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HEADER HYDROLASE 21-APR-25 9UM7
TITLE CAPETASEM9 SEC LOOP OF 12CL VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: CAPETASEM9 SEC LOOP OF 12CL VARIANT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPTOSPORANGIUM AURANTIACUM;
SOURCE 3 ORGANISM_TAXID: 134849;
SOURCE 4 GENE: SAMN05443668_101498;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PETASE, CRYPTOSPORANGIUM, AURANTIACUM, CAPETASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KIM,D.KI,J.PARK
REVDAT 1 29-APR-26 9UM7 0
JRNL AUTH K.KIM,D.KI,J.PARK
JRNL TITL MODULATION OF A NON-CATALYTIC LOOP ENHANCES PRODUCTIVE
JRNL TITL 2 ACCESS AND PET DEPOLYMERIZATION ACTIVITY IN CAPETASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 152778
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8084
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) : 1.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6654
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3840
REMARK 3 BIN FREE R VALUE SET COUNT : 372
REMARK 3 BIN FREE R VALUE : 0.3890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3999
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 0.19000
REMARK 3 B33 (A**2) : -0.63000
REMARK 3 B12 (A**2) : 0.10000
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): 0.039
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.041
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.030
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.739
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4123 ; 0.014 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 3747 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5627 ; 2.058 ; 1.787
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8608 ; 0.700 ; 1.741
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 522 ; 7.580 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 30 ; 9.173 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 587 ;11.252 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 608 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5032 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1012 ; 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): 2094 ; 1.601 ; 1.647
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2094 ; 1.592 ; 1.647
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2614 ; 2.329 ; 2.952
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2615 ; 2.330 ; 2.954
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2029 ; 3.204 ; 1.923
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2030 ; 3.203 ; 1.923
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3014 ; 4.549 ; 3.382
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4747 ; 5.497 ;18.650
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4683 ; 5.416 ;17.570
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
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
REMARK 4
REMARK 4 9UM7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-APR-25.
REMARK 100 THE DEPOSITION ID IS D_1300058238.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-AUG-24
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 : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 163278
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.260
REMARK 200 RESOLUTION RANGE LOW (A) : 175.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.78800
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: MOLREP
REMARK 200 STARTING MODEL: 7YME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% (W/V) PEG 3350, 4% (V/V) TACSIMATE
REMARK 280 PH 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 116.87567
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 233.75133
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 175.31350
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 292.18917
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 58.43783
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 116.87567
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 233.75133
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 292.18917
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 175.31350
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 58.43783
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 ALA A 41
REMARK 465 ALA A 42
REMARK 465 ALA B 41
REMARK 465 ALA B 42
REMARK 465 GLU B 303
REMARK 465 HIS B 304
REMARK 465 HIS B 305
REMARK 465 HIS B 306
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 O HOH A 628 O HOH A 628 12565 2.14
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 SER A 56 CA SER A 56 CB 0.097
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 137 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 CYS A 180 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 182 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 LYS A 186 CD - CE - NZ ANGL. DEV. = 17.1 DEGREES
REMARK 500 ARG A 266 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 137 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG B 177 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG B 266 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 266 NE - CZ - NH2 ANGL. DEV. = -3.0 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 99 -174.23 -68.30
REMARK 500 ILE A 102 57.57 30.25
REMARK 500 SER A 169 -126.41 60.60
REMARK 500 ALA A 218 60.96 -119.86
REMARK 500 HIS A 223 -91.59 -126.93
REMARK 500 PHE A 301 38.27 70.88
REMARK 500 SER B 169 -129.26 63.13
REMARK 500 HIS B 223 -90.37 -127.86
REMARK 500 PHE B 301 60.58 76.18
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 PRO A 99 GLY A 100 -99.61
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 182 0.10 SIDE CHAIN
REMARK 500 ARG B 155 0.07 SIDE CHAIN
REMARK 500 ARG B 182 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO A 99 -12.85
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9UM7 A 41 301 UNP A0A1M7II12_9ACTN
DBREF2 9UM7 A A0A1M7II12 41 299
DBREF1 9UM7 B 41 301 UNP A0A1M7II12_9ACTN
DBREF2 9UM7 B A0A1M7II12 41 299
SEQADV 9UM7 ALA A 109 UNP A0A1M7II1 ASN 109 ENGINEERED MUTATION
SEQADV 9UM7 THR A 129 UNP A0A1M7II1 VAL 129 ENGINEERED MUTATION
SEQADV 9UM7 ARG A 155 UNP A0A1M7II1 ALA 155 ENGINEERED MUTATION
SEQADV 9UM7 CYS A 180 UNP A0A1M7II1 LEU 180 ENGINEERED MUTATION
SEQADV 9UM7 THR A 196 UNP A0A1M7II1 GLY 196 ENGINEERED MUTATION
SEQADV 9UM7 LYS A 198 UNP A0A1M7II1 ARG 198 ENGINEERED MUTATION
SEQADV 9UM7 CYS A 202 UNP A0A1M7II1 ALA 202 ENGINEERED MUTATION
SEQADV 9UM7 CYS A 242 UNP A0A1M7II1 ARG 242 ENGINEERED MUTATION
SEQADV 9UM7 GLY A 280 UNP A0A1M7II1 INSERTION
SEQADV 9UM7 ALA A 281 UNP A0A1M7II1 PRO 280 ENGINEERED MUTATION
SEQADV 9UM7 GLU A 282 UNP A0A1M7II1 GLY 281 ENGINEERED MUTATION
SEQADV 9UM7 HIS A 283 UNP A0A1M7II1 PRO 282 ENGINEERED MUTATION
SEQADV 9UM7 GLN A 284 UNP A0A1M7II1 SER 283 ENGINEERED MUTATION
SEQADV 9UM7 ALA A 285 UNP A0A1M7II1 THR 284 ENGINEERED MUTATION
SEQADV 9UM7 ASP A 286 UNP A0A1M7II1 GLY 285 ENGINEERED MUTATION
SEQADV 9UM7 SER A 288 UNP A0A1M7II1 INSERTION
SEQADV 9UM7 LYS A 289 UNP A0A1M7II1 PHE 287 ENGINEERED MUTATION
SEQADV 9UM7 ARG A 290 UNP A0A1M7II1 ALA 288 ENGINEERED MUTATION
SEQADV 9UM7 ALA A 291 UNP A0A1M7II1 PRO 289 ENGINEERED MUTATION
SEQADV 9UM7 CYS A 293 UNP A0A1M7II1 SER 291 ENGINEERED MUTATION
SEQADV 9UM7 LEU A 302 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 9UM7 GLU A 303 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 9UM7 HIS A 304 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 9UM7 HIS A 305 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 9UM7 HIS A 306 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 9UM7 ALA B 109 UNP A0A1M7II1 ASN 109 ENGINEERED MUTATION
SEQADV 9UM7 THR B 129 UNP A0A1M7II1 VAL 129 ENGINEERED MUTATION
SEQADV 9UM7 ARG B 155 UNP A0A1M7II1 ALA 155 ENGINEERED MUTATION
SEQADV 9UM7 CYS B 180 UNP A0A1M7II1 LEU 180 ENGINEERED MUTATION
SEQADV 9UM7 THR B 196 UNP A0A1M7II1 GLY 196 ENGINEERED MUTATION
SEQADV 9UM7 LYS B 198 UNP A0A1M7II1 ARG 198 ENGINEERED MUTATION
SEQADV 9UM7 CYS B 202 UNP A0A1M7II1 ALA 202 ENGINEERED MUTATION
SEQADV 9UM7 CYS B 242 UNP A0A1M7II1 ARG 242 ENGINEERED MUTATION
SEQADV 9UM7 GLY B 280 UNP A0A1M7II1 INSERTION
SEQADV 9UM7 ALA B 281 UNP A0A1M7II1 PRO 280 ENGINEERED MUTATION
SEQADV 9UM7 GLU B 282 UNP A0A1M7II1 GLY 281 ENGINEERED MUTATION
SEQADV 9UM7 HIS B 283 UNP A0A1M7II1 PRO 282 ENGINEERED MUTATION
SEQADV 9UM7 GLN B 284 UNP A0A1M7II1 SER 283 ENGINEERED MUTATION
SEQADV 9UM7 ALA B 285 UNP A0A1M7II1 THR 284 ENGINEERED MUTATION
SEQADV 9UM7 ASP B 286 UNP A0A1M7II1 GLY 285 ENGINEERED MUTATION
SEQADV 9UM7 SER B 288 UNP A0A1M7II1 INSERTION
SEQADV 9UM7 LYS B 289 UNP A0A1M7II1 PHE 287 ENGINEERED MUTATION
SEQADV 9UM7 ARG B 290 UNP A0A1M7II1 ALA 288 ENGINEERED MUTATION
SEQADV 9UM7 ALA B 291 UNP A0A1M7II1 PRO 289 ENGINEERED MUTATION
SEQADV 9UM7 CYS B 293 UNP A0A1M7II1 SER 291 ENGINEERED MUTATION
SEQADV 9UM7 LEU B 302 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 9UM7 GLU B 303 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 9UM7 HIS B 304 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 9UM7 HIS B 305 UNP A0A1M7II1 EXPRESSION TAG
SEQADV 9UM7 HIS B 306 UNP A0A1M7II1 EXPRESSION TAG
SEQRES 1 A 266 ALA ALA ASP ASN PRO TYR GLN ARG GLY PRO ASP PRO THR
SEQRES 2 A 266 ASN ALA SER ILE GLU ALA ALA THR GLY PRO PHE ALA VAL
SEQRES 3 A 266 GLY THR GLN PRO ILE VAL GLY ALA SER GLY PHE GLY GLY
SEQRES 4 A 266 GLY GLN ILE TYR TYR PRO THR ASP THR SER GLN THR TYR
SEQRES 5 A 266 GLY ALA VAL VAL ILE VAL PRO GLY PHE ILE SER VAL TRP
SEQRES 6 A 266 ALA GLN LEU ALA TRP LEU GLY PRO ARG LEU ALA SER GLN
SEQRES 7 A 266 GLY PHE VAL VAL ILE GLY ILE GLU THR SER THR ILE THR
SEQRES 8 A 266 ASP LEU PRO ASP PRO ARG GLY ASP GLN ALA LEU ALA ALA
SEQRES 9 A 266 LEU ASP TRP ALA THR THR ARG SER PRO VAL ARG SER ARG
SEQRES 10 A 266 ILE ASP ARG THR ARG LEU ALA ALA ALA GLY TRP SER MET
SEQRES 11 A 266 GLY GLY GLY GLY LEU ARG ARG ALA ALA CYS GLN ARG PRO
SEQRES 12 A 266 SER LEU LYS ALA ILE VAL GLY MET ALA PRO TRP ASN THR
SEQRES 13 A 266 GLU LYS ASN TRP SER CYS VAL THR VAL PRO THR LEU PHE
SEQRES 14 A 266 PHE GLY GLY SER SER ASP ALA VAL ALA SER PRO ASN ASP
SEQRES 15 A 266 HIS ALA LYS PRO PHE TYR ASN SER ILE THR ARG ALA GLU
SEQRES 16 A 266 LYS ASP TYR ILE GLU LEU CYS ASN ALA ASP HIS PHE PHE
SEQRES 17 A 266 PRO THR SER ALA ASN THR THR MET ALA LYS TYR PHE ILE
SEQRES 18 A 266 SER TRP LEU LYS ARG TRP VAL ASP ASN ASP THR ARG TYR
SEQRES 19 A 266 THR GLN PHE LEU CYS GLY ALA GLU HIS GLN ALA ASP LEU
SEQRES 20 A 266 SER LYS ARG ALA VAL CYS ALA SER MET ASN THR CYS PRO
SEQRES 21 A 266 PHE LEU GLU HIS HIS HIS
SEQRES 1 B 266 ALA ALA ASP ASN PRO TYR GLN ARG GLY PRO ASP PRO THR
SEQRES 2 B 266 ASN ALA SER ILE GLU ALA ALA THR GLY PRO PHE ALA VAL
SEQRES 3 B 266 GLY THR GLN PRO ILE VAL GLY ALA SER GLY PHE GLY GLY
SEQRES 4 B 266 GLY GLN ILE TYR TYR PRO THR ASP THR SER GLN THR TYR
SEQRES 5 B 266 GLY ALA VAL VAL ILE VAL PRO GLY PHE ILE SER VAL TRP
SEQRES 6 B 266 ALA GLN LEU ALA TRP LEU GLY PRO ARG LEU ALA SER GLN
SEQRES 7 B 266 GLY PHE VAL VAL ILE GLY ILE GLU THR SER THR ILE THR
SEQRES 8 B 266 ASP LEU PRO ASP PRO ARG GLY ASP GLN ALA LEU ALA ALA
SEQRES 9 B 266 LEU ASP TRP ALA THR THR ARG SER PRO VAL ARG SER ARG
SEQRES 10 B 266 ILE ASP ARG THR ARG LEU ALA ALA ALA GLY TRP SER MET
SEQRES 11 B 266 GLY GLY GLY GLY LEU ARG ARG ALA ALA CYS GLN ARG PRO
SEQRES 12 B 266 SER LEU LYS ALA ILE VAL GLY MET ALA PRO TRP ASN THR
SEQRES 13 B 266 GLU LYS ASN TRP SER CYS VAL THR VAL PRO THR LEU PHE
SEQRES 14 B 266 PHE GLY GLY SER SER ASP ALA VAL ALA SER PRO ASN ASP
SEQRES 15 B 266 HIS ALA LYS PRO PHE TYR ASN SER ILE THR ARG ALA GLU
SEQRES 16 B 266 LYS ASP TYR ILE GLU LEU CYS ASN ALA ASP HIS PHE PHE
SEQRES 17 B 266 PRO THR SER ALA ASN THR THR MET ALA LYS TYR PHE ILE
SEQRES 18 B 266 SER TRP LEU LYS ARG TRP VAL ASP ASN ASP THR ARG TYR
SEQRES 19 B 266 THR GLN PHE LEU CYS GLY ALA GLU HIS GLN ALA ASP LEU
SEQRES 20 B 266 SER LYS ARG ALA VAL CYS ALA SER MET ASN THR CYS PRO
SEQRES 21 B 266 PHE LEU GLU HIS HIS HIS
HET EDO A 401 10
HET EDO A 402 4
HET EDO B 401 4
HET EDO B 402 4
HET EDO B 403 10
HET EDO B 404 10
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 6(C2 H6 O2)
FORMUL 9 HOH *360(H2 O)
HELIX 1 AA1 THR A 53 ALA A 59 1 7
HELIX 2 AA2 VAL A 104 ALA A 109 5 6
HELIX 3 AA3 TRP A 110 SER A 117 1 8
HELIX 4 AA4 LEU A 133 ARG A 151 1 19
HELIX 5 AA5 VAL A 154 SER A 156 5 3
HELIX 6 AA6 SER A 169 GLY A 174 1 6
HELIX 7 AA7 GLY A 174 ARG A 182 1 9
HELIX 8 AA8 HIS A 223 ILE A 231 1 9
HELIX 9 AA9 PHE A 247 SER A 251 5 5
HELIX 10 AB1 ASN A 253 ASP A 269 1 17
HELIX 11 AB2 ASP A 271 ARG A 273 5 3
HELIX 12 AB3 TYR A 274 GLY A 280 1 7
HELIX 13 AB4 GLY A 280 LYS A 289 1 10
HELIX 14 AB5 THR B 53 ALA B 59 1 7
HELIX 15 AB6 VAL B 104 ALA B 109 5 6
HELIX 16 AB7 TRP B 110 SER B 117 1 8
HELIX 17 AB8 LEU B 133 ARG B 151 1 19
HELIX 18 AB9 VAL B 154 SER B 156 5 3
HELIX 19 AC1 SER B 169 GLY B 174 1 6
HELIX 20 AC2 GLY B 174 ARG B 182 1 9
HELIX 21 AC3 HIS B 223 ILE B 231 1 9
HELIX 22 AC4 PHE B 247 SER B 251 5 5
HELIX 23 AC5 ASN B 253 ASP B 269 1 17
HELIX 24 AC6 ASP B 271 ARG B 273 5 3
HELIX 25 AC7 TYR B 274 GLY B 280 1 7
HELIX 26 AC8 GLY B 280 LYS B 289 1 10
SHEET 1 AA1 9 VAL A 66 PRO A 70 0
SHEET 2 AA1 9 GLY A 80 PRO A 85 -1 O TYR A 84 N GLY A 67
SHEET 3 AA1 9 VAL A 121 ILE A 125 -1 O VAL A 122 N TYR A 83
SHEET 4 AA1 9 TYR A 92 VAL A 98 1 N VAL A 95 O ILE A 123
SHEET 5 AA1 9 ILE A 158 TRP A 168 1 O ASP A 159 N TYR A 92
SHEET 6 AA1 9 ALA A 187 MET A 191 1 O MET A 191 N GLY A 167
SHEET 7 AA1 9 THR A 207 GLY A 212 1 O PHE A 210 N GLY A 190
SHEET 8 AA1 9 LYS A 236 LEU A 241 1 O LEU A 241 N GLY A 211
SHEET 9 AA1 9 VAL A 292 ASN A 297 -1 O MET A 296 N TYR A 238
SHEET 1 AA2 9 VAL B 66 PRO B 70 0
SHEET 2 AA2 9 GLY B 80 PRO B 85 -1 O TYR B 84 N GLY B 67
SHEET 3 AA2 9 VAL B 121 ILE B 125 -1 O VAL B 122 N TYR B 83
SHEET 4 AA2 9 TYR B 92 VAL B 98 1 N VAL B 95 O ILE B 123
SHEET 5 AA2 9 ILE B 158 TRP B 168 1 O ASP B 159 N TYR B 92
SHEET 6 AA2 9 ALA B 187 MET B 191 1 O MET B 191 N GLY B 167
SHEET 7 AA2 9 THR B 207 GLY B 212 1 O LEU B 208 N GLY B 190
SHEET 8 AA2 9 LYS B 236 LEU B 241 1 O LEU B 241 N GLY B 211
SHEET 9 AA2 9 ALA B 294 ASN B 297 -1 O MET B 296 N TYR B 238
SSBOND 1 CYS A 180 CYS A 202 1555 1555 2.12
SSBOND 2 CYS A 242 CYS A 293 1555 1555 2.31
SSBOND 3 CYS A 279 CYS A 299 1555 1555 2.06
SSBOND 4 CYS B 180 CYS B 202 1555 1555 1.98
SSBOND 5 CYS B 242 CYS B 293 1555 1555 2.18
SSBOND 6 CYS B 279 CYS B 299 1555 1555 2.07
CISPEP 1 CYS A 299 PRO A 300 0 5.73
CISPEP 2 CYS B 299 PRO B 300 0 5.37
CRYST1 77.952 77.952 350.627 90.00 90.00 120.00 P 61 2 2 24
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 0.012828 0.007406 0.000000 0.00000
SCALE2 0.000000 0.014813 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002852 0.00000
TER 2020 HIS A 306
TER 4001 LEU B 302
MASTER 428 0 6 26 18 0 0 6 4383 2 54 42
END |