HEADER TRANSFERASE/INHIBITOR 07-DEC-11 3V01
TITLE DISCOVERY OF NOVEL ALLOSTERIC MEK INHIBITORS POSSESSING CLASSICAL AND
TITLE 2 NON-CLASSICAL BIDENTATE SER212 INTERACTIONS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 62-393;
COMPND 5 SYNONYM: MAP KINASE KINASE 1, MAPKK 1, MKK1, ERK ACTIVATOR KINASE 1,
COMPND 6 MAPK/ERK KINASE 1, MEK 1;
COMPND 7 EC: 2.7.12.2;
COMPND 8 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: MAP2K1, MEK1, PRKMK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24B
KEYWDS KINASE, TRANSFERASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.HEALD,P.JACKSON,P.SAVY,M.JONES,E.GANCIA,B.BURTON,R.NEWMAN,J.BOGGS,
AUTHOR 2 E.CHAN,J.CHAN,E.CHOO,M.MERCHANT,M.ULTSCH,C.WIESMANN,M.BELVIN,S.PRICE
REVDAT 3 13-SEP-23 3V01 1 REMARK SEQADV LINK
REVDAT 2 18-JUL-12 3V01 1 JRNL
REVDAT 1 09-MAY-12 3V01 0
JRNL AUTH R.A.HEALD,P.JACKSON,P.SAVY,M.JONES,E.GANCIA,B.BURTON,
JRNL AUTH 2 R.NEWMAN,J.BOGGS,E.CHAN,J.CHAN,E.CHOO,M.MERCHANT,P.RUDEWICZ,
JRNL AUTH 3 M.ULTSCH,C.WIESMANN,Q.YUE,M.BELVIN,S.PRICE
JRNL TITL DISCOVERY OF NOVEL ALLOSTERIC MITOGEN-ACTIVATED PROTEIN
JRNL TITL 2 KINASE KINASE (MEK) 1,2 INHIBITORS POSSESSING BIDENTATE
JRNL TITL 3 SER212 INTERACTIONS.
JRNL REF J.MED.CHEM. V. 55 4594 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22506516
JRNL DOI 10.1021/JM2017094
REMARK 2
REMARK 2 RESOLUTION. 2.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 12675
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 640
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.71
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 705
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 27
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.30000
REMARK 3 B22 (A**2) : 2.30000
REMARK 3 B33 (A**2) : -3.45000
REMARK 3 B12 (A**2) : 1.15000
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): 0.425
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.282
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.213
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.079
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2369 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2174 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3200 ; 1.628 ; 2.012
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5083 ; 0.794 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 286 ; 5.746 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;33.976 ;24.433
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 425 ;16.008 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.346 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 349 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2553 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 448 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 500 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2119 ; 0.172 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1148 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1404 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 45 ; 0.148 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.054 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 7 ; 0.103 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 30 ; 0.155 ; 0.200
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): 1450 ; 3.559 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 586 ; 0.695 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2318 ; 5.414 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1024 ; 3.548 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 882 ; 5.638 ; 5.000
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 501 A 503
REMARK 3 RESIDUE RANGE : A 61 A 382
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1506 21.2187 -9.1333
REMARK 3 T TENSOR
REMARK 3 T11: 0.0051 T22: -0.2240
REMARK 3 T33: 0.0058 T12: 0.1440
REMARK 3 T13: -0.0016 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.5250 L22: 1.1634
REMARK 3 L33: 5.5379 L12: 0.2058
REMARK 3 L13: -0.8587 L23: 0.5917
REMARK 3 S TENSOR
REMARK 3 S11: -0.2105 S12: 0.2005 S13: -0.4247
REMARK 3 S21: -0.1336 S22: 0.0549 S23: 0.2577
REMARK 3 S31: -0.2677 S32: -0.2238 S33: 0.1555
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3V01 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069423.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13330
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.2300
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1S9J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-20% W/V PEG8K, 0.1M HEPES, 250MM
REMARK 280 NH4H2PO4, 1MM TCEP, PH 7.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
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
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 86.34733
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 43.17367
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 0.00000
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 86.34733
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 43.17367
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 ASN A 221
REMARK 465 SER A 222
REMARK 465 PHE A 223
REMARK 465 GLY A 276
REMARK 465 CYS A 277
REMARK 465 GLN A 278
REMARK 465 VAL A 279
REMARK 465 GLU A 280
REMARK 465 GLY A 281
REMARK 465 ASP A 282
REMARK 465 ALA A 283
REMARK 465 ALA A 284
REMARK 465 GLU A 285
REMARK 465 THR A 286
REMARK 465 PRO A 287
REMARK 465 PRO A 288
REMARK 465 ARG A 289
REMARK 465 PRO A 290
REMARK 465 ARG A 291
REMARK 465 THR A 292
REMARK 465 PRO A 293
REMARK 465 GLY A 294
REMARK 465 ARG A 295
REMARK 465 PRO A 296
REMARK 465 LEU A 297
REMARK 465 SER A 298
REMARK 465 SER A 299
REMARK 465 TYR A 300
REMARK 465 GLY A 301
REMARK 465 MET A 302
REMARK 465 ASP A 303
REMARK 465 SER A 304
REMARK 465 ARG A 305
REMARK 465 GLN A 383
REMARK 465 PRO A 384
REMARK 465 SER A 385
REMARK 465 THR A 386
REMARK 465 PRO A 387
REMARK 465 THR A 388
REMARK 465 HIS A 389
REMARK 465 ALA A 390
REMARK 465 ALA A 391
REMARK 465 GLY A 392
REMARK 465 VAL A 393
REMARK 465 LEU A 394
REMARK 465 GLU A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
REMARK 465 HIS A 399
REMARK 465 HIS A 400
REMARK 465 HIS A 401
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 LYS A 362 C LYS A 362 O 0.145
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 ILE A 71 -63.34 -94.60
REMARK 500 ASN A 78 53.29 18.07
REMARK 500 GLU A 102 90.66 -66.98
REMARK 500 SER A 135 -91.27 -102.31
REMARK 500 ARG A 189 -7.02 88.60
REMARK 500 ASP A 190 55.41 -156.50
REMARK 500 SER A 241 -142.70 -173.22
REMARK 500 GLU A 367 151.82 -46.01
REMARK 500 LEU A 381 -75.47 -126.06
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 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 195 OD1
REMARK 620 2 ASP A 208 OD2 81.3
REMARK 620 3 ATP A 502 O1B 85.5 161.1
REMARK 620 4 ATP A 502 O2A 152.0 87.4 98.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3V0 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V04 RELATED DB: PDB
DBREF 3V01 A 62 393 UNP Q02750 MP2K1_HUMAN 62 393
SEQADV 3V01 MET A 61 UNP Q02750 EXPRESSION TAG
SEQADV 3V01 LEU A 394 UNP Q02750 EXPRESSION TAG
SEQADV 3V01 GLU A 395 UNP Q02750 EXPRESSION TAG
SEQADV 3V01 HIS A 396 UNP Q02750 EXPRESSION TAG
SEQADV 3V01 HIS A 397 UNP Q02750 EXPRESSION TAG
SEQADV 3V01 HIS A 398 UNP Q02750 EXPRESSION TAG
SEQADV 3V01 HIS A 399 UNP Q02750 EXPRESSION TAG
SEQADV 3V01 HIS A 400 UNP Q02750 EXPRESSION TAG
SEQADV 3V01 HIS A 401 UNP Q02750 EXPRESSION TAG
SEQRES 1 A 341 MET GLU LEU LYS ASP ASP ASP PHE GLU LYS ILE SER GLU
SEQRES 2 A 341 LEU GLY ALA GLY ASN GLY GLY VAL VAL PHE LYS VAL SER
SEQRES 3 A 341 HIS LYS PRO SER GLY LEU VAL MET ALA ARG LYS LEU ILE
SEQRES 4 A 341 HIS LEU GLU ILE LYS PRO ALA ILE ARG ASN GLN ILE ILE
SEQRES 5 A 341 ARG GLU LEU GLN VAL LEU HIS GLU CYS ASN SER PRO TYR
SEQRES 6 A 341 ILE VAL GLY PHE TYR GLY ALA PHE TYR SER ASP GLY GLU
SEQRES 7 A 341 ILE SER ILE CYS MET GLU HIS MET ASP GLY GLY SER LEU
SEQRES 8 A 341 ASP GLN VAL LEU LYS LYS ALA GLY ARG ILE PRO GLU GLN
SEQRES 9 A 341 ILE LEU GLY LYS VAL SER ILE ALA VAL ILE LYS GLY LEU
SEQRES 10 A 341 THR TYR LEU ARG GLU LYS HIS LYS ILE MET HIS ARG ASP
SEQRES 11 A 341 VAL LYS PRO SER ASN ILE LEU VAL ASN SER ARG GLY GLU
SEQRES 12 A 341 ILE LYS LEU CYS ASP PHE GLY VAL SER GLY GLN LEU ILE
SEQRES 13 A 341 ASP SER MET ALA ASN SER PHE VAL GLY THR ARG SER TYR
SEQRES 14 A 341 MET SER PRO GLU ARG LEU GLN GLY THR HIS TYR SER VAL
SEQRES 15 A 341 GLN SER ASP ILE TRP SER MET GLY LEU SER LEU VAL GLU
SEQRES 16 A 341 MET ALA VAL GLY ARG TYR PRO ILE PRO PRO PRO ASP ALA
SEQRES 17 A 341 LYS GLU LEU GLU LEU MET PHE GLY CYS GLN VAL GLU GLY
SEQRES 18 A 341 ASP ALA ALA GLU THR PRO PRO ARG PRO ARG THR PRO GLY
SEQRES 19 A 341 ARG PRO LEU SER SER TYR GLY MET ASP SER ARG PRO PRO
SEQRES 20 A 341 MET ALA ILE PHE GLU LEU LEU ASP TYR ILE VAL ASN GLU
SEQRES 21 A 341 PRO PRO PRO LYS LEU PRO SER GLY VAL PHE SER LEU GLU
SEQRES 22 A 341 PHE GLN ASP PHE VAL ASN LYS CYS LEU ILE LYS ASN PRO
SEQRES 23 A 341 ALA GLU ARG ALA ASP LEU LYS GLN LEU MET VAL HIS ALA
SEQRES 24 A 341 PHE ILE LYS ARG SER ASP ALA GLU GLU VAL ASP PHE ALA
SEQRES 25 A 341 GLY TRP LEU CYS SER THR ILE GLY LEU ASN GLN PRO SER
SEQRES 26 A 341 THR PRO THR HIS ALA ALA GLY VAL LEU GLU HIS HIS HIS
SEQRES 27 A 341 HIS HIS HIS
HET 3V0 A 501 27
HET ATP A 502 31
HET MG A 503 1
HETNAM 3V0 N-{[(2R)-2,3-DIHYDROXYPROPYL]OXY}-3-[(2-FLUORO-4-
HETNAM 2 3V0 IODOPHENYL)AMINO]FURO[3,2-C]PYRIDINE-2-CARBOXAMIDE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 2 3V0 C17 H15 F I N3 O5
FORMUL 3 ATP C10 H16 N5 O13 P3
FORMUL 4 MG MG 2+
HELIX 1 1 LYS A 64 ASP A 66 5 3
HELIX 2 2 ALA A 106 GLN A 116 1 11
HELIX 3 3 VAL A 117 CYS A 121 5 5
HELIX 4 4 SER A 150 GLY A 159 1 10
HELIX 5 5 PRO A 162 LYS A 185 1 24
HELIX 6 6 LYS A 192 SER A 194 5 3
HELIX 7 7 SER A 212 ALA A 220 1 9
HELIX 8 8 SER A 231 GLY A 237 1 7
HELIX 9 9 VAL A 242 GLY A 259 1 18
HELIX 10 10 ASP A 267 PHE A 275 1 9
HELIX 11 11 ALA A 309 GLU A 320 1 12
HELIX 12 12 SER A 331 LEU A 342 1 12
HELIX 13 13 ASP A 351 VAL A 357 1 7
HELIX 14 14 HIS A 358 GLU A 367 1 10
HELIX 15 15 ASP A 370 GLY A 380 1 11
SHEET 1 A 5 PHE A 68 ALA A 76 0
SHEET 2 A 5 VAL A 81 HIS A 87 -1 O LYS A 84 N ILE A 71
SHEET 3 A 5 VAL A 93 HIS A 100 -1 O ARG A 96 N PHE A 83
SHEET 4 A 5 GLU A 138 GLU A 144 -1 O MET A 143 N ALA A 95
SHEET 5 A 5 PHE A 129 TYR A 134 -1 N PHE A 133 O SER A 140
SHEET 1 B 2 ILE A 196 VAL A 198 0
SHEET 2 B 2 ILE A 204 LEU A 206 -1 O LYS A 205 N LEU A 197
LINK OD1 ASN A 195 MG MG A 503 1555 1555 2.23
LINK OD2 ASP A 208 MG MG A 503 1555 1555 1.99
LINK O1B ATP A 502 MG MG A 503 1555 1555 1.91
LINK O2A ATP A 502 MG MG A 503 1555 1555 2.01
CISPEP 1 ILE A 263 PRO A 264 0 2.19
SITE 1 AC1 14 GLY A 77 ASN A 78 GLY A 80 LYS A 97
SITE 2 AC1 14 VAL A 127 ILE A 141 ASP A 208 PHE A 209
SITE 3 AC1 14 GLY A 210 VAL A 211 SER A 212 LEU A 215
SITE 4 AC1 14 MET A 219 ATP A 502
SITE 1 AC2 18 ALA A 76 GLY A 77 ASN A 78 GLY A 80
SITE 2 AC2 18 VAL A 82 ALA A 95 LYS A 97 MET A 143
SITE 3 AC2 18 GLU A 144 MET A 146 SER A 150 GLN A 153
SITE 4 AC2 18 LYS A 192 SER A 194 ASN A 195 ASP A 208
SITE 5 AC2 18 3V0 A 501 MG A 503
SITE 1 AC3 4 LYS A 97 ASN A 195 ASP A 208 ATP A 502
CRYST1 81.619 81.619 129.521 90.00 90.00 120.00 P 62 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 0.012252 0.007074 0.000000 0.00000
SCALE2 0.000000 0.014147 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007721 0.00000
(ATOM LINES ARE NOT SHOWN.)
END