HEADER TRANSFERASE 16-JAN-15 4XP3
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 FRAGMENT: UNP RESIDUES 8-358;
COMPND 5 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,
COMPND 6 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,
COMPND 7 MAPK 2;
COMPND 8 EC: 2.7.11.24;
COMPND 9 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 4XP3 1 REMARK SITE ATOM
REVDAT 2 19-AUG-15 4XP3 1 JRNL
REVDAT 1 12-AUG-15 4XP3 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. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.280
REMARK 3 COMPLETENESS FOR RANGE (%) : 77.9
REMARK 3 NUMBER OF REFLECTIONS : 55296
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2800
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 23.2000 - 4.8223 0.86 2906 148 0.1708 0.1800
REMARK 3 2 4.8223 - 3.8332 0.87 2915 163 0.1238 0.1459
REMARK 3 3 3.8332 - 3.3503 0.86 2916 134 0.1287 0.1437
REMARK 3 4 3.3503 - 3.0447 0.85 2820 149 0.1405 0.1578
REMARK 3 5 3.0447 - 2.8269 0.84 2853 142 0.1470 0.1829
REMARK 3 6 2.8269 - 2.6605 0.83 2787 166 0.1516 0.1990
REMARK 3 7 2.6605 - 2.5274 0.82 2718 175 0.1450 0.1806
REMARK 3 8 2.5274 - 2.4175 0.81 2681 166 0.1435 0.1843
REMARK 3 9 2.4175 - 2.3245 0.80 2732 154 0.1471 0.1884
REMARK 3 10 2.3245 - 2.2444 0.80 2670 150 0.1457 0.1940
REMARK 3 11 2.2444 - 2.1742 0.79 2670 152 0.1507 0.1987
REMARK 3 12 2.1742 - 2.1121 0.78 2580 177 0.1569 0.1808
REMARK 3 13 2.1121 - 2.0566 0.78 2592 165 0.1597 0.1913
REMARK 3 14 2.0566 - 2.0064 0.78 2650 105 0.1553 0.1752
REMARK 3 15 2.0064 - 1.9608 0.76 2595 112 0.1591 0.1999
REMARK 3 16 1.9608 - 1.9191 0.76 2512 143 0.1625 0.2577
REMARK 3 17 1.9191 - 1.8808 0.75 2547 108 0.1717 0.1886
REMARK 3 18 1.8808 - 1.8453 0.71 2419 118 0.1887 0.2644
REMARK 3 19 1.8453 - 1.8123 0.67 2284 98 0.1964 0.2205
REMARK 3 20 1.8123 - 1.7816 0.48 1649 75 0.2220 0.2637
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.070
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 : 0.009 3041
REMARK 3 ANGLE : 1.021 4116
REMARK 3 CHIRALITY : 0.043 441
REMARK 3 PLANARITY : 0.005 523
REMARK 3 DIHEDRAL : 13.273 1188
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): -13.8823 12.5481 34.2231
REMARK 3 T TENSOR
REMARK 3 T11: 0.2043 T22: 0.2186
REMARK 3 T33: 0.1672 T12: 0.0072
REMARK 3 T13: -0.0176 T23: 0.0575
REMARK 3 L TENSOR
REMARK 3 L11: 0.2661 L22: 0.4480
REMARK 3 L33: 1.9889 L12: 0.1481
REMARK 3 L13: -0.2688 L23: 0.1884
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: 0.1319 S13: 0.1581
REMARK 3 S21: -0.1752 S22: 0.1315 S23: 0.1313
REMARK 3 S31: -0.3206 S32: -0.3812 S33: -0.0995
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 119:312)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9305 7.8341 57.2330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0770 T22: 0.0570
REMARK 3 T33: 0.1014 T12: 0.0091
REMARK 3 T13: 0.0102 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.2638 L22: 0.6266
REMARK 3 L33: 0.9856 L12: 0.6351
REMARK 3 L13: 0.6321 L23: 0.2379
REMARK 3 S TENSOR
REMARK 3 S11: 0.0066 S12: -0.0053 S13: 0.0621
REMARK 3 S21: 0.0111 S22: 0.0044 S23: -0.0085
REMARK 3 S31: -0.0403 S32: 0.0339 S33: -0.0166
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 313:354)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2932 -0.7527 35.2749
REMARK 3 T TENSOR
REMARK 3 T11: 0.1913 T22: 0.1662
REMARK 3 T33: 0.1711 T12: -0.0269
REMARK 3 T13: 0.0101 T23: -0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 0.3726 L22: 1.6091
REMARK 3 L33: 2.9805 L12: 0.2405
REMARK 3 L13: -0.3157 L23: -1.6813
REMARK 3 S TENSOR
REMARK 3 S11: 0.0225 S12: 0.0769 S13: -0.0000
REMARK 3 S21: -0.3064 S22: 0.0401 S23: -0.0261
REMARK 3 S31: 0.2490 S32: 0.2559 S33: -0.0782
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN S
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5610 6.9561 49.7472
REMARK 3 T TENSOR
REMARK 3 T11: 0.1267 T22: 0.1155
REMARK 3 T33: 0.1408 T12: 0.0094
REMARK 3 T13: 0.0140 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.6867 L22: 0.7833
REMARK 3 L33: 0.7477 L12: 0.2663
REMARK 3 L13: 0.1758 L23: -0.1243
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: -0.0001 S13: 0.0214
REMARK 3 S21: -0.0283 S22: 0.0405 S23: 0.0092
REMARK 3 S31: -0.0246 S32: -0.0156 S33: -0.0265
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6100 12.8294 41.5138
REMARK 3 T TENSOR
REMARK 3 T11: 0.2964 T22: 0.3467
REMARK 3 T33: 0.2827 T12: -0.0774
REMARK 3 T13: -0.0659 T23: 0.1601
REMARK 3 L TENSOR
REMARK 3 L11: 2.0000 L22: 4.3897
REMARK 3 L33: 4.1977 L12: -0.7070
REMARK 3 L13: -2.5049 L23: 0.8660
REMARK 3 S TENSOR
REMARK 3 S11: 0.0825 S12: -0.1685 S13: 0.2631
REMARK 3 S21: -0.0014 S22: 0.0416 S23: -0.0673
REMARK 3 S31: -0.1633 S32: 0.0941 S33: -0.0859
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 4XP3 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_1000206005.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-07
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55297
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 56.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.14900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
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 (%): 47.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
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 34.84150
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: 1100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 GLY A 355
REMARK 465 TYR A 356
REMARK 465 ARG A 357
REMARK 465 SER A 358
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 HOH A 846 O HOH A 866 1.96
REMARK 500 O HOH A 808 O HOH A 878 2.04
REMARK 500 O HOH A 862 O HOH A 936 2.07
REMARK 500 O HOH A 832 O HOH A 845 2.11
REMARK 500 OE1 GLU A 10 O HOH A 501 2.11
REMARK 500 O HOH A 958 O HOH A 960 2.14
REMARK 500 O HOH A 713 O HOH A 919 2.15
REMARK 500 O HOH A 890 O HOH A 894 2.15
REMARK 500 O HOH A 695 O HOH A 704 2.15
REMARK 500 O HOH A 771 O HOH A 835 2.16
REMARK 500 O HOH A 774 O HOH A 835 2.17
REMARK 500 O HOH A 517 O HOH A 526 2.18
REMARK 500 O HOH A 803 O HOH A 918 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 ASP A 147 43.42 -147.16
REMARK 500 ASP A 165 94.31 60.88
REMARK 500 ALA A 187 179.47 65.58
REMARK 500 ASN A 199 19.12 -163.58
REMARK 500 LEU A 292 49.68 -95.45
REMARK 500 ASP A 316 91.85 -162.69
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 956 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 957 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 958 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A 959 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A 960 DISTANCE = 7.23 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DX4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 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 DMS A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 413
DBREF 4XP3 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 4XP3 CME A 159 CYS MODIFIED RESIDUE
MODRES 4XP3 CME A 252 CYS MODIFIED RESIDUE
HET CME A 159 10
HET CME A 252 10
HET DX4 A 401 11
HET SO4 A 402 5
HET DMS A 403 4
HET DMS A 404 4
HET DMS A 405 4
HET DMS A 406 4
HET DMS A 407 4
HET DMS A 408 4
HET DMS A 409 4
HET DMS A 410 4
HET DMS A 411 4
HET DMS A 412 4
HET DMS A 413 4
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM DX4 2-AMINO-1,9-DIHYDRO-6H-PURINE-6-THIONE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 1 CME 2(C5 H11 N O3 S2)
FORMUL 2 DX4 C5 H5 N5 S
FORMUL 3 SO4 O4 S 2-
FORMUL 4 DMS 11(C2 H6 O S)
FORMUL 15 HOH *460(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 LEU A 232 5 3
HELIX 10 AB1 ASP A 233 GLY A 243 1 11
HELIX 11 AB2 SER A 246 CME A 252 1 7
HELIX 12 AB3 ASN A 255 SER A 264 1 10
HELIX 13 AB4 PRO A 272 PHE A 277 1 6
HELIX 14 AB5 ASP A 281 LEU A 292 1 12
HELIX 15 AB6 GLU A 301 ALA A 307 1 7
HELIX 16 AB7 HIS A 308 GLU A 312 5 5
HELIX 17 AB8 ASP A 316 GLU A 320 5 5
HELIX 18 AB9 PRO A 337 THR A 349 1 13
HELIX 19 AC1 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 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 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
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
CISPEP 1 GLY A 20 PRO A 21 0 1.10
SITE 1 AC1 10 ALA A 50 LYS A 52 GLN A 103 ASP A 104
SITE 2 AC1 10 LEU A 105 MET A 106 LEU A 154 DMS A 404
SITE 3 AC1 10 HOH A 619 HOH A 680
SITE 1 AC2 6 TYR A 185 ARG A 189 ARG A 192 TYR A 231
SITE 2 AC2 6 HOH A 734 HOH A 767
SITE 1 AC3 3 HIS A 297 GLN A 304 HOH A 759
SITE 1 AC4 6 ASP A 109 SER A 151 CYS A 164 DX4 A 401
SITE 2 AC4 6 HOH A 600 HOH A 511
SITE 1 AC5 3 THR A 188 TRP A 190 HOH A 788
SITE 1 AC6 2 LYS A 149 SER A 151
SITE 1 AC7 3 SER A 221 PRO A 224 PHE A 277
SITE 1 AC8 1 ASN A 222
SITE 1 AC9 6 LYS A 270 TRP A 273 LEU A 285 ASP A 289
SITE 2 AC9 6 HOH A 764 HOH A 644
SITE 1 AD1 10 HIS A 118 LEU A 119 ILE A 124 LEU A 220
SITE 2 AD1 10 ASN A 279 ALA A 280 HOH A 756 HOH A 622
SITE 3 AD1 10 HOH A 635 HOH A 530
SITE 1 AD2 5 ARG A 77 TYR A 137 ALA A 323 GLU A 324
SITE 2 AD2 5 HOH A 775
SITE 1 AD3 5 LEU A 105 MET A 106 GLU A 107 ASN A 156
SITE 2 AD3 5 THR A 157
SITE 1 AD4 5 ARG A 75 PRO A 326 PHE A 327 LYS A 328
SITE 2 AD4 5 PHE A 329
CRYST1 48.600 69.683 59.819 90.00 108.91 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 0.020576 0.000000 0.007049 0.00000
SCALE2 0.000000 0.014351 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017671 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
