HEADER TRANSFERASE/TRANSFERASE INHIBITOR 31-AUG-15 5DHJ
TITLE PIM1 IN COMPLEX WITH CPD4 (3-METHYL-5-(PYRIDIN-3-YL)-1H-PYRAZOLO[3,4-
TITLE 2 C]PYRIDINE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PIM-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 120-404);
COMPND 5 EC: 2.7.11.1;
COMPND 6 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: PIM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PIM-1, KINASE, ATP-COMPETITIVE, STRUCTURE-BASED DRUG DESIGN,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.MURRAY,H.WALLWEBER
REVDAT 3 06-MAR-24 5DHJ 1 JRNL REMARK
REVDAT 2 11-NOV-15 5DHJ 1 JRNL
REVDAT 1 28-OCT-15 5DHJ 0
JRNL AUTH H.HU,X.WANG,G.K.CHAN,J.H.CHANG,S.DO,J.DRUMMOND,A.EBENS,
JRNL AUTH 2 W.LEE,J.LY,J.P.LYSSIKATOS,J.MURRAY,J.G.MOFFAT,Q.CHAO,V.TSUI,
JRNL AUTH 3 H.WALLWEBER,A.KOLESNIKOV
JRNL TITL DISCOVERY OF 3,5-SUBSTITUTED 6-AZAINDAZOLES AS POTENT
JRNL TITL 2 PAN-PIM INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 25 5258 2015
JRNL REFN ESSN 1464-3405
JRNL PMID 26459208
JRNL DOI 10.1016/J.BMCL.2015.09.052
REMARK 2
REMARK 2 RESOLUTION. 2.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_256)
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) : 2.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 15682
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 800
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 14.9400 - 4.4323 1.00 2572 134 0.1598 0.2072
REMARK 3 2 4.4323 - 3.5334 1.00 2540 132 0.1574 0.2181
REMARK 3 3 3.5334 - 3.0912 1.00 2526 137 0.1927 0.2652
REMARK 3 4 3.0912 - 2.8106 1.00 2510 132 0.1969 0.2660
REMARK 3 5 2.8106 - 2.6103 0.99 2510 133 0.2204 0.2800
REMARK 3 6 2.6103 - 2.4570 0.89 2224 132 0.2424 0.3371
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 60.28
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.23870
REMARK 3 B22 (A**2) : -0.23870
REMARK 3 B33 (A**2) : 0.47740
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 : 0.009 2296
REMARK 3 ANGLE : 1.086 3118
REMARK 3 CHIRALITY : 0.073 331
REMARK 3 PLANARITY : 0.004 406
REMARK 3 DIHEDRAL : 18.997 832
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 33:305 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7872 27.5253 0.8838
REMARK 3 T TENSOR
REMARK 3 T11: 0.1675 T22: 0.1708
REMARK 3 T33: 0.1532 T12: 0.0200
REMARK 3 T13: -0.0114 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.5930 L22: 0.8423
REMARK 3 L33: 1.1896 L12: -0.2263
REMARK 3 L13: -0.0188 L23: 0.0629
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: -0.0042 S13: -0.0297
REMARK 3 S21: 0.0199 S22: 0.1265 S23: -0.0882
REMARK 3 S31: 0.0019 S32: -0.0814 S33: 0.0000
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 5DHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213207.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-09
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 : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15774
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
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 (%) : 98.5
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.08400
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) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.54100
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, 0.2M LISO4, 0.1M TRIS-HCL,
REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 53.89267
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 26.94633
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 40.41950
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 13.47317
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 67.36583
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 28
REMARK 465 LYS A 29
REMARK 465 GLU A 30
REMARK 465 LYS A 31
REMARK 465 GLU A 32
REMARK 465 SER A 306
REMARK 465 LEU A 307
REMARK 465 SER A 308
REMARK 465 PRO A 309
REMARK 465 GLY A 310
REMARK 465 PRO A 311
REMARK 465 SER A 312
REMARK 465 LYS A 313
REMARK 465 LYS A 314
REMARK 465 LEU A 315
REMARK 465 ALA A 316
REMARK 465 ALA A 317
REMARK 465 ALA A 318
REMARK 465 LEU A 319
REMARK 465 GLU A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
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 ARG A 105 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 SER A 98 -142.00 179.51
REMARK 500 GLU A 124 117.19 -160.19
REMARK 500 ASP A 167 40.82 -151.72
REMARK 500 ASP A 186 75.26 68.77
REMARK 500 ASP A 202 28.70 -147.14
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 5E5 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DGZ RELATED DB: PDB
REMARK 900 RELATED ID: 5DIA RELATED DB: PDB
DBREF 5DHJ A 29 313 UNP P11309 PIM1_HUMAN 120 404
SEQADV 5DHJ MET A 28 UNP P11309 INITIATING METHIONINE
SEQADV 5DHJ LYS A 314 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ LEU A 315 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ ALA A 316 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ ALA A 317 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ ALA A 318 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ LEU A 319 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ GLU A 320 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ HIS A 321 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ HIS A 322 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ HIS A 323 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ HIS A 324 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ HIS A 325 UNP P11309 EXPRESSION TAG
SEQADV 5DHJ HIS A 326 UNP P11309 EXPRESSION TAG
SEQRES 1 A 299 MET LYS GLU LYS GLU PRO LEU GLU SER GLN TYR GLN VAL
SEQRES 2 A 299 GLY PRO LEU LEU GLY SER GLY GLY PHE GLY SER VAL TYR
SEQRES 3 A 299 SER GLY ILE ARG VAL SER ASP ASN LEU PRO VAL ALA ILE
SEQRES 4 A 299 LYS HIS VAL GLU LYS ASP ARG ILE SER ASP TRP GLY GLU
SEQRES 5 A 299 LEU PRO ASN GLY THR ARG VAL PRO MET GLU VAL VAL LEU
SEQRES 6 A 299 LEU LYS LYS VAL SER SER GLY PHE SER GLY VAL ILE ARG
SEQRES 7 A 299 LEU LEU ASP TRP PHE GLU ARG PRO ASP SER PHE VAL LEU
SEQRES 8 A 299 ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP LEU PHE ASP
SEQRES 9 A 299 PHE ILE THR GLU ARG GLY ALA LEU GLN GLU GLU LEU ALA
SEQRES 10 A 299 ARG SER PHE PHE TRP GLN VAL LEU GLU ALA VAL ARG HIS
SEQRES 11 A 299 CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP ILE LYS ASP
SEQRES 12 A 299 GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY GLU LEU LYS
SEQRES 13 A 299 LEU ILE ASP PHE GLY SER GLY ALA LEU LEU LYS ASP THR
SEQRES 14 A 299 VAL TYR THR ASP PHE ASP GLY THR ARG VAL TYR SER PRO
SEQRES 15 A 299 PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS GLY ARG SER
SEQRES 16 A 299 ALA ALA VAL TRP SER LEU GLY ILE LEU LEU TYR ASP MET
SEQRES 17 A 299 VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP GLU GLU ILE
SEQRES 18 A 299 ILE ARG GLY GLN VAL PHE PHE ARG GLN ARG VAL SER SER
SEQRES 19 A 299 GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU ALA LEU ARG
SEQRES 20 A 299 PRO SER ASP ARG PRO THR PHE GLU GLU ILE GLN ASN HIS
SEQRES 21 A 299 PRO TRP MET GLN ASP VAL LEU LEU PRO GLN GLU THR ALA
SEQRES 22 A 299 GLU ILE HIS LEU HIS SER LEU SER PRO GLY PRO SER LYS
SEQRES 23 A 299 LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET 5E5 A 401 16
HET PO4 A 402 5
HET PO4 A 403 5
HETNAM 5E5 3-METHYL-5-(PYRIDIN-3-YL)-2H-PYRAZOLO[3,4-C]PYRIDINE
HETNAM PO4 PHOSPHATE ION
FORMUL 2 5E5 C12 H10 N4
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 5 HOH *58(H2 O)
HELIX 1 AA1 PRO A 33 SER A 36 5 4
HELIX 2 AA2 ASP A 72 ILE A 74 5 3
HELIX 3 AA3 MET A 88 SER A 97 1 10
HELIX 4 AA4 LEU A 129 GLY A 137 1 9
HELIX 5 AA5 GLN A 140 CYS A 161 1 22
HELIX 6 AA6 LYS A 169 GLU A 171 5 3
HELIX 7 AA7 THR A 204 SER A 208 5 5
HELIX 8 AA8 PRO A 209 HIS A 216 1 8
HELIX 9 AA9 HIS A 219 GLY A 238 1 20
HELIX 10 AB1 HIS A 244 GLY A 251 1 8
HELIX 11 AB2 SER A 260 LEU A 271 1 12
HELIX 12 AB3 ARG A 274 ARG A 278 5 5
HELIX 13 AB4 THR A 280 ASN A 286 1 7
HELIX 14 AB5 HIS A 287 GLN A 291 5 5
HELIX 15 AB6 LEU A 295 LEU A 304 1 10
SHEET 1 AA1 5 TYR A 38 SER A 46 0
SHEET 2 AA1 5 SER A 51 ARG A 57 -1 O VAL A 52 N LEU A 44
SHEET 3 AA1 5 PRO A 63 GLU A 70 -1 O HIS A 68 N SER A 51
SHEET 4 AA1 5 SER A 115 GLU A 121 -1 O LEU A 120 N ALA A 65
SHEET 5 AA1 5 LEU A 106 GLU A 111 -1 N PHE A 110 O VAL A 117
SHEET 1 AA2 2 TRP A 77 GLU A 79 0
SHEET 2 AA2 2 ARG A 85 PRO A 87 -1 O VAL A 86 N GLY A 78
SHEET 1 AA3 3 VAL A 126 ASP A 128 0
SHEET 2 AA3 3 ILE A 173 ASP A 176 -1 O ILE A 175 N GLN A 127
SHEET 3 AA3 3 GLU A 181 LEU A 184 -1 O LYS A 183 N LEU A 174
SHEET 1 AA4 2 VAL A 163 LEU A 164 0
SHEET 2 AA4 2 ALA A 191 LEU A 192 -1 O ALA A 191 N LEU A 164
CISPEP 1 GLU A 124 PRO A 125 0 2.34
CISPEP 2 GLU A 124 PRO A 125 0 5.26
SITE 1 AC1 9 PHE A 49 ALA A 65 LYS A 67 GLU A 121
SITE 2 AC1 9 ARG A 122 LEU A 174 ILE A 185 ASP A 186
SITE 3 AC1 9 HOH A 550
SITE 1 AC2 5 ARG A 156 ARG A 258 SER A 261 PHE A 281
SITE 2 AC2 5 HOH A 510
SITE 1 AC3 2 GLU A 142 ARG A 145
CRYST1 97.732 97.732 80.839 90.00 90.00 120.00 P 65 6
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 0.010232 0.005907 0.000000 0.00000
SCALE2 0.000000 0.011815 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012370 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
