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HEADER HYDROLASE 30-SEP-08 3EQ7
TITLE PROLYL OLIGOPEPTIDASE COMPLEXED WITH R-PRO-(DECARBOXY-PRO)-
TITLE 2 TYPE INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROLYL OLIGOPEPTIDASE, PE, POST-PROLINE CLEAVING
COMPND 5 ENZYME;
COMPND 6 EC: 3.4.21.26
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 OTHER_DETAILS: MUSCLE
KEYWDS PROTEASE-INHIBITOR COMPLEX, CYTOPLASM, HYDROLASE, PROTEASE,
KEYWDS 2 SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KANAI,P.ARANYI,Z.BOCSKEI,G.FERENCZY,V.HARMAT,K.SIMON,
AUTHOR 2 G.NARAY-SZABO,I.HERMECZ
REVDAT 1 25-AUG-09 3EQ7 0
JRNL AUTH K.KANAI,P.ARANYI,Z.BOCSKEI,G.FERENCZY,V.HARMAT,
JRNL AUTH 2 K.SIMON,S.BATORI,G.NARAY-SZABO,I.HERMECZ
JRNL TITL PROLYL OLIGOPEPTIDASE INHIBITION BY
JRNL TITL 2 N-ACYL-PRO-PYRROLIDINE-TYPE MOLECULES
JRNL REF J.MED.CHEM. V. 51 7514 2008
JRNL REFN ISSN 0022-2623
JRNL PMID 19006380
JRNL DOI 10.1021/JM800944X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.53
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 17988
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 SET) : 0.178
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 865
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 5574
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 52
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.34
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) : 0.003
REMARK 3 BOND ANGLES (DEGREES) : 0.81
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 28.14
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUPED ISOTROPIC B-FACTORS, 2 B-
REMARK 3 VALUES/RESIDUE
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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3EQ7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-OCT-08.
REMARK 100 THE RCSB ID CODE IS RCSB049638.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-98
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : CAPILLARY COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BIOTEX
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17989
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 74.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.18500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54900
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1QFS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% MPEG 5000, 15% GLYCEROL, 20MM
REMARK 280 CALCIUM ACETATE, 0.1M TRIS, PH 8.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 36.22000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.12500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.72000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.12500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.22000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.72000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 LEU A 2
REMARK 465 SER A 3
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 4 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 5 CG CD OE1 NE2
REMARK 470 GLN A 17 OE1 NE2
REMARK 470 LYS A 23 CE NZ
REMARK 470 GLU A 44 CG CD OE1 OE2
REMARK 470 GLN A 56 CG CD OE1 NE2
REMARK 470 GLU A 107 CG CD OE1 OE2
REMARK 470 GLU A 109 CG CD OE1 OE2
REMARK 470 GLU A 169 CG CD OE1 OE2
REMARK 470 GLN A 192 CG CD OE1 NE2
REMARK 470 ASP A 194 CG OD1 OD2
REMARK 470 GLN A 267 CG CD OE1 NE2
REMARK 470 GLU A 322 CG CD OE1 OE2
REMARK 470 LYS A 335 CG CD CE NZ
REMARK 470 LYS A 390 CG CD CE NZ
REMARK 470 GLU A 416 CG CD OE1 OE2
REMARK 470 GLU A 418 CG CD OE1 OE2
REMARK 470 ARG A 420 CG CD NE CZ NH1 NH2
REMARK 470 THR A 426 OG1 CG2
REMARK 470 LYS A 428 CG CD CE NZ
REMARK 470 ILE A 430 CD1
REMARK 470 LYS A 449 CD CE NZ
REMARK 470 LYS A 546 CG CD CE NZ
REMARK 470 LYS A 621 CG CD CE NZ
REMARK 470 GLU A 624 CG CD OE1 OE2
REMARK 470 ARG A 662 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 664 CG CD NE CZ NH1 NH2
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 GLU A 13 -4.42 -54.87
REMARK 500 HIS A 20 41.53 37.68
REMARK 500 PRO A 27 -9.26 -59.40
REMARK 500 PRO A 74 108.33 -56.20
REMARK 500 TYR A 88 147.42 -170.94
REMARK 500 LEU A 106 -18.35 -43.82
REMARK 500 SER A 120 118.00 -164.47
REMARK 500 PHE A 173 54.44 34.82
REMARK 500 GLN A 192 98.87 -59.90
REMARK 500 SER A 197 56.47 -152.89
REMARK 500 HIS A 207 39.17 72.16
REMARK 500 ALA A 226 140.56 -171.99
REMARK 500 ASN A 271 67.02 -166.22
REMARK 500 LEU A 282 -86.05 -68.45
REMARK 500 ASP A 284 40.59 -96.97
REMARK 500 PHE A 286 31.54 -93.78
REMARK 500 VAL A 293 -61.28 -100.21
REMARK 500 TYR A 311 149.55 70.82
REMARK 500 GLU A 322 130.46 -35.35
REMARK 500 SER A 324 49.01 -69.39
REMARK 500 LYS A 325 -25.14 -158.12
REMARK 500 PRO A 331 151.26 -49.99
REMARK 500 SER A 346 -67.63 69.95
REMARK 500 CYS A 410 109.19 -160.15
REMARK 500 SER A 433 -17.20 -48.66
REMARK 500 LEU A 462 94.21 -69.54
REMARK 500 TYR A 473 -60.85 -134.31
REMARK 500 MET A 495 10.25 -143.04
REMARK 500 LEU A 520 -117.67 62.45
REMARK 500 SER A 554 -126.88 64.97
REMARK 500 VAL A 578 72.35 20.70
REMARK 500 THR A 590 -111.71 29.47
REMARK 500 SER A 615 109.93 -41.02
REMARK 500 ASP A 627 7.55 -63.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: 2-{3-[(2S)-4,4-DIFLUORO-2-(PYRROLIDIN-1-
REMARK 630 YLCARBONYL)PYRROLIDIN-1-YL]-3-OXOPROPYL}-ISOINDOLE-1,3(2H)-DIONE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 X99 A 1
REMARK 630 SOURCE: NULL
REMARK 630 SUBCOMP: FTF PDF PRU
REMARK 630 STRUCTURE DETAILS: NULL
REMARK 630 OTHER DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X99 A 711
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EQ8 RELATED DB: PDB
REMARK 900 RELATED ID: 3EQ9 RELATED DB: PDB
DBREF 3EQ7 A 1 710 UNP P23687 PPCE_PIG 1 710
SEQRES 1 A 710 MET LEU SER PHE GLN TYR PRO ASP VAL TYR ARG ASP GLU
SEQRES 2 A 710 THR ALA ILE GLN ASP TYR HIS GLY HIS LYS VAL CYS ASP
SEQRES 3 A 710 PRO TYR ALA TRP LEU GLU ASP PRO ASP SER GLU GLN THR
SEQRES 4 A 710 LYS ALA PHE VAL GLU ALA GLN ASN LYS ILE THR VAL PRO
SEQRES 5 A 710 PHE LEU GLU GLN CYS PRO ILE ARG GLY LEU TYR LYS GLU
SEQRES 6 A 710 ARG MET THR GLU LEU TYR ASP TYR PRO LYS TYR SER CYS
SEQRES 7 A 710 HIS PHE LYS LYS GLY LYS ARG TYR PHE TYR PHE TYR ASN
SEQRES 8 A 710 THR GLY LEU GLN ASN GLN ARG VAL LEU TYR VAL GLN ASP
SEQRES 9 A 710 SER LEU GLU GLY GLU ALA ARG VAL PHE LEU ASP PRO ASN
SEQRES 10 A 710 ILE LEU SER ASP ASP GLY THR VAL ALA LEU ARG GLY TYR
SEQRES 11 A 710 ALA PHE SER GLU ASP GLY GLU TYR PHE ALA TYR GLY LEU
SEQRES 12 A 710 SER ALA SER GLY SER ASP TRP VAL THR ILE LYS PHE MET
SEQRES 13 A 710 LYS VAL ASP GLY ALA LYS GLU LEU PRO ASP VAL LEU GLU
SEQRES 14 A 710 ARG VAL LYS PHE SER CYS MET ALA TRP THR HIS ASP GLY
SEQRES 15 A 710 LYS GLY MET PHE TYR ASN ALA TYR PRO GLN GLN ASP GLY
SEQRES 16 A 710 LYS SER ASP GLY THR GLU THR SER THR ASN LEU HIS GLN
SEQRES 17 A 710 LYS LEU TYR TYR HIS VAL LEU GLY THR ASP GLN SER GLU
SEQRES 18 A 710 ASP ILE LEU CYS ALA GLU PHE PRO ASP GLU PRO LYS TRP
SEQRES 19 A 710 MET GLY GLY ALA GLU LEU SER ASP ASP GLY ARG TYR VAL
SEQRES 20 A 710 LEU LEU SER ILE ARG GLU GLY CYS ASP PRO VAL ASN ARG
SEQRES 21 A 710 LEU TRP TYR CYS ASP LEU GLN GLN GLU SER ASN GLY ILE
SEQRES 22 A 710 THR GLY ILE LEU LYS TRP VAL LYS LEU ILE ASP ASN PHE
SEQRES 23 A 710 GLU GLY GLU TYR ASP TYR VAL THR ASN GLU GLY THR VAL
SEQRES 24 A 710 PHE THR PHE LYS THR ASN ARG HIS SER PRO ASN TYR ARG
SEQRES 25 A 710 LEU ILE ASN ILE ASP PHE THR ASP PRO GLU GLU SER LYS
SEQRES 26 A 710 TRP LYS VAL LEU VAL PRO GLU HIS GLU LYS ASP VAL LEU
SEQRES 27 A 710 GLU TRP VAL ALA CYS VAL ARG SER ASN PHE LEU VAL LEU
SEQRES 28 A 710 CYS TYR LEU HIS ASP VAL LYS ASN THR LEU GLN LEU HIS
SEQRES 29 A 710 ASP LEU ALA THR GLY ALA LEU LEU LYS ILE PHE PRO LEU
SEQRES 30 A 710 GLU VAL GLY SER VAL VAL GLY TYR SER GLY GLN LYS LYS
SEQRES 31 A 710 ASP THR GLU ILE PHE TYR GLN PHE THR SER PHE LEU SER
SEQRES 32 A 710 PRO GLY ILE ILE TYR HIS CYS ASP LEU THR LYS GLU GLU
SEQRES 33 A 710 LEU GLU PRO ARG VAL PHE ARG GLU VAL THR VAL LYS GLY
SEQRES 34 A 710 ILE ASP ALA SER ASP TYR GLN THR VAL GLN ILE PHE TYR
SEQRES 35 A 710 PRO SER LYS ASP GLY THR LYS ILE PRO MET PHE ILE VAL
SEQRES 36 A 710 HIS LYS LYS GLY ILE LYS LEU ASP GLY SER HIS PRO ALA
SEQRES 37 A 710 PHE LEU TYR GLY TYR GLY GLY PHE ASN ILE SER ILE THR
SEQRES 38 A 710 PRO ASN TYR SER VAL SER ARG LEU ILE PHE VAL ARG HIS
SEQRES 39 A 710 MET GLY GLY VAL LEU ALA VAL ALA ASN ILE ARG GLY GLY
SEQRES 40 A 710 GLY GLU TYR GLY GLU THR TRP HIS LYS GLY GLY ILE LEU
SEQRES 41 A 710 ALA ASN LYS GLN ASN CYS PHE ASP ASP PHE GLN CYS ALA
SEQRES 42 A 710 ALA GLU TYR LEU ILE LYS GLU GLY TYR THR SER PRO LYS
SEQRES 43 A 710 ARG LEU THR ILE ASN GLY GLY SER ASN GLY GLY LEU LEU
SEQRES 44 A 710 VAL ALA THR CYS ALA ASN GLN ARG PRO ASP LEU PHE GLY
SEQRES 45 A 710 CYS VAL ILE ALA GLN VAL GLY VAL MET ASP MET LEU LYS
SEQRES 46 A 710 PHE HIS LYS TYR THR ILE GLY HIS ALA TRP THR THR ASP
SEQRES 47 A 710 TYR GLY CYS SER ASP SER LYS GLN HIS PHE GLU TRP LEU
SEQRES 48 A 710 ILE LYS TYR SER PRO LEU HIS ASN VAL LYS LEU PRO GLU
SEQRES 49 A 710 ALA ASP ASP ILE GLN TYR PRO SER MET LEU LEU LEU THR
SEQRES 50 A 710 ALA ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER LEU
SEQRES 51 A 710 LYS PHE ILE ALA THR LEU GLN TYR ILE VAL GLY ARG SER
SEQRES 52 A 710 ARG LYS GLN ASN ASN PRO LEU LEU ILE HIS VAL ASP THR
SEQRES 53 A 710 LYS ALA GLY HIS GLY ALA GLY LYS PRO THR ALA LYS VAL
SEQRES 54 A 710 ILE GLU GLU VAL SER ASP MET PHE ALA PHE ILE ALA ARG
SEQRES 55 A 710 CYS LEU ASN ILE ASP TRP ILE PRO
HET X99 A 711 29
HETNAM X99 2-{3-[(2S)-4,4-DIFLUORO-2-(PYRROLIDIN-1-YLCARBONYL)
HETNAM 2 X99 PYRROLIDIN-1-YL]-3-OXOPROPYL}-ISOINDOLE-1,3(2H)-DIONE
FORMUL 2 X99 C20 H21 F2 N3 O4
FORMUL 3 HOH *52(H2 O)
HELIX 1 1 TYR A 28 ASP A 33 5 6
HELIX 2 2 SER A 36 GLN A 56 1 21
HELIX 3 3 PRO A 58 TYR A 71 1 14
HELIX 4 4 ASP A 115 SER A 120 5 6
HELIX 5 5 ASP A 218 ASP A 222 5 5
HELIX 6 6 GLN A 267 GLU A 269 5 3
HELIX 7 7 ASP A 431 SER A 433 5 3
HELIX 8 8 SER A 485 MET A 495 1 11
HELIX 9 9 GLY A 511 LYS A 516 1 6
HELIX 10 10 GLY A 517 ASN A 522 5 6
HELIX 11 11 LYS A 523 GLU A 540 1 18
HELIX 12 12 SER A 544 ARG A 547 5 4
HELIX 13 13 ASN A 555 ARG A 567 1 13
HELIX 14 14 LYS A 585 TYR A 589 5 5
HELIX 15 15 ILE A 591 ALA A 594 5 4
HELIX 16 16 TRP A 595 GLY A 600 1 6
HELIX 17 17 HIS A 607 SER A 615 1 9
HELIX 18 18 PRO A 616 ASN A 619 5 4
HELIX 19 19 PRO A 646 VAL A 660 1 15
HELIX 20 20 PRO A 685 ASN A 705 1 21
SHEET 1 A 2 ILE A 16 TYR A 19 0
SHEET 2 A 2 HIS A 22 CYS A 25 -1 O HIS A 22 N TYR A 19
SHEET 1 B 3 LYS A 75 TYR A 76 0
SHEET 2 B 3 ARG A 85 ASN A 91 -1 O ASN A 91 N LYS A 75
SHEET 3 B 3 PHE A 80 LYS A 82 -1 N PHE A 80 O PHE A 87
SHEET 1 C 4 LYS A 75 TYR A 76 0
SHEET 2 C 4 ARG A 85 ASN A 91 -1 O ASN A 91 N LYS A 75
SHEET 3 C 4 VAL A 99 GLN A 103 -1 O GLN A 103 N TYR A 86
SHEET 4 C 4 ARG A 111 LEU A 114 -1 O PHE A 113 N LEU A 100
SHEET 1 D 4 VAL A 125 PHE A 132 0
SHEET 2 D 4 TYR A 138 ALA A 145 -1 O GLY A 142 N ARG A 128
SHEET 3 D 4 VAL A 151 LYS A 157 -1 O LYS A 154 N TYR A 141
SHEET 4 D 4 LYS A 162 VAL A 171 -1 O VAL A 171 N VAL A 151
SHEET 1 E 4 MET A 176 TRP A 178 0
SHEET 2 E 4 GLY A 184 ALA A 189 -1 O PHE A 186 N ALA A 177
SHEET 3 E 4 LYS A 209 VAL A 214 -1 O HIS A 213 N MET A 185
SHEET 4 E 4 ILE A 223 ALA A 226 -1 O ALA A 226 N LEU A 210
SHEET 1 F 4 MET A 235 LEU A 240 0
SHEET 2 F 4 TYR A 246 ARG A 252 -1 O LEU A 248 N GLU A 239
SHEET 3 F 4 ARG A 260 ASP A 265 -1 O TRP A 262 N LEU A 249
SHEET 4 F 4 VAL A 280 ILE A 283 -1 O VAL A 280 N TYR A 263
SHEET 1 G 4 TYR A 290 GLU A 296 0
SHEET 2 G 4 VAL A 299 THR A 304 -1 O LYS A 303 N ASP A 291
SHEET 3 G 4 ARG A 312 ASP A 317 -1 O ILE A 316 N PHE A 300
SHEET 4 G 4 LYS A 327 VAL A 330 -1 O LYS A 327 N ASN A 315
SHEET 1 H 4 VAL A 337 VAL A 344 0
SHEET 2 H 4 PHE A 348 LEU A 354 -1 O VAL A 350 N ALA A 342
SHEET 3 H 4 ASN A 359 ASP A 365 -1 O HIS A 364 N LEU A 349
SHEET 4 H 4 LEU A 371 PHE A 375 -1 O PHE A 375 N LEU A 361
SHEET 1 I 4 SER A 381 TYR A 385 0
SHEET 2 I 4 GLU A 393 SER A 400 -1 O THR A 399 N SER A 381
SHEET 3 I 4 SER A 403 ASP A 411 -1 O ILE A 406 N PHE A 398
SHEET 4 I 4 ARG A 420 VAL A 425 -1 O ARG A 423 N ILE A 407
SHEET 1 J 8 TYR A 435 PRO A 443 0
SHEET 2 J 8 LYS A 449 LYS A 457 -1 O ILE A 450 N TYR A 442
SHEET 3 J 8 VAL A 498 ALA A 502 -1 O VAL A 501 N PHE A 453
SHEET 4 J 8 ALA A 468 TYR A 471 1 N TYR A 471 O ALA A 500
SHEET 5 J 8 THR A 549 SER A 554 1 O THR A 549 N LEU A 470
SHEET 6 J 8 CYS A 573 GLY A 579 1 O GLN A 577 N SER A 554
SHEET 7 J 8 SER A 632 ALA A 638 1 O LEU A 636 N VAL A 578
SHEET 8 J 8 LEU A 670 ASP A 675 1 O ASP A 675 N THR A 637
SITE 1 AC1 9 PHE A 173 CYS A 255 TYR A 473 PHE A 476
SITE 2 AC1 9 SER A 554 VAL A 580 TRP A 595 TYR A 599
SITE 3 AC1 9 ARG A 643
CRYST1 72.440 101.440 112.250 90.00 90.00 90.00 P 21 21 21 4
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 0.013800 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009860 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008910 0.00000
TER 5575 PRO A 710
MASTER 320 0 1 20 41 0 3 6 5655 1 29 55
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