HEADER TRANSFERASE/INHIBITOR 02-MAY-17 5VO6
TITLE CRYSTAL STRUCTURE OF JAK3 KINASE DOMAIN IN COMPLEX WITH A
TITLE 2 PYRROLOPYRIDAZINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 810-1100);
COMPND 5 SYNONYM: JANUS KINASE 3,JAK-3,LEUKOCYTE JANUS KINASE,L-JAK;
COMPND 6 EC: 2.7.10.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: JAK3;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS TRANSFER VECTOR
KEYWDS TRANSFERASE, TRANSFERASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.SACK
REVDAT 4 13-MAR-24 5VO6 1 REMARK
REVDAT 3 21-JUN-17 5VO6 1 JRNL
REVDAT 2 07-JUN-17 5VO6 1 JRNL
REVDAT 1 31-MAY-17 5VO6 0
JRNL AUTH J.HYNES,H.WU,J.KEMPSON,J.J.DUAN,Z.LU,B.JIANG,S.STACHURA,
JRNL AUTH 2 J.S.TOKARSKI,J.S.SACK,J.A.KHAN,J.S.LIPPY,R.F.ZHANG,S.PITT,
JRNL AUTH 3 G.SHEN,K.GILLOOLY,K.MCINTYRE,P.H.CARTER,J.C.BARRISH,
JRNL AUTH 4 S.G.NADLER,L.M.SALTER-CID,A.FURA,G.L.SCHIEVEN,W.J.PITTS,
JRNL AUTH 5 S.T.WROBLESKI
JRNL TITL DISCOVERY OF POTENT AND EFFICACIOUS PYRROLOPYRIDAZINES AS
JRNL TITL 2 DUAL JAK1/3 INHIBITORS.
JRNL REF BIOORG. MED. CHEM. LETT. V. 27 3101 2017
JRNL REFN ESSN 1464-3405
JRNL PMID 28539220
JRNL DOI 10.1016/J.BMCL.2017.05.043
REMARK 2
REMARK 2 RESOLUTION. 2.65 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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 9417
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.120
REMARK 3 FREE R VALUE TEST SET COUNT : 765
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 : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.96
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.05
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2608
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2120
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2398
REMARK 3 BIN R VALUE (WORKING SET) : 0.2065
REMARK 3 BIN FREE R VALUE : 0.2734
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.05
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 210
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 : 2121
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 17
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.15320
REMARK 3 B22 (A**2) : 1.81600
REMARK 3 B33 (A**2) : 4.33720
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.350
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.105
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.359
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.938
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.360
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 : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.851
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2203 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2991 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 743 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 44 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 343 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2203 ; 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 : 269 ; 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 : 2497 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.89
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.74
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 5VO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000227751.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9467
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 86.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.81300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 300K
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 23.67500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.48000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.52000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.48000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.67500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.52000
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 GLY A 808
REMARK 465 PRO A 809
REMARK 465 ALA A 810
REMARK 465 SER A 811
REMARK 465 GLN A 812
REMARK 465 ASP A 813
REMARK 465 PRO A 814
REMARK 465 LYS A 830
REMARK 465 GLY A 831
REMARK 465 ASN A 832
REMARK 465 PHE A 833
REMARK 465 ARG A 984
REMARK 465 GLU A 985
REMARK 465 PRO A 986
REMARK 465 GLY A 987
REMARK 465 GLN A 988
REMARK 465 SER A 989
REMARK 465 SER A 1040
REMARK 465 GLU A 1041
REMARK 465 ARG A 1042
REMARK 465 ASP A 1043
REMARK 465 SER A 1100
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 ILE A 816 CG1 CG2 CD1
REMARK 470 ASP A 863 CG OD1 OD2
REMARK 470 GLN A 864 CG CD OE1 NE2
REMARK 470 GLN A 865 CG CD OE1 NE2
REMARK 470 ARG A 866 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 869 CG CD OE1 NE2
REMARK 470 ARG A 895 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 896 CG CD OE1 NE2
REMARK 470 LEU A 898 CG CD1 CD2
REMARK 470 LYS A 935 CG CD CE NZ
REMARK 470 LYS A1026 CG CD CE NZ
REMARK 470 ARG A1049 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 ILE A 825 -53.72 -120.63
REMARK 500 ASP A 842 73.22 -114.73
REMARK 500 ARG A 948 -16.95 76.72
REMARK 500 ASP A 967 89.09 61.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9J4 A 4000
DBREF 5VO6 A 812 1100 UNP P52333 JAK3_HUMAN 812 1100
SEQADV 5VO6 GLY A 808 UNP P52333 EXPRESSION TAG
SEQADV 5VO6 PRO A 809 UNP P52333 EXPRESSION TAG
SEQADV 5VO6 ALA A 810 UNP P52333 EXPRESSION TAG
SEQADV 5VO6 SER A 811 UNP P52333 EXPRESSION TAG
SEQADV 5VO6 SER A 1040 UNP P52333 CYS 1040 ENGINEERED MUTATION
SEQADV 5VO6 SER A 1048 UNP P52333 CYS 1048 ENGINEERED MUTATION
SEQRES 1 A 293 GLY PRO ALA SER GLN ASP PRO THR ILE PHE GLU GLU ARG
SEQRES 2 A 293 HIS LEU LYS TYR ILE SER GLN LEU GLY LYS GLY ASN PHE
SEQRES 3 A 293 GLY SER VAL GLU LEU CYS ARG TYR ASP PRO LEU GLY ASP
SEQRES 4 A 293 ASN THR GLY ALA LEU VAL ALA VAL LYS GLN LEU GLN HIS
SEQRES 5 A 293 SER GLY PRO ASP GLN GLN ARG ASP PHE GLN ARG GLU ILE
SEQRES 6 A 293 GLN ILE LEU LYS ALA LEU HIS SER ASP PHE ILE VAL LYS
SEQRES 7 A 293 TYR ARG GLY VAL SER TYR GLY PRO GLY ARG GLN SER LEU
SEQRES 8 A 293 ARG LEU VAL MET GLU TYR LEU PRO SER GLY CYS LEU ARG
SEQRES 9 A 293 ASP PHE LEU GLN ARG HIS ARG ALA ARG LEU ASP ALA SER
SEQRES 10 A 293 ARG LEU LEU LEU TYR SER SER GLN ILE CYS LYS GLY MET
SEQRES 11 A 293 GLU TYR LEU GLY SER ARG ARG CYS VAL HIS ARG ASP LEU
SEQRES 12 A 293 ALA ALA ARG ASN ILE LEU VAL GLU SER GLU ALA HIS VAL
SEQRES 13 A 293 LYS ILE ALA ASP PHE GLY LEU ALA LYS LEU LEU PRO LEU
SEQRES 14 A 293 ASP LYS ASP TYR TYR VAL VAL ARG GLU PRO GLY GLN SER
SEQRES 15 A 293 PRO ILE PHE TRP TYR ALA PRO GLU SER LEU SER ASP ASN
SEQRES 16 A 293 ILE PHE SER ARG GLN SER ASP VAL TRP SER PHE GLY VAL
SEQRES 17 A 293 VAL LEU TYR GLU LEU PHE THR TYR CYS ASP LYS SER CYS
SEQRES 18 A 293 SER PRO SER ALA GLU PHE LEU ARG MET MET GLY SER GLU
SEQRES 19 A 293 ARG ASP VAL PRO ALA LEU SER ARG LEU LEU GLU LEU LEU
SEQRES 20 A 293 GLU GLU GLY GLN ARG LEU PRO ALA PRO PRO ALA CYS PRO
SEQRES 21 A 293 ALA GLU VAL HIS GLU LEU MET LYS LEU CYS TRP ALA PRO
SEQRES 22 A 293 SER PRO GLN ASP ARG PRO SER PHE SER ALA LEU GLY PRO
SEQRES 23 A 293 GLN LEU ASP MET LEU TRP SER
HET 9J4 A4000 28
HETNAM 9J4 4-{[(1R,3S)-3-AMINO-2,2,3-TRIMETHYLCYCLOPENTYL]AMINO}-
HETNAM 2 9J4 6-PHENYLPYRROLO[1,2-B]PYRIDAZINE-3-CARBOXAMIDE
FORMUL 2 9J4 C22 H27 N5 O
FORMUL 3 HOH *17(H2 O)
HELIX 1 AA1 GLY A 861 ALA A 877 1 17
HELIX 2 AA2 GLY A 894 LEU A 898 5 5
HELIX 3 AA3 CYS A 909 HIS A 917 1 9
HELIX 4 AA4 ARG A 918 LEU A 921 5 4
HELIX 5 AA5 ASP A 922 ARG A 943 1 22
HELIX 6 AA6 ALA A 951 ARG A 953 5 3
HELIX 7 AA7 ALA A 995 ASN A 1002 1 8
HELIX 8 AA8 ARG A 1006 THR A 1022 1 17
HELIX 9 AA9 ASP A 1025 CYS A 1028 5 4
HELIX 10 AB1 SER A 1029 GLY A 1039 1 11
HELIX 11 AB2 PRO A 1045 GLU A 1056 1 12
HELIX 12 AB3 PRO A 1067 TRP A 1078 1 12
HELIX 13 AB4 SER A 1087 LEU A 1098 1 12
SHEET 1 AA1 6 ILE A 816 GLU A 818 0
SHEET 2 AA1 6 TYR A 886 TYR A 891 1 O TYR A 891 N PHE A 817
SHEET 3 AA1 6 LEU A 900 GLU A 903 -1 O VAL A 901 N GLY A 888
SHEET 4 AA1 6 LEU A 851 GLN A 856 -1 N ALA A 853 O MET A 902
SHEET 5 AA1 6 SER A 835 TYR A 841 -1 N GLU A 837 O VAL A 854
SHEET 6 AA1 6 LEU A 822 GLY A 829 -1 N SER A 826 O LEU A 838
SHEET 1 AA2 2 CYS A 945 VAL A 946 0
SHEET 2 AA2 2 LYS A 972 LEU A 973 -1 O LYS A 972 N VAL A 946
SHEET 1 AA3 2 ILE A 955 SER A 959 0
SHEET 2 AA3 2 HIS A 962 ILE A 965 -1 O LYS A 964 N LEU A 956
SHEET 1 AA4 2 TYR A 980 VAL A 982 0
SHEET 2 AA4 2 ILE A1003 SER A1005 -1 O PHE A1004 N TYR A 981
SITE 1 AC1 14 ALA A 853 GLN A 858 HIS A 859 VAL A 884
SITE 2 AC1 14 MET A 902 GLU A 903 TYR A 904 LEU A 905
SITE 3 AC1 14 PRO A 906 GLY A 908 ARG A 953 ASN A 954
SITE 4 AC1 14 LEU A 956 HOH A4114
CRYST1 47.350 75.040 86.960 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 0.021119 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013326 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011500 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
