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HEADER HYDROLASE 06-JUN-08 3DDU
TITLE PROLYL OLIGOPEPTIDASE WITH GSK552
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROLYL OLIGOPEPTIDASE; POST-PROLINE CLEAVING
COMPND 5 ENZYME; PE;
COMPND 6 EC: 3.4.21.26;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: PREP, PEP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS POP, PROLYL OLIGOPEPTIDASE, ENDOPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.P.MADAUSS,R.A.REID,C.D.HAFFNER,A.B.MILLER
REVDAT 1 19-AUG-08 3DDU 0
JRNL AUTH C.D.HAFFNER,C.J.DIAZ,A.B.MILLER,R.A.REID,
JRNL AUTH 2 K.P.MADAUSS,A.HASSELL,M.H.HANLON,D.J.PORTER,
JRNL AUTH 3 J.D.BECHERER,L.H.CARTER
JRNL TITL PYRROLIDINYL PYRIDONE AND PYRAZINONE ANALOGUES AS
JRNL TITL 2 POTENT INHIBITORS OF PROLYL OLIGOPEPTIDASE (POP)
JRNL REF BIOORG.MED.CHEM.LETT. V. 18 4360 2008
JRNL REFN ASTM BMCLE8 UK ISSN 0960-894X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3
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) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 113121
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.300
REMARK 3 FREE R VALUE TEST SET COUNT : 8217
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.56
REMARK 3 BIN RESOLUTION RANGE LOW : 1.60
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7624
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1370
REMARK 3 BIN FREE R VALUE SET COUNT : 586
REMARK 3 BIN FREE R VALUE : 0.1810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 6933
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.17000
REMARK 3 B33 (A**2) : -0.21000
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): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.036
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.952
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5866 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3946 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7958 ; 1.298 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9604 ; 0.879 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 710 ; 6.062 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 277 ;31.908 ;24.152
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 950 ;10.957 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;12.752 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 848 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6560 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1229 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1105 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4247 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2867 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2915 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 884 ; 0.126 ; 0.200
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): 24 ; 0.195 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 39 ; 0.209 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 68 ; 0.159 ; 0.200
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): 3747 ; 0.827 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1444 ; 0.168 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5702 ; 1.153 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2615 ; 2.040 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2256 ; 2.822 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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: NULL
REMARK 4
REMARK 4 3DDU COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB047914.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-2007
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113251
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.03200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 42.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.06400
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0 .2M NAOAC 4.6, 9% PEG 4000, VAPOR
REMARK 280 DIFFUSION, 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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+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 35.61050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.92650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.94150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.92650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.61050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.94150
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 THR A 426
REMARK 465 GLY A 429
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 GLN A 5 CG CD OE1 NE2
REMARK 470 GLN A 56 CD OE1 NE2
REMARK 470 GLU A 65 OE1 OE2
REMARK 470 GLU A 69 CD OE1 OE2
REMARK 470 GLU A 107 CG CD OE1 OE2
REMARK 470 GLU A 163 CD OE1 OE2
REMARK 470 GLN A 192 CD OE1 NE2
REMARK 470 ASP A 256 CG OD1 OD2
REMARK 470 LYS A 335 CD CE NZ
REMARK 470 GLN A 388 CD OE1 NE2
REMARK 470 LYS A 428 CG CD CE NZ
REMARK 470 ASN A 483 CG OD1 ND2
REMARK 470 ILE A 498 CG1 CG2 CD1
REMARK 470 LYS A 546 CD CE NZ
REMARK 470 GLU A 624 CD OE1 OE2
REMARK 470 ARG A 664 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 GLN A 267 O HOH A 1464 4456 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 SER A 271 57.45 -152.04
REMARK 500 ASP A 284 51.21 -112.34
REMARK 500 TYR A 311 150.20 75.61
REMARK 500 ASP A 320 67.19 -152.16
REMARK 500 SER A 346 -55.66 69.56
REMARK 500 TYR A 473 -78.66 -127.24
REMARK 500 LEU A 520 -126.76 59.22
REMARK 500 SER A 554 -118.80 71.44
REMARK 500 VAL A 578 48.62 39.55
REMARK 500 THR A 590 -113.19 33.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GOL A 1000
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 801
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 802
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 803
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 804
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR RESIDUE A 805
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: 552 BINDING SITE FOR RESIDUE A 901
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE A 1000
DBREF 3DDU A 2 710 UNP P48147 PPCE_HUMAN 2 710
SEQADV 3DDU HIS A 307 UNP P48147 GLN 307 ENGINEERED
SEQADV 3DDU THR A 319 UNP P48147 TRP 319 ENGINEERED
SEQADV 3DDU THR A 360 UNP P48147 ILE 360 ENGINEERED
SEQADV 3DDU ILE A 374 UNP P48147 THR 374 ENGINEERED
SEQADV 3DDU ASN A 667 UNP P48147 SER 667 ENGINEERED
SEQRES 1 A 709 LEU SER PHE GLN TYR PRO ASP VAL TYR ARG ASP GLU THR
SEQRES 2 A 709 ALA VAL GLN ASP TYR HIS GLY HIS LYS ILE CYS ASP PRO
SEQRES 3 A 709 TYR ALA TRP LEU GLU ASP PRO ASP SER GLU GLN THR LYS
SEQRES 4 A 709 ALA PHE VAL GLU ALA GLN ASN LYS ILE THR VAL PRO PHE
SEQRES 5 A 709 LEU GLU GLN CYS PRO ILE ARG GLY LEU TYR LYS GLU ARG
SEQRES 6 A 709 MET THR GLU LEU TYR ASP TYR PRO LYS TYR SER CYS HIS
SEQRES 7 A 709 PHE LYS LYS GLY LYS ARG TYR PHE TYR PHE TYR ASN THR
SEQRES 8 A 709 GLY LEU GLN ASN GLN ARG VAL LEU TYR VAL GLN ASP SER
SEQRES 9 A 709 LEU GLU GLY GLU ALA ARG VAL PHE LEU ASP PRO ASN ILE
SEQRES 10 A 709 LEU SER ASP ASP GLY THR VAL ALA LEU ARG GLY TYR ALA
SEQRES 11 A 709 PHE SER GLU ASP GLY GLU TYR PHE ALA TYR GLY LEU SER
SEQRES 12 A 709 ALA SER GLY SER ASP TRP VAL THR ILE LYS PHE MET LYS
SEQRES 13 A 709 VAL ASP GLY ALA LYS GLU LEU PRO ASP VAL LEU GLU ARG
SEQRES 14 A 709 VAL LYS PHE SER CYS MET ALA TRP THR HIS ASP GLY LYS
SEQRES 15 A 709 GLY MET PHE TYR ASN SER TYR PRO GLN GLN ASP GLY LYS
SEQRES 16 A 709 SER ASP GLY THR GLU THR SER THR ASN LEU HIS GLN LYS
SEQRES 17 A 709 LEU TYR TYR HIS VAL LEU GLY THR ASP GLN SER GLU ASP
SEQRES 18 A 709 ILE LEU CYS ALA GLU PHE PRO ASP GLU PRO LYS TRP MET
SEQRES 19 A 709 GLY GLY ALA GLU LEU SER ASP ASP GLY ARG TYR VAL LEU
SEQRES 20 A 709 LEU SER ILE ARG GLU GLY CYS ASP PRO VAL ASN ARG LEU
SEQRES 21 A 709 TRP TYR CYS ASP LEU GLN GLN GLU SER SER GLY ILE ALA
SEQRES 22 A 709 GLY ILE LEU LYS TRP VAL LYS LEU ILE ASP ASN PHE GLU
SEQRES 23 A 709 GLY GLU TYR ASP TYR VAL THR ASN GLU GLY THR VAL PHE
SEQRES 24 A 709 THR PHE LYS THR ASN ARG HIS SER PRO ASN TYR ARG VAL
SEQRES 25 A 709 ILE ASN ILE ASP PHE THR ASP PRO GLU GLU SER LYS TRP
SEQRES 26 A 709 LYS VAL LEU VAL PRO GLU HIS GLU LYS ASP VAL LEU GLU
SEQRES 27 A 709 TRP ILE ALA CYS VAL ARG SER ASN PHE LEU VAL LEU CYS
SEQRES 28 A 709 TYR LEU HIS ASP VAL LYS ASN THR LEU GLN LEU HIS ASP
SEQRES 29 A 709 LEU THR THR GLY ALA LEU LEU LYS ILE PHE PRO LEU ASP
SEQRES 30 A 709 VAL GLY SER ILE VAL GLY TYR SER GLY GLN LYS LYS ASP
SEQRES 31 A 709 THR GLU ILE PHE TYR GLN PHE THR SER PHE LEU SER PRO
SEQRES 32 A 709 GLY ILE ILE TYR HIS CYS ASP LEU THR LYS GLU GLU LEU
SEQRES 33 A 709 GLU PRO ARG VAL PHE ARG GLU VAL THR VAL LYS GLY ILE
SEQRES 34 A 709 ASP ALA SER ASP TYR GLN THR VAL GLN ILE PHE TYR PRO
SEQRES 35 A 709 SER LYS ASP GLY THR LYS ILE PRO MET PHE ILE VAL HIS
SEQRES 36 A 709 LYS LYS GLY ILE LYS LEU ASP GLY SER HIS PRO ALA PHE
SEQRES 37 A 709 LEU TYR GLY TYR GLY GLY PHE ASN ILE SER ILE THR PRO
SEQRES 38 A 709 ASN TYR SER VAL SER ARG LEU ILE PHE VAL ARG HIS MET
SEQRES 39 A 709 GLY GLY ILE LEU ALA VAL ALA ASN ILE ARG GLY GLY GLY
SEQRES 40 A 709 GLU TYR GLY GLU THR TRP HIS LYS GLY GLY ILE LEU ALA
SEQRES 41 A 709 ASN LYS GLN ASN CYS PHE ASP ASP PHE GLN CYS ALA ALA
SEQRES 42 A 709 GLU TYR LEU ILE LYS GLU GLY TYR THR SER PRO LYS ARG
SEQRES 43 A 709 LEU THR ILE ASN GLY GLY SER ASN GLY GLY LEU LEU VAL
SEQRES 44 A 709 ALA ALA CYS ALA ASN GLN ARG PRO ASP LEU PHE GLY CYS
SEQRES 45 A 709 VAL ILE ALA GLN VAL GLY VAL MET ASP MET LEU LYS PHE
SEQRES 46 A 709 HIS LYS TYR THR ILE GLY HIS ALA TRP THR THR ASP TYR
SEQRES 47 A 709 GLY CYS SER ASP SER LYS GLN HIS PHE GLU TRP LEU VAL
SEQRES 48 A 709 LYS TYR SER PRO LEU HIS ASN VAL LYS LEU PRO GLU ALA
SEQRES 49 A 709 ASP ASP ILE GLN TYR PRO SER MET LEU LEU LEU THR ALA
SEQRES 50 A 709 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER LEU LYS
SEQRES 51 A 709 PHE ILE ALA THR LEU GLN TYR ILE VAL GLY ARG SER ARG
SEQRES 52 A 709 LYS GLN ASN ASN PRO LEU LEU ILE HIS VAL ASP THR LYS
SEQRES 53 A 709 ALA GLY HIS GLY ALA GLY LYS PRO THR ALA LYS VAL ILE
SEQRES 54 A 709 GLU GLU VAL SER ASP MET PHE ALA PHE ILE ALA ARG CYS
SEQRES 55 A 709 LEU ASN VAL ASP TRP ILE PRO
HET ACT A 801 4
HET ACT A 802 4
HET ACT A 803 4
HET ACT A 804 4
HET ACT A 805 4
HET 552 A 901 27
HET GOL A1000 5
HETNAM ACT ACETATE ION
HETNAM 552 (6S)-1-CHLORO-3-[(4-FLUOROBENZYL)OXY]-6-(PYRROLIDIN-1-
HETNAM 2 552 YLCARBONYL)PYRROLO[1,2-A]PYRAZIN-4(6H)-ONE
HETNAM GOL GLYCEROL
FORMUL 2 ACT 5(C2 H3 O2 1-)
FORMUL 7 552 C19 H17 CL F N3 O3
FORMUL 8 GOL C3 H8 O3
FORMUL 9 HOH *1234(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 GLU A 322 TRP A 326 5 5
HELIX 8 8 ASP A 431 SER A 433 5 3
HELIX 9 9 SER A 485 GLY A 496 1 12
HELIX 10 10 TYR A 510 GLY A 517 1 8
HELIX 11 11 GLY A 518 ASN A 522 5 5
HELIX 12 12 LYS A 523 GLU A 540 1 18
HELIX 13 13 SER A 544 LYS A 546 5 3
HELIX 14 14 SER A 554 ARG A 567 1 14
HELIX 15 15 PRO A 568 PHE A 571 5 4
HELIX 16 16 LYS A 585 TYR A 589 5 5
HELIX 17 17 ILE A 591 ALA A 594 5 4
HELIX 18 18 TRP A 595 GLY A 600 1 6
HELIX 19 19 SER A 604 SER A 615 1 12
HELIX 20 20 PRO A 616 ASN A 619 5 4
HELIX 21 21 PRO A 646 VAL A 660 1 15
HELIX 22 22 PRO A 685 ASN A 705 1 21
SHEET 1 A 2 VAL 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 TYR A 101 N TYR A 88
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 GLY A 129
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 SER 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 CYS A 225 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 THR A 301 N THR A 294
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 HIS A 355 -1 O VAL A 350 N ALA A 342
SHEET 3 H 4 LYS A 358 ASP A 365 -1 O LYS A 358 N HIS A 355
SHEET 4 H 4 LEU A 371 PHE A 375 -1 O LEU A 372 N LEU A 363
SHEET 1 I 4 SER A 381 SER A 386 0
SHEET 2 I 4 GLU A 393 THR A 399 -1 O GLN A 397 N VAL A 383
SHEET 3 I 4 ILE A 406 ASP A 411 -1 O TYR A 408 N TYR A 396
SHEET 4 I 4 ARG A 420 ARG A 423 -1 O PHE A 422 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 ILE A 498 ALA A 502 -1 O LEU A 499 N VAL A 455
SHEET 4 J 8 ALA A 468 TYR A 471 1 N TYR A 471 O ALA A 500
SHEET 5 J 8 LEU A 548 GLY A 553 1 O THR A 549 N LEU A 470
SHEET 6 J 8 CYS A 573 GLN A 577 1 O ILE A 575 N ILE A 550
SHEET 7 J 8 SER A 632 ALA A 638 1 O LEU A 634 N VAL A 574
SHEET 8 J 8 LEU A 670 ASP A 675 1 O LEU A 671 N MET A 633
SITE 1 AC1 4 TYR A 473 SER A 554 HIS A 680 HOH A1213
SITE 1 AC2 5 PHE A 401 ARG A 488 LEU A 499 HOH A1543
SITE 2 AC2 5 HOH A2062
SITE 1 AC3 6 PRO A 7 GLN A 657 ARG A 662 HOH A1153
SITE 2 AC3 6 HOH A1587 HOH A2116
SITE 1 AC4 5 SER A 485 SER A 487 HOH A1175 HOH A1695
SITE 2 AC4 5 HOH A1827
SITE 1 AC5 9 LEU A 70 ILE A 430 TYR A 435 LEU A 489
SITE 2 AC5 9 ILE A 490 ARG A 493 HIS A 494 HOH A1456
SITE 3 AC5 9 HOH A2236
SITE 1 AC6 8 PHE A 173 MET A 235 ARG A 252 GLY A 254
SITE 2 AC6 8 PHE A 476 SER A 554 TRP A 595 ARG A 643
SITE 1 AC7 7 ALA A 226 GLU A 227 PHE A 228 ILE A 276
SITE 2 AC7 7 HOH A1001 HOH A1244 HOH A1581
CRYST1 71.221 99.883 111.853 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 0.014041 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010012 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008940 0.00000
TER 5646 PRO A 710
MASTER 327 0 7 22 41 0 14 6 6931 1 52 55
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