HEADER TRANSFERASE 01-JUN-08 2ZOQ
TITLE STRUCTURAL DISSECTION OF HUMAN MITOGEN-ACTIVATED KINASE ERK1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: EXTRACELLULAR SIGNAL-REGULATED KINASE 1, ERK-1, INSULIN-
COMPND 5 STIMULATED MAP2 KINASE, MAP KINASE 1, MAPK 1, P44-ERK1, ERT2, P44-
COMPND 6 MAPK, MICROTUBULE-ASSOCIATED PROTEIN 2 KINASE;
COMPND 7 EC: 2.7.11.24;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MAPK3, ERK1, PRKM3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P
KEYWDS SERINE/THREONINE KINASE, ERK1, ACETYLATION, ATP-BINDING, CELL CYCLE,
KEYWDS 2 HOST-VIRUS INTERACTION, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,
KEYWDS 3 POLYMORPHISM, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KINOSHITA,T.TADA,S.NAKAE,I.YOSHIDA
REVDAT 3 15-NOV-23 2ZOQ 1 REMARK
REVDAT 2 01-NOV-23 2ZOQ 1 REMARK SEQADV LINK
REVDAT 1 07-APR-09 2ZOQ 0
JRNL AUTH T.KINOSHITA,I.YOSHIDA,S.NAKAE,K.OKITA,M.GOUDA,M.MATSUBARA,
JRNL AUTH 2 K.YOKOTA,H.ISHIGURO,T.TADA
JRNL TITL CRYSTAL STRUCTURE OF HUMAN MONO-PHOSPHORYLATED ERK1 AT
JRNL TITL 2 TYR204
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 377 1123 2008
JRNL REFN ISSN 0006-291X
JRNL PMID 18983981
JRNL DOI 10.1016/J.BBRC.2008.10.127
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 27265
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 + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1435
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : 28700
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 : 5736
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 314
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.600
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 2ZOQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1000028234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-07
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28700
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 144275.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1ERK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULPHATE, 2%
REMARK 280 POLYETHYLENEGLYCOL400, 0.1M, PH7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
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 45.77000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER 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 GLN A 7
REMARK 465 GLY A 8
REMARK 465 GLY A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 GLY A 12
REMARK 465 GLU A 13
REMARK 465 PRO A 14
REMARK 465 ARG A 15
REMARK 465 ARG A 16
REMARK 465 THR A 17
REMARK 465 GLU A 18
REMARK 465 GLY A 19
REMARK 465 VAL A 20
REMARK 465 GLY A 21
REMARK 465 PRO A 22
REMARK 465 GLY A 23
REMARK 465 LEU A 376
REMARK 465 GLU A 377
REMARK 465 ALA A 378
REMARK 465 PRO A 379
REMARK 465 LEU B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 GLN B 7
REMARK 465 GLY B 8
REMARK 465 GLY B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
REMARK 465 GLY B 12
REMARK 465 GLU B 13
REMARK 465 PRO B 14
REMARK 465 ARG B 15
REMARK 465 ARG B 16
REMARK 465 THR B 17
REMARK 465 GLU B 18
REMARK 465 GLY B 19
REMARK 465 VAL B 20
REMARK 465 GLY B 21
REMARK 465 PRO B 22
REMARK 465 GLY B 23
REMARK 465 LEU B 376
REMARK 465 GLU B 377
REMARK 465 ALA B 378
REMARK 465 PRO B 379
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 MET B 350 CG GLU B 351 1.53
REMARK 500 O PRO A 246 OE1 GLN A 253 2.08
REMARK 500 CD2 LEU B 352 O HOH B 492 2.15
REMARK 500 OG1 THR B 202 O HOH B 569 2.15
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 GLU A 50 CA - CB - CG ANGL. DEV. = -14.0 DEGREES
REMARK 500 GLU A 50 CG - CD - OE1 ANGL. DEV. = 12.6 DEGREES
REMARK 500 GLU A 50 CG - CD - OE2 ANGL. DEV. = -12.3 DEGREES
REMARK 500 ILE A 244 N - CA - C ANGL. DEV. = 24.7 DEGREES
REMARK 500 ILE A 244 CA - C - N ANGL. DEV. = 13.7 DEGREES
REMARK 500 PHE A 245 C - N - CA ANGL. DEV. = 19.1 DEGREES
REMARK 500 PHE A 245 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500 PRO B 75 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 ILE B 174 CA - CB - CG1 ANGL. DEV. = -13.8 DEGREES
REMARK 500 TYR B 250 O - C - N ANGL. DEV. = -16.8 DEGREES
REMARK 500 GLU B 351 CA - CB - CG ANGL. DEV. = -18.1 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 GLU A 27 172.13 61.87
REMARK 500 VAL A 28 79.02 58.07
REMARK 500 MET A 30 121.10 62.32
REMARK 500 LYS A 32 -119.79 76.93
REMARK 500 GLU A 50 -155.21 -20.39
REMARK 500 TYR A 53 -93.25 -73.75
REMARK 500 LYS A 65 47.36 37.85
REMARK 500 PRO A 75 -139.89 -94.59
REMARK 500 PHE A 76 -28.55 78.65
REMARK 500 ARG A 165 -4.29 69.67
REMARK 500 ASP A 184 106.79 16.61
REMARK 500 ALA A 191 -118.21 -43.35
REMARK 500 ASP A 192 69.57 88.76
REMARK 500 LEU A 201 48.24 35.80
REMARK 500 ALA A 206 153.81 -45.11
REMARK 500 ASN A 218 31.46 -158.88
REMARK 500 PHE A 245 34.44 70.72
REMARK 500 PRO A 246 -96.28 -71.95
REMARK 500 HIS A 249 89.41 121.12
REMARK 500 LEU A 251 -50.87 75.35
REMARK 500 GLN A 266 -80.34 -41.54
REMARK 500 LEU A 269 -87.90 -33.04
REMARK 500 ASN A 270 12.35 167.02
REMARK 500 CYS A 271 -21.73 65.94
REMARK 500 MET A 275 -71.30 -37.71
REMARK 500 ALA A 293 -3.89 -56.46
REMARK 500 LYS A 298 32.72 87.29
REMARK 500 LEU A 311 54.75 -102.55
REMARK 500 ASP A 335 89.25 -161.15
REMARK 500 ASP A 338 45.56 -147.76
REMARK 500 GLU A 339 72.65 -151.85
REMARK 500 PRO A 340 155.13 -47.69
REMARK 500 MET A 350 16.33 81.46
REMARK 500 GLU A 351 -43.33 129.73
REMARK 500 ASP A 354 78.79 -110.94
REMARK 500 ARG A 370 -18.09 -47.02
REMARK 500 GLU B 27 -116.22 -166.41
REMARK 500 PHE B 76 -2.97 -45.02
REMARK 500 ARG B 108 152.88 173.15
REMARK 500 ALA B 109 148.97 -39.87
REMARK 500 ASP B 166 42.51 -151.43
REMARK 500 CYS B 178 -0.66 72.17
REMARK 500 CYS B 183 -169.70 -126.97
REMARK 500 ASP B 184 71.36 58.49
REMARK 500 PHE B 185 32.61 -96.75
REMARK 500 ALA B 191 -88.32 -44.64
REMARK 500 ASP B 192 67.75 68.26
REMARK 500 GLU B 203 170.46 -58.26
REMARK 500 PTR B 204 65.77 -177.61
REMARK 500 VAL B 205 -135.12 -62.22
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 TYR B 250 19.64
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 NA A 381 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 184 OD1
REMARK 620 2 HOH A 389 O 106.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 381 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 184 OD1
REMARK 620 2 HOH B 432 O 117.6
REMARK 620 N 1
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 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5ID B 382
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5ID A 382
DBREF 2ZOQ A 1 379 UNP P27361 MK03_HUMAN 1 379
DBREF 2ZOQ B 1 379 UNP P27361 MK03_HUMAN 1 379
SEQADV 2ZOQ LEU A -2 UNP P27361 EXPRESSION TAG
SEQADV 2ZOQ GLY A -1 UNP P27361 EXPRESSION TAG
SEQADV 2ZOQ SER A 0 UNP P27361 EXPRESSION TAG
SEQADV 2ZOQ LEU B -2 UNP P27361 EXPRESSION TAG
SEQADV 2ZOQ GLY B -1 UNP P27361 EXPRESSION TAG
SEQADV 2ZOQ SER B 0 UNP P27361 EXPRESSION TAG
SEQRES 1 A 382 LEU GLY SER MET ALA ALA ALA ALA ALA GLN GLY GLY GLY
SEQRES 2 A 382 GLY GLY GLU PRO ARG ARG THR GLU GLY VAL GLY PRO GLY
SEQRES 3 A 382 VAL PRO GLY GLU VAL GLU MET VAL LYS GLY GLN PRO PHE
SEQRES 4 A 382 ASP VAL GLY PRO ARG TYR THR GLN LEU GLN TYR ILE GLY
SEQRES 5 A 382 GLU GLY ALA TYR GLY MET VAL SER SER ALA TYR ASP HIS
SEQRES 6 A 382 VAL ARG LYS THR ARG VAL ALA ILE LYS LYS ILE SER PRO
SEQRES 7 A 382 PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU
SEQRES 8 A 382 ILE GLN ILE LEU LEU ARG PHE ARG HIS GLU ASN VAL ILE
SEQRES 9 A 382 GLY ILE ARG ASP ILE LEU ARG ALA SER THR LEU GLU ALA
SEQRES 10 A 382 MET ARG ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR
SEQRES 11 A 382 ASP LEU TYR LYS LEU LEU LYS SER GLN GLN LEU SER ASN
SEQRES 12 A 382 ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY
SEQRES 13 A 382 LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP
SEQRES 14 A 382 LEU LYS PRO SER ASN LEU LEU ILE ASN THR THR CYS ASP
SEQRES 15 A 382 LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG ILE ALA ASP
SEQRES 16 A 382 PRO GLU HIS ASP HIS THR GLY PHE LEU THR GLU PTR VAL
SEQRES 17 A 382 ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN
SEQRES 18 A 382 SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL
SEQRES 19 A 382 GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE
SEQRES 20 A 382 PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE
SEQRES 21 A 382 LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN
SEQRES 22 A 382 CYS ILE ILE ASN MET LYS ALA ARG ASN TYR LEU GLN SER
SEQRES 23 A 382 LEU PRO SER LYS THR LYS VAL ALA TRP ALA LYS LEU PHE
SEQRES 24 A 382 PRO LYS SER ASP SER LYS ALA LEU ASP LEU LEU ASP ARG
SEQRES 25 A 382 MET LEU THR PHE ASN PRO ASN LYS ARG ILE THR VAL GLU
SEQRES 26 A 382 GLU ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP
SEQRES 27 A 382 PRO THR ASP GLU PRO VAL ALA GLU GLU PRO PHE THR PHE
SEQRES 28 A 382 ALA MET GLU LEU ASP ASP LEU PRO LYS GLU ARG LEU LYS
SEQRES 29 A 382 GLU LEU ILE PHE GLN GLU THR ALA ARG PHE GLN PRO GLY
SEQRES 30 A 382 VAL LEU GLU ALA PRO
SEQRES 1 B 382 LEU GLY SER MET ALA ALA ALA ALA ALA GLN GLY GLY GLY
SEQRES 2 B 382 GLY GLY GLU PRO ARG ARG THR GLU GLY VAL GLY PRO GLY
SEQRES 3 B 382 VAL PRO GLY GLU VAL GLU MET VAL LYS GLY GLN PRO PHE
SEQRES 4 B 382 ASP VAL GLY PRO ARG TYR THR GLN LEU GLN TYR ILE GLY
SEQRES 5 B 382 GLU GLY ALA TYR GLY MET VAL SER SER ALA TYR ASP HIS
SEQRES 6 B 382 VAL ARG LYS THR ARG VAL ALA ILE LYS LYS ILE SER PRO
SEQRES 7 B 382 PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU
SEQRES 8 B 382 ILE GLN ILE LEU LEU ARG PHE ARG HIS GLU ASN VAL ILE
SEQRES 9 B 382 GLY ILE ARG ASP ILE LEU ARG ALA SER THR LEU GLU ALA
SEQRES 10 B 382 MET ARG ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR
SEQRES 11 B 382 ASP LEU TYR LYS LEU LEU LYS SER GLN GLN LEU SER ASN
SEQRES 12 B 382 ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY
SEQRES 13 B 382 LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP
SEQRES 14 B 382 LEU LYS PRO SER ASN LEU LEU ILE ASN THR THR CYS ASP
SEQRES 15 B 382 LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG ILE ALA ASP
SEQRES 16 B 382 PRO GLU HIS ASP HIS THR GLY PHE LEU THR GLU PTR VAL
SEQRES 17 B 382 ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN
SEQRES 18 B 382 SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL
SEQRES 19 B 382 GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE
SEQRES 20 B 382 PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE
SEQRES 21 B 382 LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN
SEQRES 22 B 382 CYS ILE ILE ASN MET LYS ALA ARG ASN TYR LEU GLN SER
SEQRES 23 B 382 LEU PRO SER LYS THR LYS VAL ALA TRP ALA LYS LEU PHE
SEQRES 24 B 382 PRO LYS SER ASP SER LYS ALA LEU ASP LEU LEU ASP ARG
SEQRES 25 B 382 MET LEU THR PHE ASN PRO ASN LYS ARG ILE THR VAL GLU
SEQRES 26 B 382 GLU ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP
SEQRES 27 B 382 PRO THR ASP GLU PRO VAL ALA GLU GLU PRO PHE THR PHE
SEQRES 28 B 382 ALA MET GLU LEU ASP ASP LEU PRO LYS GLU ARG LEU LYS
SEQRES 29 B 382 GLU LEU ILE PHE GLN GLU THR ALA ARG PHE GLN PRO GLY
SEQRES 30 B 382 VAL LEU GLU ALA PRO
MODRES 2ZOQ PTR A 204 TYR O-PHOSPHOTYROSINE
MODRES 2ZOQ PTR B 204 TYR O-PHOSPHOTYROSINE
HET PTR A 204 16
HET PTR B 204 16
HET SO4 A 380 5
HET NA A 381 1
HET 5ID A 382 20
HET SO4 B 380 5
HET NA B 381 1
HET 5ID B 382 20
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
HETNAM 5ID (2R,3R,4S,5R)-2-(4-AMINO-5-IODO-7H-PYRROLO[2,3-
HETNAM 2 5ID D]PYRIMIDIN-7-YL)-5-(HYDROXYMETHYL)TETRAHYDROFURAN-3,
HETNAM 3 5ID 4-DIOL
HETSYN PTR PHOSPHONOTYROSINE
HETSYN 5ID 5-IODOTUBERCIDIN
FORMUL 1 PTR 2(C9 H12 N O6 P)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 NA 2(NA 1+)
FORMUL 5 5ID 2(C11 H13 I N4 O4)
FORMUL 9 HOH *314(H2 O)
HELIX 1 1 HIS A 78 PHE A 95 1 18
HELIX 2 2 LEU A 129 GLN A 136 1 8
HELIX 3 3 SER A 139 ALA A 160 1 22
HELIX 4 4 ASP A 192 ASP A 196 5 5
HELIX 5 5 THR A 207 ALA A 212 5 6
HELIX 6 6 PRO A 213 ASN A 218 1 6
HELIX 7 7 LYS A 224 ASN A 241 1 18
HELIX 8 8 LEU A 251 GLY A 262 1 12
HELIX 9 9 ASN A 274 LEU A 284 1 11
HELIX 10 10 ALA A 291 PHE A 296 1 6
HELIX 11 11 ASP A 300 LEU A 311 1 12
HELIX 12 12 THR A 320 ALA A 326 1 7
HELIX 13 13 HIS A 327 GLU A 331 5 5
HELIX 14 14 ASP A 335 GLU A 339 5 5
HELIX 15 15 GLU A 351 LEU A 355 5 5
HELIX 16 16 PRO A 356 THR A 368 1 13
HELIX 17 17 ALA A 369 GLN A 372 5 4
HELIX 18 18 HIS B 78 ARG B 94 1 17
HELIX 19 19 LEU B 129 GLN B 136 1 8
HELIX 20 20 SER B 139 ALA B 160 1 22
HELIX 21 21 LYS B 168 SER B 170 5 3
HELIX 22 22 ASP B 192 ASP B 196 5 5
HELIX 23 23 ALA B 212 LEU B 217 5 6
HELIX 24 24 LYS B 224 ASN B 241 1 18
HELIX 25 25 HIS B 249 GLY B 262 1 14
HELIX 26 26 SER B 265 ASN B 270 1 6
HELIX 27 27 ASN B 274 GLN B 282 1 9
HELIX 28 28 ALA B 291 PHE B 296 1 6
HELIX 29 29 ASP B 300 LEU B 311 1 12
HELIX 30 30 THR B 320 ALA B 326 1 7
HELIX 31 31 HIS B 327 GLU B 331 5 5
HELIX 32 32 PRO B 356 THR B 368 1 13
HELIX 33 33 ALA B 369 GLN B 372 5 4
SHEET 1 A 5 TYR A 42 GLY A 49 0
SHEET 2 A 5 MET A 55 ASP A 61 -1 O VAL A 56 N ILE A 48
SHEET 3 A 5 THR A 66 ILE A 73 -1 O LYS A 72 N MET A 55
SHEET 4 A 5 VAL A 118 ASP A 123 -1 O GLN A 122 N ALA A 69
SHEET 5 A 5 ASP A 105 LEU A 107 -1 N ASP A 105 O VAL A 121
SHEET 1 B 3 THR A 127 ASP A 128 0
SHEET 2 B 3 LEU A 172 ILE A 174 -1 O ILE A 174 N THR A 127
SHEET 3 B 3 LEU A 180 ILE A 182 -1 O LYS A 181 N LEU A 173
SHEET 1 C 2 VAL A 162 LEU A 163 0
SHEET 2 C 2 ARG A 189 ILE A 190 -1 O ARG A 189 N LEU A 163
SHEET 1 D 2 GLU B 29 VAL B 31 0
SHEET 2 D 2 GLN B 34 PHE B 36 -1 O PHE B 36 N GLU B 29
SHEET 1 E 5 TYR B 42 GLY B 51 0
SHEET 2 E 5 GLY B 54 ASP B 61 -1 O TYR B 60 N THR B 43
SHEET 3 E 5 THR B 66 ILE B 73 -1 O THR B 66 N ASP B 61
SHEET 4 E 5 VAL B 118 ASP B 123 -1 O GLN B 122 N ALA B 69
SHEET 5 E 5 ASP B 105 LEU B 107 -1 N ASP B 105 O VAL B 121
SHEET 1 F 3 THR B 127 ASP B 128 0
SHEET 2 F 3 LEU B 172 ILE B 174 -1 O ILE B 174 N THR B 127
SHEET 3 F 3 LEU B 180 ILE B 182 -1 O LYS B 181 N LEU B 173
SHEET 1 G 2 VAL B 162 LEU B 163 0
SHEET 2 G 2 ARG B 189 ILE B 190 -1 O ARG B 189 N LEU B 163
LINK C GLU A 203 N PTR A 204 1555 1555 1.33
LINK C PTR A 204 N VAL A 205 1555 1555 1.33
LINK C GLU B 203 N PTR B 204 1555 1555 1.34
LINK C PTR B 204 N VAL B 205 1555 1555 1.33
LINK OD1 ASP A 184 NA NA A 381 1555 1555 2.05
LINK NA NA A 381 O HOH A 389 1555 1555 2.62
LINK OD1 ASP B 184 NA NA B 381 1555 1555 2.11
LINK NA NA B 381 O HOH B 432 1555 1555 2.80
CISPEP 1 GLY A 39 PRO A 40 0 0.39
CISPEP 2 ILE A 244 PHE A 245 0 1.38
CISPEP 3 LYS A 248 HIS A 249 0 -3.11
CISPEP 4 LEU A 269 ASN A 270 0 -3.91
CISPEP 5 ASN A 270 CYS A 271 0 -3.66
CISPEP 6 ALA A 349 MET A 350 0 0.05
CISPEP 7 GLY B 39 PRO B 40 0 -0.23
CISPEP 8 GLU B 203 PTR B 204 0 1.95
SITE 1 AC1 3 ARG A 208 ARG A 211 TYR A 250
SITE 1 AC2 2 ARG B 84 ARG B 165
SITE 1 AC3 3 LYS B 71 CYS B 183 ASP B 184
SITE 1 AC4 2 CYS A 183 ASP A 184
SITE 1 AC5 10 ILE B 48 ALA B 69 GLN B 122 ASP B 123
SITE 2 AC5 10 MET B 125 ASP B 128 LYS B 131 SER B 170
SITE 3 AC5 10 LEU B 173 ASP B 184
SITE 1 AC6 9 ILE A 48 GLU A 50 ALA A 69 GLN A 122
SITE 2 AC6 9 ASP A 123 MET A 125 SER A 170 LEU A 173
SITE 3 AC6 9 ASP A 184
CRYST1 62.382 91.540 64.930 90.00 91.50 90.00 P 1 21 1 4
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 0.016030 0.000000 0.000420 0.00000
SCALE2 0.000000 0.010924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015406 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
