HEADER LYASE 29-SEP-08 3EP8
TITLE HUMAN ADOMETDC E178Q MUTANT COMPLEXED WITH S-ADENOSYLMETHIONINE METHYL
TITLE 2 ESTER AND NO PUTRESCINE BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-ADENOSYLMETHIONINE DECARBOXYLASE BETA CHAIN;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-67;
COMPND 5 SYNONYM: ADOMETDC, SAMDC;
COMPND 6 EC: 4.1.1.50;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: S-ADENOSYLMETHIONINE DECARBOXYLASE ALPHA CHAIN;
COMPND 10 CHAIN: A;
COMPND 11 FRAGMENT: UNP RESIDUES 69-328;
COMPND 12 SYNONYM: ADOMETDC, SAMDC;
COMPND 13 EC: 4.1.1.50;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AMD1, AMD;
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: PQE-C145S;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: AMD1, AMD;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PQE-C145S
KEYWDS ADOMETDC WITH MUTATION IN PUTRESCINE BINDING SITE, DECARBOXYLASE,
KEYWDS 2 LYASE, PYRUVATE, S-ADENOSYL-L-METHIONINE, SPERMIDINE BIOSYNTHESIS,
KEYWDS 3 ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BALE,M.M.LOPEZ,G.I.MAKHATADZE,Q.FANG,A.E.PEGG,S.E.EALICK
REVDAT 5 15-NOV-23 3EP8 1 LINK ATOM
REVDAT 4 06-SEP-23 3EP8 1 REMARK
REVDAT 3 20-OCT-21 3EP8 1 REMARK SEQADV LINK
REVDAT 2 25-OCT-17 3EP8 1 REMARK
REVDAT 1 23-DEC-08 3EP8 0
JRNL AUTH S.BALE,M.M.LOPEZ,G.I.MAKHATADZE,Q.FANG,A.E.PEGG,S.E.EALICK
JRNL TITL STRUCTURAL BASIS FOR PUTRESCINE ACTIVATION OF HUMAN
JRNL TITL 2 S-ADENOSYLMETHIONINE DECARBOXYLASE.
JRNL REF BIOCHEMISTRY V. 47 13404 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 19053272
JRNL DOI 10.1021/BI801732M
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 115700.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 23001
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 SET) : 0.209
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1106
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 1.97
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3276
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 164
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2409
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.23000
REMARK 3 B22 (A**2) : 1.02000
REMARK 3 B33 (A**2) : -6.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.98000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.380
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) : 1.390 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.260 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.900 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 43.09
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 : PROTEIN.PARAM
REMARK 3 PARAMETER FILE 2 : PVL.PARAM
REMARK 3 PARAMETER FILE 3 : SMM.PARAM
REMARK 3 PARAMETER FILE 4 : WATER.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PVL.TOP
REMARK 3 TOPOLOGY FILE 3 : SMM.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3EP8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23001
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0050
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.23800
REMARK 200 R SYM FOR SHELL (I) : 0.23800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1I7B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 8000, 100 MM TRIS, 10 MM DTT,
REMARK 280 PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 50.07300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.53650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.07300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.53650
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 353 LIES ON A SPECIAL POSITION.
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 B 1
REMARK 465 GLU B 2
REMARK 465 ALA B 3
REMARK 465 ARG B 20
REMARK 465 GLN B 21
REMARK 465 GLN B 22
REMARK 465 PRO B 23
REMARK 465 ASP B 24
REMARK 465 ALA B 25
REMARK 465 ASN B 26
REMARK 465 GLU A 166
REMARK 465 SER A 167
REMARK 465 ARG A 168
REMARK 465 VAL A 169
REMARK 465 ILE A 170
REMARK 465 SER A 171
REMARK 465 GLN A 172
REMARK 465 PRO A 173
REMARK 465 GLN A 288
REMARK 465 SER A 289
REMARK 465 SER A 290
REMARK 465 LYS A 291
REMARK 465 CYS A 292
REMARK 465 ARG A 293
REMARK 465 THR A 294
REMARK 465 VAL A 295
REMARK 465 LEU A 296
REMARK 465 ALA A 297
REMARK 465 SER A 298
REMARK 465 PRO A 299
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 165 C - N - CD ANGL. DEV. = -17.7 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 GLN B 48 48.27 73.55
REMARK 500 CYS A 82 -153.18 -126.57
REMARK 500 LEU A 86 70.02 -102.36
REMARK 500 ARG A 114 147.38 -178.48
REMARK 500 PRO A 126 32.90 -97.13
REMARK 500 SER A 154 -139.21 -134.67
REMARK 500 PHE A 250 39.85 -155.02
REMARK 500 ILE A 302 107.27 47.55
REMARK 500 PHE A 315 -54.82 -128.48
REMARK 500 ASN A 316 -104.87 -111.50
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 PYR A 68
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SMM A 368
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JEN RELATED DB: PDB
REMARK 900 RELATED ID: 1I72 RELATED DB: PDB
REMARK 900 RELATED ID: 1I7B RELATED DB: PDB
REMARK 900 RELATED ID: 1I7C RELATED DB: PDB
REMARK 900 RELATED ID: 1I7M RELATED DB: PDB
REMARK 900 RELATED ID: 1I79 RELATED DB: PDB
REMARK 900 RELATED ID: 3EP3 RELATED DB: PDB
REMARK 900 RELATED ID: 3EP4 RELATED DB: PDB
REMARK 900 RELATED ID: 3EP5 RELATED DB: PDB
REMARK 900 RELATED ID: 3EP6 RELATED DB: PDB
REMARK 900 RELATED ID: 3EP7 RELATED DB: PDB
REMARK 900 RELATED ID: 3EP9 RELATED DB: PDB
REMARK 900 RELATED ID: 3EPA RELATED DB: PDB
REMARK 900 RELATED ID: 3EPB RELATED DB: PDB
DBREF 3EP8 B 1 67 UNP P17707 DCAM_HUMAN 1 67
DBREF 3EP8 A 69 328 UNP P17707 DCAM_HUMAN 69 328
SEQADV 3EP8 GLN A 178 UNP P17707 GLU 178 ENGINEERED MUTATION
SEQRES 1 B 67 MET GLU ALA ALA HIS PHE PHE GLU GLY THR GLU LYS LEU
SEQRES 2 B 67 LEU GLU VAL TRP PHE SER ARG GLN GLN PRO ASP ALA ASN
SEQRES 3 B 67 GLN GLY SER GLY ASP LEU ARG THR ILE PRO ARG SER GLU
SEQRES 4 B 67 TRP ASP ILE LEU LEU LYS ASP VAL GLN CYS SER ILE ILE
SEQRES 5 B 67 SER VAL THR LYS THR ASP LYS GLN GLU ALA TYR VAL LEU
SEQRES 6 B 67 SER GLU
SEQRES 1 A 260 SER MET PHE VAL SER LYS ARG ARG PHE ILE LEU LYS THR
SEQRES 2 A 260 CYS GLY THR THR LEU LEU LEU LYS ALA LEU VAL PRO LEU
SEQRES 3 A 260 LEU LYS LEU ALA ARG ASP TYR SER GLY PHE ASP SER ILE
SEQRES 4 A 260 GLN SER PHE PHE TYR SER ARG LYS ASN PHE MET LYS PRO
SEQRES 5 A 260 SER HIS GLN GLY TYR PRO HIS ARG ASN PHE GLN GLU GLU
SEQRES 6 A 260 ILE GLU PHE LEU ASN ALA ILE PHE PRO ASN GLY ALA ALA
SEQRES 7 A 260 TYR CYS MET GLY ARG MET ASN SER ASP CYS TRP TYR LEU
SEQRES 8 A 260 TYR THR LEU ASP PHE PRO GLU SER ARG VAL ILE SER GLN
SEQRES 9 A 260 PRO ASP GLN THR LEU GLN ILE LEU MET SER GLU LEU ASP
SEQRES 10 A 260 PRO ALA VAL MET ASP GLN PHE TYR MET LYS ASP GLY VAL
SEQRES 11 A 260 THR ALA LYS ASP VAL THR ARG GLU SER GLY ILE ARG ASP
SEQRES 12 A 260 LEU ILE PRO GLY SER VAL ILE ASP ALA THR MET PHE ASN
SEQRES 13 A 260 PRO CYS GLY TYR SER MET ASN GLY MET LYS SER ASP GLY
SEQRES 14 A 260 THR TYR TRP THR ILE HIS ILE THR PRO GLU PRO GLU PHE
SEQRES 15 A 260 SER TYR VAL SER PHE GLU THR ASN LEU SER GLN THR SER
SEQRES 16 A 260 TYR ASP ASP LEU ILE ARG LYS VAL VAL GLU VAL PHE LYS
SEQRES 17 A 260 PRO GLY LYS PHE VAL THR THR LEU PHE VAL ASN GLN SER
SEQRES 18 A 260 SER LYS CYS ARG THR VAL LEU ALA SER PRO GLN LYS ILE
SEQRES 19 A 260 GLU GLY PHE LYS ARG LEU ASP CYS GLN SER ALA MET PHE
SEQRES 20 A 260 ASN ASP TYR ASN PHE VAL PHE THR SER PHE ALA LYS LYS
HET PYR A 68 4
HET SMM A 368 28
HETNAM PYR PYRUVIC ACID
HETNAM SMM S-ADENOSYLMETHIONINE METHYL ESTER
FORMUL 3 PYR C3 H4 O3
FORMUL 4 SMM C16 H26 N6 O5 S
FORMUL 5 HOH *206(H2 O)
HELIX 1 1 ASP B 31 ILE B 35 5 5
HELIX 2 2 PRO B 36 GLN B 48 1 13
HELIX 3 3 LEU A 86 LYS A 89 5 4
HELIX 4 4 ALA A 90 GLY A 103 1 14
HELIX 5 5 LYS A 119 GLN A 123 5 5
HELIX 6 6 ASN A 129 ALA A 139 1 11
HELIX 7 7 ASP A 185 GLN A 191 1 7
HELIX 8 8 THR A 199 SER A 207 1 9
HELIX 9 9 ILE A 209 ILE A 213 5 5
HELIX 10 10 TYR A 264 LYS A 276 1 13
SHEET 1 A 8 SER B 50 LYS B 56 0
SHEET 2 A 8 GLU B 61 SER B 66 -1 O ALA B 62 N THR B 55
SHEET 3 A 8 MET A 70 VAL A 72 -1 O VAL A 72 N GLU B 61
SHEET 4 A 8 ARG A 76 THR A 81 -1 O ILE A 78 N PHE A 71
SHEET 5 A 8 LYS B 12 SER B 19 -1 N LYS B 12 O THR A 81
SHEET 6 A 8 SER A 106 LYS A 115 -1 O SER A 113 N LEU B 13
SHEET 7 A 8 CYS A 156 LEU A 162 -1 O TYR A 158 N ARG A 114
SHEET 8 A 8 GLY A 144 GLY A 150 -1 N ALA A 145 O THR A 161
SHEET 1 B 8 VAL A 217 MET A 222 0
SHEET 2 B 8 TYR A 228 MET A 233 -1 O MET A 233 N VAL A 217
SHEET 3 B 8 TYR A 239 THR A 245 -1 O ILE A 244 N TYR A 228
SHEET 4 B 8 TYR A 252 THR A 257 -1 O TYR A 252 N THR A 245
SHEET 5 B 8 GLN A 175 LEU A 184 -1 N MET A 181 O VAL A 253
SHEET 6 B 8 PRO A 277 VAL A 286 -1 O LYS A 279 N SER A 182
SHEET 7 B 8 PHE A 320 LYS A 327 -1 O PHE A 325 N PHE A 280
SHEET 8 B 8 PHE A 305 ALA A 313 -1 N GLN A 311 O PHE A 322
LINK C PYR A 68 N SER A 69 1555 1555 1.36
LINK CA PYR A 68 N SMM A 368 1555 1555 1.30
CISPEP 1 TYR A 125 PRO A 126 0 -0.14
CISPEP 2 ASN A 224 PRO A 225 0 -0.54
SITE 1 AC1 7 SER A 69 LYS A 80 THR A 81 HIS A 243
SITE 2 AC1 7 SMM A 368 VAL B 64 LEU B 65
SITE 1 AC2 19 PYR A 68 SER A 69 THR A 81 CYS A 82
SITE 2 AC2 19 PHE A 223 ASN A 224 CYS A 226 GLY A 227
SITE 3 AC2 19 TYR A 228 SER A 229 ILE A 244 THR A 245
SITE 4 AC2 19 PRO A 246 GLU A 247 HOH A 534 PHE B 7
SITE 5 AC2 19 LEU B 65 SER B 66 GLU B 67
CRYST1 100.146 51.073 68.947 90.00 105.39 90.00 C 1 2 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 0.009985 0.000000 0.002749 0.00000
SCALE2 0.000000 0.019580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015044 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
