HEADER TRANSFERASE 14-JUN-04 1TOE
TITLE UNLIGANDED STRUCTURE OF HEXAMUTANT + A293D MUTANT OF E. COLI ASPARTATE
TITLE 2 AMINOTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE AMINOTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSAMINASE A, ASPAT;
COMPND 5 EC: 2.6.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ASPC, B0928;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: MG204;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PJO2
KEYWDS ASPARTATE AMINOTRANSFERASE HEXAMUTANT, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.CHOW,K.E.MCELROY,K.D.CORBETT,J.M.BERGER,J.F.KIRSCH
REVDAT 4 13-JUL-11 1TOE 1 VERSN
REVDAT 3 24-FEB-09 1TOE 1 VERSN
REVDAT 2 19-APR-05 1TOE 1 JRNL
REVDAT 1 05-OCT-04 1TOE 0
JRNL AUTH M.A.CHOW,K.E.MCELROY,K.D.CORBETT,J.M.BERGER,J.F.KIRSCH
JRNL TITL NARROWING SUBSTRATE SPECIFICITY IN A DIRECTLY EVOLVED
JRNL TITL 2 ENZYME: THE A293D MUTANT OF ASPARTATE AMINOTRANSFERASE
JRNL REF BIOCHEMISTRY V. 43 12780 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15461450
JRNL DOI 10.1021/BI0487544
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 33481
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1767
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2270
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3089
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.96000
REMARK 3 B22 (A**2) : -2.55000
REMARK 3 B33 (A**2) : 1.59000
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): 0.145
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.091
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.472
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3150 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4262 ; 1.309 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 389 ; 6.333 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 150 ;31.407 ;24.200
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 518 ;19.424 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;24.130 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 469 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2402 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1439 ; 0.258 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2139 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 189 ; 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): 76 ; 0.176 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.155 ; 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): 2013 ; 0.750 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3122 ; 1.216 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1296 ; 2.300 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1140 ; 3.487 ; 4.500
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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 48 A 325
REMARK 3 ORIGIN FOR THE GROUP (A): 89.1606 50.8865 35.7822
REMARK 3 T TENSOR
REMARK 3 T11: -0.0494 T22: -0.0289
REMARK 3 T33: -0.0503 T12: 0.0043
REMARK 3 T13: 0.0037 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 0.7506 L22: 1.7503
REMARK 3 L33: 0.8726 L12: -0.2424
REMARK 3 L13: -0.0361 L23: 0.0071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0133 S12: -0.1596 S13: -0.1224
REMARK 3 S21: 0.3160 S22: -0.0008 S23: -0.0223
REMARK 3 S31: 0.1487 S32: 0.0950 S33: -0.0125
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 : A 15 A 47
REMARK 3 RESIDUE RANGE : A 326 A 409
REMARK 3 ORIGIN FOR THE GROUP (A): 63.7118 58.4356 41.1392
REMARK 3 T TENSOR
REMARK 3 T11: -0.0479 T22: -0.0771
REMARK 3 T33: -0.0505 T12: -0.0269
REMARK 3 T13: 0.1387 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 3.3473 L22: 3.5572
REMARK 3 L33: 1.7357 L12: 1.5933
REMARK 3 L13: -0.4734 L23: -0.9479
REMARK 3 S TENSOR
REMARK 3 S11: 0.1037 S12: -0.0467 S13: 0.1292
REMARK 3 S21: 0.0621 S22: 0.0718 S23: 0.5116
REMARK 3 S31: 0.0959 S32: -0.0664 S33: -0.1755
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 : 1.20
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 1TOE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-04.
REMARK 100 THE RCSB ID CODE IS RCSB022794.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35904
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.5000
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) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1AHE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, PLP, EDTA, DTT,
REMARK 280 PEG 400, N-METHYLMORPHOLINE, AMMONIUM SULFATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.55850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.55850
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 42.85650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.43250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.85650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.43250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.55850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.85650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 76.43250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.55850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.85650
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 76.43250
REMARK 290 SMTRY3 8 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER, THE SECOND PART OF
REMARK 300 WHICH IS GENERATED BY THE TWO-FOLD AXIS: -X+2, -Z+1/2
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 171.42600
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 39.55850
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 241 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 TYR A 160 -45.32 -147.77
REMARK 500 ARG A 266 73.25 61.41
REMARK 500 ASN A 294 -85.92 -109.56
REMARK 500 SER A 296 -57.34 76.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 360 SER A 361 142.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 338 24.4 L L OUTSIDE RANGE
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 A 573 DISTANCE = 5.18 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 410
DBREF 1TOE A 5 400 UNP P00509 AAT_ECOLI 1 396
SEQADV 1TOE LEU A 39 UNP P00509 VAL 35 ENGINEERED
SEQADV 1TOE TYR A 41 UNP P00509 LYS 37 ENGINEERED
SEQADV 1TOE ILE A 47 UNP P00509 THR 43 ENGINEERED
SEQADV 1TOE LEU A 69 UNP P00509 ASN 64 ENGINEERED
SEQADV 1TOE SER A 109 UNP P00509 THR 104 ENGINEERED
SEQADV 1TOE LLP A 258 UNP P00509 LYS 246 MODIFIED RESIDUE
SEQADV 1TOE ASP A 293 UNP P00509 ALA 281 ENGINEERED
SEQADV 1TOE SER A 297 UNP P00509 ASN 285 ENGINEERED
SEQRES 1 A 396 MET PHE GLU ASN ILE THR ALA ALA PRO ALA ASP PRO ILE
SEQRES 2 A 396 LEU GLY LEU ALA ASP LEU PHE ARG ALA ASP GLU ARG PRO
SEQRES 3 A 396 GLY LYS ILE ASN LEU GLY ILE GLY LEU TYR TYR ASP GLU
SEQRES 4 A 396 THR GLY LYS ILE PRO VAL LEU THR SER VAL LYS LYS ALA
SEQRES 5 A 396 GLU GLN TYR LEU LEU GLU ASN GLU THR THR LYS LEU TYR
SEQRES 6 A 396 LEU GLY ILE ASP GLY ILE PRO GLU PHE GLY ARG CYS THR
SEQRES 7 A 396 GLN GLU LEU LEU PHE GLY LYS GLY SER ALA LEU ILE ASN
SEQRES 8 A 396 ASP LYS ARG ALA ARG THR ALA GLN THR PRO GLY GLY SER
SEQRES 9 A 396 GLY ALA LEU ARG VAL ALA ALA ASP PHE LEU ALA LYS ASN
SEQRES 10 A 396 THR SER VAL LYS ARG VAL TRP VAL SER ASN PRO SER TRP
SEQRES 11 A 396 PRO ASN HIS LYS SER VAL PHE ASN SER ALA GLY LEU GLU
SEQRES 12 A 396 VAL ARG GLU TYR ALA TYR TYR ASP ALA GLU ASN HIS THR
SEQRES 13 A 396 LEU ASP PHE ASP ALA LEU ILE ASN SER LEU ASN GLU ALA
SEQRES 14 A 396 GLN ALA GLY ASP VAL VAL LEU PHE HIS GLY CYS CYS HIS
SEQRES 15 A 396 ASN PRO THR GLY ILE ASP PRO THR LEU GLU GLN TRP GLN
SEQRES 16 A 396 THR LEU ALA GLN LEU SER VAL GLU LYS GLY TRP LEU PRO
SEQRES 17 A 396 LEU PHE ASP PHE ALA TYR GLN GLY PHE ALA ARG GLY LEU
SEQRES 18 A 396 GLU GLU ASP ALA GLU GLY LEU ARG ALA PHE ALA ALA MET
SEQRES 19 A 396 HIS LYS GLU LEU ILE VAL ALA SER SER TYR SER LLP ASN
SEQRES 20 A 396 PHE GLY LEU TYR ASN GLU ARG VAL GLY ALA CYS THR LEU
SEQRES 21 A 396 VAL ALA ALA ASP SER GLU THR VAL ASP ARG ALA PHE SER
SEQRES 22 A 396 GLN MET LYS ALA ALA ILE ARG ASP ASN TYR SER SER PRO
SEQRES 23 A 396 PRO ALA HIS GLY ALA SER VAL VAL ALA THR ILE LEU SER
SEQRES 24 A 396 ASN ASP ALA LEU ARG ALA ILE TRP GLU GLN GLU LEU THR
SEQRES 25 A 396 ASP MET ARG GLN ARG ILE GLN ARG MET ARG GLN LEU PHE
SEQRES 26 A 396 VAL ASN THR LEU GLN GLU LYS GLY ALA ASN ARG ASP PHE
SEQRES 27 A 396 SER PHE ILE ILE LYS GLN ASN GLY MET PHE SER PHE SER
SEQRES 28 A 396 GLY LEU THR LYS GLU GLN VAL LEU ARG LEU ARG GLU GLU
SEQRES 29 A 396 PHE GLY VAL TYR ALA VAL ALA SER GLY ARG VAL ASN VAL
SEQRES 30 A 396 ALA GLY MET THR PRO ASP ASN MET ALA PRO LEU CYS GLU
SEQRES 31 A 396 ALA ILE VAL ALA VAL LEU
MODRES 1TOE LLP A 258 LYS
HET LLP A 258 24
HET SO4 A 410 5
HETNAM LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-
HETNAM 2 LLP PYRIDIN-4-YLMETHANE)
HETNAM SO4 SULFATE ION
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP C14 H24 N3 O7 P
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *174(H2 O)
HELIX 1 1 ASP A 15 ALA A 26 1 12
HELIX 2 2 LEU A 50 GLU A 64 1 15
HELIX 3 3 ILE A 76 GLY A 89 1 14
HELIX 4 4 SER A 92 ASP A 97 1 6
HELIX 5 5 PRO A 106 THR A 123 1 18
HELIX 6 6 PRO A 141 ALA A 150 1 10
HELIX 7 7 ASP A 169 ASN A 178 1 10
HELIX 8 8 THR A 201 GLY A 216 1 16
HELIX 9 9 GLY A 231 ALA A 237 1 6
HELIX 10 10 ALA A 237 ALA A 245 1 9
HELIX 11 11 LEU A 262 ARG A 266 5 5
HELIX 12 12 ASP A 276 ASP A 293 1 18
HELIX 13 13 PRO A 299 SER A 311 1 13
HELIX 14 14 ASN A 312 LYS A 344 1 33
HELIX 15 15 SER A 351 GLN A 356 1 6
HELIX 16 16 THR A 366 GLY A 378 1 13
HELIX 17 17 ALA A 390 MET A 392 5 3
HELIX 18 18 THR A 393 LEU A 409 1 16
SHEET 1 A 2 ILE A 33 ASN A 34 0
SHEET 2 A 2 VAL A 379 TYR A 380 1 O TYR A 380 N ILE A 33
SHEET 1 B 7 ALA A 100 THR A 105 0
SHEET 2 B 7 GLY A 268 VAL A 273 -1 O LEU A 272 N ARG A 101
SHEET 3 B 7 LEU A 250 SER A 255 -1 N VAL A 252 O THR A 271
SHEET 4 B 7 LEU A 218 PHE A 223 1 N PHE A 221 O ALA A 253
SHEET 5 B 7 VAL A 185 HIS A 189 1 N PHE A 188 O ASP A 222
SHEET 6 B 7 ARG A 129 ASN A 137 1 N TRP A 134 O LEU A 187
SHEET 7 B 7 GLU A 154 ALA A 159 1 O ARG A 156 N VAL A 135
SHEET 1 C 2 TYR A 161 ASP A 162 0
SHEET 2 C 2 THR A 167 LEU A 168 -1 O THR A 167 N ASP A 162
SHEET 1 D 2 PHE A 360 PHE A 362 0
SHEET 2 D 2 ARG A 386 ASN A 388 -1 O VAL A 387 N SER A 361
LINK C SER A 257 N LLP A 258 1555 1555 1.33
LINK C LLP A 258 N ASN A 259 1555 1555 1.34
CISPEP 1 ASN A 137 PRO A 138 0 1.77
CISPEP 2 ASN A 194 PRO A 195 0 17.50
SITE 1 AC1 5 GLY A 38 TRP A 140 ASN A 194 ARG A 386
SITE 2 AC1 5 HOH A 534
CRYST1 85.713 152.865 79.117 90.00 90.00 90.00 C 2 2 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 0.011667 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006542 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
