HEADER TRANSFERASE 27-SEP-05 2B58
TITLE SSAT WITH COA_SP, SPERMINE DISORDERED, K26R MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIAMINE ACETYLTRANSFERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SPERMIDINE/SPERMINE N1, - ACETYLTRANSFERASE 1, SSAT, SSAT-1,
COMPND 5 PUTRESCINE ACETYLTRANSFERASE, POLYAMINE N-ACETYLTRANSFERASE 1;
COMPND 6 EC: 2.3.1.57;
COMPND 7 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: SAT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET13A
KEYWDS STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX
KEYWDS 2 RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.C.BEWLEY,V.GRAZIANO,J.S.JIANG,E.MATZ,F.W.STUDIER,A.P.PEGG,
AUTHOR 2 C.S.COLEMAN,J.M.FLANAGAN,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER FOR
AUTHOR 3 STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 6 03-FEB-21 2B58 1 AUTHOR REMARK SEQADV LINK
REVDAT 5 13-JUL-11 2B58 1 VERSN
REVDAT 4 26-JAN-11 2B58 1 AUTHOR
REVDAT 3 24-FEB-09 2B58 1 VERSN
REVDAT 2 07-MAR-06 2B58 1 JRNL
REVDAT 1 24-JAN-06 2B58 0
JRNL AUTH M.C.BEWLEY,V.GRAZIANO,J.S.JIANG,E.MATZ,F.W.STUDIER,A.P.PEGG,
JRNL AUTH 2 C.S.COLEMAN,J.M.FLANAGAN
JRNL TITL STRUCTURES OF WILD-TYPE AND MUTANT HUMAN SPERMIDINE/SPERMINE
JRNL TITL 2 N1-ACETYLTRANSFERASE, A POTENTIAL THERAPEUTIC DRUG TARGET
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 2063 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16455797
JRNL DOI 10.1073/PNAS.0511008103
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000
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 : 13228
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) : 0.204
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 658
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 : 1380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 82
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 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 2B58 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034690.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
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) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13228
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
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: SAD
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 (%): 46.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.08600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.04300
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 54.08600
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 27.04300
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 109.55048
REMARK 350 BIOMT3 2 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 MSE A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 GLU A 171
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 198 O HOH A 198 4675 1.15
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 MSE A 118 CG - SE - CE ANGL. DEV. = 15.6 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 MSE A 30 33.00 -146.81
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 90 0.08 SIDE CHAIN
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 COA A 172
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2B3U RELATED DB: PDB
REMARK 900 RELATED ID: 2B3V RELATED DB: PDB
REMARK 900 RELATED ID: 2B47 RELATED DB: PDB
REMARK 900 RELATED ID: 2B4B RELATED DB: PDB
REMARK 900 RELATED ID: 2B4D RELATED DB: PDB
REMARK 900 RELATED ID: 2B5G RELATED DB: PDB
REMARK 900 RELATED ID: NYSGXRC-9502A RELATED DB: TARGETDB
DBREF 2B58 A 1 171 UNP P21673 SAT1_HUMAN 1 171
SEQADV 2B58 ARG A 26 UNP P21673 LYS 26 ENGINEERED MUTATION
SEQRES 1 A 171 MSE ALA LYS PHE VAL ILE ARG PRO ALA THR ALA ALA ASP
SEQRES 2 A 171 CYS SER ASP ILE LEU ARG LEU ILE LYS GLU LEU ALA ARG
SEQRES 3 A 171 TYR GLU TYR MSE GLU GLU GLN VAL ILE LEU THR GLU LYS
SEQRES 4 A 171 ASP LEU LEU 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 MSE 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 MSE 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 MSE ARG CYS ARG CYS SER SER MSE 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 MSE ALA THR
SEQRES 14 A 171 GLU GLU
MODRES 2B58 MSE A 30 MET SELENOMETHIONINE
MODRES 2B58 MSE A 76 MET SELENOMETHIONINE
MODRES 2B58 MSE A 97 MET SELENOMETHIONINE
MODRES 2B58 MSE A 118 MET SELENOMETHIONINE
MODRES 2B58 MSE A 125 MET SELENOMETHIONINE
MODRES 2B58 MSE A 167 MET SELENOMETHIONINE
HET MSE A 30 8
HET MSE A 76 8
HET MSE A 97 8
HET MSE A 118 8
HET MSE A 125 8
HET MSE A 167 8
HET COA A 172 48
HETNAM MSE SELENOMETHIONINE
HETNAM COA COENZYME A
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 COA C21 H36 N7 O16 P3 S
FORMUL 3 HOH *82(H2 O)
HELIX 1 1 THR A 10 ALA A 12 5 3
HELIX 2 2 ASP A 13 GLU A 28 1 16
HELIX 3 3 MSE A 30 VAL A 34 5 5
HELIX 4 4 THR A 37 GLY A 47 1 11
HELIX 5 5 PRO A 60 TRP A 64 5 5
HELIX 6 6 SER A 98 ARG A 101 5 4
HELIX 7 7 GLY A 104 CYS A 120 1 17
HELIX 8 8 ASN A 133 ARG A 143 1 11
HELIX 9 9 ASP A 160 GLU A 170 1 11
SHEET 1 A 5 VAL A 5 PRO A 8 0
SHEET 2 A 5 HIS A 53 GLU A 58 -1 O VAL A 56 N ARG A 7
SHEET 3 A 5 ILE A 71 ASP A 82 -1 O VAL A 72 N ALA A 57
SHEET 4 A 5 GLY A 86 VAL A 96 -1 O GLY A 86 N ASP A 82
SHEET 5 A 5 SER A 124 HIS A 126 1 O HIS A 126 N LEU A 91
LINK C TYR A 29 N MSE A 30 1555 1555 1.33
LINK C MSE A 30 N GLU A 31 1555 1555 1.33
LINK C ALA A 75 N MSE A 76 1555 1555 1.33
LINK C MSE A 76 N TYR A 77 1555 1555 1.33
LINK C VAL A 96 N MSE A 97 1555 1555 1.33
LINK C MSE A 97 N SER A 98 1555 1555 1.34
LINK C ALA A 117 N MSE A 118 1555 1555 1.33
LINK C MSE A 118 N ARG A 119 1555 1555 1.32
LINK C SER A 124 N MSE A 125 1555 1555 1.33
LINK C MSE A 125 N HIS A 126 1555 1555 1.33
LINK C LYS A 166 N MSE A 167 1555 1555 1.34
LINK C MSE A 167 N ALA A 168 1555 1555 1.33
SITE 1 AC1 21 GLU A 28 PHE A 94 PHE A 95 VAL A 96
SITE 2 AC1 21 ARG A 101 GLY A 102 PHE A 103 GLY A 104
SITE 3 AC1 21 ILE A 105 GLY A 106 SER A 107 ASN A 133
SITE 4 AC1 21 SER A 136 PHE A 139 ARG A 142 ARG A 143
SITE 5 AC1 21 HOH A 173 HOH A 187 HOH A 204 HOH A 222
SITE 6 AC1 21 HOH A 223
CRYST1 63.249 63.249 81.129 90.00 90.00 120.00 P 62 6
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 0.015811 0.009128 0.000000 0.00000
SCALE2 0.000000 0.018256 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012326 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
