HEADER LIGASE 02-AUG-05 2AJH
TITLE CRYSTAL STRUCTURE OF THE EDITING DOMAIN OF E. COLI LEUCYL-TRNA
TITLE 2 SYNTHETASE COMPLEXES WITH METHIONINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUCYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 228-413;
COMPND 5 SYNONYM: LEUCINE--TRNA LIGASE, LEURS;
COMPND 6 EC: 6.1.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-3E-HIS
KEYWDS EDITING DOMAIN, LEUCYL-TRNA SYNTHETASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LIU,J.LIAO,B.ZHU,E.D.WANG,J.DING
REVDAT 5 13-MAR-24 2AJH 1 REMARK SEQADV
REVDAT 4 11-OCT-17 2AJH 1 REMARK
REVDAT 3 24-FEB-09 2AJH 1 VERSN
REVDAT 2 21-FEB-06 2AJH 1 JRNL AUTHOR
REVDAT 1 24-JAN-06 2AJH 0
JRNL AUTH Y.LIU,J.LIAO,B.ZHU,E.D.WANG,J.DING
JRNL TITL CRYSTAL STRUCTURES OF THE EDITING DOMAIN OF ESCHERICHIA COLI
JRNL TITL 2 LEUCYL-TRNA SYNTHETASE AND ITS COMPLEXES WITH MET AND ILE
JRNL TITL 3 REVEAL A LOCK-AND-KEY MECHANISM FOR AMINO ACID
JRNL TITL 4 DISCRIMINATION
JRNL REF BIOCHEM.J. V. 394 399 2006
JRNL REFN ISSN 0264-6021
JRNL PMID 16277600
JRNL DOI 10.1042/BJ20051249
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 18755
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) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1007
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1360
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE SET COUNT : 72
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2693
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 78
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.33000
REMARK 3 B22 (A**2) : 2.33000
REMARK 3 B33 (A**2) : -3.50000
REMARK 3 B12 (A**2) : 1.17000
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): 0.358
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.269
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2765 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3756 ; 1.474 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 358 ; 6.149 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 423 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2141 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1290 ; 0.230 ; 0.200
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): 121 ; 0.143 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 24 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.141 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1798 ; 0.815 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2852 ; 1.583 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 967 ; 2.408 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 904 ; 3.922 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 2AJH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000033966.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 123
REMARK 200 PH : 9
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19784
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.45200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: (NH4)2SO4, PH 9, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -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 -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 67.46550
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 67.46550
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 67.46550
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 0.00000
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 0.00000
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 67.46550
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 67.46550
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 67.46550
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 HIS A 223
REMARK 465 HIS A 224
REMARK 465 ALA A 225
REMARK 465 MET A 226
REMARK 465 GLY A 227
REMARK 465 MET B 218
REMARK 465 HIS B 219
REMARK 465 HIS B 220
REMARK 465 HIS B 221
REMARK 465 HIS B 222
REMARK 465 HIS B 223
REMARK 465 HIS B 224
REMARK 465 ALA B 225
REMARK 465 MET B 226
REMARK 465 GLY B 227
REMARK 465 ASN B 287
REMARK 465 THR B 288
REMARK 465 LYS B 289
REMARK 465 VAL B 290
REMARK 465 ALA B 291
REMARK 465 GLU B 292
REMARK 465 ALA B 293
REMARK 465 GLU B 294
REMARK 465 MET B 295
REMARK 465 ALA B 296
REMARK 465 VAL B 413
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 LYS A 270 CG CD CE NZ
REMARK 470 ASN A 274 CG OD1 ND2
REMARK 470 ARG A 286 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 289 CG CD CE NZ
REMARK 470 GLU A 316 CG CD OE1 OE2
REMARK 470 GLU A 329 CG CD OE1 OE2
REMARK 470 GLU A 377 CG CD OE1 OE2
REMARK 470 GLU A 393 CG CD OE1 OE2
REMARK 470 ASP B 240 CG OD1 OD2
REMARK 470 THR B 297 OG1 CG2
REMARK 470 MET B 298 CG SD CE
REMARK 470 GLN B 372 CG CD OE1 NE2
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 LEU A 267 CA - CB - CG ANGL. DEV. = 16.9 DEGREES
REMARK 500 ASP A 342 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 345 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP A 391 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP B 283 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 345 CB - CG - OD2 ANGL. DEV. = 5.8 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 ALA A 296 0.42 -64.88
REMARK 500 HIS A 341 -0.74 -152.53
REMARK 500 ASN B 275 93.56 -175.44
REMARK 500 TYR B 330 -5.16 74.07
REMARK 500 VAL B 359 -7.67 -142.70
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 MET A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MET B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AJG RELATED DB: PDB
REMARK 900 THE SAME PROTEIN
REMARK 900 RELATED ID: 2AJI RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ISOLEUCINE
DBREF 2AJH A 228 413 UNP P07813 SYL_ECOLI 228 413
DBREF 2AJH B 228 413 UNP P07813 SYL_ECOLI 228 413
SEQADV 2AJH MET A 218 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS A 219 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS A 220 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS A 221 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS A 222 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS A 223 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS A 224 UNP P07813 EXPRESSION TAG
SEQADV 2AJH ALA A 225 UNP P07813 EXPRESSION TAG
SEQADV 2AJH MET A 226 UNP P07813 EXPRESSION TAG
SEQADV 2AJH GLY A 227 UNP P07813 EXPRESSION TAG
SEQADV 2AJH MET B 218 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS B 219 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS B 220 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS B 221 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS B 222 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS B 223 UNP P07813 EXPRESSION TAG
SEQADV 2AJH HIS B 224 UNP P07813 EXPRESSION TAG
SEQADV 2AJH ALA B 225 UNP P07813 EXPRESSION TAG
SEQADV 2AJH MET B 226 UNP P07813 EXPRESSION TAG
SEQADV 2AJH GLY B 227 UNP P07813 EXPRESSION TAG
SEQRES 1 A 196 MET HIS HIS HIS HIS HIS HIS ALA MET GLY GLU GLY VAL
SEQRES 2 A 196 GLU ILE THR PHE ASN VAL ASN ASP TYR ASP ASN THR LEU
SEQRES 3 A 196 THR VAL TYR THR THR ARG PRO ASP THR PHE MET GLY CYS
SEQRES 4 A 196 THR TYR LEU ALA VAL ALA ALA GLY HIS PRO LEU ALA GLN
SEQRES 5 A 196 LYS ALA ALA GLU ASN ASN PRO GLU LEU ALA ALA PHE ILE
SEQRES 6 A 196 ASP GLU CYS ARG ASN THR LYS VAL ALA GLU ALA GLU MET
SEQRES 7 A 196 ALA THR MET GLU LYS LYS GLY VAL ASP THR GLY PHE LYS
SEQRES 8 A 196 ALA VAL HIS PRO LEU THR GLY GLU GLU ILE PRO VAL TRP
SEQRES 9 A 196 ALA ALA ASN PHE VAL LEU MET GLU TYR GLY THR GLY ALA
SEQRES 10 A 196 VAL MET ALA VAL PRO GLY HIS ASP GLN ARG ASP TYR GLU
SEQRES 11 A 196 PHE ALA SER LYS TYR GLY LEU ASN ILE LYS PRO VAL ILE
SEQRES 12 A 196 LEU ALA ALA ASP GLY SER GLU PRO ASP LEU SER GLN GLN
SEQRES 13 A 196 ALA LEU THR GLU LYS GLY VAL LEU PHE ASN SER GLY GLU
SEQRES 14 A 196 PHE ASN GLY LEU ASP HIS GLU ALA ALA PHE ASN ALA ILE
SEQRES 15 A 196 ALA ASP LYS LEU THR ALA MET GLY VAL GLY GLU ARG LYS
SEQRES 16 A 196 VAL
SEQRES 1 B 196 MET HIS HIS HIS HIS HIS HIS ALA MET GLY GLU GLY VAL
SEQRES 2 B 196 GLU ILE THR PHE ASN VAL ASN ASP TYR ASP ASN THR LEU
SEQRES 3 B 196 THR VAL TYR THR THR ARG PRO ASP THR PHE MET GLY CYS
SEQRES 4 B 196 THR TYR LEU ALA VAL ALA ALA GLY HIS PRO LEU ALA GLN
SEQRES 5 B 196 LYS ALA ALA GLU ASN ASN PRO GLU LEU ALA ALA PHE ILE
SEQRES 6 B 196 ASP GLU CYS ARG ASN THR LYS VAL ALA GLU ALA GLU MET
SEQRES 7 B 196 ALA THR MET GLU LYS LYS GLY VAL ASP THR GLY PHE LYS
SEQRES 8 B 196 ALA VAL HIS PRO LEU THR GLY GLU GLU ILE PRO VAL TRP
SEQRES 9 B 196 ALA ALA ASN PHE VAL LEU MET GLU TYR GLY THR GLY ALA
SEQRES 10 B 196 VAL MET ALA VAL PRO GLY HIS ASP GLN ARG ASP TYR GLU
SEQRES 11 B 196 PHE ALA SER LYS TYR GLY LEU ASN ILE LYS PRO VAL ILE
SEQRES 12 B 196 LEU ALA ALA ASP GLY SER GLU PRO ASP LEU SER GLN GLN
SEQRES 13 B 196 ALA LEU THR GLU LYS GLY VAL LEU PHE ASN SER GLY GLU
SEQRES 14 B 196 PHE ASN GLY LEU ASP HIS GLU ALA ALA PHE ASN ALA ILE
SEQRES 15 B 196 ALA ASP LYS LEU THR ALA MET GLY VAL GLY GLU ARG LYS
SEQRES 16 B 196 VAL
HET MET A 501 9
HET MET B 601 9
HETNAM MET METHIONINE
FORMUL 3 MET 2(C5 H11 N O2 S)
FORMUL 5 HOH *78(H2 O)
HELIX 1 1 ARG A 249 CYS A 256 5 8
HELIX 2 2 HIS A 265 GLU A 273 1 9
HELIX 3 3 ASN A 275 THR A 288 1 14
HELIX 4 4 ALA A 291 MET A 295 5 5
HELIX 5 5 ASP A 342 GLY A 353 1 12
HELIX 6 6 SER A 384 ASN A 388 5 5
HELIX 7 7 ASP A 391 MET A 406 1 16
HELIX 8 8 ARG B 249 CYS B 256 5 8
HELIX 9 9 HIS B 265 GLU B 273 1 9
HELIX 10 10 ASN B 275 CYS B 285 1 11
HELIX 11 11 ASP B 342 GLY B 353 1 12
HELIX 12 12 SER B 384 ASN B 388 5 5
HELIX 13 13 ASP B 391 MET B 406 1 16
SHEET 1 A 6 THR A 242 THR A 247 0
SHEET 2 A 6 GLY A 229 VAL A 236 -1 N VAL A 230 O THR A 247
SHEET 3 A 6 GLY A 302 VAL A 310 -1 O VAL A 310 N ASN A 235
SHEET 4 A 6 GLU A 317 ALA A 323 -1 O ILE A 318 N ALA A 309
SHEET 5 A 6 TYR A 258 ALA A 262 1 N LEU A 259 O TRP A 321
SHEET 6 A 6 ALA A 334 ALA A 337 -1 O VAL A 335 N ALA A 260
SHEET 1 B 3 THR A 242 THR A 247 0
SHEET 2 B 3 GLY A 229 VAL A 236 -1 N VAL A 230 O THR A 247
SHEET 3 B 3 GLY A 409 LYS A 412 -1 O GLU A 410 N GLU A 231
SHEET 1 C 3 LEU B 243 THR B 247 0
SHEET 2 C 3 GLY B 229 PHE B 234 -1 N ILE B 232 O VAL B 245
SHEET 3 C 3 GLY B 409 LYS B 412 -1 O GLU B 410 N GLU B 231
SHEET 1 D 4 GLY B 302 VAL B 310 0
SHEET 2 D 4 GLU B 317 ALA B 323 -1 O VAL B 320 N THR B 305
SHEET 3 D 4 TYR B 258 ALA B 262 1 N LEU B 259 O TRP B 321
SHEET 4 D 4 ALA B 334 ALA B 337 -1 O VAL B 335 N ALA B 260
SITE 1 AC1 10 HOH A 8 THR A 247 ARG A 249 THR A 252
SITE 2 AC1 10 MET A 336 VAL A 338 HIS A 341 ASP A 342
SITE 3 AC1 10 ASP A 345 HOH B 12
SITE 1 AC2 8 ASP A 364 THR B 247 ARG B 249 THR B 252
SITE 2 AC2 8 MET B 336 HIS B 341 ASP B 342 ASP B 345
CRYST1 111.518 111.518 134.931 90.00 90.00 120.00 P 63 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 0.008967 0.005177 0.000000 0.00000
SCALE2 0.000000 0.010354 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007411 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
