HEADER TRANSFERASE/TRANSFERASE INHIBITOR 18-JUL-17 5WI0
TITLE CRYSTAL STRUCTURE OF HUMAN NAMPT WITH FRAGMENT 2: 2-[(2-FLUOROPHENYL)
TITLE 2 AMINO]-6-PROPYLPYRIMIDIN-4(3H)-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NAMPT,PRE-B-CELL COLONY-ENHANCING FACTOR 1,PRE-B CELL-
COMPND 5 ENHANCING FACTOR,VISFATIN;
COMPND 6 EC: 2.4.2.12;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NAMPT, PBEF, PBEF1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293-6E
KEYWDS NAMPT, INHIBITOR, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.LONGENECKER,D.RAICH,A.V.KOREPANOVA
REVDAT 4 04-OCT-23 5WI0 1 REMARK
REVDAT 3 01-MAY-19 5WI0 1 JRNL
REVDAT 2 21-MAR-18 5WI0 1 REMARK
REVDAT 1 10-JAN-18 5WI0 0
JRNL AUTH A.KOREPANOVA,K.L.LONGENECKER,S.D.PRATT,S.C.PANCHAL,
JRNL AUTH 2 R.F.CLARK,M.LAKE,S.M.GOPALAKRISHNAN,D.RAICH,C.SUN,A.M.PETROS
JRNL TITL FRAGMENT-BASED DISCOVERY OF A POTENT NAMPT INHIBITOR.
JRNL REF BIOORG. MED. CHEM. LETT. V. 28 437 2018
JRNL REFN ESSN 1464-3405
JRNL PMID 29287958
JRNL DOI 10.1016/J.BMCL.2017.12.023
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 65452
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 3347
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.10
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.73
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4378
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2561
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4161
REMARK 3 BIN R VALUE (WORKING SET) : 0.2541
REMARK 3 BIN FREE R VALUE : 0.2956
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.96
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 217
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7422
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 629
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.90000
REMARK 3 B22 (A**2) : 1.55740
REMARK 3 B33 (A**2) : 4.34250
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.86000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.290
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.226
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.178
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.223
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.179
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.911
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.884
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 7636 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 10348 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2632 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 194 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1114 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 7636 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 972 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 9504 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.40
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.58
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5WI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000229060.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65534
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 82.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.16200
REMARK 200 R SYM (I) : 0.16200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.69700
REMARK 200 R SYM FOR SHELL (I) : 0.69700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2GVJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10K, SODIUM CHLORIDE, GLYCEROL,
REMARK 280 TRIS, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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,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 53.42800
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, 3
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
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 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 ASN A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 GLU A 6
REMARK 465 ALA A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 42
REMARK 465 LYS A 43
REMARK 465 THR A 44
REMARK 465 GLU A 45
REMARK 465 ASN A 46
REMARK 465 SER A 47
REMARK 465 LYS A 48
REMARK 465 LEU A 49
REMARK 465 ARG A 50
REMARK 465 LYS A 51
REMARK 465 VAL A 52
REMARK 465 LYS A 53
REMARK 465 GLU A 485
REMARK 465 LEU A 486
REMARK 465 GLU A 487
REMARK 465 ALA A 488
REMARK 465 ALA A 489
REMARK 465 HIS A 490
REMARK 465 HIS A 491
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 PRO B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 GLU B 6
REMARK 465 ALA B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 42
REMARK 465 LYS B 43
REMARK 465 THR B 44
REMARK 465 GLU B 45
REMARK 465 ASN B 46
REMARK 465 SER B 47
REMARK 465 LYS B 48
REMARK 465 LEU B 49
REMARK 465 ARG B 50
REMARK 465 LYS B 51
REMARK 465 VAL B 52
REMARK 465 LYS B 53
REMARK 465 GLU B 485
REMARK 465 LEU B 486
REMARK 465 GLU B 487
REMARK 465 ALA B 488
REMARK 465 ALA B 489
REMARK 465 HIS B 490
REMARK 465 HIS B 491
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 TYR A 231 -55.84 -127.72
REMARK 500 PHE A 269 54.70 -119.74
REMARK 500 TYR A 281 -52.84 -127.31
REMARK 500 GLU A 293 -75.64 -128.46
REMARK 500 ASP A 313 21.73 -142.38
REMARK 500 ASP A 416 70.80 -152.47
REMARK 500 TYR A 453 -165.27 -109.99
REMARK 500 CYS B 141 32.04 -99.92
REMARK 500 TYR B 231 -56.40 -128.07
REMARK 500 PHE B 269 54.70 -118.97
REMARK 500 TYR B 281 -51.75 -129.34
REMARK 500 GLU B 293 -75.67 -128.07
REMARK 500 ASP B 313 21.79 -141.21
REMARK 500 ASP B 416 71.51 -152.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1310 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A1311 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A1312 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A1313 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A1314 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A1315 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A1316 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A1317 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH A1318 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH A1319 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH A1320 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH B 908 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH B 909 DISTANCE = 6.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AQ1 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AQ1 B 501
DBREF 5WI0 A 1 491 UNP P43490 NAMPT_HUMAN 1 491
DBREF 5WI0 B 1 491 UNP P43490 NAMPT_HUMAN 1 491
SEQRES 1 A 491 MET ASN PRO ALA ALA GLU ALA GLU PHE ASN ILE LEU LEU
SEQRES 2 A 491 ALA THR ASP SER TYR LYS VAL THR HIS TYR LYS GLN TYR
SEQRES 3 A 491 PRO PRO ASN THR SER LYS VAL TYR SER TYR PHE GLU CYS
SEQRES 4 A 491 ARG GLU LYS LYS THR GLU ASN SER LYS LEU ARG LYS VAL
SEQRES 5 A 491 LYS TYR GLU GLU THR VAL PHE TYR GLY LEU GLN TYR ILE
SEQRES 6 A 491 LEU ASN LYS TYR LEU LYS GLY LYS VAL VAL THR LYS GLU
SEQRES 7 A 491 LYS ILE GLN GLU ALA LYS ASP VAL TYR LYS GLU HIS PHE
SEQRES 8 A 491 GLN ASP ASP VAL PHE ASN GLU LYS GLY TRP ASN TYR ILE
SEQRES 9 A 491 LEU GLU LYS TYR ASP GLY HIS LEU PRO ILE GLU ILE LYS
SEQRES 10 A 491 ALA VAL PRO GLU GLY PHE VAL ILE PRO ARG GLY ASN VAL
SEQRES 11 A 491 LEU PHE THR VAL GLU ASN THR ASP PRO GLU CYS TYR TRP
SEQRES 12 A 491 LEU THR ASN TRP ILE GLU THR ILE LEU VAL GLN SER TRP
SEQRES 13 A 491 TYR PRO ILE THR VAL ALA THR ASN SER ARG GLU GLN LYS
SEQRES 14 A 491 LYS ILE LEU ALA LYS TYR LEU LEU GLU THR SER GLY ASN
SEQRES 15 A 491 LEU ASP GLY LEU GLU TYR LYS LEU HIS ASP PHE GLY TYR
SEQRES 16 A 491 ARG GLY VAL SER SER GLN GLU THR ALA GLY ILE GLY ALA
SEQRES 17 A 491 SER ALA HIS LEU VAL ASN PHE LYS GLY THR ASP THR VAL
SEQRES 18 A 491 ALA GLY LEU ALA LEU ILE LYS LYS TYR TYR GLY THR LYS
SEQRES 19 A 491 ASP PRO VAL PRO GLY TYR SER VAL PRO ALA ALA GLU HIS
SEQRES 20 A 491 SER THR ILE THR ALA TRP GLY LYS ASP HIS GLU LYS ASP
SEQRES 21 A 491 ALA PHE GLU HIS ILE VAL THR GLN PHE SER SER VAL PRO
SEQRES 22 A 491 VAL SER VAL VAL SER ASP SER TYR ASP ILE TYR ASN ALA
SEQRES 23 A 491 CYS GLU LYS ILE TRP GLY GLU ASP LEU ARG HIS LEU ILE
SEQRES 24 A 491 VAL SER ARG SER THR GLN ALA PRO LEU ILE ILE ARG PRO
SEQRES 25 A 491 ASP SER GLY ASN PRO LEU ASP THR VAL LEU LYS VAL LEU
SEQRES 26 A 491 GLU ILE LEU GLY LYS LYS PHE PRO VAL THR GLU ASN SER
SEQRES 27 A 491 LYS GLY TYR LYS LEU LEU PRO PRO TYR LEU ARG VAL ILE
SEQRES 28 A 491 GLN GLY ASP GLY VAL ASP ILE ASN THR LEU GLN GLU ILE
SEQRES 29 A 491 VAL GLU GLY MET LYS GLN LYS MET TRP SER ILE GLU ASN
SEQRES 30 A 491 ILE ALA PHE GLY SER GLY GLY GLY LEU LEU GLN LYS LEU
SEQRES 31 A 491 THR ARG ASP LEU LEU ASN CYS SER PHE LYS CYS SER TYR
SEQRES 32 A 491 VAL VAL THR ASN GLY LEU GLY ILE ASN VAL PHE LYS ASP
SEQRES 33 A 491 PRO VAL ALA ASP PRO ASN LYS ARG SER LYS LYS GLY ARG
SEQRES 34 A 491 LEU SER LEU HIS ARG THR PRO ALA GLY ASN PHE VAL THR
SEQRES 35 A 491 LEU GLU GLU GLY LYS GLY ASP LEU GLU GLU TYR GLY GLN
SEQRES 36 A 491 ASP LEU LEU HIS THR VAL PHE LYS ASN GLY LYS VAL THR
SEQRES 37 A 491 LYS SER TYR SER PHE ASP GLU ILE ARG LYS ASN ALA GLN
SEQRES 38 A 491 LEU ASN ILE GLU LEU GLU ALA ALA HIS HIS
SEQRES 1 B 491 MET ASN PRO ALA ALA GLU ALA GLU PHE ASN ILE LEU LEU
SEQRES 2 B 491 ALA THR ASP SER TYR LYS VAL THR HIS TYR LYS GLN TYR
SEQRES 3 B 491 PRO PRO ASN THR SER LYS VAL TYR SER TYR PHE GLU CYS
SEQRES 4 B 491 ARG GLU LYS LYS THR GLU ASN SER LYS LEU ARG LYS VAL
SEQRES 5 B 491 LYS TYR GLU GLU THR VAL PHE TYR GLY LEU GLN TYR ILE
SEQRES 6 B 491 LEU ASN LYS TYR LEU LYS GLY LYS VAL VAL THR LYS GLU
SEQRES 7 B 491 LYS ILE GLN GLU ALA LYS ASP VAL TYR LYS GLU HIS PHE
SEQRES 8 B 491 GLN ASP ASP VAL PHE ASN GLU LYS GLY TRP ASN TYR ILE
SEQRES 9 B 491 LEU GLU LYS TYR ASP GLY HIS LEU PRO ILE GLU ILE LYS
SEQRES 10 B 491 ALA VAL PRO GLU GLY PHE VAL ILE PRO ARG GLY ASN VAL
SEQRES 11 B 491 LEU PHE THR VAL GLU ASN THR ASP PRO GLU CYS TYR TRP
SEQRES 12 B 491 LEU THR ASN TRP ILE GLU THR ILE LEU VAL GLN SER TRP
SEQRES 13 B 491 TYR PRO ILE THR VAL ALA THR ASN SER ARG GLU GLN LYS
SEQRES 14 B 491 LYS ILE LEU ALA LYS TYR LEU LEU GLU THR SER GLY ASN
SEQRES 15 B 491 LEU ASP GLY LEU GLU TYR LYS LEU HIS ASP PHE GLY TYR
SEQRES 16 B 491 ARG GLY VAL SER SER GLN GLU THR ALA GLY ILE GLY ALA
SEQRES 17 B 491 SER ALA HIS LEU VAL ASN PHE LYS GLY THR ASP THR VAL
SEQRES 18 B 491 ALA GLY LEU ALA LEU ILE LYS LYS TYR TYR GLY THR LYS
SEQRES 19 B 491 ASP PRO VAL PRO GLY TYR SER VAL PRO ALA ALA GLU HIS
SEQRES 20 B 491 SER THR ILE THR ALA TRP GLY LYS ASP HIS GLU LYS ASP
SEQRES 21 B 491 ALA PHE GLU HIS ILE VAL THR GLN PHE SER SER VAL PRO
SEQRES 22 B 491 VAL SER VAL VAL SER ASP SER TYR ASP ILE TYR ASN ALA
SEQRES 23 B 491 CYS GLU LYS ILE TRP GLY GLU ASP LEU ARG HIS LEU ILE
SEQRES 24 B 491 VAL SER ARG SER THR GLN ALA PRO LEU ILE ILE ARG PRO
SEQRES 25 B 491 ASP SER GLY ASN PRO LEU ASP THR VAL LEU LYS VAL LEU
SEQRES 26 B 491 GLU ILE LEU GLY LYS LYS PHE PRO VAL THR GLU ASN SER
SEQRES 27 B 491 LYS GLY TYR LYS LEU LEU PRO PRO TYR LEU ARG VAL ILE
SEQRES 28 B 491 GLN GLY ASP GLY VAL ASP ILE ASN THR LEU GLN GLU ILE
SEQRES 29 B 491 VAL GLU GLY MET LYS GLN LYS MET TRP SER ILE GLU ASN
SEQRES 30 B 491 ILE ALA PHE GLY SER GLY GLY GLY LEU LEU GLN LYS LEU
SEQRES 31 B 491 THR ARG ASP LEU LEU ASN CYS SER PHE LYS CYS SER TYR
SEQRES 32 B 491 VAL VAL THR ASN GLY LEU GLY ILE ASN VAL PHE LYS ASP
SEQRES 33 B 491 PRO VAL ALA ASP PRO ASN LYS ARG SER LYS LYS GLY ARG
SEQRES 34 B 491 LEU SER LEU HIS ARG THR PRO ALA GLY ASN PHE VAL THR
SEQRES 35 B 491 LEU GLU GLU GLY LYS GLY ASP LEU GLU GLU TYR GLY GLN
SEQRES 36 B 491 ASP LEU LEU HIS THR VAL PHE LYS ASN GLY LYS VAL THR
SEQRES 37 B 491 LYS SER TYR SER PHE ASP GLU ILE ARG LYS ASN ALA GLN
SEQRES 38 B 491 LEU ASN ILE GLU LEU GLU ALA ALA HIS HIS
HET AQ1 A 901 18
HET AQ1 B 501 18
HETNAM AQ1 2-[(2-FLUOROPHENYL)AMINO]-6-PROPYLPYRIMIDIN-4(3H)-ONE
FORMUL 3 AQ1 2(C13 H14 F N3 O)
FORMUL 5 HOH *629(H2 O)
HELIX 1 AA1 ASN A 10 ALA A 14 5 5
HELIX 2 AA2 ASP A 16 GLN A 25 5 10
HELIX 3 AA3 GLY A 61 LEU A 70 1 10
HELIX 4 AA4 THR A 76 GLN A 92 1 17
HELIX 5 AA5 ASN A 97 ASP A 109 1 13
HELIX 6 AA6 ASP A 138 TYR A 142 5 5
HELIX 7 AA7 TRP A 143 ILE A 148 1 6
HELIX 8 AA8 ILE A 148 GLN A 154 1 7
HELIX 9 AA9 SER A 155 GLY A 181 1 27
HELIX 10 AB1 GLY A 185 TYR A 188 5 4
HELIX 11 AB2 SER A 200 VAL A 213 1 14
HELIX 12 AB3 VAL A 221 TYR A 231 1 11
HELIX 13 AB4 GLU A 246 ALA A 252 1 7
HELIX 14 AB5 TRP A 253 ASP A 256 5 4
HELIX 15 AB6 HIS A 257 PHE A 269 1 13
HELIX 16 AB7 ASP A 282 LYS A 289 1 8
HELIX 17 AB8 LEU A 295 ILE A 299 5 5
HELIX 18 AB9 ASN A 316 PHE A 332 1 17
HELIX 19 AC1 ASP A 357 LYS A 371 1 15
HELIX 20 AC2 SER A 374 GLU A 376 5 3
HELIX 21 AC3 GLY A 383 GLN A 388 1 6
HELIX 22 AC4 ASP A 420 ARG A 424 5 5
HELIX 23 AC5 GLY A 446 LEU A 450 5 5
HELIX 24 AC6 SER A 472 ALA A 480 1 9
HELIX 25 AC7 ASN B 10 ALA B 14 5 5
HELIX 26 AC8 ASP B 16 GLN B 25 5 10
HELIX 27 AC9 GLY B 61 LEU B 70 1 10
HELIX 28 AD1 THR B 76 GLN B 92 1 17
HELIX 29 AD2 ASN B 97 ASP B 109 1 13
HELIX 30 AD3 ASP B 138 TYR B 142 5 5
HELIX 31 AD4 TRP B 143 ILE B 148 1 6
HELIX 32 AD5 ILE B 148 GLN B 154 1 7
HELIX 33 AD6 SER B 155 GLY B 181 1 27
HELIX 34 AD7 GLY B 185 TYR B 188 5 4
HELIX 35 AD8 SER B 200 VAL B 213 1 14
HELIX 36 AD9 VAL B 221 TYR B 231 1 11
HELIX 37 AE1 GLU B 246 ALA B 252 1 7
HELIX 38 AE2 TRP B 253 ASP B 256 5 4
HELIX 39 AE3 HIS B 257 PHE B 269 1 13
HELIX 40 AE4 ASP B 282 LYS B 289 1 8
HELIX 41 AE5 LEU B 295 ILE B 299 5 5
HELIX 42 AE6 ASN B 316 PHE B 332 1 17
HELIX 43 AE7 ASP B 357 LYS B 371 1 15
HELIX 44 AE8 SER B 374 GLU B 376 5 3
HELIX 45 AE9 GLY B 383 GLN B 388 1 6
HELIX 46 AF1 ASP B 420 ARG B 424 5 5
HELIX 47 AF2 GLY B 446 GLU B 451 5 6
HELIX 48 AF3 SER B 472 ALA B 480 1 9
SHEET 1 AA1 7 LEU A 409 ASN A 412 0
SHEET 2 AA1 7 CYS A 397 THR A 406 -1 N VAL A 404 O ILE A 411
SHEET 3 AA1 7 THR A 30 CYS A 39 -1 N TYR A 34 O TYR A 403
SHEET 4 AA1 7 PHE A 132 ASN A 136 -1 O VAL A 134 N SER A 35
SHEET 5 AA1 7 ILE A 114 ALA A 118 -1 N GLU A 115 O GLU A 135
SHEET 6 AA1 7 HIS A 459 LYS A 463 -1 O HIS A 459 N ALA A 118
SHEET 7 AA1 7 LYS A 466 VAL A 467 -1 O LYS A 466 N LYS A 463
SHEET 1 AA2 2 GLU A 56 VAL A 58 0
SHEET 2 AA2 2 VAL A 124 PRO A 126 -1 O ILE A 125 N THR A 57
SHEET 1 AA3 5 LEU A 190 ASP A 192 0
SHEET 2 AA3 5 ILE A 378 SER A 382 1 O PHE A 380 N HIS A 191
SHEET 3 AA3 5 LEU A 348 GLN A 352 1 N GLN A 352 O ALA A 379
SHEET 4 AA3 5 LEU A 308 ARG A 311 1 N ILE A 310 O ARG A 349
SHEET 5 AA3 5 VAL A 274 VAL A 277 1 N VAL A 274 O ILE A 309
SHEET 1 AA4 2 THR A 335 GLU A 336 0
SHEET 2 AA4 2 LYS A 342 LEU A 343 -1 O LEU A 343 N THR A 335
SHEET 1 AA5 2 SER A 431 ARG A 434 0
SHEET 2 AA5 2 PHE A 440 LEU A 443 -1 O VAL A 441 N HIS A 433
SHEET 1 AA6 7 LEU B 409 ASN B 412 0
SHEET 2 AA6 7 CYS B 397 THR B 406 -1 N VAL B 404 O ILE B 411
SHEET 3 AA6 7 THR B 30 CYS B 39 -1 N TYR B 34 O TYR B 403
SHEET 4 AA6 7 PHE B 132 ASN B 136 -1 O VAL B 134 N SER B 35
SHEET 5 AA6 7 ILE B 114 ALA B 118 -1 N GLU B 115 O GLU B 135
SHEET 6 AA6 7 HIS B 459 LYS B 463 -1 O HIS B 459 N ALA B 118
SHEET 7 AA6 7 LYS B 466 VAL B 467 -1 O LYS B 466 N LYS B 463
SHEET 1 AA7 2 GLU B 56 VAL B 58 0
SHEET 2 AA7 2 VAL B 124 PRO B 126 -1 O ILE B 125 N THR B 57
SHEET 1 AA8 5 LEU B 190 ASP B 192 0
SHEET 2 AA8 5 ILE B 378 SER B 382 1 O PHE B 380 N HIS B 191
SHEET 3 AA8 5 LEU B 348 GLN B 352 1 N GLN B 352 O ALA B 379
SHEET 4 AA8 5 LEU B 308 ARG B 311 1 N ILE B 310 O ARG B 349
SHEET 5 AA8 5 VAL B 274 VAL B 277 1 N VAL B 274 O ILE B 309
SHEET 1 AA9 2 THR B 335 GLU B 336 0
SHEET 2 AA9 2 LYS B 342 LEU B 343 -1 O LEU B 343 N THR B 335
SHEET 1 AB1 2 SER B 431 ARG B 434 0
SHEET 2 AB1 2 PHE B 440 LEU B 443 -1 O VAL B 441 N HIS B 433
SITE 1 AC1 11 HIS A 191 PHE A 193 ARG A 196 ASP A 219
SITE 2 AC1 11 SER A 241 VAL A 242 ALA A 244 SER A 275
SITE 3 AC1 11 ARG A 311 ASP B 16 TYR B 18
SITE 1 AC2 12 ASP A 16 TYR A 18 HIS B 191 PHE B 193
SITE 2 AC2 12 ARG B 196 ASP B 219 SER B 241 VAL B 242
SITE 3 AC2 12 ALA B 244 SER B 275 ARG B 311 HOH B 612
CRYST1 61.226 106.856 82.881 90.00 96.83 90.00 P 1 21 1 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 0.016333 0.000000 0.001956 0.00000
SCALE2 0.000000 0.009358 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012152 0.00000
(ATOM LINES ARE NOT SHOWN.)
END