HEADER TRANSFERASE/TRANSFERASE INHIBITOR 04-NOV-16 5TTS
TITLE JAK3 WITH COVALENT INHIBITOR 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (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;
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_CELL_LINE: SF21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS KINASE, COVALENT, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.F.VAJDOS
REVDAT 2 22-MAR-17 5TTS 1 JRNL
REVDAT 1 22-FEB-17 5TTS 0
JRNL AUTH A.THORARENSEN,M.E.DOWTY,M.E.BANKER,B.JUBA,J.JUSSIF,T.LIN,
JRNL AUTH 2 F.VINCENT,R.M.CZERWINSKI,A.CASIMIRO-GARCIA,R.UNWALLA,
JRNL AUTH 3 J.I.TRUJILLO,S.LIANG,P.BALBO,Y.CHE,A.M.GILBERT,M.F.BROWN,
JRNL AUTH 4 M.HAYWARD,J.MONTGOMERY,L.LEUNG,X.YANG,S.SOUCY,M.HEGEN,J.COE,
JRNL AUTH 5 J.LANGILLE,F.VAJDOS,J.CHRENCIK,J.B.TELLIEZ
JRNL TITL DESIGN OF A JANUS KINASE 3 (JAK3) SPECIFIC INHIBITOR
JRNL TITL 2 1-((2S,5R)-5-((7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)AMINO)
JRNL TITL 3 -2-METHYLPIPERIDIN-1-YL)PROP-2-EN-1-ONE (PF-06651600)
JRNL TITL 4 ALLOWING FOR THE INTERROGATION OF JAK3 SIGNALING IN HUMANS.
JRNL REF J. MED. CHEM. V. 60 1971 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28139931
JRNL DOI 10.1021/ACS.JMEDCHEM.6B01694
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
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) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 13995
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 711
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 : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.53
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.41
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2790
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2383
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2638
REMARK 3 BIN R VALUE (WORKING SET) : 0.2365
REMARK 3 BIN FREE R VALUE : 0.2658
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.45
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 152
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 : 2162
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 184
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.78790
REMARK 3 B22 (A**2) : -1.90970
REMARK 3 B33 (A**2) : 0.12180
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) : 0.293
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.402
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.262
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.342
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.253
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 : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2235 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3022 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 772 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 47 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 338 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2235 ; 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 : 271 ; 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 : 2650 ; 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) : 3.06
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.48
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 5TTS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000224820.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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 FR-E+ DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14122
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.39100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 44.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M (NH4)2SO4, 2%
REMARK 280 PHENYLUREA, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 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 23.68450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.77500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.87700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.77500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.68450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.87700
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 HIS A 859
REMARK 465 SER A 860
REMARK 465 GLY A 892
REMARK 465 PRO A 893
REMARK 465 GLY A 894
REMARK 465 ARG A 895
REMARK 465 GLN A 896
REMARK 465 SER A 897
REMARK 465 GLY A 1039
REMARK 465 CYS A 1040
REMARK 465 GLU A 1041
REMARK 465 ARG A 1042
REMARK 465 ASP A 1043
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 TYR A 981 CG CD1 CD2 CE1 CE2 CZ OH
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 GLU A1055 OE1 OE2
REMARK 470 GLU A1069 OE2
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 ASN A 832 122.31 -29.01
REMARK 500 ASP A 842 71.97 -118.60
REMARK 500 ARG A 948 -11.39 72.69
REMARK 500 ALA A 966 -169.11 -129.00
REMARK 500 ASP A 967 82.34 47.63
REMARK 500 TRP A1099 141.02 95.28
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 A4280 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A4281 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A4282 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH A4283 DISTANCE = 7.73 ANGSTROMS
REMARK 525 HOH A4284 DISTANCE = 8.93 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7KU A 4000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TTU RELATED DB: PDB
REMARK 900 RELATED ID: 5TTV RELATED DB: PDB
DBREF 5TTS A 812 1124 UNP P52333 JAK3_HUMAN 812 1124
SEQADV 5TTS MET A 804 UNP P52333 INITIATING METHIONINE
SEQADV 5TTS GLY A 805 UNP P52333 EXPRESSION TAG
SEQADV 5TTS HIS A 806 UNP P52333 EXPRESSION TAG
SEQADV 5TTS HIS A 807 UNP P52333 EXPRESSION TAG
SEQADV 5TTS HIS A 808 UNP P52333 EXPRESSION TAG
SEQADV 5TTS HIS A 809 UNP P52333 EXPRESSION TAG
SEQADV 5TTS HIS A 810 UNP P52333 EXPRESSION TAG
SEQADV 5TTS HIS A 811 UNP P52333 EXPRESSION TAG
SEQADV 5TTS SER A 1048 UNP P52333 CYS 1048 ENGINEERED MUTATION
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 7KU A4000 20
HETNAM 7KU 1-{(3R)-3-[(7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)
HETNAM 2 7KU AMINO]PIPERIDIN-1-YL}PROPAN-1-ONE
FORMUL 2 7KU C14 H19 N5 O
FORMUL 3 HOH *184(H2 O)
HELIX 1 AA1 GLU A 818 ARG A 820 5 3
HELIX 2 AA2 PRO A 862 ALA A 877 1 16
HELIX 3 AA3 CYS A 909 HIS A 917 1 9
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 LEU A 1098 1 12
SHEET 1 AA1 5 LEU A 822 GLY A 831 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 GLY A 888 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 C1 7KU A4000 1555 1555 1.81
CISPEP 1 ASN A 832 PHE A 833 0 1.92
SITE 1 AC1 11 LEU A 828 GLY A 829 ALA A 853 GLU A 903
SITE 2 AC1 11 LEU A 905 GLY A 908 CYS A 909 ARG A 911
SITE 3 AC1 11 ASP A 912 LEU A 956 HOH A4122
CRYST1 47.369 75.754 89.550 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 0.021111 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013201 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011167 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
