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HEADER HYDROLASE 21-FEB-23 8CMV
TITLE ENGINEERED PETASE ENZYME FROM LCC - C09 MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEAF-BRANCH COMPOST CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LC-CUTINASE,LCC,PET-DIGESTING ENZYME,POLY(ETHYLENE
COMPND 5 TEREPHTHALATE) HYDROLASE,PET HYDROLASE,PETASE;
COMPND 6 EC: 3.1.1.74,3.1.1.101;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED PROKARYOTIC ORGANISM;
SOURCE 3 ORGANISM_TAXID: 2725;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PLASTIC DEGRADATION, THERMAL STABLIZATION, MHET, BHET, TPA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BHATTACHARYA,H.ESTIRI,R.CASTAGNA,E.PARISINI
REVDAT 1 06-MAR-24 8CMV 0
JRNL AUTH S.BHATTACHARYA,H.ESTIRI,R.CASTAGNA,E.PARISINI
JRNL TITL ENGINEERED PETASE ENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0403
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) : 1.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 62177
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.079
REMARK 3 FREE R VALUE TEST SET COUNT : 3158
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) : 1.28
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4360
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3290
REMARK 3 BIN FREE R VALUE SET COUNT : 238
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1969
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 248
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11300
REMARK 3 B22 (A**2) : 0.11300
REMARK 3 B33 (A**2) : -0.36600
REMARK 3 B12 (A**2) : 0.05600
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): 0.046
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.048
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.004
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2093 ; 0.010 ; 0.011
REMARK 3 BOND LENGTHS OTHERS (A): 1954 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2867 ; 1.711 ; 1.652
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4493 ; 0.612 ; 1.569
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 277 ; 6.591 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 19 ;10.464 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 310 ;12.824 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 326 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2529 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 511 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 413 ; 0.237 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 60 ; 0.199 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1050 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 176 ; 0.218 ; 0.200
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): 1051 ; 1.397 ; 1.269
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1051 ; 1.388 ; 1.268
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1317 ; 2.152 ; 2.271
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1318 ; 2.162 ; 2.276
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1042 ; 2.362 ; 1.570
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1043 ; 2.361 ; 1.573
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1540 ; 3.465 ; 2.737
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1541 ; 3.463 ; 2.739
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 : MASK BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8CMV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1292128766.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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) : 0.73380
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62178
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.280
REMARK 200 RESOLUTION RANGE LOW (A) : 54.497
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 20.80
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.30
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE TRIBASIC DIHYDRATE 1M
REMARK 280 ISOPROPANOL 20% PEG 4K 20%, PH 5.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
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 17.70100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 17.70100
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 17.70100
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 ASP A 2
REMARK 465 GLY A 3
REMARK 465 VAL A 4
REMARK 465 LEU A 5
REMARK 465 TRP A 6
REMARK 465 ARG A 7
REMARK 465 VAL A 8
REMARK 465 ARG A 9
REMARK 465 THR A 10
REMARK 465 ALA A 11
REMARK 465 ALA A 12
REMARK 465 LEU A 13
REMARK 465 MET A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 LEU A 18
REMARK 465 ALA A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 TRP A 23
REMARK 465 ALA A 24
REMARK 465 LEU A 25
REMARK 465 VAL A 26
REMARK 465 TRP A 27
REMARK 465 ALA A 28
REMARK 465 SER A 29
REMARK 465 PRO A 30
REMARK 465 SER A 31
REMARK 465 VAL A 32
REMARK 465 GLU A 33
REMARK 465 ALA A 34
REMARK 465 GLN A 35
REMARK 465 LEU A 294
REMARK 465 GLU A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
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 H GLY A 54 HG SER A 111 1.04
REMARK 500 HG SER A 165 HE2 HIS A 242 1.28
REMARK 500 HG1 THR A 198 H VAL A 200 1.28
REMARK 500 HG1 THR A 287 H ASN A 289 1.31
REMARK 500 HH TYR A 78 O HOH A 504 1.59
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 H ASP A 279 HO1 GOL A 402 2565 1.17
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 151 CG - CD - NE ANGL. DEV. = 18.9 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 THR A 96 -7.27 76.22
REMARK 500 ARG A 145 12.28 -140.90
REMARK 500 SER A 165 -128.24 64.65
REMARK 500 THR A 188 57.36 35.19
REMARK 500 HIS A 218 -87.69 -122.32
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 ILE A 119 ASN A 120 149.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 65 0.09 SIDE CHAIN
REMARK 500 ARG A 131 0.12 SIDE CHAIN
REMARK 500 ARG A 151 0.11 SIDE CHAIN
REMARK 500 TYR A 255 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8CMV A 1 293 UNP G9BY57 PETH_UNKP 1 293
SEQADV 8CMV ASP A 36 UNP G9BY57 SER 36 CONFLICT
SEQADV 8CMV ARG A 40 UNP G9BY57 GLN 40 CONFLICT
SEQADV 8CMV ASP A 48 UNP G9BY57 SER 48 CONFLICT
SEQADV 8CMV LYS A 57 UNP G9BY57 SER 57 CONFLICT
SEQADV 8CMV GLY A 127 UNP G9BY57 TYR 127 CONFLICT
SEQADV 8CMV ARG A 145 UNP G9BY57 SER 145 CONFLICT
SEQADV 8CMV ARG A 209 UNP G9BY57 ALA 209 CONFLICT
SEQADV 8CMV CYS A 238 UNP G9BY57 ASP 238 CONFLICT
SEQADV 8CMV ILE A 243 UNP G9BY57 PHE 243 CONFLICT
SEQADV 8CMV ASP A 276 UNP G9BY57 ASN 276 CONFLICT
SEQADV 8CMV LYS A 278 UNP G9BY57 ASN 278 CONFLICT
SEQADV 8CMV CYS A 283 UNP G9BY57 SER 283 CONFLICT
SEQADV 8CMV LYS A 293 UNP G9BY57 GLN 293 ENGINEERED MUTATION
SEQADV 8CMV LEU A 294 UNP G9BY57 EXPRESSION TAG
SEQADV 8CMV GLU A 295 UNP G9BY57 EXPRESSION TAG
SEQADV 8CMV HIS A 296 UNP G9BY57 EXPRESSION TAG
SEQADV 8CMV HIS A 297 UNP G9BY57 EXPRESSION TAG
SEQADV 8CMV HIS A 298 UNP G9BY57 EXPRESSION TAG
SEQADV 8CMV HIS A 299 UNP G9BY57 EXPRESSION TAG
SEQADV 8CMV HIS A 300 UNP G9BY57 EXPRESSION TAG
SEQADV 8CMV HIS A 301 UNP G9BY57 EXPRESSION TAG
SEQRES 1 A 301 MET ASP GLY VAL LEU TRP ARG VAL ARG THR ALA ALA LEU
SEQRES 2 A 301 MET ALA ALA LEU LEU ALA LEU ALA ALA TRP ALA LEU VAL
SEQRES 3 A 301 TRP ALA SER PRO SER VAL GLU ALA GLN ASP ASN PRO TYR
SEQRES 4 A 301 ARG ARG GLY PRO ASN PRO THR ARG ASP ALA LEU THR ALA
SEQRES 5 A 301 ASP GLY PRO PHE LYS VAL ALA THR TYR THR VAL SER ARG
SEQRES 6 A 301 LEU SER VAL SER GLY PHE GLY GLY GLY VAL ILE TYR TYR
SEQRES 7 A 301 PRO THR GLY THR SER LEU THR PHE GLY GLY ILE ALA MET
SEQRES 8 A 301 SER PRO GLY TYR THR ALA ASP ALA SER SER LEU ALA TRP
SEQRES 9 A 301 LEU GLY ARG ARG LEU ALA SER HIS GLY PHE VAL VAL LEU
SEQRES 10 A 301 VAL ILE ASN THR ASN SER ARG PHE ASP GLY PRO ASP SER
SEQRES 11 A 301 ARG ALA SER GLN LEU SER ALA ALA LEU ASN TYR LEU ARG
SEQRES 12 A 301 THR ARG SER PRO SER ALA VAL ARG ALA ARG LEU ASP ALA
SEQRES 13 A 301 ASN ARG LEU ALA VAL ALA GLY HIS SER MET GLY GLY GLY
SEQRES 14 A 301 GLY THR LEU ARG ILE ALA GLU GLN ASN PRO SER LEU LYS
SEQRES 15 A 301 ALA ALA VAL PRO LEU THR PRO TRP HIS THR ASP LYS THR
SEQRES 16 A 301 PHE ASN THR SER VAL PRO VAL LEU ILE VAL GLY ALA GLU
SEQRES 17 A 301 ARG ASP THR VAL ALA PRO VAL SER GLN HIS ALA ILE PRO
SEQRES 18 A 301 PHE TYR GLN ASN LEU PRO SER THR THR PRO LYS VAL TYR
SEQRES 19 A 301 VAL GLU LEU CYS ASN ALA SER HIS ILE ALA PRO ASN SER
SEQRES 20 A 301 ASN ASN ALA ALA ILE SER VAL TYR THR ILE SER TRP MET
SEQRES 21 A 301 LYS LEU TRP VAL ASP ASN ASP THR ARG TYR ARG GLN PHE
SEQRES 22 A 301 LEU CYS ASP VAL LYS ASP PRO ALA LEU CYS ASP PHE ARG
SEQRES 23 A 301 THR ASN ASN ARG HIS CYS LYS LEU GLU HIS HIS HIS HIS
SEQRES 24 A 301 HIS HIS
HET IPA A 401 12
HET GOL A 402 14
HET GOL A 403 14
HET GOL A 404 14
HET GOL A 405 14
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM GOL GLYCEROL
HETSYN IPA 2-PROPANOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 IPA C3 H8 O
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 7 HOH *248(H2 O)
HELIX 1 AA1 ARG A 47 ALA A 52 5 6
HELIX 2 AA2 SER A 64 VAL A 68 5 5
HELIX 3 AA3 ASP A 98 SER A 101 5 4
HELIX 4 AA4 LEU A 102 HIS A 112 1 11
HELIX 5 AA5 GLY A 127 ARG A 145 1 19
HELIX 6 AA6 PRO A 147 ALA A 152 1 6
HELIX 7 AA7 SER A 165 ASN A 178 1 14
HELIX 8 AA8 HIS A 218 LEU A 226 1 9
HELIX 9 AA9 ILE A 243 SER A 247 5 5
HELIX 10 AB1 ASN A 249 ASP A 265 1 17
HELIX 11 AB2 ASP A 267 LEU A 274 5 8
SHEET 1 AA1 6 LYS A 57 VAL A 63 0
SHEET 2 AA1 6 GLY A 74 THR A 80 -1 O TYR A 78 N ALA A 59
SHEET 3 AA1 6 VAL A 115 ILE A 119 -1 O VAL A 116 N TYR A 77
SHEET 4 AA1 6 PHE A 86 SER A 92 1 N MET A 91 O LEU A 117
SHEET 5 AA1 6 LEU A 154 HIS A 164 1 O ASP A 155 N PHE A 86
SHEET 6 AA1 6 ALA A 184 LEU A 187 1 O LEU A 187 N GLY A 163
SHEET 1 AA2 3 VAL A 202 ALA A 207 0
SHEET 2 AA2 3 LYS A 232 LEU A 237 1 O LEU A 237 N GLY A 206
SHEET 3 AA2 3 LEU A 282 THR A 287 -1 O ARG A 286 N TYR A 234
SSBOND 1 CYS A 238 CYS A 283 1555 1555 2.04
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.02
CRYST1 108.876 108.876 35.402 90.00 90.00 120.00 P 63 6
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 0.009185 0.005303 0.000000 0.00000
SCALE2 0.000000 0.010606 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028247 0.00000
TER 4005 LYS A 293
MASTER 402 0 5 11 9 0 0 6 2245 1 72 24
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