HEADER LYASE 11-JAN-12 4D8W
TITLE SALMONELLA TYPHIMURIUM D-CYSTEINE DESULFHYDRASE SOAKED WITH D-CYS
TITLE 2 SHOWS PYRUVATE BOUND 4 A AWAY FROM ACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-CYSTEINE DESULFHYDRASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 4.4.1.15;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 90371;
SOURCE 4 GENE: DCYD, STM1953;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) ROSETTA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET C
KEYWDS FOLD TYPE II PLP-DEPENDENT ENZYME, TRYPTOPHAN SYNTHASE BETA SUBUNIT-
KEYWDS 2 LIKE PLP-DEPENDENT ENZYMES SUPERFAMILY, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.R.BHARATH,B.SHVETA,K.H.RAJESH,H.S.SAVITHRI,M.R.N.MURTHY
REVDAT 4 15-NOV-23 4D8W 1 ATOM
REVDAT 3 08-NOV-23 4D8W 1 REMARK SEQADV LINK
REVDAT 2 10-MAY-17 4D8W 1 SEQRES MODRES HET HETNAM
REVDAT 2 2 1 LINK HETATM
REVDAT 1 30-MAY-12 4D8W 0
JRNL AUTH S.R.BHARATH,S.BISHT,R.K.HARIJAN,H.S.SAVITHRI,M.R.N.MURTHY
JRNL TITL STRUCTURAL AND MUTATIONAL STUDIES ON SUBSTRATE SPECIFICITY
JRNL TITL 2 AND CATALYSIS OF SALMONELLA TYPHIMURIUM D-CYSTEINE
JRNL TITL 3 DESULFHYDRASE.
JRNL REF PLOS ONE V. 7 36267 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 22574144
JRNL DOI 10.1371/JOURNAL.PONE.0036267
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 80900
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4271
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5494
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 271
REMARK 3 BIN FREE R VALUE : 0.2860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9722
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 748
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.197
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.908
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10057 ; 0.005 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13732 ; 1.097 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1322 ; 5.426 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 389 ;38.325 ;24.833
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1539 ;12.702 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;18.734 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1615 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7593 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4D8W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI MIRROR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85215
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.34100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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: 4D8T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULPHATE, 15% (V/V)
REMARK 280 ETHYLENE GLYCOL, 0.1M HEPES, 0.2% BENZAMIDIDNE, PH 8.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 82.59500
REMARK 290 SMTRY3 2 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 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 -13
REMARK 465 ARG A -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 GLY A -3
REMARK 465 MET A -2
REMARK 465 ALA A -1
REMARK 465 SER A 0
REMARK 465 MET B -13
REMARK 465 ARG B -12
REMARK 465 GLY B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 GLY B -3
REMARK 465 MET B -2
REMARK 465 ALA B -1
REMARK 465 SER B 0
REMARK 465 VAL B 184
REMARK 465 GLY B 185
REMARK 465 MET C -13
REMARK 465 ARG C -12
REMARK 465 GLY C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 GLY C -3
REMARK 465 MET C -2
REMARK 465 ALA C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 PRO C 2
REMARK 465 LEU C 3
REMARK 465 HIS C 4
REMARK 465 HIS C 5
REMARK 465 LEU C 6
REMARK 465 MET D -13
REMARK 465 ARG D -12
REMARK 465 GLY D -11
REMARK 465 SER D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 GLY D -3
REMARK 465 MET D -2
REMARK 465 ALA D -1
REMARK 465 SER D 0
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 MET A 1 CG SD CE
REMARK 470 ARG A 8 CZ NH1 NH2
REMARK 470 ARG A 64 NE CZ NH1 NH2
REMARK 470 GLU A 182 CG CD OE1 OE2
REMARK 470 LYS A 302 CE NZ
REMARK 470 ASN A 305 CG OD1 ND2
REMARK 470 MET B 1 CG SD CE
REMARK 470 HIS B 4 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 8 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 13 CG CD OE1 OE2
REMARK 470 ARG B 64 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 145 NE CZ NH1 NH2
REMARK 470 GLU B 182 CG CD OE1 OE2
REMARK 470 THR C 7 OG1 CG2
REMARK 470 ARG C 8 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 64 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 142 CG CD1 CD2
REMARK 470 ARG C 145 NE CZ NH1 NH2
REMARK 470 GLU C 181 CD OE1 OE2
REMARK 470 GLU C 182 CG CD OE1 OE2
REMARK 470 ARG D 8 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 64 CZ NH1 NH2
REMARK 470 ARG D 145 CD NE CZ NH1 NH2
REMARK 470 GLU D 182 CG CD OE1 OE2
REMARK 470 GLU D 270 CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 HIS B 4 CB
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 182 12.17 57.65
REMARK 500 ALA A 196 -11.27 92.15
REMARK 500 SER A 221 -18.19 -143.20
REMARK 500 TYR A 287 -70.74 -113.06
REMARK 500 ASN B 113 -168.57 -100.89
REMARK 500 ALA B 196 -13.20 91.46
REMARK 500 SER B 221 -18.97 -144.97
REMARK 500 TYR B 287 -76.03 -118.45
REMARK 500 THR C 43 138.11 -32.01
REMARK 500 SER C 161 52.12 -92.63
REMARK 500 GLU C 182 10.57 58.72
REMARK 500 ALA C 196 -15.38 88.84
REMARK 500 SER C 221 -24.45 -144.03
REMARK 500 TYR C 287 -71.56 -114.67
REMARK 500 ALA D 46 57.99 39.74
REMARK 500 ALA D 196 -13.84 89.94
REMARK 500 SER D 221 -18.96 -143.51
REMARK 500 TYR D 287 -72.39 -114.99
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 CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4D8T RELATED DB: PDB
REMARK 900 SALMONELLA TYPHIMURIUM D-CYSTEINE DESULFHYDRASE AT 2.2A
REMARK 900 RELATED ID: 4D8U RELATED DB: PDB
REMARK 900 SALMONELLA TYPHIMURIUM D-CYSTEINE DESULFHYDRASE AT 3.3 A WITH 8
REMARK 900 PROTOMERS IN THE ASYMMETRIC UNIT
REMARK 900 RELATED ID: 4D92 RELATED DB: PDB
REMARK 900 SALMONELLA TYPHIMURIUM D-CYSTEINE DESULFHYDRASE SOAKED WITH BETA-
REMARK 900 CHLORO-D-ALANINE REVEALED PYRUVATE BOUND AT 4 A AWAY FROM THE
REMARK 900 ACTIVE SITE
REMARK 900 RELATED ID: 4D96 RELATED DB: PDB
REMARK 900 SALMONELLA TYPHIMURIUM D-CYSTEINE DESULFHYDRASE COMPLEXED WITH
REMARK 900 AMINO CARBOXY CYCLOPROPANE (ACC)
REMARK 900 RELATED ID: 4D97 RELATED DB: PDB
REMARK 900 SALMONELLA TYPHIMURIUM D-CYSTEINE DESULFHYDRASE COMPLEXED WITH D-
REMARK 900 SERINE; D-SERINE IS BOUND NON-COVALENTLY AT THE ACTIVE SITE
REMARK 900 RELATED ID: 4D99 RELATED DB: PDB
REMARK 900 RELATED ID: 4D9B RELATED DB: PDB
REMARK 900 RELATED ID: 4D9C RELATED DB: PDB
REMARK 900 RELATED ID: 4D9E RELATED DB: PDB
REMARK 900 RELATED ID: 4D9F RELATED DB: PDB
DBREF 4D8W A 1 328 UNP Q8ZNT7 DCYD_SALTY 1 328
DBREF 4D8W B 1 328 UNP Q8ZNT7 DCYD_SALTY 1 328
DBREF 4D8W C 1 328 UNP Q8ZNT7 DCYD_SALTY 1 328
DBREF 4D8W D 1 328 UNP Q8ZNT7 DCYD_SALTY 1 328
SEQADV 4D8W MET A -13 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W ARG A -12 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W GLY A -11 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W SER A -10 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS A -9 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS A -8 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS A -7 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS A -6 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS A -5 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS A -4 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W GLY A -3 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W MET A -2 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W ALA A -1 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W SER A 0 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W MET B -13 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W ARG B -12 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W GLY B -11 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W SER B -10 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS B -9 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS B -8 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS B -7 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS B -6 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS B -5 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS B -4 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W GLY B -3 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W MET B -2 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W ALA B -1 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W SER B 0 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W MET C -13 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W ARG C -12 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W GLY C -11 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W SER C -10 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS C -9 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS C -8 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS C -7 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS C -6 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS C -5 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS C -4 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W GLY C -3 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W MET C -2 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W ALA C -1 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W SER C 0 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W MET D -13 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W ARG D -12 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W GLY D -11 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W SER D -10 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS D -9 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS D -8 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS D -7 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS D -6 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS D -5 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W HIS D -4 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W GLY D -3 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W MET D -2 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W ALA D -1 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8W SER D 0 UNP Q8ZNT7 EXPRESSION TAG
SEQRES 1 A 342 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 A 342 SER MET PRO LEU HIS HIS LEU THR ARG PHE PRO ARG LEU
SEQRES 3 A 342 GLU PHE ILE GLY ALA PRO THR PRO LEU GLU TYR LEU PRO
SEQRES 4 A 342 ARG LEU SER ASP TYR LEU GLY ARG GLU ILE TYR ILE LYS
SEQRES 5 A 342 ARG ASP ASP VAL THR PRO ILE ALA MET GLY GLY ASN LLP
SEQRES 6 A 342 LEU ARG LYS LEU GLU PHE LEU VAL ALA ASP ALA LEU ARG
SEQRES 7 A 342 GLU GLY ALA ASP THR LEU ILE THR ALA GLY ALA ILE GLN
SEQRES 8 A 342 SER ASN HIS VAL ARG GLN THR ALA ALA VAL ALA ALA LYS
SEQRES 9 A 342 LEU GLY LEU HIS CYS VAL ALA LEU LEU GLU ASN PRO ILE
SEQRES 10 A 342 GLY THR THR ALA GLU ASN TYR LEU THR ASN GLY ASN ARG
SEQRES 11 A 342 LEU LEU LEU ASP LEU PHE ASN THR GLN ILE GLU MET CYS
SEQRES 12 A 342 ASP ALA LEU THR ASP PRO ASP ALA GLN LEU GLN THR LEU
SEQRES 13 A 342 ALA THR ARG ILE GLU ALA GLN GLY PHE ARG PRO TYR VAL
SEQRES 14 A 342 ILE PRO VAL GLY GLY SER SER ALA LEU GLY ALA MET GLY
SEQRES 15 A 342 TYR VAL GLU SER ALA LEU GLU ILE ALA GLN GLN CYS GLU
SEQRES 16 A 342 GLU VAL VAL GLY LEU SER SER VAL VAL VAL ALA SER GLY
SEQRES 17 A 342 SER ALA GLY THR HIS ALA GLY LEU ALA VAL GLY LEU GLU
SEQRES 18 A 342 HIS LEU MET PRO ASP VAL GLU LEU ILE GLY VAL THR VAL
SEQRES 19 A 342 SER ARG SER VAL ALA GLU GLN LYS PRO LYS VAL ILE ALA
SEQRES 20 A 342 LEU GLN GLN ALA ILE ALA GLY GLN LEU ALA LEU THR ALA
SEQRES 21 A 342 THR ALA ASP ILE HIS LEU TRP ASP ASP TYR PHE ALA PRO
SEQRES 22 A 342 GLY TYR GLY VAL PRO ASN ASP ALA GLY MET GLU ALA VAL
SEQRES 23 A 342 LYS LEU LEU ALA SER LEU GLU GLY VAL LEU LEU ASP PRO
SEQRES 24 A 342 VAL TYR THR GLY LYS ALA MET ALA GLY LEU ILE ASP GLY
SEQRES 25 A 342 ILE SER GLN LYS ARG PHE ASN ASP ASP GLY PRO ILE LEU
SEQRES 26 A 342 PHE ILE HIS THR GLY GLY ALA PRO ALA LEU PHE ALA TYR
SEQRES 27 A 342 HIS PRO HIS VAL
SEQRES 1 B 342 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 B 342 SER MET PRO LEU HIS HIS LEU THR ARG PHE PRO ARG LEU
SEQRES 3 B 342 GLU PHE ILE GLY ALA PRO THR PRO LEU GLU TYR LEU PRO
SEQRES 4 B 342 ARG LEU SER ASP TYR LEU GLY ARG GLU ILE TYR ILE LYS
SEQRES 5 B 342 ARG ASP ASP VAL THR PRO ILE ALA MET GLY GLY ASN LLP
SEQRES 6 B 342 LEU ARG LYS LEU GLU PHE LEU VAL ALA ASP ALA LEU ARG
SEQRES 7 B 342 GLU GLY ALA ASP THR LEU ILE THR ALA GLY ALA ILE GLN
SEQRES 8 B 342 SER ASN HIS VAL ARG GLN THR ALA ALA VAL ALA ALA LYS
SEQRES 9 B 342 LEU GLY LEU HIS CYS VAL ALA LEU LEU GLU ASN PRO ILE
SEQRES 10 B 342 GLY THR THR ALA GLU ASN TYR LEU THR ASN GLY ASN ARG
SEQRES 11 B 342 LEU LEU LEU ASP LEU PHE ASN THR GLN ILE GLU MET CYS
SEQRES 12 B 342 ASP ALA LEU THR ASP PRO ASP ALA GLN LEU GLN THR LEU
SEQRES 13 B 342 ALA THR ARG ILE GLU ALA GLN GLY PHE ARG PRO TYR VAL
SEQRES 14 B 342 ILE PRO VAL GLY GLY SER SER ALA LEU GLY ALA MET GLY
SEQRES 15 B 342 TYR VAL GLU SER ALA LEU GLU ILE ALA GLN GLN CYS GLU
SEQRES 16 B 342 GLU VAL VAL GLY LEU SER SER VAL VAL VAL ALA SER GLY
SEQRES 17 B 342 SER ALA GLY THR HIS ALA GLY LEU ALA VAL GLY LEU GLU
SEQRES 18 B 342 HIS LEU MET PRO ASP VAL GLU LEU ILE GLY VAL THR VAL
SEQRES 19 B 342 SER ARG SER VAL ALA GLU GLN LYS PRO LYS VAL ILE ALA
SEQRES 20 B 342 LEU GLN GLN ALA ILE ALA GLY GLN LEU ALA LEU THR ALA
SEQRES 21 B 342 THR ALA ASP ILE HIS LEU TRP ASP ASP TYR PHE ALA PRO
SEQRES 22 B 342 GLY TYR GLY VAL PRO ASN ASP ALA GLY MET GLU ALA VAL
SEQRES 23 B 342 LYS LEU LEU ALA SER LEU GLU GLY VAL LEU LEU ASP PRO
SEQRES 24 B 342 VAL TYR THR GLY LYS ALA MET ALA GLY LEU ILE ASP GLY
SEQRES 25 B 342 ILE SER GLN LYS ARG PHE ASN ASP ASP GLY PRO ILE LEU
SEQRES 26 B 342 PHE ILE HIS THR GLY GLY ALA PRO ALA LEU PHE ALA TYR
SEQRES 27 B 342 HIS PRO HIS VAL
SEQRES 1 C 342 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 C 342 SER MET PRO LEU HIS HIS LEU THR ARG PHE PRO ARG LEU
SEQRES 3 C 342 GLU PHE ILE GLY ALA PRO THR PRO LEU GLU TYR LEU PRO
SEQRES 4 C 342 ARG LEU SER ASP TYR LEU GLY ARG GLU ILE TYR ILE LYS
SEQRES 5 C 342 ARG ASP ASP VAL THR PRO ILE ALA MET GLY GLY ASN LLP
SEQRES 6 C 342 LEU ARG LYS LEU GLU PHE LEU VAL ALA ASP ALA LEU ARG
SEQRES 7 C 342 GLU GLY ALA ASP THR LEU ILE THR ALA GLY ALA ILE GLN
SEQRES 8 C 342 SER ASN HIS VAL ARG GLN THR ALA ALA VAL ALA ALA LYS
SEQRES 9 C 342 LEU GLY LEU HIS CYS VAL ALA LEU LEU GLU ASN PRO ILE
SEQRES 10 C 342 GLY THR THR ALA GLU ASN TYR LEU THR ASN GLY ASN ARG
SEQRES 11 C 342 LEU LEU LEU ASP LEU PHE ASN THR GLN ILE GLU MET CYS
SEQRES 12 C 342 ASP ALA LEU THR ASP PRO ASP ALA GLN LEU GLN THR LEU
SEQRES 13 C 342 ALA THR ARG ILE GLU ALA GLN GLY PHE ARG PRO TYR VAL
SEQRES 14 C 342 ILE PRO VAL GLY GLY SER SER ALA LEU GLY ALA MET GLY
SEQRES 15 C 342 TYR VAL GLU SER ALA LEU GLU ILE ALA GLN GLN CYS GLU
SEQRES 16 C 342 GLU VAL VAL GLY LEU SER SER VAL VAL VAL ALA SER GLY
SEQRES 17 C 342 SER ALA GLY THR HIS ALA GLY LEU ALA VAL GLY LEU GLU
SEQRES 18 C 342 HIS LEU MET PRO ASP VAL GLU LEU ILE GLY VAL THR VAL
SEQRES 19 C 342 SER ARG SER VAL ALA GLU GLN LYS PRO LYS VAL ILE ALA
SEQRES 20 C 342 LEU GLN GLN ALA ILE ALA GLY GLN LEU ALA LEU THR ALA
SEQRES 21 C 342 THR ALA ASP ILE HIS LEU TRP ASP ASP TYR PHE ALA PRO
SEQRES 22 C 342 GLY TYR GLY VAL PRO ASN ASP ALA GLY MET GLU ALA VAL
SEQRES 23 C 342 LYS LEU LEU ALA SER LEU GLU GLY VAL LEU LEU ASP PRO
SEQRES 24 C 342 VAL TYR THR GLY LYS ALA MET ALA GLY LEU ILE ASP GLY
SEQRES 25 C 342 ILE SER GLN LYS ARG PHE ASN ASP ASP GLY PRO ILE LEU
SEQRES 26 C 342 PHE ILE HIS THR GLY GLY ALA PRO ALA LEU PHE ALA TYR
SEQRES 27 C 342 HIS PRO HIS VAL
SEQRES 1 D 342 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA
SEQRES 2 D 342 SER MET PRO LEU HIS HIS LEU THR ARG PHE PRO ARG LEU
SEQRES 3 D 342 GLU PHE ILE GLY ALA PRO THR PRO LEU GLU TYR LEU PRO
SEQRES 4 D 342 ARG LEU SER ASP TYR LEU GLY ARG GLU ILE TYR ILE LYS
SEQRES 5 D 342 ARG ASP ASP VAL THR PRO ILE ALA MET GLY GLY ASN LLP
SEQRES 6 D 342 LEU ARG LYS LEU GLU PHE LEU VAL ALA ASP ALA LEU ARG
SEQRES 7 D 342 GLU GLY ALA ASP THR LEU ILE THR ALA GLY ALA ILE GLN
SEQRES 8 D 342 SER ASN HIS VAL ARG GLN THR ALA ALA VAL ALA ALA LYS
SEQRES 9 D 342 LEU GLY LEU HIS CYS VAL ALA LEU LEU GLU ASN PRO ILE
SEQRES 10 D 342 GLY THR THR ALA GLU ASN TYR LEU THR ASN GLY ASN ARG
SEQRES 11 D 342 LEU LEU LEU ASP LEU PHE ASN THR GLN ILE GLU MET CYS
SEQRES 12 D 342 ASP ALA LEU THR ASP PRO ASP ALA GLN LEU GLN THR LEU
SEQRES 13 D 342 ALA THR ARG ILE GLU ALA GLN GLY PHE ARG PRO TYR VAL
SEQRES 14 D 342 ILE PRO VAL GLY GLY SER SER ALA LEU GLY ALA MET GLY
SEQRES 15 D 342 TYR VAL GLU SER ALA LEU GLU ILE ALA GLN GLN CYS GLU
SEQRES 16 D 342 GLU VAL VAL GLY LEU SER SER VAL VAL VAL ALA SER GLY
SEQRES 17 D 342 SER ALA GLY THR HIS ALA GLY LEU ALA VAL GLY LEU GLU
SEQRES 18 D 342 HIS LEU MET PRO ASP VAL GLU LEU ILE GLY VAL THR VAL
SEQRES 19 D 342 SER ARG SER VAL ALA GLU GLN LYS PRO LYS VAL ILE ALA
SEQRES 20 D 342 LEU GLN GLN ALA ILE ALA GLY GLN LEU ALA LEU THR ALA
SEQRES 21 D 342 THR ALA ASP ILE HIS LEU TRP ASP ASP TYR PHE ALA PRO
SEQRES 22 D 342 GLY TYR GLY VAL PRO ASN ASP ALA GLY MET GLU ALA VAL
SEQRES 23 D 342 LYS LEU LEU ALA SER LEU GLU GLY VAL LEU LEU ASP PRO
SEQRES 24 D 342 VAL TYR THR GLY LYS ALA MET ALA GLY LEU ILE ASP GLY
SEQRES 25 D 342 ILE SER GLN LYS ARG PHE ASN ASP ASP GLY PRO ILE LEU
SEQRES 26 D 342 PHE ILE HIS THR GLY GLY ALA PRO ALA LEU PHE ALA TYR
SEQRES 27 D 342 HIS PRO HIS VAL
MODRES 4D8W LLP A 51 LYS
MODRES 4D8W LLP B 51 LYS
MODRES 4D8W LLP C 51 LYS
MODRES 4D8W LLP D 51 LYS
HET LLP A 51 24
HET LLP B 51 24
HET LLP C 51 24
HET LLP D 51 24
HET CL A 401 1
HET BEN A 402 9
HET PYR A 403 6
HET SO4 A 404 5
HET BEN B 401 9
HET EDO B 402 4
HET SO4 B 403 5
HET EDO C 401 4
HET SO4 C 402 5
HET PYR C 403 6
HET BEN D 401 9
HET PYR D 402 6
HET SO4 D 403 5
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETNAM CL CHLORIDE ION
HETNAM BEN BENZAMIDINE
HETNAM PYR PYRUVIC ACID
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 LLP 4(C14 H22 N3 O7 P)
FORMUL 5 CL CL 1-
FORMUL 6 BEN 3(C7 H8 N2)
FORMUL 7 PYR 3(C3 H4 O3)
FORMUL 8 SO4 4(O4 S 2-)
FORMUL 10 EDO 2(C2 H6 O2)
FORMUL 18 HOH *748(H2 O)
HELIX 1 1 LEU A 3 PHE A 9 5 7
HELIX 2 2 LEU A 24 GLY A 32 1 9
HELIX 3 3 ASN A 50 GLU A 65 1 16
HELIX 4 4 SER A 78 GLY A 92 1 15
HELIX 5 5 ALA A 107 ASN A 113 1 7
HELIX 6 6 ASN A 113 PHE A 122 1 10
HELIX 7 7 ASP A 134 GLN A 149 1 16
HELIX 8 8 PRO A 157 SER A 161 5 5
HELIX 9 9 SER A 162 GLU A 181 1 20
HELIX 10 10 ALA A 196 MET A 210 1 15
HELIX 11 11 SER A 223 LEU A 242 1 20
HELIX 12 12 ASN A 265 GLY A 280 1 16
HELIX 13 13 TYR A 287 GLN A 301 1 15
HELIX 14 14 PRO A 319 HIS A 325 1 7
HELIX 15 15 LEU B 3 PHE B 9 5 7
HELIX 16 16 LEU B 24 GLY B 32 1 9
HELIX 17 17 ASN B 50 GLU B 65 1 16
HELIX 18 18 SER B 78 GLY B 92 1 15
HELIX 19 19 ALA B 107 ASN B 113 1 7
HELIX 20 20 ASN B 113 PHE B 122 1 10
HELIX 21 21 ASP B 134 GLN B 149 1 16
HELIX 22 22 PRO B 157 SER B 161 5 5
HELIX 23 23 ALA B 166 CYS B 180 1 15
HELIX 24 24 ALA B 196 MET B 210 1 15
HELIX 25 25 SER B 223 LEU B 242 1 20
HELIX 26 26 ASN B 265 GLY B 280 1 16
HELIX 27 27 TYR B 287 GLN B 301 1 15
HELIX 28 28 GLY B 317 PRO B 319 5 3
HELIX 29 29 ALA B 320 HIS B 325 1 6
HELIX 30 30 LEU C 24 GLY C 32 1 9
HELIX 31 31 ASN C 50 GLU C 65 1 16
HELIX 32 32 SER C 78 LEU C 91 1 14
HELIX 33 33 ALA C 107 ASN C 113 1 7
HELIX 34 34 ASN C 113 PHE C 122 1 10
HELIX 35 35 ASP C 134 GLN C 149 1 16
HELIX 36 36 PRO C 157 SER C 161 5 5
HELIX 37 37 ALA C 166 GLU C 181 1 16
HELIX 38 38 ALA C 196 MET C 210 1 15
HELIX 39 39 SER C 223 ALA C 243 1 21
HELIX 40 40 ASN C 265 GLY C 280 1 16
HELIX 41 41 TYR C 287 GLN C 301 1 15
HELIX 42 42 PRO C 319 HIS C 325 1 7
HELIX 43 43 LEU D 3 PHE D 9 5 7
HELIX 44 44 LEU D 24 GLY D 32 1 9
HELIX 45 45 ASN D 50 GLU D 65 1 16
HELIX 46 46 SER D 78 LEU D 91 1 14
HELIX 47 47 ALA D 107 ASN D 113 1 7
HELIX 48 48 ASN D 113 PHE D 122 1 10
HELIX 49 49 ASP D 134 GLN D 149 1 16
HELIX 50 50 PRO D 157 SER D 161 5 5
HELIX 51 51 SER D 162 CYS D 180 1 19
HELIX 52 52 GLU D 181 VAL D 183 5 3
HELIX 53 53 ALA D 196 MET D 210 1 15
HELIX 54 54 SER D 223 LEU D 242 1 20
HELIX 55 55 ASN D 265 GLY D 280 1 16
HELIX 56 56 TYR D 287 GLN D 301 1 15
HELIX 57 57 PRO D 319 HIS D 325 1 7
SHEET 1 A 6 LEU A 21 TYR A 23 0
SHEET 2 A 6 ILE A 35 ARG A 39 -1 O ILE A 37 N GLU A 22
SHEET 3 A 6 ILE A 310 HIS A 314 1 O PHE A 312 N LYS A 38
SHEET 4 A 6 SER A 188 SER A 193 1 N VAL A 190 O ILE A 313
SHEET 5 A 6 GLU A 214 THR A 219 1 O ILE A 216 N VAL A 189
SHEET 6 A 6 HIS A 251 TRP A 253 1 O HIS A 251 N GLY A 217
SHEET 1 B 4 GLN A 125 MET A 128 0
SHEET 2 B 4 HIS A 94 GLU A 100 1 N ALA A 97 O GLU A 127
SHEET 3 B 4 THR A 69 ALA A 75 1 N LEU A 70 O HIS A 94
SHEET 4 B 4 PRO A 153 VAL A 155 1 O TYR A 154 N ILE A 71
SHEET 1 C 6 LEU B 21 TYR B 23 0
SHEET 2 C 6 ILE B 35 ARG B 39 -1 O ILE B 37 N GLU B 22
SHEET 3 C 6 ILE B 310 HIS B 314 1 O PHE B 312 N TYR B 36
SHEET 4 C 6 SER B 188 SER B 193 1 N VAL B 190 O LEU B 311
SHEET 5 C 6 GLU B 214 THR B 219 1 O ILE B 216 N VAL B 189
SHEET 6 C 6 HIS B 251 TRP B 253 1 O HIS B 251 N GLY B 217
SHEET 1 D 4 GLN B 125 MET B 128 0
SHEET 2 D 4 HIS B 94 GLU B 100 1 N ALA B 97 O GLN B 125
SHEET 3 D 4 THR B 69 ALA B 75 1 N LEU B 70 O VAL B 96
SHEET 4 D 4 PRO B 153 VAL B 155 1 O TYR B 154 N ILE B 71
SHEET 1 E 6 LEU C 21 TYR C 23 0
SHEET 2 E 6 ILE C 35 ARG C 39 -1 O ILE C 37 N GLU C 22
SHEET 3 E 6 ILE C 310 HIS C 314 1 O ILE C 310 N TYR C 36
SHEET 4 E 6 SER C 188 SER C 193 1 N VAL C 190 O ILE C 313
SHEET 5 E 6 GLU C 214 THR C 219 1 O ILE C 216 N VAL C 189
SHEET 6 E 6 HIS C 251 TRP C 253 1 O TRP C 253 N GLY C 217
SHEET 1 F 4 GLN C 125 MET C 128 0
SHEET 2 F 4 HIS C 94 GLU C 100 1 N ALA C 97 O GLU C 127
SHEET 3 F 4 THR C 69 ALA C 75 1 N LEU C 70 O HIS C 94
SHEET 4 F 4 PRO C 153 VAL C 155 1 O TYR C 154 N ILE C 71
SHEET 1 G 6 LEU D 21 TYR D 23 0
SHEET 2 G 6 ILE D 35 ARG D 39 -1 O ILE D 37 N GLU D 22
SHEET 3 G 6 ILE D 310 HIS D 314 1 O PHE D 312 N TYR D 36
SHEET 4 G 6 SER D 188 SER D 193 1 N VAL D 190 O ILE D 313
SHEET 5 G 6 GLU D 214 THR D 219 1 O ILE D 216 N VAL D 189
SHEET 6 G 6 LEU D 252 TRP D 253 1 O TRP D 253 N GLY D 217
SHEET 1 H 4 GLN D 125 MET D 128 0
SHEET 2 H 4 HIS D 94 GLU D 100 1 N ALA D 97 O GLU D 127
SHEET 3 H 4 THR D 69 ALA D 75 1 N LEU D 70 O HIS D 94
SHEET 4 H 4 PRO D 153 VAL D 155 1 O TYR D 154 N ILE D 71
LINK C ASN A 50 N LLP A 51 1555 1555 1.33
LINK C LLP A 51 N LEU A 52 1555 1555 1.33
LINK C ASN B 50 N LLP B 51 1555 1555 1.33
LINK C LLP B 51 N LEU B 52 1555 1555 1.33
LINK C ASN C 50 N LLP C 51 1555 1555 1.33
LINK C LLP C 51 N LEU C 52 1555 1555 1.33
LINK C ASN D 50 N LLP D 51 1555 1555 1.33
LINK C LLP D 51 N LEU D 52 1555 1555 1.33
CISPEP 1 ALA A 258 PRO A 259 0 6.88
CISPEP 2 HIS A 325 PRO A 326 0 -2.41
CISPEP 3 ALA B 258 PRO B 259 0 8.59
CISPEP 4 HIS B 325 PRO B 326 0 -1.09
CISPEP 5 ALA C 258 PRO C 259 0 5.97
CISPEP 6 HIS C 325 PRO C 326 0 -2.06
CISPEP 7 ALA D 258 PRO D 259 0 7.23
CISPEP 8 HIS D 325 PRO D 326 0 -1.30
SITE 1 AC1 2 TYR A 30 BEN A 402
SITE 1 AC2 4 TYR A 30 LEU A 31 ILE A 296 CL A 401
SITE 1 AC3 5 SER A 195 SER A 221 ARG A 222 TYR A 287
SITE 2 AC3 5 HOH A 713
SITE 1 AC4 9 LLP A 51 SER A 78 ASN A 79 HIS A 80
SITE 2 AC4 9 TYR A 261 TYR A 287 HOH A 703 HOH A 713
SITE 3 AC4 9 HOH A 716
SITE 1 AC5 5 TYR B 30 LEU B 31 TYR C 30 LEU C 31
SITE 2 AC5 5 SER C 300
SITE 1 AC6 3 VAL B 224 ALA B 225 ASP B 254
SITE 1 AC7 9 LLP B 51 SER B 78 ASN B 79 HIS B 80
SITE 2 AC7 9 TYR B 261 TYR B 287 HOH B 512 HOH B 668
SITE 3 AC7 9 HOH B 675
SITE 1 AC8 7 PRO C 264 TYR C 324 HIS C 327 VAL C 328
SITE 2 AC8 7 HOH C 531 HOH C 554 HOH C 606
SITE 1 AC9 9 LLP C 51 SER C 78 ASN C 79 HIS C 80
SITE 2 AC9 9 TYR C 261 TYR C 287 HOH C 502 HOH C 528
SITE 3 AC9 9 HOH C 641
SITE 1 BC1 7 VAL C 158 GLY C 194 SER C 195 SER C 221
SITE 2 BC1 7 ARG C 222 TYR C 261 HOH C 640
SITE 1 BC2 3 TYR D 30 LEU D 31 ILE D 296
SITE 1 BC3 8 VAL D 158 GLY D 194 SER D 195 SER D 221
SITE 2 BC3 8 ARG D 222 TYR D 261 HOH D 517 HOH D 714
SITE 1 BC4 9 LLP D 51 SER D 78 ASN D 79 HIS D 80
SITE 2 BC4 9 TYR D 261 TYR D 287 HOH D 508 HOH D 517
SITE 3 BC4 9 HOH D 716
CRYST1 66.290 165.190 68.060 90.00 118.71 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015085 0.000000 0.008262 0.00000
SCALE2 0.000000 0.006054 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016752 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
