HEADER LYASE 26-JUL-13 4LW4
TITLE STRUCTURAL CHANGES DURING CYSTEINE DESULFURASE CSDA AND SULFUR-
TITLE 2 ACCEPTOR CSDE INTERACTIONS PROVIDE INSIGHT INTO THE TRANS-
TITLE 3 PERSULFURATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE SULFINATE DESULFINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CSD;
COMPND 5 EC: 4.4.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CYSTEINE DESULFURATION PROTEIN CSDE;
COMPND 9 CHAIN: C, D;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B2810, CSDA, JW2781, YGDJ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 13 ORGANISM_TAXID: 714962;
SOURCE 14 STRAIN: IHE3034;
SOURCE 15 GENE: CSDE, ECOK1_3187;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CYSTEINE DESULFURASE, CSDA, SUFE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KIM,S.Y.PARK
REVDAT 4 08-NOV-23 4LW4 1 REMARK
REVDAT 3 24-AUG-22 4LW4 1 JRNL REMARK SEQADV LINK
REVDAT 2 21-AUG-13 4LW4 1 JRNL
REVDAT 1 07-AUG-13 4LW4 0
JRNL AUTH S.KIM,S.PARK
JRNL TITL STRUCTURAL CHANGES DURING CYSTEINE DESULFURASE CSDA AND
JRNL TITL 2 SULFUR ACCEPTOR CSDE INTERACTIONS PROVIDE INSIGHT INTO THE
JRNL TITL 3 TRANS-PERSULFURATION.
JRNL REF J.BIOL.CHEM. V. 288 27172 2013
JRNL REFN ESSN 1083-351X
JRNL PMID 23913692
JRNL DOI 10.1074/JBC.M113.480277
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 63955
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3406
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) : 4501
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.1810
REMARK 3 BIN FREE R VALUE SET COUNT : 218
REMARK 3 BIN FREE R VALUE : 0.2400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8137
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 685
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.61000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : -0.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.54000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.167
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.797
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8427 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11481 ; 1.807 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1092 ; 6.183 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 370 ;35.609 ;24.270
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1348 ;16.005 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 53 ;17.974 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1305 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6444 ; 0.010 ; 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): 5365 ; 1.111 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8563 ; 1.904 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3062 ; 3.305 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2906 ; 5.221 ; 4.500
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4LW4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000081159.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-12
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 : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67595
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 86.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 4LW2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% (W/V) POLYACRYLIC ACID 5100, 0.02M
REMARK 280 MGCL2, 0.1M HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 297K
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 38.43550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 ASN A 49
REMARK 465 VAL A 50
REMARK 465 HIS A 51
REMARK 465 ARG A 52
REMARK 465 SER A 53
REMARK 465 GLN A 54
REMARK 465 ASP A 401
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 ASP B 401
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ASN D 3
REMARK 465 PRO D 4
REMARK 465 GLN D 5
REMARK 465 PHE D 6
REMARK 465 ALA D 7
REMARK 465 CYS D 61
REMARK 465 GLN D 146
REMARK 465 VAL D 147
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG A 10 CG2 THR A 381 1.91
REMARK 500 OD1 ASP A 151 NH1 ARG A 181 2.04
REMARK 500 O LEU C 44 NH1 ARG C 89 2.17
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 LEU A 123 -56.86 -138.14
REMARK 500 VAL A 172 -63.29 -102.25
REMARK 500 LEU A 223 50.83 -97.48
REMARK 500 TRP A 245 -93.27 -99.16
REMARK 500 LYS A 250 -46.56 78.36
REMARK 500 HIS A 253 -67.79 -99.38
REMARK 500 ALA A 359 55.93 -146.28
REMARK 500 ALA B 19 151.09 -30.11
REMARK 500 SER B 53 -23.62 -145.57
REMARK 500 GLN B 54 53.89 -118.53
REMARK 500 LEU B 123 -56.41 -133.73
REMARK 500 LEU B 223 48.85 -97.85
REMARK 500 TRP B 245 -107.69 -102.61
REMARK 500 LYS B 250 -47.17 79.62
REMARK 500 HIS B 253 -72.93 -107.71
REMARK 500 ALA B 359 55.58 -141.96
REMARK 500 THR C 13 -75.47 -123.68
REMARK 500 ILE C 58 71.07 -100.51
REMARK 500 THR D 13 -81.50 -116.32
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 PLP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LW2 RELATED DB: PDB
REMARK 900 CYSTEINE DESULFURASE CSDA
DBREF 4LW4 A 1 401 UNP Q46925 CSDA_ECOLI 1 401
DBREF 4LW4 B 1 401 UNP Q46925 CSDA_ECOLI 1 401
DBREF 4LW4 C 1 147 UNP D5CZ88 D5CZ88_ECOKI 1 147
DBREF 4LW4 D 1 147 UNP D5CZ88 D5CZ88_ECOKI 1 147
SEQADV 4LW4 GLY A -2 UNP Q46925 EXPRESSION TAG
SEQADV 4LW4 SER A -1 UNP Q46925 EXPRESSION TAG
SEQADV 4LW4 HIS A 0 UNP Q46925 EXPRESSION TAG
SEQADV 4LW4 GLY B -2 UNP Q46925 EXPRESSION TAG
SEQADV 4LW4 SER B -1 UNP Q46925 EXPRESSION TAG
SEQADV 4LW4 HIS B 0 UNP Q46925 EXPRESSION TAG
SEQADV 4LW4 GLY C -2 UNP D5CZ88 EXPRESSION TAG
SEQADV 4LW4 SER C -1 UNP D5CZ88 EXPRESSION TAG
SEQADV 4LW4 HIS C 0 UNP D5CZ88 EXPRESSION TAG
SEQADV 4LW4 ASP C 49 UNP D5CZ88 GLU 49 ENGINEERED MUTATION
SEQADV 4LW4 GLY D -2 UNP D5CZ88 EXPRESSION TAG
SEQADV 4LW4 SER D -1 UNP D5CZ88 EXPRESSION TAG
SEQADV 4LW4 HIS D 0 UNP D5CZ88 EXPRESSION TAG
SEQADV 4LW4 ASP D 49 UNP D5CZ88 GLU 49 ENGINEERED MUTATION
SEQRES 1 A 404 GLY SER HIS MET ASN VAL PHE ASN PRO ALA GLN PHE ARG
SEQRES 2 A 404 ALA GLN PHE PRO ALA LEU GLN ASP ALA GLY VAL TYR LEU
SEQRES 3 A 404 ASP SER ALA ALA THR ALA LEU LYS PRO GLU ALA VAL VAL
SEQRES 4 A 404 GLU ALA THR GLN GLN PHE TYR SER LEU SER ALA GLY ASN
SEQRES 5 A 404 VAL HIS ARG SER GLN PHE ALA GLU ALA GLN ARG LEU THR
SEQRES 6 A 404 ALA ARG TYR GLU ALA ALA ARG GLU LYS VAL ALA GLN LEU
SEQRES 7 A 404 LEU ASN ALA PRO ASP ASP LYS THR ILE VAL TRP THR ARG
SEQRES 8 A 404 GLY THR THR GLU SER ILE ASN MET VAL ALA GLN CYS TYR
SEQRES 9 A 404 ALA ARG PRO ARG LEU GLN PRO GLY ASP GLU ILE ILE VAL
SEQRES 10 A 404 SER VAL ALA GLU HIS HIS ALA ASN LEU VAL PRO TRP LEU
SEQRES 11 A 404 MET VAL ALA GLN GLN THR GLY ALA LYS VAL VAL LYS LEU
SEQRES 12 A 404 PRO LEU ASN ALA GLN ARG LEU PRO ASP VAL ASP LEU LEU
SEQRES 13 A 404 PRO GLU LEU ILE THR PRO ARG SER ARG ILE LEU ALA LEU
SEQRES 14 A 404 GLY GLN MET SER ASN VAL THR GLY GLY CYS PRO ASP LEU
SEQRES 15 A 404 ALA ARG ALA ILE THR PHE ALA HIS SER ALA GLY MET VAL
SEQRES 16 A 404 VAL MET VAL ASP GLY ALA GLN GLY ALA VAL HIS PHE PRO
SEQRES 17 A 404 ALA ASP VAL GLN GLN LEU ASP ILE ASP PHE TYR ALA PHE
SEQRES 18 A 404 SER GLY HIS LYS LEU TYR GLY PRO THR GLY ILE GLY VAL
SEQRES 19 A 404 LEU TYR GLY LYS SER GLU LEU LEU GLU ALA MET SER PRO
SEQRES 20 A 404 TRP LEU GLY GLY GLY LYS MET VAL HIS GLU VAL SER PHE
SEQRES 21 A 404 ASP GLY PHE THR THR GLN SER ALA PRO TRP LYS LEU GLU
SEQRES 22 A 404 ALA GLY THR PRO ASN VAL ALA GLY VAL ILE GLY LEU SER
SEQRES 23 A 404 ALA ALA LEU GLU TRP LEU ALA ASP TYR ASP ILE ASN GLN
SEQRES 24 A 404 ALA GLU SER TRP SER ARG SER LEU ALA THR LEU ALA GLU
SEQRES 25 A 404 ASP ALA LEU ALA LYS ARG PRO GLY PHE ARG SER PHE ARG
SEQRES 26 A 404 CYS GLN ASP SER SER LEU LEU ALA PHE ASP PHE ALA GLY
SEQRES 27 A 404 VAL HIS HIS SER ASP MET VAL THR LEU LEU ALA GLU TYR
SEQRES 28 A 404 GLY ILE ALA LEU ARG ALA GLY GLN HIS CYS ALA GLN PRO
SEQRES 29 A 404 LEU LEU ALA GLU LEU GLY VAL THR GLY THR LEU ARG ALA
SEQRES 30 A 404 SER PHE ALA PRO TYR ASN THR LYS SER ASP VAL ASP ALA
SEQRES 31 A 404 LEU VAL ASN ALA VAL ASP ARG ALA LEU GLU LEU LEU VAL
SEQRES 32 A 404 ASP
SEQRES 1 B 404 GLY SER HIS MET ASN VAL PHE ASN PRO ALA GLN PHE ARG
SEQRES 2 B 404 ALA GLN PHE PRO ALA LEU GLN ASP ALA GLY VAL TYR LEU
SEQRES 3 B 404 ASP SER ALA ALA THR ALA LEU LYS PRO GLU ALA VAL VAL
SEQRES 4 B 404 GLU ALA THR GLN GLN PHE TYR SER LEU SER ALA GLY ASN
SEQRES 5 B 404 VAL HIS ARG SER GLN PHE ALA GLU ALA GLN ARG LEU THR
SEQRES 6 B 404 ALA ARG TYR GLU ALA ALA ARG GLU LYS VAL ALA GLN LEU
SEQRES 7 B 404 LEU ASN ALA PRO ASP ASP LYS THR ILE VAL TRP THR ARG
SEQRES 8 B 404 GLY THR THR GLU SER ILE ASN MET VAL ALA GLN CYS TYR
SEQRES 9 B 404 ALA ARG PRO ARG LEU GLN PRO GLY ASP GLU ILE ILE VAL
SEQRES 10 B 404 SER VAL ALA GLU HIS HIS ALA ASN LEU VAL PRO TRP LEU
SEQRES 11 B 404 MET VAL ALA GLN GLN THR GLY ALA LYS VAL VAL LYS LEU
SEQRES 12 B 404 PRO LEU ASN ALA GLN ARG LEU PRO ASP VAL ASP LEU LEU
SEQRES 13 B 404 PRO GLU LEU ILE THR PRO ARG SER ARG ILE LEU ALA LEU
SEQRES 14 B 404 GLY GLN MET SER ASN VAL THR GLY GLY CYS PRO ASP LEU
SEQRES 15 B 404 ALA ARG ALA ILE THR PHE ALA HIS SER ALA GLY MET VAL
SEQRES 16 B 404 VAL MET VAL ASP GLY ALA GLN GLY ALA VAL HIS PHE PRO
SEQRES 17 B 404 ALA ASP VAL GLN GLN LEU ASP ILE ASP PHE TYR ALA PHE
SEQRES 18 B 404 SER GLY HIS LYS LEU TYR GLY PRO THR GLY ILE GLY VAL
SEQRES 19 B 404 LEU TYR GLY LYS SER GLU LEU LEU GLU ALA MET SER PRO
SEQRES 20 B 404 TRP LEU GLY GLY GLY LYS MET VAL HIS GLU VAL SER PHE
SEQRES 21 B 404 ASP GLY PHE THR THR GLN SER ALA PRO TRP LYS LEU GLU
SEQRES 22 B 404 ALA GLY THR PRO ASN VAL ALA GLY VAL ILE GLY LEU SER
SEQRES 23 B 404 ALA ALA LEU GLU TRP LEU ALA ASP TYR ASP ILE ASN GLN
SEQRES 24 B 404 ALA GLU SER TRP SER ARG SER LEU ALA THR LEU ALA GLU
SEQRES 25 B 404 ASP ALA LEU ALA LYS ARG PRO GLY PHE ARG SER PHE ARG
SEQRES 26 B 404 CYS GLN ASP SER SER LEU LEU ALA PHE ASP PHE ALA GLY
SEQRES 27 B 404 VAL HIS HIS SER ASP MET VAL THR LEU LEU ALA GLU TYR
SEQRES 28 B 404 GLY ILE ALA LEU ARG ALA GLY GLN HIS CYS ALA GLN PRO
SEQRES 29 B 404 LEU LEU ALA GLU LEU GLY VAL THR GLY THR LEU ARG ALA
SEQRES 30 B 404 SER PHE ALA PRO TYR ASN THR LYS SER ASP VAL ASP ALA
SEQRES 31 B 404 LEU VAL ASN ALA VAL ASP ARG ALA LEU GLU LEU LEU VAL
SEQRES 32 B 404 ASP
SEQRES 1 C 150 GLY SER HIS MET THR ASN PRO GLN PHE ALA GLY HIS PRO
SEQRES 2 C 150 PHE GLY THR THR VAL THR ALA GLU THR LEU ARG ASN THR
SEQRES 3 C 150 PHE ALA PRO LEU THR GLN TRP GLU ASP LYS TYR ARG GLN
SEQRES 4 C 150 LEU ILE MET LEU GLY LYS GLN LEU PRO ALA LEU PRO ASP
SEQRES 5 C 150 GLU LEU LYS ALA GLN ALA LYS GLU ILE ALA GLY CYS GLU
SEQRES 6 C 150 ASN ARG VAL TRP LEU GLY TYR THR VAL ALA GLU ASN GLY
SEQRES 7 C 150 LYS MET HIS PHE PHE GLY ASP SER GLU GLY ARG ILE VAL
SEQRES 8 C 150 ARG GLY LEU LEU ALA VAL LEU LEU THR ALA VAL GLU GLY
SEQRES 9 C 150 LYS THR ALA ALA GLU LEU GLN ALA GLN SER PRO LEU ALA
SEQRES 10 C 150 LEU PHE ASP GLU LEU GLY LEU ARG ALA GLN LEU SER ALA
SEQRES 11 C 150 SER ARG SER GLN GLY LEU ASN ALA LEU SER GLU ALA ILE
SEQRES 12 C 150 ILE ALA ALA ALA LYS GLN VAL
SEQRES 1 D 150 GLY SER HIS MET THR ASN PRO GLN PHE ALA GLY HIS PRO
SEQRES 2 D 150 PHE GLY THR THR VAL THR ALA GLU THR LEU ARG ASN THR
SEQRES 3 D 150 PHE ALA PRO LEU THR GLN TRP GLU ASP LYS TYR ARG GLN
SEQRES 4 D 150 LEU ILE MET LEU GLY LYS GLN LEU PRO ALA LEU PRO ASP
SEQRES 5 D 150 GLU LEU LYS ALA GLN ALA LYS GLU ILE ALA GLY CYS GLU
SEQRES 6 D 150 ASN ARG VAL TRP LEU GLY TYR THR VAL ALA GLU ASN GLY
SEQRES 7 D 150 LYS MET HIS PHE PHE GLY ASP SER GLU GLY ARG ILE VAL
SEQRES 8 D 150 ARG GLY LEU LEU ALA VAL LEU LEU THR ALA VAL GLU GLY
SEQRES 9 D 150 LYS THR ALA ALA GLU LEU GLN ALA GLN SER PRO LEU ALA
SEQRES 10 D 150 LEU PHE ASP GLU LEU GLY LEU ARG ALA GLN LEU SER ALA
SEQRES 11 D 150 SER ARG SER GLN GLY LEU ASN ALA LEU SER GLU ALA ILE
SEQRES 12 D 150 ILE ALA ALA ALA LYS GLN VAL
HET PLP A 500 15
HET PLP B 500 15
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 5 PLP 2(C8 H10 N O6 P)
FORMUL 7 HOH *685(H2 O)
HELIX 1 1 ASN A 5 ALA A 11 1 7
HELIX 2 2 GLN A 12 PRO A 14 5 3
HELIX 3 3 ALA A 15 GLY A 20 1 6
HELIX 4 4 PRO A 32 SER A 44 1 13
HELIX 5 5 ALA A 56 ALA A 67 1 12
HELIX 6 6 ALA A 67 ASN A 77 1 11
HELIX 7 7 ASP A 80 LYS A 82 5 3
HELIX 8 8 GLY A 89 TYR A 101 1 13
HELIX 9 9 HIS A 119 ASN A 122 5 4
HELIX 10 10 LEU A 123 GLY A 134 1 12
HELIX 11 11 ASP A 149 ASP A 151 5 3
HELIX 12 12 LEU A 152 ILE A 157 1 6
HELIX 13 13 ASP A 178 ALA A 189 1 12
HELIX 14 14 GLN A 199 PHE A 204 1 6
HELIX 15 15 HIS A 221 LEU A 223 5 3
HELIX 16 16 LYS A 235 MET A 242 1 8
HELIX 17 17 PRO A 266 GLU A 270 5 5
HELIX 18 18 ASN A 275 ALA A 290 1 16
HELIX 19 19 ASP A 293 ALA A 313 1 21
HELIX 20 20 HIS A 337 TYR A 348 1 12
HELIX 21 21 ALA A 359 GLY A 367 1 9
HELIX 22 22 THR A 381 VAL A 400 1 20
HELIX 23 23 ASN B 5 GLN B 12 1 8
HELIX 24 24 PHE B 13 GLN B 17 5 5
HELIX 25 25 PRO B 32 LEU B 45 1 14
HELIX 26 26 GLN B 54 ASN B 77 1 24
HELIX 27 27 ASP B 80 LYS B 82 5 3
HELIX 28 28 GLY B 89 TYR B 101 1 13
HELIX 29 29 ALA B 102 LEU B 106 5 5
HELIX 30 30 HIS B 119 ASN B 122 5 4
HELIX 31 31 LEU B 123 GLY B 134 1 12
HELIX 32 32 ASP B 149 ASP B 151 5 3
HELIX 33 33 LEU B 152 ILE B 157 1 6
HELIX 34 34 ASP B 178 ALA B 189 1 12
HELIX 35 35 GLN B 199 PHE B 204 1 6
HELIX 36 36 ASP B 207 ASP B 212 1 6
HELIX 37 37 HIS B 221 LEU B 223 5 3
HELIX 38 38 LYS B 235 MET B 242 1 8
HELIX 39 39 PRO B 266 GLU B 270 5 5
HELIX 40 40 ASN B 275 ALA B 290 1 16
HELIX 41 41 ASP B 293 ALA B 313 1 21
HELIX 42 42 HIS B 337 TYR B 348 1 12
HELIX 43 43 ALA B 359 GLY B 367 1 9
HELIX 44 44 THR B 381 VAL B 400 1 20
HELIX 45 45 THR C 16 ALA C 25 1 10
HELIX 46 46 GLN C 29 LYS C 42 1 14
HELIX 47 47 PRO C 48 ALA C 53 1 6
HELIX 48 48 GLY C 85 GLU C 100 1 16
HELIX 49 49 THR C 103 GLN C 110 1 8
HELIX 50 50 LEU C 113 LEU C 119 1 7
HELIX 51 51 LEU C 125 ARG C 129 5 5
HELIX 52 52 SER C 130 VAL C 147 1 18
HELIX 53 53 THR D 16 ALA D 25 1 10
HELIX 54 54 GLN D 29 LYS D 42 1 14
HELIX 55 55 PRO D 48 ALA D 53 1 6
HELIX 56 56 GLY D 85 GLU D 100 1 16
HELIX 57 57 THR D 103 GLN D 110 1 8
HELIX 58 58 LEU D 113 LEU D 119 1 7
HELIX 59 59 LEU D 121 SER D 128 1 8
HELIX 60 60 ARG D 129 GLN D 131 5 3
HELIX 61 61 GLY D 132 LYS D 145 1 14
SHEET 1 A 2 VAL A 21 TYR A 22 0
SHEET 2 A 2 ILE A 350 ALA A 351 1 O ALA A 351 N VAL A 21
SHEET 1 B 7 ILE A 84 THR A 87 0
SHEET 2 B 7 GLY A 230 GLY A 234 -1 O LEU A 232 N VAL A 85
SHEET 3 B 7 PHE A 215 SER A 219 -1 N TYR A 216 O TYR A 233
SHEET 4 B 7 VAL A 192 ASP A 196 1 N VAL A 195 O PHE A 215
SHEET 5 B 7 SER A 161 GLY A 167 1 N LEU A 164 O MET A 194
SHEET 6 B 7 GLU A 111 SER A 115 1 N ILE A 113 O ALA A 165
SHEET 7 B 7 LYS A 136 LEU A 140 1 O LYS A 136 N ILE A 112
SHEET 1 C 2 VAL A 252 SER A 256 0
SHEET 2 C 2 GLY A 259 THR A 262 -1 O THR A 261 N HIS A 253
SHEET 1 D 4 PHE A 318 SER A 320 0
SHEET 2 D 4 LEU A 328 PHE A 333 -1 O ASP A 332 N ARG A 319
SHEET 3 D 4 THR A 371 SER A 375 -1 O ALA A 374 N LEU A 329
SHEET 4 D 4 ARG A 353 GLY A 355 -1 N ARG A 353 O ARG A 373
SHEET 1 E 2 VAL B 21 TYR B 22 0
SHEET 2 E 2 ILE B 350 ALA B 351 1 O ALA B 351 N VAL B 21
SHEET 1 F 7 ILE B 84 THR B 87 0
SHEET 2 F 7 GLY B 230 GLY B 234 -1 O GLY B 230 N THR B 87
SHEET 3 F 7 PHE B 215 SER B 219 -1 N TYR B 216 O TYR B 233
SHEET 4 F 7 VAL B 192 ASP B 196 1 N VAL B 195 O PHE B 215
SHEET 5 F 7 SER B 161 GLY B 167 1 N LEU B 164 O MET B 194
SHEET 6 F 7 GLU B 111 SER B 115 1 N GLU B 111 O ARG B 162
SHEET 7 F 7 LYS B 136 LEU B 140 1 O VAL B 138 N ILE B 112
SHEET 1 G 2 VAL B 252 SER B 256 0
SHEET 2 G 2 GLY B 259 THR B 262 -1 O THR B 261 N HIS B 253
SHEET 1 H 4 PHE B 318 SER B 320 0
SHEET 2 H 4 LEU B 328 PHE B 333 -1 O ASP B 332 N ARG B 319
SHEET 3 H 4 THR B 371 SER B 375 -1 O ALA B 374 N LEU B 329
SHEET 4 H 4 ARG B 353 GLY B 355 -1 N ARG B 353 O ARG B 373
SHEET 1 I 3 LYS C 56 GLU C 57 0
SHEET 2 I 3 VAL C 65 VAL C 71 -1 O LEU C 67 N LYS C 56
SHEET 3 I 3 MET C 77 SER C 83 -1 O HIS C 78 N THR C 70
SHEET 1 J 3 LYS D 56 ALA D 59 0
SHEET 2 J 3 ARG D 64 VAL D 71 -1 O VAL D 65 N ILE D 58
SHEET 3 J 3 MET D 77 SER D 83 -1 O PHE D 80 N GLY D 68
LINK NZ LYS A 222 C4A PLP A 500 1555 1555 1.59
LINK NZ LYS B 222 C4A PLP B 500 1555 1555 1.53
CISPEP 1 ALA A 265 PRO A 266 0 2.29
CISPEP 2 ALA B 265 PRO B 266 0 -0.12
SITE 1 AC1 14 THR A 90 THR A 91 HIS A 119 ASN A 171
SITE 2 AC1 14 ASP A 196 ALA A 198 GLN A 199 SER A 219
SITE 3 AC1 14 HIS A 221 LYS A 222 HOH A 602 HOH A 640
SITE 4 AC1 14 HOH A 781 THR B 273
SITE 1 AC2 16 GLY A 272 THR A 273 THR B 90 THR B 91
SITE 2 AC2 16 HIS B 119 ALA B 121 ASN B 171 ASP B 196
SITE 3 AC2 16 ALA B 198 GLN B 199 SER B 219 HIS B 221
SITE 4 AC2 16 LYS B 222 HOH B 640 HOH B 654 HOH B 757
CRYST1 77.135 76.871 89.361 90.00 104.48 90.00 P 1 21 1 4
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 0.012964 0.000000 0.003349 0.00000
SCALE2 0.000000 0.013009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011558 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
