HEADER TRANSFERASE 21-AUG-17 5Y8U
TITLE CRYSTAL STRUCTURE OF THE C276S MUTANT OF MAP2K7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 103-419;
COMPND 5 SYNONYM: MAPKK 7,JNK-ACTIVATING KINASE 2,MAPK/ERK KINASE 7,MEK 7,
COMPND 6 STRESS-ACTIVATED PROTEIN KINASE KINASE 4,SAPKK4,C-JUN N-TERMINAL
COMPND 7 KINASE KINASE 2,JNKK 2;
COMPND 8 EC: 2.7.12.2;
COMPND 9 ENGINEERED: YES;
COMPND 10 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: MAP2K7, JNKK2, MEK7, MKK7, PRKMK7, SKK4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 37762
KEYWDS TRANSFERASE, PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KINOSHITA
REVDAT 3 22-NOV-23 5Y8U 1 REMARK
REVDAT 2 25-OCT-17 5Y8U 1 JRNL
REVDAT 1 11-OCT-17 5Y8U 0
JRNL AUTH T.KINOSHITA,T.HASHIMOTO,Y.SOGABE,H.FUKADA,T.MATSUMOTO,M.SAWA
JRNL TITL HIGH-RESOLUTION STRUCTURE DISCLOSES THE POTENTIAL FOR
JRNL TITL 2 ALLOSTERIC REGULATION OF MITOGEN-ACTIVATED PROTEIN KINASE
JRNL TITL 3 KINASE 7
JRNL REF BIOCHEM. BIOPHYS. RES. V. 493 313 2017
JRNL REF 2 COMMUN.
JRNL REFN ESSN 1090-2104
JRNL PMID 28890347
JRNL DOI 10.1016/J.BBRC.2017.09.025
REMARK 2
REMARK 2 RESOLUTION. 2.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 8909
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 467
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) : 2.92
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 644
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 32
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2117
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.52000
REMARK 3 B22 (A**2) : -3.52000
REMARK 3 B33 (A**2) : 11.41000
REMARK 3 B12 (A**2) : -1.76000
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): 1.663
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.435
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.347
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 38.123
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2157 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2114 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2899 ; 1.689 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4875 ; 0.867 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 262 ; 8.564 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 94 ;38.382 ;23.830
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 403 ;22.139 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;18.639 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 319 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2371 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 477 ; 0.001 ; 0.020
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): 1063 ; 3.874 ; 5.426
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1062 ; 3.876 ; 5.422
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1320 ; 6.360 ; 8.099
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1321 ; 6.357 ; 8.103
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1093 ; 3.843 ; 5.615
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1091 ; 3.819 ; 5.610
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1579 ; 6.239 ; 8.282
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8731 ;11.839 ;49.194
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8729 ;11.840 ;49.198
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 : NULL
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 5Y8U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004847.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9446
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.920
REMARK 200 RESOLUTION RANGE LOW (A) : 61.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 20.00
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.00
REMARK 200 R MERGE FOR SHELL (I) : 0.80200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5B2K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM CITRATE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 87.43500
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 174.87000
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 131.15250
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 218.58750
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 43.71750
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 87.43500
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 174.87000
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 218.58750
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 131.15250
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 43.71750
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 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 LYS A 173
REMARK 465 GLU A 174
REMARK 465 GLU A 175
REMARK 465 ASN A 176
REMARK 465 LYS A 177
REMARK 465 ARG A 178
REMARK 465 ILE A 179
REMARK 465 LEU A 180
REMARK 465 MET A 181
REMARK 465 SER A 281
REMARK 465 GLY A 282
REMARK 465 ARG A 283
REMARK 465 LEU A 284
REMARK 465 VAL A 285
REMARK 465 ASP A 286
REMARK 465 SER A 287
REMARK 465 LYS A 288
REMARK 465 ALA A 289
REMARK 465 LYS A 290
REMARK 465 THR A 291
REMARK 465 ARG A 292
REMARK 465 SER A 293
REMARK 465 PRO A 310
REMARK 465 THR A 311
REMARK 465 LYS A 312
REMARK 465 PRO A 313
REMARK 465 ASP A 314
REMARK 465 TYR A 315
REMARK 465 LYS A 342
REMARK 465 THR A 343
REMARK 465 ASP A 344
REMARK 465 PHE A 345
REMARK 465 GLU A 346
REMARK 465 SER A 419
REMARK 465 PRO A 420
REMARK 465 ARG A 421
REMARK 465 THR A 422
REMARK 465 SER A 423
REMARK 465 GLY A 424
REMARK 465 VAL A 425
REMARK 465 LEU A 426
REMARK 465 SER A 427
REMARK 465 GLN A 428
REMARK 465 PRO A 429
REMARK 465 HIS A 430
REMARK 465 LEU A 431
REMARK 465 PRO A 432
REMARK 465 PHE A 433
REMARK 465 PHE A 434
REMARK 465 ARG A 435
REMARK 465 HIS A 436
REMARK 465 HIS A 437
REMARK 465 HIS A 438
REMARK 465 HIS A 439
REMARK 465 HIS A 440
REMARK 465 HIS A 441
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 OH TYR A 247 OH TYR A 247 10444 2.01
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 PRO A 307 C - N - CD ANGL. DEV. = 12.7 DEGREES
REMARK 500 PRO A 308 C - N - CD ANGL. DEV. = 19.0 DEGREES
REMARK 500 ASP A 316 CB - CA - C ANGL. DEV. = -13.2 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 ILE A 133 -37.93 -35.36
REMARK 500 CYS A 147 -157.82 -134.34
REMARK 500 ARG A 156 -38.74 -32.75
REMARK 500 SER A 170 -154.27 -119.40
REMARK 500 VAL A 185 39.17 -79.95
REMARK 500 ASN A 205 -8.34 -57.52
REMARK 500 CYS A 218 159.95 -47.02
REMARK 500 GLN A 227 49.98 36.82
REMARK 500 ASP A 259 44.12 -167.61
REMARK 500 ALA A 297 64.93 63.11
REMARK 500 ALA A 298 44.79 -98.49
REMARK 500 GLU A 303 7.56 -69.34
REMARK 500 ARG A 304 53.78 -100.44
REMARK 500 ILE A 305 12.77 -150.98
REMARK 500 ASN A 340 -17.97 -48.88
REMARK 500 LEU A 348 70.25 47.96
REMARK 500 LEU A 358 -175.54 -67.06
REMARK 500 HIS A 362 50.68 -141.68
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5Y8U A 119 435 UNP O14733 MP2K7_HUMAN 103 419
SEQADV 5Y8U SER A 276 UNP O14733 CYS 260 ENGINEERED MUTATION
SEQADV 5Y8U HIS A 436 UNP O14733 EXPRESSION TAG
SEQADV 5Y8U HIS A 437 UNP O14733 EXPRESSION TAG
SEQADV 5Y8U HIS A 438 UNP O14733 EXPRESSION TAG
SEQADV 5Y8U HIS A 439 UNP O14733 EXPRESSION TAG
SEQADV 5Y8U HIS A 440 UNP O14733 EXPRESSION TAG
SEQADV 5Y8U HIS A 441 UNP O14733 EXPRESSION TAG
SEQRES 1 A 323 THR GLY TYR LEU THR ILE GLY GLY GLN ARG TYR GLN ALA
SEQRES 2 A 323 GLU ILE ASN ASP LEU GLU ASN LEU GLY GLU MET GLY SER
SEQRES 3 A 323 GLY THR CYS GLY GLN VAL TRP LYS MET ARG PHE ARG LYS
SEQRES 4 A 323 THR GLY HIS VAL ILE ALA VAL LYS GLN MET ARG ARG SER
SEQRES 5 A 323 GLY ASN LYS GLU GLU ASN LYS ARG ILE LEU MET ASP LEU
SEQRES 6 A 323 ASP VAL VAL LEU LYS SER HIS ASP CYS PRO TYR ILE VAL
SEQRES 7 A 323 GLN CYS PHE GLY THR PHE ILE THR ASN THR ASP VAL PHE
SEQRES 8 A 323 ILE ALA MET GLU LEU MET GLY THR CYS ALA GLU LYS LEU
SEQRES 9 A 323 LYS LYS ARG MET GLN GLY PRO ILE PRO GLU ARG ILE LEU
SEQRES 10 A 323 GLY LYS MET THR VAL ALA ILE VAL LYS ALA LEU TYR TYR
SEQRES 11 A 323 LEU LYS GLU LYS HIS GLY VAL ILE HIS ARG ASP VAL LYS
SEQRES 12 A 323 PRO SER ASN ILE LEU LEU ASP GLU ARG GLY GLN ILE LYS
SEQRES 13 A 323 LEU SER ASP PHE GLY ILE SER GLY ARG LEU VAL ASP SER
SEQRES 14 A 323 LYS ALA LYS THR ARG SER ALA GLY CYS ALA ALA TYR MET
SEQRES 15 A 323 ALA PRO GLU ARG ILE ASP PRO PRO ASP PRO THR LYS PRO
SEQRES 16 A 323 ASP TYR ASP ILE ARG ALA ASP VAL TRP SER LEU GLY ILE
SEQRES 17 A 323 SER LEU VAL GLU LEU ALA THR GLY GLN PHE PRO TYR LYS
SEQRES 18 A 323 ASN CYS LYS THR ASP PHE GLU VAL LEU THR LYS VAL LEU
SEQRES 19 A 323 GLN GLU GLU PRO PRO LEU LEU PRO GLY HIS MET GLY PHE
SEQRES 20 A 323 SER GLY ASP PHE GLN SER PHE VAL LYS ASP CYS LEU THR
SEQRES 21 A 323 LYS ASP HIS ARG LYS ARG PRO LYS TYR ASN LYS LEU LEU
SEQRES 22 A 323 GLU HIS SER PHE ILE LYS ARG TYR GLU THR LEU GLU VAL
SEQRES 23 A 323 ASP VAL ALA SER TRP PHE LYS ASP VAL MET ALA LYS THR
SEQRES 24 A 323 GLU SER PRO ARG THR SER GLY VAL LEU SER GLN PRO HIS
SEQRES 25 A 323 LEU PRO PHE PHE ARG HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *20(H2 O)
HELIX 1 AA1 GLU A 132 LEU A 136 5 5
HELIX 2 AA2 VAL A 186 HIS A 190 5 5
HELIX 3 AA3 ALA A 219 GLN A 227 1 9
HELIX 4 AA4 PRO A 231 GLY A 254 1 24
HELIX 5 AA5 LYS A 261 SER A 263 5 3
HELIX 6 AA6 ARG A 318 GLY A 334 1 17
HELIX 7 AA7 THR A 349 GLU A 354 1 6
HELIX 8 AA8 SER A 366 LEU A 377 1 12
HELIX 9 AA9 LYS A 386 LEU A 391 1 6
HELIX 10 AB1 HIS A 393 LEU A 402 1 10
HELIX 11 AB2 ASP A 405 MET A 414 1 10
SHEET 1 AA1 2 TYR A 121 ILE A 124 0
SHEET 2 AA1 2 GLN A 127 GLN A 130 -1 O TYR A 129 N LEU A 122
SHEET 1 AA2 5 GLU A 137 MET A 142 0
SHEET 2 AA2 5 VAL A 150 ARG A 154 -1 O LYS A 152 N LEU A 139
SHEET 3 AA2 5 VAL A 161 ARG A 168 -1 O VAL A 164 N TRP A 151
SHEET 4 AA2 5 ASP A 207 MET A 212 -1 O MET A 212 N ALA A 163
SHEET 5 AA2 5 CYS A 198 ILE A 203 -1 N PHE A 199 O ALA A 211
SHEET 1 AA3 3 THR A 217 CYS A 218 0
SHEET 2 AA3 3 ILE A 265 LEU A 267 -1 O LEU A 267 N THR A 217
SHEET 3 AA3 3 ILE A 273 LEU A 275 -1 O LYS A 274 N LEU A 266
CISPEP 1 PRO A 307 PRO A 308 0 0.04
CRYST1 71.534 71.534 262.305 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 0.013979 0.008071 0.000000 0.00000
SCALE2 0.000000 0.016142 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003812 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
