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HEADER HYDROLASE 12-MAY-08 3D3N
TITLE CRYSTAL STRUCTURE OF LIPASE/ESTERASE (LP_2923) FROM
TITLE 2 LACTOBACILLUS PLANTARUM. NORTHEAST STRUCTURAL GENOMICS
TITLE 3 CONSORTIUM TARGET LPR108
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE LIPASE/ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM WCFS1;
SOURCE 3 STRAIN: WCFS1 / NCIMB 8826;
SOURCE 4 ATCC: BAA-793;
SOURCE 5 GENE: LP_2923, AES;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, NESG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,M.SU,J.SEETHARAMAN,L.MAO,H.JANJUA,R.XIAO,
AUTHOR 2 C.CICCOSANTI,M.MAGLAQUI,E.L.FOOTE,L.ZHAO,J.K.EVERETT,
AUTHOR 3 T.B.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST
AUTHOR 4 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 1 10-JUN-08 3D3N 0
JRNL AUTH F.FOROUHAR,M.SU,J.SEETHARAMAN,L.MAO,H.JANJUA,
JRNL AUTH 2 R.XIAO,C.CICCOSANTI,M.MAGLAQUI,E.L.FOOTE,L.ZHAO,
JRNL AUTH 3 J.K.EVERETT,T.B.ACTON,G.T.MONTELIONE,L.TONG,
JRNL AUTH 4 J.F.HUNT
JRNL TITL CRYSTAL STRUCTURE OF LIPASE/ESTERASE (LP_2923)
JRNL TITL 2 FROM LACTOBACILLUS PLANTARUM. NORTHEAST STRUCTURAL
JRNL TITL 3 GENOMICS CONSORTIUM TARGET LPR108
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 425997.160
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 66.1
REMARK 3 NUMBER OF REFLECTIONS : 26057
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) : 0.216
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2556
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 44.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1597
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 158
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3896
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.04000
REMARK 3 B22 (A**2) : 12.83000
REMARK 3 B33 (A**2) : -6.78000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.77
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 37.76
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: THE FRIEDEL PAIRS WERE USED IN
REMARK 3 PHASING. PROGRAM XTALVIEW HAS ALSO BEEN USED IN REFINEMENT
REMARK 4
REMARK 4 3D3N COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB047550.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97900
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38826
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : 0.07000
REMARK 200 FOR THE DATA SET : 11.5300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.42600
REMARK 200 R SYM FOR SHELL (I) : 0.29200
REMARK 200 FOR SHELL : 2.210
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: BNP, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.5, 5% PEG 8000,
REMARK 280 100MM CALCIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 33.03700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.88250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.51100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.88250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.03700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.51100
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: 1800 ANGSTROM**2
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 20360 ANGSTROM**2
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -10 KCAL/MOL
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 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 PHE A 28
REMARK 465 GLU A 29
REMARK 465 THR A 30
REMARK 465 GLY A 231
REMARK 465 ILE A 232
REMARK 465 HIS A 233
REMARK 465 GLY A 234
REMARK 465 LEU A 235
REMARK 465 ALA A 236
REMARK 465 LEU A 237
REMARK 465 ALA A 238
REMARK 465 ASN A 239
REMARK 465 HIS A 240
REMARK 465 VAL A 241
REMARK 465 THR A 242
REMARK 465 GLN A 243
REMARK 465 LYS A 244
REMARK 465 PRO A 245
REMARK 465 GLY A 246
REMARK 465 LYS A 247
REMARK 465 ASP A 248
REMARK 465 LYS A 249
REMARK 465 TYR A 250
REMARK 465 LEU A 251
REMARK 465 ASN A 252
REMARK 465 ASP A 253
REMARK 465 GLN A 254
REMARK 465 ALA A 255
REMARK 465 GLY A 274
REMARK 465 ASN A 275
REMARK 465 TYR A 276
REMARK 465 LEU A 277
REMARK 465 GLU A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 THR B 30
REMARK 465 GLY B 234
REMARK 465 LEU B 235
REMARK 465 ALA B 236
REMARK 465 LEU B 237
REMARK 465 ALA B 238
REMARK 465 ASN B 239
REMARK 465 HIS B 240
REMARK 465 VAL B 241
REMARK 465 THR B 242
REMARK 465 GLN B 243
REMARK 465 LYS B 244
REMARK 465 PRO B 245
REMARK 465 GLY B 246
REMARK 465 LYS B 247
REMARK 465 ASP B 248
REMARK 465 LYS B 249
REMARK 465 GLN B 254
REMARK 465 ALA B 255
REMARK 465 GLY B 274
REMARK 465 ASN B 275
REMARK 465 TYR B 276
REMARK 465 LEU B 277
REMARK 465 GLU B 278
REMARK 465 HIS B 279
REMARK 465 HIS B 280
REMARK 465 HIS B 281
REMARK 465 HIS B 282
REMARK 465 HIS B 283
REMARK 465 HIS B 284
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 230 CB SER A 230 OG 0.083
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 PHE A 45 16.76 59.11
REMARK 500 SER A 116 -121.34 50.62
REMARK 500 HIS A 139 76.05 50.96
REMARK 500 TYR A 154 56.51 31.57
REMARK 500 LEU A 159 23.23 -76.32
REMARK 500 THR A 174 141.65 -175.01
REMARK 500 ARG A 184 26.04 -75.33
REMARK 500 ALA B 11 25.51 47.58
REMARK 500 ILE B 25 -81.35 -64.36
REMARK 500 VAL B 76 152.96 -42.57
REMARK 500 SER B 116 -125.39 51.56
REMARK 500 TYR B 154 54.16 34.41
REMARK 500 THR B 174 134.33 -179.00
REMARK 500 GLN B 197 157.32 178.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 323 DISTANCE = 5.65 ANGSTROMS
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 CA B 285 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 33 OD1
REMARK 620 2 ASP B 33 OD2 46.8
REMARK 620 3 HOH B 348 O 84.3 71.1
REMARK 620 4 HOH B 346 O 78.8 82.5 153.6
REMARK 620 5 HOH B 317 O 73.5 120.3 106.8 87.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR RESIDUE B 285
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: EPE BINDING SITE FOR RESIDUE A 285
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: EPE BINDING SITE FOR RESIDUE B 286
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: LPR108 RELATED DB: TARGETDB
DBREF 3D3N A 1 276 UNP Q88TL9 Q88TL9_LACPL 1 276
DBREF 3D3N B 1 276 UNP Q88TL9 Q88TL9_LACPL 1 276
SEQADV 3D3N LEU A 277 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N GLU A 278 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS A 279 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS A 280 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS A 281 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS A 282 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS A 283 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS A 284 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N LEU B 277 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N GLU B 278 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS B 279 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS B 280 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS B 281 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS B 282 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS B 283 UNP Q88TL9 EXPRESSION TAG
SEQADV 3D3N HIS B 284 UNP Q88TL9 EXPRESSION TAG
SEQRES 1 A 284 MSE GLN VAL GLU GLN ARG THR LEU ASN THR ALA ALA HIS
SEQRES 2 A 284 PRO PHE GLN ILE THR ALA TYR TRP LEU ASP GLN ILE SER
SEQRES 3 A 284 ASP PHE GLU THR ALA VAL ASP TYR PRO ILE MSE ILE ILE
SEQRES 4 A 284 CYS PRO GLY GLY GLY PHE THR TYR HIS SER GLY ARG GLU
SEQRES 5 A 284 GLU ALA PRO ILE ALA THR ARG MSE MSE ALA ALA GLY MSE
SEQRES 6 A 284 HIS THR VAL VAL LEU ASN TYR GLN LEU ILE VAL GLY ASP
SEQRES 7 A 284 GLN SER VAL TYR PRO TRP ALA LEU GLN GLN LEU GLY ALA
SEQRES 8 A 284 THR ILE ASP TRP ILE THR THR GLN ALA SER ALA HIS HIS
SEQRES 9 A 284 VAL ASP CYS GLN ARG ILE ILE LEU ALA GLY PHE SER ALA
SEQRES 10 A 284 GLY GLY HIS VAL VAL ALA THR TYR ASN GLY VAL ALA THR
SEQRES 11 A 284 GLN PRO GLU LEU ARG THR ARG TYR HIS LEU ASP HIS TYR
SEQRES 12 A 284 GLN GLY GLN HIS ALA ALA ILE ILE LEU GLY TYR PRO VAL
SEQRES 13 A 284 ILE ASP LEU THR ALA GLY PHE PRO THR THR SER ALA ALA
SEQRES 14 A 284 ARG ASN GLN ILE THR THR ASP ALA ARG LEU TRP ALA ALA
SEQRES 15 A 284 GLN ARG LEU VAL THR PRO ALA SER LYS PRO ALA PHE VAL
SEQRES 16 A 284 TRP GLN THR ALA THR ASP GLU SER VAL PRO PRO ILE ASN
SEQRES 17 A 284 SER LEU LYS TYR VAL GLN ALA MSE LEU GLN HIS GLN VAL
SEQRES 18 A 284 ALA THR ALA TYR HIS LEU PHE GLY SER GLY ILE HIS GLY
SEQRES 19 A 284 LEU ALA LEU ALA ASN HIS VAL THR GLN LYS PRO GLY LYS
SEQRES 20 A 284 ASP LYS TYR LEU ASN ASP GLN ALA ALA ILE TRP PRO GLN
SEQRES 21 A 284 LEU ALA LEU ARG TRP LEU GLN GLU GLN GLY LEU LEU ALA
SEQRES 22 A 284 GLY ASN TYR LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 284 MSE GLN VAL GLU GLN ARG THR LEU ASN THR ALA ALA HIS
SEQRES 2 B 284 PRO PHE GLN ILE THR ALA TYR TRP LEU ASP GLN ILE SER
SEQRES 3 B 284 ASP PHE GLU THR ALA VAL ASP TYR PRO ILE MSE ILE ILE
SEQRES 4 B 284 CYS PRO GLY GLY GLY PHE THR TYR HIS SER GLY ARG GLU
SEQRES 5 B 284 GLU ALA PRO ILE ALA THR ARG MSE MSE ALA ALA GLY MSE
SEQRES 6 B 284 HIS THR VAL VAL LEU ASN TYR GLN LEU ILE VAL GLY ASP
SEQRES 7 B 284 GLN SER VAL TYR PRO TRP ALA LEU GLN GLN LEU GLY ALA
SEQRES 8 B 284 THR ILE ASP TRP ILE THR THR GLN ALA SER ALA HIS HIS
SEQRES 9 B 284 VAL ASP CYS GLN ARG ILE ILE LEU ALA GLY PHE SER ALA
SEQRES 10 B 284 GLY GLY HIS VAL VAL ALA THR TYR ASN GLY VAL ALA THR
SEQRES 11 B 284 GLN PRO GLU LEU ARG THR ARG TYR HIS LEU ASP HIS TYR
SEQRES 12 B 284 GLN GLY GLN HIS ALA ALA ILE ILE LEU GLY TYR PRO VAL
SEQRES 13 B 284 ILE ASP LEU THR ALA GLY PHE PRO THR THR SER ALA ALA
SEQRES 14 B 284 ARG ASN GLN ILE THR THR ASP ALA ARG LEU TRP ALA ALA
SEQRES 15 B 284 GLN ARG LEU VAL THR PRO ALA SER LYS PRO ALA PHE VAL
SEQRES 16 B 284 TRP GLN THR ALA THR ASP GLU SER VAL PRO PRO ILE ASN
SEQRES 17 B 284 SER LEU LYS TYR VAL GLN ALA MSE LEU GLN HIS GLN VAL
SEQRES 18 B 284 ALA THR ALA TYR HIS LEU PHE GLY SER GLY ILE HIS GLY
SEQRES 19 B 284 LEU ALA LEU ALA ASN HIS VAL THR GLN LYS PRO GLY LYS
SEQRES 20 B 284 ASP LYS TYR LEU ASN ASP GLN ALA ALA ILE TRP PRO GLN
SEQRES 21 B 284 LEU ALA LEU ARG TRP LEU GLN GLU GLN GLY LEU LEU ALA
SEQRES 22 B 284 GLY ASN TYR LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 3D3N MSE A 1 MET SELENOMETHIONINE
MODRES 3D3N MSE A 37 MET SELENOMETHIONINE
MODRES 3D3N MSE A 60 MET SELENOMETHIONINE
MODRES 3D3N MSE A 61 MET SELENOMETHIONINE
MODRES 3D3N MSE A 65 MET SELENOMETHIONINE
MODRES 3D3N MSE A 216 MET SELENOMETHIONINE
MODRES 3D3N MSE B 1 MET SELENOMETHIONINE
MODRES 3D3N MSE B 37 MET SELENOMETHIONINE
MODRES 3D3N MSE B 60 MET SELENOMETHIONINE
MODRES 3D3N MSE B 61 MET SELENOMETHIONINE
MODRES 3D3N MSE B 65 MET SELENOMETHIONINE
MODRES 3D3N MSE B 216 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 37 8
HET MSE A 60 8
HET MSE A 61 8
HET MSE A 65 8
HET MSE A 216 8
HET MSE B 1 8
HET MSE B 37 8
HET MSE B 60 8
HET MSE B 61 8
HET MSE B 65 8
HET MSE B 216 8
HET CA B 285 1
HET EPE A 285 15
HET EPE B 286 15
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 CA CA 2+
FORMUL 4 EPE 2(C8 H18 N2 O4 S)
FORMUL 6 HOH *98(H2 O)
HELIX 1 1 GLU A 52 ALA A 63 1 12
HELIX 2 2 PRO A 83 SER A 101 1 19
HELIX 3 3 SER A 116 ALA A 129 1 14
HELIX 4 4 GLN A 131 TYR A 138 1 8
HELIX 5 5 THR A 166 THR A 174 1 9
HELIX 6 6 ASP A 176 TRP A 180 5 5
HELIX 7 7 ALA A 181 VAL A 186 5 6
HELIX 8 8 PRO A 206 HIS A 219 1 14
HELIX 9 9 ALA A 256 GLN A 269 1 14
HELIX 10 10 GLU B 52 ALA B 63 1 12
HELIX 11 11 PRO B 83 THR B 98 1 16
HELIX 12 12 ALA B 117 ALA B 129 1 13
HELIX 13 13 GLN B 131 TYR B 138 1 8
HELIX 14 14 SER B 167 THR B 174 1 8
HELIX 15 15 ASP B 176 TRP B 180 5 5
HELIX 16 16 ALA B 181 LEU B 185 5 5
HELIX 17 17 PRO B 206 HIS B 219 1 14
HELIX 18 18 ILE B 257 GLN B 269 1 13
SHEET 1 A16 GLN A 2 LEU A 8 0
SHEET 2 A16 PHE A 15 TRP A 21 -1 O TRP A 21 N GLN A 2
SHEET 3 A16 HIS A 66 ASN A 71 -1 O THR A 67 N TYR A 20
SHEET 4 A16 TYR A 34 CYS A 40 1 N ILE A 39 O VAL A 68
SHEET 5 A16 VAL A 105 PHE A 115 1 O ALA A 113 N CYS A 40
SHEET 6 A16 ALA A 149 GLY A 153 1 O ILE A 151 N GLY A 114
SHEET 7 A16 ALA A 193 THR A 198 1 O PHE A 194 N LEU A 152
SHEET 8 A16 THR A 223 PHE A 228 1 O ALA A 224 N VAL A 195
SHEET 9 A16 THR B 223 PHE B 228 -1 O TYR B 225 N LEU A 227
SHEET 10 A16 ALA B 193 THR B 198 1 N VAL B 195 O ALA B 224
SHEET 11 A16 ALA B 149 GLY B 153 1 N LEU B 152 O PHE B 194
SHEET 12 A16 VAL B 105 PHE B 115 1 N LEU B 112 O ILE B 151
SHEET 13 A16 TYR B 34 CYS B 40 1 N CYS B 40 O ALA B 113
SHEET 14 A16 HIS B 66 ASN B 71 1 O VAL B 68 N ILE B 39
SHEET 15 A16 PHE B 15 TRP B 21 -1 N TYR B 20 O THR B 67
SHEET 16 A16 GLN B 2 LEU B 8 -1 N GLN B 2 O TRP B 21
LINK C MSE A 1 N GLN A 2 1555 1555 1.33
LINK C ILE A 36 N MSE A 37 1555 1555 1.33
LINK C MSE A 37 N ILE A 38 1555 1555 1.32
LINK C ARG A 59 N MSE A 60 1555 1555 1.33
LINK C MSE A 60 N MSE A 61 1555 1555 1.33
LINK C MSE A 61 N ALA A 62 1555 1555 1.33
LINK C GLY A 64 N MSE A 65 1555 1555 1.33
LINK C MSE A 65 N HIS A 66 1555 1555 1.33
LINK C ALA A 215 N MSE A 216 1555 1555 1.33
LINK C MSE A 216 N LEU A 217 1555 1555 1.33
LINK C MSE B 1 N GLN B 2 1555 1555 1.33
LINK C ILE B 36 N MSE B 37 1555 1555 1.33
LINK C MSE B 37 N ILE B 38 1555 1555 1.33
LINK C ARG B 59 N MSE B 60 1555 1555 1.33
LINK C MSE B 60 N MSE B 61 1555 1555 1.33
LINK C MSE B 61 N ALA B 62 1555 1555 1.33
LINK C GLY B 64 N MSE B 65 1555 1555 1.33
LINK C MSE B 65 N HIS B 66 1555 1555 1.33
LINK C ALA B 215 N MSE B 216 1555 1555 1.33
LINK C MSE B 216 N LEU B 217 1555 1555 1.33
LINK OD1 ASP B 33 CA CA B 285 1555 1555 2.74
LINK OD2 ASP B 33 CA CA B 285 1555 1555 2.78
LINK CA CA B 285 O HOH B 348 1555 1555 2.72
LINK CA CA B 285 O HOH B 346 1555 1555 2.59
LINK CA CA B 285 O HOH B 317 1555 1555 2.67
CISPEP 1 TYR A 82 PRO A 83 0 0.10
CISPEP 2 PHE A 163 PRO A 164 0 -0.04
CISPEP 3 TYR B 82 PRO B 83 0 0.15
CISPEP 4 PHE B 163 PRO B 164 0 0.19
SITE 1 AC1 2 ASP A 33 ASP B 33
SITE 1 AC2 5 ASP A 78 GLN A 79 SER A 80 TRP A 84
SITE 2 AC2 5 GLN A 172
SITE 1 AC3 5 ASP B 78 GLN B 79 SER B 80 TRP B 84
SITE 2 AC3 5 GLN B 172
CRYST1 66.074 93.022 95.765 90.00 90.00 90.00 P 21 21 21 8
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 0.015135 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010750 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010442 0.00000
TER 1910 ALA A 273
TER 3898 ALA B 273
MASTER 380 0 15 18 16 0 5 6 4025 2 151 44
END |