HEADER TRANSFERASE 08-FEB-08 2VO4
TITLE GLUTATHIONE TRANSFERASE FROM GLYCINE MAX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2,4-D INDUCIBLE GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLUTATHIONE-S-TRANSFERASE, GSTA;
COMPND 5 EC: 2.5.1.18
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE 3 ORGANISM_COMMON: SOYBEAN;
SOURCE 4 ORGANISM_TAXID: 3847
KEYWDS HERBICIDE, GLYCINE MAX, TRANSFERASE, TAU CLASS GST, S-(P-NITROBENZYL-
KEYWDS 2 GLUTATHIONE)
EXPDTA X-RAY DIFFRACTION
AUTHOR I.AXARLI,P.DHAVALA,A.C.PAPAGEORGIOU,N.E.LABROU
REVDAT 6 13-DEC-23 2VO4 1 REMARK
REVDAT 5 24-JUL-19 2VO4 1 REMARK
REVDAT 4 13-JUL-11 2VO4 1 VERSN
REVDAT 3 20-JAN-09 2VO4 1 JRNL REMARK
REVDAT 2 23-DEC-08 2VO4 1 REMARK
REVDAT 1 02-DEC-08 2VO4 0
JRNL AUTH I.AXARLI,P.DHAVALA,A.C.PAPAGEORGIOU,N.E.LABROU
JRNL TITL CRYSTALLOGRAPHIC AND FUNCTIONAL CHARACTERIZATION OF THE
JRNL TITL 2 FLUORODIFEN-INDUCIBLE GLUTATHIONE TRANSFERASE FROM GLYCINE
JRNL TITL 3 MAX REVEALS AN ACTIVE SITE TOPOGRAPHY SUITED FOR
JRNL TITL 4 DIPHENYLETHER HERBICIDES AND A NOVEL L-SITE.
JRNL REF J.MOL.BIOL. V. 385 984 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19014949
JRNL DOI 10.1016/J.JMB.2008.10.084
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 45117
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2400
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3280
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 174
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3622
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 94
REMARK 3 SOLVENT ATOMS : 430
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.22000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : -0.45000
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): 0.135
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.379
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3909 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5289 ; 1.634 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 466 ;10.064 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 184 ;36.227 ;24.783
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 732 ;15.984 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;17.161 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 548 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2973 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2058 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2669 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 363 ; 0.454 ; 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): 112 ; 0.253 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 47 ; 0.274 ; 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): 2308 ; 0.942 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3644 ; 1.483 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1853 ; 2.411 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1632 ; 3.721 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 219
REMARK 3 RESIDUE RANGE : A 1 A 219
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6605 -23.4754 -5.9035
REMARK 3 T TENSOR
REMARK 3 T11: -0.0927 T22: 0.0514
REMARK 3 T33: -0.0676 T12: -0.0196
REMARK 3 T13: -0.0021 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 0.7422 L22: 0.5281
REMARK 3 L33: 0.4149 L12: -0.1467
REMARK 3 L13: -0.0801 L23: 0.0416
REMARK 3 S TENSOR
REMARK 3 S11: -0.0225 S12: -0.2613 S13: 0.0294
REMARK 3 S21: 0.0288 S22: 0.0511 S23: -0.0105
REMARK 3 S31: -0.0109 S32: 0.0167 S33: -0.0286
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2VO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1290035278.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8088
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48045
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 70.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 42.00
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
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 1OYJ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 55.91500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 45.68750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 45.68750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.95750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 45.68750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 45.68750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 83.87250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 45.68750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.68750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.95750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 45.68750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.68750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 83.87250
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 55.91500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2104 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2211 LIES ON A SPECIAL POSITION.
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 O2 GOL A 1222 O HOH A 2226 1.60
REMARK 500 NH1 ARG B 92 O HOH B 2132 1.62
REMARK 500 O2 GOL B 1222 O HOH B 2210 1.68
REMARK 500 O HOH A 2154 O HOH A 2157 1.84
REMARK 500 OE1 GLN B 91 O HOH B 2131 1.94
REMARK 500 O HOH B 2118 O HOH B 2121 1.95
REMARK 500 O HOH A 2026 O HOH A 2092 1.99
REMARK 500 O HOH A 2076 O HOH B 2056 2.07
REMARK 500 O HOH B 2153 O HOH B 2154 2.16
REMARK 500 O HOH A 2054 O HOH A 2055 2.17
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 GLN A 2 N - CA - C ANGL. DEV. = -17.9 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 ASN A 39 66.84 -155.86
REMARK 500 GLU A 66 112.95 80.31
REMARK 500 ASN A 82 103.77 -7.66
REMARK 500 GLU A 137 -72.23 -6.97
REMARK 500 GLN B 2 -57.43 63.60
REMARK 500 ASN B 39 76.86 -151.28
REMARK 500 GLU B 66 113.14 78.34
REMARK 500 ASN B 82 104.40 -7.23
REMARK 500 LYS B 104 -108.18 -56.93
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 MET A 1 GLN A 2 -117.93
REMARK 500 GLU A 136 GLU A 137 134.33
REMARK 500 MET B 1 GLN B 2 32.04
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 B2009 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B2010 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH B2019 DISTANCE = 6.76 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTB A1220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTB B1220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4NM A1221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4NM B1221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1222
DBREF 2VO4 A 1 219 UNP O49235 O49235_SOYBN 1 219
DBREF 2VO4 B 1 219 UNP O49235 O49235_SOYBN 1 219
SEQADV 2VO4 GLN A 2 UNP O49235 SER 2 CONFLICT
SEQADV 2VO4 GLN B 2 UNP O49235 SER 2 CONFLICT
SEQRES 1 A 219 MET GLN ASP GLU VAL VAL LEU LEU ASP PHE TRP PRO SER
SEQRES 2 A 219 PRO PHE GLY MET ARG VAL ARG ILE ALA LEU ALA GLU LYS
SEQRES 3 A 219 GLY ILE LYS TYR GLU TYR LYS GLU GLU ASP LEU ARG ASN
SEQRES 4 A 219 LYS SER PRO LEU LEU LEU GLN MET ASN PRO VAL HIS LYS
SEQRES 5 A 219 LYS ILE PRO VAL LEU ILE HIS ASN GLY LYS PRO ILE CYS
SEQRES 6 A 219 GLU SER LEU ILE ALA VAL GLN TYR ILE GLU GLU VAL TRP
SEQRES 7 A 219 ASN ASP ARG ASN PRO LEU LEU PRO SER ASP PRO TYR GLN
SEQRES 8 A 219 ARG ALA GLN THR ARG PHE TRP ALA ASP TYR VAL ASP LYS
SEQRES 9 A 219 LYS ILE TYR ASP LEU GLY ARG LYS ILE TRP THR SER LYS
SEQRES 10 A 219 GLY GLU GLU LYS GLU ALA ALA LYS LYS GLU PHE ILE GLU
SEQRES 11 A 219 ALA LEU LYS LEU LEU GLU GLU GLN LEU GLY ASP LYS THR
SEQRES 12 A 219 TYR PHE GLY GLY ASP ASN LEU GLY PHE VAL ASP ILE ALA
SEQRES 13 A 219 LEU VAL PRO PHE TYR THR TRP PHE LYS ALA TYR GLU THR
SEQRES 14 A 219 PHE GLY THR LEU ASN ILE GLU SER GLU CYS PRO LYS PHE
SEQRES 15 A 219 ILE ALA TRP ALA LYS ARG CYS LEU GLN LYS GLU SER VAL
SEQRES 16 A 219 ALA LYS SER LEU PRO ASP GLN GLN LYS VAL TYR GLU PHE
SEQRES 17 A 219 ILE MET ASP LEU ARG LYS LYS LEU GLY ILE GLU
SEQRES 1 B 219 MET GLN ASP GLU VAL VAL LEU LEU ASP PHE TRP PRO SER
SEQRES 2 B 219 PRO PHE GLY MET ARG VAL ARG ILE ALA LEU ALA GLU LYS
SEQRES 3 B 219 GLY ILE LYS TYR GLU TYR LYS GLU GLU ASP LEU ARG ASN
SEQRES 4 B 219 LYS SER PRO LEU LEU LEU GLN MET ASN PRO VAL HIS LYS
SEQRES 5 B 219 LYS ILE PRO VAL LEU ILE HIS ASN GLY LYS PRO ILE CYS
SEQRES 6 B 219 GLU SER LEU ILE ALA VAL GLN TYR ILE GLU GLU VAL TRP
SEQRES 7 B 219 ASN ASP ARG ASN PRO LEU LEU PRO SER ASP PRO TYR GLN
SEQRES 8 B 219 ARG ALA GLN THR ARG PHE TRP ALA ASP TYR VAL ASP LYS
SEQRES 9 B 219 LYS ILE TYR ASP LEU GLY ARG LYS ILE TRP THR SER LYS
SEQRES 10 B 219 GLY GLU GLU LYS GLU ALA ALA LYS LYS GLU PHE ILE GLU
SEQRES 11 B 219 ALA LEU LYS LEU LEU GLU GLU GLN LEU GLY ASP LYS THR
SEQRES 12 B 219 TYR PHE GLY GLY ASP ASN LEU GLY PHE VAL ASP ILE ALA
SEQRES 13 B 219 LEU VAL PRO PHE TYR THR TRP PHE LYS ALA TYR GLU THR
SEQRES 14 B 219 PHE GLY THR LEU ASN ILE GLU SER GLU CYS PRO LYS PHE
SEQRES 15 B 219 ILE ALA TRP ALA LYS ARG CYS LEU GLN LYS GLU SER VAL
SEQRES 16 B 219 ALA LYS SER LEU PRO ASP GLN GLN LYS VAL TYR GLU PHE
SEQRES 17 B 219 ILE MET ASP LEU ARG LYS LYS LEU GLY ILE GLU
HET GTB A1220 30
HET 4NM A1221 11
HET GOL A1222 6
HET GTB B1220 30
HET 4NM B1221 11
HET GOL B1222 6
HETNAM GTB S-(P-NITROBENZYL)GLUTATHIONE
HETNAM 4NM 4-NITROPHENYL METHANETHIOL
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GTB 2(C17 H22 N4 O8 S)
FORMUL 4 4NM 2(C7 H8 N O2 S 1+)
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 9 HOH *430(H2 O)
HELIX 1 1 SER A 13 LYS A 26 1 14
HELIX 2 2 SER A 41 ASN A 48 1 8
HELIX 3 3 GLU A 66 TRP A 78 1 13
HELIX 4 4 ASP A 88 SER A 116 1 29
HELIX 5 5 LYS A 117 GLY A 140 1 24
HELIX 6 6 GLY A 151 THR A 162 1 12
HELIX 7 7 TRP A 163 GLY A 171 1 9
HELIX 8 8 ASN A 174 CYS A 179 1 6
HELIX 9 9 CYS A 179 GLN A 191 1 13
HELIX 10 10 LYS A 192 LYS A 197 1 6
HELIX 11 11 ASP A 201 LEU A 212 1 12
HELIX 12 12 LEU A 212 GLY A 217 1 6
HELIX 13 13 SER B 13 LYS B 26 1 14
HELIX 14 14 SER B 41 ASN B 48 1 8
HELIX 15 15 GLU B 66 TRP B 78 1 13
HELIX 16 16 ASP B 88 SER B 116 1 29
HELIX 17 17 LYS B 117 GLY B 140 1 24
HELIX 18 18 GLY B 151 THR B 162 1 12
HELIX 19 19 TRP B 163 GLY B 171 1 9
HELIX 20 20 ASN B 174 CYS B 179 1 6
HELIX 21 21 CYS B 179 LYS B 192 1 14
HELIX 22 22 LYS B 192 LYS B 197 1 6
HELIX 23 23 ASP B 201 LEU B 212 1 12
HELIX 24 24 LEU B 212 GLY B 217 1 6
SHEET 1 AA 4 GLU A 31 GLU A 34 0
SHEET 2 AA 4 VAL A 5 ASP A 9 1 O VAL A 5 N GLU A 31
SHEET 3 AA 4 VAL A 56 HIS A 59 -1 O VAL A 56 N LEU A 8
SHEET 4 AA 4 LYS A 62 CYS A 65 -1 O LYS A 62 N HIS A 59
SHEET 1 BA 4 GLU B 31 GLU B 34 0
SHEET 2 BA 4 VAL B 5 ASP B 9 1 O VAL B 5 N GLU B 31
SHEET 3 BA 4 VAL B 56 HIS B 59 -1 O VAL B 56 N LEU B 8
SHEET 4 BA 4 LYS B 62 CYS B 65 -1 O LYS B 62 N HIS B 59
CISPEP 1 ILE A 54 PRO A 55 0 0.23
CISPEP 2 ILE A 218 GLU A 219 0 14.40
CISPEP 3 ILE B 54 PRO B 55 0 -1.25
CISPEP 4 ILE B 218 GLU B 219 0 -14.42
SITE 1 AC1 19 SER A 13 PHE A 15 LEU A 37 LYS A 40
SITE 2 AC1 19 LYS A 53 ILE A 54 PRO A 55 GLU A 66
SITE 3 AC1 19 SER A 67 TYR A 107 ARG A 111 LEU A 212
SITE 4 AC1 19 LYS A 215 LEU A 216 HOH A2080 HOH A2220
SITE 5 AC1 19 HOH A2221 HOH A2223 HOH A2224
SITE 1 AC2 20 SER B 13 PHE B 15 LEU B 37 LYS B 40
SITE 2 AC2 20 LYS B 53 ILE B 54 PRO B 55 GLU B 66
SITE 3 AC2 20 SER B 67 TYR B 107 LEU B 212 LYS B 215
SITE 4 AC2 20 LEU B 216 HOH B2081 HOH B2095 HOH B2142
SITE 5 AC2 20 HOH B2203 HOH B2204 HOH B2207 HOH B2208
SITE 1 AC3 7 TRP A 11 ARG A 20 TYR A 32 LYS A 197
SITE 2 AC3 7 SER A 198 LEU A 199 PRO A 200
SITE 1 AC4 9 TRP B 11 ARG B 20 TYR B 30 TYR B 32
SITE 2 AC4 9 LYS B 197 SER B 198 LEU B 199 PRO B 200
SITE 3 AC4 9 HOH B2009
SITE 1 AC5 6 ASP A 3 VAL A 77 TRP A 78 ASP A 80
SITE 2 AC5 6 HOH A2226 HOH A2227
SITE 1 AC6 6 VAL B 77 ASN B 79 ASP B 80 HOH B2107
SITE 2 AC6 6 HOH B2210 HOH B2211
CRYST1 91.375 91.375 111.830 90.00 90.00 90.00 P 41 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 0.010944 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010944 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008942 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
