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HEADER HYDROLASE 24-NOV-19 6TJ2
TITLE EXTRACELLULAR ALPHA/BETA-HYDROLASE FROM PAENIBACILLUS SPECIES SHARES
TITLE 2 STRUCTURAL AND FUNCTIONAL HOMOLOGY TO TOBACCO SALICYLIC ACID BINDING
TITLE 3 PROTEIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PAENIBACILLUS SP. VTT E-133280;
SOURCE 3 ORGANISM_TAXID: 1986222;
SOURCE 4 GENE: CA600_10415;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA-HYDROLASE, METHYL SALICYLATE ESTERASE, PAENIBACILLUS,
KEYWDS 2 RHIZOSPHERE, SABP2, SALICYLIC ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.FULOP,R.C.WILKINSON
REVDAT 1 22-APR-20 6TJ2 0
JRNL AUTH R.C.WILKINSON,R.RAHMAN POUR,S.JAMSHIDI,V.FULOP,T.D.H.BUGG
JRNL TITL EXTRACELLULAR ALPHA/BETA-HYDROLASE FROM PAENIBACILLUS
JRNL TITL 2 SPECIES SHARES STRUCTURAL AND FUNCTIONAL HOMOLOGY TO TOBACCO
JRNL TITL 3 SALICYLIC ACID BINDING PROTEIN 2.
JRNL REF J.STRUCT.BIOL. 07496 2020
JRNL REFN ESSN 1095-8657
JRNL PMID 32224091
JRNL DOI 10.1016/J.JSB.2020.107496
REMARK 2
REMARK 2 RESOLUTION. 1.32 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.32
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 153475
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6430
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) : 1.32
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.35
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10113
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 449
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5762
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 667
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : -0.56000
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): 0.048
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.050
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.824
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5938 ; 0.015 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5403 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8063 ; 1.930 ; 1.651
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12591 ; 1.555 ; 1.573
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 729 ; 6.238 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 297 ;32.273 ;23.131
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 970 ;11.530 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;17.222 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 774 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6632 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1252 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6TJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-NOV-19.
REMARK 100 THE DEPOSITION ID IS D_1292105096.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 159905
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.320
REMARK 200 RESOLUTION RANGE LOW (A) : 57.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : 0.05900
REMARK 200 FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.73900
REMARK 200 R SYM FOR SHELL (I) : 0.73900
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 3DQZ
REMARK 200
REMARK 200 REMARK: ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 31.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FLUORIDE, 20% PEG 3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
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 23.93000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.42500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.21500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.42500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.93000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.21500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 MET A -31
REMARK 465 LYS A -30
REMARK 465 SER A -29
REMARK 465 ILE A -28
REMARK 465 HIS A -27
REMARK 465 ILE A -26
REMARK 465 LYS A -25
REMARK 465 ILE A -24
REMARK 465 VAL A -23
REMARK 465 LEU A -22
REMARK 465 ALA A -21
REMARK 465 LEU A -20
REMARK 465 CYS A -19
REMARK 465 ILE A -18
REMARK 465 SER A -17
REMARK 465 ILE A -16
REMARK 465 PHE A -15
REMARK 465 THR A -14
REMARK 465 ILE A -13
REMARK 465 MET A -12
REMARK 465 GLY A -11
REMARK 465 LEU A -10
REMARK 465 GLN A -9
REMARK 465 PRO A -8
REMARK 465 LEU A -7
REMARK 465 ASN A -6
REMARK 465 GLN A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 THR A -2
REMARK 465 VAL A -1
REMARK 465 ALA A 0
REMARK 465 ALA A 1
REMARK 465 ALA A 2
REMARK 465 ASN A 3
REMARK 465 HIS A 4
REMARK 465 LYS A 5
REMARK 465 SER A 6
REMARK 465 SER A 7
REMARK 465 THR A 8
REMARK 465 LYS A 9
REMARK 465 GLN A 10
REMARK 465 MET B -31
REMARK 465 LYS B -30
REMARK 465 SER B -29
REMARK 465 ILE B -28
REMARK 465 HIS B -27
REMARK 465 ILE B -26
REMARK 465 LYS B -25
REMARK 465 ILE B -24
REMARK 465 VAL B -23
REMARK 465 LEU B -22
REMARK 465 ALA B -21
REMARK 465 LEU B -20
REMARK 465 CYS B -19
REMARK 465 ILE B -18
REMARK 465 SER B -17
REMARK 465 ILE B -16
REMARK 465 PHE B -15
REMARK 465 THR B -14
REMARK 465 ILE B -13
REMARK 465 MET B -12
REMARK 465 GLY B -11
REMARK 465 LEU B -10
REMARK 465 GLN B -9
REMARK 465 PRO B -8
REMARK 465 LEU B -7
REMARK 465 ASN B -6
REMARK 465 GLN B -5
REMARK 465 HIS B -4
REMARK 465 SER B -3
REMARK 465 THR B -2
REMARK 465 VAL B -1
REMARK 465 ALA B 0
REMARK 465 ALA B 1
REMARK 465 ALA B 2
REMARK 465 ASN B 3
REMARK 465 HIS B 4
REMARK 465 LYS B 5
REMARK 465 SER B 6
REMARK 465 SER B 7
REMARK 465 THR B 8
REMARK 465 LYS B 9
REMARK 465 GLN B 10
REMARK 465 MET C -31
REMARK 465 LYS C -30
REMARK 465 SER C -29
REMARK 465 ILE C -28
REMARK 465 HIS C -27
REMARK 465 ILE C -26
REMARK 465 LYS C -25
REMARK 465 ILE C -24
REMARK 465 VAL C -23
REMARK 465 LEU C -22
REMARK 465 ALA C -21
REMARK 465 LEU C -20
REMARK 465 CYS C -19
REMARK 465 ILE C -18
REMARK 465 SER C -17
REMARK 465 ILE C -16
REMARK 465 PHE C -15
REMARK 465 THR C -14
REMARK 465 ILE C -13
REMARK 465 MET C -12
REMARK 465 GLY C -11
REMARK 465 LEU C -10
REMARK 465 GLN C -9
REMARK 465 PRO C -8
REMARK 465 LEU C -7
REMARK 465 ASN C -6
REMARK 465 GLN C -5
REMARK 465 HIS C -4
REMARK 465 SER C -3
REMARK 465 THR C -2
REMARK 465 VAL C -1
REMARK 465 ALA C 0
REMARK 465 ALA C 1
REMARK 465 ALA C 2
REMARK 465 ASN C 3
REMARK 465 HIS C 4
REMARK 465 LYS C 5
REMARK 465 SER C 6
REMARK 465 SER C 7
REMARK 465 THR C 8
REMARK 465 LYS C 9
REMARK 465 GLN C 10
REMARK 465 THR C 11
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 227 CD GLU A 227 OE2 -0.078
REMARK 500 GLU B 227 CD GLU B 227 OE2 -0.066
REMARK 500 GLU C 34 CD GLU C 34 OE2 -0.067
REMARK 500 GLU C 227 CD GLU C 227 OE1 -0.082
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 NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 104 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG B 104 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 GLN C 96 CB - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 ARG C 101 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG C 104 NE - CZ - NH1 ANGL. DEV. = 6.4 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 ASN A 55 88.82 -157.58
REMARK 500 SER A 85 -127.50 49.69
REMARK 500 ASN A 140 20.25 -140.00
REMARK 500 ASN B 55 88.65 -153.99
REMARK 500 ASN B 55 88.65 -163.43
REMARK 500 SER B 85 -123.17 60.28
REMARK 500 SER B 85 -130.38 40.61
REMARK 500 ASN B 140 24.24 -140.54
REMARK 500 SER C 85 -128.80 48.49
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 537 DISTANCE = 6.19 ANGSTROMS
DBREF1 6TJ2 A -31 253 UNP A0A264DUQ2_9BACL
DBREF2 6TJ2 A A0A264DUQ2 1 285
DBREF1 6TJ2 B -31 253 UNP A0A264DUQ2_9BACL
DBREF2 6TJ2 B A0A264DUQ2 1 285
DBREF1 6TJ2 C -31 253 UNP A0A264DUQ2_9BACL
DBREF2 6TJ2 C A0A264DUQ2 1 285
SEQRES 1 A 285 MET LYS SER ILE HIS ILE LYS ILE VAL LEU ALA LEU CYS
SEQRES 2 A 285 ILE SER ILE PHE THR ILE MET GLY LEU GLN PRO LEU ASN
SEQRES 3 A 285 GLN HIS SER THR VAL ALA ALA ALA ASN HIS LYS SER SER
SEQRES 4 A 285 THR LYS GLN THR PRO LEU THR PHE VAL LEU ILE HIS GLY
SEQRES 5 A 285 SER TRP ALA THR ALA GLY PHE TRP ASP GLU THR ALA SER
SEQRES 6 A 285 GLU LEU ARG LYS LEU GLY HIS THR VAL TYR THR PRO GLU
SEQRES 7 A 285 TYR ALA GLY HIS GLY ALA ASP LYS ASN ASN ASN VAL THR
SEQRES 8 A 285 HIS GLU GLN ILE THR LYS SER VAL VAL ASP TYR ILE LYS
SEQRES 9 A 285 GLN LYS ASP LEU LYS ASP PHE ILE LEU LEU GLY HIS SER
SEQRES 10 A 285 PHE GLY GLY SER VAL ILE GLN THR VAL SER GLN GLN VAL
SEQRES 11 A 285 PRO ASP ARG ILE LYS ARG ILE VAL PHE PHE ASP ALA PHE
SEQRES 12 A 285 ALA PRO LEU ASP GLY GLN SER VAL ALA ASP GLN PHE PRO
SEQRES 13 A 285 ALA GLU SER LEU LYS SER PHE GLU GLN LEU ARG ASP ALA
SEQRES 14 A 285 SER GLY ASN ASN THR ILE THR LEU PRO PHE PRO LEU PHE
SEQRES 15 A 285 ARG ASP THR PHE VAL ASN THR ALA SER LEU ALA GLN ALA
SEQRES 16 A 285 GLN ALA PHE TYR LYS GLN ALA PRO PRO GLU PRO ALA THR
SEQRES 17 A 285 PRO LEU PHE GLU LYS LEU ASP LEU LYS LYS PHE TYR SER
SEQRES 18 A 285 LEU GLN ILE PRO LYS SER TYR LEU TYR LEU THR GLU ASP
SEQRES 19 A 285 THR ALA ILE PRO GLN GLY PRO TYR GLY PHE HIS PRO THR
SEQRES 20 A 285 GLN SER SER HIS LEU GLY VAL PHE ARG PHE ILE GLU GLY
SEQRES 21 A 285 LYS GLY ASP HIS MET THR THR VAL ARG THR GLU PRO LYS
SEQRES 22 A 285 MET MET ALA GLU LEU MET VAL LYS ALA GLY ARG ASP
SEQRES 1 B 285 MET LYS SER ILE HIS ILE LYS ILE VAL LEU ALA LEU CYS
SEQRES 2 B 285 ILE SER ILE PHE THR ILE MET GLY LEU GLN PRO LEU ASN
SEQRES 3 B 285 GLN HIS SER THR VAL ALA ALA ALA ASN HIS LYS SER SER
SEQRES 4 B 285 THR LYS GLN THR PRO LEU THR PHE VAL LEU ILE HIS GLY
SEQRES 5 B 285 SER TRP ALA THR ALA GLY PHE TRP ASP GLU THR ALA SER
SEQRES 6 B 285 GLU LEU ARG LYS LEU GLY HIS THR VAL TYR THR PRO GLU
SEQRES 7 B 285 TYR ALA GLY HIS GLY ALA ASP LYS ASN ASN ASN VAL THR
SEQRES 8 B 285 HIS GLU GLN ILE THR LYS SER VAL VAL ASP TYR ILE LYS
SEQRES 9 B 285 GLN LYS ASP LEU LYS ASP PHE ILE LEU LEU GLY HIS SER
SEQRES 10 B 285 PHE GLY GLY SER VAL ILE GLN THR VAL SER GLN GLN VAL
SEQRES 11 B 285 PRO ASP ARG ILE LYS ARG ILE VAL PHE PHE ASP ALA PHE
SEQRES 12 B 285 ALA PRO LEU ASP GLY GLN SER VAL ALA ASP GLN PHE PRO
SEQRES 13 B 285 ALA GLU SER LEU LYS SER PHE GLU GLN LEU ARG ASP ALA
SEQRES 14 B 285 SER GLY ASN ASN THR ILE THR LEU PRO PHE PRO LEU PHE
SEQRES 15 B 285 ARG ASP THR PHE VAL ASN THR ALA SER LEU ALA GLN ALA
SEQRES 16 B 285 GLN ALA PHE TYR LYS GLN ALA PRO PRO GLU PRO ALA THR
SEQRES 17 B 285 PRO LEU PHE GLU LYS LEU ASP LEU LYS LYS PHE TYR SER
SEQRES 18 B 285 LEU GLN ILE PRO LYS SER TYR LEU TYR LEU THR GLU ASP
SEQRES 19 B 285 THR ALA ILE PRO GLN GLY PRO TYR GLY PHE HIS PRO THR
SEQRES 20 B 285 GLN SER SER HIS LEU GLY VAL PHE ARG PHE ILE GLU GLY
SEQRES 21 B 285 LYS GLY ASP HIS MET THR THR VAL ARG THR GLU PRO LYS
SEQRES 22 B 285 MET MET ALA GLU LEU MET VAL LYS ALA GLY ARG ASP
SEQRES 1 C 285 MET LYS SER ILE HIS ILE LYS ILE VAL LEU ALA LEU CYS
SEQRES 2 C 285 ILE SER ILE PHE THR ILE MET GLY LEU GLN PRO LEU ASN
SEQRES 3 C 285 GLN HIS SER THR VAL ALA ALA ALA ASN HIS LYS SER SER
SEQRES 4 C 285 THR LYS GLN THR PRO LEU THR PHE VAL LEU ILE HIS GLY
SEQRES 5 C 285 SER TRP ALA THR ALA GLY PHE TRP ASP GLU THR ALA SER
SEQRES 6 C 285 GLU LEU ARG LYS LEU GLY HIS THR VAL TYR THR PRO GLU
SEQRES 7 C 285 TYR ALA GLY HIS GLY ALA ASP LYS ASN ASN ASN VAL THR
SEQRES 8 C 285 HIS GLU GLN ILE THR LYS SER VAL VAL ASP TYR ILE LYS
SEQRES 9 C 285 GLN LYS ASP LEU LYS ASP PHE ILE LEU LEU GLY HIS SER
SEQRES 10 C 285 PHE GLY GLY SER VAL ILE GLN THR VAL SER GLN GLN VAL
SEQRES 11 C 285 PRO ASP ARG ILE LYS ARG ILE VAL PHE PHE ASP ALA PHE
SEQRES 12 C 285 ALA PRO LEU ASP GLY GLN SER VAL ALA ASP GLN PHE PRO
SEQRES 13 C 285 ALA GLU SER LEU LYS SER PHE GLU GLN LEU ARG ASP ALA
SEQRES 14 C 285 SER GLY ASN ASN THR ILE THR LEU PRO PHE PRO LEU PHE
SEQRES 15 C 285 ARG ASP THR PHE VAL ASN THR ALA SER LEU ALA GLN ALA
SEQRES 16 C 285 GLN ALA PHE TYR LYS GLN ALA PRO PRO GLU PRO ALA THR
SEQRES 17 C 285 PRO LEU PHE GLU LYS LEU ASP LEU LYS LYS PHE TYR SER
SEQRES 18 C 285 LEU GLN ILE PRO LYS SER TYR LEU TYR LEU THR GLU ASP
SEQRES 19 C 285 THR ALA ILE PRO GLN GLY PRO TYR GLY PHE HIS PRO THR
SEQRES 20 C 285 GLN SER SER HIS LEU GLY VAL PHE ARG PHE ILE GLU GLY
SEQRES 21 C 285 LYS GLY ASP HIS MET THR THR VAL ARG THR GLU PRO LYS
SEQRES 22 C 285 MET MET ALA GLU LEU MET VAL LYS ALA GLY ARG ASP
FORMUL 4 HOH *667(H2 O)
HELIX 1 AA1 THR A 24 PHE A 27 5 4
HELIX 2 AA2 TRP A 28 LEU A 38 1 11
HELIX 3 AA3 THR A 59 LYS A 74 1 16
HELIX 4 AA4 PHE A 86 VAL A 98 1 13
HELIX 5 AA5 VAL A 119 PHE A 123 5 5
HELIX 6 AA6 PRO A 124 GLY A 139 1 16
HELIX 7 AA7 PRO A 146 PHE A 154 1 9
HELIX 8 AA8 SER A 159 GLN A 169 1 11
HELIX 9 AA9 ALA A 175 GLU A 180 1 6
HELIX 10 AB1 LEU A 184 LEU A 190 1 7
HELIX 11 AB2 PRO A 214 HIS A 219 1 6
HELIX 12 AB3 THR A 234 GLU A 239 1 6
HELIX 13 AB4 GLU A 239 ARG A 252 1 14
HELIX 14 AB5 THR B 24 PHE B 27 5 4
HELIX 15 AB6 TRP B 28 LEU B 38 1 11
HELIX 16 AB7 THR B 59 ASP B 75 1 17
HELIX 17 AB8 PHE B 86 VAL B 98 1 13
HELIX 18 AB9 VAL B 119 PHE B 123 5 5
HELIX 19 AC1 PRO B 124 GLY B 139 1 16
HELIX 20 AC2 PRO B 146 PHE B 154 1 9
HELIX 21 AC3 SER B 159 LYS B 168 1 10
HELIX 22 AC4 ALA B 175 GLU B 180 1 6
HELIX 23 AC5 LEU B 184 LEU B 190 1 7
HELIX 24 AC6 PRO B 214 HIS B 219 1 6
HELIX 25 AC7 THR B 234 GLU B 239 1 6
HELIX 26 AC8 GLU B 239 ARG B 252 1 14
HELIX 27 AC9 THR C 24 PHE C 27 5 4
HELIX 28 AD1 TRP C 28 LEU C 38 1 11
HELIX 29 AD2 THR C 59 LYS C 74 1 16
HELIX 30 AD3 PHE C 86 VAL C 98 1 13
HELIX 31 AD4 VAL C 119 PHE C 123 5 5
HELIX 32 AD5 PRO C 124 GLY C 139 1 16
HELIX 33 AD6 PRO C 146 PHE C 154 1 9
HELIX 34 AD7 SER C 159 GLN C 169 1 11
HELIX 35 AD8 ALA C 175 GLU C 180 1 6
HELIX 36 AD9 LEU C 184 LEU C 190 1 7
HELIX 37 AE1 PRO C 214 HIS C 219 1 6
HELIX 38 AE2 THR C 234 GLU C 239 1 6
HELIX 39 AE3 GLU C 239 ARG C 252 1 14
SHEET 1 AA1 6 THR A 41 TYR A 43 0
SHEET 2 AA1 6 THR A 14 ILE A 18 1 N LEU A 17 O TYR A 43
SHEET 3 AA1 6 PHE A 79 SER A 85 1 O ILE A 80 N THR A 14
SHEET 4 AA1 6 ILE A 102 ALA A 110 1 O PHE A 108 N GLY A 83
SHEET 5 AA1 6 LYS A 194 LEU A 199 1 O SER A 195 N PHE A 107
SHEET 6 AA1 6 ARG A 224 GLY A 228 1 O ARG A 224 N TYR A 196
SHEET 1 AA2 2 THR A 142 ILE A 143 0
SHEET 2 AA2 2 GLU A 173 PRO A 174 -1 O GLU A 173 N ILE A 143
SHEET 1 AA3 6 THR B 41 TYR B 43 0
SHEET 2 AA3 6 THR B 14 ILE B 18 1 N PHE B 15 O THR B 41
SHEET 3 AA3 6 PHE B 79 SER B 85 1 O ILE B 80 N THR B 14
SHEET 4 AA3 6 ILE B 102 ALA B 110 1 O PHE B 108 N GLY B 83
SHEET 5 AA3 6 LYS B 194 LEU B 199 1 O SER B 195 N PHE B 107
SHEET 6 AA3 6 ARG B 224 GLY B 228 1 O GLY B 228 N TYR B 198
SHEET 1 AA4 2 THR B 142 ILE B 143 0
SHEET 2 AA4 2 GLU B 173 PRO B 174 -1 O GLU B 173 N ILE B 143
SHEET 1 AA5 6 THR C 41 TYR C 43 0
SHEET 2 AA5 6 THR C 14 ILE C 18 1 N LEU C 17 O TYR C 43
SHEET 3 AA5 6 PHE C 79 SER C 85 1 O ILE C 80 N THR C 14
SHEET 4 AA5 6 ILE C 102 ALA C 110 1 O PHE C 108 N GLY C 83
SHEET 5 AA5 6 LYS C 194 LEU C 199 1 O SER C 195 N PHE C 107
SHEET 6 AA5 6 ARG C 224 GLY C 228 1 O ILE C 226 N TYR C 198
SHEET 1 AA6 2 THR C 142 ILE C 143 0
SHEET 2 AA6 2 GLU C 173 PRO C 174 -1 O GLU C 173 N ILE C 143
CISPEP 1 HIS A 213 PRO A 214 0 6.65
CISPEP 2 HIS B 213 PRO B 214 0 3.53
CISPEP 3 HIS C 213 PRO C 214 0 6.59
CRYST1 47.860 112.430 126.850 90.00 90.00 90.00 P 21 21 21 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 0.020894 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008894 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007883 0.00000
TER 1924 ASP A 253
TER 3863 ASP B 253
TER 5780 ASP C 253
MASTER 459 0 0 39 24 0 0 6 6429 3 0 66
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