HEADER LYASE 20-NOV-06 2NXW
TITLE CRYSTAL STRUCTURE OF PHENYLPYRUVATE DECARBOXYLASE OF AZOSPIRILLUM
TITLE 2 BRASILENSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHENYL-3-PYRUVATE DECARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHENYL-3-PYRUVATE DECARBOXYLASE;
COMPND 5 EC: 4.1.1.43;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AZOSPIRILLUM BRASILENSE;
SOURCE 3 ORGANISM_TAXID: 192;
SOURCE 4 GENE: IPDC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 CODONPLUS-RP;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS THIAMINE PYROPHOSPHATE, ASYMMETRIC DIMER OF DIMERS, OPEN ACTIVE SITE
KEYWDS 2 LOOPS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.VERSEES,S.SPAEPEN,J.VANDERLEYDEN,J.STEYAERT
REVDAT 5 30-AUG-23 2NXW 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2NXW 1 VERSN
REVDAT 3 06-APR-11 2NXW 1 JRNL
REVDAT 2 24-FEB-09 2NXW 1 VERSN
REVDAT 1 29-MAY-07 2NXW 0
JRNL AUTH W.VERSEES,S.SPAEPEN,J.VANDERLEYDEN,J.STEYAERT
JRNL TITL THE CRYSTAL STRUCTURE OF PHENYLPYRUVATE DECARBOXYLASE FROM
JRNL TITL 2 AZOSPIRILLUM BRASILENSE AT 1.5 A RESOLUTION. IMPLICATIONS
JRNL TITL 3 FOR ITS CATALYTIC AND REGULATORY MECHANISM.
JRNL REF FEBS J. V. 274 2363 2007
JRNL REFN ISSN 1742-464X
JRNL PMID 17403037
JRNL DOI 10.1111/J.1742-4658.2007.05771.X
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 170507
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) : 0.175
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 8539
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE : 0.2300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1408
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7863
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 1337
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.11
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) : 0.17
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.406
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 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 2NXW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040438.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-05
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 : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8131
REMARK 200 MONOCHROMATOR : SI [111], HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 170507
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.3700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.38200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.540
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1OVM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 10 % GLYCEROL, 0.1 M
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 60.46250
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 60.46250
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 49.70550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.51600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 49.70550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.51600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 60.46250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 49.70550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.51600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 60.46250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 49.70550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.51600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 TETRAMER GENERATED FROM THE
REMARK 300 DIMER IN THE ASYMMETRIC UNIT BY THE OPERATION: -X+1, Y, -Z+1/2
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 99.41100
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 60.46250
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A4359 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A4668 LIES ON A SPECIAL POSITION.
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 ASN A 106
REMARK 465 ALA A 107
REMARK 465 HIS A 112
REMARK 465 HIS A 113
REMARK 465 GLN A 114
REMARK 465 GLY A 115
REMARK 465 ARG A 116
REMARK 465 THR A 117
REMARK 465 LEU A 118
REMARK 465 HIS A 540
REMARK 465 ALA A 541
REMARK 465 ALA A 542
REMARK 465 PRO A 543
REMARK 465 ARG A 544
REMARK 465 GLU A 545
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B 105
REMARK 465 ASN B 106
REMARK 465 ALA B 107
REMARK 465 GLY B 108
REMARK 465 LEU B 111
REMARK 465 HIS B 112
REMARK 465 HIS B 113
REMARK 465 GLN B 114
REMARK 465 GLY B 115
REMARK 465 ARG B 116
REMARK 465 THR B 117
REMARK 465 LEU B 118
REMARK 465 LEU B 539
REMARK 465 HIS B 540
REMARK 465 ALA B 541
REMARK 465 ALA B 542
REMARK 465 PRO B 543
REMARK 465 ARG B 544
REMARK 465 GLU B 545
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A -3 CD NE CZ NH1 NH2
REMARK 470 LYS A 126 CG CD CE NZ
REMARK 470 ARG A 185 NE CZ NH1 NH2
REMARK 470 GLU A 262 CG CD OE1 OE2
REMARK 470 ARG A 265 CD NE CZ NH1 NH2
REMARK 470 GLN A 289 CG CD OE1 NE2
REMARK 470 LYS A 296 CE NZ
REMARK 470 TYR A 309 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 339 CG CD OE1 OE2
REMARK 470 GLU A 372 CD OE1 OE2
REMARK 470 LYS A 505 CD CE NZ
REMARK 470 LYS A 537 CG CD CE NZ
REMARK 470 ARG A 538 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 119 CG OD1 OD2
REMARK 470 TRP B 181 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 181 CZ3 CH2
REMARK 470 ARG B 185 NE CZ NH1 NH2
REMARK 470 ASN B 284 CG OD1 ND2
REMARK 470 GLN B 289 CG CD OE1 NE2
REMARK 470 ARG B 290 CD NE CZ NH1 NH2
REMARK 470 LYS B 291 CE NZ
REMARK 470 GLU B 339 CG CD OE1 OE2
REMARK 470 ARG B 444 CD NE CZ NH1 NH2
REMARK 470 LYS B 505 CD CE NZ
REMARK 470 GLN B 534 CD OE1 NE2
REMARK 470 LYS B 537 CG CD CE NZ
REMARK 470 ARG B 538 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 4495 O HOH B 4495 3555 2.06
REMARK 500 O HOH A 4669 O HOH A 4669 4556 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 307 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 104 -125.93 -96.18
REMARK 500 ASN A 284 -128.75 45.45
REMARK 500 GLU A 339 126.83 -27.47
REMARK 500 ASP A 350 -162.70 -126.79
REMARK 500 ASP A 448 56.86 -143.91
REMARK 500 ASP B 350 -162.73 -122.07
REMARK 500 ASP B 448 57.76 -146.87
REMARK 500 GLN B 466 67.83 -155.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A4002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 429 OD1
REMARK 620 2 ASN A 456 OD1 85.0
REMARK 620 3 SER A 458 O 103.6 89.0
REMARK 620 4 TPP A2002 O2A 86.8 170.8 88.9
REMARK 620 5 TPP A2002 O1B 167.6 98.6 88.4 90.3
REMARK 620 6 HOH A4004 O 82.9 87.7 172.4 95.4 85.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B4001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 429 OD1
REMARK 620 2 ASN B 456 OD1 85.0
REMARK 620 3 SER B 458 O 103.1 87.2
REMARK 620 4 TPP B2001 O1B 167.3 97.7 89.5
REMARK 620 5 TPP B2001 O2A 86.0 169.3 89.3 92.4
REMARK 620 6 HOH B4005 O 83.5 89.4 172.3 84.1 95.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 3003
DBREF 2NXW A 1 545 UNP P51852 DCIP_AZOBR 1 545
DBREF 2NXW B 1 545 UNP P51852 DCIP_AZOBR 1 545
SEQADV 2NXW MET A -19 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW GLY A -18 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW SER A -17 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW SER A -16 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW HIS A -15 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS A -14 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS A -13 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS A -12 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS A -11 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS A -10 UNP P51852 EXPRESSION TAG
SEQADV 2NXW SER A -9 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW SER A -8 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW GLY A -7 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW LEU A -6 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW VAL A -5 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW PRO A -4 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW ARG A -3 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW GLY A -2 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW SER A -1 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW HIS A 0 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW GLN A 155 UNP P51852 LEU 155 CLONING ARTIFACT
SEQADV 2NXW ARG A 327 UNP P51852 GLY 327 SEE REMARK 999
SEQADV 2NXW MET B -19 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW GLY B -18 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW SER B -17 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW SER B -16 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW HIS B -15 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS B -14 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS B -13 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS B -12 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS B -11 UNP P51852 EXPRESSION TAG
SEQADV 2NXW HIS B -10 UNP P51852 EXPRESSION TAG
SEQADV 2NXW SER B -9 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW SER B -8 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW GLY B -7 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW LEU B -6 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW VAL B -5 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW PRO B -4 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW ARG B -3 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW GLY B -2 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW SER B -1 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW HIS B 0 UNP P51852 CLONING ARTIFACT
SEQADV 2NXW GLN B 155 UNP P51852 LEU 155 CLONING ARTIFACT
SEQADV 2NXW ARG B 327 UNP P51852 GLY 327 SEE REMARK 999
SEQRES 1 A 565 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 565 LEU VAL PRO ARG GLY SER HIS MET LYS LEU ALA GLU ALA
SEQRES 3 A 565 LEU LEU ARG ALA LEU LYS ASP ARG GLY ALA GLN ALA MET
SEQRES 4 A 565 PHE GLY ILE PRO GLY ASP PHE ALA LEU PRO PHE PHE LYS
SEQRES 5 A 565 VAL ALA GLU GLU THR GLN ILE LEU PRO LEU HIS THR LEU
SEQRES 6 A 565 SER HIS GLU PRO ALA VAL GLY PHE ALA ALA ASP ALA ALA
SEQRES 7 A 565 ALA ARG TYR SER SER THR LEU GLY VAL ALA ALA VAL THR
SEQRES 8 A 565 TYR GLY ALA GLY ALA PHE ASN MET VAL ASN ALA VAL ALA
SEQRES 9 A 565 GLY ALA TYR ALA GLU LYS SER PRO VAL VAL VAL ILE SER
SEQRES 10 A 565 GLY ALA PRO GLY THR THR GLU GLY ASN ALA GLY LEU LEU
SEQRES 11 A 565 LEU HIS HIS GLN GLY ARG THR LEU ASP THR GLN PHE GLN
SEQRES 12 A 565 VAL PHE LYS GLU ILE THR VAL ALA GLN ALA ARG LEU ASP
SEQRES 13 A 565 ASP PRO ALA LYS ALA PRO ALA GLU ILE ALA ARG VAL LEU
SEQRES 14 A 565 GLY ALA ALA ARG ALA GLN SER ARG PRO VAL TYR LEU GLU
SEQRES 15 A 565 ILE PRO ARG ASN MET VAL ASN ALA GLU VAL GLU PRO VAL
SEQRES 16 A 565 GLY ASP ASP PRO ALA TRP PRO VAL ASP ARG ASP ALA LEU
SEQRES 17 A 565 ALA ALA CYS ALA ASP GLU VAL LEU ALA ALA MET ARG SER
SEQRES 18 A 565 ALA THR SER PRO VAL LEU MET VAL CYS VAL GLU VAL ARG
SEQRES 19 A 565 ARG TYR GLY LEU GLU ALA LYS VAL ALA GLU LEU ALA GLN
SEQRES 20 A 565 ARG LEU GLY VAL PRO VAL VAL THR THR PHE MET GLY ARG
SEQRES 21 A 565 GLY LEU LEU ALA ASP ALA PRO THR PRO PRO LEU GLY THR
SEQRES 22 A 565 TYR ILE GLY VAL ALA GLY ASP ALA GLU ILE THR ARG LEU
SEQRES 23 A 565 VAL GLU GLU SER ASP GLY LEU PHE LEU LEU GLY ALA ILE
SEQRES 24 A 565 LEU SER ASP THR ASN PHE ALA VAL SER GLN ARG LYS ILE
SEQRES 25 A 565 ASP LEU ARG LYS THR ILE HIS ALA PHE ASP ARG ALA VAL
SEQRES 26 A 565 THR LEU GLY TYR HIS THR TYR ALA ASP ILE PRO LEU ALA
SEQRES 27 A 565 GLY LEU VAL ASP ALA LEU LEU GLU ARG LEU PRO PRO SER
SEQRES 28 A 565 ASP ARG THR THR ARG GLY LYS GLU PRO HIS ALA TYR PRO
SEQRES 29 A 565 THR GLY LEU GLN ALA ASP GLY GLU PRO ILE ALA PRO MET
SEQRES 30 A 565 ASP ILE ALA ARG ALA VAL ASN ASP ARG VAL ARG ALA GLY
SEQRES 31 A 565 GLN GLU PRO LEU LEU ILE ALA ALA ASP MET GLY ASP CYS
SEQRES 32 A 565 LEU PHE THR ALA MET ASP MET ILE ASP ALA GLY LEU MET
SEQRES 33 A 565 ALA PRO GLY TYR TYR ALA GLY MET GLY PHE GLY VAL PRO
SEQRES 34 A 565 ALA GLY ILE GLY ALA GLN CYS VAL SER GLY GLY LYS ARG
SEQRES 35 A 565 ILE LEU THR VAL VAL GLY ASP GLY ALA PHE GLN MET THR
SEQRES 36 A 565 GLY TRP GLU LEU GLY ASN CYS ARG ARG LEU GLY ILE ASP
SEQRES 37 A 565 PRO ILE VAL ILE LEU PHE ASN ASN ALA SER TRP GLU MET
SEQRES 38 A 565 LEU ARG THR PHE GLN PRO GLU SER ALA PHE ASN ASP LEU
SEQRES 39 A 565 ASP ASP TRP ARG PHE ALA ASP MET ALA ALA GLY MET GLY
SEQRES 40 A 565 GLY ASP GLY VAL ARG VAL ARG THR ARG ALA GLU LEU LYS
SEQRES 41 A 565 ALA ALA LEU ASP LYS ALA PHE ALA THR ARG GLY ARG PHE
SEQRES 42 A 565 GLN LEU ILE GLU ALA MET ILE PRO ARG GLY VAL LEU SER
SEQRES 43 A 565 ASP THR LEU ALA ARG PHE VAL GLN GLY GLN LYS ARG LEU
SEQRES 44 A 565 HIS ALA ALA PRO ARG GLU
SEQRES 1 B 565 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 565 LEU VAL PRO ARG GLY SER HIS MET LYS LEU ALA GLU ALA
SEQRES 3 B 565 LEU LEU ARG ALA LEU LYS ASP ARG GLY ALA GLN ALA MET
SEQRES 4 B 565 PHE GLY ILE PRO GLY ASP PHE ALA LEU PRO PHE PHE LYS
SEQRES 5 B 565 VAL ALA GLU GLU THR GLN ILE LEU PRO LEU HIS THR LEU
SEQRES 6 B 565 SER HIS GLU PRO ALA VAL GLY PHE ALA ALA ASP ALA ALA
SEQRES 7 B 565 ALA ARG TYR SER SER THR LEU GLY VAL ALA ALA VAL THR
SEQRES 8 B 565 TYR GLY ALA GLY ALA PHE ASN MET VAL ASN ALA VAL ALA
SEQRES 9 B 565 GLY ALA TYR ALA GLU LYS SER PRO VAL VAL VAL ILE SER
SEQRES 10 B 565 GLY ALA PRO GLY THR THR GLU GLY ASN ALA GLY LEU LEU
SEQRES 11 B 565 LEU HIS HIS GLN GLY ARG THR LEU ASP THR GLN PHE GLN
SEQRES 12 B 565 VAL PHE LYS GLU ILE THR VAL ALA GLN ALA ARG LEU ASP
SEQRES 13 B 565 ASP PRO ALA LYS ALA PRO ALA GLU ILE ALA ARG VAL LEU
SEQRES 14 B 565 GLY ALA ALA ARG ALA GLN SER ARG PRO VAL TYR LEU GLU
SEQRES 15 B 565 ILE PRO ARG ASN MET VAL ASN ALA GLU VAL GLU PRO VAL
SEQRES 16 B 565 GLY ASP ASP PRO ALA TRP PRO VAL ASP ARG ASP ALA LEU
SEQRES 17 B 565 ALA ALA CYS ALA ASP GLU VAL LEU ALA ALA MET ARG SER
SEQRES 18 B 565 ALA THR SER PRO VAL LEU MET VAL CYS VAL GLU VAL ARG
SEQRES 19 B 565 ARG TYR GLY LEU GLU ALA LYS VAL ALA GLU LEU ALA GLN
SEQRES 20 B 565 ARG LEU GLY VAL PRO VAL VAL THR THR PHE MET GLY ARG
SEQRES 21 B 565 GLY LEU LEU ALA ASP ALA PRO THR PRO PRO LEU GLY THR
SEQRES 22 B 565 TYR ILE GLY VAL ALA GLY ASP ALA GLU ILE THR ARG LEU
SEQRES 23 B 565 VAL GLU GLU SER ASP GLY LEU PHE LEU LEU GLY ALA ILE
SEQRES 24 B 565 LEU SER ASP THR ASN PHE ALA VAL SER GLN ARG LYS ILE
SEQRES 25 B 565 ASP LEU ARG LYS THR ILE HIS ALA PHE ASP ARG ALA VAL
SEQRES 26 B 565 THR LEU GLY TYR HIS THR TYR ALA ASP ILE PRO LEU ALA
SEQRES 27 B 565 GLY LEU VAL ASP ALA LEU LEU GLU ARG LEU PRO PRO SER
SEQRES 28 B 565 ASP ARG THR THR ARG GLY LYS GLU PRO HIS ALA TYR PRO
SEQRES 29 B 565 THR GLY LEU GLN ALA ASP GLY GLU PRO ILE ALA PRO MET
SEQRES 30 B 565 ASP ILE ALA ARG ALA VAL ASN ASP ARG VAL ARG ALA GLY
SEQRES 31 B 565 GLN GLU PRO LEU LEU ILE ALA ALA ASP MET GLY ASP CYS
SEQRES 32 B 565 LEU PHE THR ALA MET ASP MET ILE ASP ALA GLY LEU MET
SEQRES 33 B 565 ALA PRO GLY TYR TYR ALA GLY MET GLY PHE GLY VAL PRO
SEQRES 34 B 565 ALA GLY ILE GLY ALA GLN CYS VAL SER GLY GLY LYS ARG
SEQRES 35 B 565 ILE LEU THR VAL VAL GLY ASP GLY ALA PHE GLN MET THR
SEQRES 36 B 565 GLY TRP GLU LEU GLY ASN CYS ARG ARG LEU GLY ILE ASP
SEQRES 37 B 565 PRO ILE VAL ILE LEU PHE ASN ASN ALA SER TRP GLU MET
SEQRES 38 B 565 LEU ARG THR PHE GLN PRO GLU SER ALA PHE ASN ASP LEU
SEQRES 39 B 565 ASP ASP TRP ARG PHE ALA ASP MET ALA ALA GLY MET GLY
SEQRES 40 B 565 GLY ASP GLY VAL ARG VAL ARG THR ARG ALA GLU LEU LYS
SEQRES 41 B 565 ALA ALA LEU ASP LYS ALA PHE ALA THR ARG GLY ARG PHE
SEQRES 42 B 565 GLN LEU ILE GLU ALA MET ILE PRO ARG GLY VAL LEU SER
SEQRES 43 B 565 ASP THR LEU ALA ARG PHE VAL GLN GLY GLN LYS ARG LEU
SEQRES 44 B 565 HIS ALA ALA PRO ARG GLU
HET MG A4002 1
HET CL A4003 1
HET TPP A2002 26
HET GOL A3002 6
HET MG B4001 1
HET CL B4004 1
HET TPP B2001 26
HET GOL B3001 6
HET GOL B3003 6
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM TPP THIAMINE DIPHOSPHATE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MG 2(MG 2+)
FORMUL 4 CL 2(CL 1-)
FORMUL 5 TPP 2(C12 H19 N4 O7 P2 S 1+)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 12 HOH *1337(H2 O)
HELIX 1 1 LYS A 2 ARG A 14 1 13
HELIX 2 2 GLY A 24 PHE A 26 5 3
HELIX 3 3 ALA A 27 GLN A 38 1 12
HELIX 4 4 HIS A 47 SER A 63 1 17
HELIX 5 5 GLY A 73 ASN A 78 1 6
HELIX 6 6 MET A 79 GLU A 89 1 11
HELIX 7 7 ASP A 119 LYS A 126 1 8
HELIX 8 8 LYS A 140 SER A 156 1 17
HELIX 9 9 ASN A 166 VAL A 168 5 3
HELIX 10 10 ASP A 184 ALA A 202 1 19
HELIX 11 11 CYS A 210 TYR A 216 1 7
HELIX 12 12 LEU A 218 GLY A 230 1 13
HELIX 13 13 PHE A 237 ARG A 240 5 4
HELIX 14 14 ILE A 255 GLY A 259 5 5
HELIX 15 15 ASP A 260 GLU A 269 1 10
HELIX 16 16 ASP A 293 ARG A 295 5 3
HELIX 17 17 PRO A 316 ARG A 327 1 12
HELIX 18 18 ALA A 355 ALA A 369 1 15
HELIX 19 19 GLY A 381 MET A 388 1 8
HELIX 20 20 PHE A 406 SER A 418 1 13
HELIX 21 21 ASP A 429 GLY A 436 1 8
HELIX 22 22 TRP A 437 GLY A 440 5 4
HELIX 23 23 ASN A 441 GLY A 446 1 6
HELIX 24 24 TRP A 459 GLN A 466 1 8
HELIX 25 25 SER A 469 ASP A 473 5 5
HELIX 26 26 ARG A 478 ALA A 483 1 6
HELIX 27 27 ALA A 484 GLY A 487 5 4
HELIX 28 28 THR A 495 THR A 509 1 15
HELIX 29 29 SER A 526 LEU A 539 1 14
HELIX 30 30 LEU B 3 ARG B 14 1 12
HELIX 31 31 GLY B 24 PHE B 26 5 3
HELIX 32 32 ALA B 27 GLN B 38 1 12
HELIX 33 33 HIS B 47 SER B 63 1 17
HELIX 34 34 GLY B 73 ASN B 78 1 6
HELIX 35 35 MET B 79 GLU B 89 1 11
HELIX 36 36 ASP B 119 GLU B 127 1 9
HELIX 37 37 LYS B 140 SER B 156 1 17
HELIX 38 38 ASN B 166 VAL B 168 5 3
HELIX 39 39 ASP B 184 ALA B 202 1 19
HELIX 40 40 CYS B 210 TYR B 216 1 7
HELIX 41 41 LEU B 218 GLY B 230 1 13
HELIX 42 42 PHE B 237 ARG B 240 5 4
HELIX 43 43 ILE B 255 GLY B 259 5 5
HELIX 44 44 ASP B 260 GLU B 269 1 10
HELIX 45 45 SER B 288 ILE B 292 5 5
HELIX 46 46 PRO B 316 GLU B 326 1 11
HELIX 47 47 ALA B 355 ALA B 369 1 15
HELIX 48 48 GLY B 381 MET B 388 1 8
HELIX 49 49 PHE B 406 SER B 418 1 13
HELIX 50 50 ASP B 429 GLY B 436 1 8
HELIX 51 51 TRP B 437 GLY B 440 5 4
HELIX 52 52 ASN B 441 GLY B 446 1 6
HELIX 53 53 TRP B 459 GLN B 466 1 8
HELIX 54 54 SER B 469 ASP B 473 5 5
HELIX 55 55 ARG B 478 ALA B 484 1 7
HELIX 56 56 GLY B 485 GLY B 487 5 3
HELIX 57 57 THR B 495 THR B 509 1 15
HELIX 58 58 SER B 526 ARG B 538 1 13
SHEET 1 A 6 LEU A 42 THR A 44 0
SHEET 2 A 6 MET A 19 GLY A 21 1 N MET A 19 O HIS A 43
SHEET 3 A 6 GLY A 66 VAL A 70 1 O ALA A 69 N PHE A 20
SHEET 4 A 6 VAL A 93 ALA A 99 1 O VAL A 94 N GLY A 66
SHEET 5 A 6 VAL A 159 PRO A 164 1 O VAL A 159 N VAL A 95
SHEET 6 A 6 GLN A 132 ARG A 134 1 N ALA A 133 O GLU A 162
SHEET 1 B 6 VAL A 233 THR A 235 0
SHEET 2 B 6 PRO A 205 VAL A 209 1 N VAL A 209 O VAL A 234
SHEET 3 B 6 GLY A 272 LEU A 276 1 O PHE A 274 N MET A 208
SHEET 4 B 6 THR A 297 PHE A 301 1 O ILE A 298 N LEU A 273
SHEET 5 B 6 ALA A 304 LEU A 307 -1 O THR A 306 N HIS A 299
SHEET 6 B 6 HIS A 310 ALA A 313 -1 O TYR A 312 N VAL A 305
SHEET 1 C 6 LEU A 395 MET A 396 0
SHEET 2 C 6 LEU A 375 ALA A 378 1 N ILE A 376 O MET A 396
SHEET 3 C 6 ILE A 423 GLY A 428 1 O VAL A 426 N ALA A 377
SHEET 4 C 6 ILE A 450 ASN A 455 1 O ILE A 450 N THR A 425
SHEET 5 C 6 GLN A 514 MET A 519 1 O GLN A 514 N VAL A 451
SHEET 6 C 6 ASP A 489 VAL A 493 1 N VAL A 491 O GLU A 517
SHEET 1 D 2 MET B 1 LYS B 2 0
SHEET 2 D 2 GLU B 171 VAL B 172 -1 O VAL B 172 N MET B 1
SHEET 1 E 6 LEU B 42 THR B 44 0
SHEET 2 E 6 MET B 19 GLY B 21 1 N MET B 19 O HIS B 43
SHEET 3 E 6 GLY B 66 VAL B 70 1 O ALA B 69 N PHE B 20
SHEET 4 E 6 VAL B 93 ALA B 99 1 O VAL B 94 N GLY B 66
SHEET 5 E 6 VAL B 159 PRO B 164 1 O VAL B 159 N VAL B 95
SHEET 6 E 6 GLN B 132 ARG B 134 1 N ALA B 133 O GLU B 162
SHEET 1 F 6 VAL B 233 THR B 235 0
SHEET 2 F 6 PRO B 205 VAL B 209 1 N VAL B 209 O VAL B 234
SHEET 3 F 6 GLY B 272 LEU B 276 1 O PHE B 274 N MET B 208
SHEET 4 F 6 ILE B 298 PHE B 301 1 O ILE B 298 N LEU B 273
SHEET 5 F 6 ALA B 304 LEU B 307 -1 O THR B 306 N HIS B 299
SHEET 6 F 6 HIS B 310 TYR B 312 -1 O TYR B 312 N VAL B 305
SHEET 1 G 6 LEU B 395 MET B 396 0
SHEET 2 G 6 LEU B 375 ALA B 378 1 N ILE B 376 O MET B 396
SHEET 3 G 6 ILE B 423 GLY B 428 1 O LEU B 424 N ALA B 377
SHEET 4 G 6 ILE B 450 ASN B 455 1 O ILE B 450 N THR B 425
SHEET 5 G 6 GLN B 514 MET B 519 1 O GLN B 514 N VAL B 451
SHEET 6 G 6 ASP B 489 VAL B 493 1 N VAL B 491 O GLU B 517
LINK OD1 ASP A 429 MG MG A4002 1555 1555 2.05
LINK OD1 ASN A 456 MG MG A4002 1555 1555 2.08
LINK O SER A 458 MG MG A4002 1555 1555 2.12
LINK O2A TPP A2002 MG MG A4002 1555 1555 2.09
LINK O1B TPP A2002 MG MG A4002 1555 1555 2.08
LINK MG MG A4002 O HOH A4004 1555 1555 2.13
LINK OD1 ASP B 429 MG MG B4001 1555 1555 2.06
LINK OD1 ASN B 456 MG MG B4001 1555 1555 2.10
LINK O SER B 458 MG MG B4001 1555 1555 2.11
LINK O1B TPP B2001 MG MG B4001 1555 1555 2.06
LINK O2A TPP B2001 MG MG B4001 1555 1555 2.06
LINK MG MG B4001 O HOH B4005 1555 1555 2.12
SITE 1 AC1 5 ASP B 429 ASN B 456 SER B 458 TPP B2001
SITE 2 AC1 5 HOH B4005
SITE 1 AC2 5 ASP A 429 ASN A 456 SER A 458 TPP A2002
SITE 2 AC2 5 HOH A4004
SITE 1 AC3 5 CYS A 210 VAL A 211 THR A 236 ILE A 279
SITE 2 AC3 5 TYR A 400
SITE 1 AC4 5 CYS B 210 VAL B 211 THR B 236 ILE B 279
SITE 2 AC4 5 TYR B 400
SITE 1 AC5 22 PRO A 23 GLY A 24 GLU A 48 ASP B 382
SITE 2 AC5 22 ALA B 402 MET B 404 GLY B 428 ASP B 429
SITE 3 AC5 22 GLY B 430 ALA B 431 ASN B 456 SER B 458
SITE 4 AC5 22 TRP B 459 GLU B 460 MET B 461 LEU B 462
SITE 5 AC5 22 MG B4001 HOH B4005 HOH B4026 HOH B4052
SITE 6 AC5 22 HOH B4081 HOH B4450
SITE 1 AC6 22 ASP A 382 ALA A 402 MET A 404 GLY A 428
SITE 2 AC6 22 ASP A 429 GLY A 430 ALA A 431 ASN A 456
SITE 3 AC6 22 SER A 458 TRP A 459 GLU A 460 MET A 461
SITE 4 AC6 22 LEU A 462 MG A4002 HOH A4004 HOH A4006
SITE 5 AC6 22 HOH A4014 HOH A4091 HOH A4241 PRO B 23
SITE 6 AC6 22 GLY B 24 GLU B 48
SITE 1 AC7 9 SER B 63 THR B 64 PRO B 92 ARG B 153
SITE 2 AC7 9 SER B 156 ARG B 215 HOH B4043 HOH B4086
SITE 3 AC7 9 HOH B4248
SITE 1 AC8 7 SER A 63 THR A 64 PRO A 92 ARG A 153
SITE 2 AC8 7 SER A 156 HOH A4057 HOH A4112
SITE 1 AC9 6 HIS B 43 GLN B 415 CYS B 416 LEU B 445
SITE 2 AC9 6 GLY B 446 HOH B4039
CRYST1 99.411 179.032 120.925 90.00 90.00 90.00 C 2 2 21 16
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 0.010059 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005586 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008270 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
