HEADER TRANSFERASE/TRANSFERASE INHIBITOR 19-OCT-16 5TOZ
TITLE JAK3 WITH COVALENT INHIBITOR PF-06651600
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 812-1124;
COMPND 5 SYNONYM: JANUS KINASE 3,JAK-3,LEUKOCYTE JANUS KINASE,L-JAK;
COMPND 6 EC: 2.7.10.2;
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: 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
KEYWDS JAK3 COVALENT KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.F.VAJDOS
REVDAT 3 22-NOV-17 5TOZ 1 REMARK
REVDAT 2 28-DEC-16 5TOZ 1 JRNL REMARK
REVDAT 1 09-NOV-16 5TOZ 0
JRNL AUTH J.B.TELLIEZ,M.E.DOWTY,L.WANG,J.JUSSIF,T.LIN,L.LI,E.MOY,
JRNL AUTH 2 P.BALBO,W.LI,Y.ZHAO,K.CROUSE,C.DICKINSON,P.SYMANOWICZ,
JRNL AUTH 3 M.HEGEN,M.E.BANKER,F.VINCENT,R.UNWALLA,S.LIANG,A.M.GILBERT,
JRNL AUTH 4 M.F.BROWN,M.HAYWARD,J.MONTGOMERY,X.YANG,J.BAUMAN,
JRNL AUTH 5 J.I.TRUJILLO,A.CASIMIRO-GARCIA,F.F.VAJDOS,L.LEUNG,
JRNL AUTH 6 K.F.GEOGHEGAN,A.QUAZI,D.XUAN,L.JONES,E.HETT,K.WRIGHT,
JRNL AUTH 7 J.D.CLARK,A.THORARENSEN
JRNL TITL DISCOVERY OF A JAK3-SELECTIVE INHIBITOR: FUNCTIONAL
JRNL TITL 2 DIFFERENTIATION OF JAK3-SELECTIVE INHIBITION OVER PAN-JAK OR
JRNL TITL 3 JAK1-SELECTIVE INHIBITION.
JRNL REF ACS CHEM. BIOL. V. 11 3442 2016
JRNL REFN ESSN 1554-8937
JRNL PMID 27791347
JRNL DOI 10.1021/ACSCHEMBIO.6B00677
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 23268
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170
REMARK 3 FREE R VALUE TEST SET COUNT : 1204
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 : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.52
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2705
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2072
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2566
REMARK 3 BIN R VALUE (WORKING SET) : 0.2062
REMARK 3 BIN FREE R VALUE : 0.2251
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.14
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 139
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 : 2190
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 232
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.91400
REMARK 3 B22 (A**2) : 9.90200
REMARK 3 B33 (A**2) : 7.01200
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) : 0.220
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.166
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.143
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.154
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.138
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 : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2270 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3075 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 783 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 47 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 345 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2270 ; 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 : 275 ; 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 : 2766 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.99
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.18
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.27
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 5TOZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224568.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23329
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 47.868
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.35900
REMARK 200 R SYM FOR SHELL (I) : NULL
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: NULL
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 (%): 44.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-3350, 0.2 M AMMONIUM SULFATE,
REMARK 280 PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 23.93400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.90550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.82000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.90550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.93400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.82000
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 804
REMARK 465 GLY A 805
REMARK 465 HIS A 806
REMARK 465 HIS A 807
REMARK 465 HIS A 808
REMARK 465 HIS A 809
REMARK 465 HIS A 810
REMARK 465 HIS A 811
REMARK 465 GLN A 812
REMARK 465 ASP A 813
REMARK 465 PRO A 814
REMARK 465 PRO A 893
REMARK 465 GLY A 894
REMARK 465 ARG A 895
REMARK 465 GLN A 896
REMARK 465 GLY A 1039
REMARK 465 CYS A 1040
REMARK 465 GLU A 1041
REMARK 465 ARG A 1042
REMARK 465 GLY A 1101
REMARK 465 SER A 1102
REMARK 465 ARG A 1103
REMARK 465 GLY A 1104
REMARK 465 CYS A 1105
REMARK 465 GLU A 1106
REMARK 465 THR A 1107
REMARK 465 HIS A 1108
REMARK 465 ALA A 1109
REMARK 465 PHE A 1110
REMARK 465 THR A 1111
REMARK 465 ALA A 1112
REMARK 465 HIS A 1113
REMARK 465 PRO A 1114
REMARK 465 GLU A 1115
REMARK 465 GLY A 1116
REMARK 465 LYS A 1117
REMARK 465 HIS A 1118
REMARK 465 HIS A 1119
REMARK 465 SER A 1120
REMARK 465 LEU A 1121
REMARK 465 SER A 1122
REMARK 465 PHE A 1123
REMARK 465 SER A 1124
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 CD1
REMARK 470 ASN A 832 CG OD1 ND2
REMARK 470 PHE A 833 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 866 NE CZ NH1 NH2
REMARK 470 ARG A 870 CZ NH1 NH2
REMARK 470 LYS A 935 NZ
REMARK 470 ARG A 984 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 985 CG CD OE1 OE2
REMARK 470 LYS A1026 CD CE NZ
REMARK 470 ASP A1043 CG OD1 OD2
REMARK 470 GLU A1055 OE1 OE2
REMARK 470 GLU A1069 OE2
REMARK 470 MET A1097 SD CE
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 PHE A 833 11.97 57.52
REMARK 500 ASP A 842 66.73 -118.21
REMARK 500 ARG A 948 -7.30 70.21
REMARK 500 ASP A 967 83.47 55.17
REMARK 500 TRP A1099 103.95 88.45
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 7H4 A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1202
DBREF 5TOZ A 812 1124 UNP P52333 JAK3_HUMAN 812 1124
SEQADV 5TOZ MET A 804 UNP P52333 INITIATING METHIONINE
SEQADV 5TOZ GLY A 805 UNP P52333 EXPRESSION TAG
SEQADV 5TOZ HIS A 806 UNP P52333 EXPRESSION TAG
SEQADV 5TOZ HIS A 807 UNP P52333 EXPRESSION TAG
SEQADV 5TOZ HIS A 808 UNP P52333 EXPRESSION TAG
SEQADV 5TOZ HIS A 809 UNP P52333 EXPRESSION TAG
SEQADV 5TOZ HIS A 810 UNP P52333 EXPRESSION TAG
SEQADV 5TOZ HIS A 811 UNP P52333 EXPRESSION TAG
SEQADV 5TOZ SER A 1048 UNP P52333 CYS 1048 CONFLICT
SEQRES 1 A 321 MET GLY HIS HIS HIS HIS HIS HIS GLN ASP PRO THR ILE
SEQRES 2 A 321 PHE GLU GLU ARG HIS LEU LYS TYR ILE SER GLN LEU GLY
SEQRES 3 A 321 LYS GLY ASN PHE GLY SER VAL GLU LEU CYS ARG TYR ASP
SEQRES 4 A 321 PRO LEU GLY ASP ASN THR GLY ALA LEU VAL ALA VAL LYS
SEQRES 5 A 321 GLN LEU GLN HIS SER GLY PRO ASP GLN GLN ARG ASP PHE
SEQRES 6 A 321 GLN ARG GLU ILE GLN ILE LEU LYS ALA LEU HIS SER ASP
SEQRES 7 A 321 PHE ILE VAL LYS TYR ARG GLY VAL SER TYR GLY PRO GLY
SEQRES 8 A 321 ARG GLN SER LEU ARG LEU VAL MET GLU TYR LEU PRO SER
SEQRES 9 A 321 GLY CYS LEU ARG ASP PHE LEU GLN ARG HIS ARG ALA ARG
SEQRES 10 A 321 LEU ASP ALA SER ARG LEU LEU LEU TYR SER SER GLN ILE
SEQRES 11 A 321 CYS LYS GLY MET GLU TYR LEU GLY SER ARG ARG CYS VAL
SEQRES 12 A 321 HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU VAL GLU SER
SEQRES 13 A 321 GLU ALA HIS VAL LYS ILE ALA ASP PHE GLY LEU ALA LYS
SEQRES 14 A 321 LEU LEU PRO LEU ASP LYS ASP TYR TYR VAL VAL ARG GLU
SEQRES 15 A 321 PRO GLY GLN SER PRO ILE PHE TRP TYR ALA PRO GLU SER
SEQRES 16 A 321 LEU SER ASP ASN ILE PHE SER ARG GLN SER ASP VAL TRP
SEQRES 17 A 321 SER PHE GLY VAL VAL LEU TYR GLU LEU PHE THR TYR CYS
SEQRES 18 A 321 ASP LYS SER CYS SER PRO SER ALA GLU PHE LEU ARG MET
SEQRES 19 A 321 MET GLY CYS GLU ARG ASP VAL PRO ALA LEU SER ARG LEU
SEQRES 20 A 321 LEU GLU LEU LEU GLU GLU GLY GLN ARG LEU PRO ALA PRO
SEQRES 21 A 321 PRO ALA CYS PRO ALA GLU VAL HIS GLU LEU MET LYS LEU
SEQRES 22 A 321 CYS TRP ALA PRO SER PRO GLN ASP ARG PRO SER PHE SER
SEQRES 23 A 321 ALA LEU GLY PRO GLN LEU ASP MET LEU TRP SER GLY SER
SEQRES 24 A 321 ARG GLY CYS GLU THR HIS ALA PHE THR ALA HIS PRO GLU
SEQRES 25 A 321 GLY LYS HIS HIS SER LEU SER PHE SER
HET 7H4 A1201 21
HET SO4 A1202 5
HETNAM 7H4 1-{(2S,5R)-2-METHYL-5-[(7H-PYRROLO[2,3-D]PYRIMIDIN-4-
HETNAM 2 7H4 YL)AMINO]PIPERIDIN-1-YL}PROPAN-1-ONE
HETNAM SO4 SULFATE ION
FORMUL 2 7H4 C15 H21 N5 O
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *232(H2 O)
HELIX 1 AA1 GLU A 818 ARG A 820 5 3
HELIX 2 AA2 GLY A 861 ALA A 877 1 17
HELIX 3 AA3 CYS A 909 ARG A 918 1 10
HELIX 4 AA4 ASP A 922 ARG A 943 1 22
HELIX 5 AA5 ALA A 951 ARG A 953 5 3
HELIX 6 AA6 PRO A 990 TYR A 994 5 5
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 MET A 1038 1 10
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 1081 ARG A 1085 5 5
HELIX 14 AB5 SER A 1087 SER A 1100 1 14
SHEET 1 AA1 5 LEU A 822 LYS A 830 0
SHEET 2 AA1 5 GLY A 834 TYR A 841 -1 O ARG A 840 N LYS A 823
SHEET 3 AA1 5 ALA A 850 LEU A 857 -1 O ALA A 850 N TYR A 841
SHEET 4 AA1 5 ARG A 899 GLU A 903 -1 O MET A 902 N ALA A 853
SHEET 5 AA1 5 TYR A 886 SER A 890 -1 N ARG A 887 O VAL A 901
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
LINK SG CYS A 909 C9 7H4 A1201 1555 1555 1.81
SITE 1 AC1 14 LEU A 828 GLY A 829 ALA A 853 GLU A 903
SITE 2 AC1 14 TYR A 904 LEU A 905 GLY A 908 CYS A 909
SITE 3 AC1 14 ASP A 912 ARG A 953 LEU A 956 HOH A1307
SITE 4 AC1 14 HOH A1442 HOH A1464
SITE 1 AC2 4 ARG A 911 HOH A1370 HOH A1383 HOH A1400
CRYST1 47.868 75.640 89.811 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 0.020891 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011134 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
