HEADER HYDROLASE 27-FEB-14 4PPY
TITLE CRYSTAL STRUCTURE OF A PUTATIVE ACYLHYDROLASE (BF3764) FROM
TITLE 2 BACTEROIDES FRAGILIS NCTC 9343 AT 2.00 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACYLHYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 27-235;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES FRAGILIS;
SOURCE 3 ORGANISM_TAXID: 272559;
SOURCE 4 STRAIN: ATCC 25285 / NCTC 9343;
SOURCE 5 GENE: BF9343_3663;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PB1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS PF13472 FAMILY, GDSL-LIKE LIPASE, STRUCTURAL GENOMICS, JOINT CENTER
KEYWDS 2 FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-
KEYWDS 3 BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 3 01-FEB-23 4PPY 1 SEQADV LINK
REVDAT 2 22-NOV-17 4PPY 1 REMARK
REVDAT 1 02-APR-14 4PPY 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE ACYLHYDROLASE (BF3764) FROM
JRNL TITL 2 BACTEROIDES FRAGILIS NCTC 9343 AT 2.00 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 50307
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2560
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3481
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 190
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4867
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 503
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.67000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.174
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.330
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5091 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4803 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6951 ; 1.118 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11041 ; 0.945 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 658 ; 5.130 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 246 ;36.798 ;25.163
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 803 ;11.714 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ; 4.659 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 769 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5963 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1210 ; 0.003 ; 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): 2533 ; 0.727 ; 1.397
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2532 ; 0.723 ; 1.396
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3170 ; 1.237 ; 2.604
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
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 27 A 235
REMARK 3 ORIGIN FOR THE GROUP (A): 55.5793 32.1130 1.5444
REMARK 3 T TENSOR
REMARK 3 T11: 0.0450 T22: 0.0089
REMARK 3 T33: 0.0816 T12: 0.0058
REMARK 3 T13: -0.0086 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 1.4600 L22: 1.6062
REMARK 3 L33: 1.5319 L12: -0.0538
REMARK 3 L13: -0.2276 L23: 0.1979
REMARK 3 S TENSOR
REMARK 3 S11: 0.0349 S12: -0.0349 S13: -0.0450
REMARK 3 S21: 0.0264 S22: -0.0020 S23: -0.0795
REMARK 3 S31: 0.0222 S32: 0.1100 S33: -0.0329
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 28 B 235
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4142 32.7232 21.4421
REMARK 3 T TENSOR
REMARK 3 T11: 0.0997 T22: 0.0850
REMARK 3 T33: 0.0860 T12: -0.0007
REMARK 3 T13: 0.0100 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.7467 L22: 0.6323
REMARK 3 L33: 2.0414 L12: 0.0030
REMARK 3 L13: -0.4825 L23: -0.3234
REMARK 3 S TENSOR
REMARK 3 S11: -0.0639 S12: -0.0703 S13: -0.0587
REMARK 3 S21: 0.1174 S22: 0.0243 S23: 0.1032
REMARK 3 S31: 0.1160 S32: -0.0806 S33: 0.0396
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 28 C 235
REMARK 3 ORIGIN FOR THE GROUP (A): 88.9981 12.4509 9.5664
REMARK 3 T TENSOR
REMARK 3 T11: 0.0401 T22: 0.0899
REMARK 3 T33: 0.0930 T12: 0.0098
REMARK 3 T13: -0.0073 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 1.6878 L22: 0.4025
REMARK 3 L33: 2.0029 L12: 0.1776
REMARK 3 L13: -0.3384 L23: -0.1403
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: -0.0731 S13: 0.0850
REMARK 3 S21: 0.0130 S22: 0.0062 S23: 0.0387
REMARK 3 S31: -0.0782 S32: -0.0341 S33: -0.0125
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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.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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 3.ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS. 4.WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT.
REMARK 3 5.RAMACHANDRAN OUTLIER AT RESIDUE 112 IN ALL 3 CHAINS IS
REMARK 3 SUPPORTED BY ELECTRON DENSITY. 6.EXPERIMENTAL PHASES IN THE FORM
REMARK 3 OF HL COEFFICIENTS WERE USED AS RESTRAINTS DURING
REMARK 3 CRYSTALLOGRAPHIC REFINEMENT.
REMARK 4
REMARK 4 4PPY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979106,0.918401,0.979351
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : KOHZU: DOUBLE CRYSTAL SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 60.686
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.20300
REMARK 200 R SYM FOR SHELL (I) : 0.20300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
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 (%): 54.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20M MAGNESIUM CHLORIDE, 30.00%
REMARK 280 POLYETHYLENE GLYCOL 4000, 0.1M TRIS HYDROCHLORIDE PH 8.5,
REMARK 280 NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 101.36550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.10650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 101.36550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.10650
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: 2010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 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: 2020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 202.73100
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
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 GLY A 0
REMARK 465 GLY B 0
REMARK 465 GLN B 27
REMARK 465 GLY C 0
REMARK 465 GLN C 27
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 27 CG CD OE1 NE2
REMARK 470 LYS A 46 CG CD CE NZ
REMARK 470 LYS A 49 CG CD CE NZ
REMARK 470 ASN A 50 CG OD1 ND2
REMARK 470 GLU B 28 CG CD OE1 OE2
REMARK 470 GLU C 28 CG CD OE1 OE2
REMARK 470 LYS C 46 CE NZ
REMARK 470 LYS C 49 CG CD CE NZ
REMARK 470 ASN C 50 CG OD1 ND2
REMARK 470 ARG C 235 CG CD NE CZ NH1 NH2
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 C 395 O HOH C 395 2656 2.16
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 ASN A 59 -143.93 -107.00
REMARK 500 VAL A 99 -63.87 -120.70
REMARK 500 ALA A 112 -14.48 102.68
REMARK 500 VAL A 212 -51.30 -130.89
REMARK 500 ASP B 30 70.79 -164.52
REMARK 500 ASN B 59 -143.94 -107.44
REMARK 500 VAL B 99 -64.15 -123.00
REMARK 500 ALA B 112 -14.52 102.30
REMARK 500 VAL B 212 -50.92 -131.36
REMARK 500 ASP C 30 72.15 -166.77
REMARK 500 ASN C 59 -145.49 -107.18
REMARK 500 VAL C 99 -63.49 -122.97
REMARK 500 ALA C 112 -14.26 103.19
REMARK 500 VAL C 212 -50.59 -132.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-419039 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT (RESIDUES 27-235) WAS EXPRESSED WITH A PURIFICATION
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 4PPY A 27 235 UNP Q5L8Y8 Q5L8Y8_BACFN 27 235
DBREF 4PPY B 27 235 UNP Q5L8Y8 Q5L8Y8_BACFN 27 235
DBREF 4PPY C 27 235 UNP Q5L8Y8 Q5L8Y8_BACFN 27 235
SEQADV 4PPY GLY A 0 UNP Q5L8Y8 EXPRESSION TAG
SEQADV 4PPY GLY B 0 UNP Q5L8Y8 EXPRESSION TAG
SEQADV 4PPY GLY C 0 UNP Q5L8Y8 EXPRESSION TAG
SEQRES 1 A 210 GLY GLN GLU LYS ASP TRP ALA ASN LEU GLN ARG TYR ALA
SEQRES 2 A 210 GLN GLN ASN ALA GLU LEU PRO LYS PRO ASP LYS ASN GLU
SEQRES 3 A 210 LYS ARG VAL VAL PHE MSE GLY ASN SER ILE THR GLU GLY
SEQRES 4 A 210 TRP VAL ASN THR HIS PRO ASP PHE PHE LYS SER ASN GLY
SEQRES 5 A 210 TYR ILE GLY ARG GLY ILE GLY GLY GLN THR SER TYR GLN
SEQRES 6 A 210 PHE LEU VAL ARG PHE ARG GLU ASP VAL ILE ASN LEU SER
SEQRES 7 A 210 PRO ALA LEU VAL VAL ILE ASN ALA ALA THR ASN ASP ILE
SEQRES 8 A 210 ALA GLU ASN THR GLY ALA TYR HIS GLU ASP ARG THR PHE
SEQRES 9 A 210 GLY ASN ILE VAL SER MSE VAL GLU LEU ALA LYS ALA ASN
SEQRES 10 A 210 HIS ILE LYS VAL ILE LEU THR THR THR LEU PRO ALA ALA
SEQRES 11 A 210 ALA PHE GLY TRP ASN PRO SER ILE LYS ASP ALA PRO GLN
SEQRES 12 A 210 LYS ILE ALA SER LEU ASN ALA ARG LEU LYS ALA TYR ALA
SEQRES 13 A 210 GLN THR ASN LYS ILE PRO PHE VAL ASP TYR TYR SER SER
SEQRES 14 A 210 MSE VAL SER GLY SER ASN LYS ALA LEU ASN PRO ALA TYR
SEQRES 15 A 210 THR LYS ASP GLY VAL HIS PRO THR SER GLU GLY TYR ASP
SEQRES 16 A 210 VAL MSE GLU ASN LEU ILE GLN GLN ALA ILE ASN LYS THR
SEQRES 17 A 210 LEU ARG
SEQRES 1 B 210 GLY GLN GLU LYS ASP TRP ALA ASN LEU GLN ARG TYR ALA
SEQRES 2 B 210 GLN GLN ASN ALA GLU LEU PRO LYS PRO ASP LYS ASN GLU
SEQRES 3 B 210 LYS ARG VAL VAL PHE MSE GLY ASN SER ILE THR GLU GLY
SEQRES 4 B 210 TRP VAL ASN THR HIS PRO ASP PHE PHE LYS SER ASN GLY
SEQRES 5 B 210 TYR ILE GLY ARG GLY ILE GLY GLY GLN THR SER TYR GLN
SEQRES 6 B 210 PHE LEU VAL ARG PHE ARG GLU ASP VAL ILE ASN LEU SER
SEQRES 7 B 210 PRO ALA LEU VAL VAL ILE ASN ALA ALA THR ASN ASP ILE
SEQRES 8 B 210 ALA GLU ASN THR GLY ALA TYR HIS GLU ASP ARG THR PHE
SEQRES 9 B 210 GLY ASN ILE VAL SER MSE VAL GLU LEU ALA LYS ALA ASN
SEQRES 10 B 210 HIS ILE LYS VAL ILE LEU THR THR THR LEU PRO ALA ALA
SEQRES 11 B 210 ALA PHE GLY TRP ASN PRO SER ILE LYS ASP ALA PRO GLN
SEQRES 12 B 210 LYS ILE ALA SER LEU ASN ALA ARG LEU LYS ALA TYR ALA
SEQRES 13 B 210 GLN THR ASN LYS ILE PRO PHE VAL ASP TYR TYR SER SER
SEQRES 14 B 210 MSE VAL SER GLY SER ASN LYS ALA LEU ASN PRO ALA TYR
SEQRES 15 B 210 THR LYS ASP GLY VAL HIS PRO THR SER GLU GLY TYR ASP
SEQRES 16 B 210 VAL MSE GLU ASN LEU ILE GLN GLN ALA ILE ASN LYS THR
SEQRES 17 B 210 LEU ARG
SEQRES 1 C 210 GLY GLN GLU LYS ASP TRP ALA ASN LEU GLN ARG TYR ALA
SEQRES 2 C 210 GLN GLN ASN ALA GLU LEU PRO LYS PRO ASP LYS ASN GLU
SEQRES 3 C 210 LYS ARG VAL VAL PHE MSE GLY ASN SER ILE THR GLU GLY
SEQRES 4 C 210 TRP VAL ASN THR HIS PRO ASP PHE PHE LYS SER ASN GLY
SEQRES 5 C 210 TYR ILE GLY ARG GLY ILE GLY GLY GLN THR SER TYR GLN
SEQRES 6 C 210 PHE LEU VAL ARG PHE ARG GLU ASP VAL ILE ASN LEU SER
SEQRES 7 C 210 PRO ALA LEU VAL VAL ILE ASN ALA ALA THR ASN ASP ILE
SEQRES 8 C 210 ALA GLU ASN THR GLY ALA TYR HIS GLU ASP ARG THR PHE
SEQRES 9 C 210 GLY ASN ILE VAL SER MSE VAL GLU LEU ALA LYS ALA ASN
SEQRES 10 C 210 HIS ILE LYS VAL ILE LEU THR THR THR LEU PRO ALA ALA
SEQRES 11 C 210 ALA PHE GLY TRP ASN PRO SER ILE LYS ASP ALA PRO GLN
SEQRES 12 C 210 LYS ILE ALA SER LEU ASN ALA ARG LEU LYS ALA TYR ALA
SEQRES 13 C 210 GLN THR ASN LYS ILE PRO PHE VAL ASP TYR TYR SER SER
SEQRES 14 C 210 MSE VAL SER GLY SER ASN LYS ALA LEU ASN PRO ALA TYR
SEQRES 15 C 210 THR LYS ASP GLY VAL HIS PRO THR SER GLU GLY TYR ASP
SEQRES 16 C 210 VAL MSE GLU ASN LEU ILE GLN GLN ALA ILE ASN LYS THR
SEQRES 17 C 210 LEU ARG
MODRES 4PPY MSE A 57 MET SELENOMETHIONINE
MODRES 4PPY MSE A 135 MET SELENOMETHIONINE
MODRES 4PPY MSE A 195 MET SELENOMETHIONINE
MODRES 4PPY MSE A 222 MET SELENOMETHIONINE
MODRES 4PPY MSE B 57 MET SELENOMETHIONINE
MODRES 4PPY MSE B 135 MET SELENOMETHIONINE
MODRES 4PPY MSE B 195 MET SELENOMETHIONINE
MODRES 4PPY MSE B 222 MET SELENOMETHIONINE
MODRES 4PPY MSE C 57 MET SELENOMETHIONINE
MODRES 4PPY MSE C 135 MET SELENOMETHIONINE
MODRES 4PPY MSE C 195 MET SELENOMETHIONINE
MODRES 4PPY MSE C 222 MET SELENOMETHIONINE
HET MSE A 57 8
HET MSE A 135 8
HET MSE A 195 8
HET MSE A 222 8
HET MSE B 57 8
HET MSE B 135 8
HET MSE B 195 8
HET MSE B 222 8
HET MSE C 57 8
HET MSE C 135 8
HET MSE C 195 8
HET MSE C 222 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 4 HOH *503(H2 O)
HELIX 1 1 LEU A 34 LEU A 44 1 11
HELIX 2 2 ASN A 59 HIS A 69 1 11
HELIX 3 3 HIS A 69 GLY A 77 1 9
HELIX 4 4 THR A 87 VAL A 99 1 13
HELIX 5 5 ILE A 100 SER A 103 5 4
HELIX 6 6 ALA A 112 ALA A 117 1 6
HELIX 7 7 HIS A 124 ASN A 142 1 19
HELIX 8 8 ASP A 165 ASN A 184 1 20
HELIX 9 9 ASP A 190 MSE A 195 1 6
HELIX 10 10 PRO A 205 THR A 208 5 4
HELIX 11 11 THR A 215 ARG A 235 1 21
HELIX 12 12 LEU B 34 LEU B 44 1 11
HELIX 13 13 ASP B 48 LYS B 52 5 5
HELIX 14 14 ASN B 59 HIS B 69 1 11
HELIX 15 15 HIS B 69 GLY B 77 1 9
HELIX 16 16 THR B 87 VAL B 99 1 13
HELIX 17 17 ILE B 100 SER B 103 5 4
HELIX 18 18 ALA B 112 ALA B 117 1 6
HELIX 19 19 HIS B 124 ASN B 142 1 19
HELIX 20 20 ASP B 165 ASN B 184 1 20
HELIX 21 21 ASP B 190 MSE B 195 1 6
HELIX 22 22 PRO B 205 THR B 208 5 4
HELIX 23 23 THR B 215 ARG B 235 1 21
HELIX 24 24 LEU C 34 LEU C 44 1 11
HELIX 25 25 ASN C 59 HIS C 69 1 11
HELIX 26 26 HIS C 69 GLY C 77 1 9
HELIX 27 27 THR C 87 VAL C 99 1 13
HELIX 28 28 ILE C 100 SER C 103 5 4
HELIX 29 29 ALA C 112 ALA C 117 1 6
HELIX 30 30 HIS C 124 ASN C 142 1 19
HELIX 31 31 ASP C 165 ASN C 184 1 20
HELIX 32 32 ASP C 190 MSE C 195 1 6
HELIX 33 33 PRO C 205 THR C 208 5 4
HELIX 34 34 THR C 215 ARG C 235 1 21
SHEET 1 A 5 ILE A 79 GLY A 82 0
SHEET 2 A 5 VAL A 54 GLY A 58 1 N VAL A 54 O ILE A 79
SHEET 3 A 5 LEU A 106 ILE A 109 1 O VAL A 108 N MSE A 57
SHEET 4 A 5 LYS A 145 THR A 149 1 O ILE A 147 N ILE A 109
SHEET 5 A 5 PHE A 188 VAL A 189 1 O VAL A 189 N LEU A 148
SHEET 1 B 2 VAL A 196 SER A 197 0
SHEET 2 B 2 ALA A 202 LEU A 203 -1 O ALA A 202 N SER A 197
SHEET 1 C 5 TYR B 78 GLY B 82 0
SHEET 2 C 5 VAL B 54 GLY B 58 1 N PHE B 56 O ILE B 79
SHEET 3 C 5 LEU B 106 ILE B 109 1 O VAL B 108 N MSE B 57
SHEET 4 C 5 LYS B 145 THR B 149 1 O ILE B 147 N ILE B 109
SHEET 5 C 5 PHE B 188 VAL B 189 1 O VAL B 189 N LEU B 148
SHEET 1 D 2 VAL B 196 SER B 197 0
SHEET 2 D 2 ALA B 202 LEU B 203 -1 O ALA B 202 N SER B 197
SHEET 1 E 5 TYR C 78 GLY C 82 0
SHEET 2 E 5 VAL C 54 GLY C 58 1 N VAL C 54 O ILE C 79
SHEET 3 E 5 LEU C 106 ILE C 109 1 O VAL C 108 N MSE C 57
SHEET 4 E 5 LYS C 145 THR C 149 1 O LYS C 145 N VAL C 107
SHEET 5 E 5 PHE C 188 VAL C 189 1 O VAL C 189 N LEU C 148
SHEET 1 F 2 VAL C 196 SER C 197 0
SHEET 2 F 2 ALA C 202 LEU C 203 -1 O ALA C 202 N SER C 197
LINK C PHE A 56 N MSE A 57 1555 1555 1.33
LINK C MSE A 57 N GLY A 58 1555 1555 1.33
LINK C SER A 134 N MSE A 135 1555 1555 1.32
LINK C MSE A 135 N VAL A 136 1555 1555 1.33
LINK C SER A 194 N MSE A 195 1555 1555 1.33
LINK C MSE A 195 N VAL A 196 1555 1555 1.33
LINK C VAL A 221 N MSE A 222 1555 1555 1.33
LINK C MSE A 222 N GLU A 223 1555 1555 1.33
LINK C PHE B 56 N MSE B 57 1555 1555 1.33
LINK C MSE B 57 N GLY B 58 1555 1555 1.33
LINK C SER B 134 N MSE B 135 1555 1555 1.33
LINK C MSE B 135 N VAL B 136 1555 1555 1.33
LINK C SER B 194 N MSE B 195 1555 1555 1.33
LINK C MSE B 195 N VAL B 196 1555 1555 1.33
LINK C VAL B 221 N MSE B 222 1555 1555 1.33
LINK C MSE B 222 N GLU B 223 1555 1555 1.33
LINK C PHE C 56 N MSE C 57 1555 1555 1.33
LINK C MSE C 57 N GLY C 58 1555 1555 1.33
LINK C SER C 134 N MSE C 135 1555 1555 1.33
LINK C MSE C 135 N VAL C 136 1555 1555 1.34
LINK C SER C 194 N MSE C 195 1555 1555 1.33
LINK C MSE C 195 N VAL C 196 1555 1555 1.33
LINK C VAL C 221 N MSE C 222 1555 1555 1.33
LINK C MSE C 222 N GLU C 223 1555 1555 1.33
CRYST1 202.731 62.213 61.009 90.00 95.90 90.00 C 1 2 1 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 0.004933 0.000000 0.000509 0.00000
SCALE2 0.000000 0.016074 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016478 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
