HEADER OXIDOREDUCTASE 07-MAY-10 3MXU
TITLE CRYSTAL STRUCTURE OF GLYCINE CLEAVAGE SYSTEM PROTEIN H FROM BARTONELLA
TITLE 2 HENSELAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCINE CLEAVAGE SYSTEM H PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BARTONELLA HENSELAE;
SOURCE 3 ORGANISM_COMMON: ROCHALIMAEA HENSELAE;
SOURCE 4 ORGANISM_TAXID: 38323;
SOURCE 5 GENE: GCVH, BH12830;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, SSGCID,
KEYWDS 2 CAT-SCRATCH DISEASE, BACTEREMIA, LYMPHADENOPATHY, ENDOCARDITIS, HIV
KEYWDS 3 CO-INFECTION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 06-SEP-23 3MXU 1 REMARK SEQADV
REVDAT 1 26-MAY-10 3MXU 0
JRNL AUTH T.E.EDWARDS,A.S.GARDBERG,
JRNL AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 3 (SSGCID)
JRNL TITL CRYSTAL STRUCTURE OF GLYCINE CLEAVAGE SYSTEM PROTEIN H FROM
JRNL TITL 2 BARTONELLA HENSELAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 22981
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1179
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1574
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1000
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.16000
REMARK 3 B12 (A**2) : 0.05000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.770
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1087 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1495 ; 1.349 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 149 ; 6.029 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 47 ;36.146 ;27.447
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 177 ;11.845 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 1 ;27.373 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 174 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 823 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 687 ; 0.781 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1107 ; 1.498 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 400 ; 2.312 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 380 ; 3.791 ; 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -12 A 121
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0801 15.7998 46.6881
REMARK 3 T TENSOR
REMARK 3 T11: 0.0806 T22: 0.0172
REMARK 3 T33: 0.0467 T12: 0.0139
REMARK 3 T13: -0.0142 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 0.5135 L22: 0.7730
REMARK 3 L33: 0.7767 L12: -0.0890
REMARK 3 L13: -0.2814 L23: 0.2609
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: 0.0105 S13: 0.0144
REMARK 3 S21: -0.0900 S22: -0.0495 S23: 0.0278
REMARK 3 S31: -0.1188 S32: -0.0318 S33: 0.0487
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 3MXU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000059129.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23036
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 35.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.9500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.55700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: 3HGB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 4.0, 0.8 M
REMARK 280 AMMONIUM CITRATE, 25% ETHYLENE GLYCOL AS CRYO-PROTECTANT, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 49.45500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 28.55286
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 43.84667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 49.45500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 28.55286
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 43.84667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 49.45500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 28.55286
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 43.84667
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 49.45500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 28.55286
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 43.84667
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 49.45500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 28.55286
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 43.84667
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 49.45500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 28.55286
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 43.84667
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 57.10572
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 87.69333
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 57.10572
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 87.69333
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 57.10572
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 87.69333
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 57.10572
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 87.69333
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 57.10572
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 87.69333
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 57.10572
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 87.69333
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 S SO4 A 124 LIES ON A SPECIAL POSITION.
REMARK 375 O4 SO4 A 124 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 149 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 161 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 167 LIES ON A SPECIAL POSITION.
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 GLY A 122
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 MET A -12 CG SD CE
REMARK 470 LEU A -9 CG CD1 CD2
REMARK 470 GLN A -6 CG CD OE1 NE2
REMARK 470 LYS A 60 CG CD CE NZ
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 GLN A 103 CG CD OE1 NE2
REMARK 470 GLU A 105 CG CD OE1 OE2
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 THR A 7 -165.85 -100.95
REMARK 500 LYS A 90 53.11 -142.75
REMARK 500 LYS A 90 49.13 -140.68
REMARK 500 THR A 93 -96.49 -134.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 123
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 124
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 126
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HGB RELATED DB: PDB
REMARK 900 SAME PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS
REMARK 900 RELATED ID: BAHEA.01633.A RELATED DB: TARGETDB
DBREF 3MXU A 1 122 UNP Q6G2F0 GCSH_BARHE 1 122
SEQADV 3MXU MET A -20 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU ALA A -19 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU HIS A -18 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU HIS A -17 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU HIS A -16 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU HIS A -15 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU HIS A -14 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU HIS A -13 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU MET A -12 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU GLY A -11 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU THR A -10 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU LEU A -9 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU GLU A -8 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU ALA A -7 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU GLN A -6 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU THR A -5 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU GLN A -4 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU GLY A -3 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU PRO A -2 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU GLY A -1 UNP Q6G2F0 EXPRESSION TAG
SEQADV 3MXU SER A 0 UNP Q6G2F0 EXPRESSION TAG
SEQRES 1 A 143 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 143 ALA GLN THR GLN GLY PRO GLY SER MET SER LYS THR TYR
SEQRES 3 A 143 PHE THR GLN ASP HIS GLU TRP LEU SER VAL GLU GLY GLN
SEQRES 4 A 143 VAL VAL THR VAL GLY ILE THR ASP TYR ALA GLN GLU GLN
SEQRES 5 A 143 LEU GLY ASP LEU VAL PHE ILE ASP LEU PRO GLN ASN GLY
SEQRES 6 A 143 THR LYS LEU SER LYS GLY ASP ALA ALA ALA VAL VAL GLU
SEQRES 7 A 143 SER VAL LYS ALA ALA SER ASP VAL TYR ALA PRO LEU ASP
SEQRES 8 A 143 GLY GLU VAL VAL GLU ILE ASN ALA ALA LEU ALA GLU SER
SEQRES 9 A 143 PRO GLU LEU VAL ASN GLN LYS ALA GLU THR GLU GLY TRP
SEQRES 10 A 143 LEU TRP LYS MET THR VAL GLN ASP GLU THR GLN LEU GLU
SEQRES 11 A 143 ARG LEU LEU ASP GLU ALA ALA TYR LYS GLU LEU ILE GLY
HET CIT A 123 13
HET SO4 A 124 5
HET SO4 A 125 5
HET EDO A 126 4
HETNAM CIT CITRIC ACID
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CIT C6 H8 O7
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 EDO C2 H6 O2
FORMUL 6 HOH *156(H2 O)
HELIX 1 1 MET A -12 GLN A -4 1 9
HELIX 2 2 THR A 25 GLY A 33 1 9
HELIX 3 3 ALA A 78 GLU A 82 5 5
HELIX 4 4 SER A 83 PRO A 84 5 2
HELIX 5 5 GLU A 85 LYS A 90 1 6
HELIX 6 6 GLU A 105 GLU A 114 1 10
SHEET 1 A 7 LYS A 46 LEU A 47 0
SHEET 2 A 7 GLY A 71 ILE A 76 -1 O GLY A 71 N LEU A 47
SHEET 3 A 7 TRP A 98 THR A 101 -1 O LYS A 99 N VAL A 74
SHEET 4 A 7 VAL A 19 ILE A 24 -1 N VAL A 20 O MET A 100
SHEET 5 A 7 GLU A 11 GLU A 16 -1 N SER A 14 O THR A 21
SHEET 6 A 7 LYS A 3 PHE A 6 -1 N TYR A 5 O LEU A 13
SHEET 7 A 7 LYS A 118 GLU A 119 -1 O LYS A 118 N PHE A 6
SHEET 1 B 3 LEU A 35 ASP A 39 0
SHEET 2 B 3 ALA A 52 SER A 58 -1 O GLU A 57 N VAL A 36
SHEET 3 B 3 ALA A 62 TYR A 66 -1 O VAL A 65 N ALA A 53
SITE 1 AC1 12 HIS A 10 THR A 25 ASP A 26 TYR A 27
SITE 2 AC1 12 LYS A 49 GLU A 92 ARG A 110 LEU A 111
SITE 3 AC1 12 GLU A 114 LEU A 120 HOH A 159 HOH A 180
SITE 1 AC2 3 GLN A 8 LYS A 118 HOH A 161
SITE 1 AC3 5 LYS A 49 GLN A 107 ARG A 110 HOH A 157
SITE 2 AC3 5 HOH A 162
SITE 1 AC4 5 ASP A 39 LEU A 40 ALA A 53 HOH A 144
SITE 2 AC4 5 HOH A 241
CRYST1 98.910 98.910 131.540 90.00 90.00 120.00 H 3 2 18
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 0.010110 0.005837 0.000000 0.00000
SCALE2 0.000000 0.011674 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007602 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
