HEADER TRANSFERASE 28-APR-10 3MQD
TITLE CRYSTAL STRUCTURE OF BETA-KETOACYL SYNTHASE FROM BRUCELLA MELITENSIS
TITLE 2 WITH FOL 0758, (1-METHYL-1H-INDAZOL-3-YL) METHANOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-KETOACYL SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.3.1.4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRUCELLA MELITENSIS BIOVAR ABORTUS;
SOURCE 3 ORGANISM_TAXID: 359391;
SOURCE 4 STRAIN: ABORTUS 2308;
SOURCE 5 GENE: FABB, BAB1_2173;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS SSGCID, ALS COLLABORATIVE CRYSTALLOGRAPHY, BETA-KETOACYL SYNTHASE,
KEYWDS 2 BRUCELLA MELITENSIS, FRAGMENTS OF LIFE, STRUCTURAL GENOMICS, SEATTLE
KEYWDS 3 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 20-JUN-12 3MQD 1 REMARK VERSN
REVDAT 1 09-JUN-10 3MQD 0
JRNL AUTH SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 2 (SSGCID),J.ABENDROTH,A.GARDBERG,B.SANKARAN,B.STAKER
JRNL TITL CRYSTAL STRUCTURE OF BETA-KETOACYL SYNTHASE FROM BRUCELLA
JRNL TITL 2 MELITENSIS WITH FOL 0758, (1-METHYL-1H-INDAZOL-3-YL)
JRNL TITL 3 METHANOL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 111141
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) : 0.113
REMARK 3 R VALUE (WORKING SET) : 0.112
REMARK 3 FREE R VALUE : 0.133
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5562
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) : 1.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7795
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.1700
REMARK 3 BIN FREE R VALUE SET COUNT : 405
REMARK 3 BIN FREE R VALUE : 0.2110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3012
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 454
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 7.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.19000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.032
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.031
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.017
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.821
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3246 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2188 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4422 ; 1.693 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5356 ; 1.315 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 453 ; 6.464 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;39.148 ;23.824
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 552 ;11.459 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;15.929 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 494 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3746 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 666 ; 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): 2082 ; 1.777 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 866 ; 2.414 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3352 ; 2.535 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1164 ; 3.772 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1045 ; 5.373 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3246 ; 1.735 ; 3.000
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 : 1.40
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
REMARK 4
REMARK 4 3MQD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-10.
REMARK 100 THE RCSB ID CODE IS RCSB058868.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9774
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM Q315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 111226
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 4181.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NATIVE STRUCTURE, 3LRF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MD PACT SCREEN, H12: 20% PEG 3350,
REMARK 280 100MM BISTRISPROPANE PH 8.5, 200MM NA-MALONATE; CRYSTAL SOAKED
REMARK 280 100MM MES PH 6.5, 250MM NACL, 30% PEG 3350, 10% GLYCEROL;
REMARK 280 BRABA.00113.A AT 22.9MG/ML, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 39.03500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.81000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.03500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.81000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: BIOMOLECULE: NULL
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 300
REMARK 300 REMARK: BIOLOGICAL UNIT IS A DIMER
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 39.73577
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 62.87556
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 ALA A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 MET A -12
REMARK 465 GLY A -11
REMARK 465 THR A -10
REMARK 465 LEU A -9
REMARK 465 GLU A -8
REMARK 465 ALA A -7
REMARK 465 GLN A -6
REMARK 465 THR A -5
REMARK 465 GLN A -4
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
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 ARG A 45 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 57 CG CD OE1 OE2
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 LYS A 376 CG CD CE NZ
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 A 469 O HOH A 473 1.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 418 O HOH A 761 4646 2.05
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 GLU A 91 CG GLU A 91 CD 0.103
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 27 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 PHE A 44 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 PHE A 44 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 277 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 107 -159.46 -85.99
REMARK 500 SER A 159 42.52 -163.12
REMARK 500 ALA A 160 -129.67 56.20
REMARK 500 ARG A 218 60.45 -155.96
REMARK 500 TYR A 220 -6.65 79.09
REMARK 500 ASP A 225 27.13 -142.72
REMARK 500 TYR A 265 -80.24 -136.31
REMARK 500 ALA A 297 106.20 -9.16
REMARK 500 SER A 299 33.64 80.45
REMARK 500 LEU A 335 -118.38 62.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 478 O
REMARK 620 2 HOH A 795 O 91.8
REMARK 620 3 LEU A 283 O 87.9 82.7
REMARK 620 4 HOH A 521 O 109.4 156.5 107.4
REMARK 620 5 VAL A 286 O 168.5 79.0 84.2 81.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 500 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 342 OE1
REMARK 620 2 ASN A 294 OD1 82.2
REMARK 620 3 SER A 388 OG 108.4 90.9
REMARK 620 4 ASN A 389 O 97.1 170.7 98.1
REMARK 620 5 ASN A 294 O 156.9 79.8 86.3 98.4
REMARK 620 6 PRO A 295 O 90.6 82.7 159.0 88.0 72.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3MQ A 499
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LRF RELATED DB: PDB
REMARK 900 NATIVE STRUCTURE
REMARK 900 RELATED ID: BRABA.00113.A RELATED DB: TARGETDB
DBREF 3MQD A 1 407 UNP Q2YQQ9 Q2YQQ9_BRUA2 1 407
SEQADV 3MQD MET A -20 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD ALA A -19 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD HIS A -18 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD HIS A -17 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD HIS A -16 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD HIS A -15 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD HIS A -14 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD HIS A -13 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD MET A -12 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD GLY A -11 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD THR A -10 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD LEU A -9 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD GLU A -8 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD ALA A -7 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD GLN A -6 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD THR A -5 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD GLN A -4 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD GLY A -3 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD PRO A -2 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD GLY A -1 UNP Q2YQQ9 EXPRESSION TAG
SEQADV 3MQD SER A 0 UNP Q2YQQ9 EXPRESSION TAG
SEQRES 1 A 428 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 428 ALA GLN THR GLN GLY PRO GLY SER MET ARG ARG VAL VAL
SEQRES 3 A 428 VAL THR GLY MET GLY ILE VAL SER SER ILE GLY SER ASN
SEQRES 4 A 428 THR GLU GLU VAL THR ALA SER LEU ARG GLU ALA LYS SER
SEQRES 5 A 428 GLY ILE SER ARG ALA GLU GLU TYR ALA GLU LEU GLY PHE
SEQRES 6 A 428 ARG CYS GLN VAL HIS GLY ALA PRO ASP ILE ASP ILE GLU
SEQRES 7 A 428 SER LEU VAL ASP ARG ARG ALA MET ARG PHE HIS GLY ARG
SEQRES 8 A 428 GLY THR ALA TRP ASN HIS ILE ALA MET ASP GLN ALA ILE
SEQRES 9 A 428 ALA ASP ALA GLY LEU THR GLU GLU GLU VAL SER ASN GLU
SEQRES 10 A 428 ARG THR GLY ILE ILE MET GLY SER GLY GLY PRO SER THR
SEQRES 11 A 428 ARG THR ILE VAL ASP SER ALA ASP ILE THR ARG GLU LYS
SEQRES 12 A 428 GLY PRO LYS ARG VAL GLY PRO PHE ALA VAL PRO LYS ALA
SEQRES 13 A 428 MET SER SER THR ALA SER ALA THR LEU ALA THR PHE PHE
SEQRES 14 A 428 LYS ILE LYS GLY ILE ASN TYR SER ILE SER SER ALA CYS
SEQRES 15 A 428 ALA THR SER ASN HIS CYS ILE GLY ASN ALA TYR GLU MET
SEQRES 16 A 428 ILE GLN TYR GLY LYS GLN ASP ARG MET PHE ALA GLY GLY
SEQRES 17 A 428 CYS GLU ASP LEU ASP TRP THR LEU SER VAL LEU PHE ASP
SEQRES 18 A 428 ALA MET GLY ALA MET SER SER LYS TYR ASN ASP THR PRO
SEQRES 19 A 428 SER THR ALA SER ARG ALA TYR ASP LYS ASN ARG ASP GLY
SEQRES 20 A 428 PHE VAL ILE ALA GLY GLY ALA GLY VAL LEU VAL LEU GLU
SEQRES 21 A 428 ASP LEU GLU THR ALA LEU ALA ARG GLY ALA LYS ILE TYR
SEQRES 22 A 428 GLY GLU ILE VAL GLY TYR GLY ALA THR SER ASP GLY TYR
SEQRES 23 A 428 ASP MET VAL ALA PRO SER GLY GLU GLY ALA ILE ARG CYS
SEQRES 24 A 428 MET LYS MET ALA LEU SER THR VAL THR SER LYS ILE ASP
SEQRES 25 A 428 TYR ILE ASN PRO HIS ALA THR SER THR PRO ALA GLY ASP
SEQRES 26 A 428 ALA PRO GLU ILE GLU ALA ILE ARG GLN ILE PHE GLY ALA
SEQRES 27 A 428 GLY ASP VAL CYS PRO PRO ILE ALA ALA THR LYS SER LEU
SEQRES 28 A 428 THR GLY HIS SER LEU GLY ALA THR GLY VAL GLN GLU ALA
SEQRES 29 A 428 ILE TYR SER LEU LEU MET MET GLN ASN ASN PHE ILE CYS
SEQRES 30 A 428 GLU SER ALA HIS ILE GLU GLU LEU ASP PRO ALA PHE ALA
SEQRES 31 A 428 ASP MET PRO ILE VAL ARG LYS ARG ILE ASP ASN VAL GLN
SEQRES 32 A 428 LEU ASN THR VAL LEU SER ASN SER PHE GLY PHE GLY GLY
SEQRES 33 A 428 THR ASN ALA THR LEU VAL PHE GLN ARG TYR GLN GLY
HET NA A 500 1
HET NA A 501 1
HET CL A 502 1
HET 3MQ A 499 24
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM 3MQ (5-THIOPHEN-2-YLISOXAZOL-3-YL)METHANOL
FORMUL 2 NA 2(NA 1+)
FORMUL 4 CL CL 1-
FORMUL 5 3MQ C8 H7 N O2 S
FORMUL 6 HOH *454(H2 O)
HELIX 1 1 ASN A 18 ALA A 29 1 12
HELIX 2 2 ALA A 36 LEU A 42 1 7
HELIX 3 3 ASP A 55 VAL A 60 1 6
HELIX 4 4 ARG A 62 ARG A 66 5 5
HELIX 5 5 GLY A 69 GLY A 87 1 19
HELIX 6 6 THR A 89 SER A 94 1 6
HELIX 7 7 SER A 108 GLY A 123 1 16
HELIX 8 8 PRO A 124 GLY A 128 5 5
HELIX 9 9 ALA A 131 MET A 136 1 6
HELIX 10 10 SER A 138 PHE A 148 1 11
HELIX 11 11 SER A 159 CYS A 161 5 3
HELIX 12 12 ALA A 162 TYR A 177 1 16
HELIX 13 13 ASP A 192 MET A 202 1 11
HELIX 14 14 THR A 212 ALA A 216 5 5
HELIX 15 15 LEU A 241 ARG A 247 1 7
HELIX 16 16 GLY A 272 SER A 284 1 13
HELIX 17 17 THR A 300 GLY A 316 1 17
HELIX 18 18 ALA A 317 CYS A 321 5 5
HELIX 19 19 THR A 327 GLY A 332 1 6
HELIX 20 20 SER A 334 GLY A 336 5 3
HELIX 21 21 ALA A 337 ASN A 353 1 17
HELIX 22 22 ASP A 365 ALA A 369 5 5
SHEET 1 A 9 ASN A 154 TYR A 155 0
SHEET 2 A 9 THR A 98 SER A 104 1 N ILE A 100 O TYR A 155
SHEET 3 A 9 ARG A 182 GLU A 189 1 O PHE A 184 N GLY A 99
SHEET 4 A 9 GLY A 232 ASP A 240 -1 O LEU A 238 N MET A 183
SHEET 5 A 9 VAL A 4 VAL A 12 -1 N VAL A 5 O GLU A 239
SHEET 6 A 9 GLY A 253 SER A 262 -1 O GLY A 253 N VAL A 6
SHEET 7 A 9 THR A 396 GLN A 403 -1 O GLN A 403 N GLU A 254
SHEET 8 A 9 THR A 385 GLY A 392 -1 N GLY A 392 O THR A 396
SHEET 9 A 9 TYR A 292 ASN A 294 1 N ASN A 294 O LEU A 387
SHEET 1 B 2 ILE A 33 ARG A 35 0
SHEET 2 B 2 VAL A 48 GLY A 50 -1 O HIS A 49 N SER A 34
SHEET 1 C 2 PHE A 354 ILE A 355 0
SHEET 2 C 2 ILE A 378 ASP A 379 -1 O ILE A 378 N ILE A 355
LINK NA NA A 501 O HOH A 478 1555 1555 2.29
LINK OE1 GLU A 342 NA NA A 500 1555 1555 2.33
LINK OD1 ASN A 294 NA NA A 500 1555 1555 2.35
LINK NA NA A 501 O HOH A 795 1555 1555 2.36
LINK O LEU A 283 NA NA A 501 1555 1555 2.49
LINK OG ASER A 388 NA NA A 500 1555 1555 2.54
LINK O ASN A 389 NA NA A 500 1555 1555 2.54
LINK NA NA A 501 O HOH A 521 1555 1555 2.57
LINK O ASN A 294 NA NA A 500 1555 1555 2.59
LINK O VAL A 286 NA NA A 501 1555 1555 2.64
LINK O PRO A 295 NA NA A 500 1555 1555 2.85
SITE 1 AC1 5 ASN A 294 PRO A 295 GLU A 342 SER A 388
SITE 2 AC1 5 ASN A 389
SITE 1 AC2 5 LEU A 283 VAL A 286 HOH A 478 HOH A 521
SITE 2 AC2 5 HOH A 795
SITE 1 AC3 3 MET A 267 HOH A 476 HOH A 864
SITE 1 AC4 12 GLY A 105 GLY A 106 PRO A 107 THR A 109
SITE 2 AC4 12 VAL A 132 ALA A 135 MET A 136 ALA A 160
SITE 3 AC4 12 CYS A 161 LEU A 195 PHE A 199 LEU A 335
CRYST1 78.070 83.620 73.640 90.00 121.37 90.00 C 1 2 1 4
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 0.012809 0.000000 0.007809 0.00000
SCALE2 0.000000 0.011959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015904 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
