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HEADER HYDROLASE 22-JUL-19 6SBN
TITLE POLYESTER HYDROLASE PE-H OF PSEUDOMONAS AESTUSNIGRI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AESTUSNIGRI;
SOURCE 3 ORGANISM_TAXID: 857252;
SOURCE 4 GENE: B7O88_11480;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLYESTER DEGRADATION, PET HYDROLASE, MARINE BACTERIA, PSEUDOMONAS
KEYWDS 2 AESTUSNIGRI, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BOLLINGER,S.THIES,S.KOBUS,A.HOEPPNER,S.H.J.SMITS,K.-E.JAEGER
REVDAT 1 26-FEB-20 6SBN 0
JRNL AUTH A.BOLLINGER,S.THIES,E.KNIEPS-GRUNHAGEN,C.GERTZEN,S.KOBUS,
JRNL AUTH 2 A.HOEPPNER,M.FERRER,H.GOHLKE,S.H.J.SMITS,K.-E.JAEGER
JRNL TITL A NOVEL POLYESTER HYDROLASE FROM THE MARINE BACTERIUM
JRNL TITL 2 PSEUDOMONAS AESTUSNIGRI - STRUCTURAL AND FUNCTIONAL INSIGHTS
JRNL REF FRONT MICROBIOL 2020
JRNL REFN ESSN 1664-302X
REMARK 2
REMARK 2 RESOLUTION. 1.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 1.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 99673
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) : 0.108
REMARK 3 R VALUE (WORKING SET) : 0.107
REMARK 3 FREE R VALUE : 0.137
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2100
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.09
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7185
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.1540
REMARK 3 BIN FREE R VALUE SET COUNT : 151
REMARK 3 BIN FREE R VALUE : 0.1850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1983
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 368
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.26000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.26000
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): 0.021
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.023
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.014
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.628
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.985
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2104 ; 0.027 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1894 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2877 ; 2.206 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4376 ; 1.545 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 284 ; 6.782 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;29.963 ;22.967
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 317 ;11.204 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.522 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 308 ; 0.193 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2464 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 510 ; 0.006 ; 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): 3997 ; 6.272 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 85 ;27.420 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4218 ;12.675 ; 5.000
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 6SBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1292103430.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-18
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 : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976247
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101774
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.090
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 12.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 12.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.43000
REMARK 200 FOR SHELL : 4.700
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.5, 16 %
REMARK 280 (W/V) PEG 3000, 0.036 MM LYSO-FOSCHOLINE14, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 44.45600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.45600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.40700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.00700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.40700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.00700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.45600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.40700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.00700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.45600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.40700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.00700
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 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 1
REMARK 465 PRO A 2
REMARK 465 PHE A 3
REMARK 465 ASN A 4
REMARK 465 LYS A 5
REMARK 465 LYS A 6
REMARK 465 SER A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 LEU A 11
REMARK 465 CYS A 12
REMARK 465 GLY A 13
REMARK 465 ALA A 14
REMARK 465 GLY A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 LEU A 18
REMARK 465 PHE A 19
REMARK 465 SER A 20
REMARK 465 MET A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 LEU A 24
REMARK 465 ALA A 25
REMARK 465 ASN A 26
REMARK 465 ASN A 27
REMARK 465 PRO A 28
REMARK 465 ALA A 29
REMARK 465 PRO A 30
REMARK 465 THR A 31
REMARK 465 ASP A 32
REMARK 465 PRO A 33
REMARK 465 GLY A 34
REMARK 465 ASP A 35
REMARK 465 SER A 36
REMARK 465 GLY A 37
REMARK 465 GLY A 286
REMARK 465 PRO A 287
REMARK 465 ASN A 288
REMARK 465 HIS A 289
REMARK 465 THR A 290
REMARK 465 SER A 291
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
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 GLY A 38 N CA
REMARK 470 ARG A 63 CZ NH1 NH2
REMARK 470 ASP A 292 CG OD1 OD2
REMARK 470 LEU A 305 CG CD1 CD2
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 769 O HOH A 850 1.73
REMARK 500 O HOH A 789 O HOH A 794 1.89
REMARK 500 O HOH A 579 O HOH A 730 2.07
REMARK 500 O HOH A 604 O HOH A 830 2.15
REMARK 500 O HOH A 564 O HOH A 696 2.19
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 GLY A 75 CA GLY A 75 C 0.111
REMARK 500 GLY A 76 N GLY A 76 CA 0.119
REMARK 500 ARG A 151 CD ARG A 151 NE -0.170
REMARK 500 ARG A 151 CZ ARG A 151 NH2 -0.151
REMARK 500 GLU A 183 CD GLU A 183 OE1 0.073
REMARK 500 CYS A 285 C CYS A 285 O 0.133
REMARK 500 GLN A 294 CG GLN A 294 CD 0.145
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 66 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 LEU A 70 CB - CG - CD2 ANGL. DEV. = -17.1 DEGREES
REMARK 500 GLY A 76 C - N - CA ANGL. DEV. = -18.9 DEGREES
REMARK 500 ARG A 151 NE - CZ - NH1 ANGL. DEV. = -12.4 DEGREES
REMARK 500 ARG A 151 NE - CZ - NH2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 MET A 172 CA - CB - CG ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG A 264 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 264 NE - CZ - NH2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 CYS A 285 CA - C - O ANGL. DEV. = -17.4 DEGREES
REMARK 500 ASP A 292 O - C - N ANGL. DEV. = -16.1 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 96 -157.85 -87.47
REMARK 500 SER A 104 -159.34 -137.19
REMARK 500 ASP A 129 -87.48 -148.28
REMARK 500 SER A 171 -125.20 69.90
REMARK 500 HIS A 225 -89.46 -131.84
REMARK 500 SER A 256 -136.45 -125.87
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 865 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 866 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 867 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH A 868 DISTANCE = 7.00 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 216 OG
REMARK 620 2 HOH A 783 O 98.0
REMARK 620 3 SER A 152 OG 48.6 118.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402
DBREF1 6SBN A 1 304 UNP A0A1H6AD45_9PSED
DBREF2 6SBN A A0A1H6AD45 1 304
SEQADV 6SBN LEU A 305 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SBN GLU A 306 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SBN HIS A 307 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SBN HIS A 308 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SBN HIS A 309 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SBN HIS A 310 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SBN HIS A 311 UNP A0A1H6AD4 EXPRESSION TAG
SEQADV 6SBN HIS A 312 UNP A0A1H6AD4 EXPRESSION TAG
SEQRES 1 A 312 MET PRO PHE ASN LYS LYS SER VAL LEU ALA LEU CYS GLY
SEQRES 2 A 312 ALA GLY ALA LEU LEU PHE SER MET SER ALA LEU ALA ASN
SEQRES 3 A 312 ASN PRO ALA PRO THR ASP PRO GLY ASP SER GLY GLY GLY
SEQRES 4 A 312 SER ALA TYR GLN ARG GLY PRO ASP PRO SER VAL SER PHE
SEQRES 5 A 312 LEU GLU ALA ASP ARG GLY GLN TYR SER VAL ARG SER SER
SEQRES 6 A 312 ARG VAL SER SER LEU VAL SER GLY PHE GLY GLY GLY THR
SEQRES 7 A 312 ILE TYR TYR PRO THR GLY THR THR GLY THR MET GLY ALA
SEQRES 8 A 312 VAL VAL VAL ILE PRO GLY PHE VAL SER ALA GLU SER SER
SEQRES 9 A 312 ILE ASP TRP TRP GLY PRO LYS LEU ALA SER TYR GLY PHE
SEQRES 10 A 312 VAL VAL MET THR ILE ASP THR ASN THR GLY PHE ASP GLN
SEQRES 11 A 312 PRO PRO SER ARG ALA ARG GLN ILE ASN ASN ALA LEU ASP
SEQRES 12 A 312 TYR LEU VAL SER GLN ASN SER ARG SER SER SER PRO VAL
SEQRES 13 A 312 ARG GLY MET ILE ASP THR ASN ARG LEU GLY VAL ILE GLY
SEQRES 14 A 312 TRP SER MET GLY GLY GLY GLY THR LEU ARG VAL ALA SER
SEQRES 15 A 312 GLU GLY ARG ILE LYS ALA ALA ILE PRO LEU ALA PRO TRP
SEQRES 16 A 312 ASP THR THR SER TYR TYR ALA SER ARG SER GLN ALA PRO
SEQRES 17 A 312 THR LEU ILE PHE ALA CYS GLU SER ASP VAL ILE ALA PRO
SEQRES 18 A 312 VAL LEU GLN HIS ALA SER PRO PHE TYR ASN SER LEU PRO
SEQRES 19 A 312 SER SER ILE ASP LYS ALA PHE VAL GLU ILE ASN GLY GLY
SEQRES 20 A 312 SER HIS TYR CYS GLY ASN GLY GLY SER ILE TYR ASN ASP
SEQRES 21 A 312 VAL LEU SER ARG PHE GLY VAL SER TRP MET LYS LEU HIS
SEQRES 22 A 312 LEU ASP GLU ASP SER ARG TYR LYS GLN PHE LEU CYS GLY
SEQRES 23 A 312 PRO ASN HIS THR SER ASP SER GLN ILE SER ASP TYR ARG
SEQRES 24 A 312 GLY ASN CYS PRO TYR LEU GLU HIS HIS HIS HIS HIS HIS
HET ACT A 401 4
HET NA A 402 1
HETNAM ACT ACETATE ION
HETNAM NA SODIUM ION
FORMUL 2 ACT C2 H3 O2 1-
FORMUL 3 NA NA 1+
FORMUL 4 HOH *368(H2 O)
HELIX 1 AA1 SER A 49 ALA A 55 1 7
HELIX 2 AA2 SER A 68 GLY A 73 1 6
HELIX 3 AA3 TRP A 107 PHE A 117 1 11
HELIX 4 AA4 GLN A 130 ASN A 149 1 20
HELIX 5 AA5 SER A 171 SER A 182 1 12
HELIX 6 AA6 TYR A 201 SER A 205 5 5
HELIX 7 AA7 HIS A 225 LEU A 233 1 9
HELIX 8 AA8 TYR A 258 GLU A 276 1 19
HELIX 9 AA9 ASP A 277 LEU A 284 5 8
SHEET 1 AA1 6 VAL A 62 VAL A 67 0
SHEET 2 AA1 6 GLY A 77 PRO A 82 -1 O ILE A 79 N SER A 65
SHEET 3 AA1 6 VAL A 118 ILE A 122 -1 O VAL A 119 N TYR A 80
SHEET 4 AA1 6 MET A 89 ILE A 95 1 N VAL A 92 O MET A 120
SHEET 5 AA1 6 ILE A 160 TRP A 170 1 O ASP A 161 N MET A 89
SHEET 6 AA1 6 ALA A 188 LEU A 192 1 O LEU A 192 N GLY A 169
SHEET 1 AA2 3 THR A 209 CYS A 214 0
SHEET 2 AA2 3 LYS A 239 ILE A 244 1 O ILE A 244 N ALA A 213
SHEET 3 AA2 3 ILE A 295 GLY A 300 -1 O ASP A 297 N GLU A 243
SSBOND 1 CYS A 214 CYS A 251 1555 1555 2.04
SSBOND 2 CYS A 285 CYS A 302 1555 1555 2.04
LINK OG SER A 216 NA NA A 402 1555 1555 2.95
LINK NA NA A 402 O HOH A 783 1555 1555 2.85
LINK OG SER A 152 NA NA A 402 1555 6554 3.20
CISPEP 1 CYS A 302 PRO A 303 0 -1.82
SITE 1 AC1 7 GLY A 127 PHE A 128 SER A 133 ARG A 136
SITE 2 AC1 7 HOH A 519 HOH A 611 HOH A 650
SITE 1 AC2 6 SER A 150 ARG A 151 SER A 152 GLU A 215
SITE 2 AC2 6 SER A 216 HOH A 783
CRYST1 68.814 80.014 88.912 90.00 90.00 90.00 C 2 2 21 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 0.014532 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011247 0.00000
TER 2029 GLU A 306
MASTER 449 0 2 9 9 0 4 6 2356 1 11 24
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