HEADER TRANSFERASE 14-FEB-17 5N5M
TITLE CRYSTAL STRUCTURE OF HUMAN PIM-1 KINASE IN COMPLEX WITH A
TITLE 2 CONSENSUSPEPTIDE AND (R)-3-(2-((ISOQUINOLIN-5-YLMETHYL)(METHYL)
TITLE 3 CARBAMOYL)PHENYL)PYRROLIDIN-1-IUM
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;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: ISOFROM 2 OF PIM-1 KINASE;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PIMTIDE;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: PIM-1 CONSENSUS PEPTIDE
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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PLIC-SGC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS SERINE THREONINE KINASE, TRANSFERASE, PROTO-ONCOGENE, FRAGMENT, PIM-
KEYWDS 2 1, CONSENSUS PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SIEFKER,A.HEINE,G.KLEBE
REVDAT 3 17-JAN-24 5N5M 1 REMARK
REVDAT 2 14-AUG-19 5N5M 1 REMARK
REVDAT 1 07-MAR-18 5N5M 0
JRNL AUTH C.SIEFKER,A.HEINE,C.TAYLOR,P.KOLB,K.HARDES,A.STEINMETZER,
JRNL AUTH 2 G.KLEBE
JRNL TITL A CRYSTALLOGRAPHIC FRAGMENT STUDY WITH HUMAN PIM-1 KINASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22230
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1112
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 49.3147 - 4.4244 1.00 2689 142 0.1669 0.2099
REMARK 3 2 4.4244 - 3.5121 1.00 2649 140 0.1482 0.1828
REMARK 3 3 3.5121 - 3.0682 1.00 2637 138 0.1594 0.1947
REMARK 3 4 3.0682 - 2.7877 1.00 2636 139 0.1625 0.1994
REMARK 3 5 2.7877 - 2.5879 1.00 2620 138 0.1726 0.2118
REMARK 3 6 2.5879 - 2.4353 1.00 2629 138 0.1730 0.2023
REMARK 3 7 2.4353 - 2.3134 1.00 2626 139 0.1944 0.2701
REMARK 3 8 2.3134 - 2.2127 1.00 2632 138 0.2140 0.2515
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.400
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 : 0.008 2352
REMARK 3 ANGLE : 0.763 3196
REMARK 3 CHIRALITY : 0.051 338
REMARK 3 PLANARITY : 0.005 438
REMARK 3 DIHEDRAL : 19.820 1395
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -86.4405 88.3425 -11.2022
REMARK 3 T TENSOR
REMARK 3 T11: 0.4123 T22: 0.2925
REMARK 3 T33: 0.3770 T12: 0.0397
REMARK 3 T13: 0.0623 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.2284 L22: 0.4028
REMARK 3 L33: 0.2452 L12: 0.2636
REMARK 3 L13: -0.0159 L23: -0.0524
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: -0.0393 S13: 0.2565
REMARK 3 S21: -0.1645 S22: 0.0563 S23: -0.0034
REMARK 3 S31: -0.2387 S32: 0.0756 S33: 0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 140 )
REMARK 3 ORIGIN FOR THE GROUP (A): -92.6579 81.9271 -6.1215
REMARK 3 T TENSOR
REMARK 3 T11: 0.3168 T22: 0.1836
REMARK 3 T33: 0.2449 T12: 0.0313
REMARK 3 T13: 0.0397 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 0.3007 L22: 0.6895
REMARK 3 L33: 0.9064 L12: 0.0231
REMARK 3 L13: 0.5244 L23: 0.0475
REMARK 3 S TENSOR
REMARK 3 S11: 0.0188 S12: -0.0227 S13: 0.2478
REMARK 3 S21: 0.0262 S22: 0.1693 S23: 0.2316
REMARK 3 S31: -0.2950 S32: -0.2356 S33: 0.2086
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 141 THROUGH 305 )
REMARK 3 ORIGIN FOR THE GROUP (A): -88.9326 63.9215 -2.2331
REMARK 3 T TENSOR
REMARK 3 T11: 0.1850 T22: 0.1795
REMARK 3 T33: 0.1912 T12: 0.0217
REMARK 3 T13: -0.0131 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.7156 L22: 0.8482
REMARK 3 L33: 1.6524 L12: 0.0191
REMARK 3 L13: -0.4176 L23: -0.0300
REMARK 3 S TENSOR
REMARK 3 S11: 0.0690 S12: -0.0762 S13: -0.0176
REMARK 3 S21: 0.0109 S22: -0.0496 S23: -0.0255
REMARK 3 S31: 0.0769 S32: 0.0349 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -84.7211 74.1284 9.6829
REMARK 3 T TENSOR
REMARK 3 T11: 0.4510 T22: 0.4007
REMARK 3 T33: 0.3483 T12: -0.0677
REMARK 3 T13: 0.0142 T23: -0.1432
REMARK 3 L TENSOR
REMARK 3 L11: 0.1267 L22: 0.1781
REMARK 3 L33: 0.0527 L12: -0.0063
REMARK 3 L13: 0.0787 L23: 0.0238
REMARK 3 S TENSOR
REMARK 3 S11: -0.1228 S12: -0.2786 S13: 0.1047
REMARK 3 S21: -0.0308 S22: 0.2152 S23: -0.3055
REMARK 3 S31: -0.0378 S32: 0.1229 S33: 0.0626
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 5N5M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003387.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-16
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 : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : SILICON
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22235
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.930
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.98
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.210
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: 3WE8
REMARK 200
REMARK 200 REMARK: HEXAGONAL ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES MGCL2 GLYCEROL DTT BIS-TRIS
REMARK 280 -PROPANE PEG3350 ETHYLENE-GLYCOL DMSO, PH 7.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, 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 53.51133
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 26.75567
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 40.13350
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 13.37783
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 66.88917
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 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 ALA B 1
REMARK 465 PRO B 11
REMARK 465 PRO B 12
REMARK 465 THR B 13
REMARK 465 ALA B 14
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 PRO A 33 CG CD
REMARK 470 LEU A 34 CD1 CD2
REMARK 470 GLU A 35 CG CD OE1 OE2
REMARK 470 SER A 36 OG
REMARK 470 GLN A 39 CD OE1 NE2
REMARK 470 VAL A 58 CG1 CG2
REMARK 470 SER A 59 OG
REMARK 470 ARG A 73 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 74 CD1
REMARK 470 SER A 75 OG
REMARK 470 ASP A 76 OD1 OD2
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 LEU A 80 CG CD1 CD2
REMARK 470 PRO A 81 CG CD
REMARK 470 ASN A 82 OD1 ND2
REMARK 470 THR A 84 OG1 CG2
REMARK 470 ARG A 85 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 94 CD CE NZ
REMARK 470 SER A 98 OG
REMARK 470 PHE A 100 CD1 CE1 CZ
REMARK 470 ARG A 105 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 183 NZ
REMARK 470 ASP A 202 OD1 OD2
REMARK 470 GLN A 252 OE1 NE2
REMARK 470 ARG A 274 CZ NH1 NH2
REMARK 470 GLN A 297 OE1 NE2
REMARK 470 LYS B 3 CD CE NZ
REMARK 470 HIS B 7 O
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 ASP A 60 17.60 -141.48
REMARK 500 SER A 101 -178.46 -170.43
REMARK 500 ASP A 167 46.07 -146.02
REMARK 500 ASP A 186 81.96 60.49
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 8O8 A 401
DBREF 5N5M A 1 313 UNP P11309 PIM1_HUMAN 1 313
DBREF 5N5M B 1 14 PDB 5N5M 5N5M 1 14
SEQADV 5N5M GLY A 250 UNP P11309 ARG 250 ENGINEERED MUTATION
SEQRES 1 A 313 MET LEU LEU SER LYS ILE ASN SER LEU ALA HIS LEU ARG
SEQRES 2 A 313 ALA ALA PRO CYS ASN ASP LEU HIS ALA THR LYS LEU ALA
SEQRES 3 A 313 PRO GLY LYS GLU LYS GLU PRO LEU GLU SER GLN TYR GLN
SEQRES 4 A 313 VAL GLY PRO LEU LEU GLY SER GLY GLY PHE GLY SER VAL
SEQRES 5 A 313 TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO VAL ALA
SEQRES 6 A 313 ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP TRP GLY
SEQRES 7 A 313 GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU VAL VAL
SEQRES 8 A 313 LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY VAL ILE
SEQRES 9 A 313 ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER PHE VAL
SEQRES 10 A 313 LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP LEU PHE
SEQRES 11 A 313 ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU GLU LEU
SEQRES 12 A 313 ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA VAL ARG
SEQRES 13 A 313 HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP ILE LYS
SEQRES 14 A 313 ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY GLU LEU
SEQRES 15 A 313 LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU LYS ASP
SEQRES 16 A 313 THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL TYR SER
SEQRES 17 A 313 PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS GLY ARG
SEQRES 18 A 313 SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU TYR ASP
SEQRES 19 A 313 MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP GLU GLU
SEQRES 20 A 313 ILE ILE GLY GLY GLN VAL PHE PHE ARG GLN ARG VAL SER
SEQRES 21 A 313 SEP GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU ALA LEU
SEQRES 22 A 313 ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE GLN ASN
SEQRES 23 A 313 HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN GLU THR
SEQRES 24 A 313 ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY PRO SER
SEQRES 25 A 313 LYS
SEQRES 1 B 14 ALA ARG LYS ARG ARG ARG HIS PRO SER GLY PRO PRO THR
SEQRES 2 B 14 ALA
MODRES 5N5M SEP A 261 SER MODIFIED RESIDUE
HET SEP A 261 10
HET 8O8 A 401 26
HETNAM SEP PHOSPHOSERINE
HETNAM 8O8 ~{N}-(ISOQUINOLIN-5-YLMETHYL)-~{N}-METHYL-2-[(3~{R})-
HETNAM 2 8O8 PYRROLIDIN-3-YL]BENZAMIDE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 8O8 C22 H23 N3 O
FORMUL 4 HOH *135(H2 O)
HELIX 1 AA1 PRO A 33 GLN A 37 1 5
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 GLY A 47 0
SHEET 2 AA1 5 GLY A 50 ARG A 57 -1 O VAL A 52 N LEU A 44
SHEET 3 AA1 5 PRO A 63 GLU A 70 -1 O ILE A 66 N TYR A 53
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
LINK C SER A 260 N SEP A 261 1555 1555 1.33
LINK C SEP A 261 N AGLU A 262 1555 1555 1.33
LINK C SEP A 261 N BGLU A 262 1555 1555 1.33
CISPEP 1 GLU A 124 PRO A 125 0 -0.12
SITE 1 AC1 10 GLY A 45 PHE A 49 ALA A 65 GLU A 121
SITE 2 AC1 10 ARG A 122 GLU A 171 ASN A 172 LEU A 174
SITE 3 AC1 10 ASP A 186 HOH A 550
CRYST1 98.605 98.605 80.267 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 0.010141 0.005855 0.000000 0.00000
SCALE2 0.000000 0.011710 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012458 0.00000
(ATOM LINES ARE NOT SHOWN.)
END