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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 14-JAN-08 3BXP
TITLE CRYSTAL STRUCTURE OF PUTATIVE CARBOXYLESTERASE
TITLE 2 (NP_786266.1) FROM LACTOBACILLUS PLANTARUM AT 1.70 A
TITLE 3 RESOLUTION
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 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: WCFS1 / NCIMB 8826;
SOURCE 5 ATCC: BAA-793;
SOURCE 6 GENE: NP_786266.1, LP_2923;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS NP_786266.1, PUTATIVE CARBOXYLESTERASE, STRUCTURAL GENOMICS,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, PSI-2, STRUCTURAL GENOMICS, UNKNOWN
KEYWDS 4 FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 29-JAN-08 3BXP 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE CARBOXYLESTERASE
JRNL TITL 2 (NP_786266.1) FROM LACTOBACILLUS PLANTARUM AT 1.70
JRNL TITL 3 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0067
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 59208
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 + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2995
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3704
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 199
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4563
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : -0.74000
REMARK 3 B33 (A**2) : -0.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.101
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.098
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.975
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4298 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2733 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5899 ; 1.527 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6676 ; 1.079 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 548 ; 6.153 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;32.966 ;23.880
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 612 ;11.926 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;16.119 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 664 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4877 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 876 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2681 ; 1.917 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1081 ; 0.587 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4324 ; 2.766 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1617 ; 4.129 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1575 ; 5.611 ;11.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 273
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9313 31.5463 44.6912
REMARK 3 T TENSOR
REMARK 3 T11: -0.0215 T22: -0.0208
REMARK 3 T33: -0.0313 T12: -0.0111
REMARK 3 T13: 0.0063 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.5254 L22: 0.6750
REMARK 3 L33: 0.3616 L12: 0.0481
REMARK 3 L13: 0.1517 L23: -0.0103
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: -0.0370 S13: -0.0193
REMARK 3 S21: 0.0030 S22: -0.0106 S23: 0.0644
REMARK 3 S31: -0.0487 S32: -0.0211 S33: 0.0035
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 0 B 273
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1381 48.2340 16.4949
REMARK 3 T TENSOR
REMARK 3 T11: -0.0470 T22: -0.0244
REMARK 3 T33: -0.0203 T12: -0.0077
REMARK 3 T13: 0.0024 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.2831 L22: 0.7687
REMARK 3 L33: 0.8606 L12: -0.0972
REMARK 3 L13: 0.0345 L23: -0.0731
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: 0.0132 S13: -0.0236
REMARK 3 S21: 0.0258 S22: -0.0086 S23: 0.0398
REMARK 3 S31: 0.0156 S32: -0.0474 S33: 0.0055
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS
REMARK 3 ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO
REMARK 3 PARTIAL S-MET INCORPORATION. 4. CHLORIDE ION, HEPES AND 1,2-
REMARK 3 PROPANEDIOL MOLECULES FROM CRYSTALLIZATION ARE MODELED IN THIS
REMARK 3 STRUCTURE.
REMARK 4
REMARK 4 3BXP 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 RCSB046086.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-2007
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 : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97901
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 (HORIZONTAL FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59209
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 28.433
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.53200
REMARK 200 R SYM FOR SHELL (I) : 0.53200
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 30.0% 1,2-PROPANEDIOL,
REMARK 280 20.0% PEG 400, 0.1M HEPES PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 47.11100
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 1800 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 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 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 GLY A 274
REMARK 465 ASN A 275
REMARK 465 TYR A 276
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 TYR B 250
REMARK 465 GLY B 274
REMARK 465 ASN B 275
REMARK 465 TYR B 276
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 2 CD OE1 NE2
REMARK 470 ARG A 51 CZ NH1 NH2
REMARK 470 GLU A 133 CD OE1 OE2
REMARK 470 ARG A 137 NE CZ NH1 NH2
REMARK 470 GLU A 202 CG CD OE1 OE2
REMARK 470 ASP A 248 CG OD1 OD2
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 LEU A 251 CG CD1 CD2
REMARK 470 ASN A 252 CG OD1 ND2
REMARK 470 ASP A 253 OD1 OD2
REMARK 470 ASP B 27 CG OD1 OD2
REMARK 470 ARG B 51 CZ NH1 NH2
REMARK 470 GLU B 133 CG CD OE1 OE2
REMARK 470 ARG B 178 CZ NH1 NH2
REMARK 470 GLU B 202 CG CD OE1 OE2
REMARK 470 ASP B 253 CG OD1 OD2
REMARK 470 GLN B 254 CG CD OE1 NE2
REMARK 470 ARG B 264 CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 NH2 ARG B 135 O LEU B 140 1.77
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS A 142 N - CA - CB ANGL. DEV. = -12.3 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 HIS A 104 67.79 63.12
REMARK 500 SER A 116 -116.71 50.27
REMARK 500 LEU A 159 11.31 -69.32
REMARK 500 ALA A 161 46.57 -101.41
REMARK 500 SER A 203 -162.49 -160.70
REMARK 500 HIS B 104 70.64 67.31
REMARK 500 SER B 116 -124.40 47.86
REMARK 500 TYR B 154 57.28 34.04
REMARK 500 THR B 174 141.61 -176.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: EPE BINDING SITE FOR RESIDUE B 278
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: EPE BINDING SITE FOR RESIDUE A 277
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: PGO BINDING SITE FOR RESIDUE B 279
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: PGR BINDING SITE FOR RESIDUE A 278
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: PGR BINDING SITE FOR RESIDUE B 280
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: PGR BINDING SITE FOR RESIDUE B 281
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: PGO BINDING SITE FOR RESIDUE A 279
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: PGO BINDING SITE FOR RESIDUE A 280
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: PGO BINDING SITE FOR RESIDUE A 281
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 379483 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3BXP A 1 276 UNP Q88TL9 Q88TL9_LACPL 1 276
DBREF 3BXP B 1 276 UNP Q88TL9 Q88TL9_LACPL 1 276
SEQADV 3BXP GLY A 0 UNP Q88TL9 LEADER SEQUENCE
SEQADV 3BXP GLY B 0 UNP Q88TL9 LEADER SEQUENCE
SEQRES 1 A 277 GLY MSE GLN VAL GLU GLN ARG THR LEU ASN THR ALA ALA
SEQRES 2 A 277 HIS PRO PHE GLN ILE THR ALA TYR TRP LEU ASP GLN ILE
SEQRES 3 A 277 SER ASP PHE GLU THR ALA VAL ASP TYR PRO ILE MSE ILE
SEQRES 4 A 277 ILE CYS PRO GLY GLY GLY PHE THR TYR HIS SER GLY ARG
SEQRES 5 A 277 GLU GLU ALA PRO ILE ALA THR ARG MSE MSE ALA ALA GLY
SEQRES 6 A 277 MSE HIS THR VAL VAL LEU ASN TYR GLN LEU ILE VAL GLY
SEQRES 7 A 277 ASP GLN SER VAL TYR PRO TRP ALA LEU GLN GLN LEU GLY
SEQRES 8 A 277 ALA THR ILE ASP TRP ILE THR THR GLN ALA SER ALA HIS
SEQRES 9 A 277 HIS VAL ASP CYS GLN ARG ILE ILE LEU ALA GLY PHE SER
SEQRES 10 A 277 ALA GLY GLY HIS VAL VAL ALA THR TYR ASN GLY VAL ALA
SEQRES 11 A 277 THR GLN PRO GLU LEU ARG THR ARG TYR HIS LEU ASP HIS
SEQRES 12 A 277 TYR GLN GLY GLN HIS ALA ALA ILE ILE LEU GLY TYR PRO
SEQRES 13 A 277 VAL ILE ASP LEU THR ALA GLY PHE PRO THR THR SER ALA
SEQRES 14 A 277 ALA ARG ASN GLN ILE THR THR ASP ALA ARG LEU TRP ALA
SEQRES 15 A 277 ALA GLN ARG LEU VAL THR PRO ALA SER LYS PRO ALA PHE
SEQRES 16 A 277 VAL TRP GLN THR ALA THR ASP GLU SER VAL PRO PRO ILE
SEQRES 17 A 277 ASN SER LEU LYS TYR VAL GLN ALA MSE LEU GLN HIS GLN
SEQRES 18 A 277 VAL ALA THR ALA TYR HIS LEU PHE GLY SER GLY ILE HIS
SEQRES 19 A 277 GLY LEU ALA LEU ALA ASN HIS VAL THR GLN LYS PRO GLY
SEQRES 20 A 277 LYS ASP LYS TYR LEU ASN ASP GLN ALA ALA ILE TRP PRO
SEQRES 21 A 277 GLN LEU ALA LEU ARG TRP LEU GLN GLU GLN GLY LEU LEU
SEQRES 22 A 277 ALA GLY ASN TYR
SEQRES 1 B 277 GLY MSE GLN VAL GLU GLN ARG THR LEU ASN THR ALA ALA
SEQRES 2 B 277 HIS PRO PHE GLN ILE THR ALA TYR TRP LEU ASP GLN ILE
SEQRES 3 B 277 SER ASP PHE GLU THR ALA VAL ASP TYR PRO ILE MSE ILE
SEQRES 4 B 277 ILE CYS PRO GLY GLY GLY PHE THR TYR HIS SER GLY ARG
SEQRES 5 B 277 GLU GLU ALA PRO ILE ALA THR ARG MSE MSE ALA ALA GLY
SEQRES 6 B 277 MSE HIS THR VAL VAL LEU ASN TYR GLN LEU ILE VAL GLY
SEQRES 7 B 277 ASP GLN SER VAL TYR PRO TRP ALA LEU GLN GLN LEU GLY
SEQRES 8 B 277 ALA THR ILE ASP TRP ILE THR THR GLN ALA SER ALA HIS
SEQRES 9 B 277 HIS VAL ASP CYS GLN ARG ILE ILE LEU ALA GLY PHE SER
SEQRES 10 B 277 ALA GLY GLY HIS VAL VAL ALA THR TYR ASN GLY VAL ALA
SEQRES 11 B 277 THR GLN PRO GLU LEU ARG THR ARG TYR HIS LEU ASP HIS
SEQRES 12 B 277 TYR GLN GLY GLN HIS ALA ALA ILE ILE LEU GLY TYR PRO
SEQRES 13 B 277 VAL ILE ASP LEU THR ALA GLY PHE PRO THR THR SER ALA
SEQRES 14 B 277 ALA ARG ASN GLN ILE THR THR ASP ALA ARG LEU TRP ALA
SEQRES 15 B 277 ALA GLN ARG LEU VAL THR PRO ALA SER LYS PRO ALA PHE
SEQRES 16 B 277 VAL TRP GLN THR ALA THR ASP GLU SER VAL PRO PRO ILE
SEQRES 17 B 277 ASN SER LEU LYS TYR VAL GLN ALA MSE LEU GLN HIS GLN
SEQRES 18 B 277 VAL ALA THR ALA TYR HIS LEU PHE GLY SER GLY ILE HIS
SEQRES 19 B 277 GLY LEU ALA LEU ALA ASN HIS VAL THR GLN LYS PRO GLY
SEQRES 20 B 277 LYS ASP LYS TYR LEU ASN ASP GLN ALA ALA ILE TRP PRO
SEQRES 21 B 277 GLN LEU ALA LEU ARG TRP LEU GLN GLU GLN GLY LEU LEU
SEQRES 22 B 277 ALA GLY ASN TYR
MODRES 3BXP MSE A 1 MET SELENOMETHIONINE
MODRES 3BXP MSE A 37 MET SELENOMETHIONINE
MODRES 3BXP MSE A 60 MET SELENOMETHIONINE
MODRES 3BXP MSE A 61 MET SELENOMETHIONINE
MODRES 3BXP MSE A 65 MET SELENOMETHIONINE
MODRES 3BXP MSE A 216 MET SELENOMETHIONINE
MODRES 3BXP MSE B 1 MET SELENOMETHIONINE
MODRES 3BXP MSE B 37 MET SELENOMETHIONINE
MODRES 3BXP MSE B 60 MET SELENOMETHIONINE
MODRES 3BXP MSE B 61 MET SELENOMETHIONINE
MODRES 3BXP MSE B 65 MET SELENOMETHIONINE
MODRES 3BXP 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 CL B 277 1
HET EPE A 277 15
HET PGR A 278 5
HET PGO A 279 5
HET PGO A 280 5
HET PGO A 281 5
HET EPE B 278 15
HET PGO B 279 5
HET PGR B 280 5
HET PGR B 281 5
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM PGR R-1,2-PROPANEDIOL
HETNAM PGO S-1,2-PROPANEDIOL
HETSYN EPE HEPES
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 CL CL 1-
FORMUL 4 EPE 2(C8 H18 N2 O4 S)
FORMUL 5 PGR 3(C3 H8 O2)
FORMUL 6 PGO 4(C3 H8 O2)
FORMUL 13 HOH *383(H2 O)
HELIX 1 1 GLU A 52 ALA A 63 1 12
HELIX 2 2 PRO A 83 HIS A 104 1 22
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 ASP A 248 GLN A 269 1 22
HELIX 10 10 GLU B 52 ALA B 63 1 12
HELIX 11 11 PRO B 83 GLN B 99 1 17
HELIX 12 12 GLN B 99 HIS B 104 1 6
HELIX 13 13 ALA B 117 ALA B 129 1 13
HELIX 14 14 GLN B 131 TYR B 138 1 8
HELIX 15 15 THR B 166 THR B 174 1 9
HELIX 16 16 ASP B 176 TRP B 180 5 5
HELIX 17 17 ALA B 181 VAL B 186 5 6
HELIX 18 18 PRO B 206 HIS B 219 1 14
HELIX 19 19 SER B 230 LEU B 235 5 6
HELIX 20 20 ALA B 256 GLN B 269 1 14
SHEET 1 A16 MSE A 1 LEU A 8 0
SHEET 2 A16 PHE A 15 LEU A 22 -1 O ALA A 19 N GLU A 4
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 LEU A 112
SHEET 7 A16 ALA A 193 GLN A 197 1 O PHE A 194 N LEU A 152
SHEET 8 A16 THR A 223 LEU A 227 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 GLY B 114 O GLY B 153
SHEET 13 A16 TYR B 34 CYS B 40 1 N ILE B 38 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 LEU B 22 -1 N TYR B 20 O THR B 67
SHEET 16 A16 MSE B 1 LEU B 8 -1 N GLU B 4 O ALA B 19
CISPEP 1 TYR A 82 PRO A 83 0 4.86
CISPEP 2 PHE A 163 PRO A 164 0 1.02
CISPEP 3 TYR B 82 PRO B 83 0 4.56
CISPEP 4 PHE B 163 PRO B 164 0 3.41
SITE 1 AC1 5 ASP B 78 GLN B 79 SER B 80 TRP B 84
SITE 2 AC1 5 GLN B 172
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 4 TYR B 20 ALA B 54 ALA B 57 THR B 58
SITE 1 AC4 8 ALA A 224 HIS A 226 LEU A 261 GLU A 268
SITE 2 AC4 8 PHE B 228 GLY B 229 SER B 230 HIS B 233
SITE 1 AC5 3 GLN A 214 PRO B 206 ILE B 207
SITE 1 AC6 4 ASP A 33 ALA A 100 SER A 101 ASP B 33
SITE 1 AC7 8 ARG A 135 ASP A 141 TYR A 143 GLN A 144
SITE 2 AC7 8 ARG B 135 ASP B 141 TYR B 143 GLN B 144
SITE 1 AC8 4 GLN A 108 GLN A 146 ALA A 148 LYS A 191
SITE 1 AC9 2 ALA A 54 THR A 58
CRYST1 53.595 94.222 58.758 90.00 107.47 90.00 P 1 21 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 0.018659 0.000000 0.005871 0.00000
SCALE2 0.000000 0.010613 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017841 0.00000
TER 2053 ALA A 273
TER 4116 ALA B 273
MASTER 414 0 22 20 16 0 13 6 4563 2 161 44
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