HEADER TRANSFERASE (AMINOTRANSFERASE) 23-AUG-95 1ARH
TITLE ASPARTATE AMINOTRANSFERASE, Y225R/R386A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE AMINOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ASPARTATE TRANSAMINASE;
COMPND 5 EC: 2.6.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: 600 TIMES INCREASED BETA-DECARBOXYLASE
COMPND 9 ACTIVITY
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: TY103;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TY103;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PKDHE19
KEYWDS TRANSFERASE (AMINOTRANSFERASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR V.N.MALASHKEVICH,J.N.JANSONIUS
REVDAT 3 24-FEB-09 1ARH 1 VERSN
REVDAT 2 01-APR-03 1ARH 1 JRNL
REVDAT 1 14-NOV-95 1ARH 0
JRNL AUTH R.GRABER,P.KASPER,V.N.MALASHKEVICH,E.SANDMEIER,
JRNL AUTH 2 P.BERGER,H.GEHRING,J.N.JANSONIUS,P.CHRISTEN
JRNL TITL CHANGING THE REACTION SPECIFICITY OF A
JRNL TITL 2 PYRIDOXAL-5'-PHOSPHATE-DEPENDENT ENZYME.
JRNL REF EUR.J.BIOCHEM. V. 232 686 1995
JRNL REFN ISSN 0014-2956
JRNL PMID 7556224
JRNL DOI 10.1111/J.1432-1033.1995.TB20861.X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT V. 4-C
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 43040
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6124
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 372
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 35.300
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.010 ; 0.020 ; 6306
REMARK 3 BOND ANGLES (DEGREES) : 2.060 ; 3.000 ; 8512
REMARK 3 TORSION ANGLES (DEGREES) : 25.000; 15.000; 3758
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.007 ; 0.020 ; 178
REMARK 3 GENERAL PLANES (A) : 0.011 ; 0.020 ; 918
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 3.200 ; 0.200 ; 6544
REMARK 3 NON-BONDED CONTACTS (A) : 0.017 ; 0.100 ; 23
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : MOEWS AND KRETSINGER, JMB (1975) 91,201-22
REMARK 3 KSOL : 0.72
REMARK 3 BSOL : 253.90
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : ENGH AND HUBER
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : B-CORRELATION METHOD
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ARH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-93
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS FAST
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 39.80500
REMARK 290 SMTRY3 2 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: MTRIX
REMARK 300 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
REMARK 300 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300 SECOND.
REMARK 300
REMARK 300 APPLIED TO TRANSFORMED TO
REMARK 300 MTRIX RESIDUES RESIDUES RMSD
REMARK 300 M1 A 5 .. A 409 B 5 .. B 409 0.280
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: 6380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 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 NE2 GLN B 331 O HOH B 571 2.16
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 GLU A 43 CD GLU A 43 OE1 0.069
REMARK 500 GLU A 62 CD GLU A 62 OE2 0.066
REMARK 500 GLU A 85 CD GLU A 85 OE1 0.067
REMARK 500 GLU A 164 CD GLU A 164 OE2 0.067
REMARK 500 GLU A 179 CD GLU A 179 OE2 0.072
REMARK 500 GLU A 235 CD GLU A 235 OE1 0.076
REMARK 500 GLU A 320 CD GLU A 320 OE2 0.070
REMARK 500 GLU B 62 CD GLU B 62 OE2 0.068
REMARK 500 GLU B 85 CD GLU B 85 OE1 0.067
REMARK 500 GLU B 214 CD GLU B 214 OE2 0.068
REMARK 500 GLU B 234 CD GLU B 234 OE2 0.066
REMARK 500 GLU B 278 CD GLU B 278 OE2 0.069
REMARK 500 GLU B 320 CD GLU B 320 OE1 0.070
REMARK 500 GLU B 402 CD GLU B 402 OE2 0.066
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 ASP A 22 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP A 22 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ASP A 117 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 169 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 169 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP A 184 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 236 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 236 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 GLU A 376 CB - CA - C ANGL. DEV. = -15.6 DEGREES
REMARK 500 PHE A 377 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ASP B 15 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP B 15 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP B 22 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 22 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP B 27 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 42 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 42 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASP B 162 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP B 169 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP B 171 CB - CG - OD1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP B 184 CB - CG - OD1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ASP B 184 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 236 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 313 CB - CG - OD2 ANGL. DEV. = -5.4 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 PRO A 30 -86.46 -39.80
REMARK 500 ILE A 37 127.48 -171.65
REMARK 500 GLU A 43 -19.29 -45.41
REMARK 500 TYR A 160 -55.94 -145.29
REMARK 500 ALA A 229 -74.65 -85.52
REMARK 500 ARG A 266 64.63 68.53
REMARK 500 ASN A 294 -83.81 -104.60
REMARK 500 SER A 296 -64.00 87.04
REMARK 500 GLU A 343 -4.36 -58.45
REMARK 500 LEU A 365 153.95 -45.52
REMARK 500 ALA A 407 -6.26 -54.90
REMARK 500 GLU B 7 -39.28 -36.66
REMARK 500 ILE B 17 -60.89 -92.47
REMARK 500 ALA B 26 41.01 -99.17
REMARK 500 GLU B 28 62.11 -103.36
REMARK 500 PRO B 30 -100.65 -47.21
REMARK 500 TYR B 70 142.08 -39.18
REMARK 500 TYR B 160 -47.61 -148.97
REMARK 500 ALA B 229 -69.91 -97.95
REMARK 500 MET B 246 18.82 -150.90
REMARK 500 TYR B 263 -50.31 -27.28
REMARK 500 ARG B 266 68.84 64.99
REMARK 500 ASN B 294 -79.84 -104.03
REMARK 500 SER B 296 -59.45 81.70
REMARK 500 HIS B 301 -71.46 -39.14
REMARK 500 LYS B 344 -5.84 -44.74
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 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: (11X,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 LEU A 23 21.0 L L OUTSIDE RANGE
REMARK 500 ARG A 81 24.9 L L OUTSIDE RANGE
REMARK 500 THR A 83 21.7 L L OUTSIDE RANGE
REMARK 500 LYS A 90 23.3 L L OUTSIDE RANGE
REMARK 500 VAL A 146 23.1 L L OUTSIDE RANGE
REMARK 500 PHE A 170 23.3 L L OUTSIDE RANGE
REMARK 500 ASN A 175 17.7 L L OUTSIDE RANGE
REMARK 500 ASN A 259 22.4 L L OUTSIDE RANGE
REMARK 500 VAL A 273 18.9 L L OUTSIDE RANGE
REMARK 500 HIS A 301 19.8 L L OUTSIDE RANGE
REMARK 500 ASN A 347 23.2 L L OUTSIDE RANGE
REMARK 500 PHE A 377 14.8 L L OUTSIDE RANGE
REMARK 500 ILE A 404 18.3 L L OUTSIDE RANGE
REMARK 500 GLU B 43 23.0 L L OUTSIDE RANGE
REMARK 500 THR B 51 24.8 L L OUTSIDE RANGE
REMARK 500 ASN B 63 24.8 L L OUTSIDE RANGE
REMARK 500 PHE B 88 24.9 L L OUTSIDE RANGE
REMARK 500 VAL B 114 20.9 L L OUTSIDE RANGE
REMARK 500 VAL B 133 24.5 L L OUTSIDE RANGE
REMARK 500 GLU B 154 22.0 L L OUTSIDE RANGE
REMARK 500 ASN B 259 22.6 L L OUTSIDE RANGE
REMARK 500 VAL B 273 21.5 L L OUTSIDE RANGE
REMARK 500 SER B 277 23.2 L L OUTSIDE RANGE
REMARK 500 HIS B 301 22.9 L L OUTSIDE RANGE
REMARK 500 VAL B 370 24.0 L L OUTSIDE RANGE
REMARK 500 ASN B 396 24.9 L L OUTSIDE RANGE
REMARK 500 VAL B 408 24.5 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 B 415 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH B 416 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH A 469 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH A 487 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH A 489 DISTANCE = 12.40 ANGSTROMS
REMARK 525 HOH B 495 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH B 520 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH A 533 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 533 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH B 537 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH A 541 DISTANCE = 8.78 ANGSTROMS
REMARK 525 HOH A 555 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH A 564 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH A 565 DISTANCE = 7.96 ANGSTROMS
REMARK 525 HOH A 576 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH A 581 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 581 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH B 583 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH A 600 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH A 601 DISTANCE = 5.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: BCT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PPD A 411
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PPD B 411
DBREF 1ARH A 5 409 UNP P00509 AAT_ECOLI 1 396
DBREF 1ARH B 5 409 UNP P00509 AAT_ECOLI 1 396
SEQADV 1ARH ARG A 225 UNP P00509 TYR 214 ENGINEERED
SEQADV 1ARH ALA A 386 UNP P00509 ARG 374 ENGINEERED
SEQADV 1ARH ARG B 225 UNP P00509 TYR 214 ENGINEERED
SEQADV 1ARH ALA B 386 UNP P00509 ARG 374 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 VAL TYR LYS ASP GLU
SEQRES 4 A 396 THR GLY LYS THR PRO VAL LEU THR SER VAL LYS LYS ALA
SEQRES 5 A 396 GLU GLN TYR LEU LEU GLU ASN GLU THR THR LYS ASN 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 THR
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 ARG 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 LYS 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 ALA ASN TYR SER ASN 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 ALA 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
SEQRES 1 B 396 MET PHE GLU ASN ILE THR ALA ALA PRO ALA ASP PRO ILE
SEQRES 2 B 396 LEU GLY LEU ALA ASP LEU PHE ARG ALA ASP GLU ARG PRO
SEQRES 3 B 396 GLY LYS ILE ASN LEU GLY ILE GLY VAL TYR LYS ASP GLU
SEQRES 4 B 396 THR GLY LYS THR PRO VAL LEU THR SER VAL LYS LYS ALA
SEQRES 5 B 396 GLU GLN TYR LEU LEU GLU ASN GLU THR THR LYS ASN TYR
SEQRES 6 B 396 LEU GLY ILE ASP GLY ILE PRO GLU PHE GLY ARG CYS THR
SEQRES 7 B 396 GLN GLU LEU LEU PHE GLY LYS GLY SER ALA LEU ILE ASN
SEQRES 8 B 396 ASP LYS ARG ALA ARG THR ALA GLN THR PRO GLY GLY THR
SEQRES 9 B 396 GLY ALA LEU ARG VAL ALA ALA ASP PHE LEU ALA LYS ASN
SEQRES 10 B 396 THR SER VAL LYS ARG VAL TRP VAL SER ASN PRO SER TRP
SEQRES 11 B 396 PRO ASN HIS LYS SER VAL PHE ASN SER ALA GLY LEU GLU
SEQRES 12 B 396 VAL ARG GLU TYR ALA TYR TYR ASP ALA GLU ASN HIS THR
SEQRES 13 B 396 LEU ASP PHE ASP ALA LEU ILE ASN SER LEU ASN GLU ALA
SEQRES 14 B 396 GLN ALA GLY ASP VAL VAL LEU PHE HIS GLY CYS CYS HIS
SEQRES 15 B 396 ASN PRO THR GLY ILE ASP PRO THR LEU GLU GLN TRP GLN
SEQRES 16 B 396 THR LEU ALA GLN LEU SER VAL GLU LYS GLY TRP LEU PRO
SEQRES 17 B 396 LEU PHE ASP PHE ALA ARG GLN GLY PHE ALA ARG GLY LEU
SEQRES 18 B 396 GLU GLU ASP ALA GLU GLY LEU ARG ALA PHE ALA ALA MET
SEQRES 19 B 396 HIS LYS GLU LEU ILE VAL ALA SER SER TYR SER LYS ASN
SEQRES 20 B 396 PHE GLY LEU TYR ASN GLU ARG VAL GLY ALA CYS THR LEU
SEQRES 21 B 396 VAL ALA ALA ASP SER GLU THR VAL ASP ARG ALA PHE SER
SEQRES 22 B 396 GLN MET LYS ALA ALA ILE ARG ALA ASN TYR SER ASN PRO
SEQRES 23 B 396 PRO ALA HIS GLY ALA SER VAL VAL ALA THR ILE LEU SER
SEQRES 24 B 396 ASN ASP ALA LEU ARG ALA ILE TRP GLU GLN GLU LEU THR
SEQRES 25 B 396 ASP MET ARG GLN ARG ILE GLN ARG MET ARG GLN LEU PHE
SEQRES 26 B 396 VAL ASN THR LEU GLN GLU LYS GLY ALA ASN ARG ASP PHE
SEQRES 27 B 396 SER PHE ILE ILE LYS GLN ASN GLY MET PHE SER PHE SER
SEQRES 28 B 396 GLY LEU THR LYS GLU GLN VAL LEU ARG LEU ARG GLU GLU
SEQRES 29 B 396 PHE GLY VAL TYR ALA VAL ALA SER GLY ALA VAL ASN VAL
SEQRES 30 B 396 ALA GLY MET THR PRO ASP ASN MET ALA PRO LEU CYS GLU
SEQRES 31 B 396 ALA ILE VAL ALA VAL LEU
HET PPD A 411 24
HET PPD B 411 24
HETNAM PPD 2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-
HETNAM 2 PPD YLMETHYLENE)-AMINO]-SUCCINIC ACID
HETSYN PPD PYRIDOXYL-ASPARTIC ACID-5-MONOPHOSPHATE
FORMUL 3 PPD 2(C12 H17 N2 O9 P)
FORMUL 5 HOH *371(H2 O)
HELIX 1 1 LEU A 18 ALA A 26 1 9
HELIX 2 2 THR A 51 ASN A 63 1 13
HELIX 3 3 PRO A 77 PHE A 88 1 12
HELIX 4 4 ALA A 93 ASN A 96 1 4
HELIX 5 5 GLY A 107 ASN A 122 1 16
HELIX 6 6 PRO A 141 ALA A 150 5 10
HELIX 7 7 PHE A 170 GLU A 179 1 10
HELIX 8 8 LEU A 202 LYS A 215 1 14
HELIX 9 9 GLU A 235 MET A 246 5 12
HELIX 10 10 TYR A 263 GLU A 265 5 3
HELIX 11 11 SER A 277 ARG A 292 1 16
HELIX 12 12 ALA A 300 SER A 311 1 12
HELIX 13 13 ASP A 313 LYS A 344 1 32
HELIX 14 14 SER A 351 LYS A 355 5 5
HELIX 15 15 LYS A 367 GLU A 375 1 9
HELIX 16 16 VAL A 389 GLY A 391 5 3
HELIX 17 17 MET A 397 VAL A 408 1 11
HELIX 18 18 LEU B 18 ARG B 25 1 8
HELIX 19 19 THR B 51 ASN B 63 1 13
HELIX 20 20 PRO B 77 PHE B 88 1 12
HELIX 21 21 ALA B 93 ASN B 96 1 4
HELIX 22 22 GLY B 107 ASN B 122 1 16
HELIX 23 23 ASN B 142 ALA B 150 1 9
HELIX 24 24 PHE B 170 GLU B 179 1 10
HELIX 25 25 LEU B 202 LYS B 215 1 14
HELIX 26 26 LEU B 233 ALA B 244 1 12
HELIX 27 27 SER B 277 ARG B 292 1 16
HELIX 28 28 ALA B 300 SER B 311 1 12
HELIX 29 29 ASP B 313 GLU B 343 1 31
HELIX 30 30 SER B 351 LYS B 355 5 5
HELIX 31 31 LYS B 367 GLU B 375 1 9
HELIX 32 32 VAL B 389 GLY B 391 5 3
HELIX 33 33 PRO B 394 ALA B 407 1 13
SHEET 1 A 5 ALA A 100 PRO A 106 0
SHEET 2 A 5 VAL A 267 VAL A 273 -1 N LEU A 272 O ARG A 101
SHEET 3 A 5 LEU A 250 SER A 255 -1 N SER A 254 O ALA A 269
SHEET 4 A 5 LEU A 218 PHE A 223 1 N PHE A 221 O ILE A 251
SHEET 5 A 5 VAL A 185 HIS A 189 1 N VAL A 186 O LEU A 218
SHEET 1 B 2 ARG A 129 ASN A 137 0
SHEET 2 B 2 GLU A 154 ALA A 159 1 N GLU A 154 O VAL A 133
SHEET 1 C 2 PHE A 360 PHE A 362 0
SHEET 2 C 2 ALA A 386 ASN A 388 -1 N VAL A 387 O SER A 361
SHEET 1 D 5 ALA B 100 PRO B 106 0
SHEET 2 D 5 VAL B 267 VAL B 273 -1 N LEU B 272 O ARG B 101
SHEET 3 D 5 LEU B 250 SER B 255 -1 N SER B 254 O ALA B 269
SHEET 4 D 5 LEU B 218 PHE B 223 1 N PRO B 219 O ILE B 251
SHEET 5 D 5 VAL B 185 HIS B 189 1 N VAL B 186 O LEU B 218
SHEET 1 E 2 ARG B 129 ASN B 137 0
SHEET 2 E 2 GLU B 154 ALA B 159 1 N GLU B 154 O VAL B 133
SHEET 1 F 2 PHE B 360 PHE B 362 0
SHEET 2 F 2 ALA B 386 ASN B 388 -1 N VAL B 387 O SER B 361
CISPEP 1 ASN A 137 PRO A 138 0 1.83
CISPEP 2 ASN A 194 PRO A 195 0 11.82
CISPEP 3 ASN B 137 PRO B 138 0 4.30
CISPEP 4 ASN B 194 PRO B 195 0 11.43
SITE 1 ACT 24 ASP A 15 ILE A 17 LEU A 18 ILE A 37
SITE 2 ACT 24 GLY A 38 VAL A 39 TYR B 70 GLY A 107
SITE 3 ACT 24 GLY A 108 THR A 109 TRP A 140 ASN A 194
SITE 4 ACT 24 ASP A 222 ALA A 224 ARG A 225 SER A 255
SITE 5 ACT 24 LYS A 258 ARG A 266 ARG B 292 SER B 296
SITE 6 ACT 24 ASN B 297 PHE A 360 ALA A 386 PPD A 411
SITE 1 BCT 24 ASP B 15 ILE B 17 LEU B 18 ILE B 37
SITE 2 BCT 24 GLY B 38 VAL B 39 TYR A 70 GLY B 107
SITE 3 BCT 24 GLY B 108 THR B 109 TRP B 140 ASN B 194
SITE 4 BCT 24 ASP B 222 ALA B 224 ARG B 225 SER B 255
SITE 5 BCT 24 LYS B 258 ARG B 266 ARG A 292 SER A 296
SITE 6 BCT 24 ASN A 297 PHE B 360 ALA B 386 PPD B 411
SITE 1 AC1 17 ILE A 37 GLY A 38 GLY A 108 THR A 109
SITE 2 AC1 17 TRP A 140 ASN A 194 ASP A 222 ARG A 225
SITE 3 AC1 17 SER A 255 SER A 257 LYS A 258 ARG A 266
SITE 4 AC1 17 PHE A 360 HOH A 443 TYR B 70 ARG B 292
SITE 5 AC1 17 HOH B 413
SITE 1 AC2 18 TYR A 70 ARG A 292 ILE B 17 GLY B 38
SITE 2 AC2 18 GLY B 108 THR B 109 TRP B 140 ASN B 194
SITE 3 AC2 18 ASP B 222 ARG B 225 SER B 255 SER B 257
SITE 4 AC2 18 LYS B 258 ARG B 266 PHE B 360 HOH B 424
SITE 5 AC2 18 HOH B 450 HOH B 590
CRYST1 84.120 79.610 89.850 90.00 117.91 90.00 P 1 21 1 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 0.011888 0.000000 0.006297 0.00000
SCALE2 0.000000 0.012561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012595 0.00000
MTRIX1 1 -1.000000 -0.002240 -0.002100 0.19615 1
MTRIX2 1 0.002250 -1.000000 -0.001590 83.07156 1
MTRIX3 1 -0.002100 -0.001590 1.000000 0.07188 1
(ATOM LINES ARE NOT SHOWN.)
END
