HEADER TRANSFERASE/TRANSFERASE INHIBITOR 26-FEB-18 6CJ5
TITLE CRYSTAL STRUCTURE OF MNK2-D228G IN COMPLEX WITH INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAP KINASE-INTERACTING SERINE/THREONINE-PROTEIN KINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAP KINASE SIGNAL-INTEGRATING KINASE 2,MNK2;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MKNK2, GPRK7, MNK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K-12
KEYWDS INHIBITOR KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.HAN
REVDAT 1 09-MAY-18 6CJ5 0
JRNL AUTH S.H.REICH,P.A.SPRENGELER,G.G.CHIANG,J.R.APPLEMAN,J.CHEN,
JRNL AUTH 2 J.CLARINE,B.EAM,J.T.ERNST,Q.HAN,V.K.GOEL,E.Z.R.HAN,V.HUANG,
JRNL AUTH 3 I.N.J.HUNG,A.JEMISON,K.A.JESSEN,J.MOLTER,D.MURPHY,M.NEAL,
JRNL AUTH 4 G.S.PARKER,M.SHAGHAFI,S.SPERRY,J.STAUNTON,C.R.STUMPF,
JRNL AUTH 5 P.A.THOMPSON,C.TRAN,S.E.WEBBER,C.J.WEGERSKI,H.ZHENG,
JRNL AUTH 6 K.R.WEBSTER
JRNL TITL STRUCTURE-BASED DESIGN OF PYRIDONE-AMINAL EFT508 TARGETING
JRNL TITL 2 DYSREGULATED TRANSLATION BY SELECTIVE MITOGEN-ACTIVATED
JRNL TITL 3 PROTEIN KINASE INTERACTING KINASES 1 AND 2 (MNK1/2)
JRNL TITL 4 INHIBITION.
JRNL REF J. MED. CHEM. V. 61 3516 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29526098
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01795
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 11166
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 569
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 742
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 39
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2163
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 8
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.53000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : 0.79000
REMARK 3 B12 (A**2) : -0.26000
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): 0.554
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.353
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.273
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.905
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2230 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3008 ; 1.891 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 267 ; 8.825 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;43.794 ;24.071
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 382 ;20.337 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;20.788 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 319 ; 0.120 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1711 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 6CJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000232844.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11166
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 90.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-30% (W/V) POLYACRYLIC ACID 5100, 1
REMARK 280 -5% PEG 400, AND 50 MM HEPES (PH 7.5), VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 300.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 48.26667
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 24.13333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 24.13333
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 48.26667
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 LEU A 229
REMARK 465 GLY A 230
REMARK 465 SER A 231
REMARK 465 GLY A 232
REMARK 465 ILE A 233
REMARK 465 LYS A 234
REMARK 465 LEU A 235
REMARK 465 ASN A 236
REMARK 465 GLY A 237
REMARK 465 ASP A 238
REMARK 465 CYS A 239
REMARK 465 SER A 240
REMARK 465 PRO A 241
REMARK 465 ILE A 242
REMARK 465 SER A 243
REMARK 465 THR A 244
REMARK 465 PRO A 245
REMARK 465 GLU A 246
REMARK 465 LEU A 247
REMARK 465 LEU A 248
REMARK 465 THR A 249
REMARK 465 PRO A 250
REMARK 465 CYS A 251
REMARK 465 GLY A 300
REMARK 465 SER A 301
REMARK 465 ASP A 302
REMARK 465 TRP A 305
REMARK 465 ASP A 306
REMARK 465 ARG A 307
REMARK 465 GLY A 308
REMARK 465 GLU A 309
REMARK 465 ALA A 372
REMARK 465 PRO A 373
REMARK 465 GLU A 374
REMARK 465 ASN A 375
REMARK 465 THR A 376
REMARK 465 LEU A 377
REMARK 465 PRO A 378
REMARK 465 THR A 379
REMARK 465 PRO A 380
REMARK 465 MET A 381
REMARK 465 VAL A 382
REMARK 465 LEU A 383
REMARK 465 GLN A 384
REMARK 465 ARG A 385
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 ILE A 122 CD1
REMARK 470 GLY A 370 O
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 C HIS A 121 N ARG A 123 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 365 CG HIS A 365 CD2 0.055
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ILE A 122 N - CA - C ANGL. DEV. = -19.3 DEGREES
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 THR A 72 66.04 -114.31
REMARK 500 PHE A 75 -66.65 -132.91
REMARK 500 VAL A 89 125.64 70.83
REMARK 500 ALA A 94 34.00 -72.31
REMARK 500 HIS A 95 -94.88 176.27
REMARK 500 ALA A 96 -101.15 -64.02
REMARK 500 ARG A 97 135.78 -173.65
REMARK 500 THR A 106 -8.28 -140.53
REMARK 500 SER A 107 -12.55 73.65
REMARK 500 PRO A 119 155.29 -31.88
REMARK 500 HIS A 121 35.65 -83.66
REMARK 500 ILE A 122 6.31 -66.86
REMARK 500 SER A 124 -9.55 -58.87
REMARK 500 ASP A 153 -29.91 80.83
REMARK 500 ARG A 175 -51.92 69.81
REMARK 500 ARG A 204 -9.69 74.74
REMARK 500 SER A 253 8.52 -54.97
REMARK 500 PHE A 265 4.10 -62.91
REMARK 500 ALA A 313 -3.11 -50.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 299 SG
REMARK 620 2 CYS A 311 SG 111.1
REMARK 620 3 CYS A 314 SG 129.2 54.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F4G A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6CJE RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN
DBREF 6CJ5 A 72 385 UNP Q9HBH9 MKNK2_HUMAN 72 385
SEQADV 6CJ5 GLY A 70 UNP Q9HBH9 EXPRESSION TAG
SEQADV 6CJ5 SER A 71 UNP Q9HBH9 EXPRESSION TAG
SEQADV 6CJ5 GLY A 228 UNP Q9HBH9 ASP 228 ENGINEERED MUTATION
SEQRES 1 A 316 GLY SER THR ASP SER PHE SER GLY ARG PHE GLU ASP VAL
SEQRES 2 A 316 TYR GLN LEU GLN GLU ASP VAL LEU GLY GLU GLY ALA HIS
SEQRES 3 A 316 ALA ARG VAL GLN THR CYS ILE ASN LEU ILE THR SER GLN
SEQRES 4 A 316 GLU TYR ALA VAL LYS ILE ILE GLU LYS GLN PRO GLY HIS
SEQRES 5 A 316 ILE ARG SER ARG VAL PHE ARG GLU VAL GLU MET LEU TYR
SEQRES 6 A 316 GLN CYS GLN GLY HIS ARG ASN VAL LEU GLU LEU ILE GLU
SEQRES 7 A 316 PHE PHE GLU GLU GLU ASP ARG PHE TYR LEU VAL PHE GLU
SEQRES 8 A 316 LYS MET ARG GLY GLY SER ILE LEU SER HIS ILE HIS LYS
SEQRES 9 A 316 ARG ARG HIS PHE ASN GLU LEU GLU ALA SER VAL VAL VAL
SEQRES 10 A 316 GLN ASP VAL ALA SER ALA LEU ASP PHE LEU HIS ASN LYS
SEQRES 11 A 316 GLY ILE ALA HIS ARG ASP LEU LYS PRO GLU ASN ILE LEU
SEQRES 12 A 316 CYS GLU HIS PRO ASN GLN VAL SER PRO VAL LYS ILE CYS
SEQRES 13 A 316 ASP PHE GLY LEU GLY SER GLY ILE LYS LEU ASN GLY ASP
SEQRES 14 A 316 CYS SER PRO ILE SER THR PRO GLU LEU LEU THR PRO CYS
SEQRES 15 A 316 GLY SER ALA GLU TYR MET ALA PRO GLU VAL VAL GLU ALA
SEQRES 16 A 316 PHE SER GLU GLU ALA SER ILE TYR ASP LYS ARG CYS ASP
SEQRES 17 A 316 LEU TRP SER LEU GLY VAL ILE LEU TYR ILE LEU LEU SER
SEQRES 18 A 316 GLY TYR PRO PRO PHE VAL GLY ARG CYS GLY SER ASP CYS
SEQRES 19 A 316 GLY TRP ASP ARG GLY GLU ALA CYS PRO ALA CYS GLN ASN
SEQRES 20 A 316 MET LEU PHE GLU SER ILE GLN GLU GLY LYS TYR GLU PHE
SEQRES 21 A 316 PRO ASP LYS ASP TRP ALA HIS ILE SER CYS ALA ALA LYS
SEQRES 22 A 316 ASP LEU ILE SER LYS LEU LEU VAL ARG ASP ALA LYS GLN
SEQRES 23 A 316 ARG LEU SER ALA ALA GLN VAL LEU GLN HIS PRO TRP VAL
SEQRES 24 A 316 GLN GLY CYS ALA PRO GLU ASN THR LEU PRO THR PRO MET
SEQRES 25 A 316 VAL LEU GLN ARG
HET ZN A 401 1
HET F4G A 402 18
HETNAM ZN ZINC ION
HETNAM F4G 3-(PYRIDIN-3-YL)IMIDAZO[1,2-A]PYRIDINE-8-CARBOXAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 F4G C13 H10 N4 O
FORMUL 4 HOH *8(H2 O)
HELIX 1 AA1 ARG A 78 ASP A 81 5 4
HELIX 2 AA2 ILE A 122 CYS A 136 1 15
HELIX 3 AA3 SER A 166 ARG A 175 1 10
HELIX 4 AA4 ASN A 178 LYS A 199 1 22
HELIX 5 AA5 LYS A 207 GLU A 209 5 3
HELIX 6 AA6 GLY A 252 MET A 257 5 6
HELIX 7 AA7 ALA A 258 PHE A 265 1 8
HELIX 8 AA8 SER A 266 ASP A 273 1 8
HELIX 9 AA9 ARG A 275 GLY A 291 1 17
HELIX 10 AB1 CYS A 311 GLY A 325 1 15
HELIX 11 AB2 PRO A 330 ALA A 335 1 6
HELIX 12 AB3 SER A 338 LEU A 349 1 12
HELIX 13 AB4 SER A 358 HIS A 365 1 8
HELIX 14 AB5 HIS A 365 GLY A 370 1 6
SHEET 1 AA1 5 TYR A 83 LEU A 85 0
SHEET 2 AA1 5 ARG A 97 ASN A 103 -1 O ILE A 102 N GLN A 84
SHEET 3 AA1 5 GLU A 109 GLU A 116 -1 O TYR A 110 N CYS A 101
SHEET 4 AA1 5 ARG A 154 GLU A 160 -1 O PHE A 159 N ALA A 111
SHEET 5 AA1 5 LEU A 145 GLU A 150 -1 N GLU A 147 O VAL A 158
SHEET 1 AA2 2 ILE A 211 CYS A 213 0
SHEET 2 AA2 2 VAL A 222 ILE A 224 -1 O LYS A 223 N LEU A 212
SSBOND 1 CYS A 311 CYS A 314 1555 1555 2.07
LINK SG CYS A 299 ZN ZN A 401 1555 1555 2.00
LINK SG CYS A 311 ZN ZN A 401 1555 1555 2.44
LINK SG CYS A 314 ZN ZN A 401 1555 1555 1.93
CISPEP 1 SER A 220 PRO A 221 0 28.56
SITE 1 AC1 3 CYS A 299 CYS A 311 CYS A 314
SITE 1 AC2 6 LEU A 90 ALA A 111 MET A 162 GLY A 165
SITE 2 AC2 6 LEU A 212 ASP A 226
CRYST1 105.370 105.370 72.400 90.00 90.00 120.00 P 32 2 1 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 0.009490 0.005479 0.000000 0.00000
SCALE2 0.000000 0.010959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013812 0.00000
(ATOM LINES ARE NOT SHOWN.)
END