HEADER LYASE 14-MAR-06 2DGM
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB IN COMPLEX WITH IODIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE DECARBOXYLASE BETA;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: GAD-BETA, GADB;
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 STRAIN: JM109;
SOURCE 5 GENE: GADB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS GADB COMPLEXED WITH IODIDE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.GRUETTER,G.CAPITANI,H.GUT
REVDAT 4 25-OCT-23 2DGM 1 REMARK LINK
REVDAT 3 13-JUL-11 2DGM 1 VERSN
REVDAT 2 24-FEB-09 2DGM 1 VERSN
REVDAT 1 20-JUN-06 2DGM 0
JRNL AUTH H.GUT,E.PENNACCHIETTI,R.A.JOHN,F.BOSSA,G.CAPITANI,
JRNL AUTH 2 D.DE BIASE,M.G.GRUETTER
JRNL TITL ESCHERICHIA COLI ACID RESISTANCE: PH-SENSING, ACTIVATION BY
JRNL TITL 2 CHLORIDE AND AUTOINHIBITION IN GADB
JRNL REF EMBO J. V. 25 2643 2006
JRNL REFN ISSN 0261-4189
JRNL PMID 16675957
JRNL DOI 10.1038/SJ.EMBOJ.7601107
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.CAPITANI,D.DE BIASE,C.AURIZI,H.GUT,F.BOSSA,M.G.GRUETTER
REMARK 1 TITL CRYSTAL STRUCTURE AND FUNCTIONAL ANALYSIS OF ESCHERICHIA
REMARK 1 TITL 2 COLI GLUTAMATE DECARBOXYLASE
REMARK 1 REF EMBO J. V. 22 4027 2003
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 12912902
REMARK 1 DOI 10.1093/EMBOJ/CDG403
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
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) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 191251
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) : 0.227
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5338
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 296
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 : 21578
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 1923
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.00
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.260
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 2DGM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025394.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 90.0
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) : 1.300
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200 MONOCHROMATOR
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 : 191280
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1PMM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.135M SODIUM ACETATE, 0.7M SODIUM
REMARK 280 FORMATE, 13% PEG 4000, PH 4.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 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: 57140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 86370 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 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 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 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 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 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 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 LEU A 187 48.43 -90.87
REMARK 500 ALA A 244 42.47 -104.29
REMARK 500 LEU A 250 -63.35 -123.65
REMARK 500 ASP A 261 -144.69 -99.52
REMARK 500 LYS A 276 -114.67 -105.50
REMARK 500 PHE A 317 -100.31 -112.61
REMARK 500 PHE A 429 71.84 -115.61
REMARK 500 PRO B 184 119.94 -37.93
REMARK 500 GLN B 186 68.71 -154.14
REMARK 500 LEU B 187 38.28 -83.88
REMARK 500 ALA B 244 41.12 -103.51
REMARK 500 LEU B 250 -67.87 -125.75
REMARK 500 ASP B 261 -143.63 -95.59
REMARK 500 LYS B 276 -117.38 -102.69
REMARK 500 ASP B 291 -177.23 -170.55
REMARK 500 TYR B 305 105.08 -162.17
REMARK 500 PHE B 317 -94.62 -111.62
REMARK 500 PHE B 429 69.00 -111.54
REMARK 500 SER C 29 -3.95 -143.76
REMARK 500 LEU C 187 49.15 -89.96
REMARK 500 LEU C 250 -68.82 -124.52
REMARK 500 ASP C 261 -144.55 -96.41
REMARK 500 LYS C 276 -120.22 -102.24
REMARK 500 LEU C 306 70.73 37.84
REMARK 500 PHE C 317 -103.38 -115.40
REMARK 500 PHE C 429 71.96 -111.25
REMARK 500 PRO D 161 71.67 -68.28
REMARK 500 GLN D 186 71.93 -153.82
REMARK 500 LEU D 187 44.10 -86.39
REMARK 500 ALA D 244 40.35 -103.68
REMARK 500 LEU D 250 -68.25 -122.27
REMARK 500 ALA D 255 61.47 -151.09
REMARK 500 ASP D 261 -146.92 -97.89
REMARK 500 LYS D 276 -112.74 -100.49
REMARK 500 PHE D 317 -100.41 -116.67
REMARK 500 PHE D 429 66.61 -115.02
REMARK 500 PRO E 184 125.21 -37.21
REMARK 500 GLN E 186 74.42 -150.31
REMARK 500 LEU E 187 46.23 -86.54
REMARK 500 ALA E 244 41.93 -105.37
REMARK 500 ASP E 261 -147.15 -94.65
REMARK 500 LYS E 276 -116.75 -102.94
REMARK 500 PHE E 317 -103.79 -116.61
REMARK 500 PHE E 429 67.55 -117.95
REMARK 500 SER F 29 -7.08 -140.92
REMARK 500 GLN F 186 76.58 -150.38
REMARK 500 LEU F 187 42.15 -88.33
REMARK 500 ALA F 244 40.59 -106.70
REMARK 500 LEU F 250 -65.25 -123.06
REMARK 500 ALA F 255 60.58 -152.06
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2331
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2332
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2333
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 2334
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 2335
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2336
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2337
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2338
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 2339
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2342
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2343
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 2346
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 2347
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2348
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2349
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2350
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 2351
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 2352
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 2353
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2354
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 2355
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2356
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 2357
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 2358
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 2359
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD F 2360
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP F 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2550
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2560
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 2570
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 2580
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 2590
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2600
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 2610
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 2620
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 2630
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 2640
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 2650
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 2660
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 2670
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY E 2519
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 2833
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PMM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB (LOW PH)
REMARK 900 RELATED ID: 1PMO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI GADB (NEUTRAL PH)
REMARK 900 RELATED ID: 2DGK RELATED DB: PDB
REMARK 900 N-TERMINAL DELETION MUTANT OF THE SAME PROTEIN IN AN AUTOINHIBITED
REMARK 900 STATE (ALDAMINE)
REMARK 900 RELATED ID: 2DGL RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH BROMIDE
DBREF 2DGM A 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 2DGM B 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 2DGM C 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 2DGM D 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 2DGM E 1 466 UNP P69910 DCEB_ECOLI 1 466
DBREF 2DGM 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 IOD A2331 1
HET IOD A2337 1
HET IOD A2343 1
HET IOD A2349 1
HET IOD A2355 1
HET IOD A2361 1
HET PLP A 500 15
HET FMT A2550 3
HET FMT A2560 3
HET FMT A2600 3
HET IOD B2332 1
HET IOD B2333 1
HET IOD B2338 1
HET IOD B2344 1
HET IOD B2350 1
HET IOD B2356 1
HET PLP B 500 15
HET FMT B2650 3
HET IOD C2339 1
HET IOD C2345 1
HET IOD C2351 1
HET IOD C2357 1
HET PLP C 501 15
HET FMT C2610 3
HET IOD D2334 1
HET IOD D2340 1
HET IOD D2346 1
HET IOD D2352 1
HET IOD D2358 1
HET IOD D2362 1
HET PLP D 501 15
HET FMT D2570 3
HET FMT D2580 3
HET FMT D2630 3
HET IOD E2335 1
HET IOD E2341 1
HET IOD E2347 1
HET IOD E2353 1
HET IOD E2359 1
HET PLP E 502 15
HET FMT E2620 3
HET ACY E2519 4
HET PEG E2833 7
HET IOD F2336 1
HET IOD F2342 1
HET IOD F2348 1
HET IOD F2354 1
HET IOD F2360 1
HET PLP F 502 15
HET FMT F2590 3
HET FMT F2640 3
HET FMT F2660 3
HET FMT F2670 3
HETNAM IOD IODIDE ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM FMT FORMIC ACID
HETNAM ACY ACETIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 7 IOD 32(I 1-)
FORMUL 13 PLP 6(C8 H10 N O6 P)
FORMUL 14 FMT 13(C H2 O2)
FORMUL 48 ACY C2 H4 O2
FORMUL 49 PEG C4 H10 O3
FORMUL 60 HOH *1923(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 GLY A 54 5 4
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 GLY A 412 THR A 416 5 5
HELIX 19 19 GLU A 430 HIS A 451 1 22
HELIX 20 20 LYS B 3 ASP B 15 1 13
HELIX 21 21 ALA B 20 SER B 24 5 5
HELIX 22 22 ARG B 38 LEU B 50 1 13
HELIX 23 23 TYR B 51 GLY B 54 5 4
HELIX 24 24 ASN B 55 ASN B 59 5 5
HELIX 25 25 ASP B 69 SER B 79 1 11
HELIX 26 26 TYR B 90 TRP B 108 1 19
HELIX 27 27 GLY B 125 ALA B 147 1 23
HELIX 28 28 ILE B 164 TRP B 173 1 10
HELIX 29 29 ASP B 190 CYS B 198 1 9
HELIX 30 30 PHE B 219 GLY B 235 1 17
HELIX 31 31 SER B 246 PHE B 249 5 4
HELIX 32 32 LEU B 250 ALA B 255 1 6
HELIX 33 33 ASP B 291 LEU B 295 5 5
HELIX 34 34 PRO B 296 VAL B 300 5 5
HELIX 35 35 ALA B 321 LYS B 359 1 39
HELIX 36 36 THR B 391 LEU B 401 1 11
HELIX 37 37 GLU B 430 HIS B 451 1 22
HELIX 38 38 LYS C 3 ASP C 15 1 13
HELIX 39 39 ALA C 20 SER C 24 5 5
HELIX 40 40 ARG C 38 LEU C 50 1 13
HELIX 41 41 TYR C 51 ASP C 53 5 3
HELIX 42 42 ASN C 55 ASN C 59 5 5
HELIX 43 43 ASP C 69 SER C 79 1 11
HELIX 44 44 TYR C 90 TRP C 108 1 19
HELIX 45 45 GLY C 125 GLY C 149 1 25
HELIX 46 46 ILE C 164 TRP C 173 1 10
HELIX 47 47 ASP C 190 CYS C 198 1 9
HELIX 48 48 PHE C 219 GLY C 235 1 17
HELIX 49 49 SER C 246 PHE C 249 5 4
HELIX 50 50 LEU C 250 ALA C 255 1 6
HELIX 51 51 ASP C 291 LEU C 295 5 5
HELIX 52 52 PRO C 296 VAL C 300 5 5
HELIX 53 53 ALA C 321 LYS C 359 1 39
HELIX 54 54 THR C 391 LEU C 401 1 11
HELIX 55 55 GLY C 412 THR C 416 5 5
HELIX 56 56 GLU C 430 HIS C 451 1 22
HELIX 57 57 PRO C 452 GLN C 455 5 4
HELIX 58 58 LYS D 3 ASP D 15 1 13
HELIX 59 59 ALA D 20 SER D 24 5 5
HELIX 60 60 ARG D 38 LEU D 50 1 13
HELIX 61 61 TYR D 51 GLY D 54 5 4
HELIX 62 62 ASN D 55 ASN D 59 5 5
HELIX 63 63 ASP D 69 ILE D 80 1 12
HELIX 64 64 TYR D 90 TRP D 108 1 19
HELIX 65 65 GLY D 125 ALA D 147 1 23
HELIX 66 66 ILE D 164 TRP D 173 1 10
HELIX 67 67 ASP D 190 CYS D 198 1 9
HELIX 68 68 PHE D 219 GLY D 235 1 17
HELIX 69 69 SER D 246 PHE D 249 5 4
HELIX 70 70 LEU D 250 ALA D 255 1 6
HELIX 71 71 ASP D 291 LEU D 295 5 5
HELIX 72 72 PRO D 296 VAL D 300 5 5
HELIX 73 73 ALA D 321 LYS D 359 1 39
HELIX 74 74 THR D 391 LEU D 401 1 11
HELIX 75 75 GLY D 412 THR D 416 5 5
HELIX 76 76 GLU D 430 HIS D 451 1 22
HELIX 77 77 PRO D 452 GLN D 455 5 4
HELIX 78 78 LYS E 3 ASP E 15 1 13
HELIX 79 79 ALA E 20 SER E 24 5 5
HELIX 80 80 ARG E 38 LEU E 50 1 13
HELIX 81 81 TYR E 51 GLY E 54 5 4
HELIX 82 82 ASN E 55 ASN E 59 5 5
HELIX 83 83 ASP E 69 ILE E 80 1 12
HELIX 84 84 TYR E 90 TRP E 108 1 19
HELIX 85 85 GLY E 125 GLY E 149 1 25
HELIX 86 86 GLN E 163 TRP E 173 1 11
HELIX 87 87 ASP E 190 CYS E 198 1 9
HELIX 88 88 PHE E 219 GLY E 235 1 17
HELIX 89 89 SER E 246 PHE E 249 5 4
HELIX 90 90 LEU E 250 ALA E 255 1 6
HELIX 91 91 ASP E 291 LEU E 295 5 5
HELIX 92 92 PRO E 296 VAL E 300 5 5
HELIX 93 93 ALA E 321 LYS E 359 1 39
HELIX 94 94 THR E 391 LEU E 401 1 11
HELIX 95 95 GLY E 412 THR E 416 5 5
HELIX 96 96 GLU E 430 ASP E 450 1 21
HELIX 97 97 LYS F 3 ASP F 15 1 13
HELIX 98 98 ALA F 20 SER F 24 5 5
HELIX 99 99 ARG F 38 LEU F 50 1 13
HELIX 100 100 TYR F 51 GLY F 54 5 4
HELIX 101 101 ASN F 55 ASN F 59 5 5
HELIX 102 102 ASP F 69 SER F 79 1 11
HELIX 103 103 TYR F 90 TRP F 108 1 19
HELIX 104 104 GLY F 125 ALA F 147 1 23
HELIX 105 105 ILE F 164 TRP F 173 1 10
HELIX 106 106 ASP F 190 CYS F 198 1 9
HELIX 107 107 PHE F 219 GLY F 235 1 17
HELIX 108 108 SER F 246 PHE F 249 5 4
HELIX 109 109 LEU F 250 ALA F 255 1 6
HELIX 110 110 ASP F 291 LEU F 295 5 5
HELIX 111 111 PRO F 296 VAL F 300 5 5
HELIX 112 112 ALA F 321 LYS F 359 1 39
HELIX 113 113 THR F 391 LEU F 401 1 11
HELIX 114 114 GLY F 412 THR F 416 5 5
HELIX 115 115 GLU F 430 HIS F 451 1 22
HELIX 116 116 PRO F 452 GLN F 455 5 4
SHEET 1 A 4 GLY A 120 THR A 123 0
SHEET 2 A 4 GLY A 285 TRP A 289 -1 O VAL A 287 N THR A 121
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 ILE A 310 N VAL A 303
SHEET 1 D 4 TYR A 363 THR A 368 0
SHEET 2 D 4 ALA A 377 LEU A 382 -1 O CYS A 379 N ILE A 366
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 ILE B 270 O ILE B 288
SHEET 4 E 4 MET B 240 ASP B 243 1 N MET B 240 O LYS B 268
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 CYS B 379 N ILE B 366
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 CYS C 379 N ILE C 366
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 MET D 240 O LYS D 268
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 CYS D 379 N ILE D 366
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 MET E 240 O LYS E 268
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 CYS E 379 N ILE E 366
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 CYS F 379 N ILE F 366
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 1.34
LINK NZ LYS B 276 C4A PLP B 500 1555 1555 1.32
LINK NZ LYS C 276 C4A PLP C 501 1555 1555 1.34
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 2 SER A 16 ARG F 427
SITE 1 AC2 2 SER B 16 ARG C 427
SITE 1 AC3 2 ARG B 427 SER C 16
SITE 1 AC4 2 SER D 16 ARG E 427
SITE 1 AC5 2 ARG D 427 SER E 16
SITE 1 AC6 2 ARG A 427 SER F 16
SITE 1 AC7 2 LYS A 381 ILE A 418
SITE 1 AC8 1 ILE B 418
SITE 1 AC9 2 LYS C 381 ILE C 418
SITE 1 BC1 1 ILE F 418
SITE 1 BC2 1 LYS A 453
SITE 1 BC3 1 LYS D 453
SITE 1 BC4 1 HIS E 451
SITE 1 BC5 1 LYS F 453
SITE 1 BC6 2 TRP A 67 HIS A 73
SITE 1 BC7 3 ASN A 81 ASP B 68 HIS B 73
SITE 1 BC8 4 TRP C 67 ASP C 68 HIS C 73 ASN D 81
SITE 1 BC9 3 ASN C 81 ASP D 68 HIS D 73
SITE 1 CC1 4 TRP E 67 ASP E 68 HIS E 73 ASN F 81
SITE 1 CC2 1 HIS F 73
SITE 1 CC3 3 LEU A 382 THR A 391 LEU A 392
SITE 1 CC4 3 LEU B 382 THR B 391 LEU B 392
SITE 1 CC5 3 LEU C 382 THR C 391 LEU C 392
SITE 1 CC6 3 LEU D 382 THR D 391 LEU D 392
SITE 1 CC7 2 THR E 391 LEU E 392
SITE 1 CC8 2 THR F 391 LEU F 392
SITE 1 CC9 15 GLY A 125 SER A 126 SER A 127 GLN A 163
SITE 2 CC9 15 THR A 208 THR A 212 ASP A 243 ALA A 245
SITE 3 CC9 15 SER A 273 HIS A 275 LYS A 276 HOH A2651
SITE 4 CC9 15 PHE B 317 SER B 318 HOH B2680
SITE 1 DC1 15 PHE A 317 SER A 318 HOH A2637 GLY B 125
SITE 2 DC1 15 SER B 126 SER B 127 GLN B 163 CYS B 165
SITE 3 DC1 15 THR B 212 ASP B 243 ALA B 245 SER B 273
SITE 4 DC1 15 HIS B 275 LYS B 276 HOH B2703
SITE 1 DC2 15 GLY C 125 SER C 126 SER C 127 GLN C 163
SITE 2 DC2 15 THR C 208 THR C 212 ASP C 243 ALA C 245
SITE 3 DC2 15 SER C 273 HIS C 275 LYS C 276 HOH C2619
SITE 4 DC2 15 PHE D 317 SER D 318 HOH D2673
SITE 1 DC3 15 PHE C 317 SER C 318 HOH C2649 GLY D 125
SITE 2 DC3 15 SER D 126 SER D 127 GLN D 163 CYS D 165
SITE 3 DC3 15 THR D 212 ASP D 243 ALA D 245 SER D 273
SITE 4 DC3 15 HIS D 275 LYS D 276 HOH D2649
SITE 1 DC4 15 SER E 126 SER E 127 GLN E 163 CYS E 165
SITE 2 DC4 15 THR E 208 THR E 212 ASP E 243 ALA E 245
SITE 3 DC4 15 SER E 273 HIS E 275 LYS E 276 HOH E2857
SITE 4 DC4 15 PHE F 317 SER F 318 HOH F2688
SITE 1 DC5 15 PHE E 317 SER E 318 HOH E2869 GLY F 125
SITE 2 DC5 15 SER F 126 SER F 127 GLN F 163 CYS F 165
SITE 3 DC5 15 THR F 212 ASP F 243 ALA F 245 SER F 273
SITE 4 DC5 15 HIS F 275 LYS F 276 HOH F2711
SITE 1 DC6 4 ASN A 83 ASP A 86 THR B 62 PHE B 63
SITE 1 DC7 4 THR A 62 PHE A 63 ASN B 83 ASP B 86
SITE 1 DC8 4 ASN C 83 ASP C 86 THR D 62 PHE D 63
SITE 1 DC9 5 THR C 62 PHE C 63 CYS C 64 ASN D 83
SITE 2 DC9 5 ASP D 86
SITE 1 EC1 4 ASN E 83 ASP E 86 THR F 62 PHE F 63
SITE 1 EC2 5 TRP A 84 ASP A 97 THR A 121 ASN A 122
SITE 2 EC2 5 HOH A2720
SITE 1 EC3 5 ASP C 97 LEU C 98 THR C 121 ASN C 122
SITE 2 EC3 5 HOH C2725
SITE 1 EC4 5 TRP E 84 ASP E 97 THR E 121 ASN E 122
SITE 2 EC4 5 HOH E2973
SITE 1 EC5 7 TRP D 84 ASP D 97 LEU D 98 GLY D 120
SITE 2 EC5 7 THR D 121 ASN D 122 HOH D2778
SITE 1 EC6 5 TRP F 84 ASP F 97 THR F 121 ASN F 122
SITE 2 EC6 5 HOH F2726
SITE 1 EC7 6 TRP B 84 ASP B 97 THR B 121 ASN B 122
SITE 2 EC7 6 HOH B2707 HOH B2848
SITE 1 EC8 4 LEU F 98 ALA F 118 GLY F 120 GLY F 311
SITE 1 EC9 6 PRO F 111 ARG F 290 ASP F 291 HOH F2678
SITE 2 EC9 6 HOH F2793 HOH F2810
SITE 1 FC1 6 THR E 62 PHE E 63 ASN F 83 ASP F 86
SITE 2 FC1 6 PHE F 317 SER F 318
SITE 1 FC2 8 ASP E 228 ASP E 237 ASP E 239 PRO E 265
SITE 2 FC2 8 ARG E 266 LYS E 268 HOH E2933 HOH E3104
CRYST1 91.336 91.804 93.914 76.65 76.94 78.04 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 0.010949 -0.002319 -0.002132 0.00000
SCALE2 0.000000 0.011134 -0.002192 0.00000
SCALE3 0.000000 0.000000 0.011141 0.00000
(ATOM LINES ARE NOT SHOWN.)
END