HEADER LYASE 11-JAN-12 4D8T
TITLE CRYSTAL STRUCTURE OF D-CYSTEINE DESULFHYDRASE FROM SALMONELLA
TITLE 2 TYPHIMURIUM AT 2.2 A RESOLUTION
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 06-DEC-23 4D8T 1 REMARK
REVDAT 3 08-NOV-23 4D8T 1 REMARK SEQADV LINK
REVDAT 2 10-MAY-17 4D8T 1 SEQRES MODRES HET HETNAM
REVDAT 2 2 1 HETATM
REVDAT 1 30-MAY-12 4D8T 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. 2.28 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) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 54711
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2926
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) : 2.29
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3638
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 191
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9678
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.381
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.245
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.618
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9969 ; 0.006 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13606 ; 1.171 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1306 ; 5.536 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 384 ;38.355 ;24.583
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1529 ;13.892 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;15.638 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1598 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7517 ; 0.005 ; 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 4D8T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070026.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-09
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 : 63892
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
REMARK 200 RESOLUTION RANGE LOW (A) : 60.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.20100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100
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 1J0B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULPHATE, 15% (V/V)
REMARK 280 ETHYLENE GLYCOL, 0.1M HEPES, 0.2% BENZAMIDINE, 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 82.72500
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: 4150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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: 4060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 MET B 1
REMARK 465 PRO B 2
REMARK 465 LEU B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 LEU B 6
REMARK 465 GLU B 181
REMARK 465 GLU B 182
REMARK 465 VAL B 183
REMARK 465 VAL B 184
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 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 CD NE CZ NH1 NH2
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 GLU B 108 CD OE1 OE2
REMARK 470 ARG B 145 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 178 OE1 NE2
REMARK 470 LEU C 6 CG CD1 CD2
REMARK 470 ARG C 8 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 181 CD OE1 OE2
REMARK 470 GLU C 182 CG CD OE1 OE2
REMARK 470 MET D 1 CG SD CE
REMARK 470 ARG D 8 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 64 CZ NH1 NH2
REMARK 470 ARG D 152 NE CZ NH1 NH2
REMARK 470 GLU D 171 CD OE1 OE2
REMARK 470 GLU D 182 CG CD OE1 OE2
REMARK 470 ASN D 305 CG OD1 ND2
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 GLU B 108 CG
REMARK 480 GLU B 127 CG CD OE1
REMARK 480 GLN B 178 CG CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 46 65.96 30.89
REMARK 500 ASN A 113 -163.76 -100.17
REMARK 500 GLU A 182 1.56 59.01
REMARK 500 ALA A 196 -2.79 94.55
REMARK 500 SER A 221 -16.29 -141.72
REMARK 500 TYR A 287 -71.59 -109.43
REMARK 500 ASP A 306 -152.33 -159.31
REMARK 500 ALA B 46 57.72 39.93
REMARK 500 ASN B 113 -164.93 -100.66
REMARK 500 ALA B 196 -14.24 91.21
REMARK 500 SER B 221 -15.03 -142.41
REMARK 500 TYR B 287 -81.22 -116.57
REMARK 500 ALA C 46 62.37 36.02
REMARK 500 GLU C 182 19.93 56.55
REMARK 500 VAL C 183 -52.02 -120.03
REMARK 500 ALA C 196 -16.72 92.96
REMARK 500 SER C 221 -22.26 -141.62
REMARK 500 TYR C 287 -77.34 -114.87
REMARK 500 VAL D 42 72.37 -107.49
REMARK 500 ALA D 46 68.37 29.38
REMARK 500 GLU D 182 -23.18 -174.32
REMARK 500 ALA D 196 -16.35 93.09
REMARK 500 ASP D 306 -153.53 -143.16
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN D 402
REMARK 900
REMARK 900 RELATED ENTRIES
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: 4D8W RELATED DB: PDB
REMARK 900 SALMONELLA TYPHIMURIUM D-CYSTEINE DESULFHYDRASE SOAKED WITH D-CYS
REMARK 900 REVEALED PYRUVATE BOUND AT 4 A AWAY FROM THE ACTIVE SITE
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 4D8T A 1 328 UNP Q8ZNT7 DCYD_SALTY 1 328
DBREF 4D8T B 1 328 UNP Q8ZNT7 DCYD_SALTY 1 328
DBREF 4D8T C 1 328 UNP Q8ZNT7 DCYD_SALTY 1 328
DBREF 4D8T D 1 328 UNP Q8ZNT7 DCYD_SALTY 1 328
SEQADV 4D8T MET A -13 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T ARG A -12 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T GLY A -11 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T SER A -10 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS A -9 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS A -8 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS A -7 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS A -6 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS A -5 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS A -4 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T GLY A -3 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T MET A -2 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T ALA A -1 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T SER A 0 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T MET B -13 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T ARG B -12 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T GLY B -11 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T SER B -10 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS B -9 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS B -8 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS B -7 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS B -6 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS B -5 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS B -4 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T GLY B -3 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T MET B -2 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T ALA B -1 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T SER B 0 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T MET C -13 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T ARG C -12 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T GLY C -11 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T SER C -10 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS C -9 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS C -8 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS C -7 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS C -6 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS C -5 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS C -4 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T GLY C -3 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T MET C -2 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T ALA C -1 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T SER C 0 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T MET D -13 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T ARG D -12 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T GLY D -11 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T SER D -10 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS D -9 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS D -8 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS D -7 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS D -6 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS D -5 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T HIS D -4 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T GLY D -3 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T MET D -2 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T ALA D -1 UNP Q8ZNT7 EXPRESSION TAG
SEQADV 4D8T 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 4D8T LLP A 51 LYS
MODRES 4D8T LLP B 51 LYS
MODRES 4D8T LLP C 51 LYS
MODRES 4D8T 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 SO4 A 401 5
HET CL A 402 1
HET BEN A 403 9
HET SO4 B 401 5
HET BEN B 402 9
HET BEN B 403 9
HET SO4 C 401 5
HET BEN C 402 9
HET SO4 D 401 5
HET BEN D 402 9
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 SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM BEN BENZAMIDINE
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP 4(C14 H22 N3 O7 P)
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 6 CL CL 1-
FORMUL 7 BEN 5(C7 H8 N2)
FORMUL 15 HOH *450(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 ALA A 318 HIS A 325 1 8
HELIX 15 15 LEU B 24 GLY B 32 1 9
HELIX 16 16 ASN B 50 GLU B 65 1 16
HELIX 17 17 SER B 78 GLY B 92 1 15
HELIX 18 18 ALA B 107 ASN B 113 1 7
HELIX 19 19 ASN B 113 PHE B 122 1 10
HELIX 20 20 ASP B 134 ALA B 148 1 15
HELIX 21 21 PRO B 157 SER B 161 5 5
HELIX 22 22 SER B 162 CYS B 180 1 19
HELIX 23 23 ALA B 196 MET B 210 1 15
HELIX 24 24 SER B 223 LEU B 242 1 20
HELIX 25 25 ASN B 265 GLY B 280 1 16
HELIX 26 26 TYR B 287 GLN B 301 1 15
HELIX 27 27 PRO B 319 HIS B 325 1 7
HELIX 28 28 LEU C 24 GLY C 32 1 9
HELIX 29 29 ASN C 50 GLU C 65 1 16
HELIX 30 30 SER C 78 GLY C 92 1 15
HELIX 31 31 ALA C 107 ASN C 113 1 7
HELIX 32 32 ASN C 113 PHE C 122 1 10
HELIX 33 33 ASP C 134 GLN C 149 1 16
HELIX 34 34 PRO C 157 SER C 161 5 5
HELIX 35 35 SER C 162 GLU C 181 1 20
HELIX 36 36 ALA C 196 MET C 210 1 15
HELIX 37 37 SER C 223 LEU C 242 1 20
HELIX 38 38 ASN C 265 GLY C 280 1 16
HELIX 39 39 TYR C 287 GLN C 301 1 15
HELIX 40 40 PRO C 319 HIS C 325 1 7
HELIX 41 41 LEU D 3 PHE D 9 5 7
HELIX 42 42 LEU D 24 GLY D 32 1 9
HELIX 43 43 ASN D 50 GLU D 65 1 16
HELIX 44 44 SER D 78 GLY D 92 1 15
HELIX 45 45 ALA D 107 ASN D 113 1 7
HELIX 46 46 ASN D 113 PHE D 122 1 10
HELIX 47 47 ASP D 134 GLN D 149 1 16
HELIX 48 48 PRO D 157 SER D 161 5 5
HELIX 49 49 SER D 162 CYS D 180 1 19
HELIX 50 50 ALA D 196 MET D 210 1 15
HELIX 51 51 SER D 223 LEU D 242 1 20
HELIX 52 52 ASN D 265 GLY D 280 1 16
HELIX 53 53 TYR D 287 GLN D 301 1 15
HELIX 54 54 ALA D 318 HIS D 325 1 8
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 ILE A 310 N TYR A 36
SHEET 4 A 6 SER A 188 SER A 193 1 N VAL A 190 O LEU A 311
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 TRP A 253 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 ILE B 310 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 GLU B 127
SHEET 3 D 4 THR B 69 ALA B 75 1 N LEU B 70 O HIS B 94
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 PHE C 312 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 LEU C 99 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 ILE D 310 N TYR D 36
SHEET 4 G 6 SER D 188 SER D 193 1 N SER D 188 O LEU D 311
SHEET 5 G 6 GLU D 214 THR D 219 1 O ILE D 216 N VAL D 189
SHEET 6 G 6 HIS D 251 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 1.34
CISPEP 1 ALA A 258 PRO A 259 0 5.14
CISPEP 2 HIS A 325 PRO A 326 0 -1.03
CISPEP 3 ALA B 258 PRO B 259 0 6.19
CISPEP 4 HIS B 325 PRO B 326 0 -0.45
CISPEP 5 ALA C 258 PRO C 259 0 5.97
CISPEP 6 HIS C 325 PRO C 326 0 -3.51
CISPEP 7 ALA D 258 PRO D 259 0 5.50
CISPEP 8 HIS D 325 PRO D 326 0 -1.27
SITE 1 AC1 8 LLP A 51 SER A 78 ASN A 79 HIS A 80
SITE 2 AC1 8 TYR A 261 TYR A 287 HOH A 532 HOH A 589
SITE 1 AC2 2 TYR A 30 BEN A 403
SITE 1 AC3 3 TYR A 30 LEU A 31 CL A 402
SITE 1 AC4 9 LLP B 51 SER B 78 ASN B 79 HIS B 80
SITE 2 AC4 9 TYR B 261 TYR B 287 HOH B 524 HOH B 531
SITE 3 AC4 9 HOH B 563
SITE 1 AC5 4 TYR B 30 LEU B 31 TYR C 30 LEU C 31
SITE 1 AC6 5 ASP B 266 ALA B 267 GLU B 270 ARG C 26
SITE 2 AC6 5 SER C 277
SITE 1 AC7 8 LLP C 51 SER C 78 ASN C 79 HIS C 80
SITE 2 AC7 8 TYR C 261 TYR C 287 HOH C 546 HOH C 563
SITE 1 AC8 6 ARG B 26 LEU B 274 SER B 277 LEU B 278
SITE 2 AC8 6 ALA C 267 GLU C 270
SITE 1 AC9 9 LLP D 51 SER D 78 ASN D 79 HIS D 80
SITE 2 AC9 9 TYR D 261 TYR D 287 HOH D 599 HOH D 600
SITE 3 AC9 9 HOH D 601
SITE 1 BC1 2 TYR D 30 LEU D 31
CRYST1 66.483 165.450 69.208 90.00 119.01 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 0.015041 0.000000 0.008341 0.00000
SCALE2 0.000000 0.006044 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016522 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
