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HEADER HYDROLASE 19-NOV-23 8V16
TITLE ESTERASE WITH A MONOMERIC COOPERATIVE, HYSTERESIS OR ALLOKAIRY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE 1;
COMPND 3 CHAIN: C, A, B, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED PROTEOBACTERIUM;
SOURCE 3 ORGANISM_TAXID: 153809;
SOURCE 4 GENE: ADE1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: RP
KEYWDS ESTERASE, HYSTERESIS/ALLOKAIRY, METAGENOMIC, ALPHA/BETA-HYDROLASES,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.GUZZO,T.G.C.VINCES,A.B.VISNARDI
REVDAT 1 23-OCT-24 8V16 0
JRNL AUTH T.C.VINCES,A.S.DE SOUZA,C.F.CARVALHO,A.B.VISNARDI,
JRNL AUTH 2 R.D.TEIXEIRA,E.E.LLONTOP,B.A.P.BISMARA,E.J.VICENTE,
JRNL AUTH 3 J.O.PEREIRA,R.F.DE SOUZA,M.YONAMINE,S.R.MARANA,C.S.FARAH,
JRNL AUTH 4 C.R.GUZZO
JRNL TITL MONOMERIC ESTERASE: INSIGHTS INTO COOPERATIVE BEHAVIOR,
JRNL TITL 2 HYSTERESIS/ALLOKAIRY.
JRNL REF BIOCHEMISTRY V. 63 1178 2024
JRNL REFN ISSN 0006-2960
JRNL PMID 38669355
JRNL DOI 10.1021/ACS.BIOCHEM.3C00668
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0352
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 88267
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) : 0.180
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4413
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6098
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 321
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8190
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 357
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.21500
REMARK 3 B22 (A**2) : 0.25600
REMARK 3 B33 (A**2) : -1.47100
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): 0.145
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.469
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8434 ; 0.008 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 7930 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11455 ; 1.484 ; 1.649
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18466 ; 0.490 ; 1.557
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1063 ; 6.134 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 51 ;10.908 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1397 ;15.326 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1299 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9532 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1608 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1685 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 59 ; 0.202 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4049 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 337 ; 0.136 ; 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): 4246 ; 2.967 ; 3.261
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4246 ; 2.967 ; 3.261
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5299 ; 3.953 ; 4.871
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5300 ; 3.953 ; 4.871
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4188 ; 4.208 ; 3.820
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4189 ; 4.207 ; 3.820
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6152 ; 6.268 ; 5.509
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6153 ; 6.267 ; 5.510
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 8V16 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-23.
REMARK 100 THE DEPOSITION ID IS D_1000279327.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS SIRIUS
REMARK 200 BEAMLINE : MANACA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9772
REMARK 200 MONOCHROMATOR : HORIZONTAL DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR (DCM) EQUIPPED
REMARK 200 WITH TWO PAIRS OF SI CRYSTALS
REMARK 200 (111 AND 311)
REMARK 200 OPTICS : VERTICAL FOCUSING MIRROR (SIDE
REMARK 200 -BOUNCE SAGITTAL CYLINDRICAL
REMARK 200 MIRROR)
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM
REMARK 280 CACODYLATE TRIHYDRATE PH 6.5 AND, 30% W/V POLYETHYLENE GLYCOL 8,
REMARK 280 000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.15K
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 36.03800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.68550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.94550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.68550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.03800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.94550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 2
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 PRO C 131
REMARK 465 GLU C 132
REMARK 465 SER C 133
REMARK 465 LEU C 134
REMARK 465 LYS C 135
REMARK 465 ALA C 136
REMARK 465 LEU C 137
REMARK 465 GLU C 138
REMARK 465 GLY C 139
REMARK 465 ARG C 140
REMARK 465 ALA C 141
REMARK 465 GLY C 142
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 GLU A 138
REMARK 465 GLY A 139
REMARK 465 ARG A 140
REMARK 465 ALA A 141
REMARK 465 GLY A 142
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
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 252 NE - CZ - NH2 ANGL. DEV. = -4.2 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 SER C 94 -119.66 59.66
REMARK 500 CYS C 118 58.83 35.94
REMARK 500 SER A 94 -117.15 59.44
REMARK 500 CYS A 118 57.20 36.62
REMARK 500 PRO A 131 0.36 -62.83
REMARK 500 VAL A 198 -3.78 -143.71
REMARK 500 SER B 94 -119.94 57.37
REMARK 500 CYS B 118 61.21 35.12
REMARK 500 VAL B 198 -14.05 -145.93
REMARK 500 SER D 94 -123.46 61.79
REMARK 500 TYR D 107 49.70 -141.25
REMARK 500 CYS D 118 59.58 34.97
REMARK 500 ASP D 216 43.52 -100.26
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 C 87 0.09 SIDE CHAIN
REMARK 500 ARG C 252 0.07 SIDE CHAIN
REMARK 500 ARG A 175 0.09 SIDE CHAIN
REMARK 500 ARG A 197 0.14 SIDE CHAIN
REMARK 500 ARG A 252 0.11 SIDE CHAIN
REMARK 500 ARG B 140 0.15 SIDE CHAIN
REMARK 500 ARG B 197 0.09 SIDE CHAIN
REMARK 500 ARG B 252 0.10 SIDE CHAIN
REMARK 500 ARG D 175 0.08 SIDE CHAIN
REMARK 500 ARG D 183 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8V16 C 1 268 UNP A0A8E4UR43_9PROT
DBREF2 8V16 C A0A8E4UR43 1 268
DBREF1 8V16 A 1 268 UNP A0A8E4UR43_9PROT
DBREF2 8V16 A A0A8E4UR43 1 268
DBREF1 8V16 B 1 268 UNP A0A8E4UR43_9PROT
DBREF2 8V16 B A0A8E4UR43 1 268
DBREF1 8V16 D 1 268 UNP A0A8E4UR43_9PROT
DBREF2 8V16 D A0A8E4UR43 1 268
SEQADV 8V16 VAL C -5 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 PRO C -4 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 ARG C -3 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 GLY C -2 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 SER C -1 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 HIS C 0 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 VAL A -5 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 PRO A -4 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 ARG A -3 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 GLY A -2 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 SER A -1 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 HIS A 0 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 VAL B -5 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 PRO B -4 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 ARG B -3 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 GLY B -2 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 SER B -1 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 HIS B 0 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 VAL D -5 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 PRO D -4 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 ARG D -3 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 GLY D -2 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 SER D -1 UNP A0A8E4UR4 EXPRESSION TAG
SEQADV 8V16 HIS D 0 UNP A0A8E4UR4 EXPRESSION TAG
SEQRES 1 C 274 VAL PRO ARG GLY SER HIS MET LEU TYR ALA GLN VAL ASN
SEQRES 2 C 274 GLY ILE ASN LEU HIS TYR GLU ILE GLU GLY GLN GLY GLN
SEQRES 3 C 274 PRO LEU LEU LEU ILE MET GLY LEU GLY ALA PRO ALA ALA
SEQRES 4 C 274 ALA TRP ASP PRO ILE PHE VAL GLN THR LEU THR LYS THR
SEQRES 5 C 274 HIS GLN VAL ILE ILE TYR ASP ASN ARG GLY THR GLY LEU
SEQRES 6 C 274 SER ASP LYS PRO ASP MET PRO TYR SER ILE ALA MET PHE
SEQRES 7 C 274 ALA SER ASP ALA VAL GLY LEU LEU ASP ALA LEU ASN ILE
SEQRES 8 C 274 PRO ARG ALA HIS VAL PHE GLY VAL SER MET GLY GLY MET
SEQRES 9 C 274 ILE ALA GLN GLU LEU ALA ILE HIS TYR PRO GLN ARG VAL
SEQRES 10 C 274 ALA SER LEU ILE LEU GLY CYS THR THR PRO GLY GLY LYS
SEQRES 11 C 274 HIS ALA VAL PRO ALA PRO PRO GLU SER LEU LYS ALA LEU
SEQRES 12 C 274 GLU GLY ARG ALA GLY LEU THR PRO GLU GLU ALA ILE ARG
SEQRES 13 C 274 GLU GLY TRP LYS LEU SER PHE SER GLU GLU PHE ILE HIS
SEQRES 14 C 274 THR HIS LYS ALA GLU LEU GLU ALA HIS ILE PRO ARG LEU
SEQRES 15 C 274 LEU ALA GLN LEU THR PRO ARG PHE ALA TYR GLU ARG HIS
SEQRES 16 C 274 PHE GLN ALA THR MET THR LEU ARG VAL PHE LYS GLN LEU
SEQRES 17 C 274 LYS GLU ILE GLN ALA PRO THR LEU VAL ALA THR GLY ARG
SEQRES 18 C 274 ASP ASP MET LEU ILE PRO ALA VAL ASN SER GLU ILE LEU
SEQRES 19 C 274 ALA ARG GLU ILE PRO GLY ALA GLU LEU ALA ILE PHE GLU
SEQRES 20 C 274 SER ALA GLY HIS GLY PHE VAL THR SER ALA ARG GLU PRO
SEQRES 21 C 274 PHE LEU LYS VAL LEU LYS GLU PHE LEU ALA ARG GLN SER
SEQRES 22 C 274 VAL
SEQRES 1 A 274 VAL PRO ARG GLY SER HIS MET LEU TYR ALA GLN VAL ASN
SEQRES 2 A 274 GLY ILE ASN LEU HIS TYR GLU ILE GLU GLY GLN GLY GLN
SEQRES 3 A 274 PRO LEU LEU LEU ILE MET GLY LEU GLY ALA PRO ALA ALA
SEQRES 4 A 274 ALA TRP ASP PRO ILE PHE VAL GLN THR LEU THR LYS THR
SEQRES 5 A 274 HIS GLN VAL ILE ILE TYR ASP ASN ARG GLY THR GLY LEU
SEQRES 6 A 274 SER ASP LYS PRO ASP MET PRO TYR SER ILE ALA MET PHE
SEQRES 7 A 274 ALA SER ASP ALA VAL GLY LEU LEU ASP ALA LEU ASN ILE
SEQRES 8 A 274 PRO ARG ALA HIS VAL PHE GLY VAL SER MET GLY GLY MET
SEQRES 9 A 274 ILE ALA GLN GLU LEU ALA ILE HIS TYR PRO GLN ARG VAL
SEQRES 10 A 274 ALA SER LEU ILE LEU GLY CYS THR THR PRO GLY GLY LYS
SEQRES 11 A 274 HIS ALA VAL PRO ALA PRO PRO GLU SER LEU LYS ALA LEU
SEQRES 12 A 274 GLU GLY ARG ALA GLY LEU THR PRO GLU GLU ALA ILE ARG
SEQRES 13 A 274 GLU GLY TRP LYS LEU SER PHE SER GLU GLU PHE ILE HIS
SEQRES 14 A 274 THR HIS LYS ALA GLU LEU GLU ALA HIS ILE PRO ARG LEU
SEQRES 15 A 274 LEU ALA GLN LEU THR PRO ARG PHE ALA TYR GLU ARG HIS
SEQRES 16 A 274 PHE GLN ALA THR MET THR LEU ARG VAL PHE LYS GLN LEU
SEQRES 17 A 274 LYS GLU ILE GLN ALA PRO THR LEU VAL ALA THR GLY ARG
SEQRES 18 A 274 ASP ASP MET LEU ILE PRO ALA VAL ASN SER GLU ILE LEU
SEQRES 19 A 274 ALA ARG GLU ILE PRO GLY ALA GLU LEU ALA ILE PHE GLU
SEQRES 20 A 274 SER ALA GLY HIS GLY PHE VAL THR SER ALA ARG GLU PRO
SEQRES 21 A 274 PHE LEU LYS VAL LEU LYS GLU PHE LEU ALA ARG GLN SER
SEQRES 22 A 274 VAL
SEQRES 1 B 274 VAL PRO ARG GLY SER HIS MET LEU TYR ALA GLN VAL ASN
SEQRES 2 B 274 GLY ILE ASN LEU HIS TYR GLU ILE GLU GLY GLN GLY GLN
SEQRES 3 B 274 PRO LEU LEU LEU ILE MET GLY LEU GLY ALA PRO ALA ALA
SEQRES 4 B 274 ALA TRP ASP PRO ILE PHE VAL GLN THR LEU THR LYS THR
SEQRES 5 B 274 HIS GLN VAL ILE ILE TYR ASP ASN ARG GLY THR GLY LEU
SEQRES 6 B 274 SER ASP LYS PRO ASP MET PRO TYR SER ILE ALA MET PHE
SEQRES 7 B 274 ALA SER ASP ALA VAL GLY LEU LEU ASP ALA LEU ASN ILE
SEQRES 8 B 274 PRO ARG ALA HIS VAL PHE GLY VAL SER MET GLY GLY MET
SEQRES 9 B 274 ILE ALA GLN GLU LEU ALA ILE HIS TYR PRO GLN ARG VAL
SEQRES 10 B 274 ALA SER LEU ILE LEU GLY CYS THR THR PRO GLY GLY LYS
SEQRES 11 B 274 HIS ALA VAL PRO ALA PRO PRO GLU SER LEU LYS ALA LEU
SEQRES 12 B 274 GLU GLY ARG ALA GLY LEU THR PRO GLU GLU ALA ILE ARG
SEQRES 13 B 274 GLU GLY TRP LYS LEU SER PHE SER GLU GLU PHE ILE HIS
SEQRES 14 B 274 THR HIS LYS ALA GLU LEU GLU ALA HIS ILE PRO ARG LEU
SEQRES 15 B 274 LEU ALA GLN LEU THR PRO ARG PHE ALA TYR GLU ARG HIS
SEQRES 16 B 274 PHE GLN ALA THR MET THR LEU ARG VAL PHE LYS GLN LEU
SEQRES 17 B 274 LYS GLU ILE GLN ALA PRO THR LEU VAL ALA THR GLY ARG
SEQRES 18 B 274 ASP ASP MET LEU ILE PRO ALA VAL ASN SER GLU ILE LEU
SEQRES 19 B 274 ALA ARG GLU ILE PRO GLY ALA GLU LEU ALA ILE PHE GLU
SEQRES 20 B 274 SER ALA GLY HIS GLY PHE VAL THR SER ALA ARG GLU PRO
SEQRES 21 B 274 PHE LEU LYS VAL LEU LYS GLU PHE LEU ALA ARG GLN SER
SEQRES 22 B 274 VAL
SEQRES 1 D 274 VAL PRO ARG GLY SER HIS MET LEU TYR ALA GLN VAL ASN
SEQRES 2 D 274 GLY ILE ASN LEU HIS TYR GLU ILE GLU GLY GLN GLY GLN
SEQRES 3 D 274 PRO LEU LEU LEU ILE MET GLY LEU GLY ALA PRO ALA ALA
SEQRES 4 D 274 ALA TRP ASP PRO ILE PHE VAL GLN THR LEU THR LYS THR
SEQRES 5 D 274 HIS GLN VAL ILE ILE TYR ASP ASN ARG GLY THR GLY LEU
SEQRES 6 D 274 SER ASP LYS PRO ASP MET PRO TYR SER ILE ALA MET PHE
SEQRES 7 D 274 ALA SER ASP ALA VAL GLY LEU LEU ASP ALA LEU ASN ILE
SEQRES 8 D 274 PRO ARG ALA HIS VAL PHE GLY VAL SER MET GLY GLY MET
SEQRES 9 D 274 ILE ALA GLN GLU LEU ALA ILE HIS TYR PRO GLN ARG VAL
SEQRES 10 D 274 ALA SER LEU ILE LEU GLY CYS THR THR PRO GLY GLY LYS
SEQRES 11 D 274 HIS ALA VAL PRO ALA PRO PRO GLU SER LEU LYS ALA LEU
SEQRES 12 D 274 GLU GLY ARG ALA GLY LEU THR PRO GLU GLU ALA ILE ARG
SEQRES 13 D 274 GLU GLY TRP LYS LEU SER PHE SER GLU GLU PHE ILE HIS
SEQRES 14 D 274 THR HIS LYS ALA GLU LEU GLU ALA HIS ILE PRO ARG LEU
SEQRES 15 D 274 LEU ALA GLN LEU THR PRO ARG PHE ALA TYR GLU ARG HIS
SEQRES 16 D 274 PHE GLN ALA THR MET THR LEU ARG VAL PHE LYS GLN LEU
SEQRES 17 D 274 LYS GLU ILE GLN ALA PRO THR LEU VAL ALA THR GLY ARG
SEQRES 18 D 274 ASP ASP MET LEU ILE PRO ALA VAL ASN SER GLU ILE LEU
SEQRES 19 D 274 ALA ARG GLU ILE PRO GLY ALA GLU LEU ALA ILE PHE GLU
SEQRES 20 D 274 SER ALA GLY HIS GLY PHE VAL THR SER ALA ARG GLU PRO
SEQRES 21 D 274 PHE LEU LYS VAL LEU LYS GLU PHE LEU ALA ARG GLN SER
SEQRES 22 D 274 VAL
HET GOL A 301 6
HET GOL A 302 6
HET GOL B 301 6
HET GOL B 302 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *357(H2 O)
HELIX 1 AA1 PRO C 31 TRP C 35 5 5
HELIX 2 AA2 ASP C 36 THR C 44 1 9
HELIX 3 AA3 SER C 68 LEU C 83 1 16
HELIX 4 AA4 SER C 94 TYR C 107 1 14
HELIX 5 AA5 THR C 144 LYS C 154 1 11
HELIX 6 AA6 SER C 158 HIS C 165 1 8
HELIX 7 AA7 HIS C 165 ALA C 178 1 14
HELIX 8 AA8 PRO C 182 THR C 193 1 12
HELIX 9 AA9 VAL C 198 ILE C 205 5 8
HELIX 10 AB1 ALA C 222 ILE C 232 1 11
HELIX 11 AB2 GLY C 246 ALA C 251 1 6
HELIX 12 AB3 ALA C 251 ARG C 265 1 15
HELIX 13 AB4 PRO A 31 TRP A 35 5 5
HELIX 14 AB5 ASP A 36 THR A 44 1 9
HELIX 15 AB6 SER A 68 LEU A 83 1 16
HELIX 16 AB7 SER A 94 TYR A 107 1 14
HELIX 17 AB8 PRO A 130 LEU A 137 1 8
HELIX 18 AB9 THR A 144 PHE A 157 1 14
HELIX 19 AC1 SER A 158 HIS A 165 1 8
HELIX 20 AC2 HIS A 165 ALA A 171 1 7
HELIX 21 AC3 HIS A 172 GLN A 179 1 8
HELIX 22 AC4 PRO A 182 THR A 193 1 12
HELIX 23 AC5 VAL A 198 ILE A 205 5 8
HELIX 24 AC6 ALA A 222 ILE A 232 1 11
HELIX 25 AC7 GLY A 246 ALA A 251 1 6
HELIX 26 AC8 ALA A 251 ARG A 265 1 15
HELIX 27 AC9 PRO B 31 TRP B 35 5 5
HELIX 28 AD1 ASP B 36 THR B 44 1 9
HELIX 29 AD2 SER B 68 LEU B 83 1 16
HELIX 30 AD3 SER B 94 TYR B 107 1 14
HELIX 31 AD4 PRO B 130 ARG B 140 1 11
HELIX 32 AD5 ALA B 141 LEU B 143 5 3
HELIX 33 AD6 THR B 144 PHE B 157 1 14
HELIX 34 AD7 SER B 158 HIS B 165 1 8
HELIX 35 AD8 HIS B 165 HIS B 172 1 8
HELIX 36 AD9 HIS B 172 GLN B 179 1 8
HELIX 37 AE1 PRO B 182 THR B 193 1 12
HELIX 38 AE2 VAL B 198 ILE B 205 5 8
HELIX 39 AE3 ALA B 222 ILE B 232 1 11
HELIX 40 AE4 GLY B 246 ALA B 251 1 6
HELIX 41 AE5 ALA B 251 ARG B 265 1 15
HELIX 42 AE6 PRO D 31 TRP D 35 5 5
HELIX 43 AE7 ASP D 36 THR D 44 1 9
HELIX 44 AE8 SER D 68 LEU D 83 1 16
HELIX 45 AE9 SER D 94 TYR D 107 1 14
HELIX 46 AF1 PRO D 130 ALA D 136 1 7
HELIX 47 AF2 THR D 144 PHE D 157 1 14
HELIX 48 AF3 SER D 158 HIS D 165 1 8
HELIX 49 AF4 HIS D 165 HIS D 172 1 8
HELIX 50 AF5 HIS D 172 ALA D 178 1 7
HELIX 51 AF6 PRO D 182 THR D 193 1 12
HELIX 52 AF7 GLN D 201 ILE D 205 5 5
HELIX 53 AF8 ALA D 222 ILE D 232 1 11
HELIX 54 AF9 GLY D 246 ALA D 251 1 6
HELIX 55 AG1 ALA D 251 ALA D 264 1 14
SHEET 1 AA116 GLU C 236 PHE C 240 0
SHEET 2 AA116 THR C 209 GLY C 214 1 N VAL C 211 O GLU C 236
SHEET 3 AA116 VAL C 111 GLY C 117 1 N LEU C 114 O LEU C 210
SHEET 4 AA116 ALA C 88 VAL C 93 1 N VAL C 90 O ILE C 115
SHEET 5 AA116 GLN C 20 ILE C 25 1 N LEU C 23 O HIS C 89
SHEET 6 AA116 HIS C 47 TYR C 52 1 O GLN C 48 N LEU C 22
SHEET 7 AA116 ILE C 9 GLU C 16 -1 N GLU C 16 O VAL C 49
SHEET 8 AA116 LEU C 2 VAL C 6 -1 N VAL C 6 O ILE C 9
SHEET 9 AA116 LEU D 2 VAL D 6 -1 O TYR D 3 N TYR C 3
SHEET 10 AA116 ILE D 9 GLU D 16 -1 O ILE D 9 N VAL D 6
SHEET 11 AA116 GLN D 48 TYR D 52 -1 O VAL D 49 N GLU D 16
SHEET 12 AA116 PRO D 21 ILE D 25 1 N LEU D 24 O ILE D 50
SHEET 13 AA116 ALA D 88 VAL D 93 1 O HIS D 89 N LEU D 23
SHEET 14 AA116 VAL D 111 GLY D 117 1 O ILE D 115 N VAL D 90
SHEET 15 AA116 THR D 209 GLY D 214 1 O ALA D 212 N LEU D 116
SHEET 16 AA116 GLU D 236 PHE D 240 1 O GLU D 236 N THR D 209
SHEET 1 AA2 8 LEU A 2 VAL A 6 0
SHEET 2 AA2 8 ILE A 9 GLU A 16 -1 O LEU A 11 N ALA A 4
SHEET 3 AA2 8 HIS A 47 TYR A 52 -1 O ILE A 51 N GLU A 14
SHEET 4 AA2 8 GLN A 20 ILE A 25 1 N LEU A 22 O ILE A 50
SHEET 5 AA2 8 ALA A 88 VAL A 93 1 O HIS A 89 N LEU A 23
SHEET 6 AA2 8 VAL A 111 GLY A 117 1 O GLY A 117 N GLY A 92
SHEET 7 AA2 8 THR A 209 GLY A 214 1 O LEU A 210 N LEU A 116
SHEET 8 AA2 8 GLU A 236 PHE A 240 1 O GLU A 236 N VAL A 211
SHEET 1 AA3 8 LEU B 2 VAL B 6 0
SHEET 2 AA3 8 ILE B 9 GLU B 16 -1 O ILE B 9 N VAL B 6
SHEET 3 AA3 8 GLN B 48 TYR B 52 -1 O VAL B 49 N GLU B 16
SHEET 4 AA3 8 PRO B 21 ILE B 25 1 N LEU B 22 O ILE B 50
SHEET 5 AA3 8 ALA B 88 VAL B 93 1 O HIS B 89 N LEU B 23
SHEET 6 AA3 8 VAL B 111 GLY B 117 1 O GLY B 117 N GLY B 92
SHEET 7 AA3 8 THR B 209 GLY B 214 1 O LEU B 210 N LEU B 114
SHEET 8 AA3 8 GLU B 236 PHE B 240 1 O ALA B 238 N VAL B 211
CRYST1 72.076 105.891 145.371 90.00 90.00 90.00 P 21 21 21 16
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 0.013874 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009444 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006879 0.00000
TER 1988 VAL C 268
TER 4029 VAL A 268
TER 6146 VAL B 268
TER 8218 VAL D 268
MASTER 381 0 4 55 32 0 0 6 8571 4 24 88
END |