HEADER TRANSFERASE/TRANSFERASE INHIBITOR 04-MAR-11 3QYZ
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: 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: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
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 TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING CELL CYCLE,
KEYWDS 2 PHOSPHORYLATION, PROTEIN KINASE, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GELIN,S.POCHET,F.HOH,M.PIROCHI,J.-F.GUICHOU,J.-L.FERRER,G.LABESSE
REVDAT 3 08-NOV-17 3QYZ 1 REMARK
REVDAT 2 21-MAR-12 3QYZ 1 JRNL
REVDAT 1 24-AUG-11 3QYZ 0
JRNL AUTH A.LE MAIRE,M.GELIN,S.POCHET,F.HOH,M.PIROCCHI,J.F.GUICHOU,
JRNL AUTH 2 J.L.FERRER,G.LABESSE
JRNL TITL IN-PLATE PROTEIN CRYSTALLIZATION, IN SITU LIGAND SOAKING AND
JRNL TITL 2 X-RAY DIFFRACTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 67 747 2011
JRNL REFN ISSN 0907-4449
JRNL PMID 21904027
JRNL DOI 10.1107/S0907444911023249
REMARK 2
REMARK 2 RESOLUTION. 1.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 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) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.0
REMARK 3 NUMBER OF REFLECTIONS : 62817
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5599
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 46.1893 - 4.5352 0.94 3871 198 0.1782 0.2138
REMARK 3 2 4.5352 - 3.6002 0.94 3856 211 0.1350 0.1330
REMARK 3 3 3.6002 - 3.1452 0.93 3831 180 0.1460 0.1791
REMARK 3 4 3.1452 - 2.8577 0.93 3788 205 0.1609 0.1854
REMARK 3 5 2.8577 - 2.6529 0.93 3856 215 0.1666 0.2070
REMARK 3 6 2.6529 - 2.4965 0.92 3713 234 0.1508 0.1747
REMARK 3 7 2.4965 - 2.3715 0.92 3788 214 0.1510 0.2291
REMARK 3 8 2.3715 - 2.2682 0.92 3778 225 0.1457 0.2049
REMARK 3 9 2.2682 - 2.1809 0.93 3832 196 0.1422 0.1589
REMARK 3 10 2.1809 - 2.1057 0.93 3774 247 0.1387 0.1660
REMARK 3 11 2.1057 - 2.0398 0.94 3853 214 0.1416 0.1818
REMARK 3 12 2.0398 - 1.9815 0.94 3896 167 0.1450 0.1730
REMARK 3 13 1.9815 - 1.9293 0.95 3916 191 0.1408 0.2006
REMARK 3 14 1.9293 - 1.8823 0.95 3927 182 0.1411 0.1759
REMARK 3 15 1.8823 - 1.8395 0.96 3971 186 0.1293 0.2043
REMARK 3 16 1.8395 - 1.8003 0.96 3948 171 0.1373 0.2091
REMARK 3 17 1.8003 - 1.7643 0.96 4020 202 0.1505 0.1985
REMARK 3 18 1.7643 - 1.7310 0.95 3798 195 0.1645 0.2067
REMARK 3 19 1.7310 - 1.7001 0.94 3955 194 0.1679 0.2251
REMARK 3 20 1.7001 - 1.6713 0.94 3804 204 0.1914 0.2392
REMARK 3 21 1.6713 - 1.6443 0.89 3715 192 0.1973 0.2380
REMARK 3 22 1.6443 - 1.6190 0.87 3540 183 0.2132 0.2555
REMARK 3 23 1.6190 - 1.5952 0.84 3431 204 0.2339 0.2609
REMARK 3 24 1.5952 - 1.5728 0.79 3231 181 0.2426 0.3180
REMARK 3 25 1.5728 - 1.5515 0.74 3036 174 0.2817 0.2906
REMARK 3 26 1.5515 - 1.5313 0.69 2822 137 0.2911 0.3370
REMARK 3 27 1.5313 - 1.5122 0.63 2631 132 0.3069 0.3355
REMARK 3 28 1.5122 - 1.4940 0.58 2423 134 0.3370 0.3935
REMARK 3 29 1.4940 - 1.4766 0.52 2131 114 0.3681 0.3973
REMARK 3 30 1.4766 - 1.4600 0.46 1884 117 0.4197 0.4303
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.49
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 89.75
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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) : -0.74860
REMARK 3 B22 (A**2) : 0.85580
REMARK 3 B33 (A**2) : -2.73150
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.22600
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 3089
REMARK 3 ANGLE : 1.092 4179
REMARK 3 CHIRALITY : 0.074 473
REMARK 3 PLANARITY : 0.006 517
REMARK 3 DIHEDRAL : 16.074 1214
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 3QYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064280.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-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 : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : ASYMMETRIC LAUE 001
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62817
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 46.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
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) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.6
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: ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: ISOMORPHOUS REPLACEMENT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG MME 2000, 0.1M MES, 0.1M
REMARK 280 AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291.15K
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 35.11850
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 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 14
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 GLY A 8 N CA
REMARK 470 LYS A 97 CG CD CE NZ
REMARK 470 PHE A 329 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 336 CB CG CD1 CD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 351 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 TYR A 34 41.84 -149.29
REMARK 500 ASP A 147 43.38 -149.49
REMARK 500 ASP A 165 83.49 59.89
REMARK 500 ALA A 187 179.24 60.59
REMARK 500 ASN A 199 17.76 -163.56
REMARK 500 LEU A 292 47.41 -96.26
REMARK 500 ASP A 316 93.51 -160.80
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 Z8B A 359
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 363
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 366
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 367
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 369
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 370
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 372
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 373
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QYU RELATED DB: PDB
REMARK 900 RELATED ID: 3QYW RELATED DB: PDB
DBREF 3QYZ A 1 358 UNP P63086 MK01_RAT 1 358
SEQADV 3QYZ HIS A -5 UNP P63086 EXPRESSION TAG
SEQADV 3QYZ HIS A -4 UNP P63086 EXPRESSION TAG
SEQADV 3QYZ HIS A -3 UNP P63086 EXPRESSION TAG
SEQADV 3QYZ HIS A -2 UNP P63086 EXPRESSION TAG
SEQADV 3QYZ HIS A -1 UNP P63086 EXPRESSION TAG
SEQADV 3QYZ 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 3QYZ CME A 159 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 159 10
HET Z8B A 359 22
HET DMS A 360 4
HET DMS A 361 4
HET DMS A 362 4
HET DMS A 363 4
HET DMS A 364 4
HET DMS A 365 4
HET DMS A 366 4
HET DMS A 367 4
HET DMS A 368 4
HET DMS A 369 4
HET DMS A 370 4
HET SO4 A 371 10
HET SO4 A 372 5
HET BME A 373 4
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM Z8B 5'-AZIDO-8-BROMO-5'-DEOXYADENOSINE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM SO4 SULFATE ION
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 1 CME C5 H11 N O3 S2
FORMUL 2 Z8B C10 H11 BR N8 O3
FORMUL 3 DMS 11(C2 H6 O S)
FORMUL 14 SO4 2(O4 S 2-)
FORMUL 16 BME C2 H6 O S
FORMUL 17 HOH *448(H2 O)
HELIX 1 1 HIS A 59 PHE A 76 1 18
HELIX 2 2 LEU A 110 GLN A 117 1 8
HELIX 3 3 SER A 120 ALA A 141 1 22
HELIX 4 4 LYS A 149 SER A 151 5 3
HELIX 5 5 ASP A 173 ASP A 177 5 5
HELIX 6 6 THR A 188 ARG A 192 5 5
HELIX 7 7 ALA A 193 ASN A 199 1 7
HELIX 8 8 LYS A 205 ASN A 222 1 18
HELIX 9 9 HIS A 230 LEU A 232 5 3
HELIX 10 10 ASP A 233 GLY A 243 1 11
HELIX 11 11 SER A 246 CYS A 252 1 7
HELIX 12 12 ASN A 255 SER A 264 1 10
HELIX 13 13 PRO A 272 PHE A 277 1 6
HELIX 14 14 ASP A 281 LEU A 292 1 12
HELIX 15 15 GLU A 301 ALA A 307 1 7
HELIX 16 16 HIS A 308 GLU A 312 5 5
HELIX 17 17 ASP A 316 GLU A 320 5 5
HELIX 18 18 PRO A 337 THR A 349 1 13
HELIX 19 19 ALA A 350 GLN A 353 5 4
SHEET 1 A 5 TYR A 23 GLU A 31 0
SHEET 2 A 5 GLY A 35 ASP A 42 -1 O TYR A 41 N THR A 24
SHEET 3 A 5 VAL A 47 ILE A 54 -1 O VAL A 49 N ALA A 40
SHEET 4 A 5 VAL A 99 ASP A 104 -1 O VAL A 99 N ILE A 54
SHEET 5 A 5 ASP A 86 ILE A 88 -1 N ILE A 88 O TYR A 100
SHEET 1 B 3 THR A 108 ASP A 109 0
SHEET 2 B 3 LEU A 153 LEU A 155 -1 O LEU A 155 N THR A 108
SHEET 3 B 3 LEU A 161 ILE A 163 -1 O LYS A 162 N LEU A 154
SHEET 1 C 2 VAL A 143 LEU A 144 0
SHEET 2 C 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 1.34
LINK C CME A 159 N ASP A 160 1555 1555 1.33
CISPEP 1 GLY A 20 PRO A 21 0 1.23
CISPEP 2 GLN A 353 PRO A 354 0 -4.00
SITE 1 AC1 15 GLY A 30 GLU A 31 GLY A 32 VAL A 37
SITE 2 AC1 15 ALA A 50 GLN A 103 ASP A 104 LEU A 105
SITE 3 AC1 15 MET A 106 ASP A 109 LYS A 112 LEU A 154
SITE 4 AC1 15 DMS A 362 HOH A 563 HOH A 721
SITE 1 AC2 7 LYS A 136 HIS A 139 SER A 140 LYS A 205
SITE 2 AC2 7 GLU A 303 HOH A 730 HOH A 762
SITE 1 AC3 3 THR A 188 TRP A 190 HOH A 627
SITE 1 AC4 5 GLY A 32 ALA A 33 TYR A 34 GLY A 35
SITE 2 AC4 5 Z8B A 359
SITE 1 AC5 2 LEU A 114 ASN A 222
SITE 1 AC6 3 ASN A 236 GLY A 240 LYS A 268
SITE 1 AC7 5 SER A 221 ARG A 223 PRO A 224 ILE A 225
SITE 2 AC7 5 PHE A 277
SITE 1 AC8 5 ASP A 122 HIS A 123 ILE A 254 ARG A 259
SITE 2 AC8 5 TYR A 314
SITE 1 AC9 6 GLU A 79 ASN A 80 TYR A 126 GLN A 130
SITE 2 AC9 6 ARG A 133 HOH A 581
SITE 1 BC1 4 HIS A 297 GLN A 304 HOH A 451 HOH A 589
SITE 1 BC2 8 HIS A 118 LEU A 119 LEU A 220 ASN A 279
SITE 2 BC2 8 ALA A 280 HOH A 428 HOH A 501 HOH A 624
SITE 1 BC3 5 ARG A 77 TYR A 137 ALA A 323 GLU A 324
SITE 2 BC3 5 HOH A 775
SITE 1 BC4 5 TYR A 185 ARG A 189 ARG A 192 TYR A 231
SITE 2 BC4 5 HOH A 472
SITE 1 BC5 4 ARG A 65 ARG A 68 LEU A 168 ARG A 170
SITE 1 BC6 2 LEU A 232 TYR A 261
CRYST1 48.689 70.237 59.482 90.00 108.53 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 0.020539 0.000000 0.006884 0.00000
SCALE2 0.000000 0.014238 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017731 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
