HEADER LYASE 19-JUN-00 1F61
TITLE CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE LYASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 4.1.3.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET30B
KEYWDS ALPHA-BETA BARREL, SWAPPED HELICES, APO-ENZYME, OPEN CONFORMATION,
KEYWDS 2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, TB
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM, TBSGC, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.SHARMA,S.SHARMA,K.H.HOENER ZU BENTRUP,J.D.MCKINNEY,D.G.RUSSELL,
AUTHOR 2 W.R.JACOBS JR.,J.C.SACCHETTINI,TB STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (TBSGC)
REVDAT 5 07-FEB-24 1F61 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 1F61 1 VERSN
REVDAT 3 24-FEB-09 1F61 1 VERSN
REVDAT 2 01-FEB-05 1F61 1 JRNL AUTHOR KEYWDS REMARK
REVDAT 1 30-AUG-00 1F61 0
JRNL AUTH V.SHARMA,S.SHARMA,K.HOENER ZU BENTRUP,J.D.MCKINNEY,
JRNL AUTH 2 D.G.RUSSELL,W.R.JACOBS JR.,J.C.SACCHETTINI
JRNL TITL STRUCTURE OF ISOCITRATE LYASE, A PERSISTENCE FACTOR OF
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS.
JRNL REF NAT.STRUCT.BIOL. V. 7 663 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 10932251
JRNL DOI 10.1038/77964
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 665225.860
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 77576
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 SET) : 0.165
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8587
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12410
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1389
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6484
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 692
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.26000
REMARK 3 B22 (A**2) : 3.26000
REMARK 3 B33 (A**2) : -6.51000
REMARK 3 B12 (A**2) : 1.66000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.040
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.750 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.210 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.220 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.870 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 54.25
REMARK 3
REMARK 3 NCS MODEL : CONSTR
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011286.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-APR-99; 13-JUN-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0; 100.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 19-ID; 14-BM-D
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791; 0.9798
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 1; ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 97699
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.08
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, HEPES, PH 8.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 192.27000
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 96.13500
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 144.20250
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.06750
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 240.33750
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 192.27000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 96.13500
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 48.06750
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 144.20250
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 240.33750
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 29140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -190.0 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 350 BIOMT1 2 0.500000 -0.866025 0.000000 65.12250
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 112.79548
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 48.06750
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 A 977 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 978 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1049 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 976 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 979 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1013 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1077 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 0
REMARK 465 THR A 419
REMARK 465 GLY A 420
REMARK 465 SER A 421
REMARK 465 THR A 422
REMARK 465 GLU A 423
REMARK 465 GLU A 424
REMARK 465 GLY A 425
REMARK 465 GLN A 426
REMARK 465 PHE A 427
REMARK 465 HIS A 428
REMARK 465 MET B 0
REMARK 465 THR B 419
REMARK 465 GLY B 420
REMARK 465 SER B 421
REMARK 465 THR B 422
REMARK 465 GLU B 423
REMARK 465 GLU B 424
REMARK 465 GLY B 425
REMARK 465 GLN B 426
REMARK 465 PHE B 427
REMARK 465 HIS B 428
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 ALA A 276 O HOH A 533 2.16
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 1157 O HOH A 1157 10665 1.50
REMARK 500 O HOH A 1159 O HOH A 1159 10665 1.85
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 50 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 404 NE - CZ - NH2 ANGL. DEV. = -3.4 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 ASP A 98 10.83 -160.03
REMARK 500 ALA A 99 51.76 -156.26
REMARK 500 GLN A 109 39.88 -146.10
REMARK 500 GLU A 155 -132.00 53.46
REMARK 500 ASP A 183 38.96 -97.07
REMARK 500 GLN A 369 -124.15 42.96
REMARK 500 ASP B 98 11.07 -157.17
REMARK 500 ALA B 99 50.45 -155.69
REMARK 500 GLN B 109 35.20 -147.13
REMARK 500 GLU B 155 -130.25 46.49
REMARK 500 ASP B 183 40.23 -100.77
REMARK 500 HIS B 193 120.93 -37.70
REMARK 500 PRO B 222 47.10 -83.53
REMARK 500 GLN B 369 -126.48 46.54
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 451 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 108 OD2
REMARK 620 2 ASP A 108 OD1 50.4
REMARK 620 3 GLU A 155 OE1 136.2 85.8
REMARK 620 4 HOH A 575 O 137.2 165.4 85.4
REMARK 620 5 HOH A 690 O 80.6 98.4 110.0 95.6
REMARK 620 6 HOH A 699 O 91.0 82.8 82.2 84.5 167.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 452 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 108 OD2
REMARK 620 2 ASP B 108 OD1 50.9
REMARK 620 3 GLU B 155 OE1 143.3 92.3
REMARK 620 4 HOH B 595 O 82.7 96.3 105.2
REMARK 620 5 HOH B 635 O 90.7 89.5 87.9 165.3
REMARK 620 6 HOH B 705 O 129.5 174.1 86.9 89.5 84.6
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 MG A 451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 452
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV0467 RELATED DB: TARGETDB
DBREF 1F61 A 0 428 UNP P0A5H3 ACEA_MYCTU 1 428
DBREF 1F61 B 0 428 UNP P0A5H3 ACEA_MYCTU 1 428
SEQADV 1F61 ALA A 1 UNP P0A5H3 INSERTION
SEQADV 1F61 ALA B 1 UNP P0A5H3 INSERTION
SEQRES 1 A 429 MET ALA SER VAL VAL GLY THR PRO LYS SER ALA GLU GLN
SEQRES 2 A 429 ILE GLN GLN GLU TRP ASP THR ASN PRO ARG TRP LYS ASP
SEQRES 3 A 429 VAL THR ARG THR TYR SER ALA GLU ASP VAL VAL ALA LEU
SEQRES 4 A 429 GLN GLY SER VAL VAL GLU GLU HIS THR LEU ALA ARG ARG
SEQRES 5 A 429 GLY ALA GLU VAL LEU TRP GLU GLN LEU HIS ASP LEU GLU
SEQRES 6 A 429 TRP VAL ASN ALA LEU GLY ALA LEU THR GLY ASN MET ALA
SEQRES 7 A 429 VAL GLN GLN VAL ARG ALA GLY LEU LYS ALA ILE TYR LEU
SEQRES 8 A 429 SER GLY TRP GLN VAL ALA GLY ASP ALA ASN LEU SER GLY
SEQRES 9 A 429 HIS THR TYR PRO ASP GLN SER LEU TYR PRO ALA ASN SER
SEQRES 10 A 429 VAL PRO GLN VAL VAL ARG ARG ILE ASN ASN ALA LEU GLN
SEQRES 11 A 429 ARG ALA ASP GLN ILE ALA LYS ILE GLU GLY ASP THR SER
SEQRES 12 A 429 VAL GLU ASN TRP LEU ALA PRO ILE VAL ALA ASP GLY GLU
SEQRES 13 A 429 ALA GLY PHE GLY GLY ALA LEU ASN VAL TYR GLU LEU GLN
SEQRES 14 A 429 LYS ALA LEU ILE ALA ALA GLY VAL ALA GLY SER HIS TRP
SEQRES 15 A 429 GLU ASP GLN LEU ALA SER GLU LYS LYS CYS GLY HIS LEU
SEQRES 16 A 429 GLY GLY LYS VAL LEU ILE PRO THR GLN GLN HIS ILE ARG
SEQRES 17 A 429 THR LEU THR SER ALA ARG LEU ALA ALA ASP VAL ALA ASP
SEQRES 18 A 429 VAL PRO THR VAL VAL ILE ALA ARG THR ASP ALA GLU ALA
SEQRES 19 A 429 ALA THR LEU ILE THR SER ASP VAL ASP GLU ARG ASP GLN
SEQRES 20 A 429 PRO PHE ILE THR GLY GLU ARG THR ARG GLU GLY PHE TYR
SEQRES 21 A 429 ARG THR LYS ASN GLY ILE GLU PRO CYS ILE ALA ARG ALA
SEQRES 22 A 429 LYS ALA TYR ALA PRO PHE ALA ASP LEU ILE TRP MET GLU
SEQRES 23 A 429 THR GLY THR PRO ASP LEU GLU ALA ALA ARG GLN PHE SER
SEQRES 24 A 429 GLU ALA VAL LYS ALA GLU TYR PRO ASP GLN MET LEU ALA
SEQRES 25 A 429 TYR ASN CYS SER PRO SER PHE ASN TRP LYS LYS HIS LEU
SEQRES 26 A 429 ASP ASP ALA THR ILE ALA LYS PHE GLN LYS GLU LEU ALA
SEQRES 27 A 429 ALA MET GLY PHE LYS PHE GLN PHE ILE THR LEU ALA GLY
SEQRES 28 A 429 PHE HIS ALA LEU ASN TYR SER MET PHE ASP LEU ALA TYR
SEQRES 29 A 429 GLY TYR ALA GLN ASN GLN MET SER ALA TYR VAL GLU LEU
SEQRES 30 A 429 GLN GLU ARG GLU PHE ALA ALA GLU GLU ARG GLY TYR THR
SEQRES 31 A 429 ALA THR LYS HIS GLN ARG GLU VAL GLY ALA GLY TYR PHE
SEQRES 32 A 429 ASP ARG ILE ALA THR THR VAL ASP PRO ASN SER SER THR
SEQRES 33 A 429 THR ALA LEU THR GLY SER THR GLU GLU GLY GLN PHE HIS
SEQRES 1 B 429 MET ALA SER VAL VAL GLY THR PRO LYS SER ALA GLU GLN
SEQRES 2 B 429 ILE GLN GLN GLU TRP ASP THR ASN PRO ARG TRP LYS ASP
SEQRES 3 B 429 VAL THR ARG THR TYR SER ALA GLU ASP VAL VAL ALA LEU
SEQRES 4 B 429 GLN GLY SER VAL VAL GLU GLU HIS THR LEU ALA ARG ARG
SEQRES 5 B 429 GLY ALA GLU VAL LEU TRP GLU GLN LEU HIS ASP LEU GLU
SEQRES 6 B 429 TRP VAL ASN ALA LEU GLY ALA LEU THR GLY ASN MET ALA
SEQRES 7 B 429 VAL GLN GLN VAL ARG ALA GLY LEU LYS ALA ILE TYR LEU
SEQRES 8 B 429 SER GLY TRP GLN VAL ALA GLY ASP ALA ASN LEU SER GLY
SEQRES 9 B 429 HIS THR TYR PRO ASP GLN SER LEU TYR PRO ALA ASN SER
SEQRES 10 B 429 VAL PRO GLN VAL VAL ARG ARG ILE ASN ASN ALA LEU GLN
SEQRES 11 B 429 ARG ALA ASP GLN ILE ALA LYS ILE GLU GLY ASP THR SER
SEQRES 12 B 429 VAL GLU ASN TRP LEU ALA PRO ILE VAL ALA ASP GLY GLU
SEQRES 13 B 429 ALA GLY PHE GLY GLY ALA LEU ASN VAL TYR GLU LEU GLN
SEQRES 14 B 429 LYS ALA LEU ILE ALA ALA GLY VAL ALA GLY SER HIS TRP
SEQRES 15 B 429 GLU ASP GLN LEU ALA SER GLU LYS LYS CYS GLY HIS LEU
SEQRES 16 B 429 GLY GLY LYS VAL LEU ILE PRO THR GLN GLN HIS ILE ARG
SEQRES 17 B 429 THR LEU THR SER ALA ARG LEU ALA ALA ASP VAL ALA ASP
SEQRES 18 B 429 VAL PRO THR VAL VAL ILE ALA ARG THR ASP ALA GLU ALA
SEQRES 19 B 429 ALA THR LEU ILE THR SER ASP VAL ASP GLU ARG ASP GLN
SEQRES 20 B 429 PRO PHE ILE THR GLY GLU ARG THR ARG GLU GLY PHE TYR
SEQRES 21 B 429 ARG THR LYS ASN GLY ILE GLU PRO CYS ILE ALA ARG ALA
SEQRES 22 B 429 LYS ALA TYR ALA PRO PHE ALA ASP LEU ILE TRP MET GLU
SEQRES 23 B 429 THR GLY THR PRO ASP LEU GLU ALA ALA ARG GLN PHE SER
SEQRES 24 B 429 GLU ALA VAL LYS ALA GLU TYR PRO ASP GLN MET LEU ALA
SEQRES 25 B 429 TYR ASN CYS SER PRO SER PHE ASN TRP LYS LYS HIS LEU
SEQRES 26 B 429 ASP ASP ALA THR ILE ALA LYS PHE GLN LYS GLU LEU ALA
SEQRES 27 B 429 ALA MET GLY PHE LYS PHE GLN PHE ILE THR LEU ALA GLY
SEQRES 28 B 429 PHE HIS ALA LEU ASN TYR SER MET PHE ASP LEU ALA TYR
SEQRES 29 B 429 GLY TYR ALA GLN ASN GLN MET SER ALA TYR VAL GLU LEU
SEQRES 30 B 429 GLN GLU ARG GLU PHE ALA ALA GLU GLU ARG GLY TYR THR
SEQRES 31 B 429 ALA THR LYS HIS GLN ARG GLU VAL GLY ALA GLY TYR PHE
SEQRES 32 B 429 ASP ARG ILE ALA THR THR VAL ASP PRO ASN SER SER THR
SEQRES 33 B 429 THR ALA LEU THR GLY SER THR GLU GLU GLY GLN PHE HIS
HET MG A 451 1
HET MG B 452 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *692(H2 O)
HELIX 1 1 SER A 9 ASN A 20 1 12
HELIX 2 2 PRO A 21 LYS A 24 5 4
HELIX 3 3 SER A 31 LEU A 38 1 8
HELIX 4 4 HIS A 46 LEU A 63 1 18
HELIX 5 5 THR A 73 ALA A 83 1 11
HELIX 6 6 SER A 91 ALA A 99 1 9
HELIX 7 7 ASN A 115 GLY A 139 1 25
HELIX 8 8 GLY A 160 GLY A 175 1 16
HELIX 9 9 LEU A 185 LYS A 189 5 5
HELIX 10 10 PRO A 201 ALA A 219 1 19
HELIX 11 11 ASP A 245 PRO A 247 5 3
HELIX 12 12 GLY A 264 ALA A 276 1 13
HELIX 13 13 PRO A 277 ALA A 279 5 3
HELIX 14 14 ASP A 290 ALA A 303 1 14
HELIX 15 15 ASN A 319 LEU A 324 1 6
HELIX 16 16 ASP A 325 MET A 339 1 15
HELIX 17 17 LEU A 348 GLN A 369 1 22
HELIX 18 18 GLN A 369 GLU A 384 1 16
HELIX 19 19 GLU A 385 GLY A 387 5 3
HELIX 20 20 LYS A 392 VAL A 397 1 6
HELIX 21 21 GLY A 398 ASP A 410 1 13
HELIX 22 22 SER B 9 ASN B 20 1 12
HELIX 23 23 PRO B 21 LYS B 24 5 4
HELIX 24 24 SER B 31 GLN B 39 1 9
HELIX 25 25 HIS B 46 LEU B 63 1 18
HELIX 26 26 THR B 73 ALA B 83 1 11
HELIX 27 27 SER B 91 ALA B 99 1 9
HELIX 28 28 ASN B 115 GLY B 139 1 25
HELIX 29 29 GLY B 160 GLY B 175 1 16
HELIX 30 30 LEU B 185 LYS B 189 5 5
HELIX 31 31 PRO B 201 ALA B 219 1 19
HELIX 32 32 ASP B 245 PRO B 247 5 3
HELIX 33 33 GLY B 264 ALA B 276 1 13
HELIX 34 34 PRO B 277 ALA B 279 5 3
HELIX 35 35 ASP B 290 TYR B 305 1 16
HELIX 36 36 ASN B 319 LEU B 324 1 6
HELIX 37 37 ASP B 325 MET B 339 1 15
HELIX 38 38 LEU B 348 GLN B 369 1 22
HELIX 39 39 GLN B 369 GLU B 384 1 16
HELIX 40 40 GLU B 385 GLY B 387 5 3
HELIX 41 41 LYS B 392 VAL B 397 1 6
HELIX 42 42 GLY B 398 ASP B 410 1 13
SHEET 1 A 8 VAL A 66 LEU A 69 0
SHEET 2 A 8 PHE A 341 ILE A 346 1 O LYS A 342 N VAL A 66
SHEET 3 A 8 MET A 309 ASN A 313 1 O LEU A 310 N PHE A 343
SHEET 4 A 8 LEU A 281 MET A 284 1 O ILE A 282 N ALA A 311
SHEET 5 A 8 VAL A 224 THR A 229 1 O VAL A 225 N LEU A 281
SHEET 6 A 8 GLY A 178 GLU A 182 1 O SER A 179 N ILE A 226
SHEET 7 A 8 ILE A 150 ASP A 153 1 O ILE A 150 N GLY A 178
SHEET 8 A 8 ILE A 88 LEU A 90 1 O ILE A 88 N VAL A 151
SHEET 1 B 4 VAL A 198 LEU A 199 0
SHEET 2 B 4 LEU A 236 ILE A 237 1 O LEU A 236 N LEU A 199
SHEET 3 B 4 TYR A 259 THR A 261 -1 N TYR A 259 O ILE A 237
SHEET 4 B 4 ILE A 249 ARG A 253 -1 N THR A 250 O ARG A 260
SHEET 1 C 8 VAL B 66 LEU B 69 0
SHEET 2 C 8 PHE B 341 ILE B 346 1 O LYS B 342 N VAL B 66
SHEET 3 C 8 MET B 309 ASN B 313 1 O LEU B 310 N PHE B 343
SHEET 4 C 8 LEU B 281 MET B 284 1 O ILE B 282 N ALA B 311
SHEET 5 C 8 VAL B 224 THR B 229 1 O VAL B 225 N LEU B 281
SHEET 6 C 8 GLY B 178 GLU B 182 1 O SER B 179 N ILE B 226
SHEET 7 C 8 ILE B 150 ASP B 153 1 O ILE B 150 N GLY B 178
SHEET 8 C 8 ILE B 88 LEU B 90 1 O ILE B 88 N VAL B 151
SHEET 1 D 4 VAL B 198 LEU B 199 0
SHEET 2 D 4 LEU B 236 ILE B 237 1 O LEU B 236 N LEU B 199
SHEET 3 D 4 TYR B 259 THR B 261 -1 N TYR B 259 O ILE B 237
SHEET 4 D 4 ILE B 249 ARG B 253 -1 N THR B 250 O ARG B 260
LINK OD2 ASP A 108 MG MG A 451 1555 1555 2.73
LINK OD1 ASP A 108 MG MG A 451 1555 1555 2.47
LINK OE1 GLU A 155 MG MG A 451 1555 1555 2.52
LINK MG MG A 451 O HOH A 575 1555 1555 2.53
LINK MG MG A 451 O HOH A 690 1555 1555 2.25
LINK MG MG A 451 O HOH A 699 1555 1555 2.29
LINK OD2 ASP B 108 MG MG B 452 1555 1555 2.76
LINK OD1 ASP B 108 MG MG B 452 1555 1555 2.30
LINK OE1 GLU B 155 MG MG B 452 1555 1555 2.34
LINK MG MG B 452 O HOH B 595 1555 1555 2.35
LINK MG MG B 452 O HOH B 635 1555 1555 2.21
LINK MG MG B 452 O HOH B 705 1555 1555 2.52
SITE 1 AC1 5 ASP A 108 GLU A 155 HOH A 575 HOH A 690
SITE 2 AC1 5 HOH A 699
SITE 1 AC2 5 ASP B 108 GLU B 155 HOH B 595 HOH B 635
SITE 2 AC2 5 HOH B 705
CRYST1 130.245 130.245 288.405 90.00 90.00 120.00 P 65 2 2 24
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 0.007678 0.004433 0.000000 0.00000
SCALE2 0.000000 0.008866 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003467 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
