HEADER TRANSFERASE/TRANSFERASE INHIBITOR 13-JUL-12 4G31
TITLE CRYSTAL STRUCTURE OF GSK6414 BOUND TO PERK (R587-R1092, DELETE A660-
TITLE 2 T867) AT 2.28 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 588-660,869-1093;
COMPND 5 SYNONYM: PKR-LIKE ENDOPLASMIC RETICULUM KINASE, PERK, PANCREATIC
COMPND 6 EIF2-ALPHA KINASE, HSPEK;
COMPND 7 EC: 2.7.11.1;
COMPND 8 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: EIF2AK3, PEK, PERK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DELETION MUTANT, CATALYTIC DOMAIN, SYNTHETIC INHIBITOR, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.T.GAMPE,J.M.AXTEN
REVDAT 5 28-FEB-24 4G31 1 REMARK SEQADV
REVDAT 4 15-NOV-17 4G31 1 REMARK
REVDAT 3 26-JUL-17 4G31 1 SOURCE
REVDAT 2 05-SEP-12 4G31 1 JRNL
REVDAT 1 08-AUG-12 4G31 0
JRNL AUTH J.M.AXTEN,J.R.MEDINA,Y.FENG,A.SHU,S.P.ROMERIL,S.W.GRANT,
JRNL AUTH 2 W.H.LI,D.A.HEERDING,E.MINTHORN,T.MENCKEN,C.ATKINS,Q.LIU,
JRNL AUTH 3 S.RABINDRAN,R.KUMAR,X.HONG,A.GOETZ,T.STANLEY,J.D.TAYLOR,
JRNL AUTH 4 S.D.SIGETHY,G.H.TOMBERLIN,A.M.HASSELL,K.M.KAHLER,
JRNL AUTH 5 L.M.SHEWCHUK,R.T.GAMPE
JRNL TITL DISCOVERY OF
JRNL TITL 2 7-METHYL-5-(1-{[3-(TRIFLUOROMETHYL)PHENYL]ACETYL}-2,
JRNL TITL 3 3-DIHYDRO-1H-INDOL-5-YL)-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE
JRNL TITL 4 (GSK2606414), A POTENT AND SELECTIVE FIRST-IN-CLASS
JRNL TITL 5 INHIBITOR OF PROTEIN KINASE R (PKR)-LIKE ENDOPLASMIC
JRNL TITL 6 RETICULUM KINASE (PERK).
JRNL REF J.MED.CHEM. V. 55 7193 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22827572
JRNL DOI 10.1021/JM300713S
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 22515
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.240
REMARK 3 FREE R VALUE TEST SET COUNT : 730
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 42.6571 - 3.8980 0.99 4572 132 0.1915 0.2143
REMARK 3 2 3.8980 - 3.0942 1.00 4405 134 0.1874 0.2287
REMARK 3 3 3.0942 - 2.7032 1.00 4301 137 0.2244 0.2509
REMARK 3 4 2.7032 - 2.4561 1.00 4269 157 0.2403 0.3293
REMARK 3 5 2.4561 - 2.2800 1.00 4238 170 0.2725 0.3234
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 57.25
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.840
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.66930
REMARK 3 B22 (A**2) : 7.66930
REMARK 3 B33 (A**2) : -15.33850
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2083
REMARK 3 ANGLE : 0.989 2819
REMARK 3 CHIRALITY : 0.067 305
REMARK 3 PLANARITY : 0.005 357
REMARK 3 DIHEDRAL : 15.362 787
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4G31 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073674.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22515
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 14.50
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.10
REMARK 200 R MERGE FOR SHELL (I) : 0.39500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.710
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BTP, PH 7.0, 3.5-4.9 M LINEAR
REMARK 280 GRADIENT OF AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.94367
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 105.88733
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.41550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 132.35917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 26.47183
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 52.94367
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 105.88733
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 132.35917
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 79.41550
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 26.47183
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1359 LIES ON A SPECIAL POSITION.
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 602
REMARK 465 PHE A 603
REMARK 465 THR A 870
REMARK 465 THR A 871
REMARK 465 GLU A 872
REMARK 465 LYS A 873
REMARK 465 LEU A 874
REMARK 465 GLN A 875
REMARK 465 PRO A 876
REMARK 465 SER A 877
REMARK 465 SER A 878
REMARK 465 PRO A 879
REMARK 465 THR A 959
REMARK 465 ALA A 960
REMARK 465 MET A 961
REMARK 465 ASP A 962
REMARK 465 GLN A 963
REMARK 465 ASP A 964
REMARK 465 GLU A 965
REMARK 465 GLU A 966
REMARK 465 GLU A 967
REMARK 465 GLN A 968
REMARK 465 THR A 969
REMARK 465 VAL A 970
REMARK 465 LEU A 971
REMARK 465 THR A 972
REMARK 465 PRO A 973
REMARK 465 MET A 974
REMARK 465 PRO A 975
REMARK 465 ALA A 976
REMARK 465 TYR A 977
REMARK 465 ALA A 978
REMARK 465 ARG A 979
REMARK 465 HIS A 980
REMARK 465 THR A 981
REMARK 465 GLY A 982
REMARK 465 GLN A 983
REMARK 465 VAL A 984
REMARK 465 ASP A 1080
REMARK 465 PHE A 1081
REMARK 465 PRO A 1082
REMARK 465 GLY A 1083
REMARK 465 LYS A 1084
REMARK 465 THR A 1085
REMARK 465 VAL A 1086
REMARK 465 LEU A 1087
REMARK 465 ARG A 1088
REMARK 465 GLN A 1089
REMARK 465 ARG A 1090
REMARK 465 SER A 1091
REMARK 465 ARG A 1092
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 LEU A 589 CD1 CD2
REMARK 470 ARG A 600 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 624 CD NE CZ NH1 NH2
REMARK 470 ASN A 627 CG OD1 ND2
REMARK 470 ARG A 628 CD NE CZ NH1 NH2
REMARK 470 GLU A 629 CG CD OE1 OE2
REMARK 470 LYS A 634 CD CE NZ
REMARK 470 LYS A 868 CG CD CE NZ
REMARK 470 ASN A 869 CG OD1 ND2
REMARK 470 LYS A 880 CG CD CE NZ
REMARK 470 LYS A 892 CD CE NZ
REMARK 470 GLU A 909 OE1 OE2
REMARK 470 ASP A 947 CG OD1 OD2
REMARK 470 VAL A 958 CG1 CG2
REMARK 470 LYS A 987 NZ
REMARK 470 SER A 999 OG
REMARK 470 LEU A1041 CG CD1 CD2
REMARK 470 GLN A1044 OE1 NE2
REMARK 470 ASP A1078 CG OD1 OD2
REMARK 470 LEU A1079 CG CD1 CD2
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 GLN A 596 152.21 174.30
REMARK 500 ARG A 935 -18.64 80.73
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 GOL A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0WH A 1102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QD2 RELATED DB: PDB
REMARK 900 RELATED ID: 4G34 RELATED DB: PDB
DBREF 4G31 A 587 659 UNP Q9NZJ5 E2AK3_HUMAN 588 660
DBREF 4G31 A 868 1092 UNP Q9NZJ5 E2AK3_HUMAN 869 1093
SEQADV 4G31 GLY A 586 UNP Q9NZJ5 EXPRESSION TAG
SEQRES 1 A 299 GLY ARG TYR LEU THR ASP PHE GLU PRO ILE GLN CYS LEU
SEQRES 2 A 299 GLY ARG GLY GLY PHE GLY VAL VAL PHE GLU ALA LYS ASN
SEQRES 3 A 299 LYS VAL ASP ASP CYS ASN TYR ALA ILE LYS ARG ILE ARG
SEQRES 4 A 299 LEU PRO ASN ARG GLU LEU ALA ARG GLU LYS VAL MET ARG
SEQRES 5 A 299 GLU VAL LYS ALA LEU ALA LYS LEU GLU HIS PRO GLY ILE
SEQRES 6 A 299 VAL ARG TYR PHE ASN ALA TRP LEU GLU LYS ASN THR THR
SEQRES 7 A 299 GLU LYS LEU GLN PRO SER SER PRO LYS VAL TYR LEU TYR
SEQRES 8 A 299 ILE GLN MET GLN LEU CYS ARG LYS GLU ASN LEU LYS ASP
SEQRES 9 A 299 TRP MET ASN GLY ARG CYS THR ILE GLU GLU ARG GLU ARG
SEQRES 10 A 299 SER VAL CYS LEU HIS ILE PHE LEU GLN ILE ALA GLU ALA
SEQRES 11 A 299 VAL GLU PHE LEU HIS SER LYS GLY LEU MET HIS ARG ASP
SEQRES 12 A 299 LEU LYS PRO SER ASN ILE PHE PHE THR MET ASP ASP VAL
SEQRES 13 A 299 VAL LYS VAL GLY ASP PHE GLY LEU VAL THR ALA MET ASP
SEQRES 14 A 299 GLN ASP GLU GLU GLU GLN THR VAL LEU THR PRO MET PRO
SEQRES 15 A 299 ALA TYR ALA ARG HIS THR GLY GLN VAL GLY THR LYS LEU
SEQRES 16 A 299 TYR MET SER PRO GLU GLN ILE HIS GLY ASN SER TYR SER
SEQRES 17 A 299 HIS LYS VAL ASP ILE PHE SER LEU GLY LEU ILE LEU PHE
SEQRES 18 A 299 GLU LEU LEU TYR PRO PHE SER THR GLN MET GLU ARG VAL
SEQRES 19 A 299 ARG THR LEU THR ASP VAL ARG ASN LEU LYS PHE PRO PRO
SEQRES 20 A 299 LEU PHE THR GLN LYS TYR PRO CYS GLU TYR VAL MET VAL
SEQRES 21 A 299 GLN ASP MET LEU SER PRO SER PRO MET GLU ARG PRO GLU
SEQRES 22 A 299 ALA ILE ASN ILE ILE GLU ASN ALA VAL PHE GLU ASP LEU
SEQRES 23 A 299 ASP PHE PRO GLY LYS THR VAL LEU ARG GLN ARG SER ARG
HET GOL A1101 6
HET 0WH A1102 33
HETNAM GOL GLYCEROL
HETNAM 0WH 1-[5-(4-AMINO-7-METHYL-7H-PYRROLO[2,3-D]PYRIMIDIN-5-
HETNAM 2 0WH YL)-2,3-DIHYDRO-1H-INDOL-1-YL]-2-[3-(TRIFLUOROMETHYL)
HETNAM 3 0WH PHENYL]ETHANONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 0WH C24 H20 F3 N5 O
FORMUL 4 HOH *161(H2 O)
HELIX 1 1 GLY A 586 ASP A 591 1 6
HELIX 2 2 ARG A 628 ALA A 643 1 16
HELIX 3 3 ASN A 894 GLY A 901 1 8
HELIX 4 4 THR A 904 ARG A 908 5 5
HELIX 5 5 GLU A 909 LYS A 930 1 22
HELIX 6 6 LYS A 938 SER A 940 5 3
HELIX 7 7 SER A 991 HIS A 996 1 6
HELIX 8 8 HIS A 1002 TYR A 1018 1 17
HELIX 9 9 THR A 1022 ASN A 1035 1 14
HELIX 10 10 PRO A 1039 TYR A 1046 1 8
HELIX 11 11 TYR A 1046 LEU A 1057 1 12
HELIX 12 12 SER A 1060 ARG A 1064 5 5
HELIX 13 13 GLU A 1066 GLU A 1072 1 7
HELIX 14 14 ASN A 1073 GLU A 1077 5 5
SHEET 1 A 5 PHE A 592 GLY A 599 0
SHEET 2 A 5 VAL A 605 ASN A 611 -1 O VAL A 606 N LEU A 598
SHEET 3 A 5 ASN A 617 LEU A 625 -1 O ILE A 620 N PHE A 607
SHEET 4 A 5 VAL A 881 GLN A 888 -1 O MET A 887 N ALA A 619
SHEET 5 A 5 TYR A 653 GLU A 659 -1 N TRP A 657 O TYR A 884
SHEET 1 B 2 ILE A 942 PHE A 944 0
SHEET 2 B 2 VAL A 950 VAL A 952 -1 O LYS A 951 N PHE A 943
SITE 1 AC1 8 HIS A 647 PRO A 648 GLY A 649 GLN A 919
SITE 2 AC1 8 GLU A 922 ALA A 923 VAL A 949 VAL A 950
SITE 1 AC2 16 ALA A 619 VAL A 639 LEU A 642 ALA A 643
SITE 2 AC2 16 VAL A 651 TYR A 653 ILE A 885 MET A 887
SITE 3 AC2 16 GLN A 888 CYS A 890 PHE A 943 GLY A 953
SITE 4 AC2 16 ASP A 954 PHE A 955 HOH A1355 HOH A1356
CRYST1 101.119 101.119 158.831 90.00 90.00 120.00 P 61 2 2 12
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 0.009889 0.005710 0.000000 0.00000
SCALE2 0.000000 0.011419 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006296 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
