HEADER TRANSFERASE(AMINOTRANSFERASE) 10-MAY-94 1AIA
TITLE STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE
TITLE 2 AMINOTRANSFERASE K258H LACKING THE PYRIDOXAL-5'-PHOSPHATE BINDING
TITLE 3 LYSINE RESIDUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE AMINOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.6.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE(AMINOTRANSFERASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR J.JAEGER,J.N.JANSONIUS
REVDAT 4 07-FEB-24 1AIA 1 REMARK SEQADV
REVDAT 3 25-JUL-12 1AIA 1 COMPND SEQADV VERSN
REVDAT 2 24-FEB-09 1AIA 1 VERSN
REVDAT 1 15-OCT-94 1AIA 0
JRNL AUTH V.N.MALASHKEVICH,J.JAGER,M.ZIAK,U.SAUDER,H.GEHRING,
JRNL AUTH 2 P.CHRISTEN,J.N.JANSONIUS
JRNL TITL STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE
JRNL TITL 2 AMINOTRANSFERASE K258H LACKING THE PYRIDOXAL
JRNL TITL 3 5'-PHOSPHATE-BINDING LYSINE RESIDUE.
JRNL REF BIOCHEMISTRY V. 34 405 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7819232
JRNL DOI 10.1021/BI00002A004
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 49125
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.210
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 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6140
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 3.020
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AIA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
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 : NULL
REMARK 200 R MERGE (I) : NULL
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 39.90000
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: THE ASYMMETRIC UNIT CONTAINS A DIMER OF ASPARTATE
REMARK 300 AMINOTRANSFERASE.
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: 7380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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: 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 143 NE2 HIS A 143 CD2 -0.074
REMARK 500 HIS A 193 NE2 HIS A 193 CD2 -0.072
REMARK 500 HIS A 258 NE2 HIS A 258 CD2 -0.072
REMARK 500 HIS A 301 NE2 HIS A 301 CD2 -0.066
REMARK 500 HIS B 143 NE2 HIS B 143 CD2 -0.083
REMARK 500 HIS B 166 NE2 HIS B 166 CD2 -0.072
REMARK 500 TRP B 217 CG TRP B 217 CD2 -0.103
REMARK 500 HIS B 258 NE2 HIS B 258 CD2 -0.078
REMARK 500 HIS B 301 NE2 HIS B 301 CD2 -0.069
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 ASN A 8 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 ALA A 11 N - CA - C ANGL. DEV. = 17.3 DEGREES
REMARK 500 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 VAL A 39 N - CA - CB ANGL. DEV. = -14.5 DEGREES
REMARK 500 LYS A 41 N - CA - CB ANGL. DEV. = -12.3 DEGREES
REMARK 500 LYS A 41 CB - CG - CD ANGL. DEV. = -20.4 DEGREES
REMARK 500 TYR A 59 CB - CG - CD1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 81 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 129 CB - CG - CD ANGL. DEV. = -20.2 DEGREES
REMARK 500 ARG A 129 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TRP A 134 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 TRP A 140 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 140 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 TYR A 161 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP A 169 CA - C - N ANGL. DEV. = -17.9 DEGREES
REMARK 500 ASN A 178 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 TRP A 205 CD1 - CG - CD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TRP A 205 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 TRP A 217 CD1 - CG - CD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 TRP A 217 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 TRP A 217 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 GLU A 238 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG A 241 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LEU A 250 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ARG A 266 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 266 NE - CZ - NH2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 LEU A 272 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 VAL A 280 CB - CA - C ANGL. DEV. = -13.8 DEGREES
REMARK 500 TRP A 319 CD1 - CG - CD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 TRP A 319 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 319 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 319 CG - CD2 - CE3 ANGL. DEV. = 6.1 DEGREES
REMARK 500 GLN A 328 CA - CB - CG ANGL. DEV. = -14.8 DEGREES
REMARK 500 ARG A 329 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 329 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG A 334 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 334 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ALA A 346 CA - C - N ANGL. DEV. = -17.5 DEGREES
REMARK 500 ASN A 347 N - CA - CB ANGL. DEV. = -12.7 DEGREES
REMARK 500 LYS A 355 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 THR A 366 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 THR A 366 CA - CB - CG2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 VAL B 39 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 LYS B 68 CA - CB - CG ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG B 81 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 THR B 105 N - CA - CB ANGL. DEV. = -13.8 DEGREES
REMARK 500 TRP B 140 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP B 140 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 77 ANGLE DEVIATIONS.
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 12 121.58 62.38
REMARK 500 ALA A 26 4.80 -69.09
REMARK 500 GLU A 28 48.06 33.06
REMARK 500 PRO A 30 -104.96 -32.83
REMARK 500 TYR A 160 -46.00 -152.62
REMARK 500 GLU A 179 -95.46 65.98
REMARK 500 ALA A 180 60.08 31.82
REMARK 500 GLN A 181 151.26 -14.70
REMARK 500 ALA A 229 -65.61 -103.07
REMARK 500 LEU A 250 146.08 -170.73
REMARK 500 ARG A 266 76.93 62.74
REMARK 500 ASN A 294 -75.72 -116.33
REMARK 500 SER A 296 -55.08 76.82
REMARK 500 PHE B 6 -27.13 69.67
REMARK 500 ALA B 26 -22.21 -177.78
REMARK 500 GLU B 28 57.48 26.46
REMARK 500 PRO B 30 -77.35 -71.41
REMARK 500 PRO B 106 79.40 -68.99
REMARK 500 TYR B 160 -52.04 -148.81
REMARK 500 ARG B 230 -68.19 61.42
REMARK 500 ARG B 266 81.15 59.19
REMARK 500 ASN B 294 -74.06 -105.65
REMARK 500 SER B 296 -63.37 71.88
REMARK 500 PHE B 377 138.42 97.18
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 ARG B 29 PRO B 30 -143.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: ACB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP B 411
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RESIDUE NUMBERING USED IN THIS ENTRY CONFORMS TO THE
REMARK 999 AMINO ACID SEQUENCE OF THE CHICKEN CYTOSOLIC ISOENZYME.
REMARK 999 HENCE, THE RESIDUE NUMBERING STARTS WITH MET 5 AND RESIDUES
REMARK 999 127, 128, 130, 131, 132, 153, 232 AND 406 OF BOTH CHAINS
REMARK 999 HAVE NOT BEEN INCLUDED.
DBREF 1AIA A 5 409 UNP P00509 AAT_ECOLI 1 396
DBREF 1AIA B 5 409 UNP P00509 AAT_ECOLI 1 396
SEQADV 1AIA HIS A 258 UNP P00509 LYS 246 ENGINEERED MUTATION
SEQADV 1AIA HIS B 258 UNP P00509 LYS 246 ENGINEERED MUTATION
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 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 HIS 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 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
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 TYR 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 HIS 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 ARG 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 PMP A 411 16
HET PMP B 411 16
HETNAM PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
HETSYN PMP PYRIDOXAMINE-5'-PHOSPHATE
FORMUL 3 PMP 2(C8 H13 N2 O5 P)
HELIX 1 A1 PRO A 16 ALA A 26 1 11
HELIX 2 A2 THR A 51 ASN A 63 1 13
HELIX 3 A3 PRO A 77 PHE A 88 1 12
HELIX 4 A4 ALA A 93 ASP A 97 1 5
HELIX 5 A5 GLY A 107 ASN A 122 1 16
HELIX 6 A6 ASN A 142 ALA A 150 1 9
HELIX 7 A7 PHE A 170 LEU A 177 1 8
HELIX 8 A8 LEU A 202 LYS A 215 1 14
HELIX 9 A9 GLU A 238 MET A 246 1 9
HELIX 10 A11 SER A 277 ASN A 294 1 18
HELIX 11 A12 ALA A 300 SER A 311 1 12
HELIX 12 A13 ASP A 313 GLU A 343 1 31
HELIX 13 A14 SER A 351 LYS A 355 1 5
HELIX 14 A15 LYS A 367 PHE A 377 1 11
HELIX 15 A16 ASP A 395 ALA A 407 1 12
HELIX 16 B1 PRO B 16 ALA B 26 1 11
HELIX 17 B2 THR B 51 ASN B 63 1 13
HELIX 18 B3 PRO B 77 PHE B 88 1 12
HELIX 19 B4 ALA B 93 ASP B 97 1 5
HELIX 20 B5 GLY B 107 ASN B 122 1 16
HELIX 21 B6 ASN B 142 ALA B 150 1 9
HELIX 22 B7 PHE B 170 LEU B 177 1 8
HELIX 23 B8 LEU B 202 LYS B 215 1 14
HELIX 24 B9 GLU B 238 MET B 246 1 9
HELIX 25 B11 SER B 277 ASN B 294 1 18
HELIX 26 B12 ALA B 300 SER B 311 1 12
HELIX 27 B13 ASP B 313 GLU B 343 1 31
HELIX 28 B14 SER B 351 LYS B 355 1 5
HELIX 29 B15 LYS B 367 PHE B 377 1 11
HELIX 30 B16 ASP B 395 ALA B 407 1 12
SHEET 1 S1A 7 ALA A 100 PRO A 106 0
SHEET 2 S1A 7 VAL A 267 VAL A 273 -1
SHEET 3 S1A 7 LEU A 250 SER A 255 -1
SHEET 4 S1A 7 LEU A 218 PHE A 223 1
SHEET 5 S1A 7 VAL A 185 HIS A 189 1
SHEET 6 S1A 7 ARG A 129 ASN A 137 1
SHEET 7 S1A 7 GLU A 154 ALA A 159 1
SHEET 1 S2A 2 ILE A 33 LEU A 35 0
SHEET 2 S2A 2 GLY A 378 TYR A 380 1
SHEET 1 S3A 2 MET A 359 PHE A 362 0
SHEET 2 S3A 2 ARG A 386 VAL A 389 -1
SHEET 1 S1B 7 ALA B 100 PRO B 106 0
SHEET 2 S1B 7 VAL B 267 VAL B 273 -1
SHEET 3 S1B 7 LEU B 250 SER B 255 -1
SHEET 4 S1B 7 LEU B 218 PHE B 223 1
SHEET 5 S1B 7 VAL B 185 HIS B 189 1
SHEET 6 S1B 7 ARG B 129 ASN B 137 1
SHEET 7 S1B 7 GLU B 154 ALA B 159 1
SHEET 1 S2B 2 ILE B 33 LEU B 35 0
SHEET 2 S2B 2 GLY B 378 TYR B 380 1
SHEET 1 S3B 2 MET B 359 PHE B 362 0
SHEET 2 S3B 2 ARG B 386 VAL B 389 -1
CISPEP 1 ASN A 137 PRO A 138 0 -5.84
CISPEP 2 ASN A 194 PRO A 195 0 13.48
CISPEP 3 ASN B 137 PRO B 138 0 -6.91
CISPEP 4 ASN B 194 PRO B 195 0 13.21
SITE 1 ACA 3 HIS A 258 ARG B 292 ARG A 386
SITE 1 ACB 3 HIS B 258 ARG A 292 ARG B 386
SITE 1 AC1 12 GLY A 107 GLY A 108 THR A 109 TRP A 140
SITE 2 AC1 12 ASN A 194 ASP A 222 TYR A 225 SER A 255
SITE 3 AC1 12 SER A 257 HIS A 258 ARG A 266 TYR B 70
SITE 1 AC2 11 TYR A 70 GLY B 108 THR B 109 TRP B 140
SITE 2 AC2 11 ASN B 194 ASP B 222 TYR B 225 SER B 255
SITE 3 AC2 11 SER B 257 HIS B 258 ARG B 266
CRYST1 86.900 79.800 89.900 90.00 118.90 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 0.011507 0.000000 0.006352 0.00000
SCALE2 0.000000 0.012531 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012706 0.00000
MTRIX1 1 -0.999990 -0.000640 -0.000150 0.04040 1
MTRIX2 1 0.000640 -0.999990 -0.001160 83.69090 1
MTRIX3 1 -0.000150 -0.000150 0.999999 0.07640 1
(ATOM LINES ARE NOT SHOWN.)
END