HEADER TRANSFERASE 25-APR-19 6OPK
TITLE PHOSPHORYLATED ERK2 WITH VERTEX-11E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,
COMPND 5 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,
COMPND 6 MAPK 2;
COMPND 7 EC: 2.7.11.24;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: MAPK1, ERK2, MAPK, PRKM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ERK 2, MITOGEN ACTIVATED PROTEIN KINASE 2, MAP KINASE 2, SIGNALING
KEYWDS 2 PROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.P.VIGERS,J.RUDOLPH
REVDAT 3 18-DEC-19 6OPK 1 REMARK
REVDAT 2 14-AUG-19 6OPK 1 JRNL
REVDAT 1 31-JUL-19 6OPK 0
JRNL AUTH L.M.PEGRAM,J.C.LIDDLE,Y.XIAO,M.HOH,J.RUDOLPH,D.B.IVERSON,
JRNL AUTH 2 G.P.VIGERS,D.SMITH,H.ZHANG,W.WANG,J.G.MOFFAT,N.G.AHN
JRNL TITL ACTIVATION LOOP DYNAMICS ARE CONTROLLED BY
JRNL TITL 2 CONFORMATION-SELECTIVE INHIBITORS OF ERK2.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 15463 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31311868
JRNL DOI 10.1073/PNAS.1906824116
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 16372
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 896
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) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1191
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.3970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2839
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
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) : 73.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.02000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.388
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.262
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.224
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.702
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): 2945 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2709 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3996 ; 1.657 ; 1.664
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6299 ; 1.187 ; 1.575
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 345 ; 7.163 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 158 ;34.813 ;22.532
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 518 ;16.743 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;21.327 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 374 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3222 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 597 ; 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): 1383 ; 6.005 ; 7.623
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1382 ; 5.997 ; 7.621
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1727 ; 8.330 ;11.438
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1728 ; 8.329 ;11.440
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1562 ; 6.577 ; 8.093
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1526 ; 6.595 ; 8.149
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2218 ; 9.130 ;12.009
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3192 ;11.217 ;86.743
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3134 ;11.264 ;87.375
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 6OPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1000241143.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : DIALS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19482
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.470
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.93000
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: PHASER
REMARK 200 STARTING MODEL: 2ERK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16.5% PEG3350,100 MM TRIS-HCL PH 8.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 20.99300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.30050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.06950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.30050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.99300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.06950
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 ALA A 7
REMARK 465 GLY A 8
REMARK 465 GLY A 355
REMARK 465 TYR A 356
REMARK 465 ARG A 357
REMARK 465 SER A 358
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 VAL A 19 48.92 -107.64
REMARK 500 ARG A 146 7.16 80.93
REMARK 500 ASP A 147 48.83 -152.04
REMARK 500 ASP A 165 87.88 49.18
REMARK 500 ALA A 187 169.84 65.20
REMARK 500 ASN A 199 58.75 -143.14
REMARK 500 LEU A 292 42.26 -89.82
REMARK 500 LEU A 333 93.90 -66.24
REMARK 500 ARG A 351 -2.59 -49.74
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 390 A 401
DBREF 6OPK A 7 358 UNP P63086 MK01_RAT 7 358
SEQRES 1 A 352 ALA GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL
SEQRES 2 A 352 GLY PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY
SEQRES 3 A 352 ALA TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN
SEQRES 4 A 352 LYS VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU
SEQRES 5 A 352 HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS
SEQRES 6 A 352 ILE LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE
SEQRES 7 A 352 ASN ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS
SEQRES 8 A 352 ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU
SEQRES 9 A 352 TYR LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS
SEQRES 10 A 352 ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS
SEQRES 11 A 352 TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS
SEQRES 12 A 352 PRO SER ASN LEU LEU LEU ASN THR THR CYS ASP LEU LYS
SEQRES 13 A 352 ILE CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP
SEQRES 14 A 352 HIS ASP HIS THR GLY PHE LEU TPO GLU PTR VAL ALA THR
SEQRES 15 A 352 ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS
SEQRES 16 A 352 GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS
SEQRES 17 A 352 ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO
SEQRES 18 A 352 GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY
SEQRES 19 A 352 ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE
SEQRES 20 A 352 ILE ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO
SEQRES 21 A 352 HIS LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN
SEQRES 22 A 352 ALA ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU
SEQRES 23 A 352 THR PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA
SEQRES 24 A 352 LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER
SEQRES 25 A 352 ASP GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET
SEQRES 26 A 352 GLU LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU
SEQRES 27 A 352 ILE PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG
SEQRES 28 A 352 SER
MODRES 6OPK TPO A 183 THR MODIFIED RESIDUE
MODRES 6OPK PTR A 185 TYR MODIFIED RESIDUE
HET TPO A 183 11
HET PTR A 185 16
HET 390 A 401 34
HETNAM TPO PHOSPHOTHREONINE
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM 390 4-{2-[(2-CHLORO-4-FLUOROPHENYL)AMINO]-5-
HETNAM 2 390 METHYLPYRIMIDIN-4-YL}-N-[(1S)-1-(3-CHLOROPHENYL)-2-
HETNAM 3 390 HYDROXYETHYL]-1H-PYRROLE-2-CARBOXAMIDE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 2 390 C24 H20 CL2 F N5 O2
FORMUL 3 HOH *20(H2 O)
HELIX 1 AA1 HIS A 59 PHE A 76 1 18
HELIX 2 AA2 LEU A 110 GLN A 117 1 8
HELIX 3 AA3 SER A 120 ALA A 141 1 22
HELIX 4 AA4 LYS A 149 SER A 151 5 3
HELIX 5 AA5 THR A 188 ALA A 193 5 6
HELIX 6 AA6 PRO A 194 ASN A 199 1 6
HELIX 7 AA7 LYS A 205 ASN A 222 1 18
HELIX 8 AA8 HIS A 230 GLY A 243 1 14
HELIX 9 AA9 SER A 246 CYS A 252 1 7
HELIX 10 AB1 ASN A 255 SER A 264 1 10
HELIX 11 AB2 PRO A 272 PHE A 277 1 6
HELIX 12 AB3 ASP A 281 LEU A 292 1 12
HELIX 13 AB4 GLU A 301 ALA A 307 1 7
HELIX 14 AB5 HIS A 308 GLU A 312 5 5
HELIX 15 AB6 ASP A 316 GLU A 320 5 5
HELIX 16 AB7 LYS A 328 LEU A 333 5 6
HELIX 17 AB8 PRO A 337 ALA A 350 1 14
HELIX 18 AB9 ARG A 351 GLN A 353 5 3
SHEET 1 AA1 2 MET A 11 VAL A 12 0
SHEET 2 AA1 2 GLN A 15 VAL A 16 -1 O GLN A 15 N VAL A 12
SHEET 1 AA2 5 TYR A 23 GLY A 32 0
SHEET 2 AA2 5 GLY A 35 ASP A 42 -1 O VAL A 37 N GLY A 30
SHEET 3 AA2 5 VAL A 47 ILE A 54 -1 O LYS A 53 N MET A 36
SHEET 4 AA2 5 VAL A 99 ASP A 104 -1 O GLN A 103 N ALA A 50
SHEET 5 AA2 5 ASP A 86 ILE A 88 -1 N ASP A 86 O VAL A 102
SHEET 1 AA3 3 THR A 108 ASP A 109 0
SHEET 2 AA3 3 LEU A 153 LEU A 155 -1 O LEU A 155 N THR A 108
SHEET 3 AA3 3 LEU A 161 ILE A 163 -1 O LYS A 162 N LEU A 154
SHEET 1 AA4 2 VAL A 143 LEU A 144 0
SHEET 2 AA4 2 ARG A 170 VAL A 171 -1 O ARG A 170 N LEU A 144
LINK C LEU A 182 N TPO A 183 1555 1555 1.34
LINK C TPO A 183 N GLU A 184 1555 1555 1.33
LINK C GLU A 184 N PTR A 185 1555 1555 1.33
LINK C PTR A 185 N VAL A 186 1555 1555 1.34
SITE 1 AC1 13 ILE A 29 GLU A 31 TYR A 34 ALA A 50
SITE 2 AC1 13 LYS A 52 GLN A 103 ASP A 104 MET A 106
SITE 3 AC1 13 ASP A 109 LYS A 112 LEU A 154 ASP A 165
SITE 4 AC1 13 HOH A 506
CRYST1 41.986 78.139 152.601 90.00 90.00 90.00 P 21 21 21 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 0.023817 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012798 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006553 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
