HEADER UNKNOWN FUNCTION 03-OCT-12 4HEC
TITLE CRYSTAL STRUCTURE OF A PUTATIVE UNCHARACTERIZED PROTEIN FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: MT2234.1, RV2179C;
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, MYCOBACTERIUM TUBERCULOSIS, STRUCTURAL GENOMICS, SEATTLE
KEYWDS 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 5 28-FEB-24 4HEC 1 REMARK SEQADV LINK
REVDAT 4 20-SEP-17 4HEC 1 REMARK
REVDAT 3 12-FEB-14 4HEC 1 JRNL
REVDAT 2 18-DEC-13 4HEC 1 JRNL
REVDAT 1 17-OCT-12 4HEC 0
JRNL AUTH J.ABENDROTH,A.OLLODART,E.S.ANDREWS,P.J.MYLER,B.L.STAKER,
JRNL AUTH 2 T.E.EDWARDS,V.L.ARCUS,C.GRUNDNER
JRNL TITL MYCOBACTERIUM TUBERCULOSIS RV2179C PROTEIN ESTABLISHES A NEW
JRNL TITL 2 EXORIBONUCLEASE FAMILY WITH BROAD PHYLOGENETIC DISTRIBUTION.
JRNL REF J.BIOL.CHEM. V. 289 2139 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24311791
JRNL DOI 10.1074/JBC.M113.525683
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 38.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 31227
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1645
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) : 2217
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 109
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.68000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.67000
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): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.126
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.611
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2692 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2475 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3686 ; 1.652 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5683 ; 0.860 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 329 ; 5.600 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 135 ;29.271 ;22.222
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 421 ;11.828 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;22.951 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 396 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3035 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 647 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
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 : A 0 A 159
REMARK 3 RESIDUE RANGE : A 301 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3990 17.0880 81.3230
REMARK 3 T TENSOR
REMARK 3 T11: 0.0668 T22: 0.0145
REMARK 3 T33: 0.0348 T12: 0.0045
REMARK 3 T13: -0.0116 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 1.1551 L22: 1.2706
REMARK 3 L33: 1.4490 L12: 0.1391
REMARK 3 L13: -0.3673 L23: -0.4798
REMARK 3 S TENSOR
REMARK 3 S11: 0.0486 S12: 0.0147 S13: 0.0073
REMARK 3 S21: -0.1098 S22: -0.0411 S23: 0.0195
REMARK 3 S31: -0.0359 S32: -0.1085 S33: -0.0075
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 0 B 162
REMARK 3 RESIDUE RANGE : B 301 B 301
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3850 2.0010 99.0070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0769 T22: 0.0501
REMARK 3 T33: 0.0418 T12: -0.0278
REMARK 3 T13: 0.0066 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.9015 L22: 1.2827
REMARK 3 L33: 1.3609 L12: -0.1701
REMARK 3 L13: -0.1892 L23: -0.1476
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: -0.1742 S13: -0.0551
REMARK 3 S21: 0.1035 S22: -0.0455 S23: 0.0212
REMARK 3 S31: 0.0455 S32: -0.0525 S33: 0.0296
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 RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4HEC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : RIGAKU VARIMAX
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32926
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : 0.03600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.2900
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 (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: DE NOVO PHASING WITH IODIDE IONS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EMBIO JCSG+ B4: 10% PEG 8000, 8%
REMARK 280 ETHYLENE GLYCOL, 100MM HEPES PH 7.5; MYTUD.18400.A.A1.PS01434 AT
REMARK 280 12.8MG/ML + 2.5MM AMPPNP AND MGCL2, CRYO: 20% EG; THE STRUCTURE
REMARK 280 WAS SOLVED VIA IODIDE SAD: A CRYSTAL WAS SOAKED IN RESERVOIR
REMARK 280 PLUS 20% ETHYLENE GLYCOL AND 750MM NAI, ANOMALOUS AMPLITUDES ARE
REMARK 280 DEPOSITED, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.39000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.02000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.36000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.02000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.39000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.36000
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 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: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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 ARG A 136
REMARK 465 PRO A 137
REMARK 465 ARG A 138
REMARK 465 ASP A 139
REMARK 465 VAL A 140
REMARK 465 THR A 160
REMARK 465 ASP A 161
REMARK 465 ASP A 162
REMARK 465 ALA A 163
REMARK 465 GLY A 164
REMARK 465 ARG A 165
REMARK 465 GLY A 166
REMARK 465 ALA A 167
REMARK 465 ALA A 168
REMARK 465 ARG A 169
REMARK 465 MET B -20
REMARK 465 ALA B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 MET B -12
REMARK 465 GLY B -11
REMARK 465 THR B -10
REMARK 465 LEU B -9
REMARK 465 GLU B -8
REMARK 465 ALA B -7
REMARK 465 GLN B -6
REMARK 465 THR B -5
REMARK 465 GLN B -4
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 ALA B 163
REMARK 465 GLY B 164
REMARK 465 ARG B 165
REMARK 465 GLY B 166
REMARK 465 ALA B 167
REMARK 465 ALA B 168
REMARK 465 ARG B 169
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 GLU A 42 CG CD OE1 OE2
REMARK 470 ARG A 49 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 62 CG CD OE1 NE2
REMARK 470 HIS A 141 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 62 CG CD OE1 NE2
REMARK 470 ARG B 132 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 136 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 138 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 139 CG OD1 OD2
REMARK 470 VAL B 140 CG1 CG2
REMARK 470 ASP B 162 CG OD1 OD2
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 79 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 71 NE - CZ - NH1 ANGL. DEV. = 3.1 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 HIS A 15 -52.14 -129.31
REMARK 500 ALA B 94 -103.89 31.97
REMARK 500 ASP B 139 66.54 -106.21
REMARK 500 THR B 160 159.68 -36.25
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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 7 OD1
REMARK 620 2 HOH A 422 O 81.2
REMARK 620 3 HOH A 437 O 102.2 103.3
REMARK 620 4 HOH A 494 O 84.9 165.4 84.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 7 OD1
REMARK 620 2 THR B 8 O 86.0
REMARK 620 3 ASP B 96 OD1 86.4 86.3
REMARK 620 4 HOH B 427 O 146.8 97.3 126.7
REMARK 620 5 HOH B 432 O 82.5 167.6 88.4 94.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-MYTUD.18400.A RELATED DB: TARGETTRACK
DBREF 4HEC A 1 169 UNP O53513 O53513_MYCTU 1 168
DBREF 4HEC B 1 169 UNP O53513 O53513_MYCTU 1 168
SEQADV 4HEC MET A -20 UNP O53513 EXPRESSION TAG
SEQADV 4HEC ALA A -19 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS A -18 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS A -17 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS A -16 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS A -15 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS A -14 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS A -13 UNP O53513 EXPRESSION TAG
SEQADV 4HEC MET A -12 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLY A -11 UNP O53513 EXPRESSION TAG
SEQADV 4HEC THR A -10 UNP O53513 EXPRESSION TAG
SEQADV 4HEC LEU A -9 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLU A -8 UNP O53513 EXPRESSION TAG
SEQADV 4HEC ALA A -7 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLN A -6 UNP O53513 EXPRESSION TAG
SEQADV 4HEC THR A -5 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLN A -4 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLY A -3 UNP O53513 EXPRESSION TAG
SEQADV 4HEC PRO A -2 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLY A -1 UNP O53513 EXPRESSION TAG
SEQADV 4HEC SER A 0 UNP O53513 EXPRESSION TAG
SEQADV 4HEC VAL A 2 UNP O53513 EXPRESSION TAG
SEQADV 4HEC MET B -20 UNP O53513 EXPRESSION TAG
SEQADV 4HEC ALA B -19 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS B -18 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS B -17 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS B -16 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS B -15 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS B -14 UNP O53513 EXPRESSION TAG
SEQADV 4HEC HIS B -13 UNP O53513 EXPRESSION TAG
SEQADV 4HEC MET B -12 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLY B -11 UNP O53513 EXPRESSION TAG
SEQADV 4HEC THR B -10 UNP O53513 EXPRESSION TAG
SEQADV 4HEC LEU B -9 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLU B -8 UNP O53513 EXPRESSION TAG
SEQADV 4HEC ALA B -7 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLN B -6 UNP O53513 EXPRESSION TAG
SEQADV 4HEC THR B -5 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLN B -4 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLY B -3 UNP O53513 EXPRESSION TAG
SEQADV 4HEC PRO B -2 UNP O53513 EXPRESSION TAG
SEQADV 4HEC GLY B -1 UNP O53513 EXPRESSION TAG
SEQADV 4HEC SER B 0 UNP O53513 EXPRESSION TAG
SEQADV 4HEC VAL B 2 UNP O53513 EXPRESSION TAG
SEQRES 1 A 190 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 190 ALA GLN THR GLN GLY PRO GLY SER MET VAL ARG TYR PHE
SEQRES 3 A 190 TYR ASP THR GLU PHE ILE GLU ASP GLY HIS THR ILE GLU
SEQRES 4 A 190 LEU ILE SER ILE GLY VAL VAL ALA GLU ASP GLY ARG GLU
SEQRES 5 A 190 TYR TYR ALA VAL SER THR GLU PHE ASP PRO GLU ARG ALA
SEQRES 6 A 190 GLY SER TRP VAL ARG THR HIS VAL LEU PRO LYS LEU PRO
SEQRES 7 A 190 PRO PRO ALA SER GLN LEU TRP ARG SER ARG GLN GLN ILE
SEQRES 8 A 190 ARG LEU ASP LEU GLU GLU PHE LEU ARG ILE ASP GLY THR
SEQRES 9 A 190 ASP SER ILE GLU LEU TRP ALA TRP VAL GLY ALA TYR ASP
SEQRES 10 A 190 HIS VAL ALA LEU CYS GLN LEU TRP GLY PRO MET THR ALA
SEQRES 11 A 190 LEU PRO PRO THR VAL PRO ARG PHE THR ARG GLU LEU ARG
SEQRES 12 A 190 GLN LEU TRP GLU ASP ARG GLY CYS PRO ARG MET PRO PRO
SEQRES 13 A 190 ARG PRO ARG ASP VAL HIS ASP ALA LEU VAL ASP ALA ARG
SEQRES 14 A 190 ASP GLN LEU ARG ARG PHE ARG LEU ILE THR SER THR ASP
SEQRES 15 A 190 ASP ALA GLY ARG GLY ALA ALA ARG
SEQRES 1 B 190 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 B 190 ALA GLN THR GLN GLY PRO GLY SER MET VAL ARG TYR PHE
SEQRES 3 B 190 TYR ASP THR GLU PHE ILE GLU ASP GLY HIS THR ILE GLU
SEQRES 4 B 190 LEU ILE SER ILE GLY VAL VAL ALA GLU ASP GLY ARG GLU
SEQRES 5 B 190 TYR TYR ALA VAL SER THR GLU PHE ASP PRO GLU ARG ALA
SEQRES 6 B 190 GLY SER TRP VAL ARG THR HIS VAL LEU PRO LYS LEU PRO
SEQRES 7 B 190 PRO PRO ALA SER GLN LEU TRP ARG SER ARG GLN GLN ILE
SEQRES 8 B 190 ARG LEU ASP LEU GLU GLU PHE LEU ARG ILE ASP GLY THR
SEQRES 9 B 190 ASP SER ILE GLU LEU TRP ALA TRP VAL GLY ALA TYR ASP
SEQRES 10 B 190 HIS VAL ALA LEU CYS GLN LEU TRP GLY PRO MET THR ALA
SEQRES 11 B 190 LEU PRO PRO THR VAL PRO ARG PHE THR ARG GLU LEU ARG
SEQRES 12 B 190 GLN LEU TRP GLU ASP ARG GLY CYS PRO ARG MET PRO PRO
SEQRES 13 B 190 ARG PRO ARG ASP VAL HIS ASP ALA LEU VAL ASP ALA ARG
SEQRES 14 B 190 ASP GLN LEU ARG ARG PHE ARG LEU ILE THR SER THR ASP
SEQRES 15 B 190 ASP ALA GLY ARG GLY ALA ALA ARG
HET MG A 301 1
HET MG B 301 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *220(H2 O)
HELIX 1 1 ASP A 40 ALA A 44 5 5
HELIX 2 2 GLY A 45 VAL A 52 1 8
HELIX 3 3 LEU A 53 LEU A 56 5 4
HELIX 4 4 SER A 66 LEU A 78 1 13
HELIX 5 5 GLY A 93 GLN A 102 1 10
HELIX 6 6 PRO A 106 LEU A 110 5 5
HELIX 7 7 LEU A 121 ARG A 128 1 8
HELIX 8 8 ASP A 142 SER A 159 1 18
HELIX 9 9 ASP B 40 ALA B 44 5 5
HELIX 10 10 GLY B 45 VAL B 52 1 8
HELIX 11 11 LEU B 53 LEU B 56 5 4
HELIX 12 12 SER B 66 LEU B 78 1 13
HELIX 13 13 ALA B 94 GLN B 102 1 9
HELIX 14 14 LEU B 103 GLY B 105 5 3
HELIX 15 15 PRO B 106 LEU B 110 5 5
HELIX 16 16 LEU B 121 ARG B 128 1 8
HELIX 17 17 ASP B 142 SER B 159 1 18
SHEET 1 A 6 TRP A 64 ARG A 65 0
SHEET 2 A 6 GLU A 31 SER A 36 1 N VAL A 35 O ARG A 65
SHEET 3 A 6 ILE A 17 ALA A 26 -1 N ILE A 20 O SER A 36
SHEET 4 A 6 MET A 1 GLU A 12 -1 N ILE A 11 O GLU A 18
SHEET 5 A 6 SER A 85 ALA A 90 1 O GLU A 87 N TYR A 4
SHEET 6 A 6 ARG A 119 GLU A 120 1 O ARG A 119 N LEU A 88
SHEET 1 B 6 TRP B 64 ARG B 65 0
SHEET 2 B 6 GLU B 31 SER B 36 1 N VAL B 35 O ARG B 65
SHEET 3 B 6 ILE B 17 ALA B 26 -1 N VAL B 24 O TYR B 32
SHEET 4 B 6 MET B 1 GLU B 12 -1 N ILE B 11 O GLU B 18
SHEET 5 B 6 SER B 85 ALA B 90 1 O TRP B 89 N TYR B 4
SHEET 6 B 6 ARG B 119 GLU B 120 1 O ARG B 119 N LEU B 88
LINK OD1 ASP A 7 MG MG A 301 1555 1555 2.19
LINK MG MG A 301 O HOH A 422 1555 1555 2.03
LINK MG MG A 301 O HOH A 437 1555 1555 2.12
LINK MG MG A 301 O HOH A 494 1555 1555 2.29
LINK OD1 ASP B 7 MG MG B 301 1555 1555 2.60
LINK O THR B 8 MG MG B 301 1555 1555 2.29
LINK OD1 ASP B 96 MG MG B 301 1555 1555 2.49
LINK MG MG B 301 O HOH B 427 1555 1555 2.34
LINK MG MG B 301 O HOH B 432 1555 1555 2.33
SITE 1 AC1 5 ASP A 7 ASP A 96 HOH A 422 HOH A 437
SITE 2 AC1 5 HOH A 494
SITE 1 AC2 5 ASP B 7 THR B 8 ASP B 96 HOH B 427
SITE 2 AC2 5 HOH B 432
CRYST1 42.780 76.720 106.040 90.00 90.00 90.00 P 21 21 21 8
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 0.023375 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013034 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009430 0.00000
(ATOM LINES ARE NOT SHOWN.)
END