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HEADER HYDROLASE 31-JAN-07 2OQI
TITLE HUMAN DIPEPTIDYL PEPTIDASE IV (DPP4) WITH PIPERIDINONE-
TITLE 2 CONSTRAINED PHENETHYLAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 (DIPEPTIDYL PEPTIDASE IV)
COMPND 3 (DPP IV) (T-CELL ACTIVATION ANTIGEN CD26) (TP103)
COMPND 4 (ADENOSINE DEAMINASE COMPLEXING PROTEIN 2) (ADABP);
COMPND 5 CHAIN: A, B, C, D;
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 GENE: DPP4, ADCP2, CD26;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM
KEYWDS SERINE-PEPTIDASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.PEI,X.LI,T.W.VON GELDERN,K.L.LONGENECKER,D.PIREH,
AUTHOR 2 K.D.STEWART,B.J.BACKES,C.LAI,T.H.LUBBEN,S.J.BALLARON,
AUTHOR 3 D.W.BENO,A.J.KEMPF-GROTE,H.L.SHAM,J.M.TREVILLYAN
REVDAT 2 24-APR-07 2OQI 1 JRNL
REVDAT 1 03-APR-07 2OQI 0
JRNL AUTH Z.PEI,X.LI,T.W.GELDERN,K.LONGENECKER,D.PIREH,
JRNL AUTH 2 K.D.STEWART,B.J.BACKES,C.LAI,T.H.LUBBEN,
JRNL AUTH 3 S.J.BALLARON,D.W.BENO,A.J.KEMPF-GROTE,H.L.SHAM,
JRNL AUTH 4 J.M.TREVILLYAN
JRNL TITL DISCOVERY AND STRUCTURE-ACTIVITY RELATIONSHIPS OF
JRNL TITL 2 PIPERIDINONE- AND PIPERIDINE-CONSTRAINED
JRNL TITL 3 PHENETHYLAMINES AS NOVEL, POTENT, AND SELECTIVE
JRNL TITL 4 DIPEPTIDYL PEPTIDASE IV INHIBITORS.
JRNL REF J.MED.CHEM. V. 50 1983 2007
JRNL REFN ASTM JMCMAR US ISSN 0022-2623
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 83542
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 4148
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1207
REMARK 3 BIN R VALUE (WORKING SET) : 0.3740
REMARK 3 BIN FREE R VALUE : 0.4170
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 75
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23792
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 15.01800
REMARK 3 B22 (A**2) : -0.52700
REMARK 3 B33 (A**2) : -14.49000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.08400
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : LIG.PAR
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OQI COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-2007.
REMARK 100 THE RCSB ID CODE IS RCSB041462.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86018
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.37400
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,1/2+Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 63.65000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B
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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 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 LEU A 765
REMARK 465 PRO A 766
REMARK 465 LEU B 765
REMARK 465 PRO B 766
REMARK 465 LEU C 765
REMARK 465 PRO C 766
REMARK 465 LEU D 765
REMARK 465 PRO D 766
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 OE1 GLU A 237 OG1 THR B 251 2.19
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR A 280 CA THR A 280 CB 0.056
REMARK 500 MET A 293 SD MET A 293 CE -0.054
REMARK 500 MET A 325 SD MET A 325 CE -0.096
REMARK 500 ARG A 358 CB ARG A 358 CG -0.062
REMARK 500 GLU A 361 CB GLU A 361 CG 0.056
REMARK 500 MET A 503 SD MET A 503 CE 0.096
REMARK 500 MET A 528 SD MET A 528 CE -0.083
REMARK 500 MET A 591 SD MET A 591 CE -0.065
REMARK 500 MET A 616 CG MET A 616 SD 0.068
REMARK 500 MET A 671 SD MET A 671 CE -0.062
REMARK 500 MET B 293 SD MET B 293 CE -0.076
REMARK 500 ARG B 358 CB ARG B 358 CG -0.062
REMARK 500 GLU B 361 CB GLU B 361 CG 0.055
REMARK 500 MET B 503 SD MET B 503 CE 0.116
REMARK 500 MET B 509 SD MET B 509 CE 0.069
REMARK 500 MET B 528 SD MET B 528 CE -0.078
REMARK 500 MET B 733 SD MET B 733 CE -0.096
REMARK 500 MET B 755 SD MET B 755 CE -0.111
REMARK 500 MET C 348 SD MET C 348 CE 0.074
REMARK 500 LYS C 423 CG LYS C 423 CD -0.064
REMARK 500 MET C 425 SD MET C 425 CE -0.054
REMARK 500 MET C 503 SD MET C 503 CE 0.071
REMARK 500 MET C 528 SD MET C 528 CE -0.056
REMARK 500 MET C 755 SD MET C 755 CE -0.134
REMARK 500 MET D 293 SD MET D 293 CE -0.087
REMARK 500 MET D 348 SD MET D 348 CE 0.082
REMARK 500 MET D 503 SD MET D 503 CE 0.059
REMARK 500 MET D 591 SD MET D 591 CE -0.058
REMARK 500 MET D 616 CG MET D 616 SD 0.057
REMARK 500 MET D 755 SD MET D 755 CE -0.128
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 206 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 PHE A 240 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 ILE A 287 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 LEU A 300 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 ILE A 319 N - CA - C ANGL. DEV. =-12.2 DEGREES
REMARK 500 CYS A 339 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 VAL A 341 N - CA - C ANGL. DEV. =-17.0 DEGREES
REMARK 500 ARG A 358 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 GLN A 388 N - CA - C ANGL. DEV. =-12.3 DEGREES
REMARK 500 TRP A 402 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 SER A 458 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 PRO A 541 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 GLY A 617 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 VAL A 711 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 SER B 158 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 VAL B 160 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLU B 206 N - CA - C ANGL. DEV. = 10.9 DEGREES
REMARK 500 PHE B 240 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 ILE B 287 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 PRO B 290 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 LEU B 300 N - CA - C ANGL. DEV. =-11.8 DEGREES
REMARK 500 ILE B 319 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 VAL B 341 N - CA - C ANGL. DEV. =-15.8 DEGREES
REMARK 500 GLN B 388 N - CA - C ANGL. DEV. =-11.8 DEGREES
REMARK 500 TRP B 402 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 SER B 458 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 PRO B 541 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 GLY B 617 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 VAL B 711 N - CA - C ANGL. DEV. =-12.0 DEGREES
REMARK 500 SER B 764 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 LEU C 55 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 GLY C 111 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 LEU C 142 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 GLU C 206 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 LEU C 214 CA - CB - CG ANGL. DEV. = 11.1 DEGREES
REMARK 500 ILE C 236 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 PRO C 290 C - N - CA ANGL. DEV. = 10.6 DEGREES
REMARK 500 LEU C 300 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 ILE C 319 N - CA - C ANGL. DEV. =-12.0 DEGREES
REMARK 500 ARG C 358 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 GLU C 378 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 GLN C 388 N - CA - C ANGL. DEV. =-12.6 DEGREES
REMARK 500 SER C 458 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 ILE C 517 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ILE C 529 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 PRO C 541 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 VAL C 656 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 VAL C 711 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 LEU D 55 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 GLY D 111 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 LEU D 142 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 GLU D 206 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU D 214 CA - CB - CG ANGL. DEV. = 11.2 DEGREES
REMARK 500 PRO D 290 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU D 300 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ILE D 319 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 ARG D 358 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 GLU D 378 N - CA - C ANGL. DEV. =-12.7 DEGREES
REMARK 500 GLN D 388 N - CA - C ANGL. DEV. =-12.7 DEGREES
REMARK 500 SER D 458 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ILE D 517 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 ILE D 529 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 PRO D 541 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 ILE D 573 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 GLY D 617 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 VAL D 656 N - CA - C ANGL. DEV. =-11.7 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 GLU A 521 -58.78 85.41
REMARK 500 SER A 630 -119.40 56.38
REMARK 500 GLU B 521 -59.01 85.00
REMARK 500 ARG C 40 -164.19 26.76
REMARK 500 SER C 278 -9.60 149.79
REMARK 500 GLU C 521 -46.25 84.45
REMARK 500 ARG D 40 -165.70 26.73
REMARK 500 SER D 278 -9.49 149.62
REMARK 500 GLU D 521 -45.49 84.03
DBREF 2OQI A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 2OQI B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 2OQI C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 2OQI D 39 766 UNP P27487 DPP4_HUMAN 39 766
SEQRES 1 A 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 B 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 B 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 B 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 B 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 B 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 B 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 B 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 B 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 B 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 B 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 B 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 B 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 B 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 B 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 B 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 B 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 B 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 B 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 B 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 B 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 B 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 B 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 B 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 B 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 B 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 B 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 B 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 B 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 B 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 B 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 B 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 B 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 B 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 B 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 B 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 B 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 B 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 B 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 B 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 B 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 B 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 B 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 B 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 B 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 B 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 B 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 B 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 B 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 B 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 B 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 B 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 B 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 B 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 B 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 B 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 C 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 C 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 C 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 C 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 C 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 C 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 C 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 C 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 C 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 C 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 C 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 C 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 C 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 C 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 C 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 C 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 C 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 C 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 C 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 C 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 C 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 C 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 C 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 C 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 C 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 C 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 C 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 C 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 C 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 C 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 C 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 C 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 C 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 C 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 C 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 C 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 C 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 C 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 C 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 C 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 C 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 C 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 C 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 C 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 C 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 C 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 C 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 C 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 C 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 C 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 C 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 C 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 C 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 C 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 C 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 C 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 D 728 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 D 728 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 D 728 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 D 728 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 D 728 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 D 728 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 D 728 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 D 728 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 D 728 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 D 728 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 D 728 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 D 728 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 D 728 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 D 728 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 D 728 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 D 728 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 D 728 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 D 728 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 D 728 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 D 728 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 D 728 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 D 728 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 D 728 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 D 728 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 D 728 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 D 728 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 D 728 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 D 728 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 D 728 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 D 728 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 D 728 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 D 728 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 D 728 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 D 728 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 D 728 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 D 728 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 D 728 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 D 728 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 D 728 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 D 728 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 D 728 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 D 728 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 D 728 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 D 728 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 D 728 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 D 728 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 D 728 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 D 728 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 D 728 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 D 728 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 D 728 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 D 728 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 D 728 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 D 728 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 D 728 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 D 728 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
HET GGO 901 28
HETNAM GGO (4R,5R)-5-AMINO-1-[2-(1,3-BENZODIOXOL-5-YL)ETHYL]-4-
HETNAM 2 GGO (2,4,5-TRIFLUOROPHENYL)PIPERIDIN-2-ONE
FORMUL 5 GGO C20 H19 N2 O3 F3
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 GLU A 91 ASP A 96 5 6
HELIX 3 3 ASP A 200 GLU A 206 1 7
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 GLU A 421 MET A 425 5 5
HELIX 6 6 ASN A 497 GLN A 505 1 9
HELIX 7 7 ASN A 562 THR A 570 1 9
HELIX 8 8 GLY A 587 HIS A 592 1 6
HELIX 9 9 ALA A 593 ASN A 595 5 3
HELIX 10 10 THR A 600 LYS A 615 1 16
HELIX 11 11 SER A 630 GLY A 641 1 12
HELIX 12 12 ARG A 658 TYR A 662 5 5
HELIX 13 13 ASP A 663 GLY A 672 1 10
HELIX 14 14 ASN A 679 SER A 686 1 8
HELIX 15 15 VAL A 688 VAL A 698 5 11
HELIX 16 16 PHE A 713 VAL A 726 1 14
HELIX 17 17 SER A 744 SER A 764 1 21
HELIX 18 18 THR B 44 ASN B 51 1 8
HELIX 19 19 GLU B 91 ASP B 96 5 6
HELIX 20 20 ASP B 200 GLU B 206 1 7
HELIX 21 21 PRO B 290 ILE B 295 1 6
HELIX 22 22 GLU B 421 MET B 425 5 5
HELIX 23 23 ASN B 497 GLN B 505 1 9
HELIX 24 24 ASN B 562 THR B 570 1 9
HELIX 25 25 GLY B 587 HIS B 592 1 6
HELIX 26 26 ALA B 593 ASN B 595 5 3
HELIX 27 27 THR B 600 LYS B 615 1 16
HELIX 28 28 SER B 630 GLY B 641 1 12
HELIX 29 29 ARG B 658 TYR B 662 5 5
HELIX 30 30 ASP B 663 GLY B 672 1 10
HELIX 31 31 ASN B 679 SER B 686 1 8
HELIX 32 32 VAL B 688 VAL B 698 5 11
HELIX 33 33 HIS B 712 VAL B 726 1 15
HELIX 34 34 SER B 744 SER B 764 1 21
HELIX 35 35 THR C 44 LYS C 50 1 7
HELIX 36 36 ASN C 92 GLY C 99 5 8
HELIX 37 37 ASP C 200 GLU C 206 1 7
HELIX 38 38 PRO C 290 ILE C 295 1 6
HELIX 39 39 GLU C 421 MET C 425 5 5
HELIX 40 40 ASN C 497 GLN C 505 1 9
HELIX 41 41 ASN C 562 THR C 570 1 9
HELIX 42 42 GLY C 587 HIS C 592 1 6
HELIX 43 43 ALA C 593 ASN C 595 5 3
HELIX 44 44 THR C 600 LYS C 615 1 16
HELIX 45 45 SER C 630 GLY C 641 1 12
HELIX 46 46 ARG C 658 TYR C 662 5 5
HELIX 47 47 ASP C 663 GLY C 672 1 10
HELIX 48 48 ASN C 679 SER C 686 1 8
HELIX 49 49 VAL C 688 VAL C 698 5 11
HELIX 50 50 PHE C 713 GLY C 727 1 15
HELIX 51 51 SER C 744 SER C 764 1 21
HELIX 52 52 THR D 44 LYS D 50 1 7
HELIX 53 53 ASN D 92 GLY D 99 5 8
HELIX 54 54 ASP D 200 GLU D 206 1 7
HELIX 55 55 PRO D 290 ILE D 295 1 6
HELIX 56 56 GLU D 421 MET D 425 5 5
HELIX 57 57 ASN D 497 GLN D 505 1 9
HELIX 58 58 ASN D 562 THR D 570 1 9
HELIX 59 59 GLY D 587 HIS D 592 1 6
HELIX 60 60 ALA D 593 ASN D 595 5 3
HELIX 61 61 THR D 600 LYS D 615 1 16
HELIX 62 62 SER D 630 GLY D 641 1 12
HELIX 63 63 ARG D 658 TYR D 662 5 5
HELIX 64 64 ASP D 663 GLY D 672 1 10
HELIX 65 65 ASN D 679 SER D 686 1 8
HELIX 66 66 VAL D 688 VAL D 698 5 11
HELIX 67 67 PHE D 713 GLY D 727 1 15
HELIX 68 68 SER D 744 SER D 764 1 21
SHEET 1 A 2 LYS A 41 THR A 42 0
SHEET 2 A 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 B 4 LEU A 60 TRP A 62 0
SHEET 2 B 4 GLU A 67 LYS A 71 -1 O LEU A 69 N ARG A 61
SHEET 3 B 4 ILE A 76 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 B 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 C 4 ILE A 102 ILE A 107 0
SHEET 2 C 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 C 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 C 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 D 4 TRP A 154 TRP A 157 0
SHEET 2 D 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 D 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 D 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 E 3 ILE A 194 ASN A 196 0
SHEET 2 E 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 194 ASN A 196 0
SHEET 2 F 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 F 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 F 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 G 2 LEU A 235 PHE A 240 0
SHEET 2 G 2 LYS A 250 PRO A 255 -1 O VAL A 252 N TYR A 238
SHEET 1 H 4 HIS A 298 TRP A 305 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O VAL A 324 N TRP A 315
SHEET 4 H 4 TRP A 337 CYS A 339 -1 O ASN A 338 N ASP A 329
SHEET 1 I 4 HIS A 298 TRP A 305 0
SHEET 2 I 4 ARG A 310 ARG A 317 -1 O SER A 312 N THR A 304
SHEET 3 I 4 TYR A 322 TYR A 330 -1 O VAL A 324 N TRP A 315
SHEET 4 I 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 J 4 HIS A 363 PHE A 364 0
SHEET 2 J 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 J 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 J 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 K 4 VAL A 404 LEU A 410 0
SHEET 2 K 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 K 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 K 4 ASP A 438 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 L 4 TYR A 457 PHE A 461 0
SHEET 2 L 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 L 4 LEU A 479 SER A 484 -1 O HIS A 483 N TYR A 468
SHEET 4 L 4 GLY A 490 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 M 8 SER A 511 LEU A 519 0
SHEET 2 M 8 THR A 522 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 M 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 M 8 TYR A 540 ASP A 545 1 N LEU A 543 O ILE A 574
SHEET 5 M 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 542
SHEET 6 M 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 M 8 GLU A 699 GLY A 705 1 O ILE A 703 N ALA A 652
SHEET 8 M 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 N 2 LYS B 41 THR B 42 0
SHEET 2 N 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 O 4 LEU B 60 TRP B 62 0
SHEET 2 O 4 GLU B 67 LYS B 71 -1 O LEU B 69 N ARG B 61
SHEET 3 O 4 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 O 4 SER B 86 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 P 4 ILE B 102 ILE B 107 0
SHEET 2 P 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 P 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 P 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 Q 4 TRP B 154 TRP B 157 0
SHEET 2 Q 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
SHEET 3 Q 4 ASP B 171 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 Q 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 R 3 ILE B 194 ASN B 196 0
SHEET 2 R 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 R 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 S 4 ILE B 194 ASN B 196 0
SHEET 2 S 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 S 4 THR B 265 ASN B 272 -1 O PHE B 269 N TYR B 225
SHEET 4 S 4 SER B 284 ILE B 287 -1 O ILE B 285 N VAL B 270
SHEET 1 T 2 LEU B 235 PHE B 240 0
SHEET 2 T 2 LYS B 250 PRO B 255 -1 O VAL B 252 N TYR B 238
SHEET 1 U 4 HIS B 298 TRP B 305 0
SHEET 2 U 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 U 4 TYR B 322 TYR B 330 -1 O VAL B 324 N TRP B 315
SHEET 4 U 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 V 4 HIS B 298 TRP B 305 0
SHEET 2 V 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 V 4 TYR B 322 TYR B 330 -1 O VAL B 324 N TRP B 315
SHEET 4 V 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 W 4 HIS B 363 PHE B 364 0
SHEET 2 W 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 W 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 W 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 X 4 VAL B 404 LEU B 410 0
SHEET 2 X 4 TYR B 414 SER B 419 -1 O TYR B 416 N ALA B 409
SHEET 3 X 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 X 4 ASP B 438 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 Y 4 TYR B 457 PHE B 461 0
SHEET 2 Y 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 Y 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 Y 4 GLY B 490 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 Z 8 SER B 511 LEU B 519 0
SHEET 2 Z 8 THR B 522 LEU B 530 -1 O LEU B 530 N SER B 511
SHEET 3 Z 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 Z 8 TYR B 540 ASP B 545 1 N LEU B 543 O ILE B 574
SHEET 5 Z 8 VAL B 619 TRP B 629 1 O ALA B 625 N LEU B 542
SHEET 6 Z 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 Z 8 GLU B 699 GLY B 705 1 O ILE B 703 N ALA B 652
SHEET 8 Z 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AA 2 LYS C 41 THR C 42 0
SHEET 2 AA 2 VAL C 507 GLN C 508 1 O GLN C 508 N LYS C 41
SHEET 1 AB 4 ARG C 61 TRP C 62 0
SHEET 2 AB 4 GLU C 67 TYR C 70 -1 O LEU C 69 N ARG C 61
SHEET 3 AB 4 ILE C 76 ASN C 80 -1 O PHE C 79 N TYR C 68
SHEET 4 AB 4 SER C 86 LEU C 90 -1 O SER C 87 N VAL C 78
SHEET 1 AC 4 ILE C 102 ILE C 107 0
SHEET 2 AC 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AC 4 TYR C 128 ASP C 136 -1 O SER C 131 N TYR C 118
SHEET 4 AC 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AD 4 TRP C 154 TRP C 157 0
SHEET 2 AD 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 AD 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AD 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AE 3 ILE C 194 ASN C 196 0
SHEET 2 AE 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AE 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AF 4 ILE C 194 ASN C 196 0
SHEET 2 AF 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AF 4 THR C 265 ASN C 272 -1 O VAL C 271 N LEU C 223
SHEET 4 AF 4 SER C 284 ILE C 287 -1 O ILE C 285 N VAL C 270
SHEET 1 AG 2 LEU C 235 PHE C 240 0
SHEET 2 AG 2 LYS C 250 PRO C 255 -1 O VAL C 252 N TYR C 238
SHEET 1 AH 4 HIS C 298 THR C 307 0
SHEET 2 AH 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AH 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AH 4 TRP C 337 CYS C 339 -1 O ASN C 338 N ASP C 329
SHEET 1 AI 4 HIS C 298 THR C 307 0
SHEET 2 AI 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AI 4 TYR C 322 TYR C 330 -1 O ASP C 326 N LEU C 313
SHEET 4 AI 4 HIS C 345 MET C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AJ 4 HIS C 363 PHE C 364 0
SHEET 2 AJ 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AJ 4 ARG C 382 GLN C 388 -1 O PHE C 387 N PHE C 371
SHEET 4 AJ 4 LYS C 391 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AK 4 VAL C 404 LEU C 410 0
SHEET 2 AK 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AK 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AK 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AL 4 TYR C 457 PHE C 461 0
SHEET 2 AL 4 TYR C 467 CYS C 472 -1 O GLN C 469 N SER C 460
SHEET 3 AL 4 LEU C 479 SER C 484 -1 O THR C 481 N LEU C 470
SHEET 4 AL 4 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AM 8 SER C 511 LEU C 519 0
SHEET 2 AM 8 THR C 522 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AM 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AM 8 TYR C 540 ASP C 545 1 N ASP C 545 O ALA C 576
SHEET 5 AM 8 VAL C 619 TRP C 629 1 O ALA C 625 N LEU C 542
SHEET 6 AM 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AM 8 GLU C 699 GLY C 705 1 O ILE C 703 N ALA C 652
SHEET 8 AM 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AN 2 LYS D 41 THR D 42 0
SHEET 2 AN 2 VAL D 507 GLN D 508 1 O GLN D 508 N LYS D 41
SHEET 1 AO 4 ARG D 61 TRP D 62 0
SHEET 2 AO 4 GLU D 67 TYR D 70 -1 O LEU D 69 N ARG D 61
SHEET 3 AO 4 ILE D 76 ASN D 80 -1 O PHE D 79 N TYR D 68
SHEET 4 AO 4 SER D 86 LEU D 90 -1 O SER D 87 N VAL D 78
SHEET 1 AP 4 ILE D 102 ILE D 107 0
SHEET 2 AP 4 PHE D 113 LYS D 122 -1 O LEU D 115 N SER D 106
SHEET 3 AP 4 TYR D 128 ASP D 136 -1 O SER D 131 N TYR D 118
SHEET 4 AP 4 GLN D 141 LEU D 142 -1 O GLN D 141 N ASP D 136
SHEET 1 AQ 4 TRP D 154 TRP D 157 0
SHEET 2 AQ 4 LEU D 164 TRP D 168 -1 O VAL D 167 N TRP D 154
SHEET 3 AQ 4 ASP D 171 LYS D 175 -1 O LYS D 175 N LEU D 164
SHEET 4 AQ 4 TYR D 183 ARG D 184 -1 O TYR D 183 N VAL D 174
SHEET 1 AR 3 ILE D 194 ASN D 196 0
SHEET 2 AR 3 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AR 3 LEU D 214 TRP D 216 -1 N TRP D 215 O ALA D 224
SHEET 1 AS 4 ILE D 194 ASN D 196 0
SHEET 2 AS 4 PHE D 222 ASN D 229 -1 O PHE D 228 N TYR D 195
SHEET 3 AS 4 THR D 265 ASN D 272 -1 O PHE D 269 N TYR D 225
SHEET 4 AS 4 SER D 284 ILE D 287 -1 O ILE D 285 N VAL D 270
SHEET 1 AT 2 LEU D 235 PHE D 240 0
SHEET 2 AT 2 LYS D 250 PRO D 255 -1 O VAL D 252 N TYR D 238
SHEET 1 AU 4 HIS D 298 THR D 307 0
SHEET 2 AU 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AU 4 TYR D 322 TYR D 330 -1 O ASP D 326 N LEU D 313
SHEET 4 AU 4 TRP D 337 CYS D 339 -1 O ASN D 338 N ASP D 329
SHEET 1 AV 4 HIS D 298 THR D 307 0
SHEET 2 AV 4 ARG D 310 ARG D 317 -1 O SER D 312 N THR D 304
SHEET 3 AV 4 TYR D 322 TYR D 330 -1 O ASP D 326 N LEU D 313
SHEET 4 AV 4 HIS D 345 MET D 348 -1 O HIS D 345 N MET D 325
SHEET 1 AW 4 HIS D 363 PHE D 364 0
SHEET 2 AW 4 SER D 370 SER D 376 -1 O TYR D 372 N HIS D 363
SHEET 3 AW 4 ARG D 382 GLN D 388 -1 O PHE D 387 N PHE D 371
SHEET 4 AW 4 LYS D 391 PHE D 396 -1 O LYS D 391 N GLN D 388
SHEET 1 AX 4 VAL D 404 LEU D 410 0
SHEET 2 AX 4 TYR D 414 SER D 419 -1 O TYR D 416 N ALA D 409
SHEET 3 AX 4 ASN D 430 GLN D 435 -1 O TYR D 432 N TYR D 417
SHEET 4 AX 4 VAL D 442 CYS D 444 -1 O THR D 443 N LYS D 433
SHEET 1 AY 4 TYR D 457 PHE D 461 0
SHEET 2 AY 4 TYR D 467 CYS D 472 -1 O GLN D 469 N SER D 460
SHEET 3 AY 4 LEU D 479 SER D 484 -1 O THR D 481 N LEU D 470
SHEET 4 AY 4 LYS D 489 GLU D 495 -1 O GLU D 495 N TYR D 480
SHEET 1 AZ 8 SER D 511 LEU D 519 0
SHEET 2 AZ 8 THR D 522 LEU D 530 -1 O LEU D 530 N SER D 511
SHEET 3 AZ 8 ILE D 574 PHE D 578 -1 O VAL D 575 N ILE D 529
SHEET 4 AZ 8 TYR D 540 ASP D 545 1 N ASP D 545 O ALA D 576
SHEET 5 AZ 8 VAL D 619 TRP D 629 1 O ALA D 625 N LEU D 542
SHEET 6 AZ 8 CYS D 649 VAL D 653 1 O VAL D 653 N GLY D 628
SHEET 7 AZ 8 GLU D 699 GLY D 705 1 O ILE D 703 N ALA D 652
SHEET 8 AZ 8 GLN D 731 TYR D 735 1 O GLN D 731 N TYR D 700
SSBOND 1 CYS A 328 CYS A 339
SSBOND 2 CYS A 385 CYS A 394
SSBOND 3 CYS A 444 CYS A 447
SSBOND 4 CYS A 454 CYS A 472
SSBOND 5 CYS A 649 CYS A 762
SSBOND 6 CYS B 328 CYS B 339
SSBOND 7 CYS B 385 CYS B 394
SSBOND 8 CYS B 444 CYS B 447
SSBOND 9 CYS B 454 CYS B 472
SSBOND 10 CYS B 649 CYS B 762
SSBOND 11 CYS C 328 CYS C 339
SSBOND 12 CYS C 385 CYS C 394
SSBOND 13 CYS C 444 CYS C 447
SSBOND 14 CYS C 454 CYS C 472
SSBOND 15 CYS C 649 CYS C 762
SSBOND 16 CYS D 328 CYS D 339
SSBOND 17 CYS D 385 CYS D 394
SSBOND 18 CYS D 444 CYS D 447
SSBOND 19 CYS D 454 CYS D 472
SSBOND 20 CYS D 649 CYS D 762
CISPEP 1 ALA A 289 PRO A 290 0 0.74
CISPEP 2 GLY A 474 PRO A 475 0 -0.13
CISPEP 3 ALA B 289 PRO B 290 0 -0.66
CISPEP 4 GLY B 474 PRO B 475 0 0.35
CISPEP 5 ALA C 289 PRO C 290 0 -0.86
CISPEP 6 GLY C 474 PRO C 475 0 0.22
CISPEP 7 ALA D 289 PRO D 290 0 1.59
CISPEP 8 GLY D 474 PRO D 475 0 0.00
CRYST1 119.294 127.300 126.799 90.00 96.45 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008383 0.000000 0.000948 0.00000
SCALE2 0.000000 0.007855 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007937 0.00000
TER 5949 SER A 764
TER 11898 SER B 764
TER 17847 SER C 764
TER 23796 SER D 764
MASTER 378 0 1 68 204 0 0 623820 4 68 224
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