| content |
HEADER HYDROLASE 11-APR-14 4Q34
TITLE CRYSTAL STRUCTURE OF A PUTATIVE ESTERASE (BDI_1566) FROM
TITLE 2 PARABACTEROIDES DISTASONIS ATCC 8503 AT 1.60 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 20-341;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARABACTEROIDES DISTASONIS;
SOURCE 3 ORGANISM_TAXID: 435591;
SOURCE 4 STRAIN: ATCC 8503 / DSM 20701 / NCTC 11152;
SOURCE 5 GENE: BDI_1566;
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 ALPHA/BETA HYDROLASE FAMILY (PF12697), STRUCTURAL GENOMICS, JOINT
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 3 PSI-BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 18-JUN-14 4Q34 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE ESTERASE (BDI_1566) FROM
JRNL TITL 2 PARABACTEROIDES DISTASONIS ATCC 8503 AT 1.60 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 50204
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) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2562
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3391
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2572
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 322
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.64000
REMARK 3 B22 (A**2) : 1.64000
REMARK 3 B33 (A**2) : -3.29000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.075
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.298
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2813 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2625 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3840 ; 1.513 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6057 ; 0.800 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 359 ; 6.023 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 141 ;33.304 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 428 ;13.725 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;17.163 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 406 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3233 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 695 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
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 21 A 341
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4565 7.2488 90.3092
REMARK 3 T TENSOR
REMARK 3 T11: 0.0485 T22: 0.0413
REMARK 3 T33: 0.1110 T12: 0.0086
REMARK 3 T13: -0.0053 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.5226 L22: 0.3273
REMARK 3 L33: 0.8388 L12: -0.0786
REMARK 3 L13: -0.0993 L23: -0.0135
REMARK 3 S TENSOR
REMARK 3 S11: 0.0058 S12: 0.0405 S13: -0.0640
REMARK 3 S21: -0.0419 S22: -0.0045 S23: -0.0030
REMARK 3 S31: 0.1090 S32: 0.0240 S33: -0.0013
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 0.75
REMARK 3 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 3.ATOM RECORD CONTAINS 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 TLS ASSIGNMENT. 5.CHLORIDE
REMARK 3 (CL) FROM THE CRYSTALLIZATION AND GLYCEROL (GOL) USED AS A
REMARK 3 CRYOPROTECTANT HAVE BEEN MODELED INTO THE STRUCTURE
REMARK 4
REMARK 4 4Q34 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085543.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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) : 0.97895,0.97843
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING);
REMARK 200 SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50356
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 29.663
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 7.720
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.25300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.330
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD,SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.00M LITHIUM CHLORIDE, 20.00%
REMARK 280 POLYETHYLENE GLYCOL 6000, 0.1M CITRIC ACID PH 5.0, NANODROP,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.79550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 29.66350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 29.66350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.39775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 29.66350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 29.66350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 157.19325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 29.66350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 29.66350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 52.39775
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 29.66350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 29.66350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 157.19325
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 104.79550
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: 8410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 209.59100
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 A 521 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 GLY A 0
REMARK 465 ASP A 20
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 GLU A 21 CG CD OE1 OE2
REMARK 470 ILE A 236 CG1 CG2 CD1
REMARK 470 LYS A 241 CG CD CE NZ
REMARK 470 GLU A 273 CD OE1 OE2
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 DISTANCE
REMARK 500 OD2 ASP A 126 O HOH A 700 2.14
REMARK 500 O HOH A 623 O HOH A 760 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 O3 GOL A 407 O HOH A 617 7556 2.12
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 GLU A 81 -149.16 -94.44
REMARK 500 ALA A 112 31.89 -95.52
REMARK 500 SER A 194 -114.29 60.86
REMARK 500 PHE A 317 69.68 -113.19
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 CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 408
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-419709 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT (RESIDUES 20-341) 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 4Q34 A 20 341 UNP A6LCA7 A6LCA7_PARD8 20 341
SEQADV 4Q34 GLY A 0 UNP A6LCA7 LEADER SEQUENCE
SEQRES 1 A 323 GLY ASP GLU ARG VAL LEU MSE VAL ASP GLU GLN GLY SER
SEQRES 2 A 323 PHE ALA VAL GLY GLY THR VAL LEU VAL ASP SER LEU GLY
SEQRES 3 A 323 HIS THR PHE HIS GLY ASP HIS ALA TYR VAL PHE TYR GLN
SEQRES 4 A 323 LYS PRO VAL GLY ALA ARG LYS TYR PRO LEU VAL PHE ALA
SEQRES 5 A 323 HIS GLY VAL GLY GLN PHE SER LYS THR TRP GLU THR THR
SEQRES 6 A 323 PRO ASP GLY ARG GLU GLY PHE GLN ASN ILE PHE LEU ARG
SEQRES 7 A 323 ARG ARG PHE CYS VAL TYR LEU VAL ASP GLN PRO ARG ARG
SEQRES 8 A 323 GLY ASN ALA GLY ARG GLY THR GLU SER VAL THR ILE SER
SEQRES 9 A 323 PRO ALA PHE ASP GLU GLU VAL TRP PHE ASN ARG PHE ARG
SEQRES 10 A 323 VAL GLY ILE TRP PRO ASP TYR PHE GLU GLY VAL GLN PHE
SEQRES 11 A 323 LYS ARG ASP LYS GLU THR LEU ASP GLN TYR PHE ARG GLN
SEQRES 12 A 323 MSE THR PRO THR ILE GLY THR THR ASP PHE GLU VAL TYR
SEQRES 13 A 323 SER ASP ALA TYR ALA ALA LEU PHE ASP LYS ILE GLY PRO
SEQRES 14 A 323 GLY VAL PHE ILE THR HIS SER GLN GLY GLY PRO VAL GLY
SEQRES 15 A 323 TRP ASN THR LEU LEU LYS THR ARG ASN ILE LYS ALA ILE
SEQRES 16 A 323 ALA SER TYR GLU PRO GLY GLY ALA VAL PRO PHE PRO GLU
SEQRES 17 A 323 GLY GLN LEU PRO GLU GLU ALA LYS PHE ILE THR LEU SER
SEQRES 18 A 323 LYS LYS MSE GLU GLY ILE GLU VAL PRO MSE SER VAL PHE
SEQRES 19 A 323 MSE GLU TYR THR LYS VAL PRO ILE VAL ILE TYR TYR GLY
SEQRES 20 A 323 ASP ASN LEU PRO GLU THR ASP GLU ARG PRO GLU LEU TYR
SEQRES 21 A 323 GLU TRP THR ARG ARG LEU ARG LEU MSE LYS ILE TRP ALA
SEQRES 22 A 323 LYS MSE LEU ASN ASP GLN GLY GLY ASP VAL THR VAL ILE
SEQRES 23 A 323 HIS LEU PRO GLU VAL GLY LEU HIS GLY ASN THR HIS PHE
SEQRES 24 A 323 PRO MSE SER ASP LEU ASN ASN ILE GLU VAL ALA ASP LEU
SEQRES 25 A 323 LEU SER GLU TRP LEU HIS THR LYS ALA LEU ASP
MODRES 4Q34 MSE A 25 MET SELENOMETHIONINE
MODRES 4Q34 MSE A 162 MET SELENOMETHIONINE
MODRES 4Q34 MSE A 242 MET SELENOMETHIONINE
MODRES 4Q34 MSE A 249 MET SELENOMETHIONINE
MODRES 4Q34 MSE A 253 MET SELENOMETHIONINE
MODRES 4Q34 MSE A 287 MET SELENOMETHIONINE
MODRES 4Q34 MSE A 293 MET SELENOMETHIONINE
MODRES 4Q34 MSE A 319 MET SELENOMETHIONINE
HET MSE A 25 13
HET MSE A 162 13
HET MSE A 242 13
HET MSE A 249 8
HET MSE A 253 8
HET MSE A 287 8
HET MSE A 293 8
HET MSE A 319 8
HET CL A 401 1
HET CL A 402 1
HET CL A 403 1
HET GOL A 404 6
HET GOL A 405 6
HET GOL A 406 6
HET GOL A 407 6
HET GOL A 408 6
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 CL 3(CL 1-)
FORMUL 5 GOL 5(C3 H8 O3)
FORMUL 10 HOH *322(H2 O)
HELIX 1 1 PHE A 76 GLU A 81 5 6
HELIX 2 2 GLY A 89 ARG A 97 1 9
HELIX 3 3 ARG A 109 GLY A 113 5 5
HELIX 4 4 ASP A 126 PHE A 134 1 9
HELIX 5 5 ASP A 151 GLN A 161 1 11
HELIX 6 6 ASP A 170 GLY A 186 1 17
HELIX 7 7 GLN A 195 LEU A 204 1 10
HELIX 8 8 LEU A 205 THR A 207 5 3
HELIX 9 9 PRO A 230 LYS A 234 5 5
HELIX 10 10 PRO A 248 MSE A 253 1 6
HELIX 11 11 GLU A 254 LYS A 257 5 4
HELIX 12 12 ARG A 274 ASP A 296 1 23
HELIX 13 13 PRO A 307 GLY A 310 5 4
HELIX 14 14 ASN A 323 LYS A 338 1 16
SHEET 1 A 8 VAL A 26 VAL A 34 0
SHEET 2 A 8 ALA A 52 PRO A 59 -1 O LYS A 58 N GLU A 28
SHEET 3 A 8 VAL A 101 ASP A 105 -1 O LEU A 103 N PHE A 55
SHEET 4 A 8 LEU A 67 ALA A 70 1 N LEU A 67 O TYR A 102
SHEET 5 A 8 GLY A 188 HIS A 193 1 O ILE A 191 N VAL A 68
SHEET 6 A 8 ILE A 210 TYR A 216 1 O LYS A 211 N GLY A 188
SHEET 7 A 8 ILE A 260 TYR A 264 1 O VAL A 261 N SER A 215
SHEET 8 A 8 VAL A 301 HIS A 305 1 O ILE A 304 N ILE A 262
SHEET 1 B 2 THR A 37 VAL A 40 0
SHEET 2 B 2 THR A 46 GLY A 49 -1 O PHE A 47 N LEU A 39
SHEET 1 C 2 GLY A 137 ILE A 138 0
SHEET 2 C 2 ASP A 141 TYR A 142 -1 O ASP A 141 N ILE A 138
SHEET 1 D 2 VAL A 222 PRO A 225 0
SHEET 2 D 2 GLY A 244 VAL A 247 1 O ILE A 245 N PHE A 224
LINK C LEU A 24 N MSE A 25 1555 1555 1.33
LINK C MSE A 25 N VAL A 26 1555 1555 1.32
LINK C GLN A 161 N MSE A 162 1555 1555 1.34
LINK C MSE A 162 N THR A 163 1555 1555 1.33
LINK C LYS A 241 N MSE A 242 1555 1555 1.34
LINK C MSE A 242 N GLU A 243 1555 1555 1.34
LINK C PRO A 248 N MSE A 249 1555 1555 1.33
LINK C MSE A 249 N SER A 250 1555 1555 1.33
LINK C PHE A 252 N MSE A 253 1555 1555 1.34
LINK C MSE A 253 N GLU A 254 1555 1555 1.34
LINK C LEU A 286 N MSE A 287 1555 1555 1.33
LINK C MSE A 287 N LYS A 288 1555 1555 1.34
LINK C LYS A 292 N MSE A 293 1555 1555 1.33
LINK C MSE A 293 N LEU A 294 1555 1555 1.33
LINK C PRO A 318 N MSE A 319 1555 1555 1.32
LINK C MSE A 319 N SER A 320 1555 1555 1.35
CISPEP 1 TRP A 139 PRO A 140 0 6.37
SITE 1 AC1 2 ARG A 133 GLN A 195
SITE 1 AC2 2 LYS A 149 ARG A 150
SITE 1 AC3 4 ASN A 132 ARG A 274 HOH A 613 HOH A 631
SITE 1 AC4 6 TYR A 53 PHE A 55 GLU A 81 GLN A 91
SITE 2 AC4 6 LEU A 103 HOH A 514
SITE 1 AC5 4 ASP A 126 VAL A 129 ARG A 133 GLU A 276
SITE 1 AC6 7 LEU A 204 THR A 207 ARG A 208 ASN A 209
SITE 2 AC6 7 ILE A 210 LYS A 257 HOH A 671
SITE 1 AC7 10 GLY A 35 GLY A 36 VAL A 38 ASP A 156
SITE 2 AC7 10 ARG A 160 ASN A 295 HOH A 617 HOH A 670
SITE 3 AC7 10 HOH A 679 HOH A 722
SITE 1 AC8 4 PHE A 32 LYS A 58 TYR A 102 LYS A 184
CRYST1 59.327 59.327 209.591 90.00 90.00 90.00 P 41 21 2 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 0.016856 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016856 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004771 0.00000
TER 2694 ASP A 341
MASTER 406 0 16 14 14 0 12 6 2927 1 125 25
END |