LinkDB: 2Z7L
Original site: 2Z7L
Chemical substance (3) PDB-CCD (3) Chemical reaction (1) KEGG ENZYME (1) Protein sequence (3) UniProt (1) SWISS-PROT (1) PDBSTR (1) Protein domain (7) InterPro (6) Pfam (1) Literature (1) PubMed (1) All databases (15)
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HEADER TRANSFERASE 27-AUG-07 2Z7L
TITLE UNPHOSPHORYLATED MITOGEN ACTIVATED PROTEIN KINASE ERK2 IN
TITLE 2 COMPLEX WITH (4-{[5-CARBAMOYL-4-(3-METHYLANILINO)PYRIMIDIN
TITLE 3 2-YL]AMINO}PHENYL)ACETIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EXTRACELLULAR SIGNAL-REGULATED KINASE 2, ERK-2,
COMPND 5 MITOGEN-ACTIVATED PROTEIN KINASE 2, MAP KINASE 2, MAPK 2,
COMPND 6 P42-MAPK, ERT1;
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;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING,
KEYWDS 2 CELL CYCLE, PHOSPHORYLATION, ACETYLATION, NUCLEOTIDE-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR N.KATAYAMA,H.KURIHARA
REVDAT 3 24-FEB-09 2Z7L 1 VERSN
REVDAT 2 11-NOV-08 2Z7L 1 JRNL
REVDAT 1 12-AUG-08 2Z7L 0
JRNL AUTH N.KATAYAMA,M.ORITA,T.YAMAGUCHI,H.HISAMICHI,
JRNL AUTH 2 S.KUROMITSU,H.KURIHARA,H.SAKASHITA,Y.MATSUMOTO,
JRNL AUTH 3 S.FUJITA,T.NIIMI
JRNL TITL IDENTIFICATION OF A KEY ELEMENT FOR
JRNL TITL 2 HYDROGEN-BONDING PATTERNS BETWEEN PROTEIN KINASES
JRNL TITL 3 AND THEIR INHIBITORS
JRNL REF PROTEINS V. 73 795 2008
JRNL REFN ISSN 0887-3585
JRNL PMID 18767165
JRNL DOI 10.1002/PROT.22207
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 397568.940
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.0
REMARK 3 NUMBER OF REFLECTIONS : 12380
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1271
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 49.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1128
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 125
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2690
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 129
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.53000
REMARK 3 B22 (A**2) : 10.79000
REMARK 3 B33 (A**2) : -5.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.28
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.70
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.250 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.030 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.830 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.650 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 60.13
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2Z7L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-AUG-07.
REMARK 100 THE RCSB ID CODE IS RCSB027621.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12389
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 44.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07700
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: CNX 2002
REMARK 200 STARTING MODEL: PDB ENTRY 3ERK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG550 MME, ETHYLENE GLYCOL, BETA-
REMARK 280 MERCAPTOETHANOL, PH7.0, VAPOR DIFFUSION, SITTING DROP
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 34.98100
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 MET A -5
REMARK 465 ALA A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 MET A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 GLY A 10
REMARK 465 PRO A 11
REMARK 465 GLU A 12
REMARK 465 MET A 13
REMARK 465 VAL A 14
REMARK 465 ARG A 15
REMARK 465 GLY A 16
REMARK 465 GLN A 17
REMARK 465 GLY A 34
REMARK 465 ALA A 35
REMARK 465 TYR A 36
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 ASP A 336
REMARK 465 ASP A 337
REMARK 465 TYR A 358
REMARK 465 ARG A 359
REMARK 465 SER A 360
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 SER A 29 122.28 179.36
REMARK 500 ILE A 31 -47.18 -132.03
REMARK 500 SER A 57 49.23 -157.40
REMARK 500 THR A 63 22.45 -70.74
REMARK 500 TYR A 64 16.36 -152.09
REMARK 500 LYS A 99 -82.87 -117.74
REMARK 500 THR A 110 -168.04 -177.08
REMARK 500 THR A 118 -29.86 -156.16
REMARK 500 ASP A 149 33.77 -148.43
REMARK 500 ASP A 167 86.62 66.29
REMARK 500 ASP A 175 60.45 -150.94
REMARK 500 HIS A 178 56.92 -118.61
REMARK 500 LEU A 184 60.05 64.43
REMARK 500 ALA A 189 150.05 -40.28
REMARK 500 LEU A 200 -54.50 -122.98
REMARK 500 ASN A 201 5.90 -162.93
REMARK 500 ARG A 225 139.32 -173.23
REMARK 500 PHE A 228 76.08 -117.22
REMARK 500 TYR A 233 -72.45 -27.01
REMARK 500 LEU A 294 66.99 -101.41
REMARK 500 ASP A 318 89.34 -157.27
REMARK 500 GLU A 341 -38.74 -157.44
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 SO4 A 2100
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S91 A 1001
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 2001
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 2002
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 2003
DBREF 2Z7L A 3 360 UNP P63086 MK01_RAT 1 358
SEQADV 2Z7L MET A -5 UNP P63086 EXPRESSION TAG
SEQADV 2Z7L ALA A -4 UNP P63086 EXPRESSION TAG
SEQADV 2Z7L HIS A -3 UNP P63086 EXPRESSION TAG
SEQADV 2Z7L HIS A -2 UNP P63086 EXPRESSION TAG
SEQADV 2Z7L HIS A -1 UNP P63086 EXPRESSION TAG
SEQADV 2Z7L HIS A 0 UNP P63086 EXPRESSION TAG
SEQADV 2Z7L HIS A 1 UNP P63086 EXPRESSION TAG
SEQADV 2Z7L HIS A 2 UNP P63086 EXPRESSION TAG
SEQRES 1 A 366 MET ALA HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA
SEQRES 2 A 366 ALA ALA GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP
SEQRES 3 A 366 VAL GLY PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU
SEQRES 4 A 366 GLY ALA TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU
SEQRES 5 A 366 ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE
SEQRES 6 A 366 GLU HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE
SEQRES 7 A 366 LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY
SEQRES 8 A 366 ILE ASN ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET
SEQRES 9 A 366 LYS ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP
SEQRES 10 A 366 LEU TYR LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP
SEQRES 11 A 366 HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU
SEQRES 12 A 366 LYS TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU
SEQRES 13 A 366 LYS PRO SER ASN LEU LEU LEU ASN THR THR CYS ASP LEU
SEQRES 14 A 366 LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO
SEQRES 15 A 366 ASP HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA
SEQRES 16 A 366 THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER
SEQRES 17 A 366 LYS GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY
SEQRES 18 A 366 CYS ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE
SEQRES 19 A 366 PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU
SEQRES 20 A 366 GLY ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS
SEQRES 21 A 366 ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU
SEQRES 22 A 366 PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO
SEQRES 23 A 366 ASN ALA ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET
SEQRES 24 A 366 LEU THR PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN
SEQRES 25 A 366 ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO
SEQRES 26 A 366 SER ASP GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP
SEQRES 27 A 366 MET GLU LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU
SEQRES 28 A 366 LEU ILE PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR
SEQRES 29 A 366 ARG SER
HET SO4 A2100 5
HET S91 A1001 28
HET BME A2001 4
HET BME A2002 4
HET BME A2003 4
HETNAM SO4 SULFATE ION
HETNAM S91 [4-({5-(AMINOCARBONYL)-4-[(3-METHYLPHENYL)
HETNAM 2 S91 AMINO]PYRIMIDIN-2-YL}AMINO)PHENYL]ACETIC ACID
HETNAM BME BETA-MERCAPTOETHANOL
HETSYN S91 (4-{[5-CARBAMOYL-4-(3-METHYLANILINO)PYRIMIDIN-2-
HETSYN 2 S91 YL]AMINO}PHENYL)ACETIC ACID
FORMUL 2 SO4 O4 S 2-
FORMUL 3 S91 C20 H19 N5 O3
FORMUL 4 BME 3(C2 H6 O S)
FORMUL 7 HOH *129(H2 O)
HELIX 1 1 SER A 57 TYR A 64 5 8
HELIX 2 2 CYS A 65 PHE A 78 1 14
HELIX 3 3 LEU A 112 LYS A 117 1 6
HELIX 4 4 SER A 122 ALA A 143 1 22
HELIX 5 5 LYS A 151 SER A 153 5 3
HELIX 6 6 ASP A 175 ASP A 179 5 5
HELIX 7 7 THR A 190 ARG A 194 5 5
HELIX 8 8 ALA A 195 MET A 199 5 5
HELIX 9 9 LYS A 207 ASN A 224 1 18
HELIX 10 10 HIS A 232 GLY A 245 1 14
HELIX 11 11 SER A 248 ILE A 255 1 8
HELIX 12 12 ASN A 257 LEU A 267 1 11
HELIX 13 13 PRO A 274 PHE A 279 1 6
HELIX 14 14 ASP A 283 LEU A 294 1 12
HELIX 15 15 ASN A 297 ARG A 301 5 5
HELIX 16 16 GLU A 303 ALA A 309 1 7
HELIX 17 17 HIS A 310 GLU A 314 5 5
HELIX 18 18 ASP A 318 GLU A 322 5 5
HELIX 19 19 GLU A 341 THR A 351 1 11
SHEET 1 A 3 TYR A 25 THR A 26 0
SHEET 2 A 3 MET A 38 ASP A 44 -1 O TYR A 43 N THR A 26
SHEET 3 A 3 TYR A 30 GLY A 32 -1 N ILE A 31 O VAL A 39
SHEET 1 B 5 TYR A 25 THR A 26 0
SHEET 2 B 5 MET A 38 ASP A 44 -1 O TYR A 43 N THR A 26
SHEET 3 B 5 VAL A 49 ILE A 56 -1 O LYS A 55 N MET A 38
SHEET 4 B 5 VAL A 101 ASP A 106 -1 O VAL A 101 N ILE A 56
SHEET 5 B 5 ASP A 88 ILE A 90 -1 N ASP A 88 O VAL A 104
SHEET 1 C 3 THR A 110 ASP A 111 0
SHEET 2 C 3 LEU A 155 LEU A 157 -1 O LEU A 157 N THR A 110
SHEET 3 C 3 LEU A 163 ILE A 165 -1 O LYS A 164 N LEU A 156
SHEET 1 D 2 VAL A 145 LEU A 146 0
SHEET 2 D 2 ARG A 172 VAL A 173 -1 O ARG A 172 N LEU A 146
LINK SG CYS A 161 S2 BME A2001 1555 1555 2.03
LINK SG CYS A 254 S2 BME A2002 1555 1555 2.03
LINK SG CYS A 166 S2 BME A2003 1555 1555 2.04
SITE 1 AC1 3 ARG A 191 ARG A 194 TYR A 233
SITE 1 AC2 10 ILE A 31 GLY A 32 LYS A 54 GLN A 105
SITE 2 AC2 10 ASP A 106 MET A 108 THR A 110 ASP A 111
SITE 3 AC2 10 LYS A 114 LEU A 156
SITE 1 AC3 6 PHE A 129 ASN A 158 THR A 159 CYS A 161
SITE 2 AC3 6 LEU A 258 HOH A2222
SITE 1 AC4 3 CYS A 254 ASN A 297 HIS A 299
SITE 1 AC5 4 SER A 153 ASN A 154 CYS A 166 ASP A 167
CRYST1 48.873 69.962 60.775 90.00 109.58 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 0.020461 0.000000 0.007276 0.00000
SCALE2 0.000000 0.014294 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017464 0.00000
(ATOM LINES ARE NOT SHOWN.)
END