HEADER LIGASE/RNA 24-APR-12 4ARI
TITLE TERNARY COMPLEX OF E. COLI LEUCYL-TRNA SYNTHETASE, TRNA(LEU) AND THE
TITLE 2 BENZOXABOROLE AN2679 IN THE EDITING CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUCINE--TRNA LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LEUCYL-TRNA SYNTHETASE, LEURS;
COMPND 5 EC: 6.1.1.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TRNA-LEU5 (UAA ISOACEPTOR);
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: UNMODIFIED T7 TRANSCRIPT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-15B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 13 ORGANISM_TAXID: 83333
KEYWDS LIGASE-RNA COMPLEX, LIGASE, NUCLEOTIDE(ATP)-BINDING, PROTEIN
KEYWDS 2 BIOSYNTHESIS, CLASS I AMINOACYL-TRNA SYNTHETASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PALENCIA,T.CREPIN,M.T.VU,T.L.LINCECUM JR,S.A.MARTINIS,S.CUSACK
REVDAT 5 20-DEC-23 4ARI 1 REMARK LINK
REVDAT 4 15-MAY-19 4ARI 1 SEQRES LINK
REVDAT 3 25-JUL-12 4ARI 1 JRNL
REVDAT 2 20-JUN-12 4ARI 1 JRNL
REVDAT 1 13-JUN-12 4ARI 0
JRNL AUTH A.PALENCIA,T.CREPIN,M.T.VU,T.L.LINCECUM JR,S.A.MARTINIS,
JRNL AUTH 2 S.CUSACK
JRNL TITL STRUCTURAL DYNAMICS OF THE AMINOACYLATION AND PROOFREADING
JRNL TITL 2 FUNCTIONAL CYCLE OF BACTERIAL LEUCYL-TRNA SYNTHETASE
JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 677 2012
JRNL REFN ISSN 1545-9993
JRNL PMID 22683997
JRNL DOI 10.1038/NSMB.2317
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0116
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) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 90.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 71134
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3759
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) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.14
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3937
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 199
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6521
REMARK 3 NUCLEIC ACID ATOMS : 1720
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 324
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.37000
REMARK 3 B22 (A**2) : 0.44000
REMARK 3 B33 (A**2) : -0.08000
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): 0.206
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.182
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.660
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8619 ; 0.011 ; 0.018
REMARK 3 BOND LENGTHS OTHERS (A): 5315 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12076 ; 1.497 ; 1.840
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12938 ; 0.994 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 819 ; 6.016 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 318 ;31.331 ;24.465
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1134 ;15.542 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;18.819 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1306 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8414 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1794 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4ARI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1290052174.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74893
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
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 (%) : 96.7
REMARK 200 DATA REDUNDANCY : 3.910
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1H3N
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE TERNARY COMPLEX ECLEURS-TRNA
REMARK 280 -AN2679 WAS CRYSTALLIZED FROM 0.1 M SODIUM ACETATE (PH 5.6), 14-
REMARK 280 18% (W/V) PEG 6000 AND 20 MM NACL. THE CRYSTALS WERE FROZEN IN
REMARK 280 LIQUID NITROGEN USING 22% (V/V) ETHYLENE GLYCOL AS CRYOPROTECTANT
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 38.09000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.51500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.47000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.51500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.09000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.47000
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: 6110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 ASN A 157
REMARK 465 TRP A 158
REMARK 465 CYS A 159
REMARK 465 PRO A 160
REMARK 465 ASN A 161
REMARK 465 ASP A 162
REMARK 465 GLN A 163
REMARK 465 THR A 164
REMARK 465 VAL A 165
REMARK 465 LEU A 166
REMARK 465 ALA A 167
REMARK 465 ASN A 168
REMARK 465 GLU A 169
REMARK 465 GLN A 170
REMARK 465 VAL A 171
REMARK 465 ILE A 172
REMARK 465 ASP A 173
REMARK 465 GLY A 174
REMARK 465 CYS A 175
REMARK 465 CYS A 176
REMARK 465 TRP A 177
REMARK 465 ARG A 178
REMARK 465 CYS A 179
REMARK 465 ASP A 180
REMARK 465 THR A 181
REMARK 465 LYS A 182
REMARK 465 VAL A 183
REMARK 465 GLU A 184
REMARK 465 ARG A 185
REMARK 465 LYS A 186
REMARK 465 LYS A 289
REMARK 465 VAL A 290
REMARK 465 ALA A 291
REMARK 465 GLU A 292
REMARK 465 ALA A 293
REMARK 465 GLU A 294
REMARK 465 MET A 295
REMARK 465 ALA A 296
REMARK 465 THR A 297
REMARK 465 MET A 298
REMARK 465 U B 32
REMARK 465 U B 33
REMARK 465 U B 34
REMARK 465 A B 35
REMARK 465 A B 36
REMARK 465 A B 37
REMARK 465 A B 38
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 HIS A 0 CB CG ND1 CD2 CE1 NE2
REMARK 470 THR A 288 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2087 O HOH A 2090 1.96
REMARK 500 OH TYR A 849 O3 GOL A 1862 2.10
REMARK 500 OH TYR A 65 O HOH A 2043 2.14
REMARK 500 OP1 G B 13 O HOH A 2224 2.15
REMARK 500 OE2 GLU A 367 O HOH A 2140 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 533 CG HIS A 533 CD2 0.059
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 344 NE - CZ - NH2 ANGL. DEV. = -3.2 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 TYR A 132 -60.15 -90.01
REMARK 500 ASP A 240 43.28 -88.91
REMARK 500 ASN A 287 -89.63 -73.07
REMARK 500 VAL A 359 -1.30 -140.09
REMARK 500 CYS A 505 54.13 -165.20
REMARK 500 MET A 536 -97.22 -108.00
REMARK 500 ASP A 596 -178.82 -66.25
REMARK 500 THR A 741 27.16 -143.75
REMARK 500 LYS A 853 -54.92 -138.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2121 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A2186 DISTANCE = 6.95 ANGSTROMS
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 A1865 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 236 O
REMARK 620 2 TYR A 239 O 88.8
REMARK 620 3 HOH A2108 O 79.8 102.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1076 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U B 8 OP1
REMARK 620 2 G B 9 OP2 81.4
REMARK 620 3 HOH B2003 O 71.5 76.6
REMARK 620 4 HOH B2005 O 152.2 85.4 81.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1861
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1862
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1863
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1864
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1865
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1076
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AJG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EDITING DOMAIN OF E. COLI LEUCYL-TRNA
REMARK 900 SYNTHETASE
REMARK 900 RELATED ID: 2AJH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EDITING DOMAIN OF E. COLI LEUCYL-TRNA
REMARK 900 SYNTHETASE COMPLEXES WITH METHIONINE
REMARK 900 RELATED ID: 2AJI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE EDITING DOMAIN OF E. COLI LEUCYL-TRNA
REMARK 900 SYNTHETASE COMPLEXES WITH ISOLEUCINE
REMARK 900 RELATED ID: 4AQ7 RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF E. COLI LEUCYL-TRNA SYNTHETASE, TRNA(LEU) AND
REMARK 900 LEUCYL-ADENYLATE ANALOGUE IN THE AMINOACYLATION CONFORMATION
REMARK 900 RELATED ID: 4ARC RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF E. COLI LEUCYL-TRNA SYNTHETASE, TRNA(LEU) AND
REMARK 900 LEUCINE IN THE EDITING CONFORMATION
REMARK 900 RELATED ID: 4AS1 RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF E. COLI LEUCYL-TRNA SYNTHETASE, TRNA(LEU) AND
REMARK 900 THE BENZOXABOROLE AN2679 IN THE EDITING CONFORMATION
DBREF 4ARI A 1 860 UNP P07813 SYL_ECOLI 1 860
DBREF 4ARI B 1 76 PDB 4ARI 4ARI 1 76
SEQADV 4ARI MET A -19 UNP P07813 EXPRESSION TAG
SEQADV 4ARI GLY A -18 UNP P07813 EXPRESSION TAG
SEQADV 4ARI SER A -17 UNP P07813 EXPRESSION TAG
SEQADV 4ARI SER A -16 UNP P07813 EXPRESSION TAG
SEQADV 4ARI HIS A -15 UNP P07813 EXPRESSION TAG
SEQADV 4ARI HIS A -14 UNP P07813 EXPRESSION TAG
SEQADV 4ARI HIS A -13 UNP P07813 EXPRESSION TAG
SEQADV 4ARI HIS A -12 UNP P07813 EXPRESSION TAG
SEQADV 4ARI HIS A -11 UNP P07813 EXPRESSION TAG
SEQADV 4ARI HIS A -10 UNP P07813 EXPRESSION TAG
SEQADV 4ARI SER A -9 UNP P07813 EXPRESSION TAG
SEQADV 4ARI SER A -8 UNP P07813 EXPRESSION TAG
SEQADV 4ARI GLY A -7 UNP P07813 EXPRESSION TAG
SEQADV 4ARI LEU A -6 UNP P07813 EXPRESSION TAG
SEQADV 4ARI VAL A -5 UNP P07813 EXPRESSION TAG
SEQADV 4ARI PRO A -4 UNP P07813 EXPRESSION TAG
SEQADV 4ARI ARG A -3 UNP P07813 EXPRESSION TAG
SEQADV 4ARI GLY A -2 UNP P07813 EXPRESSION TAG
SEQADV 4ARI SER A -1 UNP P07813 EXPRESSION TAG
SEQRES 1 A 880 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 880 LEU VAL PRO ARG GLY SER HIS MET GLN GLU GLN TYR ARG
SEQRES 3 A 880 PRO GLU GLU ILE GLU SER LYS VAL GLN LEU HIS TRP ASP
SEQRES 4 A 880 GLU LYS ARG THR PHE GLU VAL THR GLU ASP GLU SER LYS
SEQRES 5 A 880 GLU LYS TYR TYR CYS LEU SER MET LEU PRO TYR PRO SER
SEQRES 6 A 880 GLY ARG LEU HIS MET GLY HIS VAL ARG ASN TYR THR ILE
SEQRES 7 A 880 GLY ASP VAL ILE ALA ARG TYR GLN ARG MET LEU GLY LYS
SEQRES 8 A 880 ASN VAL LEU GLN PRO ILE GLY TRP ASP ALA PHE GLY LEU
SEQRES 9 A 880 PRO ALA GLU GLY ALA ALA VAL LYS ASN ASN THR ALA PRO
SEQRES 10 A 880 ALA PRO TRP THR TYR ASP ASN ILE ALA TYR MET LYS ASN
SEQRES 11 A 880 GLN LEU LYS MET LEU GLY PHE GLY TYR ASP TRP SER ARG
SEQRES 12 A 880 GLU LEU ALA THR CYS THR PRO GLU TYR TYR ARG TRP GLU
SEQRES 13 A 880 GLN LYS PHE PHE THR GLU LEU TYR LYS LYS GLY LEU VAL
SEQRES 14 A 880 TYR LYS LYS THR SER ALA VAL ASN TRP CYS PRO ASN ASP
SEQRES 15 A 880 GLN THR VAL LEU ALA ASN GLU GLN VAL ILE ASP GLY CYS
SEQRES 16 A 880 CYS TRP ARG CYS ASP THR LYS VAL GLU ARG LYS GLU ILE
SEQRES 17 A 880 PRO GLN TRP PHE ILE LYS ILE THR ALA TYR ALA ASP GLU
SEQRES 18 A 880 LEU LEU ASN ASP LEU ASP LYS LEU ASP HIS TRP PRO ASP
SEQRES 19 A 880 THR VAL LYS THR MET GLN ARG ASN TRP ILE GLY ARG SER
SEQRES 20 A 880 GLU GLY VAL GLU ILE THR PHE ASN VAL ASN ASP TYR ASP
SEQRES 21 A 880 ASN THR LEU THR VAL TYR THR THR ARG PRO ASP THR PHE
SEQRES 22 A 880 MET GLY CYS THR TYR LEU ALA VAL ALA ALA GLY HIS PRO
SEQRES 23 A 880 LEU ALA GLN LYS ALA ALA GLU ASN ASN PRO GLU LEU ALA
SEQRES 24 A 880 ALA PHE ILE ASP GLU CYS ARG ASN THR LYS VAL ALA GLU
SEQRES 25 A 880 ALA GLU MET ALA THR MET GLU LYS LYS GLY VAL ASP THR
SEQRES 26 A 880 GLY PHE LYS ALA VAL HIS PRO LEU THR GLY GLU GLU ILE
SEQRES 27 A 880 PRO VAL TRP ALA ALA ASN PHE VAL LEU MET GLU TYR GLY
SEQRES 28 A 880 THR GLY ALA VAL MET ALA VAL PRO GLY HIS ASP GLN ARG
SEQRES 29 A 880 ASP TYR GLU PHE ALA SER LYS TYR GLY LEU ASN ILE LYS
SEQRES 30 A 880 PRO VAL ILE LEU ALA ALA ASP GLY SER GLU PRO ASP LEU
SEQRES 31 A 880 SER GLN GLN ALA LEU THR GLU LYS GLY VAL LEU PHE ASN
SEQRES 32 A 880 SER GLY GLU PHE ASN GLY LEU ASP HIS GLU ALA ALA PHE
SEQRES 33 A 880 ASN ALA ILE ALA ASP LYS LEU THR ALA MET GLY VAL GLY
SEQRES 34 A 880 GLU ARG LYS VAL ASN TYR ARG LEU ARG ASP TRP GLY VAL
SEQRES 35 A 880 SER ARG GLN ARG TYR TRP GLY ALA PRO ILE PRO MET VAL
SEQRES 36 A 880 THR LEU GLU ASP GLY THR VAL MET PRO THR PRO ASP ASP
SEQRES 37 A 880 GLN LEU PRO VAL ILE LEU PRO GLU ASP VAL VAL MET ASP
SEQRES 38 A 880 GLY ILE THR SER PRO ILE LYS ALA ASP PRO GLU TRP ALA
SEQRES 39 A 880 LYS THR THR VAL ASN GLY MET PRO ALA LEU ARG GLU THR
SEQRES 40 A 880 ASP THR PHE ASP THR PHE MET GLU SER SER TRP TYR TYR
SEQRES 41 A 880 ALA ARG TYR THR CYS PRO GLN TYR LYS GLU GLY MET LEU
SEQRES 42 A 880 ASP SER GLU ALA ALA ASN TYR TRP LEU PRO VAL ASP ILE
SEQRES 43 A 880 TYR ILE GLY GLY ILE GLU HIS ALA ILE MET HIS LEU LEU
SEQRES 44 A 880 TYR PHE ARG PHE PHE HIS LYS LEU MET ARG ASP ALA GLY
SEQRES 45 A 880 MET VAL ASN SER ASP GLU PRO ALA LYS GLN LEU LEU CYS
SEQRES 46 A 880 GLN GLY MET VAL LEU ALA ASP ALA PHE TYR TYR VAL GLY
SEQRES 47 A 880 GLU ASN GLY GLU ARG ASN TRP VAL SER PRO VAL ASP ALA
SEQRES 48 A 880 ILE VAL GLU ARG ASP GLU LYS GLY ARG ILE VAL LYS ALA
SEQRES 49 A 880 LYS ASP ALA ALA GLY HIS GLU LEU VAL TYR THR GLY MET
SEQRES 50 A 880 SER LYS MET SER LYS SER LYS ASN ASN GLY ILE ASP PRO
SEQRES 51 A 880 GLN VAL MET VAL GLU ARG TYR GLY ALA ASP THR VAL ARG
SEQRES 52 A 880 LEU PHE MET MET PHE ALA SER PRO ALA ASP MET THR LEU
SEQRES 53 A 880 GLU TRP GLN GLU SER GLY VAL GLU GLY ALA ASN ARG PHE
SEQRES 54 A 880 LEU LYS ARG VAL TRP LYS LEU VAL TYR GLU HIS THR ALA
SEQRES 55 A 880 LYS GLY ASP VAL ALA ALA LEU ASN VAL ASP ALA LEU THR
SEQRES 56 A 880 GLU ASN GLN LYS ALA LEU ARG ARG ASP VAL HIS LYS THR
SEQRES 57 A 880 ILE ALA LYS VAL THR ASP ASP ILE GLY ARG ARG GLN THR
SEQRES 58 A 880 PHE ASN THR ALA ILE ALA ALA ILE MET GLU LEU MET ASN
SEQRES 59 A 880 LYS LEU ALA LYS ALA PRO THR ASP GLY GLU GLN ASP ARG
SEQRES 60 A 880 ALA LEU MET GLN GLU ALA LEU LEU ALA VAL VAL ARG MET
SEQRES 61 A 880 LEU ASN PRO PHE THR PRO HIS ILE CYS PHE THR LEU TRP
SEQRES 62 A 880 GLN GLU LEU LYS GLY GLU GLY ASP ILE ASP ASN ALA PRO
SEQRES 63 A 880 TRP PRO VAL ALA ASP GLU LYS ALA MET VAL GLU ASP SER
SEQRES 64 A 880 THR LEU VAL VAL VAL GLN VAL ASN GLY LYS VAL ARG ALA
SEQRES 65 A 880 LYS ILE THR VAL PRO VAL ASP ALA THR GLU GLU GLN VAL
SEQRES 66 A 880 ARG GLU ARG ALA GLY GLN GLU HIS LEU VAL ALA LYS TYR
SEQRES 67 A 880 LEU ASP GLY VAL THR VAL ARG LYS VAL ILE TYR VAL PRO
SEQRES 68 A 880 GLY LYS LEU LEU ASN LEU VAL VAL GLY
SEQRES 1 B 87 G C C C G G A U G G U G G
SEQRES 2 B 87 A A U C G G U A G A C A C
SEQRES 3 B 87 A A G G G A U U U A A A A
SEQRES 4 B 87 U C C C U C G G C G U U C
SEQRES 5 B 87 G C G C U G U G C G G G U
SEQRES 6 B 87 U C A A G U C C C G C U C
SEQRES 7 B 87 C G G G U A C C N79
MODRES 4ARI N79 B 76 A
HET N79 B 76 31
HET GOL A1861 6
HET GOL A1862 6
HET GOL A1863 6
HET GOL A1864 6
HET MG A1865 1
HET MG B1076 1
HETNAM N79 [(1S,5R,6R,8R)-6-(6-AMINOPURIN-9-YL)SPIRO[2,4,7-TRIOXA-
HETNAM 2 N79 3-BORANUIDABICYCLO[3.3.0]OCTANE-3,9'-8-OXA-9-
HETNAM 3 N79 BORANUIDABICYCLO[4.3.0]NONA-1(6),2,4-TRIENE]-8-
HETNAM 4 N79 YL]METHYL DIHYDROGEN PHOSPHATE
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 N79 C17 H18 B N5 O8 P 1-
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 7 MG 2(MG 2+)
FORMUL 9 HOH *324(H2 O)
HELIX 1 1 ARG A 6 LYS A 21 1 16
HELIX 2 2 HIS A 49 LEU A 69 1 21
HELIX 3 3 LEU A 84 ASN A 93 1 10
HELIX 4 4 ALA A 96 LEU A 115 1 20
HELIX 5 5 ASP A 120 GLU A 124 5 5
HELIX 6 6 THR A 129 LYS A 146 1 18
HELIX 7 7 ILE A 195 ALA A 197 5 3
HELIX 8 8 TYR A 198 ASP A 205 1 8
HELIX 9 9 LEU A 206 LEU A 209 5 4
HELIX 10 10 PRO A 213 GLY A 225 1 13
HELIX 11 11 ARG A 249 CYS A 256 5 8
HELIX 12 12 HIS A 265 GLU A 273 1 9
HELIX 13 13 ASN A 275 THR A 288 1 14
HELIX 14 14 ASP A 342 GLY A 353 1 12
HELIX 15 15 SER A 384 ASN A 388 5 5
HELIX 16 16 ASP A 391 MET A 406 1 16
HELIX 17 17 PRO A 446 LEU A 450 5 5
HELIX 18 18 SER A 465 ASP A 470 1 6
HELIX 19 19 THR A 492 SER A 497 1 6
HELIX 20 20 TRP A 498 TYR A 503 1 6
HELIX 21 21 ASP A 514 LEU A 522 1 9
HELIX 22 22 GLY A 530 ALA A 534 5 5
HELIX 23 23 MET A 536 ALA A 551 1 16
HELIX 24 24 SER A 587 ALA A 591 5 5
HELIX 25 25 ASP A 629 GLY A 638 1 10
HELIX 26 26 GLY A 638 ALA A 649 1 12
HELIX 27 27 GLN A 659 LYS A 683 1 25
HELIX 28 28 THR A 695 ARG A 718 1 24
HELIX 29 29 THR A 721 ALA A 739 1 19
HELIX 30 30 GLY A 743 ASN A 762 1 20
HELIX 31 31 THR A 765 LEU A 776 1 12
HELIX 32 32 ASP A 781 ALA A 785 5 5
HELIX 33 33 ASP A 791 VAL A 796 1 6
HELIX 34 34 THR A 821 GLN A 831 1 11
HELIX 35 35 GLU A 832 LYS A 837 1 6
SHEET 1 AA 4 ASN A 72 LEU A 74 0
SHEET 2 AA 4 LYS A 34 SER A 39 1 O TYR A 35 N LEU A 74
SHEET 3 AA 4 VAL A 524 ILE A 528 1 N ASP A 525 O TYR A 36
SHEET 4 AA 4 ALA A 560 LEU A 564 1 N LYS A 561 O VAL A 524
SHEET 1 AB 2 GLY A 78 TRP A 79 0
SHEET 2 AB 2 LEU A 125 ALA A 126 1 O LEU A 125 N TRP A 79
SHEET 1 AC 3 VAL A 149 SER A 154 0
SHEET 2 AC 3 ILE A 188 ILE A 193 -1 O ILE A 188 N SER A 154
SHEET 3 AC 3 TRP A 420 GLY A 421 -1 O TRP A 420 N ILE A 193
SHEET 1 AD 3 THR A 242 THR A 247 0
SHEET 2 AD 3 ARG A 226 ASN A 235 -1 O VAL A 230 N THR A 247
SHEET 3 AD 3 GLY A 409 TYR A 415 -1 O GLU A 410 N GLU A 231
SHEET 1 AE 4 GLY A 302 VAL A 310 0
SHEET 2 AE 4 GLU A 317 ALA A 323 -1 O ILE A 318 N ALA A 309
SHEET 3 AE 4 TYR A 258 VAL A 261 1 O LEU A 259 N TRP A 321
SHEET 4 AE 4 ALA A 334 ALA A 337 -1 O VAL A 335 N ALA A 260
SHEET 1 AF 2 SER A 423 ARG A 424 0
SHEET 2 AF 2 THR A 489 PHE A 490 -1 O THR A 489 N ARG A 424
SHEET 1 AG 4 VAL A 442 PRO A 444 0
SHEET 2 AG 4 MET A 434 LEU A 437 -1 O VAL A 435 N MET A 443
SHEET 3 AG 4 MET A 481 ARG A 485 -1 O LEU A 484 N THR A 436
SHEET 4 AG 4 LYS A 475 VAL A 478 -1 O THR A 476 N ALA A 483
SHEET 1 AH 2 ARG A 583 VAL A 586 0
SHEET 2 AH 2 VAL A 569 VAL A 577 -1 O PHE A 574 N VAL A 586
SHEET 1 AI 5 ILE A 592 ARG A 595 0
SHEET 2 AI 5 ILE A 601 LYS A 605 -1 N VAL A 602 O GLU A 594
SHEET 3 AI 5 GLU A 611 LYS A 619 -1 O LEU A 612 N ALA A 604
SHEET 4 AI 5 VAL A 569 VAL A 577 -1 O ALA A 571 N SER A 618
SHEET 5 AI 5 ARG A 583 VAL A 586 -1 O ASN A 584 N TYR A 576
SHEET 1 AJ 5 ILE A 592 ARG A 595 0
SHEET 2 AJ 5 ILE A 601 LYS A 605 -1 N VAL A 602 O GLU A 594
SHEET 3 AJ 5 GLU A 611 LYS A 619 -1 O LEU A 612 N ALA A 604
SHEET 4 AJ 5 VAL A 569 VAL A 577 -1 O ALA A 571 N SER A 618
SHEET 5 AJ 5 LEU A 656 GLU A 657 1 O LEU A 656 N LEU A 570
SHEET 1 AK 4 LYS A 809 PRO A 817 0
SHEET 2 AK 4 SER A 799 VAL A 806 -1 O THR A 800 N VAL A 816
SHEET 3 AK 4 LEU A 854 GLY A 860 1 O LEU A 855 N GLN A 805
SHEET 4 AK 4 THR A 843 VAL A 850 -1 O THR A 843 N GLY A 860
LINK O3' C B 75 P N79 B 76 1555 1555 1.60
LINK O VAL A 236 MG MG A1865 1555 1555 2.56
LINK O TYR A 239 MG MG A1865 1555 1555 2.02
LINK MG MG A1865 O HOH A2108 1555 1555 2.50
LINK OP1 U B 8 MG MG B1076 1555 1555 1.99
LINK OP2 G B 9 MG MG B1076 1555 1555 2.25
LINK MG MG B1076 O HOH B2003 1555 1555 2.45
LINK MG MG B1076 O HOH B2005 1555 1555 1.81
CISPEP 1 LEU A 450 PRO A 451 0 0.42
CISPEP 2 LEU A 522 PRO A 523 0 -1.52
SITE 1 AC1 8 THR A 196 ALA A 197 ALA A 199 ASP A 200
SITE 2 AC1 8 ASP A 819 ALA A 820 GOL A1862 HOH A2091
SITE 1 AC2 9 ALA A 197 TYR A 198 GLU A 201 ALA A 820
SITE 2 AC2 9 THR A 821 GLU A 822 TYR A 849 GOL A1861
SITE 3 AC2 9 HOH A2091
SITE 1 AC3 6 ARG A 759 PRO A 786 TRP A 787 PRO A 788
SITE 2 AC3 6 VAL A 789 GOL A1864
SITE 1 AC4 6 HIS A 706 GLU A 752 ARG A 759 VAL A 789
SITE 2 AC4 6 GOL A1863 HOH A2275
SITE 1 AC5 3 VAL A 236 TYR A 239 HOH A2108
SITE 1 AC6 4 U B 8 G B 9 HOH B2003 HOH B2005
CRYST1 76.180 118.940 141.030 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013127 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008408 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007091 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
