HEADER TRANSFERASE/TRANSFERASE INHIBITOR 13-JUN-13 4L7F
TITLE CO-CRYSTAL STRUCTURE OF JNK1 AND AX13587
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 7-362;
COMPND 5 SYNONYM: MAP KINASE 8, MAPK 8, JNK-46, STRESS-ACTIVATED PROTEIN
COMPND 6 KINASE 1C, SAPK1C, STRESS-ACTIVATED PROTEIN KINASE JNK1, C-JUN N-
COMPND 7 TERMINAL KINASE 1;
COMPND 8 EC: 2.7.11.24;
COMPND 9 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: MAPK8, JNK1, PRKM8, SAPK1, SAPK1C
KEYWDS PROTEIN KINASE FOLD, PROTEIN KINASE, JUN-C, PHOSPHORYLATION,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.L.WALTER,G.M.RANIERI,A.M.RIGGS,H.WEISSIG,B.LI,K.R.SHREDER
REVDAT 3 28-FEB-24 4L7F 1 REMARK SEQADV
REVDAT 2 09-OCT-13 4L7F 1 JRNL
REVDAT 1 21-AUG-13 4L7F 0
JRNL AUTH B.LI,O.M.COCIORVA,T.NOMANBHOY,H.WEISSIG,Q.LI,K.NAKAMURA,
JRNL AUTH 2 M.LIYANAGE,M.C.ZHANG,A.Y.SHIH,A.ABAN,Y.HU,J.CAJICA,L.PHAM,
JRNL AUTH 3 J.W.KOZARICH,K.R.SHREDER
JRNL TITL HIT-TO-LEAD OPTIMIZATION AND KINASE SELECTIVITY OF
JRNL TITL 2 IMIDAZO[1,2-A]QUINOXALIN-4-AMINE DERIVED JNK1 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 23 5217 2013
JRNL REFN ISSN 0960-894X
JRNL PMID 23916259
JRNL DOI 10.1016/J.BMCL.2013.06.087
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 47049
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2380
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3291
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2871
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 449
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.55000
REMARK 3 B22 (A**2) : 0.55000
REMARK 3 B33 (A**2) : -0.83000
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): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.581
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3211 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 26 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4399 ; 1.470 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): 59 ; 3.612 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 423 ; 5.774 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 149 ;36.234 ;24.430
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 624 ;15.152 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;22.028 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 486 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2434 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 12 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1463 ; 0.208 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 37 ; 0.274 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2195 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5 ; 0.127 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 357 ; 0.214 ; 0.200
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): 76 ; 0.206 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 30 ; 0.254 ; 0.200
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): 1965 ; 1.068 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3116 ; 1.710 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1475 ; 2.428 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1245 ; 3.865 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 4L7F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080275.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
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 : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47064
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 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: MOLECULAR REPLACEMENT
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 (%): 68.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 67.90100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.20266
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.40267
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 67.90100
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 39.20266
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 31.40267
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 67.90100
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 39.20266
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.40267
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 78.40532
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 62.80533
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 78.40532
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 62.80533
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 78.40532
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 62.80533
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 ALA A 173
REMARK 465 ARG A 174
REMARK 465 THR A 175
REMARK 465 ALA A 176
REMARK 465 GLY A 177
REMARK 465 THR A 178
REMARK 465 SER A 179
REMARK 465 PHE A 180
REMARK 465 MET A 181
REMARK 465 MET A 182
REMARK 465 THR A 183
REMARK 465 PRO A 184
REMARK 465 TYR A 185
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 VAL A 186 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 624 O HOH A 934 1.63
REMARK 500 O HOH A 582 O HOH A 722 1.63
REMARK 500 O HOH A 576 O HOH A 913 1.89
REMARK 500 O HOH A 522 O HOH A 710 2.05
REMARK 500 NH2 ARG A 72 O HOH A 934 2.06
REMARK 500 OE1 GLN A 64 O HOH A 766 2.08
REMARK 500 O HOH A 710 O HOH A 876 2.10
REMARK 500 O HOH A 684 O HOH A 691 2.13
REMARK 500 O HOH A 743 O HOH A 848 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 640 O HOH A 938 9554 1.93
REMARK 500 O HOH A 553 O HOH A 938 9554 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 34 -152.16 -137.63
REMARK 500 ALA A 36 -53.35 84.17
REMARK 500 GLN A 102 -52.03 -124.96
REMARK 500 ARG A 150 -18.64 73.90
REMARK 500 CYS A 163 1.36 83.60
REMARK 500 CYS A 163 2.38 83.06
REMARK 500 ASP A 339 119.68 -37.23
REMARK 500 LYS A 340 7.61 54.84
REMARK 500 LEU A 342 54.57 -107.04
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 1V5 A 401
DBREF 4L7F A 7 362 UNP P45983 MK08_HUMAN 7 362
SEQADV 4L7F SER A 5 UNP P45983 EXPRESSION TAG
SEQADV 4L7F LEU A 6 UNP P45983 EXPRESSION TAG
SEQADV 4L7F TRP A 363 UNP P45983 EXPRESSION TAG
SEQADV 4L7F ARG A 364 UNP P45983 EXPRESSION TAG
SEQADV 4L7F LYS A 365 UNP P45983 EXPRESSION TAG
SEQADV 4L7F GLY A 366 UNP P45983 EXPRESSION TAG
SEQADV 4L7F ILE A 367 UNP P45983 EXPRESSION TAG
SEQADV 4L7F ILE A 368 UNP P45983 EXPRESSION TAG
SEQADV 4L7F THR A 369 UNP P45983 EXPRESSION TAG
SEQADV 4L7F ILE A 370 UNP P45983 EXPRESSION TAG
SEQADV 4L7F THR A 371 UNP P45983 EXPRESSION TAG
SEQRES 1 A 367 SER LEU ASP ASN ASN PHE TYR SER VAL GLU ILE GLY ASP
SEQRES 2 A 367 SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU LYS
SEQRES 3 A 367 PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA ALA
SEQRES 4 A 367 TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS LYS
SEQRES 5 A 367 LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS ARG
SEQRES 6 A 367 ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN HIS
SEQRES 7 A 367 LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO GLN
SEQRES 8 A 367 LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL MET
SEQRES 9 A 367 GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN MET
SEQRES 10 A 367 GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR GLN
SEQRES 11 A 367 MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY ILE
SEQRES 12 A 367 ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL LYS
SEQRES 13 A 367 SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU ALA
SEQRES 14 A 367 ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR VAL
SEQRES 15 A 367 VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU GLY
SEQRES 16 A 367 MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL GLY
SEQRES 17 A 367 CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU PHE
SEQRES 18 A 367 PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL ILE
SEQRES 19 A 367 GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS LYS
SEQRES 20 A 367 LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG PRO
SEQRES 21 A 367 LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO ASP
SEQRES 22 A 367 VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU LYS
SEQRES 23 A 367 ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU VAL
SEQRES 24 A 367 ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA LEU
SEQRES 25 A 367 GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER GLU
SEQRES 26 A 367 ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN LEU
SEQRES 27 A 367 ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU LEU
SEQRES 28 A 367 ILE TYR LYS GLU VAL MET ASP TRP ARG LYS GLY ILE ILE
SEQRES 29 A 367 THR ILE THR
HET 1V5 A 401 60
HETNAM 1V5 N-[1-(4-FLUOROPHENYL)CYCLOPROPYL]-4-[(TRANS-4-
HETNAM 2 1V5 HYDROXYCYCLOHEXYL)AMINO]IMIDAZO[1,2-A]QUINOXALINE-8-
HETNAM 3 1V5 CARBOXAMIDE
FORMUL 2 1V5 C26 H26 F N5 O2
FORMUL 3 HOH *449(H2 O)
HELIX 1 1 ASN A 63 VAL A 80 1 18
HELIX 2 2 LEU A 115 GLN A 120 1 6
HELIX 3 3 ASP A 124 SER A 144 1 21
HELIX 4 4 LYS A 153 SER A 155 5 3
HELIX 5 5 ALA A 193 LEU A 198 1 6
HELIX 6 6 ASN A 205 HIS A 221 1 17
HELIX 7 7 ASP A 229 GLY A 242 1 14
HELIX 8 8 CYS A 245 LYS A 250 1 6
HELIX 9 9 GLN A 253 ARG A 263 1 11
HELIX 10 10 SER A 270 PHE A 275 1 6
HELIX 11 11 PRO A 276 PHE A 280 5 5
HELIX 12 12 LYS A 290 LEU A 302 1 13
HELIX 13 13 SER A 311 HIS A 318 1 8
HELIX 14 14 ILE A 321 TYR A 325 5 5
HELIX 15 15 ASP A 326 GLU A 331 1 6
HELIX 16 16 THR A 348 GLY A 366 1 19
SHEET 1 A 2 PHE A 10 ILE A 15 0
SHEET 2 A 2 SER A 18 LEU A 23 -1 O SER A 18 N ILE A 15
SHEET 1 B 5 TYR A 26 GLY A 33 0
SHEET 2 B 5 ILE A 39 ASP A 45 -1 O VAL A 40 N ILE A 32
SHEET 3 B 5 ARG A 50 SER A 58 -1 O ILE A 54 N CYS A 41
SHEET 4 B 5 ASP A 103 GLU A 109 -1 O VAL A 104 N LEU A 57
SHEET 5 B 5 ASN A 90 PHE A 92 -1 N PHE A 92 O TYR A 105
SHEET 1 C 3 ALA A 113 ASN A 114 0
SHEET 2 C 3 ILE A 157 VAL A 159 -1 O VAL A 159 N ALA A 113
SHEET 3 C 3 LEU A 165 ILE A 167 -1 O LYS A 166 N VAL A 158
CISPEP 1 GLY A 33 SER A 34 0 -4.87
SITE 1 AC1 19 GLN A 37 GLY A 38 VAL A 40 ALA A 53
SITE 2 AC1 19 LYS A 55 LYS A 56 LEU A 57 GLU A 109
SITE 3 AC1 19 MET A 111 ASP A 112 ALA A 113 ASN A 114
SITE 4 AC1 19 GLN A 117 ASN A 156 LEU A 168 HOH A 554
SITE 5 AC1 19 HOH A 569 HOH A 771 HOH A 816
CRYST1 135.802 135.802 94.208 90.00 90.00 120.00 H 3 9
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 0.007364 0.004251 0.000000 0.00000
SCALE2 0.000000 0.008503 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010615 0.00000
(ATOM LINES ARE NOT SHOWN.)
END