HEADER LYASE 04-AUG-04 1U83
TITLE PSL SYNTHASE FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOSULFOLACTATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: (2R)-PHOSPHO-3-SULFOLACTATE SYNTHASE, PSL SYNTHASE;
COMPND 5 EC: 4.4.1.19;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: COMA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS BACILLUS SUBTILIS, STRUCTURAL GENOMICS, PHOSPHOSULFOLACTATE SYNTHASE,
KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.CUFF,X.XU,A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 6 11-OCT-17 1U83 1 REMARK
REVDAT 5 26-SEP-12 1U83 1 AUTHOR
REVDAT 4 13-JUL-11 1U83 1 VERSN
REVDAT 3 24-FEB-09 1U83 1 VERSN
REVDAT 2 18-JAN-05 1U83 1 AUTHOR KEYWDS REMARK
REVDAT 1 14-SEP-04 1U83 0
JRNL AUTH M.E.CUFF,X.XU,A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK
JRNL TITL PSL SYNTHASE FROM BACILLUS SUBTILIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.04
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 : 13466
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) : 0.188
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 671
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1591
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 70
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1809
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 176
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
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 : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 66.77
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 : GOL.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : GOL.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023363.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 150
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945, 0.97921
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : SBC2
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13466
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 46.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.56300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.170
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM PHOSPHATE, BIS-TRIS, ETHYLENE
REMARK 280 GLYCOL, GLYCEROL, PH 7.0, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
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 46.03550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.03550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.03550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.03550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.03550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.03550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 46.03550
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 46.03550
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 46.03550
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 46.03550
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 46.03550
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 46.03550
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 46.03550
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 46.03550
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 46.03550
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 46.03550
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 46.03550
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 46.03550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE:
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN. THE BIOLOGICAL UNIT IS UNKNOWN.
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 10490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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 0.000000 0.000000 1.000000 -46.03550
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 46.03550
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 92.07100
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 46.03550
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 92.07100
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 46.03550
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 A1132 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 MSE A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 ARG A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 141
REMARK 465 GLU A 142
REMARK 465 LEU A 143
REMARK 465 ALA A 144
REMARK 465 SER A 145
REMARK 465 ARG A 146
REMARK 465 ALA A 171
REMARK 465 ARG A 172
REMARK 465 GLU A 173
REMARK 465 SER A 174
REMARK 465 GLY A 175
REMARK 465 THR A 176
REMARK 465 GLY A 177
REMARK 465 GLY A 178
REMARK 465 ILE A 179
REMARK 465 CYS A 180
REMARK 465 SER A 181
REMARK 465 SER A 182
REMARK 465 SER A 183
REMARK 465 GLY A 184
REMARK 465 ASP A 185
REMARK 465 VAL A 186
REMARK 465 ARG A 187
REMARK 465 PHE A 188
REMARK 465 LEU A 252
REMARK 465 GLY A 253
REMARK 465 SER A 254
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 TRP A 51 -120.35 26.86
REMARK 500 ASN A 109 38.41 -141.14
REMARK 500 THR A 111 -55.54 -122.58
REMARK 500 PRO A 113 108.84 -58.83
REMARK 500 SER A 149 -123.25 -87.43
REMARK 500 SER A 196 59.33 -67.95
REMARK 500 ASP A 198 2.49 80.91
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 PO4 A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1112
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC1199 RELATED DB: TARGETDB
DBREF 1U83 A 1 252 UNP O06739 COMA_BACSU 1 252
SEQADV 1U83 MSE A -21 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 GLY A -20 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 SER A -19 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 SER A -18 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 HIS A -17 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 HIS A -16 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 HIS A -15 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 HIS A -14 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 HIS A -13 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 HIS A -12 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 SER A -11 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 SER A -10 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 GLY A -9 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 ARG A -8 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 GLU A -7 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 ASN A -6 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 LEU A -5 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 TYR A -4 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 PHE A -3 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 GLN A -2 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 GLY A -1 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 HIS A 0 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 MSE A 1 UNP O06739 MET 1 MODIFIED RESIDUE
SEQADV 1U83 MSE A 114 UNP O06739 MET 114 MODIFIED RESIDUE
SEQADV 1U83 MSE A 160 UNP O06739 MET 160 MODIFIED RESIDUE
SEQADV 1U83 GLY A 253 UNP O06739 CLONING ARTIFACT
SEQADV 1U83 SER A 254 UNP O06739 CLONING ARTIFACT
SEQRES 1 A 276 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 276 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE ASN ASP PHE
SEQRES 3 A 276 SER LEU GLU LEU PRO VAL ARG THR ASN LYS PRO ARG GLU
SEQRES 4 A 276 THR GLY GLN SER ILE LEU ILE ASP ASN GLY TYR PRO LEU
SEQRES 5 A 276 GLN PHE PHE LYS ASP ALA ILE ALA GLY ALA SER ASP TYR
SEQRES 6 A 276 ILE ASP PHE VAL LYS PHE GLY TRP GLY THR SER LEU LEU
SEQRES 7 A 276 THR LYS ASP LEU GLU GLU LYS ILE SER THR LEU LYS GLU
SEQRES 8 A 276 HIS ASP ILE THR PHE PHE PHE GLY GLY THR LEU PHE GLU
SEQRES 9 A 276 LYS TYR VAL SER GLN LYS LYS VAL ASN GLU PHE HIS ARG
SEQRES 10 A 276 TYR CYS THR TYR PHE GLY CYS GLU TYR ILE GLU ILE SER
SEQRES 11 A 276 ASN GLY THR LEU PRO MSE THR ASN LYS GLU LYS ALA ALA
SEQRES 12 A 276 TYR ILE ALA ASP PHE SER ASP GLU PHE LEU VAL LEU SER
SEQRES 13 A 276 GLU VAL GLY SER LYS ASP ALA GLU LEU ALA SER ARG GLN
SEQRES 14 A 276 SER SER GLU GLU TRP LEU GLU TYR ILE VAL GLU ASP MSE
SEQRES 15 A 276 GLU ALA GLY ALA GLU LYS VAL ILE THR GLU ALA ARG GLU
SEQRES 16 A 276 SER GLY THR GLY GLY ILE CYS SER SER SER GLY ASP VAL
SEQRES 17 A 276 ARG PHE GLN ILE VAL ASP ASP ILE ILE SER SER ASP ILE
SEQRES 18 A 276 ASP ILE ASN ARG LEU ILE PHE GLU ALA PRO ASN LYS THR
SEQRES 19 A 276 LEU GLN GLN GLY PHE ILE GLN LYS ILE GLY PRO ASN VAL
SEQRES 20 A 276 ASN LEU ALA ASN ILE PRO PHE HIS ASP ALA ILE ALA LEU
SEQRES 21 A 276 GLU THR LEU ARG LEU GLY LEU ARG SER ASP THR PHE PHE
SEQRES 22 A 276 LEU GLY SER
MODRES 1U83 MSE A 114 MET SELENOMETHIONINE
MODRES 1U83 MSE A 160 MET SELENOMETHIONINE
HET MSE A 114 8
HET MSE A 160 8
HET PO4 A1000 5
HET PO4 A1001 5
HET GOL A1110 6
HET GOL A1111 6
HET GOL A1112 6
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 7 HOH *176(H2 O)
HELIX 1 1 PRO A 29 SER A 41 1 13
HELIX 2 2 ASP A 42 ILE A 44 5 3
HELIX 3 3 GLY A 52 THR A 57 5 6
HELIX 4 4 ASP A 59 HIS A 70 1 12
HELIX 5 5 GLY A 77 GLN A 87 1 11
HELIX 6 6 LYS A 89 PHE A 100 1 12
HELIX 7 7 THR A 115 SER A 127 1 13
HELIX 8 8 GLU A 150 GLY A 163 1 14
HELIX 9 9 ILE A 190 SER A 196 1 7
HELIX 10 10 ASP A 200 ASN A 202 5 3
HELIX 11 11 ASN A 210 GLY A 222 1 13
HELIX 12 12 ASP A 234 LEU A 243 1 10
HELIX 13 13 ARG A 246 PHE A 250 5 5
SHEET 1 A 8 THR A 73 PHE A 76 0
SHEET 2 A 8 PHE A 46 PHE A 49 1 N PHE A 49 O PHE A 75
SHEET 3 A 8 SER A 21 ASP A 25 1 N LEU A 23 O LYS A 48
SHEET 4 A 8 LEU A 227 PRO A 231 1 O LEU A 227 N ILE A 22
SHEET 5 A 8 LEU A 204 GLU A 207 1 N PHE A 206 O ALA A 228
SHEET 6 A 8 ALA A 164 THR A 169 1 N THR A 169 O ILE A 205
SHEET 7 A 8 LEU A 131 GLU A 135 1 N SER A 134 O ILE A 168
SHEET 8 A 8 TYR A 104 ILE A 107 1 N ILE A 105 O LEU A 133
LINK C PRO A 113 N MSE A 114 1555 1555 1.32
LINK C MSE A 114 N THR A 115 1555 1555 1.33
LINK C ASP A 159 N MSE A 160 1555 1555 1.33
LINK C MSE A 160 N GLU A 161 1555 1555 1.33
CISPEP 1 LYS A 14 PRO A 15 0 -0.25
SITE 1 AC1 10 LYS A 48 TRP A 51 GLY A 77 GLY A 78
SITE 2 AC1 10 THR A 79 GLU A 106 LYS A 139 GOL A1110
SITE 3 AC1 10 HOH A1223 HOH A1278
SITE 1 AC2 9 ASN A 210 LYS A 211 HIS A 233 ASP A 234
SITE 2 AC2 9 HOH A1120 HOH A1174 HOH A1211 HOH A1232
SITE 3 AC2 9 HOH A1273
SITE 1 AC3 8 ILE A 24 LYS A 48 GLU A 135 LYS A 139
SITE 2 AC3 8 GLU A 207 ASN A 229 PO4 A1000 HOH A1204
SITE 1 AC4 4 SER A 5 LEU A 6 HOH A1208 HOH A1247
SITE 1 AC5 9 ARG A 16 GLU A 17 GLN A 20 ASP A 45
SITE 2 AC5 9 PHE A 46 THR A 73 TYR A 104 HOH A1136
SITE 3 AC5 9 HOH A1222
CRYST1 92.071 92.071 92.071 90.00 90.00 90.00 P 21 3 12
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 0.010861 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010861 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010861 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
