HEADER TRANSFERASE 10-DEC-08 3FHR
TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF MITOGEN-ACTIVATED PROTEIN KINASE-
TITLE 2 ACTIVATED PROTEIN KINASE 3 (MK3)-INHIBITOR COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAP KINASE-ACTIVATED PROTEIN KINASE 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 33-349;
COMPND 5 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE-ACTIVATED PROTEIN KINASE 3
COMPND 6 (MK3), MAPK-ACTIVATED PROTEIN KINASE 3, MAPKAP KINASE 3, MAPKAPK-3,
COMPND 7 CHROMOSOME 3P KINASE, 3PK;
COMPND 8 EC: 2.7.11.1;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PROPRIETARY VECTOR
KEYWDS KINASE-INHIBITOR COMPLEX, ATP-BINDING, KINASE, NUCLEOTIDE-BINDING,
KEYWDS 2 NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN KINASE,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.K.Y.CHENG,J.BARKER,S.PALAN,B.FELICETTI,M.WHITTAKER,T.HESTERKAMP
REVDAT 3 20-MAR-24 3FHR 1 REMARK SEQADV
REVDAT 2 29-JAN-14 3FHR 1 JRNL VERSN
REVDAT 1 15-DEC-09 3FHR 0
JRNL AUTH R.CHENG,B.FELICETTI,S.PALAN,I.TOOGOOD-JOHNSON,C.SCHEICH,
JRNL AUTH 2 J.BARKER,M.WHITTAKER,T.HESTERKAMP
JRNL TITL HIGH-RESOLUTION CRYSTAL STRUCTURE OF HUMAN MAPKAP KINASE 3
JRNL TITL 2 IN COMPLEX WITH A HIGH AFFINITY LIGAND
JRNL REF PROTEIN SCI. V. 19 168 2010
JRNL REFN ISSN 0961-8368
JRNL PMID 19937655
JRNL DOI 10.1002/PRO.294
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 26526
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1423
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1681
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.3790
REMARK 3 BIN FREE R VALUE SET COUNT : 83
REMARK 3 BIN FREE R VALUE : 0.4760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2212
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 108
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.67000
REMARK 3 B22 (A**2) : -2.31000
REMARK 3 B33 (A**2) : -1.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.27000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.163
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.324
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2300 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3110 ; 1.581 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 6.298 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 111 ;36.417 ;24.505
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 416 ;18.099 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;19.233 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 335 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1736 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1141 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1529 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 159 ; 0.181 ; 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): 39 ; 0.205 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.221 ; 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): 1409 ; 0.973 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2210 ; 1.648 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1026 ; 2.211 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 898 ; 3.342 ; 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 3FHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9769
REMARK 200 MONOCHROMATOR : DOUBLE SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27952
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 31.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.370
REMARK 200 R MERGE (I) : 0.05100
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.54
REMARK 200 R MERGE FOR SHELL (I) : 0.45100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10%-15% PEG 3350, 100MM BISTRIS
REMARK 280 PROPANE/CITRIC ACID, PH 5.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 42.34400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.41600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 42.34400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.41600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 14
REMARK 465 ALA A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 HIS A 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 GLY A 24
REMARK 465 LEU A 25
REMARK 465 GLU A 26
REMARK 465 VAL A 27
REMARK 465 LEU A 28
REMARK 465 PHE A 29
REMARK 465 GLN A 30
REMARK 465 GLY A 31
REMARK 465 PRO A 32
REMARK 465 GLY A 134
REMARK 465 THR A 195
REMARK 465 GLN A 196
REMARK 465 ASN A 197
REMARK 465 ALA A 198
REMARK 465 LEU A 199
REMARK 465 GLN A 200
REMARK 465 THR A 201
REMARK 465 PRO A 202
REMARK 465 CYS A 203
REMARK 465 TYR A 204
REMARK 465 THR A 205
REMARK 465 PRO A 206
REMARK 465 TYR A 207
REMARK 465 TYR A 208
REMARK 465 VAL A 209
REMARK 465 ALA A 210
REMARK 465 PRO A 211
REMARK 465 GLU A 212
REMARK 465 VAL A 213
REMARK 465 LEU A 214
REMARK 465 GLY A 215
REMARK 465 PRO A 216
REMARK 465 TYR A 243
REMARK 465 SER A 244
REMARK 465 ASN A 245
REMARK 465 THR A 246
REMARK 465 GLY A 247
REMARK 465 GLN A 248
REMARK 465 ALA A 249
REMARK 465 ILE A 250
REMARK 465 SER A 251
REMARK 465 PRO A 252
REMARK 465 GLY A 253
REMARK 465 MET A 254
REMARK 465 LYS A 255
REMARK 465 ARG A 256
REMARK 465 ARG A 257
REMARK 465 ILE A 258
REMARK 465 ARG A 259
REMARK 465 LEU A 260
REMARK 465 GLY A 261
REMARK 465 GLN A 262
REMARK 465 TYR A 263
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 O26 P4O A 1 O HOH A 428 2.14
REMARK 500 O GLY A 123 O HOH A 387 2.17
REMARK 500 O HOH A 8 O HOH A 425 2.17
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 VAL A 39 CB - CA - C ANGL. DEV. = -12.2 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 MET A 121 77.07 -102.80
REMARK 500 ASP A 166 37.29 -152.62
REMARK 500 ASP A 187 91.12 72.02
REMARK 500 CYS A 237 -23.75 -146.79
REMARK 500 SER A 274 141.19 -34.29
REMARK 500 GLN A 312 34.09 -76.35
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 P4O A 1
DBREF 3FHR A 33 349 UNP Q16644 MAPK3_HUMAN 33 349
SEQADV 3FHR MET A 14 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR ALA A 15 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR HIS A 16 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR HIS A 17 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR HIS A 18 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR HIS A 19 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR HIS A 20 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR HIS A 21 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR SER A 22 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR SER A 23 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR GLY A 24 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR LEU A 25 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR GLU A 26 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR VAL A 27 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR LEU A 28 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR PHE A 29 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR GLN A 30 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR GLY A 31 UNP Q16644 EXPRESSION TAG
SEQADV 3FHR PRO A 32 UNP Q16644 EXPRESSION TAG
SEQRES 1 A 336 MET ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU
SEQRES 2 A 336 VAL LEU PHE GLN GLY PRO GLU PRO LYS LYS TYR ALA VAL
SEQRES 3 A 336 THR ASP ASP TYR GLN LEU SER LYS GLN VAL LEU GLY LEU
SEQRES 4 A 336 GLY VAL ASN GLY LYS VAL LEU GLU CYS PHE HIS ARG ARG
SEQRES 5 A 336 THR GLY GLN LYS CYS ALA LEU LYS LEU LEU TYR ASP SER
SEQRES 6 A 336 PRO LYS ALA ARG GLN GLU VAL ASP HIS HIS TRP GLN ALA
SEQRES 7 A 336 SER GLY GLY PRO HIS ILE VAL CYS ILE LEU ASP VAL TYR
SEQRES 8 A 336 GLU ASN MET HIS HIS GLY LYS ARG CYS LEU LEU ILE ILE
SEQRES 9 A 336 MET GLU CYS MET GLU GLY GLY GLU LEU PHE SER ARG ILE
SEQRES 10 A 336 GLN GLU ARG GLY ASP GLN ALA PHE THR GLU ARG GLU ALA
SEQRES 11 A 336 ALA GLU ILE MET ARG ASP ILE GLY THR ALA ILE GLN PHE
SEQRES 12 A 336 LEU HIS SER HIS ASN ILE ALA HIS ARG ASP VAL LYS PRO
SEQRES 13 A 336 GLU ASN LEU LEU TYR THR SER LYS GLU LYS ASP ALA VAL
SEQRES 14 A 336 LEU LYS LEU THR ASP PHE GLY PHE ALA LYS GLU THR THR
SEQRES 15 A 336 GLN ASN ALA LEU GLN THR PRO CYS TYR THR PRO TYR TYR
SEQRES 16 A 336 VAL ALA PRO GLU VAL LEU GLY PRO GLU LYS TYR ASP LYS
SEQRES 17 A 336 SER CYS ASP MET TRP SER LEU GLY VAL ILE MET TYR ILE
SEQRES 18 A 336 LEU LEU CYS GLY PHE PRO PRO PHE TYR SER ASN THR GLY
SEQRES 19 A 336 GLN ALA ILE SER PRO GLY MET LYS ARG ARG ILE ARG LEU
SEQRES 20 A 336 GLY GLN TYR GLY PHE PRO ASN PRO GLU TRP SER GLU VAL
SEQRES 21 A 336 SER GLU ASP ALA LYS GLN LEU ILE ARG LEU LEU LEU LYS
SEQRES 22 A 336 THR ASP PRO THR GLU ARG LEU THR ILE THR GLN PHE MET
SEQRES 23 A 336 ASN HIS PRO TRP ILE ASN GLN SER MET VAL VAL PRO GLN
SEQRES 24 A 336 THR PRO LEU HIS THR ALA ARG VAL LEU GLN GLU ASP LYS
SEQRES 25 A 336 ASP HIS TRP ASP GLU VAL LYS GLU GLU MET THR SER ALA
SEQRES 26 A 336 LEU ALA THR MET ARG VAL ASP TYR ASP GLN VAL
HET P4O A 1 26
HETNAM P4O 2-(2-QUINOLIN-3-YLPYRIDIN-4-YL)-1,5,6,7-TETRAHYDRO-4H-
HETNAM 2 P4O PYRROLO[3,2-C]PYRIDIN-4-ONE
FORMUL 2 P4O C21 H16 N4 O
FORMUL 3 HOH *108(H2 O)
HELIX 1 1 ALA A 38 ASP A 41 5 4
HELIX 2 2 SER A 78 SER A 92 1 15
HELIX 3 3 LEU A 126 GLU A 132 1 7
HELIX 4 4 THR A 139 HIS A 160 1 22
HELIX 5 5 LYS A 168 GLU A 170 5 3
HELIX 6 6 GLU A 217 GLY A 238 1 22
HELIX 7 7 SER A 274 LEU A 285 1 12
HELIX 8 8 ASP A 288 ARG A 292 5 5
HELIX 9 9 THR A 294 HIS A 301 1 8
HELIX 10 10 HIS A 301 GLN A 306 1 6
HELIX 11 11 SER A 307 VAL A 310 5 4
HELIX 12 12 HIS A 316 ASP A 324 1 9
HELIX 13 13 HIS A 327 VAL A 344 1 18
SHEET 1 A 5 TYR A 43 GLY A 53 0
SHEET 2 A 5 GLY A 56 HIS A 63 -1 O GLY A 56 N GLY A 53
SHEET 3 A 5 LYS A 69 TYR A 76 -1 O LEU A 72 N LEU A 59
SHEET 4 A 5 LYS A 111 GLU A 119 -1 O LEU A 114 N LEU A 75
SHEET 5 A 5 ILE A 100 HIS A 108 -1 N LEU A 101 O ILE A 117
SHEET 1 B 3 GLY A 124 GLU A 125 0
SHEET 2 B 3 LEU A 172 TYR A 174 -1 O TYR A 174 N GLY A 124
SHEET 3 B 3 LEU A 183 LEU A 185 -1 O LYS A 184 N LEU A 173
SHEET 1 C 2 ILE A 162 ALA A 163 0
SHEET 2 C 2 LYS A 192 GLU A 193 -1 O LYS A 192 N ALA A 163
CISPEP 1 ASN A 267 PRO A 268 0 0.36
SITE 1 AC1 17 LEU A 52 GLY A 53 VAL A 58 ALA A 71
SITE 2 AC1 17 LYS A 73 GLU A 119 MET A 121 GLU A 122
SITE 3 AC1 17 GLY A 124 ASN A 171 LEU A 173 THR A 186
SITE 4 AC1 17 ASP A 187 GLU A 275 HOH A 372 HOH A 428
SITE 5 AC1 17 HOH A 433
CRYST1 84.688 74.832 60.664 90.00 107.34 90.00 C 1 2 1 4
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 0.011808 0.000000 0.003687 0.00000
SCALE2 0.000000 0.013363 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017269 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
