HEADER TRANSFERASE 19-OCT-10 3PA9
TITLE MECHANISM OF INACTIVATION OF E. COLI ASPARTATE AMINOTRANSFERASE BY
TITLE 2 (S)-4-AMINO-4,5-DIHYDRO-2-FURANCARBOXYLIC ACID (S-ADFA) PH 7.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE AMINOTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.6.1.1;
COMPND 5 ENGINEERED: 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 PLP, PMP, SADFA, CATALYTIC LYSINE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.LIU,E.POZHARSKI,M.FU,R.B.SILVERMAN,D.RINGE
REVDAT 4 06-SEP-23 3PA9 1 REMARK SHEET
REVDAT 3 17-JUL-19 3PA9 1 REMARK LINK
REVDAT 2 11-MAY-11 3PA9 1 JRNL
REVDAT 1 01-DEC-10 3PA9 0
JRNL AUTH D.LIU,E.POZHARSKI,M.FU,R.B.SILVERMAN,D.RINGE
JRNL TITL MECHANISM OF INACTIVATION OF ESCHERICHIA COLI ASPARTATE
JRNL TITL 2 AMINOTRANSFERASE BY
JRNL TITL 3 (S)-4-AMINO-4,5-DIHYDRO-2-FURANCARBOXYLIC ACID .
JRNL REF BIOCHEMISTRY V. 49 10507 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 21033689
JRNL DOI 10.1021/BI101325Z
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 53395
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2851
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3775
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 206
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3069
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.59000
REMARK 3 B22 (A**2) : 0.55000
REMARK 3 B33 (A**2) : 0.04000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.485
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3580 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4898 ; 1.269 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 482 ; 5.600 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 174 ;34.140 ;24.253
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 612 ;13.484 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;16.314 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 536 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2755 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1852 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2444 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 380 ; 0.128 ; 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): 140 ; 0.194 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 43 ; 0.121 ; 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): 2186 ; 0.974 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3474 ; 1.543 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1543 ; 2.445 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1381 ; 3.552 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3PA9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-OCT-10.
REMARK 100 THE DEPOSITION ID IS D_1000062152.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67102
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 77.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1AMQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 297K
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 39.51650
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 39.51650
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 77.06750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.76600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 77.06750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.76600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.51650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 77.06750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.76600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 39.51650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 77.06750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.76600
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 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: 14210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.0 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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 SER A 245 C LYS A 246 N 0.140
REMARK 500 LYS A 246 C ASN A 247 N 0.207
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 LEU A 14 133.66 66.90
REMARK 500 THR A 43 72.39 -116.75
REMARK 500 TYR A 149 -52.97 -148.57
REMARK 500 ALA A 218 -74.74 -95.89
REMARK 500 ALA A 218 -74.74 -87.48
REMARK 500 ARG A 254 74.81 65.61
REMARK 500 ASN A 282 -74.83 -110.42
REMARK 500 SER A 284 -57.75 78.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE STARTING INACTIVATOR MOLECULE (S)-4-AMINO-4,5-DYHIDRO-2-
REMARK 600 FURANCARBOXYLIC ACID (S-ADFA) UNDERGOES A CHEMICAL TRANSFORMATION
REMARK 600 BY IRREVERSIBLY BINDING TO THE ACTIVE SITE RESIDUE K246 OF ASPC.
REMARK 600 THE LIGAND PJ7 REPRESENTS FINAL PRODUCT
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PJ7 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 397
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 399
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 411
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PAA RELATED DB: PDB
DBREF 3PA9 A 1 396 UNP D3H0F7 D3H0F7_ECO44 1 396
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 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 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
HET PJ7 A 500 16
HET PMP A 600 16
HET GOL A 397 6
HET GOL A 398 6
HET GOL A 399 12
HET GOL A 400 6
HET GOL A 401 12
HET GOL A 402 6
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET GOL A 406 6
HET GOL A 407 6
HET SO4 A 408 5
HET SO4 A 409 5
HET SO4 A 410 5
HET SO4 A 411 5
HETNAM PJ7 4-AMINOFURAN-2-CARBOXYLIC ACID
HETNAM PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN PMP PYRIDOXAMINE-5'-PHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 PJ7 C5 H5 N O3
FORMUL 3 PMP C8 H13 N2 O5 P
FORMUL 4 GOL 11(C3 H8 O3)
FORMUL 15 SO4 4(O4 S 2-)
FORMUL 19 HOH *420(H2 O)
HELIX 1 1 GLY A 15 ASP A 23 1 9
HELIX 2 2 LEU A 46 GLU A 60 1 15
HELIX 3 3 ILE A 71 GLY A 84 1 14
HELIX 4 4 SER A 87 ASP A 92 1 6
HELIX 5 5 PRO A 101 THR A 118 1 18
HELIX 6 6 PRO A 131 ALA A 140 1 10
HELIX 7 7 ASP A 158 ASN A 167 1 10
HELIX 8 8 THR A 190 GLY A 205 1 16
HELIX 9 9 GLY A 220 ALA A 225 1 6
HELIX 10 10 ALA A 225 HIS A 235 1 11
HELIX 11 11 LEU A 250 ARG A 254 5 5
HELIX 12 12 ASP A 264 ALA A 281 1 18
HELIX 13 13 PRO A 287 SER A 299 1 13
HELIX 14 14 ASN A 300 LYS A 332 1 33
HELIX 15 15 SER A 339 GLN A 344 1 6
HELIX 16 16 THR A 354 GLY A 366 1 13
HELIX 17 17 ALA A 378 MET A 380 5 3
HELIX 18 18 THR A 381 LEU A 396 1 16
SHEET 1 A 2 ILE A 29 ASN A 30 0
SHEET 2 A 2 VAL A 367 TYR A 368 1 O TYR A 368 N ILE A 29
SHEET 1 B 6 ALA A 95 THR A 100 0
SHEET 2 B 6 GLY A 256 VAL A 261 -1 O LEU A 260 N ARG A 96
SHEET 3 B 6 LEU A 207 PHE A 212 1 N PHE A 210 O ALA A 241
SHEET 4 B 6 VAL A 174 HIS A 178 1 N PHE A 177 O ASP A 211
SHEET 5 B 6 ARG A 122 ASN A 127 1 N TRP A 124 O LEU A 176
SHEET 6 B 6 GLU A 143 ALA A 148 1 O GLU A 143 N VAL A 123
SHEET 1 C 2 TYR A 150 ASP A 151 0
SHEET 2 C 2 THR A 156 LEU A 157 -1 O THR A 156 N ASP A 151
SHEET 1 D 2 PHE A 348 PHE A 350 0
SHEET 2 D 2 ARG A 374 ASN A 376 -1 O VAL A 375 N SER A 349
LINK NZ LYS A 246 C5 APJ7 A 500 1555 1555 1.37
LINK NZ LYS A 246 C5 BPJ7 A 500 1555 1555 1.36
CISPEP 1 ASN A 127 PRO A 128 0 5.08
CISPEP 2 ASN A 183 PRO A 184 0 15.05
SITE 1 AC1 12 GLY A 34 TYR A 65 TRP A 130 ASN A 183
SITE 2 AC1 12 TYR A 214 LYS A 246 ARG A 280 PHE A 348
SITE 3 AC1 12 ARG A 374 GOL A 400 HOH A 436 PMP A 600
SITE 1 AC2 15 TYR A 65 GLY A 102 GLY A 103 THR A 104
SITE 2 AC2 15 TRP A 130 ASN A 183 ASP A 211 TYR A 214
SITE 3 AC2 15 SER A 243 SER A 245 LYS A 246 ARG A 254
SITE 4 AC2 15 HOH A 436 PJ7 A 500 HOH A 773
SITE 1 AC3 6 ASN A 138 GLY A 141 SO4 A 411 HOH A 655
SITE 2 AC3 6 HOH A 657 HOH A 808
SITE 1 AC4 8 ILE A 68 ALA A 277 ARG A 280 HOH A 480
SITE 2 AC4 8 HOH A 511 HOH A 532 HOH A 674 HOH A 791
SITE 1 AC5 5 ARG A 315 GLN A 316 GLN A 319 ARG A 320
SITE 2 AC5 5 HOH A 778
SITE 1 AC6 9 ILE A 13 TYR A 65 ARG A 280 ASN A 285
SITE 2 AC6 9 HOH A 448 HOH A 471 PJ7 A 500 HOH A 507
SITE 3 AC6 9 HOH A 547
SITE 1 AC7 10 GLY A 216 GLY A 220 LEU A 221 GLU A 308
SITE 2 AC7 10 LEU A 311 THR A 312 ARG A 315 GOL A 406
SITE 3 AC7 10 HOH A 564 HOH A 709
SITE 1 AC8 10 PRO A 72 GLY A 75 ARG A 76 GLN A 79
SITE 2 AC8 10 ALA A 95 ARG A 96 THR A 97 HOH A 422
SITE 3 AC8 10 HOH A 726 HOH A 815
SITE 1 AC9 6 ASN A 4 SER A 372 HOH A 549 HOH A 587
SITE 2 AC9 6 HOH A 696 HOH A 715
SITE 1 BC1 5 TYR A 55 ASN A 300 HOH A 415 HOH A 536
SITE 2 BC1 5 HOH A 665
SITE 1 BC2 9 PRO A 189 THR A 190 LEU A 191 ARG A 219
SITE 2 BC2 9 ASN A 345 GOL A 407 HOH A 426 HOH A 631
SITE 3 BC2 9 HOH A 769
SITE 1 BC3 7 GLY A 220 LEU A 221 GLU A 222 GLU A 223
SITE 2 BC3 7 GOL A 401 HOH A 685 HOH A 709
SITE 1 BC4 10 ASP A 188 PRO A 189 THR A 190 ARG A 219
SITE 2 BC4 10 ASN A 345 GOL A 405 HOH A 426 HOH A 591
SITE 3 BC4 10 HOH A 631 HOH A 828
SITE 1 BC5 3 PRO A 72 ARG A 76 HOH A 438
SITE 1 BC6 2 ARG A 122 ARG A 360
SITE 1 BC7 4 ARG A 96 LYS A 276 HOH A 479 HOH A 557
SITE 1 BC8 7 LYS A 134 ASN A 138 GLU A 143 VAL A 144
SITE 2 BC8 7 ARG A 145 GOL A 397 HOH A 655
CRYST1 154.135 85.532 79.033 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 0.006488 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011692 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012653 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
