HEADER TRANSFERASE 19-JAN-18 6FJ0
TITLE CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN ADENOSINE DERIVATIVE
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 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GELIN,G.LABESSE
REVDAT 1 30-JAN-19 6FJ0 0
JRNL AUTH M.GELIN,S.POCHET,G.LABESSE
JRNL TITL CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN ADENOSINE
JRNL TITL 2 DERIVATIVE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 44235
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 4011
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.8152 - 5.0945 0.97 2805 132 0.2023 0.2179
REMARK 3 2 5.0945 - 4.0446 0.90 2536 161 0.1471 0.1602
REMARK 3 3 4.0446 - 3.5336 0.91 2610 127 0.1459 0.1623
REMARK 3 4 3.5336 - 3.2106 0.92 2678 125 0.1500 0.1776
REMARK 3 5 3.2106 - 2.9805 0.92 2666 128 0.1578 0.1543
REMARK 3 6 2.9805 - 2.8048 0.92 2642 137 0.1578 0.2048
REMARK 3 7 2.8048 - 2.6644 0.92 2603 157 0.1581 0.1774
REMARK 3 8 2.6644 - 2.5484 0.92 2588 156 0.1592 0.2010
REMARK 3 9 2.5484 - 2.4503 0.92 2663 148 0.1571 0.2100
REMARK 3 10 2.4503 - 2.3658 0.92 2621 152 0.1577 0.2092
REMARK 3 11 2.3658 - 2.2918 0.93 2609 159 0.1587 0.2046
REMARK 3 12 2.2918 - 2.2263 0.92 2652 142 0.1564 0.1854
REMARK 3 13 2.2263 - 2.1677 0.93 2690 138 0.1512 0.1809
REMARK 3 14 2.1677 - 2.1148 0.93 2568 172 0.1541 0.1904
REMARK 3 15 2.1148 - 2.0667 0.94 2723 167 0.1511 0.1657
REMARK 3 16 2.0667 - 2.0227 0.94 2657 134 0.1607 0.2090
REMARK 3 17 2.0227 - 1.9823 0.94 2751 102 0.1731 0.2356
REMARK 3 18 1.9823 - 1.9449 0.93 2672 112 0.1797 0.2291
REMARK 3 19 1.9449 - 1.9101 0.94 2721 152 0.1676 0.2059
REMARK 3 20 1.9101 - 1.8778 0.94 2702 114 0.1769 0.1946
REMARK 3 21 1.8778 - 1.8475 0.94 2680 135 0.1732 0.2362
REMARK 3 22 1.8475 - 1.8190 0.95 2775 100 0.1777 0.2194
REMARK 3 23 1.8190 - 1.7923 0.94 2663 139 0.1874 0.2262
REMARK 3 24 1.7923 - 1.7671 0.94 2762 135 0.2005 0.2420
REMARK 3 25 1.7671 - 1.7432 0.95 2681 134 0.2130 0.2763
REMARK 3 26 1.7432 - 1.7205 0.94 2681 151 0.2276 0.2948
REMARK 3 27 1.7205 - 1.6990 0.93 2654 141 0.2393 0.2438
REMARK 3 28 1.6990 - 1.6786 0.90 2627 126 0.2622 0.3392
REMARK 3 29 1.6786 - 1.6590 0.86 2411 135 0.2620 0.3263
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.10
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.3011 17.9893 30.6855
REMARK 3 T TENSOR
REMARK 3 T11: 0.4217 T22: 0.6493
REMARK 3 T33: 0.2639 T12: 0.0666
REMARK 3 T13: -0.1325 T23: 0.1671
REMARK 3 L TENSOR
REMARK 3 L11: 2.5677 L22: 0.5681
REMARK 3 L33: 2.3871 L12: -0.2996
REMARK 3 L13: -0.0525 L23: 1.0735
REMARK 3 S TENSOR
REMARK 3 S11: -0.2831 S12: -0.0755 S13: 0.8519
REMARK 3 S21: -0.2939 S22: 0.2689 S23: 0.1643
REMARK 3 S31: -0.9256 S32: -0.6505 S33: 0.2258
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 60 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0706 8.8663 30.9936
REMARK 3 T TENSOR
REMARK 3 T11: 0.1949 T22: 0.4482
REMARK 3 T33: 0.0702 T12: -0.0796
REMARK 3 T13: -0.0910 T23: 0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 0.4828 L22: 0.4888
REMARK 3 L33: 3.6630 L12: -0.0969
REMARK 3 L13: 0.0901 L23: -0.2324
REMARK 3 S TENSOR
REMARK 3 S11: -0.1651 S12: 0.1742 S13: 0.0952
REMARK 3 S21: -0.2365 S22: 0.1558 S23: -0.1051
REMARK 3 S31: -0.1761 S32: 0.0550 S33: -0.0639
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 99 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3773 8.8582 49.5505
REMARK 3 T TENSOR
REMARK 3 T11: 0.0572 T22: 0.3034
REMARK 3 T33: 0.1355 T12: 0.0188
REMARK 3 T13: 0.0051 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 1.1710 L22: 1.1608
REMARK 3 L33: 1.1525 L12: 0.2946
REMARK 3 L13: 0.2995 L23: 0.1793
REMARK 3 S TENSOR
REMARK 3 S11: -0.0339 S12: -0.0187 S13: 0.1767
REMARK 3 S21: -0.0245 S22: 0.0367 S23: 0.2295
REMARK 3 S31: -0.0819 S32: -0.2698 S33: 0.0431
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6512 10.0383 45.1682
REMARK 3 T TENSOR
REMARK 3 T11: 0.1608 T22: 0.3612
REMARK 3 T33: 0.1919 T12: -0.0076
REMARK 3 T13: 0.0086 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 2.3122 L22: 0.5098
REMARK 3 L33: 1.2510 L12: 1.0997
REMARK 3 L13: 1.2445 L23: 0.5196
REMARK 3 S TENSOR
REMARK 3 S11: -0.2135 S12: 0.3273 S13: 0.0909
REMARK 3 S21: -0.0396 S22: 0.2550 S23: -0.2273
REMARK 3 S31: -0.2067 S32: 0.2880 S33: 0.0020
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 189 THROUGH 319 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3373 10.1109 60.9377
REMARK 3 T TENSOR
REMARK 3 T11: 0.0893 T22: 0.2549
REMARK 3 T33: 0.1065 T12: -0.0005
REMARK 3 T13: -0.0038 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 1.7480 L22: 1.2347
REMARK 3 L33: 0.9052 L12: 1.1016
REMARK 3 L13: 0.6919 L23: 0.2730
REMARK 3 S TENSOR
REMARK 3 S11: 0.0375 S12: -0.0871 S13: 0.0960
REMARK 3 S21: 0.1034 S22: -0.0591 S23: -0.0011
REMARK 3 S31: -0.0235 S32: 0.0691 S33: 0.0154
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 320 THROUGH 353 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4572 4.1005 29.0161
REMARK 3 T TENSOR
REMARK 3 T11: 0.2966 T22: 0.5277
REMARK 3 T33: 0.2153 T12: -0.0573
REMARK 3 T13: 0.0308 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.1441 L22: 1.2306
REMARK 3 L33: 1.1598 L12: -0.0788
REMARK 3 L13: 0.2979 L23: -0.8364
REMARK 3 S TENSOR
REMARK 3 S11: -0.0571 S12: 0.2631 S13: 0.0949
REMARK 3 S21: -0.5351 S22: -0.0703 S23: -0.1929
REMARK 3 S31: 0.2656 S32: 0.5464 S33: 0.0553
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6FJ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1200008412.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93930
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 : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.19
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44257
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.659
REMARK 200 RESOLUTION RANGE LOW (A) : 43.811
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.02900
REMARK 200 R SYM (I) : 0.02900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.16200
REMARK 200 R SYM FOR SHELL (I) : 0.16200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3QYZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 2000, 0.1M MES PH 6.5, 0.1M
REMARK 280 AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, 0.002M MAGNESIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 34.89500
REMARK 290 SMTRY3 2 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 TOTAL BURIED SURFACE AREA: 1000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 GLY A 8
REMARK 465 ASP A 330
REMARK 465 MET A 331
REMARK 465 GLU A 332
REMARK 465 LEU A 333
REMARK 465 ASP A 334
REMARK 465 PRO A 354
REMARK 465 GLY A 355
REMARK 465 TYR A 356
REMARK 465 ARG A 357
REMARK 465 SER A 358
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 ARG A 13 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 470 PHE A 329 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 335 CB CG OD1 OD2
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 ARG A 13 44.69 18.99
REMARK 500 ASP A 147 42.37 -149.70
REMARK 500 ASP A 165 87.40 55.58
REMARK 500 ALA A 187 176.72 65.93
REMARK 500 ASN A 199 18.37 -161.94
REMARK 500 LEU A 292 48.20 -93.51
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 DMS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue A3N A 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QYZ RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FI3 RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FI6 RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
DBREF 6FJ0 A 1 358 UNP P63086 MK01_RAT 1 358
SEQADV 6FJ0 HIS A -5 UNP P63086 EXPRESSION TAG
SEQADV 6FJ0 HIS A -4 UNP P63086 EXPRESSION TAG
SEQADV 6FJ0 HIS A -3 UNP P63086 EXPRESSION TAG
SEQADV 6FJ0 HIS A -2 UNP P63086 EXPRESSION TAG
SEQADV 6FJ0 HIS A -1 UNP P63086 EXPRESSION TAG
SEQADV 6FJ0 HIS A 0 UNP P63086 EXPRESSION TAG
SEQRES 1 A 364 HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA ALA ALA
SEQRES 2 A 364 GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY
SEQRES 3 A 364 PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA
SEQRES 4 A 364 TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS
SEQRES 5 A 364 VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS
SEQRES 6 A 364 GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE
SEQRES 7 A 364 LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN
SEQRES 8 A 364 ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP
SEQRES 9 A 364 VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR
SEQRES 10 A 364 LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE
SEQRES 11 A 364 CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR
SEQRES 12 A 364 ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 13 A 364 SER ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE
SEQRES 14 A 364 CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS
SEQRES 15 A 364 ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG
SEQRES 16 A 364 TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY
SEQRES 17 A 364 TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE
SEQRES 18 A 364 LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY
SEQRES 19 A 364 LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE
SEQRES 20 A 364 LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE
SEQRES 21 A 364 ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS
SEQRES 22 A 364 LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA
SEQRES 23 A 364 ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR
SEQRES 24 A 364 PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU
SEQRES 25 A 364 ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP
SEQRES 26 A 364 GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU
SEQRES 27 A 364 LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE
SEQRES 28 A 364 PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER
MODRES 6FJ0 CME A 159 CYS MODIFIED RESIDUE
HET CME A 159 10
HET DMS A 401 4
HET DMS A 402 4
HET DMS A 403 4
HET DMS A 404 4
HET SO4 A 405 5
HET A3N A 406 22
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM SO4 SULFATE ION
HETNAM A3N 5'-DEOXY-5'-(PROP-2-YN-1-YLAMINO)ADENOSINE
FORMUL 1 CME C5 H11 N O3 S2
FORMUL 2 DMS 4(C2 H6 O S)
FORMUL 6 SO4 O4 S 2-
FORMUL 7 A3N C13 H16 N6 O3
FORMUL 8 HOH *330(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 ASP A 173 ASP A 177 5 5
HELIX 6 AA6 THR A 188 ARG A 192 5 5
HELIX 7 AA7 ALA A 193 ASN A 199 1 7
HELIX 8 AA8 LYS A 205 ASN A 222 1 18
HELIX 9 AA9 LEU A 232 GLY A 243 1 12
HELIX 10 AB1 SER A 246 CYS A 252 1 7
HELIX 11 AB2 ASN A 255 SER A 264 1 10
HELIX 12 AB3 PRO A 272 PHE A 277 1 6
HELIX 13 AB4 ASP A 281 LEU A 292 1 12
HELIX 14 AB5 GLU A 301 ALA A 307 1 7
HELIX 15 AB6 HIS A 308 GLU A 312 5 5
HELIX 16 AB7 ASP A 316 GLU A 320 5 5
HELIX 17 AB8 PRO A 337 THR A 349 1 13
HELIX 18 AB9 ALA A 350 GLN A 353 5 4
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 GLU A 31 0
SHEET 2 AA2 5 GLY A 35 ASP A 42 -1 O TYR A 41 N THR A 24
SHEET 3 AA2 5 VAL A 47 ILE A 54 -1 O VAL A 49 N ALA A 40
SHEET 4 AA2 5 VAL A 99 ASP A 104 -1 O VAL A 99 N ILE A 54
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 THR A 158 N CME A 159 1555 1555 1.33
LINK C CME A 159 N ASP A 160 1555 1555 1.33
SITE 1 AC1 2 LYS A 149 SER A 151
SITE 1 AC2 4 ASP A 122 HIS A 123 ARG A 259 TYR A 314
SITE 1 AC3 4 HIS A 297 LYS A 298 ARG A 299 GLN A 304
SITE 1 AC4 4 GLY A 32 ALA A 33 TYR A 34 GLY A 35
SITE 1 AC5 4 ARG A 189 ARG A 192 TYR A 231 HOH A 675
SITE 1 AC6 9 GLU A 31 VAL A 37 ALA A 50 GLN A 103
SITE 2 AC6 9 ASP A 104 MET A 106 ASP A 109 LYS A 112
SITE 3 AC6 9 HOH A 647
CRYST1 48.550 69.790 59.370 90.00 108.63 90.00 P 1 21 1 2
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 0.020597 0.000000 0.006944 0.00000
SCALE2 0.000000 0.014329 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017775 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
