| content |
HEADER HYDROLASE 02-OCT-10 2XT0
TITLE DEHALOGENASE DPPA FROM PLESIOCYSTIS PACIFICA SIR-I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DPPA DEHALOGENASE;
COMPND 5 EC: 3.8.1.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLESIOCYSTIS PACIFICA;
SOURCE 3 ORGANISM_TAXID: 191768;
SOURCE 4 STRAIN: SIR-I;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS HYDROLASE, ALPHA-BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR X.BOGDANOVIC,G.J.PALM,W.HINRICHS
REVDAT 1 10-AUG-11 2XT0 0
JRNL AUTH M.HESSELER,X.BOGDANOVIC,A.HIDALGO,J.BERENGUER,G.J.PALM,
JRNL AUTH 2 W.HINRICHS,U.T.BORNSCHEUER
JRNL TITL CLONING, FUNCTIONAL EXPRESSION, BIOCHEMICAL
JRNL TITL 2 CHARACTERIZATION, AND STRUCTURAL ANALYSIS OF A HALOALKANE
JRNL TITL 3 DEHALOGENASE FROM PLESIOCYSTIS PACIFICA SIR-1.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. V. 91 1049 2011
JRNL REFN ISSN 0175-7598
JRNL PMID 21603934
JRNL DOI 10.1007/S00253-011-3328-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.BOGDANOVIC,M.HESSELER,G.J.PALM,U.T.BORNSCHEUER,W.HINRICHS
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES
REMARK 1 TITL 2 OF THE PUTATIVE HALOALKANE DEHALOGENASE DPPA FROM
REMARK 1 TITL 3 PLESIOCYSTIS PACIFICA SIR-I.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 66 828 2010
REMARK 1 REFN ISSN 1744-3091
REMARK 1 PMID 20606284
REMARK 1 DOI 10.1107/S1744309110018932
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.04
REMARK 3 NUMBER OF REFLECTIONS : 25826
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) : 0.22081
REMARK 3 R VALUE (WORKING SET) : 0.21931
REMARK 3 FREE R VALUE : 0.24801
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1375
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) : 1.900
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.949
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1775
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.456
REMARK 3 BIN FREE R VALUE SET COUNT : 84
REMARK 3 BIN FREE R VALUE : 0.511
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2311
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.519
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14
REMARK 3 B22 (A**2) : -0.21
REMARK 3 B33 (A**2) : 0.06
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.176
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.419
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2399 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1649 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3271 ; 1.854 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3983 ; 1.085 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 300 ; 6.827 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 111 ;28.324 ;22.883
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 354 ;13.979 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;15.600 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 339 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2712 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 519 ; 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): 1487 ; 1.072 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 599 ; 0.362 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2389 ; 1.638 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 912 ; 2.729 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 880 ; 4.039 ; 4.500
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 1 A 164
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4973 18.9705 51.5628
REMARK 3 T TENSOR
REMARK 3 T11: 0.0802 T22: 0.0692
REMARK 3 T33: 0.0980 T12: 0.0023
REMARK 3 T13: -0.0057 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.9713 L22: 1.2971
REMARK 3 L33: 1.8347 L12: 0.4181
REMARK 3 L13: 0.0754 L23: -0.1812
REMARK 3 S TENSOR
REMARK 3 S11: 0.0066 S12: -0.0242 S13: -0.0537
REMARK 3 S21: 0.0508 S22: -0.0321 S23: -0.0864
REMARK 3 S31: 0.0525 S32: 0.1436 S33: 0.0255
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 : A 165 A 226
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1078 22.7121 41.8150
REMARK 3 T TENSOR
REMARK 3 T11: 0.1163 T22: 0.1175
REMARK 3 T33: 0.1195 T12: 0.0097
REMARK 3 T13: 0.0031 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 1.0721 L22: 0.5047
REMARK 3 L33: 1.5888 L12: 0.2813
REMARK 3 L13: 0.4809 L23: -0.7106
REMARK 3 S TENSOR
REMARK 3 S11: -0.0697 S12: 0.0553 S13: 0.0413
REMARK 3 S21: -0.0002 S22: 0.0559 S23: 0.0422
REMARK 3 S31: -0.0647 S32: -0.0758 S33: 0.0137
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 : A 227 A 297
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1684 12.5626 60.9103
REMARK 3 T TENSOR
REMARK 3 T11: 0.1347 T22: 0.1353
REMARK 3 T33: 0.1250 T12: -0.0416
REMARK 3 T13: -0.0024 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 1.5813 L22: 3.4567
REMARK 3 L33: 1.7886 L12: -0.8090
REMARK 3 L13: -0.7912 L23: 0.8611
REMARK 3 S TENSOR
REMARK 3 S11: 0.0694 S12: -0.0886 S13: -0.2179
REMARK 3 S21: 0.1952 S22: -0.1376 S23: 0.3050
REMARK 3 S31: 0.1590 S32: -0.1369 S33: 0.0683
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 WITH TLS ADDED. THE NUMBER OF UNIQUE
REMARK 3 REFLECTIONS FOR REFINEMENT IS 25826 AND FOR DATA PROCESSING 25613.
REMARK 3 THIS IS DUE TO A DIFFERENT RESOLUTION USED FOR REFINEMENT (1.9 A)
REMARK 3 AND PROCESSING (1.95 A).
REMARK 4
REMARK 4 2XT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-10.
REMARK 100 THE PDBE ID CODE IS EBI-45648.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX 007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MULTILAYER OPTIC
REMARK 200 OPTICS : OSMIC MULTILAYER OPTIC
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (SATURN92)
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR V.1.3.6
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR V.1.3.6
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25613
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.95
REMARK 200 RESOLUTION RANGE LOW (A) : 38.68
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 5.5
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.1
REMARK 200 R MERGE FOR SHELL (I) : 0.44
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1EDB
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.8M (NH4)2SO4,
REMARK 280 5% PEG400
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 23.63100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.25050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.63100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.25050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.5 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 -1.000000 0.000000 0.000000 47.26200
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 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 O HOH A 2161 O HOH A 2242 1.97
REMARK 500 O HOH A 2236 O HOH A 2240 2.01
REMARK 500 O HOH A 2088 O HOH A 2186 2.03
REMARK 500 NH2 ARG A 209 O HOH A 2206 2.14
REMARK 500 O HOH A 2038 O HOH A 2087 2.16
REMARK 500 O HOH A 2144 O HOH A 2160 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 ALA A 94 CA ALA A 94 CB 0.144
REMARK 500 GLU A 255 CB GLU A 255 CG 0.125
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 LEU A 66 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG A 227 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 227 NE - CZ - NH2 ANGL. DEV. = -3.7 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 PRO A 56 63.88 -108.41
REMARK 500 SER A 57 -167.87 -108.78
REMARK 500 ASP A 123 -132.89 43.55
REMARK 500 ASN A 147 102.58 -25.13
REMARK 500 LEU A 173 118.86 -37.37
REMARK 500 VAL A 251 -68.14 -127.23
REMARK 500 LEU A 252 41.29 -103.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 13 LEU A 14 -144.54
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 SO4 A1298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1301
DBREF 2XT0 A 1 297 UNP A6G7B1 A6G7B1_9DELT 1 297
SEQADV 2XT0 ARG A 265 UNP A6G7B1 GLY 265 CLONING ARTIFACT
SEQRES 1 A 297 MET GLU PHE VAL ARG THR PRO ASP ASP ARG PHE ALA ASP
SEQRES 2 A 297 LEU PRO ASP PHE PRO TYR ALA PRO HIS TYR LEU GLU GLY
SEQRES 3 A 297 LEU PRO GLY PHE GLU GLY LEU ARG MET HIS TYR VAL ASP
SEQRES 4 A 297 GLU GLY PRO ARG ASP ALA GLU HIS THR PHE LEU CYS LEU
SEQRES 5 A 297 HIS GLY GLU PRO SER TRP SER PHE LEU TYR ARG LYS MET
SEQRES 6 A 297 LEU PRO VAL PHE THR ALA ALA GLY GLY ARG VAL VAL ALA
SEQRES 7 A 297 PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS PRO THR
SEQRES 8 A 297 ASP ASP ALA VAL TYR THR PHE GLY PHE HIS ARG ARG SER
SEQRES 9 A 297 LEU LEU ALA PHE LEU ASP ALA LEU GLN LEU GLU ARG VAL
SEQRES 10 A 297 THR LEU VAL CYS GLN ASP TRP GLY GLY ILE LEU GLY LEU
SEQRES 11 A 297 THR LEU PRO VAL ASP ARG PRO GLN LEU VAL ASP ARG LEU
SEQRES 12 A 297 ILE VAL MET ASN THR ALA LEU ALA VAL GLY LEU SER PRO
SEQRES 13 A 297 GLY LYS GLY PHE GLU SER TRP ARG ASP PHE VAL ALA ASN
SEQRES 14 A 297 SER PRO ASP LEU ASP VAL GLY LYS LEU MET GLN ARG ALA
SEQRES 15 A 297 ILE PRO GLY ILE THR ASP ALA GLU VAL ALA ALA TYR ASP
SEQRES 16 A 297 ALA PRO PHE PRO GLY PRO GLU PHE LYS ALA GLY VAL ARG
SEQRES 17 A 297 ARG PHE PRO ALA ILE VAL PRO ILE THR PRO ASP MET GLU
SEQRES 18 A 297 GLY ALA GLU ILE GLY ARG GLN ALA MET SER PHE TRP SER
SEQRES 19 A 297 THR GLN TRP SER GLY PRO THR PHE MET ALA VAL GLY ALA
SEQRES 20 A 297 GLN ASP PRO VAL LEU GLY PRO GLU VAL MET GLY MET LEU
SEQRES 21 A 297 ARG GLN ALA ILE ARG GLY CYS PRO GLU PRO MET ILE VAL
SEQRES 22 A 297 GLU ALA GLY GLY HIS PHE VAL GLN GLU HIS GLY GLU PRO
SEQRES 23 A 297 ILE ALA ARG ALA ALA LEU ALA ALA PHE GLY GLN
HET SO4 A1298 5
HET SO4 A1299 5
HET SO4 A1300 5
HET SO4 A1301 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 3 HOH *260(H2 O)
HELIX 1 1 PRO A 7 ALA A 12 5 6
HELIX 2 2 TRP A 58 ARG A 63 5 6
HELIX 3 3 MET A 65 ALA A 72 1 8
HELIX 4 4 ASP A 92 TYR A 96 5 5
HELIX 5 5 THR A 97 GLN A 113 1 17
HELIX 6 6 GLN A 122 LEU A 130 1 9
HELIX 7 7 THR A 131 ARG A 136 1 6
HELIX 8 8 GLY A 157 ASN A 169 1 13
HELIX 9 9 ASP A 174 ILE A 183 1 10
HELIX 10 10 THR A 187 ALA A 196 1 10
HELIX 11 11 GLY A 200 PHE A 203 5 4
HELIX 12 12 LYS A 204 PHE A 210 1 7
HELIX 13 13 PRO A 211 VAL A 214 5 4
HELIX 14 14 GLY A 222 GLN A 236 1 15
HELIX 15 15 GLY A 253 ILE A 264 1 12
HELIX 16 16 PHE A 279 HIS A 283 5 5
HELIX 17 17 GLY A 284 PHE A 295 1 12
SHEET 1 AA 2 PHE A 3 VAL A 4 0
SHEET 2 AA 2 LYS A 89 PRO A 90 -1 O LYS A 89 N VAL A 4
SHEET 1 AB 8 HIS A 22 LEU A 24 0
SHEET 2 AB 8 MET A 35 GLU A 40 -1 O MET A 35 N LEU A 24
SHEET 3 AB 8 ARG A 75 PRO A 79 -1 O VAL A 76 N GLU A 40
SHEET 4 AB 8 THR A 48 LEU A 52 1 O PHE A 49 N VAL A 77
SHEET 5 AB 8 VAL A 117 CYS A 121 1 O THR A 118 N LEU A 50
SHEET 6 AB 8 VAL A 140 MET A 146 1 N ASP A 141 O VAL A 117
SHEET 7 AB 8 THR A 241 GLY A 246 1 O PHE A 242 N VAL A 145
SHEET 8 AB 8 MET A 271 VAL A 273 1 O MET A 271 N VAL A 245
CISPEP 1 GLU A 55 PRO A 56 0 -12.08
SITE 1 AC1 6 GLU A 221 GLY A 222 ALA A 223 GLU A 224
SITE 2 AC1 6 ILE A 225 HOH A2257
SITE 1 AC2 4 HIS A 22 ARG A 43 ARG A 289 HOH A2258
SITE 1 AC3 3 ARG A 10 ASP A 195 HOH A2259
SITE 1 AC4 5 GLN A 262 ILE A 264 ARG A 265 GLY A 266
SITE 2 AC4 5 HOH A2260
CRYST1 47.262 108.501 67.312 90.00 90.00 90.00 P 21 21 2 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 0.021159 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009217 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014856 0.00000
TER 2312 GLN A 297
MASTER 412 0 4 17 10 0 6 6 2591 1 20 23
END |