HEADER TRANSFERASE 28-AUG-19 6SO1
TITLE FRAGMENT N13569A IN COMPLEX WITH MAP KINASE P38-ALPHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAPK 14,CRK1,MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA,MAP
COMPND 5 KINASE P38 ALPHA;
COMPND 6 EC: 2.7.11.24;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: MAPK14, CRK1, CSBP1, CSBP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FBDD, FRAGMENT BASED DRUG DESIGN, P38, MAPK14, KINASE, TRANSFERASE.,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.E.NICHOLS,G.F.DE NICOLA
REVDAT 3 24-JAN-24 6SO1 1 REMARK
REVDAT 2 14-OCT-20 6SO1 1 JRNL LINK
REVDAT 1 02-OCT-19 6SO1 0
JRNL AUTH C.NICHOLS,J.NG,A.KESHU,G.KELLY,M.R.CONTE,M.S.MARBER,
JRNL AUTH 2 F.FRATERNALI,G.F.DE NICOLA
JRNL TITL MINING THE PDB FOR TRACTABLE CASES WHERE X-RAY
JRNL TITL 2 CRYSTALLOGRAPHY COMBINED WITH FRAGMENT SCREENS CAN BE USED
JRNL TITL 3 TO SYSTEMATICALLY DESIGN PROTEIN-PROTEIN INHIBITORS: TWO
JRNL TITL 4 TEST CASES ILLUSTRATED BY IL1 BETA-IL1R AND P38 ALPHA-TAB1
JRNL TITL 5 COMPLEXES.
JRNL REF J.MED.CHEM. V. 63 7559 2020
JRNL REFN ISSN 0022-2623
JRNL PMID 32543856
JRNL DOI 10.1021/ACS.JMEDCHEM.0C00403
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 58976
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2943
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 29.1800 - 4.5800 0.98 2870 137 0.1735 0.1639
REMARK 3 2 4.5800 - 3.6300 1.00 2783 146 0.1560 0.1790
REMARK 3 3 3.6300 - 3.1800 0.97 2705 119 0.1746 0.1855
REMARK 3 4 3.1800 - 2.8900 0.99 2698 141 0.1944 0.2105
REMARK 3 5 2.8900 - 2.6800 1.00 2676 172 0.1950 0.2358
REMARK 3 6 2.6800 - 2.5200 0.99 2713 131 0.1953 0.2241
REMARK 3 7 2.5200 - 2.4000 0.98 2635 136 0.1968 0.2050
REMARK 3 8 2.4000 - 2.2900 0.98 2660 135 0.1895 0.2133
REMARK 3 9 2.2900 - 2.2000 0.99 2658 158 0.1904 0.2059
REMARK 3 10 2.2000 - 2.1300 1.00 2685 143 0.1857 0.1972
REMARK 3 11 2.1300 - 2.0600 1.00 2679 135 0.1951 0.2301
REMARK 3 12 2.0600 - 2.0000 1.00 2649 148 0.1997 0.2095
REMARK 3 13 2.0000 - 1.9500 1.00 2677 138 0.1933 0.2057
REMARK 3 14 1.9500 - 1.9000 1.00 2648 143 0.1926 0.2386
REMARK 3 15 1.9000 - 1.8600 0.96 2563 149 0.1906 0.2140
REMARK 3 16 1.8600 - 1.8200 0.98 2604 129 0.2056 0.2307
REMARK 3 17 1.8200 - 1.7800 0.99 2681 138 0.2208 0.2852
REMARK 3 18 1.7800 - 1.7500 1.00 2663 120 0.2366 0.2368
REMARK 3 19 1.7500 - 1.7200 1.00 2635 140 0.2602 0.3134
REMARK 3 20 1.7200 - 1.6900 1.00 2644 157 0.2629 0.2775
REMARK 3 21 1.6900 - 1.6600 0.93 2507 128 0.3075 0.3653
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) : 0.213
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.507
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.77
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 : 0.007 2815
REMARK 3 ANGLE : 0.818 3832
REMARK 3 CHIRALITY : 0.052 432
REMARK 3 PLANARITY : 0.005 497
REMARK 3 DIHEDRAL : 2.363 2318
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6SO1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1292104026.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59026
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 29.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8500
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) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.960
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: 4LOO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27.5% PEG3350, 0.1M MAGNESIUM
REMARK 280 CHLORIDE, 0.1M MAGNESIUM ACETATE, 0.1M BIS-TRIS PROPANE PH6.9,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 22.84150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.40350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.94150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.40350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.84150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.94150
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 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 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 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 GLN A -9
REMARK 465 ASP A -8
REMARK 465 PRO A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 GLU A 4
REMARK 465 SER A 32
REMARK 465 GLY A 33
REMARK 465 ALA A 34
REMARK 465 ALA A 172
REMARK 465 ARG A 173
REMARK 465 LEU A 353
REMARK 465 ASP A 354
REMARK 465 GLN A 355
REMARK 465 GLU A 356
REMARK 465 GLU A 357
REMARK 465 MET A 358
REMARK 465 GLU A 359
REMARK 465 SER A 360
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 10 CZ NH1 NH2
REMARK 470 LEU A 13 CD1 CD2
REMARK 470 ASN A 14 CG OD1 ND2
REMARK 470 LYS A 15 CG CD CE NZ
REMARK 470 TYR A 35 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 45 CE NZ
REMARK 470 ARG A 49 CD NE CZ NH1 NH2
REMARK 470 ARG A 57 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 67 NE CZ NH1 NH2
REMARK 470 GLU A 97 CG CD OE1 OE2
REMARK 470 ILE A 116 CG1 CG2 CD1
REMARK 470 VAL A 117 CG1 CG2
REMARK 470 LYS A 118 CG CD CE NZ
REMARK 470 GLN A 120 OE1 NE2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 ARG A 149 NE CZ NH1 NH2
REMARK 470 GLU A 160 CG CD OE1 OE2
REMARK 470 GLU A 178 CG CD OE1 OE2
REMARK 470 ILE A 193 CD1
REMARK 470 LYS A 248 CD CE NZ
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 30 -40.06 -136.46
REMARK 500 ASN A 100 -30.07 -137.26
REMARK 500 ASN A 115 11.40 -69.28
REMARK 500 ILE A 116 -45.32 -131.84
REMARK 500 ARG A 149 -11.61 79.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 409 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 155 OD1
REMARK 620 2 ASP A 168 OD2 96.2
REMARK 620 3 HOH A 503 O 91.1 98.6
REMARK 620 4 HOH A 614 O 89.3 86.5 174.8
REMARK 620 5 HOH A 631 O 89.6 174.0 79.8 95.0
REMARK 620 6 HOH A 666 O 176.3 87.5 88.6 90.7 86.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LO5 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 411
DBREF 6SO1 A 1 360 UNP P47811 MK14_MOUSE 1 360
SEQADV 6SO1 MET A -20 UNP P47811 INITIATING METHIONINE
SEQADV 6SO1 GLY A -19 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 SER A -18 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 SER A -17 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 HIS A -16 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 HIS A -15 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 HIS A -14 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 HIS A -13 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 HIS A -12 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 HIS A -11 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 SER A -10 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 GLN A -9 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 ASP A -8 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 PRO A -7 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 GLU A -6 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 ASN A -5 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 LEU A -4 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 TYR A -3 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 PHE A -2 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 GLN A -1 UNP P47811 EXPRESSION TAG
SEQADV 6SO1 GLY A 0 UNP P47811 EXPRESSION TAG
SEQRES 1 A 381 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 381 PRO GLU ASN LEU TYR PHE GLN GLY MET SER GLN GLU ARG
SEQRES 3 A 381 PRO THR PHE TYR ARG GLN GLU LEU ASN LYS THR ILE TRP
SEQRES 4 A 381 GLU VAL PRO GLU ARG TYR GLN ASN LEU SER PRO VAL GLY
SEQRES 5 A 381 SER GLY ALA TYR GLY SER VAL CYS ALA ALA PHE ASP THR
SEQRES 6 A 381 LYS THR GLY HIS ARG VAL ALA VAL LYS LYS LEU SER ARG
SEQRES 7 A 381 PRO PHE GLN SER ILE ILE HIS ALA LYS ARG THR TYR ARG
SEQRES 8 A 381 GLU LEU ARG LEU LEU LYS HIS MET LYS HIS GLU ASN VAL
SEQRES 9 A 381 ILE GLY LEU LEU ASP VAL PHE THR PRO ALA ARG SER LEU
SEQRES 10 A 381 GLU GLU PHE ASN ASP VAL TYR LEU VAL THR HIS LEU MET
SEQRES 11 A 381 GLY ALA ASP LEU ASN ASN ILE VAL LYS CYS GLN LYS LEU
SEQRES 12 A 381 THR ASP ASP HIS VAL GLN PHE LEU ILE TYR GLN ILE LEU
SEQRES 13 A 381 ARG GLY LEU LYS TYR ILE HIS SER ALA ASP ILE ILE HIS
SEQRES 14 A 381 ARG ASP LEU LYS PRO SER ASN LEU ALA VAL ASN GLU ASP
SEQRES 15 A 381 CYS GLU LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG HIS
SEQRES 16 A 381 THR ASP ASP GLU MET THR GLY TYR VAL ALA THR ARG TRP
SEQRES 17 A 381 TYR ARG ALA PRO GLU ILE MET LEU ASN TRP MET HIS TYR
SEQRES 18 A 381 ASN GLN THR VAL ASP ILE TRP SER VAL GLY CYS ILE MET
SEQRES 19 A 381 ALA GLU LEU LEU THR GLY ARG THR LEU PHE PRO GLY THR
SEQRES 20 A 381 ASP HIS ILE ASP GLN LEU LYS LEU ILE LEU ARG LEU VAL
SEQRES 21 A 381 GLY THR PRO GLY ALA GLU LEU LEU LYS LYS ILE SER SER
SEQRES 22 A 381 GLU SER ALA ARG ASN TYR ILE GLN SER LEU ALA GLN MET
SEQRES 23 A 381 PRO LYS MET ASN PHE ALA ASN VAL PHE ILE GLY ALA ASN
SEQRES 24 A 381 PRO LEU ALA VAL ASP LEU LEU GLU LYS MET LEU VAL LEU
SEQRES 25 A 381 ASP SER ASP LYS ARG ILE THR ALA ALA GLN ALA LEU ALA
SEQRES 26 A 381 HIS ALA TYR PHE ALA GLN TYR HIS ASP PRO ASP ASP GLU
SEQRES 27 A 381 PRO VAL ALA ASP PRO TYR ASP GLN SER PHE GLU SER ARG
SEQRES 28 A 381 ASP LEU LEU ILE ASP GLU TRP LYS SER LEU THR TYR ASP
SEQRES 29 A 381 GLU VAL ILE SER PHE VAL PRO PRO PRO LEU ASP GLN GLU
SEQRES 30 A 381 GLU MET GLU SER
HET LO5 A 401 17
HET CL A 402 1
HET CL A 403 1
HET CL A 404 1
HET CL A 405 1
HET CL A 406 1
HET CL A 407 1
HET CL A 408 1
HET MG A 409 1
HET SO4 A 410 5
HET SO4 A 411 5
HETNAM LO5 1-(1,3-BENZODIOXOL-5-YL)-~{N}-[[(2~{R})-OXOLAN-2-
HETNAM 2 LO5 YL]METHYL]METHANAMINE
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
FORMUL 2 LO5 C13 H17 N O3
FORMUL 3 CL 7(CL 1-)
FORMUL 10 MG MG 2+
FORMUL 11 SO4 2(O4 S 2-)
FORMUL 13 HOH *270(H2 O)
HELIX 1 AA1 SER A 61 MET A 78 1 18
HELIX 2 AA2 SER A 95 PHE A 99 5 5
HELIX 3 AA3 LEU A 113 LYS A 118 1 6
HELIX 4 AA4 THR A 123 ALA A 144 1 22
HELIX 5 AA5 LYS A 152 SER A 154 5 3
HELIX 6 AA6 ASP A 176 THR A 180 5 5
HELIX 7 AA7 VAL A 183 TYR A 188 1 6
HELIX 8 AA8 ALA A 190 LEU A 195 1 6
HELIX 9 AA9 GLN A 202 GLY A 219 1 18
HELIX 10 AB1 ASP A 227 GLY A 240 1 14
HELIX 11 AB2 GLY A 243 LYS A 248 1 6
HELIX 12 AB3 SER A 252 SER A 261 1 10
HELIX 13 AB4 ASN A 269 VAL A 273 5 5
HELIX 14 AB5 ASN A 278 LEU A 289 1 12
HELIX 15 AB6 ASP A 292 ARG A 296 5 5
HELIX 16 AB7 THR A 298 ALA A 304 1 7
HELIX 17 AB8 HIS A 305 ALA A 309 5 5
HELIX 18 AB9 GLN A 325 ARG A 330 5 6
HELIX 19 AC1 LEU A 333 SER A 347 1 15
SHEET 1 AA1 2 PHE A 8 LEU A 13 0
SHEET 2 AA1 2 THR A 16 PRO A 21 -1 O TRP A 18 N GLN A 11
SHEET 1 AA2 5 TYR A 24 GLY A 31 0
SHEET 2 AA2 5 GLY A 36 ASP A 43 -1 O ALA A 40 N SER A 28
SHEET 3 AA2 5 ARG A 49 LEU A 55 -1 O VAL A 52 N CYS A 39
SHEET 4 AA2 5 TYR A 103 HIS A 107 -1 O LEU A 104 N LYS A 53
SHEET 5 AA2 5 ASP A 88 PHE A 90 -1 N ASP A 88 O VAL A 105
SHEET 1 AA3 3 ALA A 111 ASP A 112 0
SHEET 2 AA3 3 LEU A 156 VAL A 158 -1 O VAL A 158 N ALA A 111
SHEET 3 AA3 3 LEU A 164 ILE A 166 -1 O LYS A 165 N ALA A 157
LINK OD1 ASN A 155 MG MG A 409 1555 1555 2.10
LINK OD2 ASP A 168 MG MG A 409 1555 1555 2.16
LINK MG MG A 409 O HOH A 503 1555 1555 2.26
LINK MG MG A 409 O HOH A 614 1555 1555 2.03
LINK MG MG A 409 O HOH A 631 1555 1555 2.07
LINK MG MG A 409 O HOH A 666 1555 1555 2.16
SITE 1 AC1 8 THR A 221 LEU A 222 LEU A 234 ARG A 237
SITE 2 AC1 8 LEU A 238 ASP A 324 SER A 326 HOH A 534
SITE 1 AC2 5 GLU A 22 ARG A 23 HOH A 640 HOH A 722
SITE 2 AC2 5 HOH A 766
SITE 1 AC3 5 THR A 91 ALA A 93 GLU A 98 ASN A 100
SITE 2 AC3 5 ASP A 101
SITE 1 AC4 5 GLY A 85 HIS A 107 LYS A 165 HOH A 510
SITE 2 AC4 5 HOH A 541
SITE 1 AC5 6 ARG A 73 ARG A 220 PRO A 322 ASP A 324
SITE 2 AC5 6 HOH A 621 HOH A 648
SITE 1 AC6 5 ASN A 114 PRO A 153 SER A 154 HOH A 627
SITE 2 AC6 5 HOH A 656
SITE 1 AC7 2 ALA A 144 TYR A 323
SITE 1 AC8 3 MET A 268 ASN A 269 HOH A 639
SITE 1 AC9 6 ASN A 155 ASP A 168 HOH A 503 HOH A 614
SITE 2 AC9 6 HOH A 631 HOH A 666
SITE 1 AD1 5 ARG A 220 THR A 221 ARG A 330 HOH A 501
SITE 2 AD1 5 HOH A 529
SITE 1 AD2 5 LYS A 152 HIS A 174 HOH A 503 HOH A 631
SITE 2 AD2 5 HOH A 666
CRYST1 45.683 85.883 126.807 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 0.021890 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011644 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007886 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
