HEADER TRANSFERASE/TRANSFERASE INHIBITOR 29-OCT-14 4WT6
TITLE CRYSTAL STRUCTURE OF HUMAN PIM-1 KINASE IN COMPLEX WITH A
TITLE 2 THIADIAZOLAMINE-INDOLE INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PIM-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 124-396;
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: 562
KEYWDS TRANSFERASE, SERINE/THREONINE PROTEIN KINASE, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MOHR
REVDAT 2 27-DEC-23 4WT6 1 SOURCE KEYWDS JRNL REMARK
REVDAT 1 11-FEB-15 4WT6 0
JRNL AUTH B.WU,H.L.WANG,V.J.CEE,B.A.LANMAN,T.NIXEY,L.PETTUS,A.B.REED,
JRNL AUTH 2 R.P.WURZ,N.GUERRERO,C.SASTRI,J.WINSTON,J.R.LIPFORD,M.R.LEE,
JRNL AUTH 3 C.MOHR,K.L.ANDREWS,A.S.TASKER
JRNL TITL DISCOVERY OF 5-(1H-INDOL-5-YL)-1,3,4-THIADIAZOL-2-AMINES AS
JRNL TITL 2 POTENT PIM INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 25 775 2015
JRNL REFN ESSN 1464-3405
JRNL PMID 25616902
JRNL DOI 10.1016/J.BMCL.2014.12.091
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 18743
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 972
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1356
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2225
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.56000
REMARK 3 B22 (A**2) : -0.56000
REMARK 3 B33 (A**2) : 1.81000
REMARK 3 B12 (A**2) : -0.28000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.211
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.177
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.130
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.535
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2321 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2172 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3150 ; 1.189 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4964 ; 0.739 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 272 ; 5.253 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;34.323 ;23.136
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 380 ;13.896 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;14.473 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 333 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2610 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 564 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1091 ; 1.863 ; 4.243
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1090 ; 1.864 ; 4.241
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1362 ; 3.088 ; 6.353
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1363 ; 3.088 ; 6.356
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1230 ; 1.930 ; 4.475
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1230 ; 1.930 ; 4.475
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1789 ; 3.283 ; 6.624
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2664 ; 5.257 ;33.485
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2621 ; 5.203 ;33.395
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4WT6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000204462.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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 SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX HF
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19781
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.39100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.950
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M LICL, 0.1M TRIS, 20% PEG6K, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING 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 53.86667
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 26.93333
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 40.40000
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 13.46667
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 67.33333
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 20
REMARK 465 ALA A 21
REMARK 465 HIS A 22
REMARK 465 HIS A 23
REMARK 465 HIS A 24
REMARK 465 HIS A 25
REMARK 465 HIS A 26
REMARK 465 HIS A 27
REMARK 465 ASP A 28
REMARK 465 GLU A 29
REMARK 465 VAL A 30
REMARK 465 ASP A 31
REMARK 465 GLY A 32
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 186 72.70 54.14
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 3U6 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WSY RELATED DB: PDB
DBREF 4WT6 A 33 305 UNP P11309 PIM1_HUMAN 124 396
SEQADV 4WT6 MET A 20 UNP P11309 INITIATING METHIONINE
SEQADV 4WT6 ALA A 21 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 HIS A 22 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 HIS A 23 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 HIS A 24 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 HIS A 25 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 HIS A 26 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 HIS A 27 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 ASP A 28 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 GLU A 29 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 VAL A 30 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 ASP A 31 UNP P11309 EXPRESSION TAG
SEQADV 4WT6 GLY A 32 UNP P11309 EXPRESSION TAG
SEQRES 1 A 286 MET ALA HIS HIS HIS HIS HIS HIS ASP GLU VAL ASP GLY
SEQRES 2 A 286 PRO LEU GLU SER GLN TYR GLN VAL GLY PRO LEU LEU GLY
SEQRES 3 A 286 SER GLY GLY PHE GLY SER VAL TYR SER GLY ILE ARG VAL
SEQRES 4 A 286 SER ASP ASN LEU PRO VAL ALA ILE LYS HIS VAL GLU LYS
SEQRES 5 A 286 ASP ARG ILE SER ASP TRP GLY GLU LEU PRO ASN GLY THR
SEQRES 6 A 286 ARG VAL PRO MET GLU VAL VAL LEU LEU LYS LYS VAL SER
SEQRES 7 A 286 SER GLY PHE SER GLY VAL ILE ARG LEU LEU ASP TRP PHE
SEQRES 8 A 286 GLU ARG PRO ASP SER PHE VAL LEU ILE LEU GLU ARG PRO
SEQRES 9 A 286 GLU PRO VAL GLN ASP LEU PHE ASP PHE ILE THR GLU ARG
SEQRES 10 A 286 GLY ALA LEU GLN GLU GLU LEU ALA ARG SER PHE PHE TRP
SEQRES 11 A 286 GLN VAL LEU GLU ALA VAL ARG HIS CYS HIS ASN CYS GLY
SEQRES 12 A 286 VAL LEU HIS ARG ASP ILE LYS ASP GLU ASN ILE LEU ILE
SEQRES 13 A 286 ASP LEU ASN ARG GLY GLU LEU LYS LEU ILE ASP PHE GLY
SEQRES 14 A 286 SER GLY ALA LEU LEU LYS ASP THR VAL TYR THR ASP PHE
SEQRES 15 A 286 ASP GLY THR ARG VAL TYR SER PRO PRO GLU TRP ILE ARG
SEQRES 16 A 286 TYR HIS ARG TYR HIS GLY ARG SER ALA ALA VAL TRP SER
SEQRES 17 A 286 LEU GLY ILE LEU LEU TYR ASP MET VAL CYS GLY ASP ILE
SEQRES 18 A 286 PRO PHE GLU HIS ASP GLU GLU ILE ILE ARG GLY GLN VAL
SEQRES 19 A 286 PHE PHE ARG GLN ARG VAL SER SER GLU CYS GLN HIS LEU
SEQRES 20 A 286 ILE ARG TRP CYS LEU ALA LEU ARG PRO SER ASP ARG PRO
SEQRES 21 A 286 THR PHE GLU GLU ILE GLN ASN HIS PRO TRP MET GLN ASP
SEQRES 22 A 286 VAL LEU LEU PRO GLN GLU THR ALA GLU ILE HIS LEU HIS
HET 3U6 A 401 27
HET GOL A 402 6
HETNAM 3U6 6-[5-(5-AMINO-1,3,4-THIADIAZOL-2-YL)-1H-INDOL-3-YL]-N-
HETNAM 2 3U6 CYCLOPENTYLPYRIDIN-2-AMINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 3U6 C20 H20 N6 S
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *143(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 LYS A 169 GLU A 171 5 3
HELIX 6 AA6 ASP A 186 GLY A 190 5 5
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 SER A 54 N PRO A 42
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 118 N LYS A 67
SHEET 5 AA1 5 LEU A 106 GLU A 111 -1 N ASP A 108 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 -0.69
SITE 1 AC1 10 GLY A 45 PHE A 49 ALA A 65 LYS A 67
SITE 2 AC1 10 GLU A 121 VAL A 126 LEU A 174 ILE A 185
SITE 3 AC1 10 ASP A 186 HOH A 641
SITE 1 AC2 3 ASP A 108 TRP A 109 HOH A 596
CRYST1 98.184 98.184 80.800 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 0.010185 0.005880 0.000000 0.00000
SCALE2 0.000000 0.011761 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012376 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
