HEADER LYASE 11-JUN-03 1PMM
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB (LOW PH)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: GAD-BETA;
COMPND 5 EC: 4.1.1.15;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: GADB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS LOW-PH FORM OF GADB, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.CAPITANI,D.DE BIASE,C.AURIZI,H.GUT,F.BOSSA,M.G.GRUTTER
REVDAT 3 13-JUL-11 1PMM 1 VERSN
REVDAT 2 24-FEB-09 1PMM 1 VERSN
REVDAT 1 17-FEB-04 1PMM 0
JRNL AUTH G.CAPITANI,D.DE BIASE,C.AURIZI,H.GUT,F.BOSSA,M.G.GRUTTER
JRNL TITL CRYSTAL STRUCTURE AND FUNCTIONAL ANALYSIS OF ESCHERICHIA
JRNL TITL 2 COLI GLUTAMATE DECARBOXYLASE
JRNL REF EMBO J. V. 22 4027 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12912902
JRNL DOI 10.1093/EMBOJ/CDG403
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 178480
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 SET) : 0.182
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5238
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE : 0.1870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148
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 : 21444
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 114
REMARK 3 SOLVENT ATOMS : 1842
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.37700
REMARK 3 B22 (A**2) : -0.37600
REMARK 3 B33 (A**2) : -0.12400
REMARK 3 B12 (A**2) : 0.50600
REMARK 3 B13 (A**2) : -0.25300
REMARK 3 B23 (A**2) : -0.34900
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.23
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.75
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1PMM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-03.
REMARK 100 THE RCSB ID CODE IS RCSB019428.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 178481
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 24.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.16200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, SODIUM ACETATE, PEG
REMARK 280 4000, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 HEXAMER
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 48750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 86180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -209.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 LYS A 453
REMARK 465 LEU A 454
REMARK 465 GLN A 455
REMARK 465 GLY A 456
REMARK 465 ILE A 457
REMARK 465 ALA A 458
REMARK 465 GLN A 459
REMARK 465 GLN A 460
REMARK 465 ASN A 461
REMARK 465 SER A 462
REMARK 465 PHE A 463
REMARK 465 LYS A 464
REMARK 465 HIS A 465
REMARK 465 THR A 466
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 LYS B 453
REMARK 465 LEU B 454
REMARK 465 GLN B 455
REMARK 465 GLY B 456
REMARK 465 ILE B 457
REMARK 465 ALA B 458
REMARK 465 GLN B 459
REMARK 465 GLN B 460
REMARK 465 ASN B 461
REMARK 465 SER B 462
REMARK 465 PHE B 463
REMARK 465 LYS B 464
REMARK 465 HIS B 465
REMARK 465 THR B 466
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 LYS C 3
REMARK 465 LYS C 453
REMARK 465 LEU C 454
REMARK 465 GLN C 455
REMARK 465 GLY C 456
REMARK 465 ILE C 457
REMARK 465 ALA C 458
REMARK 465 GLN C 459
REMARK 465 GLN C 460
REMARK 465 ASN C 461
REMARK 465 SER C 462
REMARK 465 PHE C 463
REMARK 465 LYS C 464
REMARK 465 HIS C 465
REMARK 465 THR C 466
REMARK 465 MET D 1
REMARK 465 ASP D 2
REMARK 465 LYS D 453
REMARK 465 LEU D 454
REMARK 465 GLN D 455
REMARK 465 GLY D 456
REMARK 465 ILE D 457
REMARK 465 ALA D 458
REMARK 465 GLN D 459
REMARK 465 GLN D 460
REMARK 465 ASN D 461
REMARK 465 SER D 462
REMARK 465 PHE D 463
REMARK 465 LYS D 464
REMARK 465 HIS D 465
REMARK 465 THR D 466
REMARK 465 MET E 1
REMARK 465 ASP E 2
REMARK 465 LYS E 3
REMARK 465 LYS E 453
REMARK 465 LEU E 454
REMARK 465 GLN E 455
REMARK 465 GLY E 456
REMARK 465 ILE E 457
REMARK 465 ALA E 458
REMARK 465 GLN E 459
REMARK 465 GLN E 460
REMARK 465 ASN E 461
REMARK 465 SER E 462
REMARK 465 PHE E 463
REMARK 465 LYS E 464
REMARK 465 HIS E 465
REMARK 465 THR E 466
REMARK 465 MET F 1
REMARK 465 ASP F 2
REMARK 465 LYS F 453
REMARK 465 LEU F 454
REMARK 465 GLN F 455
REMARK 465 GLY F 456
REMARK 465 ILE F 457
REMARK 465 ALA F 458
REMARK 465 GLN F 459
REMARK 465 GLN F 460
REMARK 465 ASN F 461
REMARK 465 SER F 462
REMARK 465 PHE F 463
REMARK 465 LYS F 464
REMARK 465 HIS F 465
REMARK 465 THR F 466
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 244 42.50 -107.37
REMARK 500 LEU A 250 -62.56 -121.84
REMARK 500 ALA A 255 58.03 -150.71
REMARK 500 ASP A 261 -147.02 -98.39
REMARK 500 LYS A 276 -114.14 -102.21
REMARK 500 TYR A 305 111.06 -160.41
REMARK 500 PHE A 317 -99.20 -116.47
REMARK 500 SER B 29 -0.94 -141.88
REMARK 500 GLN B 186 77.30 -154.32
REMARK 500 LEU B 187 41.68 -88.93
REMARK 500 ALA B 244 40.78 -106.56
REMARK 500 LEU B 250 -66.50 -124.07
REMARK 500 ALA B 255 60.07 -151.03
REMARK 500 ASP B 261 -144.23 -102.36
REMARK 500 LYS B 276 -115.18 -101.68
REMARK 500 PHE B 317 -99.30 -119.20
REMARK 500 PHE B 429 64.39 -119.11
REMARK 500 SER C 29 -1.92 -142.62
REMARK 500 LEU C 187 48.83 -89.00
REMARK 500 LEU C 250 -64.96 -120.94
REMARK 500 ASP C 261 -144.96 -97.50
REMARK 500 LYS C 276 -111.94 -100.03
REMARK 500 PHE C 317 -101.23 -116.01
REMARK 500 PHE C 429 69.26 -111.45
REMARK 500 LEU D 187 42.12 -87.60
REMARK 500 ALA D 244 40.69 -104.75
REMARK 500 LEU D 250 -66.27 -125.76
REMARK 500 ALA D 255 59.13 -148.90
REMARK 500 ASP D 261 -143.17 -100.56
REMARK 500 LYS D 276 -113.52 -98.84
REMARK 500 TYR D 305 107.51 -163.86
REMARK 500 PHE D 317 -97.68 -117.63
REMARK 500 HIS D 451 63.97 -151.12
REMARK 500 SER E 29 -4.43 -142.40
REMARK 500 LEU E 187 44.61 -84.49
REMARK 500 ALA E 255 60.42 -154.38
REMARK 500 ASP E 261 -145.45 -95.82
REMARK 500 LYS E 276 -111.33 -100.67
REMARK 500 PHE E 317 -98.79 -117.25
REMARK 500 PHE E 429 66.77 -118.17
REMARK 500 LEU F 187 46.57 -86.56
REMARK 500 LEU F 250 -65.02 -123.07
REMARK 500 ASP F 261 -147.06 -101.59
REMARK 500 LYS F 276 -115.51 -99.69
REMARK 500 PHE F 317 -99.84 -119.70
REMARK 500 PHE F 429 68.68 -117.07
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 A5675 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH A5730 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH B6817 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH C8766 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH D7759 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH D7811 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH D7837 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH D7848 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH E9716 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH F 699 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH F 775 DISTANCE = 5.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 5518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 6518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY D 7518
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 8518
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY E 9518
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY E 9519
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PMO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT NEUTRAL PH
DBREF 1PMM A 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 1PMM B 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 1PMM C 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 1PMM D 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 1PMM E 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 1PMM F 1 466 UNP P69910 DCEB_ECOLI 1 466
SEQRES 1 A 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 A 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 A 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 A 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 A 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 A 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 A 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 A 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 A 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 A 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 A 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 A 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 A 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 A 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 A 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 A 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 A 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 A 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 A 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 A 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 A 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 A 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 A 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 A 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 A 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 A 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 A 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 A 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 A 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 A 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 A 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 A 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 A 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 A 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 A 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 A 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 B 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 B 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 B 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 B 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 B 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 B 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 B 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 B 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 B 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 B 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 B 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 B 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 B 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 B 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 B 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 B 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 B 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 B 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 B 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 B 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 B 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 B 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 B 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 B 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 B 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 B 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 B 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 B 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 B 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 B 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 B 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 B 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 B 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 B 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 B 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 B 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 C 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 C 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 C 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 C 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 C 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 C 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 C 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 C 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 C 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 C 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 C 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 C 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 C 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 C 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 C 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 C 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 C 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 C 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 C 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 C 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 C 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 C 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 C 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 C 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 C 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 C 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 C 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 C 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 C 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 C 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 C 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 C 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 C 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 C 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 C 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 C 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 D 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 D 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 D 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 D 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 D 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 D 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 D 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 D 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 D 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 D 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 D 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 D 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 D 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 D 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 D 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 D 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 D 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 D 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 D 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 D 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 D 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 D 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 D 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 D 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 D 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 D 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 D 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 D 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 D 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 D 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 D 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 D 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 D 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 D 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 D 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 D 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 E 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 E 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 E 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 E 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 E 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 E 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 E 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 E 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 E 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 E 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 E 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 E 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 E 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 E 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 E 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 E 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 E 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 E 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 E 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 E 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 E 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 E 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 E 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 E 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 E 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 E 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 E 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 E 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 E 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 E 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 E 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 E 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 E 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 E 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 E 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 E 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
SEQRES 1 F 466 MET ASP LYS LYS GLN VAL THR ASP LEU ARG SER GLU LEU
SEQRES 2 F 466 LEU ASP SER ARG PHE GLY ALA LYS SER ILE SER THR ILE
SEQRES 3 F 466 ALA GLU SER LYS ARG PHE PRO LEU HIS GLU MET ARG ASP
SEQRES 4 F 466 ASP VAL ALA PHE GLN ILE ILE ASN ASP GLU LEU TYR LEU
SEQRES 5 F 466 ASP GLY ASN ALA ARG GLN ASN LEU ALA THR PHE CYS GLN
SEQRES 6 F 466 THR TRP ASP ASP GLU ASN VAL HIS LYS LEU MET ASP LEU
SEQRES 7 F 466 SER ILE ASN LYS ASN TRP ILE ASP LYS GLU GLU TYR PRO
SEQRES 8 F 466 GLN SER ALA ALA ILE ASP LEU ARG CYS VAL ASN MET VAL
SEQRES 9 F 466 ALA ASP LEU TRP HIS ALA PRO ALA PRO LYS ASN GLY GLN
SEQRES 10 F 466 ALA VAL GLY THR ASN THR ILE GLY SER SER GLU ALA CYS
SEQRES 11 F 466 MET LEU GLY GLY MET ALA MET LYS TRP ARG TRP ARG LYS
SEQRES 12 F 466 ARG MET GLU ALA ALA GLY LYS PRO THR ASP LYS PRO ASN
SEQRES 13 F 466 LEU VAL CYS GLY PRO VAL GLN ILE CYS TRP HIS LYS PHE
SEQRES 14 F 466 ALA ARG TYR TRP ASP VAL GLU LEU ARG GLU ILE PRO MET
SEQRES 15 F 466 ARG PRO GLY GLN LEU PHE MET ASP PRO LYS ARG MET ILE
SEQRES 16 F 466 GLU ALA CYS ASP GLU ASN THR ILE GLY VAL VAL PRO THR
SEQRES 17 F 466 PHE GLY VAL THR TYR THR GLY ASN TYR GLU PHE PRO GLN
SEQRES 18 F 466 PRO LEU HIS ASP ALA LEU ASP LYS PHE GLN ALA ASP THR
SEQRES 19 F 466 GLY ILE ASP ILE ASP MET HIS ILE ASP ALA ALA SER GLY
SEQRES 20 F 466 GLY PHE LEU ALA PRO PHE VAL ALA PRO ASP ILE VAL TRP
SEQRES 21 F 466 ASP PHE ARG LEU PRO ARG VAL LYS SER ILE SER ALA SER
SEQRES 22 F 466 GLY HIS LYS PHE GLY LEU ALA PRO LEU GLY CYS GLY TRP
SEQRES 23 F 466 VAL ILE TRP ARG ASP GLU GLU ALA LEU PRO GLN GLU LEU
SEQRES 24 F 466 VAL PHE ASN VAL ASP TYR LEU GLY GLY GLN ILE GLY THR
SEQRES 25 F 466 PHE ALA ILE ASN PHE SER ARG PRO ALA GLY GLN VAL ILE
SEQRES 26 F 466 ALA GLN TYR TYR GLU PHE LEU ARG LEU GLY ARG GLU GLY
SEQRES 27 F 466 TYR THR LYS VAL GLN ASN ALA SER TYR GLN VAL ALA ALA
SEQRES 28 F 466 TYR LEU ALA ASP GLU ILE ALA LYS LEU GLY PRO TYR GLU
SEQRES 29 F 466 PHE ILE CYS THR GLY ARG PRO ASP GLU GLY ILE PRO ALA
SEQRES 30 F 466 VAL CYS PHE LYS LEU LYS ASP GLY GLU ASP PRO GLY TYR
SEQRES 31 F 466 THR LEU TYR ASP LEU SER GLU ARG LEU ARG LEU ARG GLY
SEQRES 32 F 466 TRP GLN VAL PRO ALA PHE THR LEU GLY GLY GLU ALA THR
SEQRES 33 F 466 ASP ILE VAL VAL MET ARG ILE MET CYS ARG ARG GLY PHE
SEQRES 34 F 466 GLU MET ASP PHE ALA GLU LEU LEU LEU GLU ASP TYR LYS
SEQRES 35 F 466 ALA SER LEU LYS TYR LEU SER ASP HIS PRO LYS LEU GLN
SEQRES 36 F 466 GLY ILE ALA GLN GLN ASN SER PHE LYS HIS THR
HET PLP A 500 15
HET PLP B 500 15
HET PLP C 501 15
HET PLP D 501 15
HET PLP E 502 15
HET PLP F 502 15
HET ACY A5518 4
HET ACY B6518 4
HET ACY D7518 4
HET ACY C8518 4
HET ACY E9518 4
HET ACY E9519 4
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM ACY ACETIC ACID
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 7 PLP 6(C8 H10 N O6 P)
FORMUL 13 ACY 6(C2 H4 O2)
FORMUL 19 HOH *1842(H2 O)
HELIX 1 1 LYS A 3 ASP A 15 1 13
HELIX 2 2 ALA A 20 SER A 24 5 5
HELIX 3 3 ARG A 38 LEU A 50 1 13
HELIX 4 4 TYR A 51 ASP A 53 5 3
HELIX 5 5 ASN A 55 ASN A 59 5 5
HELIX 6 6 ASP A 69 SER A 79 1 11
HELIX 7 7 TYR A 90 TRP A 108 1 19
HELIX 8 8 GLY A 125 GLY A 149 1 25
HELIX 9 9 GLN A 163 TRP A 173 1 11
HELIX 10 10 ASP A 190 CYS A 198 1 9
HELIX 11 11 PHE A 219 GLY A 235 1 17
HELIX 12 12 SER A 246 PHE A 249 5 4
HELIX 13 13 LEU A 250 ALA A 255 1 6
HELIX 14 14 ASP A 291 LEU A 295 5 5
HELIX 15 15 PRO A 296 VAL A 300 5 5
HELIX 16 16 ALA A 321 LYS A 359 1 39
HELIX 17 17 THR A 391 LEU A 401 1 11
HELIX 18 18 GLU A 430 HIS A 451 1 22
HELIX 19 19 LYS B 3 ASP B 15 1 13
HELIX 20 20 ALA B 20 SER B 24 5 5
HELIX 21 21 ARG B 38 LEU B 50 1 13
HELIX 22 22 TYR B 51 ASP B 53 5 3
HELIX 23 23 ASN B 55 ASN B 59 5 5
HELIX 24 24 ASP B 69 SER B 79 1 11
HELIX 25 25 TYR B 90 TRP B 108 1 19
HELIX 26 26 GLY B 125 ALA B 147 1 23
HELIX 27 27 ILE B 164 TRP B 173 1 10
HELIX 28 28 ASP B 190 CYS B 198 1 9
HELIX 29 29 PHE B 219 GLY B 235 1 17
HELIX 30 30 SER B 246 PHE B 249 5 4
HELIX 31 31 LEU B 250 ALA B 255 1 6
HELIX 32 32 ASP B 291 LEU B 295 5 5
HELIX 33 33 PRO B 296 VAL B 300 5 5
HELIX 34 34 ALA B 321 LYS B 359 1 39
HELIX 35 35 THR B 391 LEU B 401 1 11
HELIX 36 36 GLU B 430 HIS B 451 1 22
HELIX 37 37 LYS C 4 ASP C 15 1 12
HELIX 38 38 ALA C 20 SER C 24 5 5
HELIX 39 39 ARG C 38 LEU C 50 1 13
HELIX 40 40 TYR C 51 ASP C 53 5 3
HELIX 41 41 ASN C 55 ASN C 59 5 5
HELIX 42 42 ASP C 69 SER C 79 1 11
HELIX 43 43 TYR C 90 TRP C 108 1 19
HELIX 44 44 GLY C 125 GLY C 149 1 25
HELIX 45 45 ILE C 164 TRP C 173 1 10
HELIX 46 46 ASP C 190 CYS C 198 1 9
HELIX 47 47 PHE C 219 GLY C 235 1 17
HELIX 48 48 SER C 246 PHE C 249 5 4
HELIX 49 49 LEU C 250 ALA C 255 1 6
HELIX 50 50 ASP C 291 LEU C 295 5 5
HELIX 51 51 PRO C 296 VAL C 300 5 5
HELIX 52 52 ALA C 321 LYS C 359 1 39
HELIX 53 53 THR C 391 LEU C 401 1 11
HELIX 54 54 GLY C 412 THR C 416 5 5
HELIX 55 55 GLU C 430 HIS C 451 1 22
HELIX 56 56 LYS D 3 ASP D 15 1 13
HELIX 57 57 ALA D 20 SER D 24 5 5
HELIX 58 58 ARG D 38 LEU D 50 1 13
HELIX 59 59 TYR D 51 ASP D 53 5 3
HELIX 60 60 ASN D 55 ASN D 59 5 5
HELIX 61 61 ASP D 69 SER D 79 1 11
HELIX 62 62 TYR D 90 TRP D 108 1 19
HELIX 63 63 GLY D 125 ALA D 148 1 24
HELIX 64 64 ILE D 164 TRP D 173 1 10
HELIX 65 65 ASP D 190 CYS D 198 1 9
HELIX 66 66 PHE D 219 GLY D 235 1 17
HELIX 67 67 SER D 246 PHE D 249 5 4
HELIX 68 68 LEU D 250 ALA D 255 1 6
HELIX 69 69 ASP D 291 LEU D 295 5 5
HELIX 70 70 PRO D 296 VAL D 300 5 5
HELIX 71 71 ALA D 321 LYS D 359 1 39
HELIX 72 72 THR D 391 LEU D 401 1 11
HELIX 73 73 GLY D 412 THR D 416 5 5
HELIX 74 74 GLU D 430 ASP D 450 1 21
HELIX 75 75 LYS E 4 ASP E 15 1 12
HELIX 76 76 ALA E 20 SER E 24 5 5
HELIX 77 77 ARG E 38 LEU E 50 1 13
HELIX 78 78 TYR E 51 ASP E 53 5 3
HELIX 79 79 ASN E 55 ASN E 59 5 5
HELIX 80 80 ASP E 69 SER E 79 1 11
HELIX 81 81 TYR E 90 TRP E 108 1 19
HELIX 82 82 GLY E 125 GLY E 149 1 25
HELIX 83 83 ILE E 164 TRP E 173 1 10
HELIX 84 84 ASP E 190 CYS E 198 1 9
HELIX 85 85 PHE E 219 GLY E 235 1 17
HELIX 86 86 SER E 246 PHE E 249 5 4
HELIX 87 87 LEU E 250 ALA E 255 1 6
HELIX 88 88 ASP E 291 LEU E 295 5 5
HELIX 89 89 PRO E 296 VAL E 300 5 5
HELIX 90 90 ALA E 321 LYS E 359 1 39
HELIX 91 91 THR E 391 LEU E 401 1 11
HELIX 92 92 GLY E 412 THR E 416 5 5
HELIX 93 93 GLU E 430 ASP E 450 1 21
HELIX 94 94 LYS F 3 ASP F 15 1 13
HELIX 95 95 ALA F 20 SER F 24 5 5
HELIX 96 96 ARG F 38 LEU F 50 1 13
HELIX 97 97 TYR F 51 ASP F 53 5 3
HELIX 98 98 ASN F 55 ASN F 59 5 5
HELIX 99 99 ASP F 69 ILE F 80 1 12
HELIX 100 100 TYR F 90 TRP F 108 1 19
HELIX 101 101 GLY F 125 ALA F 148 1 24
HELIX 102 102 ILE F 164 TRP F 173 1 10
HELIX 103 103 ASP F 190 CYS F 198 1 9
HELIX 104 104 PHE F 219 GLY F 235 1 17
HELIX 105 105 SER F 246 PHE F 249 5 4
HELIX 106 106 LEU F 250 ALA F 255 1 6
HELIX 107 107 ASP F 291 LEU F 295 5 5
HELIX 108 108 PRO F 296 VAL F 300 5 5
HELIX 109 109 ALA F 321 LYS F 359 1 39
HELIX 110 110 THR F 391 ARG F 400 1 10
HELIX 111 111 LEU F 401 GLY F 403 5 3
HELIX 112 112 GLY F 412 THR F 416 5 5
HELIX 113 113 GLU F 430 HIS F 451 1 22
SHEET 1 A 4 GLY A 120 THR A 123 0
SHEET 2 A 4 GLY A 285 TRP A 289 -1 O GLY A 285 N THR A 123
SHEET 3 A 4 VAL A 267 SER A 273 -1 N ALA A 272 O TRP A 286
SHEET 4 A 4 MET A 240 ASP A 243 1 N ILE A 242 O SER A 271
SHEET 1 B 3 GLU A 176 GLU A 179 0
SHEET 2 B 3 ASN A 156 CYS A 159 1 N LEU A 157 O ARG A 178
SHEET 3 B 3 THR A 202 VAL A 206 1 O ILE A 203 N ASN A 156
SHEET 1 C 2 PHE A 301 TYR A 305 0
SHEET 2 C 2 GLY A 308 THR A 312 -1 O THR A 312 N PHE A 301
SHEET 1 D 4 TYR A 363 THR A 368 0
SHEET 2 D 4 ALA A 377 LEU A 382 -1 O LYS A 381 N GLU A 364
SHEET 3 D 4 VAL A 419 MET A 424 -1 O ILE A 423 N VAL A 378
SHEET 4 D 4 ALA A 408 THR A 410 -1 N PHE A 409 O VAL A 420
SHEET 1 E 4 GLY B 120 THR B 123 0
SHEET 2 E 4 GLY B 285 TRP B 289 -1 O GLY B 285 N THR B 123
SHEET 3 E 4 VAL B 267 SER B 273 -1 N ALA B 272 O TRP B 286
SHEET 4 E 4 MET B 240 ASP B 243 1 N ILE B 242 O SER B 271
SHEET 1 F 3 GLU B 176 GLU B 179 0
SHEET 2 F 3 ASN B 156 CYS B 159 1 N LEU B 157 O ARG B 178
SHEET 3 F 3 THR B 202 VAL B 206 1 O ILE B 203 N ASN B 156
SHEET 1 G 2 PHE B 301 TYR B 305 0
SHEET 2 G 2 GLY B 308 THR B 312 -1 O THR B 312 N PHE B 301
SHEET 1 H 4 TYR B 363 THR B 368 0
SHEET 2 H 4 ALA B 377 LEU B 382 -1 O LYS B 381 N GLU B 364
SHEET 3 H 4 VAL B 419 MET B 424 -1 O ILE B 423 N VAL B 378
SHEET 4 H 4 ALA B 408 THR B 410 -1 N PHE B 409 O VAL B 420
SHEET 1 I 4 GLY C 120 THR C 123 0
SHEET 2 I 4 GLY C 285 TRP C 289 -1 O GLY C 285 N THR C 123
SHEET 3 I 4 VAL C 267 SER C 273 -1 N ALA C 272 O TRP C 286
SHEET 4 I 4 MET C 240 ASP C 243 1 N ILE C 242 O SER C 271
SHEET 1 J 3 GLU C 176 GLU C 179 0
SHEET 2 J 3 ASN C 156 CYS C 159 1 N LEU C 157 O ARG C 178
SHEET 3 J 3 THR C 202 VAL C 206 1 O ILE C 203 N ASN C 156
SHEET 1 K 2 PHE C 301 TYR C 305 0
SHEET 2 K 2 GLY C 308 THR C 312 -1 O THR C 312 N PHE C 301
SHEET 1 L 4 TYR C 363 THR C 368 0
SHEET 2 L 4 ALA C 377 LEU C 382 -1 O LYS C 381 N GLU C 364
SHEET 3 L 4 VAL C 419 MET C 424 -1 O ILE C 423 N VAL C 378
SHEET 4 L 4 ALA C 408 THR C 410 -1 N PHE C 409 O VAL C 420
SHEET 1 M 4 GLY D 120 THR D 123 0
SHEET 2 M 4 GLY D 285 TRP D 289 -1 O GLY D 285 N THR D 123
SHEET 3 M 4 VAL D 267 SER D 273 -1 N ALA D 272 O TRP D 286
SHEET 4 M 4 MET D 240 ASP D 243 1 N ILE D 242 O SER D 271
SHEET 1 N 3 GLU D 176 GLU D 179 0
SHEET 2 N 3 ASN D 156 CYS D 159 1 N LEU D 157 O ARG D 178
SHEET 3 N 3 THR D 202 VAL D 206 1 O ILE D 203 N ASN D 156
SHEET 1 O 2 PHE D 301 TYR D 305 0
SHEET 2 O 2 GLY D 308 THR D 312 -1 O THR D 312 N PHE D 301
SHEET 1 P 4 TYR D 363 THR D 368 0
SHEET 2 P 4 ALA D 377 LEU D 382 -1 O LYS D 381 N GLU D 364
SHEET 3 P 4 VAL D 419 MET D 424 -1 O ILE D 423 N VAL D 378
SHEET 4 P 4 ALA D 408 THR D 410 -1 N PHE D 409 O VAL D 420
SHEET 1 Q 4 GLY E 120 THR E 123 0
SHEET 2 Q 4 GLY E 285 TRP E 289 -1 O GLY E 285 N THR E 123
SHEET 3 Q 4 VAL E 267 SER E 273 -1 N ALA E 272 O TRP E 286
SHEET 4 Q 4 MET E 240 ASP E 243 1 N ILE E 242 O SER E 271
SHEET 1 R 3 GLU E 176 GLU E 179 0
SHEET 2 R 3 ASN E 156 CYS E 159 1 N LEU E 157 O ARG E 178
SHEET 3 R 3 THR E 202 VAL E 206 1 O ILE E 203 N ASN E 156
SHEET 1 S 2 PHE E 301 TYR E 305 0
SHEET 2 S 2 GLY E 308 THR E 312 -1 O GLY E 308 N TYR E 305
SHEET 1 T 4 TYR E 363 THR E 368 0
SHEET 2 T 4 ALA E 377 LEU E 382 -1 O LYS E 381 N GLU E 364
SHEET 3 T 4 VAL E 419 MET E 424 -1 O ILE E 423 N VAL E 378
SHEET 4 T 4 ALA E 408 THR E 410 -1 N PHE E 409 O VAL E 420
SHEET 1 U 4 GLY F 120 THR F 123 0
SHEET 2 U 4 GLY F 285 TRP F 289 -1 O GLY F 285 N THR F 123
SHEET 3 U 4 VAL F 267 SER F 273 -1 N ALA F 272 O TRP F 286
SHEET 4 U 4 MET F 240 ASP F 243 1 N MET F 240 O LYS F 268
SHEET 1 V 3 GLU F 176 GLU F 179 0
SHEET 2 V 3 ASN F 156 CYS F 159 1 N LEU F 157 O ARG F 178
SHEET 3 V 3 THR F 202 VAL F 206 1 O ILE F 203 N ASN F 156
SHEET 1 W 2 PHE F 301 TYR F 305 0
SHEET 2 W 2 GLY F 308 THR F 312 -1 O THR F 312 N PHE F 301
SHEET 1 X 4 TYR F 363 THR F 368 0
SHEET 2 X 4 ALA F 377 LEU F 382 -1 O LYS F 381 N GLU F 364
SHEET 3 X 4 VAL F 419 MET F 424 -1 O ILE F 423 N VAL F 378
SHEET 4 X 4 ALA F 408 THR F 410 -1 N PHE F 409 O VAL F 420
LINK NZ LYS A 276 C4A PLP A 500 1555 1555 1.33
LINK NZ LYS B 276 C4A PLP B 500 1555 1555 1.33
LINK NZ LYS C 276 C4A PLP C 501 1555 1555 1.33
LINK NZ LYS D 276 C4A PLP D 501 1555 1555 1.33
LINK NZ LYS E 276 C4A PLP E 502 1555 1555 1.33
LINK NZ LYS F 276 C4A PLP F 502 1555 1555 1.33
SITE 1 AC1 16 GLY A 125 SER A 126 SER A 127 GLN A 163
SITE 2 AC1 16 CYS A 165 THR A 208 THR A 212 ASP A 243
SITE 3 AC1 16 ALA A 245 SER A 273 HIS A 275 LYS A 276
SITE 4 AC1 16 HOH A5552 HOH A5567 PHE B 317 SER B 318
SITE 1 AC2 16 PHE A 317 SER A 318 GLY B 125 SER B 126
SITE 2 AC2 16 SER B 127 GLN B 163 CYS B 165 THR B 208
SITE 3 AC2 16 THR B 212 ASP B 243 ALA B 245 SER B 273
SITE 4 AC2 16 HIS B 275 LYS B 276 HOH B6552 HOH B6574
SITE 1 AC3 16 GLY C 125 SER C 126 SER C 127 GLN C 163
SITE 2 AC3 16 CYS C 165 THR C 208 THR C 212 ASP C 243
SITE 3 AC3 16 ALA C 245 SER C 273 HIS C 275 LYS C 276
SITE 4 AC3 16 HOH C8528 PHE D 317 SER D 318 HOH D7561
SITE 1 AC4 16 PHE C 317 SER C 318 GLY D 125 SER D 126
SITE 2 AC4 16 SER D 127 GLN D 163 CYS D 165 THR D 208
SITE 3 AC4 16 THR D 212 ASP D 243 ALA D 245 SER D 273
SITE 4 AC4 16 HIS D 275 LYS D 276 HOH D7538 HOH D7566
SITE 1 AC5 16 GLY E 125 SER E 126 SER E 127 GLN E 163
SITE 2 AC5 16 CYS E 165 THR E 208 THR E 212 ASP E 243
SITE 3 AC5 16 ALA E 245 SER E 273 HIS E 275 LYS E 276
SITE 4 AC5 16 HOH E9548 PHE F 317 SER F 318 HOH F 520
SITE 1 AC6 16 PHE E 317 SER E 318 HOH E9562 GLY F 125
SITE 2 AC6 16 SER F 126 SER F 127 GLN F 163 CYS F 165
SITE 3 AC6 16 THR F 208 THR F 212 ASP F 243 ALA F 245
SITE 4 AC6 16 SER F 273 HIS F 275 LYS F 276 HOH F 544
SITE 1 AC7 7 ASN A 83 ASP A 86 PHE A 317 SER A 318
SITE 2 AC7 7 HOH A5654 THR B 62 PHE B 63
SITE 1 AC8 6 THR A 62 PHE A 63 ASN B 83 ASP B 86
SITE 2 AC8 6 SER B 318 HOH B6689
SITE 1 AC9 5 ASN C 83 ASP C 86 SER C 318 THR D 62
SITE 2 AC9 5 PHE D 63
SITE 1 BC1 6 THR C 62 PHE C 63 HOH C8740 ASN D 83
SITE 2 BC1 6 ASP D 86 SER D 318
SITE 1 BC2 6 ASN E 83 ASP E 86 SER E 318 HOH E9537
SITE 2 BC2 6 THR F 62 PHE F 63
SITE 1 BC3 6 THR E 62 PHE E 63 HOH E9678 ASN F 83
SITE 2 BC3 6 ASP F 86 SER F 318
CRYST1 90.780 91.406 93.686 76.80 77.10 78.24 P 1 6
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 0.011016 -0.002293 -0.002123 0.00000
SCALE2 0.000000 0.011175 -0.002182 0.00000
SCALE3 0.000000 0.000000 0.011157 0.00000
(ATOM LINES ARE NOT SHOWN.)
END