| content |
HEADER HYDROLASE 30-MAR-09 3GUU
TITLE X-RAY STRUCTURE OF CANDIDA ANTARCTICA LIPASE A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ANTARCTICA;
SOURCE 3 ORGANISM_TAXID: 34362;
SOURCE 4 OTHER_DETAILS: COMMERIAL ENZYME ROCHE CHIRAZYME L-5
KEYWDS CANDIDA, LIPASE, PROTEIN STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.-M.BRANDT,X.-G.LI,Y.NYMALM-REJSTROM,T.AIRENNE,L.T.KANERVA,
AUTHOR 2 T.A.SALMINEN
REVDAT 1 31-MAR-10 3GUU 0
JRNL AUTH A.-M.BRANDT,X.-G.LI,Y.NYMALM-REJSTROM,T.AIRENNE,
JRNL AUTH 2 L.T.KANERVA,T.A.SALMINEN
JRNL TITL THE CRYSTAL STRUCTURE OF LIPASE A FROM CANDIDA
JRNL TITL 2 ANTARCTICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0040
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 71879
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3784
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5208
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 275
REMARK 3 BIN FREE R VALUE : 0.2300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6535
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 499
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : -0.94000
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): 0.166
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.158
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.309
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6789 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 8 ; 0.120 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9286 ; 1.713 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16 ; 3.689 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 868 ; 6.131 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 277 ;32.190 ;25.018
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 978 ;15.092 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;19.455 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1035 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5250 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3377 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 17 ; 0.375 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4686 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5 ; 0.124 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 541 ; 0.178 ; 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): 50 ; 0.178 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.134 ; 0.200
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): 4444 ; 0.869 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7018 ; 1.339 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2689 ; 2.366 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2268 ; 3.487 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 12 A 441 5
REMARK 3 1 B 12 B 441 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1711 ; 0.15 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 1524 ; 0.33 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1711 ; 0.84 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1524 ; 1.16 ; 10.00
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3GUU COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052334.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93300
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : INTEGRATE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86764
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.17400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.43300
REMARK 200 R SYM FOR SHELL (I) : 0.43400
REMARK 200 FOR SHELL : 4.420
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2VEO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULFATE, 12%
REMARK 280 GLYCEROL, 100MM TRIS-HCL PH 8.5 , VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 294.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -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 -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 150.20000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 46.05000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 46.05000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 225.30000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 46.05000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 46.05000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 75.10000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 46.05000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.05000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 225.30000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 46.05000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.05000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 75.10000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 150.20000
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 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 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 -20
REMARK 465 ARG A -19
REMARK 465 VAL A -18
REMARK 465 SER A -17
REMARK 465 LEU A -16
REMARK 465 ARG A -15
REMARK 465 SER A -14
REMARK 465 ILE A -13
REMARK 465 THR A -12
REMARK 465 SER A -11
REMARK 465 LEU A -10
REMARK 465 LEU A -9
REMARK 465 ALA A -8
REMARK 465 ALA A -7
REMARK 465 ALA A -6
REMARK 465 THR A -5
REMARK 465 ALA A -4
REMARK 465 ALA A -3
REMARK 465 VAL A -2
REMARK 465 LEU A -1
REMARK 465 ALA A 0
REMARK 465 ALA A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 GLU A 5
REMARK 465 THR A 6
REMARK 465 LEU A 7
REMARK 465 ASP A 8
REMARK 465 ARG A 9
REMARK 465 ARG A 10
REMARK 465 MET B -20
REMARK 465 ARG B -19
REMARK 465 VAL B -18
REMARK 465 SER B -17
REMARK 465 LEU B -16
REMARK 465 ARG B -15
REMARK 465 SER B -14
REMARK 465 ILE B -13
REMARK 465 THR B -12
REMARK 465 SER B -11
REMARK 465 LEU B -10
REMARK 465 LEU B -9
REMARK 465 ALA B -8
REMARK 465 ALA B -7
REMARK 465 ALA B -6
REMARK 465 THR B -5
REMARK 465 ALA B -4
REMARK 465 ALA B -3
REMARK 465 VAL B -2
REMARK 465 LEU B -1
REMARK 465 ALA B 0
REMARK 465 ALA B 1
REMARK 465 PRO B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 GLU B 5
REMARK 465 THR B 6
REMARK 465 LEU B 7
REMARK 465 ASP B 8
REMARK 465 ARG B 9
REMARK 465 ARG B 10
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 PRO A 441 O
REMARK 470 PRO B 441 O
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 B 588 O HOH B 676 1.60
REMARK 500 O HOH A 608 O HOH A 665 1.75
REMARK 500 O HOH A 625 O HOH A 650 1.96
REMARK 500 CG1 ILE B 127 O HOH B 631 2.05
REMARK 500 O HOH B 607 O HOH B 667 2.08
REMARK 500 OE1 GLU A 365 O HOH A 453 2.13
REMARK 500 O HOH A 668 O HOH B 621 2.15
REMARK 500 OE1 GLN B 65 O HOH B 673 2.15
REMARK 500 ND1 HIS A 245 O3 GOL A 443 2.16
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 ASP A 95 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 247 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 326 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 LEU A 367 CA - CB - CG ANGL. DEV. = -22.6 DEGREES
REMARK 500 ARG B 60 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 60 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 LEU B 367 CA - CB - CG ANGL. DEV. = -22.2 DEGREES
REMARK 500 LEU B 367 CB - CG - CD1 ANGL. DEV. = 10.8 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 TYR A 22 45.70 -95.86
REMARK 500 VAL A 120 -165.21 -115.54
REMARK 500 LEU A 121 -123.10 68.17
REMARK 500 ILE A 150 4.41 85.32
REMARK 500 SER A 184 -127.42 64.77
REMARK 500 ALA A 201 59.97 -140.79
REMARK 500 CYS A 273 -167.84 -110.33
REMARK 500 GLU A 308 49.56 -91.32
REMARK 500 ILE A 404 -63.62 -108.05
REMARK 500 TYR B 22 54.63 -96.82
REMARK 500 THR B 61 -157.65 -131.20
REMARK 500 VAL B 120 -159.36 -107.23
REMARK 500 LEU B 121 -126.99 69.79
REMARK 500 ILE B 150 -0.32 80.73
REMARK 500 SER B 184 -122.58 61.21
REMARK 500 CYS B 273 -161.53 -124.27
REMARK 500 GLU B 308 54.63 -95.42
REMARK 500 ILE B 404 -66.25 -124.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP B 122 24.1 L L OUTSIDE RANGE
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 619 DISTANCE = 5.20 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 442
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 443
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 442
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 443
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS NO UNP REFERENCE SEQUENCE DATABASE FOR THIS PROTEIN
REMARK 999 AT THE TIME OF PROCESSING.
REMARK 999 THIS SEQUENCE IS REFERRED IN CAN.J.BOT. VOL 73 (1995), PP.
REMARK 999 S869-S875; HOEGH, S. ET.
DBREF 3GUU A -20 441 PDB 3GUU 3GUU 1 462
DBREF 3GUU B -20 441 PDB 3GUU 3GUU 1 462
SEQRES 1 A 462 MET ARG VAL SER LEU ARG SER ILE THR SER LEU LEU ALA
SEQRES 2 A 462 ALA ALA THR ALA ALA VAL LEU ALA ALA PRO ALA ALA GLU
SEQRES 3 A 462 THR LEU ASP ARG ARG ALA ALA LEU PRO ASN PRO TYR ASP
SEQRES 4 A 462 ASP PRO PHE TYR THR THR PRO SER ASN ILE GLY THR PHE
SEQRES 5 A 462 ALA LYS GLY GLN VAL ILE GLN SER ARG LYS VAL PRO THR
SEQRES 6 A 462 ASP ILE GLY ASN ALA ASN ASN ALA ALA SER PHE GLN LEU
SEQRES 7 A 462 GLN TYR ARG THR THR ASN THR GLN ASN GLU ALA VAL ALA
SEQRES 8 A 462 ASP VAL ALA THR VAL TRP ILE PRO ALA LYS PRO ALA SER
SEQRES 9 A 462 PRO PRO LYS ILE PHE SER TYR GLN VAL TYR GLU ASP ALA
SEQRES 10 A 462 THR ALA LEU ASP CYS ALA PRO SER TYR SER TYR LEU THR
SEQRES 11 A 462 GLY LEU ASP GLN PRO ASN LYS VAL THR ALA VAL LEU ASP
SEQRES 12 A 462 THR PRO ILE ILE ILE GLY TRP ALA LEU GLN GLN GLY TYR
SEQRES 13 A 462 TYR VAL VAL SER SER ASP HIS GLU GLY PHE LYS ALA ALA
SEQRES 14 A 462 PHE ILE ALA GLY TYR GLU GLU GLY MET ALA ILE LEU ASP
SEQRES 15 A 462 GLY ILE ARG ALA LEU LYS ASN TYR GLN ASN LEU PRO SER
SEQRES 16 A 462 ASP SER LYS VAL ALA LEU GLU GLY TYR SER GLY GLY ALA
SEQRES 17 A 462 HIS ALA THR VAL TRP ALA THR SER LEU ALA GLU SER TYR
SEQRES 18 A 462 ALA PRO GLU LEU ASN ILE VAL GLY ALA SER HIS GLY GLY
SEQRES 19 A 462 THR PRO VAL SER ALA LYS ASP THR PHE THR PHE LEU ASN
SEQRES 20 A 462 GLY GLY PRO PHE ALA GLY PHE ALA LEU ALA GLY VAL SER
SEQRES 21 A 462 GLY LEU SER LEU ALA HIS PRO ASP MET GLU SER PHE ILE
SEQRES 22 A 462 GLU ALA ARG LEU ASN ALA LYS GLY GLN ARG THR LEU LYS
SEQRES 23 A 462 GLN ILE ARG GLY ARG GLY PHE CYS LEU PRO GLN VAL VAL
SEQRES 24 A 462 LEU THR TYR PRO PHE LEU ASN VAL PHE SER LEU VAL ASN
SEQRES 25 A 462 ASP THR ASN LEU LEU ASN GLU ALA PRO ILE ALA SER ILE
SEQRES 26 A 462 LEU LYS GLN GLU THR VAL VAL GLN ALA GLU ALA SER TYR
SEQRES 27 A 462 THR VAL SER VAL PRO LYS PHE PRO ARG PHE ILE TRP HIS
SEQRES 28 A 462 ALA ILE PRO ASP GLU ILE VAL PRO TYR GLN PRO ALA ALA
SEQRES 29 A 462 THR TYR VAL LYS GLU GLN CYS ALA LYS GLY ALA ASN ILE
SEQRES 30 A 462 ASN PHE SER PRO TYR PRO ILE ALA GLU HIS LEU THR ALA
SEQRES 31 A 462 GLU ILE PHE GLY LEU VAL PRO SER LEU TRP PHE ILE LYS
SEQRES 32 A 462 GLN ALA PHE ASP GLY THR THR PRO LYS VAL ILE CYS GLY
SEQRES 33 A 462 THR PRO ILE PRO ALA ILE ALA GLY ILE THR THR PRO SER
SEQRES 34 A 462 ALA ASP GLN VAL LEU GLY SER ASP LEU ALA ASN GLN LEU
SEQRES 35 A 462 ARG SER LEU ASP GLY LYS GLN SER ALA PHE GLY LYS PRO
SEQRES 36 A 462 PHE GLY PRO ILE THR PRO PRO
SEQRES 1 B 462 MET ARG VAL SER LEU ARG SER ILE THR SER LEU LEU ALA
SEQRES 2 B 462 ALA ALA THR ALA ALA VAL LEU ALA ALA PRO ALA ALA GLU
SEQRES 3 B 462 THR LEU ASP ARG ARG ALA ALA LEU PRO ASN PRO TYR ASP
SEQRES 4 B 462 ASP PRO PHE TYR THR THR PRO SER ASN ILE GLY THR PHE
SEQRES 5 B 462 ALA LYS GLY GLN VAL ILE GLN SER ARG LYS VAL PRO THR
SEQRES 6 B 462 ASP ILE GLY ASN ALA ASN ASN ALA ALA SER PHE GLN LEU
SEQRES 7 B 462 GLN TYR ARG THR THR ASN THR GLN ASN GLU ALA VAL ALA
SEQRES 8 B 462 ASP VAL ALA THR VAL TRP ILE PRO ALA LYS PRO ALA SER
SEQRES 9 B 462 PRO PRO LYS ILE PHE SER TYR GLN VAL TYR GLU ASP ALA
SEQRES 10 B 462 THR ALA LEU ASP CYS ALA PRO SER TYR SER TYR LEU THR
SEQRES 11 B 462 GLY LEU ASP GLN PRO ASN LYS VAL THR ALA VAL LEU ASP
SEQRES 12 B 462 THR PRO ILE ILE ILE GLY TRP ALA LEU GLN GLN GLY TYR
SEQRES 13 B 462 TYR VAL VAL SER SER ASP HIS GLU GLY PHE LYS ALA ALA
SEQRES 14 B 462 PHE ILE ALA GLY TYR GLU GLU GLY MET ALA ILE LEU ASP
SEQRES 15 B 462 GLY ILE ARG ALA LEU LYS ASN TYR GLN ASN LEU PRO SER
SEQRES 16 B 462 ASP SER LYS VAL ALA LEU GLU GLY TYR SER GLY GLY ALA
SEQRES 17 B 462 HIS ALA THR VAL TRP ALA THR SER LEU ALA GLU SER TYR
SEQRES 18 B 462 ALA PRO GLU LEU ASN ILE VAL GLY ALA SER HIS GLY GLY
SEQRES 19 B 462 THR PRO VAL SER ALA LYS ASP THR PHE THR PHE LEU ASN
SEQRES 20 B 462 GLY GLY PRO PHE ALA GLY PHE ALA LEU ALA GLY VAL SER
SEQRES 21 B 462 GLY LEU SER LEU ALA HIS PRO ASP MET GLU SER PHE ILE
SEQRES 22 B 462 GLU ALA ARG LEU ASN ALA LYS GLY GLN ARG THR LEU LYS
SEQRES 23 B 462 GLN ILE ARG GLY ARG GLY PHE CYS LEU PRO GLN VAL VAL
SEQRES 24 B 462 LEU THR TYR PRO PHE LEU ASN VAL PHE SER LEU VAL ASN
SEQRES 25 B 462 ASP THR ASN LEU LEU ASN GLU ALA PRO ILE ALA SER ILE
SEQRES 26 B 462 LEU LYS GLN GLU THR VAL VAL GLN ALA GLU ALA SER TYR
SEQRES 27 B 462 THR VAL SER VAL PRO LYS PHE PRO ARG PHE ILE TRP HIS
SEQRES 28 B 462 ALA ILE PRO ASP GLU ILE VAL PRO TYR GLN PRO ALA ALA
SEQRES 29 B 462 THR TYR VAL LYS GLU GLN CYS ALA LYS GLY ALA ASN ILE
SEQRES 30 B 462 ASN PHE SER PRO TYR PRO ILE ALA GLU HIS LEU THR ALA
SEQRES 31 B 462 GLU ILE PHE GLY LEU VAL PRO SER LEU TRP PHE ILE LYS
SEQRES 32 B 462 GLN ALA PHE ASP GLY THR THR PRO LYS VAL ILE CYS GLY
SEQRES 33 B 462 THR PRO ILE PRO ALA ILE ALA GLY ILE THR THR PRO SER
SEQRES 34 B 462 ALA ASP GLN VAL LEU GLY SER ASP LEU ALA ASN GLN LEU
SEQRES 35 B 462 ARG SER LEU ASP GLY LYS GLN SER ALA PHE GLY LYS PRO
SEQRES 36 B 462 PHE GLY PRO ILE THR PRO PRO
HET 1PE A 442 16
HET GOL A 443 6
HET 1PE B 442 16
HET SO4 B 443 5
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN 1PE PEG400
FORMUL 3 1PE 2(C10 H22 O6)
FORMUL 4 GOL C3 H8 O3
FORMUL 6 SO4 O4 S 2-
FORMUL 7 HOH *499(H2 O)
HELIX 1 1 ASN A 15 THR A 23 5 9
HELIX 2 2 ASN A 27 PHE A 31 5 5
HELIX 3 3 THR A 44 ASN A 50 1 7
HELIX 4 4 ALA A 98 CYS A 101 5 4
HELIX 5 5 ALA A 102 LEU A 108 1 7
HELIX 6 6 ASN A 115 VAL A 120 5 6
HELIX 7 7 LEU A 121 GLN A 133 1 13
HELIX 8 8 ALA A 151 GLN A 170 1 20
HELIX 9 9 SER A 184 ALA A 201 1 18
HELIX 10 10 SER A 217 ASN A 226 1 10
HELIX 11 11 PHE A 230 HIS A 245 1 16
HELIX 12 12 HIS A 245 ALA A 254 1 10
HELIX 13 13 ASN A 257 ARG A 268 1 12
HELIX 14 14 CYS A 273 TYR A 281 1 9
HELIX 15 15 ASN A 285 VAL A 290 5 6
HELIX 16 16 ASN A 294 GLU A 298 5 5
HELIX 17 17 PRO A 300 GLU A 308 1 9
HELIX 18 18 PRO A 338 LYS A 352 1 15
HELIX 19 19 GLU A 365 GLY A 373 1 9
HELIX 20 20 GLY A 373 GLY A 387 1 15
HELIX 21 21 SER A 408 GLY A 414 1 7
HELIX 22 22 GLY A 414 LEU A 424 1 11
HELIX 23 23 ASN B 15 THR B 23 5 9
HELIX 24 24 ASN B 27 PHE B 31 5 5
HELIX 25 25 THR B 44 ASN B 51 1 8
HELIX 26 26 ALA B 98 CYS B 101 5 4
HELIX 27 27 ALA B 102 LEU B 108 1 7
HELIX 28 28 ASN B 115 VAL B 120 5 6
HELIX 29 29 ASP B 122 GLN B 133 1 12
HELIX 30 30 ALA B 151 GLN B 170 1 20
HELIX 31 31 SER B 184 ALA B 201 1 18
HELIX 32 32 SER B 217 ASN B 226 1 10
HELIX 33 33 PHE B 230 HIS B 245 1 16
HELIX 34 34 HIS B 245 ALA B 254 1 10
HELIX 35 35 ASN B 257 GLY B 269 1 13
HELIX 36 36 CYS B 273 TYR B 281 1 9
HELIX 37 37 ASN B 285 VAL B 290 5 6
HELIX 38 38 ASN B 294 GLU B 298 5 5
HELIX 39 39 PRO B 300 LYS B 306 1 7
HELIX 40 40 PRO B 338 LYS B 352 1 15
HELIX 41 41 GLU B 365 GLY B 373 1 9
HELIX 42 42 GLY B 373 GLY B 387 1 15
HELIX 43 43 SER B 408 GLY B 414 1 7
HELIX 44 44 GLY B 414 SER B 423 1 10
SHEET 1 A 9 VAL A 36 LYS A 41 0
SHEET 2 A 9 ALA A 53 THR A 62 -1 O GLN A 58 N GLN A 38
SHEET 3 A 9 ALA A 68 ILE A 77 -1 O VAL A 69 N THR A 61
SHEET 4 A 9 TYR A 136 SER A 140 -1 O SER A 139 N THR A 74
SHEET 5 A 9 LYS A 86 GLN A 91 1 N PHE A 88 O TYR A 136
SHEET 6 A 9 LYS A 177 TYR A 183 1 O ALA A 179 N SER A 89
SHEET 7 A 9 ASN A 205 GLY A 212 1 O VAL A 207 N VAL A 178
SHEET 8 A 9 PRO A 325 ALA A 331 1 O PHE A 327 N ALA A 209
SHEET 9 A 9 ASN A 355 TYR A 361 1 O ASN A 357 N ARG A 326
SHEET 1 B 9 VAL B 36 LYS B 41 0
SHEET 2 B 9 ALA B 53 THR B 62 -1 O GLN B 58 N ILE B 37
SHEET 3 B 9 ALA B 68 ILE B 77 -1 O VAL B 69 N THR B 61
SHEET 4 B 9 TYR B 136 SER B 140 -1 O SER B 139 N THR B 74
SHEET 5 B 9 LYS B 86 GLN B 91 1 N PHE B 88 O TYR B 136
SHEET 6 B 9 LYS B 177 TYR B 183 1 O LYS B 177 N ILE B 87
SHEET 7 B 9 ASN B 205 GLY B 212 1 O VAL B 207 N VAL B 178
SHEET 8 B 9 PRO B 325 ALA B 331 1 O PHE B 327 N HIS B 211
SHEET 9 B 9 ASN B 355 TYR B 361 1 O SER B 359 N ILE B 328
SSBOND 1 CYS A 101 CYS A 273 1555 1555 1.96
SSBOND 2 CYS A 350 CYS A 394 1555 1555 2.07
SSBOND 3 CYS B 101 CYS B 273 1555 1555 2.05
SSBOND 4 CYS B 350 CYS B 394 1555 1555 2.10
CISPEP 1 SER A 83 PRO A 84 0 -2.19
CISPEP 2 ALA A 299 PRO A 300 0 4.35
CISPEP 3 SER B 83 PRO B 84 0 -1.77
CISPEP 4 ALA B 299 PRO B 300 0 1.46
SITE 1 AC1 11 ASP A 95 PHE A 149 SER A 184 GLY A 185
SITE 2 AC1 11 ALA A 218 THR A 221 PHE A 222 PHE A 233
SITE 3 AC1 11 LEU A 241 LEU A 296 PHE A 431
SITE 1 AC2 7 GLN A 65 HIS A 245 PRO A 246 ASP A 247
SITE 2 AC2 7 MET A 248 PRO A 300 ILE A 304
SITE 1 AC3 9 ASP B 95 SER B 184 GLY B 185 ALA B 218
SITE 2 AC3 9 THR B 221 PHE B 222 PHE B 233 VAL B 238
SITE 3 AC3 9 LEU B 296
SITE 1 AC4 4 HIS B 245 PRO B 246 ASP B 247 MET B 248
CRYST1 92.100 92.100 300.400 90.00 90.00 90.00 P 43 21 2 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 0.010858 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010858 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003329 0.00000
TER 3273 PRO A 441
TER 6537 PRO B 441
MASTER 479 0 4 44 18 0 9 6 7077 2 51 72
END |