE A 412 PRO A 414 -1 O ILE A 413 N GLU A 363
SHEET 1 AA7 2 ILE A 313 THR A 317 0
SHEET 2 AA7 2 ALA A 326 ARG A 330 -1 O ASP A 327 N VAL A 316
SHEET 1 AA8 4 VAL A 375 TRP A 383 0
SHEET 2 AA8 4 ALA A 390 ASP A 396 -1 O LEU A 395 N TYR A 377
SHEET 3 AA8 4 ARG A 401 ILE A 407 -1 O ILE A 407 N ALA A 390
SHEET 4 AA8 4 LEU A 436 THR A 442 -1 O LEU A 436 N LEU A 406
SHEET 1 AA9 4 PHE A 453 VAL A 455 0
SHEET 2 AA9 4 GLU A 463 SER A 470 -1 O ILE A 467 N HIS A 454
SHEET 3 AA9 4 HIS A 478 ILE A 485 -1 O ILE A 482 N PHE A 466
SHEET 4 AA9 4 ILE A 508 ALA A 513 -1 O ILE A 512 N LYS A 481
SHEET 1 AB1 4 GLN A 530 ASP A 532 0
SHEET 2 AB1 4 LEU A 537 GLY A 542 -1 O TYR A 539 N GLN A 530
SHEET 3 AB1 4 HIS A 551 SER A 556 -1 O TYR A 553 N PHE A 540
SHEET 4 AB1 4 THR A 564 ARG A 565 -1 O THR A 564 N VAL A 554
SHEET 1 AB2 4 SER A 572 ILE A 577 0
SHEET 2 AB2 4 PHE A 583 SER A 589 -1 O LYS A 587 N SER A 574
SHEET 3 AB2 4 CYS A 596 SER A 603 -1 O CYS A 596 N TYR A 588
SHEET 4 AB2 4 THR A 613 LEU A 621 -1 O ALA A 618 N LEU A 599
SHEET 1 AB3 5 GLU B 49 PRO B 50 0
SHEET 2 AB3 5 LYS B 660 PHE B 667 1 O LYS B 661 N GLU B 49
SHEET 3 AB3 5 VAL B 698 ILE B 702 1 O VAL B 698 N VAL B 665
SHEET 4 AB3 5 THR B 645 TYR B 651 -1 N TYR B 651 O VAL B 699
SHEET 5 AB3 5 GLU B 634 GLU B 639 -1 N PHE B 636 O GLY B 648
SHEET 1 AB4 6 GLU B 49 PRO B 50 0
SHEET 2 AB4 6 LYS B 660 PHE B 667 1 O LYS B 661 N GLU B 49
SHEET 3 AB4 6 ILE B 744 TRP B 754 1 O GLY B 750 N LEU B 666
SHEET 4 AB4 6 VAL B 774 GLY B 778 1 O GLY B 778 N GLY B 753
SHEET 5 AB4 6 LEU B 825 GLY B 830 1 O LEU B 828 N ALA B 777
SHEET 6 AB4 6 ASP B 856 TYR B 860 1 O ASP B 856 N LEU B 827
SHEET 1 AB5 4 HIS B 81 LYS B 87 0
SHEET 2 AB5 4 HIS B 95 ALA B 103 -1 O ARG B 98 N VAL B 86
SHEET 3 AB5 4 THR B 112 PRO B 119 -1 O PHE B 114 N TYR B 101
SHEET 4 AB5 4 LYS B 133 PRO B 134 -1 O LYS B 133 N TYR B 115
SHEET 1 AB6 4 ASP B 170 HIS B 172 0
SHEET 2 AB6 4 THR B 177 ALA B 182 -1 O LEU B 179 N ASP B 170
SHEET 3 AB6 4 GLY B 185 LYS B 190 -1 O VAL B 189 N PHE B 178
SHEET 4 AB6 4 ASN B 205 LEU B 206 -1 O ASN B 205 N HIS B 188
SHEET 1 AB7 4 MET B 216 CYS B 221 0
SHEET 2 AB7 4 ASP B 224 HIS B 232 -1 O ILE B 231 N MET B 216
SHEET 3 AB7 4 ASP B 235 ASN B 240 -1 O TRP B 237 N PHE B 230
SHEET 4 AB7 4 GLU B 246 ARG B 248 -1 O ARG B 247 N ILE B 238
SHEET 1 AB8 3 ARG B 264 ALA B 266 0
SHEET 2 AB8 3 LYS B 297 ASP B 307 -1 O ASN B 306 N SER B 265
SHEET 3 AB8 3 GLU B 290 THR B 291 -1 N GLU B 290 O ILE B 298
SHEET 1 AB9 5 TYR B 283 TRP B 285 0
SHEET 2 AB9 5 LYS B 297 ASP B 307 -1 O LEU B 302 N TRP B 284
SHEET 3 AB9 5 LYS B 340 ILE B 350 -1 O ILE B 350 N LYS B 297
SHEET 4 AB9 5 ILE B 356 LEU B 364 -1 O LYS B 362 N MET B 345
SHEET 5 AB9 5 PHE B 412 PRO B 414 -1 O ILE B 413 N GLU B 363
SHEET 1 AC1 2 ILE B 313 THR B 317 0
SHEET 2 AC1 2 ALA B 326 ARG B 330 -1 O ASP B 327 N VAL B 316
SHEET 1 AC2 4 VAL B 375 TRP B 383 0
SHEET 2 AC2 4 ALA B 390 ASP B 396 -1 O LEU B 395 N GLU B 376
SHEET 3 AC2 4 ARG B 401 ILE B 407 -1 O ILE B 407 N ALA B 390
SHEET 4 AC2 4 LEU B 436 THR B 442 -1 O TYR B 439 N ILE B 404
SHEET 1 AC3 4 PHE B 453 VAL B 455 0
SHEET 2 AC3 4 GLU B 463 SER B 470 -1 O ILE B 467 N HIS B 454
SHEET 3 AC3 4 HIS B 478 ILE B 485 -1 O TYR B 480 N PHE B 468
SHEET 4 AC3 4 ILE B 508 ALA B 513 -1 O ILE B 512 N LYS B 481
SHEET 1 AC4 4 GLN B 530 ASP B 532 0
SHEET 2 AC4 4 LEU B 537 GLY B 542 -1 O TYR B 539 N GLN B 530
SHEET 3 AC4 4 HIS B 551 SER B 556 -1 O TYR B 553 N PHE B 540
SHEET 4 AC4 4 THR B 564 ARG B 565 -1 O THR B 564 N VAL B 554
SHEET 1 AC5 4 SER B 572 ILE B 577 0
SHEET 2 AC5 4 PHE B 583 SER B 589 -1 O LYS B 587 N SER B 574
SHEET 3 AC5 4 CYS B 596 SER B 603 -1 O TYR B 600 N PHE B 584
SHEET 4 AC5 4 THR B 613 LEU B 621 -1 O ALA B 618 N LEU B 599
SHEET 1 AC6 5 GLU C 49 PRO C 50 0
SHEET 2 AC6 5 LYS C 660 PHE C 667 1 O LYS C 661 N GLU C 49
SHEET 3 AC6 5 VAL C 698 ILE C 702 1 O VAL C 698 N VAL C 665
SHEET 4 AC6 5 THR C 645 TYR C 651 -1 N TYR C 651 O VAL C 699
SHEET 5 AC6 5 GLU C 634 GLU C 639 -1 N PHE C 636 O GLY C 648
SHEET 1 AC7 6 GLU C 49 PRO C 50 0
SHEET 2 AC7 6 LYS C 660 PHE C 667 1 O LYS C 661 N GLU C 49
SHEET 3 AC7 6 ILE C 744 TRP C 754 1 O GLY C 750 N THR C 664
SHEET 4 AC7 6 PHE C 772 GLY C 778 1 O GLY C 778 N GLY C 753
SHEET 5 AC7 6 LEU C 825 GLY C 830 1 O LEU C 828 N ALA C 777
SHEET 6 AC7 6 ASP C 856 TYR C 860 1 O ASP C 856 N LEU C 827
SHEET 1 AC8 4 HIS C 81 LYS C 87 0
SHEET 2 AC8 4 HIS C 95 ALA C 103 -1 O LEU C 102 N HIS C 81
SHEET 3 AC8 4 THR C 112 PRO C 119 -1 O PHE C 114 N TYR C 101
SHEET 4 AC8 4 LYS C 133 PRO C 134 -1 O LYS C 133 N TYR C 115
SHEET 1 AC9 4 TYR C 169 TYR C 171 0
SHEET 2 AC9 4 THR C 177 ALA C 182 -1 O LEU C 179 N ASP C 170
SHEET 3 AC9 4 GLY C 185 LYS C 190 -1 O TYR C 187 N PHE C 180
SHEET 4 AC9 4 ASN C 205 LEU C 206 -1 O ASN C 205 N HIS C 188
SHEET 1 AD1 4 ARG C 215 CYS C 221 0
SHEET 2 AD1 4 ASP C 224 HIS C 232 -1 O ILE C 231 N MET C 216
SHEET 3 AD1 4 ASP C 235 ASN C 240 -1 O TRP C 237 N PHE C 230
SHEET 4 AD1 4 GLU C 246 ARG C 248 -1 O ARG C 247 N ILE C 238
SHEET 1 AD2 3 ARG C 264 ALA C 266 0
SHEET 2 AD2 3 LYS C 297 ASP C 307 -1 O ASN C 306 N SER C 265
SHEET 3 AD2 3 GLU C 290 THR C 291 -1 N GLU C 290 O ILE C 298
SHEET 1 AD3 5 TYR C 283 TRP C 285 0
SHEET 2 AD3 5 LYS C 297 ASP C 307 -1 O LEU C 302 N TRP C 284
SHEET 3 AD3 5 LYS C 340 ILE C 350 -1 O ILE C 350 N LYS C 297
SHEET 4 AD3 5 ILE C 356 LEU C 364 -1 O LYS C 362 N MET C 345
SHEET 5 AD3 5 PHE C 412 PRO C 414 -1 O ILE C 413 N GLU C 363
SHEET 1 AD4 2 ILE C 313 THR C 317 0
SHEET 2 AD4 2 ALA C 326 ARG C 330 -1 O ASP C 327 N VAL C 316
SHEET 1 AD5 4 VAL C 375 TRP C 383 0
SHEET 2 AD5 4 ALA C 390 ASP C 396 -1 O TRP C 391 N GLY C 382
SHEET 3 AD5 4 ARG C 401 ILE C 407 -1 O ILE C 407 N ALA C 390
SHEET 4 AD5 4 LEU C 436 THR C 442 -1 O LEU C 436 N LEU C 406
SHEET 1 AD6 4 PHE C 453 VAL C 455 0
SHEET 2 AD6 4 GLU C 463 SER C 470 -1 O ILE C 467 N HIS C 454
SHEET 3 AD6 4 HIS C 478 ILE C 485 -1 O ILE C 482 N PHE C 466
SHEET 4 AD6 4 ILE C 508 ALA C 513 -1 O LYS C 509 N THR C 483
SHEET 1 AD7 4 GLN C 530 ASP C 532 0
SHEET 2 AD7 4 LEU C 537 GLY C 542 -1 O TYR C 539 N GLN C 530
SHEET 3 AD7 4 HIS C 551 SER C 556 -1 O TYR C 553 N PHE C 540
SHEET 4 AD7 4 THR C 564 ARG C 565 -1 O THR C 564 N VAL C 554
SHEET 1 AD8 4 SER C 572 ILE C 577 0
SHEET 2 AD8 4 PHE C 583 SER C 589 -1 O LYS C 587 N SER C 574
SHEET 3 AD8 4 CYS C 596 SER C 603 -1 O CYS C 596 N TYR C 588
SHEET 4 AD8 4 THR C 613 LEU C 621 -1 O ALA C 618 N LEU C 599
LINK O ARG A 158 CA CA A 902 1555 1555 2.47
LINK O GLN A 274 CA CA A 902 1555 1555 2.59
LINK OD1 ASP A 278 CA CA A 902 1555 1555 2.52
LINK OH TYR A 280 CA CA A 902 1555 1555 2.53
LINK C SER A 707 N CME A 708 1555 1555 1.33
LINK C CME A 708 N HIS A 709 1555 1555 1.33
LINK O ARG B 158 CA CA B 901 1555 1555 2.36
LINK O GLN B 274 CA CA B 901 1555 1555 2.78
LINK OD1 ASP B 278 CA CA B 901 1555 1555 2.70
LINK OH TYR B 280 CA CA B 901 1555 1555 2.79
LINK C SER B 707 N CME B 708 1555 1555 1.32
LINK C CME B 708 N HIS B 709 1555 1555 1.33
LINK O ARG C 158 CA CA C 901 1555 1555 2.51
LINK O GLN C 274 CA CA C 901 1555 1555 2.70
LINK OD1 ASP C 278 CA CA C 901 1555 1555 2.57
LINK OH TYR C 280 CA CA C 901 1555 1555 2.60
LINK C SER C 707 N CME C 708 1555 1555 1.33
LINK C CME C 708 N HIS C 709 1555 1555 1.34
LINK CA CA A 902 O HOH A1019 1555 1555 2.51
LINK CA CA C 901 O HOH C1042 1555 1555 2.52
SITE 1 AC1 6 HIS A 172 PRO A 222 ALA A 223 PRO A 287
SITE 2 AC1 6 LYS A 288 ALA A 289
SITE 1 AC2 5 ARG A 158 GLN A 274 ASP A 278 TYR A 280
SITE 2 AC2 5 HOH A1019
SITE 1 AC3 5 ARG B 158 GLN B 274 GLU B 275 ASP B 278
SITE 2 AC3 5 TYR B 280
SITE 1 AC4 5 ARG C 158 GLN C 274 ASP C 278 TYR C 280
SITE 2 AC4 5 HOH C1042
SITE 1 AC5 7 PHE A 667 TYR A 669 VAL A 674 TYR A 686
SITE 2 AC5 7 ARG A 688 TYR A 876 ARG D 12
SITE 1 AC6 7 TYR B 669 TYR B 686 ARG B 688 TYR B 876
SITE 2 AC6 7 ARG E 12 PHE E 13 HOH E 201
SITE 1 AC7 6 TYR C 686 ARG C 688 TYR C 876 LEU C 880
SITE 2 AC7 6 ARG F 12 PHE F 13
CRYST1 162.830 246.371 261.191 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 0.006141 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004059 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003829 0.00000
TER 6850 VAL A 897
TER 13672 VAL B 897
TER 20488 VAL C 897
TER 20558 GLY D 17
TER 20628 GLY E 17
TER 20698 GLY F 17
MASTER 579 0 10 62 147 0 14 621351 6 119 213
END |