HEADER TRANSFERASE/TRANSFERASE INHIBITOR 22-JUN-14 4QP1
TITLE CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH N-CYCLOHEXYL-9H-PURIN-6-
TITLE 2 AMINE
CAVEAT 4QP1 C-N BONDS BETWEEN RESIDUES ASP 124 AND NEP 125 ARE OUTSIDE
CAVEAT 2 4QP1 OF ACCEPTED RANGE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MAP KINASE 1, MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED
COMPND 5 KINASE 2, ERK-2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED
COMPND 6 PROTEIN KINASE 2, MAP KINASE 2, MAPK 2;
COMPND 7 EC: 2.7.11.24;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MAPK1, ERK2, PRKM1, PRKM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YIN,W.WANG
REVDAT 2 16-DEC-15 4QP1 1 JRNL
REVDAT 1 23-SEP-15 4QP1 0
JRNL AUTH D.J.BURDICK,S.WANG,C.HEISE,B.PAN,J.DRUMMOND,J.YIN,L.GOESER,
JRNL AUTH 2 S.MAGNUSON,J.BLANEY,J.MOFFAT,W.WANG,H.CHEN
JRNL TITL FRAGMENT-BASED DISCOVERY OF POTENT ERK2 PYRROLOPYRAZINE
JRNL TITL 2 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 25 4728 2015
JRNL REFN ISSN 0960-894X
JRNL PMID 26338362
JRNL DOI 10.1016/J.BMCL.2015.08.048
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 27243
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1250
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 49.3331 - 7.0697 1.00 2664 114 0.2080 0.2532
REMARK 3 2 7.0697 - 5.6140 1.00 2673 101 0.2163 0.2529
REMARK 3 3 5.6140 - 4.9051 1.00 2649 132 0.1903 0.1944
REMARK 3 4 4.9051 - 4.4569 1.00 2631 151 0.1651 0.2335
REMARK 3 5 4.4569 - 4.1376 1.00 2605 169 0.1614 0.2667
REMARK 3 6 4.1376 - 3.8938 1.00 2649 136 0.1734 0.2029
REMARK 3 7 3.8938 - 3.6989 1.00 2627 170 0.1784 0.2344
REMARK 3 8 3.6989 - 3.5379 1.00 2635 126 0.1913 0.2802
REMARK 3 9 3.5379 - 3.4017 1.00 2633 159 0.2063 0.2585
REMARK 3 10 3.4017 - 3.2844 1.00 2628 137 0.2241 0.2767
REMARK 3 11 3.2844 - 3.1817 1.00 2615 130 0.2200 0.3049
REMARK 3 12 3.1817 - 3.0908 0.99 2640 139 0.2253 0.2454
REMARK 3 13 3.0908 - 3.0094 0.99 2625 132 0.2362 0.3027
REMARK 3 14 3.0094 - 2.9360 0.99 2612 137 0.2434 0.2589
REMARK 3 15 2.9360 - 2.8693 0.98 2544 180 0.2629 0.3143
REMARK 3 16 2.8693 - 2.8082 0.98 2636 117 0.2774 0.3196
REMARK 3 17 2.8082 - 2.7520 0.97 2539 119 0.2755 0.2909
REMARK 3 18 2.7520 - 2.7001 0.96 2574 151 0.2848 0.3156
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.003 5800
REMARK 3 ANGLE : 0.656 7855
REMARK 3 CHIRALITY : 0.051 856
REMARK 3 PLANARITY : 0.003 1007
REMARK 3 DIHEDRAL : 13.085 2180
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 12:108 OR RESID 336:360 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5281 -28.6670 -17.9642
REMARK 3 T TENSOR
REMARK 3 T11: -0.1314 T22: 0.1747
REMARK 3 T33: 0.3873 T12: 0.7750
REMARK 3 T13: 0.1495 T23: 0.1973
REMARK 3 L TENSOR
REMARK 3 L11: 2.6784 L22: 2.6886
REMARK 3 L33: 1.9427 L12: -0.0907
REMARK 3 L13: 1.1289 L23: 1.2576
REMARK 3 S TENSOR
REMARK 3 S11: -1.2836 S12: -0.3113 S13: -0.3731
REMARK 3 S21: -0.3588 S22: 1.1561 S23: 0.5730
REMARK 3 S31: -0.5220 S32: 0.6124 S33: -0.2095
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 109:329 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0949 -32.2862 -27.7694
REMARK 3 T TENSOR
REMARK 3 T11: 0.1947 T22: 0.2290
REMARK 3 T33: 0.2631 T12: -0.0077
REMARK 3 T13: 0.0013 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 2.0888 L22: 1.8121
REMARK 3 L33: 2.2286 L12: -0.5387
REMARK 3 L13: 0.0712 L23: -0.3998
REMARK 3 S TENSOR
REMARK 3 S11: -0.1453 S12: -0.0587 S13: 0.0441
REMARK 3 S21: -0.0652 S22: 0.0396 S23: -0.1671
REMARK 3 S31: 0.0085 S32: 0.1946 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND (RESID 12:108 OR RESID 335:357 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2107 -62.0201 -52.5521
REMARK 3 T TENSOR
REMARK 3 T11: 0.6075 T22: 0.5408
REMARK 3 T33: 0.4388 T12: 0.1732
REMARK 3 T13: -0.1663 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 1.0043 L22: 0.6850
REMARK 3 L33: 0.9518 L12: -0.5513
REMARK 3 L13: 0.1784 L23: -0.0230
REMARK 3 S TENSOR
REMARK 3 S11: -0.1307 S12: -0.1281 S13: -0.2508
REMARK 3 S21: 0.3967 S22: 0.0117 S23: -0.1760
REMARK 3 S31: 0.6303 S32: 0.2852 S33: -0.1566
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 109:334 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8342 -41.7639 -62.6623
REMARK 3 T TENSOR
REMARK 3 T11: 0.3072 T22: 0.3465
REMARK 3 T33: 0.2863 T12: 0.0104
REMARK 3 T13: -0.0489 T23: -0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 0.7689 L22: 1.6500
REMARK 3 L33: 3.1874 L12: 0.0270
REMARK 3 L13: 0.5299 L23: 0.8564
REMARK 3 S TENSOR
REMARK 3 S11: -0.1020 S12: -0.1136 S13: -0.0181
REMARK 3 S21: -0.0222 S22: -0.0101 S23: 0.0540
REMARK 3 S31: -0.3595 S32: -0.3971 S33: -0.0053
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 4QP1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-14.
REMARK 100 THE RCSB ID CODE IS RCSB086332.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN COOLED DUAL
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27253
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 0.2 M PROLINE, AND 0.1 M
REMARK 280 HEPES PH7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 137.29750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.40400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.40400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 68.64875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.40400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.40400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 205.94625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.40400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.40400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 68.64875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.40400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.40400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 205.94625
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 137.29750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 MET A -8
REMARK 465 GLY A -7
REMARK 465 SER A -6
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 ALA A 9
REMARK 465 GLY A 10
REMARK 465 PRO A 11
REMARK 465 LYS A 330
REMARK 465 PHE A 331
REMARK 465 ASP A 332
REMARK 465 MET A 333
REMARK 465 GLU A 334
REMARK 465 LEU A 335
REMARK 465 MET B -8
REMARK 465 GLY B -7
REMARK 465 SER B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 ALA B 7
REMARK 465 GLY B 8
REMARK 465 ALA B 9
REMARK 465 GLY B 10
REMARK 465 PRO B 11
REMARK 465 ASN B 257
REMARK 465 ARG B 261
REMARK 465 TYR B 358
REMARK 465 ARG B 359
REMARK 465 SER B 360
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 O PHE B 329 O HOH B 519 2.17
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 GLN A 17 112.55 59.54
REMARK 500 ASP A 20 72.41 56.92
REMARK 500 ILE A 31 -60.72 -103.81
REMARK 500 ALA A 35 84.10 57.81
REMARK 500 TYR A 36 53.33 39.35
REMARK 500 THR A 110 -168.22 -163.76
REMARK 500 ARG A 148 -5.61 74.21
REMARK 500 ASP A 149 43.23 -142.95
REMARK 500 ASP A 167 79.32 65.18
REMARK 500 ASP A 175 79.54 -162.79
REMARK 500 HIS A 180 -15.09 -140.99
REMARK 500 THR A 181 14.70 59.54
REMARK 500 PHE A 183 -72.71 -59.22
REMARK 500 TYR A 187 87.78 -66.42
REMARK 500 SER A 202 78.46 49.09
REMARK 500 TYR A 205 23.91 -141.27
REMARK 500 ASN A 262 -45.48 -153.84
REMARK 500 LEU A 294 43.96 -103.64
REMARK 500 ASP A 318 86.89 -160.66
REMARK 500 ASP A 337 37.24 -96.77
REMARK 500 VAL B 14 -72.59 -144.97
REMARK 500 ARG B 15 -75.70 -132.90
REMARK 500 GLN B 17 -131.99 -153.61
REMARK 500 ALA B 35 71.99 -61.63
REMARK 500 ASP B 149 42.43 -153.50
REMARK 500 ASP B 167 85.87 57.57
REMARK 500 ASP B 175 82.40 -152.58
REMARK 500 HIS B 178 47.23 -84.74
REMARK 500 HIS B 180 -92.77 -126.54
REMARK 500 PHE B 183 -92.27 -70.18
REMARK 500 ALA B 189 148.06 68.05
REMARK 500 LEU B 200 -62.98 -95.34
REMARK 500 ASN B 201 -111.06 -122.74
REMARK 500 LYS B 203 -173.85 -68.04
REMARK 500 SER B 223 -4.13 -145.03
REMARK 500 SER B 248 -159.07 -81.16
REMARK 500 CYS B 254 57.82 -111.72
REMARK 500 ASP B 318 91.78 -161.94
REMARK 500 LYS B 330 -4.41 -140.06
REMARK 500 PHE B 331 100.38 47.43
REMARK 500 GLU B 334 98.21 -62.39
REMARK 500 PRO B 356 3.23 -67.56
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 EMU A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMU B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QP2 RELATED DB: PDB
REMARK 900 RELATED ID: 4QP3 RELATED DB: PDB
REMARK 900 RELATED ID: 4QP4 RELATED DB: PDB
REMARK 900 RELATED ID: 4QP6 RELATED DB: PDB
REMARK 900 RELATED ID: 4QP7 RELATED DB: PDB
REMARK 900 RELATED ID: 4QP8 RELATED DB: PDB
REMARK 900 RELATED ID: 4QP9 RELATED DB: PDB
REMARK 900 RELATED ID: 4QPA RELATED DB: PDB
DBREF 4QP1 A 1 360 UNP P28482 MK01_HUMAN 1 360
DBREF 4QP1 B 1 360 UNP P28482 MK01_HUMAN 1 360
SEQADV 4QP1 MET A -8 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 GLY A -7 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 SER A -6 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS A -5 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS A -4 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS A -3 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS A -2 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS A -1 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS A 0 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 MET B -8 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 GLY B -7 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 SER B -6 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS B -5 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS B -4 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS B -3 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS B -2 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS B -1 UNP P28482 EXPRESSION TAG
SEQADV 4QP1 HIS B 0 UNP P28482 EXPRESSION TAG
SEQRES 1 A 369 MET GLY SER HIS HIS HIS HIS HIS HIS MET ALA ALA ALA
SEQRES 2 A 369 ALA ALA ALA GLY ALA GLY PRO GLU MET VAL ARG GLY GLN
SEQRES 3 A 369 VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR
SEQRES 4 A 369 ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR
SEQRES 5 A 369 ASP ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE
SEQRES 6 A 369 SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU
SEQRES 7 A 369 ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN
SEQRES 8 A 369 ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE
SEQRES 9 A 369 GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET
SEQRES 10 A 369 GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU
SEQRES 11 A 369 SER ASN ASP NEP ILE CYS TYR PHE LEU TYR GLN ILE LEU
SEQRES 12 A 369 ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS
SEQRES 13 A 369 ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR
SEQRES 14 A 369 CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL
SEQRES 15 A 369 ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU THR GLU
SEQRES 16 A 369 TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET
SEQRES 17 A 369 LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP
SEQRES 18 A 369 SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG
SEQRES 19 A 369 PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN
SEQRES 20 A 369 HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP
SEQRES 21 A 369 LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU
SEQRES 22 A 369 LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG
SEQRES 23 A 369 LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU
SEQRES 24 A 369 ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU
SEQRES 25 A 369 VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR
SEQRES 26 A 369 TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE
SEQRES 27 A 369 LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS
SEQRES 28 A 369 LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN
SEQRES 29 A 369 PRO GLY TYR ARG SER
SEQRES 1 B 369 MET GLY SER HIS HIS HIS HIS HIS HIS MET ALA ALA ALA
SEQRES 2 B 369 ALA ALA ALA GLY ALA GLY PRO GLU MET VAL ARG GLY GLN
SEQRES 3 B 369 VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR
SEQRES 4 B 369 ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR
SEQRES 5 B 369 ASP ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE
SEQRES 6 B 369 SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU
SEQRES 7 B 369 ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN
SEQRES 8 B 369 ILE ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE
SEQRES 9 B 369 GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET
SEQRES 10 B 369 GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU
SEQRES 11 B 369 SER ASN ASP NEP ILE CYS TYR PHE LEU TYR GLN ILE LEU
SEQRES 12 B 369 ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS
SEQRES 13 B 369 ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR
SEQRES 14 B 369 CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL
SEQRES 15 B 369 ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU THR GLU
SEQRES 16 B 369 TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET
SEQRES 17 B 369 LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP
SEQRES 18 B 369 SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG
SEQRES 19 B 369 PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN
SEQRES 20 B 369 HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP
SEQRES 21 B 369 LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU
SEQRES 22 B 369 LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG
SEQRES 23 B 369 LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU
SEQRES 24 B 369 ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU
SEQRES 25 B 369 VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR
SEQRES 26 B 369 TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE
SEQRES 27 B 369 LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS
SEQRES 28 B 369 LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN
SEQRES 29 B 369 PRO GLY TYR ARG SER
MODRES 4QP1 NEP A 125 HIS N1-PHOSPHONOHISTIDINE
MODRES 4QP1 NEP B 125 HIS N1-PHOSPHONOHISTIDINE
HET NEP A 125 14
HET NEP B 125 14
HET EMU A 401 17
HET IMD A 402 5
HET EMU B 401 17
HET IMD B 402 5
HETNAM NEP N1-PHOSPHONOHISTIDINE
HETNAM EMU N-BENZYL-9H-PURIN-6-AMINE
HETNAM IMD IMIDAZOLE
HETSYN EMU BENZYLAMINOPURINE
FORMUL 1 NEP 2(C6 H10 N3 O5 P)
FORMUL 3 EMU 2(C12 H11 N5)
FORMUL 4 IMD 2(C3 H5 N2 1+)
FORMUL 7 HOH *186(H2 O)
HELIX 1 1 HIS A 61 PHE A 78 1 18
HELIX 2 2 LEU A 112 GLN A 119 1 8
HELIX 3 3 SER A 122 ASP A 124 1 3
HELIX 4 4 ILE A 126 ALA A 143 1 18
HELIX 5 5 LYS A 151 SER A 153 5 3
HELIX 6 6 THR A 190 ARG A 194 5 5
HELIX 7 7 ALA A 195 SER A 202 1 8
HELIX 8 8 LYS A 207 ASN A 224 1 18
HELIX 9 9 HIS A 232 GLY A 245 1 14
HELIX 10 10 SER A 248 CYS A 254 1 7
HELIX 11 11 LYS A 259 LEU A 267 1 9
HELIX 12 12 PRO A 274 PHE A 279 1 6
HELIX 13 13 ASP A 283 LEU A 294 1 12
HELIX 14 14 GLU A 303 ALA A 309 1 7
HELIX 15 15 HIS A 310 GLU A 314 5 5
HELIX 16 16 ASP A 318 GLU A 322 5 5
HELIX 17 17 PRO A 339 THR A 351 1 13
HELIX 18 18 ALA A 352 GLN A 355 5 4
HELIX 19 19 HIS B 61 PHE B 78 1 18
HELIX 20 20 LEU B 112 GLN B 119 1 8
HELIX 21 21 SER B 122 ASP B 124 1 3
HELIX 22 22 ILE B 126 ALA B 143 1 18
HELIX 23 23 LYS B 151 SER B 153 5 3
HELIX 24 24 THR B 190 ARG B 194 5 5
HELIX 25 25 ALA B 195 ASN B 201 1 7
HELIX 26 26 LYS B 207 LEU B 222 1 16
HELIX 27 27 HIS B 232 GLY B 245 1 14
HELIX 28 28 PRO B 274 PHE B 279 1 6
HELIX 29 29 ASP B 283 LEU B 294 1 12
HELIX 30 30 GLU B 303 ALA B 309 1 7
HELIX 31 31 HIS B 310 GLU B 314 5 5
HELIX 32 32 ASP B 318 GLU B 322 5 5
HELIX 33 33 PRO B 339 THR B 351 1 13
HELIX 34 34 ALA B 352 GLN B 355 5 4
SHEET 1 A 5 TYR A 25 GLY A 32 0
SHEET 2 A 5 GLY A 37 ASP A 44 -1 O TYR A 43 N THR A 26
SHEET 3 A 5 VAL A 49 ILE A 56 -1 O LYS A 55 N MET A 38
SHEET 4 A 5 VAL A 101 ASP A 106 -1 O VAL A 101 N ILE A 56
SHEET 5 A 5 ASP A 88 ILE A 90 -1 N ASP A 88 O VAL A 104
SHEET 1 B 3 THR A 110 ASP A 111 0
SHEET 2 B 3 LEU A 155 LEU A 157 -1 O LEU A 157 N THR A 110
SHEET 3 B 3 LEU A 163 ILE A 165 -1 O LYS A 164 N LEU A 156
SHEET 1 C 2 VAL A 145 LEU A 146 0
SHEET 2 C 2 ARG A 172 VAL A 173 -1 O ARG A 172 N LEU A 146
SHEET 1 D 2 TYR B 25 THR B 26 0
SHEET 2 D 2 TYR B 43 ASP B 44 -1 O TYR B 43 N THR B 26
SHEET 1 E 5 TYR B 30 GLU B 33 0
SHEET 2 E 5 MET B 38 CYS B 40 -1 O VAL B 39 N ILE B 31
SHEET 3 E 5 VAL B 51 ILE B 56 -1 O LYS B 55 N MET B 38
SHEET 4 E 5 VAL B 101 ASP B 106 -1 O GLN B 105 N ALA B 52
SHEET 5 E 5 ASP B 88 ILE B 90 -1 N ASP B 88 O VAL B 104
SHEET 1 F 3 THR B 110 ASP B 111 0
SHEET 2 F 3 LEU B 155 LEU B 157 -1 O LEU B 157 N THR B 110
SHEET 3 F 3 LEU B 163 ILE B 165 -1 O LYS B 164 N LEU B 156
SHEET 1 G 2 VAL B 145 LEU B 146 0
SHEET 2 G 2 ARG B 172 VAL B 173 -1 O ARG B 172 N LEU B 146
LINK C NEP A 125 N ILE A 126 1555 1555 1.33
LINK C NEP B 125 N ILE B 126 1555 1555 1.33
CISPEP 1 GLY A 22 PRO A 23 0 -0.01
SITE 1 AC1 7 GLU A 33 ALA A 52 GLN A 105 ASP A 106
SITE 2 AC1 7 MET A 108 LEU A 156 IMD A 402
SITE 1 AC2 6 MET A 108 GLU A 109 THR A 110 ASP A 111
SITE 2 AC2 6 LYS A 114 EMU A 401
SITE 1 AC3 5 ALA B 52 GLN B 105 ASP B 106 MET B 108
SITE 2 AC3 5 IMD B 402
SITE 1 AC4 5 MET B 108 THR B 110 ASP B 111 LYS B 114
SITE 2 AC4 5 EMU B 401
CRYST1 82.808 82.808 274.595 90.00 90.00 90.00 P 41 21 2 16
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 0.012076 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012076 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003642 0.00000
(ATOM LINES ARE NOT SHOWN.)
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