HEADER TRANSFERASE 03-DEC-07 3BJ8
TITLE SPERMINE/SPERMIDINE N1-ACETYLTRANSFERASE FROM MOUSE: CRYSTAL
TITLE 2 STRUCTURE OF A TERNARY COMPLEX REVEALS SOLVENT-MEDIATED
TITLE 3 SPERMINE BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIAMINE ACETYLTRANSFERASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: SPERMIDINE/SPERMINE N(1)-ACETYLTRANSFERASE 1,
COMPND 5 SSAT, SSAT-1, PUTRESCINE ACETYLTRANSFERASE, POLYAMINE N-
COMPND 6 ACETYLTRANSFERASE 1;
COMPND 7 EC: 2.3.1.57;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: SAT1, SAT;
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: PET15B
KEYWDS SSAT, COA, SPERMINE, TERNARY COMPLEX, ACYLTRANSFERASE,
KEYWDS 2 CYTOPLASM, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.J.MONTEMAYOR,D.W.HOFFMAN
REVDAT 3 22-SEP-09 3BJ8 1 SOURCE
REVDAT 2 24-FEB-09 3BJ8 1 VERSN
REVDAT 1 16-SEP-08 3BJ8 0
JRNL AUTH E.J.MONTEMAYOR,D.W.HOFFMAN
JRNL TITL THE CRYSTAL STRUCTURE OF SPERMIDINE/SPERMINE
JRNL TITL 2 N1-ACETYLTRANSFERASE IN COMPLEX WITH SPERMINE
JRNL TITL 3 PROVIDES INSIGHTS INTO SUBSTRATE BINDING AND
JRNL TITL 4 CATALYSIS.
JRNL REF BIOCHEMISTRY V. 47 9145 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18690703
JRNL DOI 10.1021/BI8009357
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1261162.780
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 35223
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) : 0.232
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1744
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5513
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 254
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5328
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 206
REMARK 3 SOLVENT ATOMS : 213
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.65000
REMARK 3 B22 (A**2) : -4.51000
REMARK 3 B33 (A**2) : -1.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.30
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) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.97
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) : 1.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.270 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.110 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.090 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 33.25
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_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : COA.PARAM
REMARK 3 PARAMETER FILE 4 : SPM.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : COA.TOP
REMARK 3 TOPOLOGY FILE 4 : SPM.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3BJ8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-08.
REMARK 100 THE RCSB ID CODE IS RCSB045587.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35462
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 39.000
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) : 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) : 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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 9.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 38.62500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.75000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.56000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.75000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.62500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.56000
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8660 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
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: 9230 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 1
REMARK 465 ALA A 2
REMARK 465 SER A 149
REMARK 465 SER A 150
REMARK 465 GLU A 151
REMARK 465 GLU A 152
REMARK 465 GLU A 170
REMARK 465 GLU A 171
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 149
REMARK 465 SER B 150
REMARK 465 GLU B 151
REMARK 465 GLU B 152
REMARK 465 ALA B 169
REMARK 465 GLU B 170
REMARK 465 GLU B 171
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 LYS C 61
REMARK 465 GLU C 62
REMARK 465 HIS C 63
REMARK 465 TRP C 64
REMARK 465 THR C 65
REMARK 465 SER C 149
REMARK 465 SER C 150
REMARK 465 GLU C 151
REMARK 465 GLU C 152
REMARK 465 GLU C 170
REMARK 465 GLU C 171
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 SER D 149
REMARK 465 SER D 150
REMARK 465 GLU D 151
REMARK 465 GLU D 152
REMARK 465 ALA D 168
REMARK 465 ALA D 169
REMARK 465 GLU D 170
REMARK 465 GLU D 171
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 31 1.36 -67.98
REMARK 500 ARG A 121 34.08 71.11
REMARK 500 GLU C 67 -34.56 178.27
REMARK 500 PRO C 83 -9.10 -59.36
REMARK 500 MET D 30 51.67 174.39
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 SPM C 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 400
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B 401
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA C 402
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BJ7 RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH COENZYME A
DBREF 3BJ8 A 1 171 UNP P48026 SAT1_MOUSE 1 171
DBREF 3BJ8 B 1 171 UNP P48026 SAT1_MOUSE 1 171
DBREF 3BJ8 C 1 171 UNP P48026 SAT1_MOUSE 1 171
DBREF 3BJ8 D 1 171 UNP P48026 SAT1_MOUSE 1 171
SEQRES 1 A 171 MET ALA LYS PHE LYS ILE ARG PRO ALA THR ALA SER ASP
SEQRES 2 A 171 CYS SER ASP ILE LEU ARG LEU ILE LYS GLU LEU ALA LYS
SEQRES 3 A 171 TYR GLU TYR MET GLU ASP GLN VAL ILE LEU THR GLU LYS
SEQRES 4 A 171 ASP LEU GLN GLU ASP GLY PHE GLY GLU HIS PRO PHE TYR
SEQRES 5 A 171 HIS CYS LEU VAL ALA GLU VAL PRO LYS GLU HIS TRP THR
SEQRES 6 A 171 PRO GLU GLY HIS SER ILE VAL GLY PHE ALA MET TYR TYR
SEQRES 7 A 171 PHE THR TYR ASP PRO TRP ILE GLY LYS LEU LEU TYR LEU
SEQRES 8 A 171 GLU ASP PHE PHE VAL MET SER ASP TYR ARG GLY PHE GLY
SEQRES 9 A 171 ILE GLY SER GLU ILE LEU LYS ASN LEU SER GLN VAL ALA
SEQRES 10 A 171 MET LYS CYS ARG CYS SER SER MET HIS PHE LEU VAL ALA
SEQRES 11 A 171 GLU TRP ASN GLU PRO SER ILE ASN PHE TYR LYS ARG ARG
SEQRES 12 A 171 GLY ALA SER ASP LEU SER SER GLU GLU GLY TRP ARG LEU
SEQRES 13 A 171 PHE LYS ILE ASP LYS GLU TYR LEU LEU LYS MET ALA ALA
SEQRES 14 A 171 GLU GLU
SEQRES 1 B 171 MET ALA LYS PHE LYS ILE ARG PRO ALA THR ALA SER ASP
SEQRES 2 B 171 CYS SER ASP ILE LEU ARG LEU ILE LYS GLU LEU ALA LYS
SEQRES 3 B 171 TYR GLU TYR MET GLU ASP GLN VAL ILE LEU THR GLU LYS
SEQRES 4 B 171 ASP LEU GLN GLU ASP GLY PHE GLY GLU HIS PRO PHE TYR
SEQRES 5 B 171 HIS CYS LEU VAL ALA GLU VAL PRO LYS GLU HIS TRP THR
SEQRES 6 B 171 PRO GLU GLY HIS SER ILE VAL GLY PHE ALA MET TYR TYR
SEQRES 7 B 171 PHE THR TYR ASP PRO TRP ILE GLY LYS LEU LEU TYR LEU
SEQRES 8 B 171 GLU ASP PHE PHE VAL MET SER ASP TYR ARG GLY PHE GLY
SEQRES 9 B 171 ILE GLY SER GLU ILE LEU LYS ASN LEU SER GLN VAL ALA
SEQRES 10 B 171 MET LYS CYS ARG CYS SER SER MET HIS PHE LEU VAL ALA
SEQRES 11 B 171 GLU TRP ASN GLU PRO SER ILE ASN PHE TYR LYS ARG ARG
SEQRES 12 B 171 GLY ALA SER ASP LEU SER SER GLU GLU GLY TRP ARG LEU
SEQRES 13 B 171 PHE LYS ILE ASP LYS GLU TYR LEU LEU LYS MET ALA ALA
SEQRES 14 B 171 GLU GLU
SEQRES 1 C 171 MET ALA LYS PHE LYS ILE ARG PRO ALA THR ALA SER ASP
SEQRES 2 C 171 CYS SER ASP ILE LEU ARG LEU ILE LYS GLU LEU ALA LYS
SEQRES 3 C 171 TYR GLU TYR MET GLU ASP GLN VAL ILE LEU THR GLU LYS
SEQRES 4 C 171 ASP LEU GLN GLU ASP GLY PHE GLY GLU HIS PRO PHE TYR
SEQRES 5 C 171 HIS CYS LEU VAL ALA GLU VAL PRO LYS GLU HIS TRP THR
SEQRES 6 C 171 PRO GLU GLY HIS SER ILE VAL GLY PHE ALA MET TYR TYR
SEQRES 7 C 171 PHE THR TYR ASP PRO TRP ILE GLY LYS LEU LEU TYR LEU
SEQRES 8 C 171 GLU ASP PHE PHE VAL MET SER ASP TYR ARG GLY PHE GLY
SEQRES 9 C 171 ILE GLY SER GLU ILE LEU LYS ASN LEU SER GLN VAL ALA
SEQRES 10 C 171 MET LYS CYS ARG CYS SER SER MET HIS PHE LEU VAL ALA
SEQRES 11 C 171 GLU TRP ASN GLU PRO SER ILE ASN PHE TYR LYS ARG ARG
SEQRES 12 C 171 GLY ALA SER ASP LEU SER SER GLU GLU GLY TRP ARG LEU
SEQRES 13 C 171 PHE LYS ILE ASP LYS GLU TYR LEU LEU LYS MET ALA ALA
SEQRES 14 C 171 GLU GLU
SEQRES 1 D 171 MET ALA LYS PHE LYS ILE ARG PRO ALA THR ALA SER ASP
SEQRES 2 D 171 CYS SER ASP ILE LEU ARG LEU ILE LYS GLU LEU ALA LYS
SEQRES 3 D 171 TYR GLU TYR MET GLU ASP GLN VAL ILE LEU THR GLU LYS
SEQRES 4 D 171 ASP LEU GLN GLU ASP GLY PHE GLY GLU HIS PRO PHE TYR
SEQRES 5 D 171 HIS CYS LEU VAL ALA GLU VAL PRO LYS GLU HIS TRP THR
SEQRES 6 D 171 PRO GLU GLY HIS SER ILE VAL GLY PHE ALA MET TYR TYR
SEQRES 7 D 171 PHE THR TYR ASP PRO TRP ILE GLY LYS LEU LEU TYR LEU
SEQRES 8 D 171 GLU ASP PHE PHE VAL MET SER ASP TYR ARG GLY PHE GLY
SEQRES 9 D 171 ILE GLY SER GLU ILE LEU LYS ASN LEU SER GLN VAL ALA
SEQRES 10 D 171 MET LYS CYS ARG CYS SER SER MET HIS PHE LEU VAL ALA
SEQRES 11 D 171 GLU TRP ASN GLU PRO SER ILE ASN PHE TYR LYS ARG ARG
SEQRES 12 D 171 GLY ALA SER ASP LEU SER SER GLU GLU GLY TRP ARG LEU
SEQRES 13 D 171 PHE LYS ILE ASP LYS GLU TYR LEU LEU LYS MET ALA ALA
SEQRES 14 D 171 GLU GLU
HET SPM C 500 14
HET COA A 400 48
HET COA B 401 48
HET COA C 402 48
HET COA D 403 48
HETNAM SPM SPERMINE
HETNAM COA COENZYME A
FORMUL 5 SPM C10 H26 N4
FORMUL 6 COA 4(C21 H36 N7 O16 P3 S)
FORMUL 10 HOH *213(H2 O)
HELIX 1 1 THR A 10 SER A 12 5 3
HELIX 2 2 ASP A 13 TYR A 27 1 15
HELIX 3 3 THR A 37 GLY A 47 1 11
HELIX 4 4 PRO A 60 TRP A 64 5 5
HELIX 5 5 SER A 98 ARG A 101 5 4
HELIX 6 6 GLY A 104 ARG A 121 1 18
HELIX 7 7 ASN A 133 ARG A 142 1 10
HELIX 8 8 LYS A 161 ALA A 169 1 9
HELIX 9 9 THR B 10 SER B 12 5 3
HELIX 10 10 ASP B 13 ALA B 25 1 13
HELIX 11 11 MET B 30 VAL B 34 5 5
HELIX 12 12 THR B 37 PHE B 46 1 10
HELIX 13 13 PRO B 60 TRP B 64 5 5
HELIX 14 14 SER B 98 ARG B 101 5 4
HELIX 15 15 GLY B 104 ARG B 121 1 18
HELIX 16 16 ASN B 133 ARG B 142 1 10
HELIX 17 17 LYS B 161 ALA B 168 1 8
HELIX 18 18 THR C 10 SER C 12 5 3
HELIX 19 19 ASP C 13 GLU C 28 1 16
HELIX 20 20 TYR C 29 VAL C 34 5 6
HELIX 21 21 THR C 37 GLY C 47 1 11
HELIX 22 22 SER C 98 ARG C 101 5 4
HELIX 23 23 GLY C 104 ARG C 121 1 18
HELIX 24 24 ASN C 133 ARG C 142 1 10
HELIX 25 25 LYS C 161 ALA C 169 1 9
HELIX 26 26 THR D 10 SER D 12 5 3
HELIX 27 27 ASP D 13 GLU D 28 1 16
HELIX 28 28 TYR D 29 VAL D 34 5 6
HELIX 29 29 THR D 37 PHE D 46 1 10
HELIX 30 30 PRO D 60 TRP D 64 5 5
HELIX 31 31 SER D 98 ARG D 101 5 4
HELIX 32 32 GLY D 104 CYS D 120 1 17
HELIX 33 33 ASN D 133 ARG D 142 1 10
HELIX 34 34 LYS D 161 MET D 167 1 7
SHEET 1 A 7 LYS A 5 PRO A 8 0
SHEET 2 A 7 HIS A 53 GLU A 58 -1 O GLU A 58 N LYS A 5
SHEET 3 A 7 ILE A 71 ASP A 82 -1 O TYR A 77 N HIS A 53
SHEET 4 A 7 GLY A 86 VAL A 96 -1 O GLY A 86 N ASP A 82
SHEET 5 A 7 SER A 124 ALA A 130 1 O HIS A 126 N LEU A 91
SHEET 6 A 7 TRP B 154 ASP B 160 -1 O ARG B 155 N VAL A 129
SHEET 7 A 7 SER A 146 ASP A 147 -1 N SER A 146 O LYS B 158
SHEET 1 B 7 LYS B 5 PRO B 8 0
SHEET 2 B 7 HIS B 53 GLU B 58 -1 O VAL B 56 N ARG B 7
SHEET 3 B 7 ILE B 71 ASP B 82 -1 O TYR B 77 N HIS B 53
SHEET 4 B 7 GLY B 86 VAL B 96 -1 O TYR B 90 N TYR B 78
SHEET 5 B 7 SER B 124 ALA B 130 1 O HIS B 126 N LEU B 91
SHEET 6 B 7 TRP A 154 ASP A 160 -1 N PHE A 157 O PHE B 127
SHEET 7 B 7 SER B 146 ASP B 147 -1 O SER B 146 N LYS A 158
SHEET 1 C 7 LYS C 5 PRO C 8 0
SHEET 2 C 7 HIS C 53 GLU C 58 -1 O GLU C 58 N LYS C 5
SHEET 3 C 7 ILE C 71 ASP C 82 -1 O TYR C 77 N HIS C 53
SHEET 4 C 7 GLY C 86 VAL C 96 -1 O ASP C 93 N MET C 76
SHEET 5 C 7 SER C 124 ALA C 130 1 O HIS C 126 N LEU C 91
SHEET 6 C 7 TRP D 154 ASP D 160 -1 O ARG D 155 N VAL C 129
SHEET 7 C 7 SER C 146 ASP C 147 -1 N SER C 146 O LYS D 158
SHEET 1 D 7 LYS D 5 PRO D 8 0
SHEET 2 D 7 HIS D 53 GLU D 58 -1 O VAL D 56 N ARG D 7
SHEET 3 D 7 ILE D 71 ASP D 82 -1 O TYR D 77 N HIS D 53
SHEET 4 D 7 GLY D 86 VAL D 96 -1 O ASP D 93 N MET D 76
SHEET 5 D 7 SER D 124 ALA D 130 1 O SER D 124 N LEU D 89
SHEET 6 D 7 TRP C 154 ASP C 160 -1 N PHE C 157 O PHE D 127
SHEET 7 D 7 SER D 146 ASP D 147 -1 O SER D 146 N LYS C 158
SSBOND 1 CYS A 120 CYS A 122 1555 1555 2.04
SSBOND 2 CYS B 120 CYS B 122 1555 1555 2.04
SITE 1 AC1 4 ASP C 93 LEU C 128 ASP D 82 HIS D 126
SITE 1 AC2 11 PHE A 94 PHE A 95 ARG A 101 GLY A 102
SITE 2 AC2 11 PHE A 103 GLY A 104 GLY A 106 SER A 107
SITE 3 AC2 11 PHE A 139 ARG A 142 ARG A 143
SITE 1 AC3 14 PHE B 94 ARG B 101 GLY B 102 PHE B 103
SITE 2 AC3 14 GLY B 104 GLY B 106 SER B 107 PRO B 135
SITE 3 AC3 14 PHE B 139 ARG B 142 ARG B 143 PRO C 135
SITE 4 AC3 14 ASN C 138 PHE C 139
SITE 1 AC4 11 SER B 98 ARG B 101 ARG C 101 GLY C 102
SITE 2 AC4 11 PHE C 103 GLY C 104 GLY C 106 SER C 107
SITE 3 AC4 11 PRO C 135 PHE C 139 ARG C 143
SITE 1 AC5 14 TYR A 27 SER A 98 TYR D 27 PHE D 94
SITE 2 AC5 14 PHE D 95 ARG D 101 GLY D 102 PHE D 103
SITE 3 AC5 14 GLY D 104 GLY D 106 SER D 107 PHE D 139
SITE 4 AC5 14 ARG D 142 ARG D 143
CRYST1 77.250 97.120 105.500 90.00 90.00 90.00 P 21 21 21 16
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 0.012945 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010297 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009479 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
