HEADER TRANSFERASE 23-JAN-96 1GOL
TITLE COORDINATES OF RAT MAP KINASE ERK2 WITH AN ARGININE MUTATION AT
TITLE 2 POSITION 52
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXTRACELLULAR REGULATED KINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAP KINASE ERK2;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 GENE: ERK2;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: NPT7-5;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BL21;
SOURCE 12 EXPRESSION_SYSTEM_GENE: ERK2
KEYWDS TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING, CELL
KEYWDS 2 CYCLE, PHOSPHORYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.HARKINS,F.ZHANG,E.J.GOLDSMITH
REVDAT 5 07-FEB-24 1GOL 1 REMARK
REVDAT 4 03-NOV-21 1GOL 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1GOL 1 VERSN
REVDAT 2 01-APR-03 1GOL 1 JRNL
REVDAT 1 12-MAR-97 1GOL 0
JRNL AUTH M.J.ROBINSON,P.C.HARKINS,J.ZHANG,R.BAER,J.W.HAYCOCK,
JRNL AUTH 2 M.H.COBB,E.J.GOLDSMITH
JRNL TITL MUTATION OF POSITION 52 IN ERK2 CREATES A NONPRODUCTIVE
JRNL TITL 2 BINDING MODE FOR ADENOSINE 5'-TRIPHOSPHATE.
JRNL REF BIOCHEMISTRY V. 35 5641 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8639522
JRNL DOI 10.1021/BI952723E
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.ZHANG,F.ZHANG,D.EBERT,M.H.COBB,E.J.GOLDSMITH
REMARK 1 TITL ACTIVITY OF THE MAP KINASE ERK2 IS CONTROLLED BY A FLEXIBLE
REMARK 1 TITL 2 SURFACE LOOP
REMARK 1 REF STRUCTURE V. 3 299 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.ZHANG,A.STRAND,D.ROBBINS,M.H.COBB,E.J.GOLDSMITH
REMARK 1 TITL ATOMIC STRUCTURE OF THE MAP KINASE ERK2 AT 2.3 A RESOLUTION
REMARK 1 REF NATURE V. 367 704 1994
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 3
REMARK 1 AUTH F.ZHANG,D.J.ROBBINS,M.H.COBB,E.J.GOLDSMITH
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF
REMARK 1 TITL 2 EXTRACELLULAR SIGNAL-REGULATED KINASE-2/MAP KINASE WITH AN
REMARK 1 TITL 3 INCORPORATED HIS-TAG
REMARK 1 REF J.MOL.BIOL. V. 233 550 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2901
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 79
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173647.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-95
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.05600
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 35.71000
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 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 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 CD1 ILE A 207 O HOH A 514 1.96
REMARK 500 O ASN A 236 O HOH A 813 2.03
REMARK 500 NZ LYS A 270 O HOH A 525 2.04
REMARK 500 OG1 THR A 204 O HOH A 514 2.08
REMARK 500 O HOH A 609 O HOH A 719 2.11
REMARK 500 OD2 ASP A 249 O HOH A 605 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A 8 C PRO A 9 N 0.246
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 278 C - N - CA ANGL. DEV. = 9.6 DEGREES
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 ALA A 3 -31.07 62.00
REMARK 500 ALA A 4 25.60 -64.47
REMARK 500 GLU A 10 -10.80 63.22
REMARK 500 MET A 11 164.52 164.22
REMARK 500 VAL A 12 -125.83 62.60
REMARK 500 GLN A 15 -101.39 -80.60
REMARK 500 PHE A 17 56.67 -167.11
REMARK 500 THR A 24 -130.34 -83.38
REMARK 500 ASN A 25 114.46 -11.80
REMARK 500 GLU A 31 -133.05 -154.82
REMARK 500 ALA A 33 37.46 -73.64
REMARK 500 TYR A 34 -37.35 -140.55
REMARK 500 PHE A 57 -4.73 -58.72
REMARK 500 ASP A 147 36.23 -148.67
REMARK 500 ASP A 165 79.82 71.89
REMARK 500 ASN A 199 27.79 -163.72
REMARK 500 ASP A 316 89.65 -163.80
REMARK 500 LYS A 328 134.39 -173.80
REMARK 500 MET A 331 -17.03 151.54
REMARK 500 GLU A 332 70.79 -41.04
REMARK 500 ASP A 334 1.56 -60.64
REMARK 500 LEU A 336 123.34 -177.79
REMARK 500 LYS A 338 8.94 -65.82
REMARK 500 PRO A 354 17.44 -65.74
REMARK 500 TYR A 356 61.39 -104.47
REMARK 500 ARG A 357 -33.15 176.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 191 0.07 SIDE CHAIN
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 582 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 152 ND2
REMARK 620 2 ASP A 165 OD2 71.0
REMARK 620 3 ATP A 581 O1G 151.5 100.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 582
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 581
DBREF 1GOL A 1 358 UNP P63086 MK01_RAT 1 358
SEQADV 1GOL ARG A 52 UNP P63086 LYS 52 ENGINEERED MUTATION
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 ARG 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 CYS 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
HET MG A 582 1
HET ATP A 581 31
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 ATP C10 H16 N5 O13 P3
FORMUL 4 HOH *79(H2 O)
HELIX 1 1 GLN A 60 ARG A 75 1 16
HELIX 2 2 LEU A 110 THR A 116 1 7
HELIX 3 3 ASN A 121 ALA A 141 1 21
HELIX 4 4 PRO A 150 ASN A 152 5 3
HELIX 5 5 PRO A 174 HIS A 176 5 3
HELIX 6 6 ARG A 189 TYR A 191 5 3
HELIX 7 7 PRO A 194 ILE A 196 5 3
HELIX 8 8 LYS A 205 SER A 221 5 17
HELIX 9 9 TYR A 231 LEU A 242 1 12
HELIX 10 10 GLN A 247 CYS A 252 1 6
HELIX 11 11 LEU A 256 SER A 264 1 9
HELIX 12 12 TRP A 273 LEU A 276 1 4
HELIX 13 13 SER A 282 MET A 291 1 10
HELIX 14 14 VAL A 302 LEU A 306 1 5
HELIX 15 15 PRO A 309 LEU A 311 5 3
HELIX 16 16 PRO A 317 ASP A 319 5 3
HELIX 17 17 LYS A 342 PHE A 352 1 11
HELIX 18 18 PRO A 354 TYR A 356 5 3
SHEET 1 A 5 LEU A 26 TYR A 28 0
SHEET 2 A 5 VAL A 37 ASP A 42 -1 N SER A 39 O SER A 27
SHEET 3 A 5 VAL A 47 ILE A 54 -1 N ILE A 51 O CYS A 38
SHEET 4 A 5 VAL A 99 ASP A 104 -1 N GLN A 103 O ALA A 50
SHEET 5 A 5 ILE A 84 ILE A 88 -1 N ILE A 88 O TYR A 100
SHEET 1 B 2 LEU A 153 LEU A 155 0
SHEET 2 B 2 LEU A 161 ILE A 163 -1 N LYS A 162 O LEU A 154
LINK ND2 ASN A 152 MG MG A 582 1555 1555 2.61
LINK OD2 ASP A 165 MG MG A 582 1555 1555 2.58
LINK O1G ATP A 581 MG MG A 582 1555 1555 2.62
SITE 1 AC1 3 ASN A 152 ASP A 165 ATP A 581
SITE 1 AC2 7 VAL A 37 ALA A 50 ASP A 104 MET A 106
SITE 2 AC2 7 ASP A 109 LYS A 112 MG A 582
CRYST1 49.320 71.420 61.250 90.00 109.75 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 0.020276 0.000000 0.007280 0.00000
SCALE2 0.000000 0.014002 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017347 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
