HEADER TRANSFERASE 16-JAN-15 4XP2
TITLE CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN INHIBITOR
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,F.ALLEMAND,G.LABESSE,J.F.GUICHOU
REVDAT 3 06-SEP-17 4XP2 1 REMARK
REVDAT 2 19-AUG-15 4XP2 1 JRNL
REVDAT 1 12-AUG-15 4XP2 0
JRNL AUTH M.GELIN,V.DELFOSSE,F.ALLEMAND,F.HOH,Y.SALLAZ-DAMAZ,
JRNL AUTH 2 M.PIROCCHI,W.BOURGUET,J.L.FERRER,G.LABESSE,J.F.GUICHOU
JRNL TITL COMBINING `DRY' CO-CRYSTALLIZATION AND IN SITU DIFFRACTION
JRNL TITL 2 TO FACILITATE LIGAND SCREENING BY X-RAY CRYSTALLOGRAPHY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 1777 2015
JRNL REFN ESSN 1399-0047
JRNL PMID 26249358
JRNL DOI 10.1107/S1399004715010342
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.120
REMARK 3 COMPLETENESS FOR RANGE (%) : 67.0
REMARK 3 NUMBER OF REFLECTIONS : 50815
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) : 0.185
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 2503
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 28.2991 - 4.5750 0.65 2622 126 0.1788 0.2085
REMARK 3 2 4.5750 - 3.6337 0.61 2429 138 0.1412 0.1543
REMARK 3 3 3.6337 - 3.1751 0.63 2511 122 0.1682 0.2057
REMARK 3 4 3.1751 - 2.8851 0.65 2619 129 0.1766 0.2112
REMARK 3 5 2.8851 - 2.6785 0.64 2580 146 0.1771 0.2291
REMARK 3 6 2.6785 - 2.5207 0.66 2628 156 0.1722 0.2333
REMARK 3 7 2.5207 - 2.3945 0.67 2708 147 0.1711 0.2335
REMARK 3 8 2.3945 - 2.2903 0.68 2701 164 0.1732 0.2593
REMARK 3 9 2.2903 - 2.2022 0.68 2684 127 0.1879 0.2220
REMARK 3 10 2.2022 - 2.1262 0.68 2719 167 0.1746 0.2438
REMARK 3 11 2.1262 - 2.0597 0.68 2727 162 0.1946 0.2212
REMARK 3 12 2.0597 - 2.0009 0.69 2777 121 0.1963 0.2551
REMARK 3 13 2.0009 - 1.9482 0.69 2762 133 0.2181 0.2959
REMARK 3 14 1.9482 - 1.9007 0.69 2774 143 0.2473 0.3448
REMARK 3 15 1.9007 - 1.8575 0.70 2788 128 0.2681 0.3211
REMARK 3 16 1.8575 - 1.8180 0.69 2787 119 0.2870 0.3364
REMARK 3 17 1.8180 - 1.7816 0.70 2839 148 0.3395 0.3704
REMARK 3 18 1.7816 - 1.7480 0.66 2657 127 0.3755 0.3860
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 : 0.35
REMARK 3 B_SOL : 53.96
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.30770
REMARK 3 B22 (A**2) : 2.21580
REMARK 3 B33 (A**2) : -1.90820
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.08870
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 2933
REMARK 3 ANGLE : 0.951 3970
REMARK 3 CHIRALITY : 0.064 435
REMARK 3 PLANARITY : 0.004 502
REMARK 3 DIHEDRAL : 13.640 1133
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 9:118)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6207 12.2774 34.1932
REMARK 3 T TENSOR
REMARK 3 T11: 0.2668 T22: 0.1891
REMARK 3 T33: 0.1372 T12: -0.0046
REMARK 3 T13: -0.0428 T23: 0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 0.5514 L22: 0.2166
REMARK 3 L33: 1.8662 L12: 0.3002
REMARK 3 L13: 0.0572 L23: 0.3973
REMARK 3 S TENSOR
REMARK 3 S11: -0.1093 S12: 0.1756 S13: 0.1235
REMARK 3 S21: -0.2172 S22: 0.1422 S23: 0.0795
REMARK 3 S31: -0.3980 S32: -0.2020 S33: -0.0055
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 119:312)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2067 7.9098 57.3453
REMARK 3 T TENSOR
REMARK 3 T11: 0.1044 T22: 0.1115
REMARK 3 T33: 0.1411 T12: 0.0069
REMARK 3 T13: 0.0094 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.7758 L22: 0.4781
REMARK 3 L33: 0.9734 L12: 0.5546
REMARK 3 L13: 0.6146 L23: 0.3147
REMARK 3 S TENSOR
REMARK 3 S11: 0.0041 S12: 0.0019 S13: 0.0486
REMARK 3 S21: 0.0264 S22: 0.0206 S23: 0.0066
REMARK 3 S31: 0.0096 S32: 0.0506 S33: -0.0244
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 313:354)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3320 -0.6371 35.5849
REMARK 3 T TENSOR
REMARK 3 T11: 0.1961 T22: 0.2413
REMARK 3 T33: 0.1628 T12: -0.0343
REMARK 3 T13: 0.0295 T23: -0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 0.5162 L22: 0.7708
REMARK 3 L33: 1.2497 L12: 0.0043
REMARK 3 L13: 0.7647 L23: -0.1152
REMARK 3 S TENSOR
REMARK 3 S11: -0.0292 S12: 0.2273 S13: -0.0620
REMARK 3 S21: -0.3013 S22: 0.0652 S23: -0.0083
REMARK 3 S31: 0.3968 S32: 0.4825 S33: -0.0700
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN S
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0648 6.2991 51.0661
REMARK 3 T TENSOR
REMARK 3 T11: 0.1584 T22: 0.1586
REMARK 3 T33: 0.1750 T12: -0.0063
REMARK 3 T13: 0.0103 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.1888 L22: 0.4415
REMARK 3 L33: 0.6176 L12: -0.0106
REMARK 3 L13: 0.1730 L23: 0.1031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: -0.0043 S13: -0.0203
REMARK 3 S21: -0.0224 S22: 0.0408 S23: -0.0072
REMARK 3 S31: -0.0206 S32: 0.0291 S33: -0.0072
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0153 13.7636 41.3115
REMARK 3 T TENSOR
REMARK 3 T11: 0.5817 T22: 0.6779
REMARK 3 T33: 0.2131 T12: -0.2131
REMARK 3 T13: -0.0260 T23: -0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 7.9849 L22: 5.2389
REMARK 3 L33: 6.4828 L12: 6.4577
REMARK 3 L13: 6.3376 L23: 4.9712
REMARK 3 S TENSOR
REMARK 3 S11: -0.0521 S12: 0.0295 S13: -0.0623
REMARK 3 S21: -0.1655 S22: 0.2680 S23: -0.1623
REMARK 3 S31: -0.0484 S32: -0.1916 S33: -0.1633
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 4XP2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205980.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAY-08
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 : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97970
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69472
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 28.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.7
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.28900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 3QYW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG MME 2000, 0.1M MES PH 6.5,
REMARK 280 0.1M AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, VAPOR
REMARK 280 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 35.15700
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 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 LEU A 336
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 PHE A 329 CG CD1 CD2 CE1 CE2 CZ
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 ASP A 147 42.08 -142.93
REMARK 500 ASP A 165 85.42 60.84
REMARK 500 ASN A 199 19.44 -160.28
REMARK 500 LEU A 292 47.92 -98.12
REMARK 500 ASP A 316 94.20 -161.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 772 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A 773 DISTANCE = 5.97 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TT4 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 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405
DBREF 4XP2 A 8 358 UNP P63086 MK01_RAT 8 358
SEQRES 1 A 351 GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY
SEQRES 2 A 351 PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA
SEQRES 3 A 351 TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS
SEQRES 4 A 351 VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS
SEQRES 5 A 351 GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE
SEQRES 6 A 351 LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN
SEQRES 7 A 351 ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP
SEQRES 8 A 351 VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR
SEQRES 9 A 351 LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE
SEQRES 10 A 351 CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR
SEQRES 11 A 351 ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 12 A 351 SER ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE
SEQRES 13 A 351 CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS
SEQRES 14 A 351 ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG
SEQRES 15 A 351 TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY
SEQRES 16 A 351 TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE
SEQRES 17 A 351 LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY
SEQRES 18 A 351 LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE
SEQRES 19 A 351 LEU GLY SER PRO SER GLN GLU ASP LEU ASN CME ILE ILE
SEQRES 20 A 351 ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS
SEQRES 21 A 351 LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA
SEQRES 22 A 351 ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR
SEQRES 23 A 351 PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU
SEQRES 24 A 351 ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP
SEQRES 25 A 351 GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU
SEQRES 26 A 351 LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE
SEQRES 27 A 351 PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER
MODRES 4XP2 CME A 159 CYS MODIFIED RESIDUE
MODRES 4XP2 CME A 252 CYS MODIFIED RESIDUE
HET CME A 159 10
HET CME A 252 10
HET TT4 A 401 13
HET DMS A 402 4
HET DMS A 403 4
HET SO4 A 404 10
HET SO4 A 405 5
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM TT4 1-PHENYL-1H-1,2,4-TRIAZOLE-3,5-DIAMINE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM SO4 SULFATE ION
FORMUL 1 CME 2(C5 H11 N O3 S2)
FORMUL 2 TT4 C8 H9 N5
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *273(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 HIS A 230 GLY A 243 1 14
HELIX 10 AB1 SER A 246 CME A 252 1 7
HELIX 11 AB2 ASN A 255 LEU A 265 1 11
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 LYS A 338 THR A 349 1 12
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 MET A 36 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 47 N ASP A 42
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
LINK C ASN A 251 N CME A 252 1555 1555 1.33
LINK C CME A 252 N ILE A 253 1555 1555 1.33
SITE 1 AC1 4 ALA A 50 GLN A 103 ASP A 104 MET A 106
SITE 1 AC2 6 LYS A 136 HIS A 139 SER A 140 LYS A 205
SITE 2 AC2 6 GLU A 303 HOH A 710
SITE 1 AC3 4 HIS A 123 TYR A 126 ILE A 254 ARG A 259
SITE 1 AC4 7 TYR A 185 ARG A 189 ARG A 192 TYR A 231
SITE 2 AC4 7 HOH A 539 HOH A 603 HOH A 647
SITE 1 AC5 5 HIS A 297 LYS A 298 ARG A 299 ILE A 300
SITE 2 AC5 5 GLN A 304
CRYST1 48.637 70.314 59.827 90.00 108.93 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 0.020561 0.000000 0.007052 0.00000
SCALE2 0.000000 0.014222 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017671 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
