HEADER TRANSFERASE/TRANSFERASE INHIBITOR 07-NOV-16 5TUR
TITLE PIM-1 KINASE IN COMPLEX WITH A 7-AZAINDOLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PIM-1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.11.1;
COMPND 5 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: 562
KEYWDS KINASE, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR I.MECHIN,Y.ZHANG,R.WANG,J.D.BATCHELOR,L.MCLEAN
REVDAT 2 06-MAR-24 5TUR 1 REMARK
REVDAT 1 11-OCT-17 5TUR 0
JRNL AUTH C.BARBERIS,N.MOORCROFT,C.ARENDT,M.LEVIT,S.MORENO-MAZZA,
JRNL AUTH 2 J.BATCHELOR,I.MECHIN,T.MAJID
JRNL TITL DISCOVERY OF N-SUBSTITUTED 7-AZAINDOLES AS PIM1 KINASE
JRNL TITL 2 INHIBITORS - PART I.
JRNL REF BIOORG. MED. CHEM. LETT. V. 27 4730 2017
JRNL REFN ESSN 1464-3405
JRNL PMID 28947155
JRNL DOI 10.1016/J.BMCL.2017.08.069
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11_2567: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 9343
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.920
REMARK 3 FREE R VALUE TEST SET COUNT : 927
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 37.4953 - 5.6333 0.99 1226 136 0.1825 0.2004
REMARK 3 2 5.6333 - 4.4737 1.00 1202 135 0.1754 0.2185
REMARK 3 3 4.4737 - 3.9089 1.00 1197 127 0.1844 0.2298
REMARK 3 4 3.9089 - 3.5518 1.00 1207 129 0.1978 0.2745
REMARK 3 5 3.5518 - 3.2974 1.00 1196 139 0.2383 0.2655
REMARK 3 6 3.2974 - 3.1031 1.00 1197 125 0.2564 0.3134
REMARK 3 7 3.1031 - 2.9477 1.00 1191 136 0.2802 0.3363
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.002 2294
REMARK 3 ANGLE : 0.668 3113
REMARK 3 CHIRALITY : 0.043 330
REMARK 3 PLANARITY : 0.005 403
REMARK 3 DIHEDRAL : 13.256 1348
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 5TUR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000224859.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-07
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 : 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) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9343
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.948
REMARK 200 RESOLUTION RANGE LOW (A) : 37.492
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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 (%): 49.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M IMIDAZOLE, 1M NAACETATE, 20%
REMARK 280 GLYCEROL PH 6.5, VAPOR DIFFUSION, TEMPERATURE 277K
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 53.86133
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 26.93067
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 40.39600
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 13.46533
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 67.32667
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 -90
REMARK 465 PRO A -89
REMARK 465 HIS A -88
REMARK 465 GLU A -87
REMARK 465 PRO A -86
REMARK 465 HIS A -85
REMARK 465 GLU A -84
REMARK 465 PRO A -83
REMARK 465 LEU A -82
REMARK 465 THR A -81
REMARK 465 PRO A -80
REMARK 465 PRO A -79
REMARK 465 PHE A -78
REMARK 465 SER A -77
REMARK 465 ALA A -76
REMARK 465 LEU A -75
REMARK 465 PRO A -74
REMARK 465 ASP A -73
REMARK 465 PRO A -72
REMARK 465 ALA A -71
REMARK 465 GLY A -70
REMARK 465 ALA A -69
REMARK 465 PRO A -68
REMARK 465 SER A -67
REMARK 465 ARG A -66
REMARK 465 ARG A -65
REMARK 465 GLN A -64
REMARK 465 SER A -63
REMARK 465 ARG A -62
REMARK 465 GLN A -61
REMARK 465 ARG A -60
REMARK 465 PRO A -59
REMARK 465 GLN A -58
REMARK 465 LEU A -57
REMARK 465 SER A -56
REMARK 465 SER A -55
REMARK 465 ASP A -54
REMARK 465 SER A -53
REMARK 465 PRO A -52
REMARK 465 SER A -51
REMARK 465 ALA A -50
REMARK 465 PHE A -49
REMARK 465 ARG A -48
REMARK 465 ALA A -47
REMARK 465 SER A -46
REMARK 465 ARG A -45
REMARK 465 SER A -44
REMARK 465 HIS A -43
REMARK 465 SER A -42
REMARK 465 ARG A -41
REMARK 465 ASN A -40
REMARK 465 ALA A -39
REMARK 465 THR A -38
REMARK 465 ARG A -37
REMARK 465 SER A -36
REMARK 465 HIS A -35
REMARK 465 SER A -34
REMARK 465 HIS A -33
REMARK 465 SER A -32
REMARK 465 HIS A -31
REMARK 465 SER A -30
REMARK 465 PRO A -29
REMARK 465 ARG A -28
REMARK 465 HIS A -27
REMARK 465 SER A -26
REMARK 465 LEU A -25
REMARK 465 ARG A -24
REMARK 465 HIS A -23
REMARK 465 SER A -22
REMARK 465 PRO A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 CYS A -16
REMARK 465 GLY A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 SER A -12
REMARK 465 GLY A -11
REMARK 465 HIS A -10
REMARK 465 ARG A -9
REMARK 465 PRO A -8
REMARK 465 CYS A -7
REMARK 465 ALA A -6
REMARK 465 ASP A -5
REMARK 465 ILE A -4
REMARK 465 LEU A -3
REMARK 465 GLU A -2
REMARK 465 VAL A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 ILE A 6
REMARK 465 ASN A 7
REMARK 465 SER A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 HIS A 11
REMARK 465 LEU A 12
REMARK 465 ARG A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 CYS A 17
REMARK 465 ASN A 18
REMARK 465 ASP A 19
REMARK 465 LEU A 20
REMARK 465 HIS A 21
REMARK 465 ALA A 22
REMARK 465 THR A 23
REMARK 465 LYS A 24
REMARK 465 LEU A 25
REMARK 465 ALA A 26
REMARK 465 PRO A 27
REMARK 465 GLY A 28
REMARK 465 LYS A 29
REMARK 465 GLU A 30
REMARK 465 LYS A 31
REMARK 465 GLU A 32
REMARK 465 PRO A 33
REMARK 465 GLY A 83
REMARK 465 SER A 98
REMARK 465 GLY A 99
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 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 GLU A 35 30.78 -98.95
REMARK 500 GLU A 124 116.47 -163.93
REMARK 500 ASP A 167 50.11 -150.25
REMARK 500 ASP A 186 85.71 58.79
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 7LK A 401
DBREF 5TUR A -90 313 UNP P11309 PIM1_HUMAN 1 404
SEQRES 1 A 404 MET PRO HIS GLU PRO HIS GLU PRO LEU THR PRO PRO PHE
SEQRES 2 A 404 SER ALA LEU PRO ASP PRO ALA GLY ALA PRO SER ARG ARG
SEQRES 3 A 404 GLN SER ARG GLN ARG PRO GLN LEU SER SER ASP SER PRO
SEQRES 4 A 404 SER ALA PHE ARG ALA SER ARG SER HIS SER ARG ASN ALA
SEQRES 5 A 404 THR ARG SER HIS SER HIS SER HIS SER PRO ARG HIS SER
SEQRES 6 A 404 LEU ARG HIS SER PRO GLY SER GLY SER CYS GLY SER SER
SEQRES 7 A 404 SER GLY HIS ARG PRO CYS ALA ASP ILE LEU GLU VAL GLY
SEQRES 8 A 404 MET LEU LEU SER LYS ILE ASN SER LEU ALA HIS LEU ARG
SEQRES 9 A 404 ALA ALA PRO CYS ASN ASP LEU HIS ALA THR LYS LEU ALA
SEQRES 10 A 404 PRO GLY LYS GLU LYS GLU PRO LEU GLU SER GLN TYR GLN
SEQRES 11 A 404 VAL GLY PRO LEU LEU GLY SER GLY GLY PHE GLY SER VAL
SEQRES 12 A 404 TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO VAL ALA
SEQRES 13 A 404 ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP TRP GLY
SEQRES 14 A 404 GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU VAL VAL
SEQRES 15 A 404 LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY VAL ILE
SEQRES 16 A 404 ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER PHE VAL
SEQRES 17 A 404 LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP LEU PHE
SEQRES 18 A 404 ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU GLU LEU
SEQRES 19 A 404 ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA VAL ARG
SEQRES 20 A 404 HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP ILE LYS
SEQRES 21 A 404 ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY GLU LEU
SEQRES 22 A 404 LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU LYS ASP
SEQRES 23 A 404 THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL TYR SER
SEQRES 24 A 404 PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS GLY ARG
SEQRES 25 A 404 SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU TYR ASP
SEQRES 26 A 404 MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP GLU GLU
SEQRES 27 A 404 ILE ILE ARG GLY GLN VAL PHE PHE ARG GLN ARG VAL SER
SEQRES 28 A 404 SER GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU ALA LEU
SEQRES 29 A 404 ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE GLN ASN
SEQRES 30 A 404 HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN GLU THR
SEQRES 31 A 404 ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY PRO SER
SEQRES 32 A 404 LYS
HET 7LK A 401 24
HETNAM 7LK 1-METHYL-2-[4-(PIPERAZIN-1-YL)PHENYL]-1H-PYRROLO[2,3-
HETNAM 2 7LK B]PYRIDINE-4-CARBONITRILE
FORMUL 2 7LK C19 H19 N5
FORMUL 3 HOH *3(H2 O)
HELIX 1 AA1 ASP A 72 ILE A 74 5 3
HELIX 2 AA2 MET A 88 SER A 97 1 10
HELIX 3 AA3 LEU A 129 GLY A 137 1 9
HELIX 4 AA4 GLN A 140 CYS A 161 1 22
HELIX 5 AA5 THR A 204 SER A 208 5 5
HELIX 6 AA6 PRO A 209 HIS A 216 1 8
HELIX 7 AA7 HIS A 219 GLY A 238 1 20
HELIX 8 AA8 HIS A 244 GLY A 251 1 8
HELIX 9 AA9 SER A 260 LEU A 271 1 12
HELIX 10 AB1 ARG A 274 ARG A 278 5 5
HELIX 11 AB2 THR A 280 ASN A 286 1 7
HELIX 12 AB3 HIS A 287 GLN A 291 5 5
HELIX 13 AB4 LEU A 295 LEU A 304 1 10
SHEET 1 AA1 5 TYR A 38 GLY A 47 0
SHEET 2 AA1 5 GLY A 50 ARG A 57 -1 O ILE A 56 N GLN A 39
SHEET 3 AA1 5 PRO A 63 GLU A 70 -1 O VAL A 64 N GLY A 55
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 LEU A 107 O ILE A 119
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 GLU A 181 N ASP A 176
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 -2.40
SITE 1 AC1 7 VAL A 52 ALA A 65 ILE A 104 LEU A 120
SITE 2 AC1 7 ARG A 122 ASP A 131 LEU A 174
CRYST1 97.747 97.747 80.792 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 0.010230 0.005907 0.000000 0.00000
SCALE2 0.000000 0.011813 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012377 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
