HEADER TRANSFERASE 04-FEB-13 3ZLX
TITLE CRYSTAL STRUCTURE OF MEK1 IN COMPLEX WITH FRAGMENT 18
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAP KINASE KINASE 1, MAPKK 1, MKK1, ERK ACTIVATOR KINASE 1,
COMPND 5 MAPK/ERK KINASE 1, MEK 1, MEK1;
COMPND 6 EC: 2.7.12.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF21
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.AMANING,M.LOWINSKY,F.VALLEE,V.STEIER,C.MARCIREAU,A.UGOLINI,
AUTHOR 2 C.DELORME,G.MCCORT,C.ANDOUCHE,S.VOUGIER,S.LLOPART,N.HALLAND,A.RAK
REVDAT 4 24-APR-19 3ZLX 1 SOURCE
REVDAT 3 02-MAY-18 3ZLX 1 REMARK
REVDAT 2 29-MAY-13 3ZLX 1 JRNL
REVDAT 1 22-MAY-13 3ZLX 0
JRNL AUTH K.AMANING,M.LOWINSKI,F.VALLEE,V.STEIER,C.MARCIREAU,
JRNL AUTH 2 A.UGOLINI,C.DELORME,F.FOUCALT,G.MCCORT,N.DERIMAY,C.ANDOUCHE,
JRNL AUTH 3 S.VOUGIER,S.LLOPART,N.HALLAND,A.RAK
JRNL TITL THE USE OF VIRTUAL SCREENING AND DIFFERENTIAL SCANNING
JRNL TITL 2 FLUORIMETRY FOR THE RAPID IDENTIFICATION OF FRAGMENTS ACTIVE
JRNL TITL 3 AGAINST MEK1.
JRNL REF BIOORG.MED.CHEM.LETT. V. 23 3620 2013
JRNL REFN ISSN 0960-894X
JRNL PMID 23648182
JRNL DOI 10.1016/J.BMCL.2013.04.003
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 20515
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1051
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.32
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.43
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2897
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2081
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2764
REMARK 3 BIN R VALUE (WORKING SET) : 0.2058
REMARK 3 BIN FREE R VALUE : 0.2582
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.59
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 133
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2438
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.05950
REMARK 3 B22 (A**2) : -0.05950
REMARK 3 B33 (A**2) : 0.11890
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.273
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.236
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.187
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.221
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.182
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2484 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3342 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 898 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 63 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 354 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2484 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 313 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2925 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.12
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.55
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ZLX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1290055728.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : 20598
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 63.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.000
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: APPROPRIATE SINGLE CRYSTALS WERE GROWN
REMARK 280 USING THIS SET-UP IN PEG 4000 18%, TRIS 100MM PH7.7, DMSO 2% AND
REMARK 280 CACL2 0.2M AND WERE EXTRACTED FROM THE LOW VOLUME DROPS, CRYO-
REMARK 280 PROTECTED IN MOTHER LIQUOR WITH 20% GLYCEROL AND FLASH COOLED
REMARK 280 FOR SYNCHROTRON COLLECTION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 73.91900
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 147.83800
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 110.87850
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 184.79750
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 36.95950
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 73.91900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 147.83800
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 184.79750
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 110.87850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.95950
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2037 LIES ON A SPECIAL POSITION.
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 GLY A 36
REMARK 465 LEU A 37
REMARK 465 GLU A 38
REMARK 465 ASN A 221
REMARK 465 SER A 222
REMARK 465 PHE A 223
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 ASN A 298
REMARK 465 LYS A 299
REMARK 465 LYS 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 PRO A 306
REMARK 465 GLN A 383
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 ALA A 220 C O CB
REMARK 470 CYS A 277 C O CB SG
REMARK 470 ASN A 382 C O CB CG OD1 ND2
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 2034 O HOH A 2034 9554 1.25
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 ASP A 136 67.45 37.55
REMARK 500 ARG A 189 -17.62 80.52
REMARK 500 ASP A 190 51.28 -140.66
REMARK 500 HIS A 239 105.65 -48.69
REMARK 500 SER A 241 -159.20 -128.10
REMARK 500 VAL A 329 -36.39 -134.89
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 5EZ A 1383
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZLS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MEK1 IN COMPLEX WITH FRAGMENT SAR198059
REMARK 900 RELATED ID: 3ZLW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MEK1 IN COMPLEX WITH FRAGMENT 3
REMARK 900 RELATED ID: 3ZLY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MEK1 IN COMPLEX WITH FRAGMENT 8
REMARK 900 RELATED ID: 3ZM4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MEK1 IN COMPLEX WITH FRAGMENT 1
DBREF 3ZLX A 37 383 UNP Q02750 MP2K1_HUMAN 37 383
SEQADV 3ZLX GLY A 36 UNP Q02750 EXPRESSION TAG
SEQADV 3ZLX ASN A 298 UNP Q02750 SER 298 ENGINEERED MUTATION
SEQADV 3ZLX LYS A 299 UNP Q02750 SER 299 ENGINEERED MUTATION
SEQADV 3ZLX LYS A 300 UNP Q02750 TYR 300 ENGINEERED MUTATION
SEQRES 1 A 348 GLY LEU GLU GLU LEU GLU LEU ASP GLU GLN GLN ARG LYS
SEQRES 2 A 348 ARG LEU GLU ALA PHE LEU THR GLN LYS GLN LYS VAL GLY
SEQRES 3 A 348 GLU LEU LYS ASP ASP ASP PHE GLU LYS ILE SER GLU LEU
SEQRES 4 A 348 GLY ALA GLY ASN GLY GLY VAL VAL PHE LYS VAL SER HIS
SEQRES 5 A 348 LYS PRO SER GLY LEU VAL MET ALA ARG LYS LEU ILE HIS
SEQRES 6 A 348 LEU GLU ILE LYS PRO ALA ILE ARG ASN GLN ILE ILE ARG
SEQRES 7 A 348 GLU LEU GLN VAL LEU HIS GLU CYS ASN SER PRO TYR ILE
SEQRES 8 A 348 VAL GLY PHE TYR GLY ALA PHE TYR SER ASP GLY GLU ILE
SEQRES 9 A 348 SER ILE CYS MET GLU HIS MET ASP GLY GLY SER LEU ASP
SEQRES 10 A 348 GLN VAL LEU LYS LYS ALA GLY ARG ILE PRO GLU GLN ILE
SEQRES 11 A 348 LEU GLY LYS VAL SER ILE ALA VAL ILE LYS GLY LEU THR
SEQRES 12 A 348 TYR LEU ARG GLU LYS HIS LYS ILE MET HIS ARG ASP VAL
SEQRES 13 A 348 LYS PRO SER ASN ILE LEU VAL ASN SER ARG GLY GLU ILE
SEQRES 14 A 348 LYS LEU CYS ASP PHE GLY VAL SER GLY GLN LEU ILE ASP
SEQRES 15 A 348 SER MET ALA ASN SER PHE VAL GLY THR ARG SER TYR MET
SEQRES 16 A 348 SER PRO GLU ARG LEU GLN GLY THR HIS TYR SER VAL GLN
SEQRES 17 A 348 SER ASP ILE TRP SER MET GLY LEU SER LEU VAL GLU MET
SEQRES 18 A 348 ALA VAL GLY ARG TYR PRO ILE PRO PRO PRO ASP ALA LYS
SEQRES 19 A 348 GLU LEU GLU LEU MET PHE GLY CYS GLN VAL GLU GLY ASP
SEQRES 20 A 348 ALA ALA GLU THR PRO PRO ARG PRO ARG THR PRO GLY ARG
SEQRES 21 A 348 PRO LEU ASN LYS LYS GLY MET ASP SER ARG PRO PRO MET
SEQRES 22 A 348 ALA ILE PHE GLU LEU LEU ASP TYR ILE VAL ASN GLU PRO
SEQRES 23 A 348 PRO PRO LYS LEU PRO SER GLY VAL PHE SER LEU GLU PHE
SEQRES 24 A 348 GLN ASP PHE VAL ASN LYS CYS LEU ILE LYS ASN PRO ALA
SEQRES 25 A 348 GLU ARG ALA ASP LEU LYS GLN LEU MET VAL HIS ALA PHE
SEQRES 26 A 348 ILE LYS ARG SER ASP ALA GLU GLU VAL ASP PHE ALA GLY
SEQRES 27 A 348 TRP LEU CYS SER THR ILE GLY LEU ASN GLN
HET 5EZ A1383 19
HETNAM 5EZ 7-CHORO-6-[(3R)-PYRROLIDIN-3-YLMETHOXY]ISOQUINOLIN-
HETNAM 2 5EZ 1(2H)-ONE
FORMUL 2 5EZ C14 H15 CL N2 O2
FORMUL 3 HOH *91(H2 O)
HELIX 1 1 ASP A 43 LYS A 59 1 17
HELIX 2 2 LYS A 64 ASP A 66 5 3
HELIX 3 3 LYS A 104 GLN A 116 1 13
HELIX 4 4 VAL A 117 GLU A 120 5 4
HELIX 5 5 SER A 150 GLY A 159 1 10
HELIX 6 6 PRO A 162 LYS A 185 1 24
HELIX 7 7 LYS A 192 SER A 194 5 3
HELIX 8 8 SER A 212 MET A 219 1 8
HELIX 9 9 SER A 231 GLN A 236 1 6
HELIX 10 10 VAL A 242 GLY A 259 1 18
HELIX 11 11 ASP A 267 GLY A 276 1 10
HELIX 12 12 ALA A 309 GLU A 320 1 12
HELIX 13 13 SER A 331 ILE A 343 1 13
HELIX 14 14 ASP A 351 VAL A 357 1 7
HELIX 15 15 HIS A 358 GLU A 367 1 10
HELIX 16 16 ASP A 370 GLY A 380 1 11
SHEET 1 AA 5 PHE A 68 ALA A 76 0
SHEET 2 AA 5 GLY A 80 HIS A 87 -1 O VAL A 82 N LEU A 74
SHEET 3 AA 5 VAL A 93 HIS A 100 -1 O MET A 94 N VAL A 85
SHEET 4 AA 5 GLU A 138 MET A 143 -1 O ILE A 139 N ILE A 99
SHEET 5 AA 5 PHE A 129 SER A 135 -1 N TYR A 130 O CYS A 142
SHEET 1 AB 2 ILE A 196 VAL A 198 0
SHEET 2 AB 2 ILE A 204 LEU A 206 -1 O LYS A 205 N LEU A 197
CISPEP 1 ILE A 263 PRO A 264 0 2.06
SITE 1 AC1 12 LEU A 74 ALA A 76 ALA A 95 MET A 143
SITE 2 AC1 12 GLU A 144 HIS A 145 MET A 146 SER A 150
SITE 3 AC1 12 ASP A 152 GLN A 153 LEU A 197 HOH A2033
CRYST1 76.930 76.930 221.757 90.00 90.00 120.00 P 61 2 2 12
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 0.012999 0.007505 0.000000 0.00000
SCALE2 0.000000 0.015010 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004509 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
