HEADER TRANSFERASE 02-FEB-18 6FN5
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 13-MAR-19 6FN5 0
JRNL AUTH M.GELIN,S.POCHET,G.LABESSE
JRNL TITL NONE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.93 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.180
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.8
REMARK 3 NUMBER OF REFLECTIONS : 27183
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 2531
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 23.2937 - 5.0476 0.90 2663 135 0.1873 0.2096
REMARK 3 2 5.0476 - 4.0131 0.92 2716 162 0.1491 0.1824
REMARK 3 3 4.0131 - 3.5078 0.92 2726 132 0.1630 0.1856
REMARK 3 4 3.5078 - 3.1879 0.91 2695 142 0.1796 0.2318
REMARK 3 5 3.1879 - 2.9599 0.91 2682 132 0.1977 0.2251
REMARK 3 6 2.9599 - 2.7857 0.91 2727 143 0.2063 0.2939
REMARK 3 7 2.7857 - 2.6464 0.91 2681 145 0.2245 0.2813
REMARK 3 8 2.6464 - 2.5313 0.90 2651 189 0.2300 0.2724
REMARK 3 9 2.5313 - 2.4340 0.91 2669 143 0.2386 0.2614
REMARK 3 10 2.4340 - 2.3501 0.90 2657 149 0.2355 0.2762
REMARK 3 11 2.3501 - 2.2767 0.91 2701 160 0.2472 0.2500
REMARK 3 12 2.2767 - 2.2116 0.90 2666 135 0.2774 0.2742
REMARK 3 13 2.2116 - 2.1535 0.90 2627 172 0.2868 0.3043
REMARK 3 14 2.1535 - 2.1010 0.90 2630 165 0.2983 0.3416
REMARK 3 15 2.1010 - 2.0532 0.90 2621 150 0.3131 0.3368
REMARK 3 16 2.0532 - 2.0096 0.89 2751 94 0.3322 0.3492
REMARK 3 17 2.0096 - 1.9694 0.88 2605 113 0.3501 0.3620
REMARK 3 18 1.9694 - 1.9322 0.44 1323 70 0.3314 0.3455
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.800
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.84
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 : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 9:118)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2330 12.1579 33.5886
REMARK 3 T TENSOR
REMARK 3 T11: 0.4497 T22: 0.3450
REMARK 3 T33: 0.3601 T12: -0.0176
REMARK 3 T13: -0.0819 T23: 0.0720
REMARK 3 L TENSOR
REMARK 3 L11: 1.3703 L22: 0.6874
REMARK 3 L33: 4.3049 L12: 0.0557
REMARK 3 L13: -0.5580 L23: 0.0488
REMARK 3 S TENSOR
REMARK 3 S11: -0.1048 S12: 0.3384 S13: 0.3803
REMARK 3 S21: -0.3841 S22: 0.2124 S23: 0.2617
REMARK 3 S31: -0.7067 S32: -0.3154 S33: -0.0870
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 119:312)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1550 7.9758 56.4296
REMARK 3 T TENSOR
REMARK 3 T11: 0.2169 T22: 0.1739
REMARK 3 T33: 0.2466 T12: 0.0237
REMARK 3 T13: 0.0230 T23: 0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 2.4923 L22: 1.4415
REMARK 3 L33: 2.3134 L12: 1.2795
REMARK 3 L13: 1.4850 L23: 0.6198
REMARK 3 S TENSOR
REMARK 3 S11: 0.0278 S12: 0.0100 S13: 0.1341
REMARK 3 S21: 0.1223 S22: 0.0170 S23: -0.0436
REMARK 3 S31: -0.0918 S32: 0.1098 S33: -0.0442
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 313:354)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7778 -0.0040 34.6086
REMARK 3 T TENSOR
REMARK 3 T11: 0.3696 T22: 0.3829
REMARK 3 T33: 0.2667 T12: -0.1342
REMARK 3 T13: -0.0238 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.9474 L22: 2.8543
REMARK 3 L33: 4.0883 L12: 0.0395
REMARK 3 L13: -0.1351 L23: -2.0549
REMARK 3 S TENSOR
REMARK 3 S11: 0.0119 S12: 0.3030 S13: 0.1026
REMARK 3 S21: -0.6436 S22: -0.0116 S23: -0.0057
REMARK 3 S31: 0.3292 S32: 0.7866 S33: 0.0217
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN S
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6749 21.4627 48.2282
REMARK 3 T TENSOR
REMARK 3 T11: 0.6540 T22: 0.3867
REMARK 3 T33: 0.5344 T12: -0.1875
REMARK 3 T13: -0.0363 T23: 0.2149
REMARK 3 L TENSOR
REMARK 3 L11: 2.0000 L22: 2.0000
REMARK 3 L33: 2.0000 L12: 2.0000
REMARK 3 L13: 2.0000 L23: 2.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.4207 S12: 0.2270 S13: -1.1115
REMARK 3 S21: 0.8427 S22: 0.2103 S23: -1.5766
REMARK 3 S31: -1.2147 S32: 0.2796 S33: 0.2134
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 6FN5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008619.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.19
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27188
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.932
REMARK 200 RESOLUTION RANGE LOW (A) : 27.298
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.52500
REMARK 200 R SYM FOR SHELL (I) : 0.52500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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 (%): 46.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
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 34.94400
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: 580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 GLY A 32
REMARK 465 ALA A 33
REMARK 465 LYS A 328
REMARK 465 PHE A 329
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 ASP A 335
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 MET A 11 CG SD CE
REMARK 470 PRO A 354 C O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU A 312 O HOH A 501 2.19
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 29 -58.78 -124.97
REMARK 500 MET A 36 140.40 -177.07
REMARK 500 ASP A 147 39.82 -145.35
REMARK 500 ASP A 165 90.82 58.41
REMARK 500 ASN A 199 13.85 -160.49
REMARK 500 LEU A 292 46.40 -91.18
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 DVZ 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 SO4 A 404
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
REMARK 900 RELATED ID: 6FJ0 RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FJB RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FJZ RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FLE RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FLV RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FMA RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
DBREF 6FN5 A 1 358 UNP P63086 MK01_RAT 1 358
SEQADV 6FN5 HIS A -5 UNP P63086 EXPRESSION TAG
SEQADV 6FN5 HIS A -4 UNP P63086 EXPRESSION TAG
SEQADV 6FN5 HIS A -3 UNP P63086 EXPRESSION TAG
SEQADV 6FN5 HIS A -2 UNP P63086 EXPRESSION TAG
SEQADV 6FN5 HIS A -1 UNP P63086 EXPRESSION TAG
SEQADV 6FN5 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 6FN5 CME A 159 CYS MODIFIED RESIDUE
HET CME A 159 10
HET DVZ A 401 26
HET DMS A 402 4
HET DMS A 403 4
HET SO4 A 404 10
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM DVZ [(2~{R},3~{S},4~{R},5~{R})-5-[6-AZANYL-8-(2-HYDROXY-2-
HETNAM 2 DVZ OXOETHYLSULFANYL)PURIN-9-YL]-3,4-BIS(OXIDANYL)OXOLAN-
HETNAM 3 DVZ 2-YL]METHYLIMINO-AZANYLIDENE-AZANIUM
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM SO4 SULFATE ION
FORMUL 1 CME C5 H11 N O3 S2
FORMUL 2 DVZ C12 H15 N8 O5 S 1+
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *186(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 MET A 197 5 5
HELIX 8 AA8 LYS A 205 ASN A 222 1 18
HELIX 9 AA9 HIS A 230 GLY A 243 1 14
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 GLU A 10 MET A 11 0
SHEET 2 AA1 2 VAL A 16 PHE A 17 -1 O PHE A 17 N GLU A 10
SHEET 1 AA2 5 TYR A 23 GLY A 30 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 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 ARG A 89 -1 N ILE A 88 O TYR A 100
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
CISPEP 1 GLY A 20 PRO A 21 0 0.36
CISPEP 2 GLN A 353 PRO A 354 0 -3.98
SITE 1 AC1 9 GLY A 30 GLU A 31 VAL A 37 ALA A 50
SITE 2 AC1 9 LYS A 52 ASP A 104 MET A 106 ASP A 109
SITE 3 AC1 9 LYS A 112
SITE 1 AC2 1 THR A 116
SITE 1 AC3 4 LYS A 298 ARG A 299 GLN A 304 HOH A 572
SITE 1 AC4 4 ARG A 189 ARG A 192 TYR A 231 HOH A 527
CRYST1 49.425 69.888 59.452 90.00 109.52 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 0.020233 0.000000 0.007173 0.00000
SCALE2 0.000000 0.014309 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017846 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
