HEADER TRANSFERASE 22-JUL-08 3DWG
TITLE CRYSTAL STRUCTURE OF A SULFUR CARRIER PROTEIN COMPLEX FOUND IN THE
TITLE 2 CYSTEINE BIOSYNTHETIC PATHWAY OF MYCOBACTERIUM TUBERCULOSIS
CAVEAT 3DWG ABNORMALLY SHORT LINK BETWEEN LYS A51 AND PLP A401
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE SYNTHASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: O-ACETYLSERINE SULFHYDRYLASE B, O-ACETYLSERINE(THIOL)-LYASE
COMPND 5 B, CSASE B;
COMPND 6 EC: 2.5.1.47;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 9.5 KDA CULTURE FILTRATE ANTIGEN CFP10A;
COMPND 10 CHAIN: C;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 ATCC: 25618;
SOURCE 6 GENE: CYSM, RV1336, MT1377, MTCY130.21;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)B834;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 13 ORGANISM_TAXID: 83332;
SOURCE 14 STRAIN: H37RV;
SOURCE 15 ATCC: 25618;
SOURCE 16 GENE: CFP10A, RV1335, MT1376.1, MTCY130.20;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS SULFUR CARRIER PROTEIN COMPLEX, BETA-GRASP FOLD, AMINO-ACID
KEYWDS 2 BIOSYNTHESIS, CYSTEINE BIOSYNTHESIS, PYRIDOXAL PHOSPHATE,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.T.JURGENSON,K.E.BURNS,T.P.BEGLEY,S.E.EALICK
REVDAT 4 13-JUL-11 3DWG 1 VERSN
REVDAT 3 24-FEB-09 3DWG 1 VERSN
REVDAT 2 14-OCT-08 3DWG 1 JRNL
REVDAT 1 23-SEP-08 3DWG 0
JRNL AUTH C.T.JURGENSON,K.E.BURNS,T.P.BEGLEY,S.E.EALICK
JRNL TITL CRYSTAL STRUCTURE OF A SULFUR CARRIER PROTEIN COMPLEX FOUND
JRNL TITL 2 IN THE CYSTEINE BIOSYNTHETIC PATHWAY OF MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS.
JRNL REF BIOCHEMISTRY V. 47 10354 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18771296
JRNL DOI 10.1021/BI800915J
REMARK 2
REMARK 2 RESOLUTION. 1.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 105098
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
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 : 5513
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) : 1.53
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6263
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 312
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5425
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 985
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.69
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): 0.080
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.481
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5590 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7632 ; 1.899 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 746 ; 5.559 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 221 ;34.259 ;23.258
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 838 ;13.670 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;19.066 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 881 ; 0.131 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4268 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3020 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3865 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 847 ; 0.185 ; 0.200
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): 85 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 68 ; 0.216 ; 0.200
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): 3731 ; 1.333 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5803 ; 1.941 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2093 ; 3.018 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1823 ; 4.410 ; 4.500
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3DWG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-08.
REMARK 100 THE RCSB ID CODE IS RCSB048574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-05; 22-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 5.80
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 24-ID-C; 8-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950; 0.97950
REMARK 200 MONOCHROMATOR : SI(220); SI(111)
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105098
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.180
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7-10% W/V PEG 4000, 0.1 M SODIUM
REMARK 280 CITRATE PH 5.8, 0.2 M AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 295K, PH 5.80
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 40.21300
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS THE BIOLOGICAL UNIT CONSISTING
REMARK 300 OF TWO CYSM PROTOMERS AND ONE CYSO PROTOMER.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLU B 126
REMARK 465 GLY B 127
REMARK 465 GLY B 128
REMARK 465 SER B 129
REMARK 465 MET C 1
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 GLU A 138 CG CD OE1 OE2
REMARK 470 ASP A 223 CG OD1 OD2
REMARK 470 SER A 309 OG
REMARK 470 ASP A 311 CG OD1 OD2
REMARK 470 ASP A 312 CG OD1 OD2
REMARK 470 ARG B -1 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 0 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 30 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 31 CG OD1 OD2
REMARK 470 ARG B 69 CG CD NE CZ NH1 NH2
REMARK 470 PRO B 102 CG CD
REMARK 470 GLU B 103 CG CD OE1 OE2
REMARK 470 VAL B 133 CG1 CG2
REMARK 470 THR B 142 OG1 CG2
REMARK 470 PRO B 144 CG CD
REMARK 470 SER B 145 OG
REMARK 470 TYR B 150 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR B 152 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 211 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 249 CG CD NE CZ NH1 NH2
REMARK 470 SER B 309 OG
REMARK 470 LEU B 310 CG CD1 CD2
REMARK 470 GLU B 314 CG CD OE1 OE2
REMARK 470 ASN C 2 CG OD1
REMARK 470 GLU C 44 CG CD OE1 OE2
REMARK 470 SER C 50 OG
REMARK 470 LYS C 54 CG CD CE NZ
REMARK 470 ARG C 57 CG CD NE CZ NH1 NH2
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 O HOH B 687 O HOH B 965 1.77
REMARK 500 CE MET B 190 O HOH B 1004 1.94
REMARK 500 N ARG A -1 O HOH A 821 2.04
REMARK 500 O HOH A 736 O HOH A 810 2.13
REMARK 500 O ASP A 31 O HOH A 831 2.14
REMARK 500 O HOH B 934 O HOH B 947 2.14
REMARK 500 O HOH B 950 O HOH B 971 2.16
REMARK 500 O HOH B 992 O HOH B 1018 2.16
REMARK 500 OG1 THR A 237 O HOH A 526 2.17
REMARK 500 NH1 ARG A 197 O HOH A 745 2.18
REMARK 500 O HOH A 731 O HOH B 800 2.18
REMARK 500 O HOH B 877 O HOH B 996 2.19
REMARK 500 O HOH B 926 O HOH B 996 2.19
REMARK 500 O HOH B 927 O HOH B 947 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER B 49 CB SER B 49 OG 0.092
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 53 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 109 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 239 CB - CG - CD ANGL. DEV. = 20.6 DEGREES
REMARK 500 ARG A 239 CD - NE - CZ ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG A 239 NE - CZ - NH1 ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 239 NE - CZ - NH2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP C 67 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 19 77.25 -109.53
REMARK 500 ARG A 44 57.45 -93.83
REMARK 500 ASN A 104 50.86 -97.82
REMARK 500 TYR A 150 79.31 67.97
REMARK 500 THR A 186 -2.10 78.10
REMARK 500 ASP A 312 -27.57 87.61
REMARK 500 PRO B 77 46.78 -82.74
REMARK 500 THR B 131 -44.33 178.22
REMARK 500 ALA B 141 -73.03 -50.02
REMARK 500 TYR B 150 86.15 47.86
REMARK 500 THR B 186 -2.04 76.91
REMARK 500 ARG B 211 54.35 -95.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 634 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH A 639 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH A 647 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 663 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH A 668 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 673 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH A 703 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH A 724 DISTANCE = 5.60 ANGSTROMS
REMARK 525 HOH A 774 DISTANCE = 5.72 ANGSTROMS
REMARK 525 HOH A 778 DISTANCE = 5.72 ANGSTROMS
REMARK 525 HOH A 789 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A 791 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 804 DISTANCE = 7.91 ANGSTROMS
REMARK 525 HOH A 811 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 839 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B 760 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH B 789 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B 831 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH B 849 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH B 860 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH B 921 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH B 929 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH B 933 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH B 944 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH B 967 DISTANCE = 5.68 ANGSTROMS
REMARK 525 HOH B 969 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH B 975 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH B 983 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH B 990 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH C 131 DISTANCE = 7.66 ANGSTROMS
REMARK 525 HOH C 161 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH C 177 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH C 195 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH C 200 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH C 204 DISTANCE = 5.80 ANGSTROMS
REMARK 525 HOH C 208 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH C 218 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH C 230 DISTANCE = 5.77 ANGSTROMS
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DWI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS CYSM, THE
REMARK 900 CYSTEINE SYNTHASE B
REMARK 900 RELATED ID: 3DWM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS CYSO, AN
REMARK 900 ANTIGEN
DBREF 3DWG A 1 323 UNP P63873 CYSM_MYCTU 1 323
DBREF 3DWG B 1 323 UNP P63873 CYSM_MYCTU 1 323
DBREF 3DWG C 1 93 UNP P0A646 CF1A_MYCTU 1 93
SEQADV 3DWG ARG A -1 UNP P63873 EXPRESSION TAG
SEQADV 3DWG HIS A 0 UNP P63873 EXPRESSION TAG
SEQADV 3DWG ARG B -1 UNP P63873 EXPRESSION TAG
SEQADV 3DWG HIS B 0 UNP P63873 EXPRESSION TAG
SEQRES 1 A 325 ARG HIS MET THR ARG TYR ASP SER LEU LEU GLN ALA LEU
SEQRES 2 A 325 GLY ASN THR PRO LEU VAL GLY LEU GLN ARG LEU SER PRO
SEQRES 3 A 325 ARG TRP ASP ASP GLY ARG ASP GLY PRO HIS VAL ARG LEU
SEQRES 4 A 325 TRP ALA LYS LEU GLU ASP ARG ASN PRO THR GLY SER ILE
SEQRES 5 A 325 LYS ASP ARG PRO ALA VAL ARG MET ILE GLU GLN ALA GLU
SEQRES 6 A 325 ALA ASP GLY LEU LEU ARG PRO GLY ALA THR ILE LEU GLU
SEQRES 7 A 325 PRO THR SER GLY ASN THR GLY ILE SER LEU ALA MET ALA
SEQRES 8 A 325 ALA ARG LEU LYS GLY TYR ARG LEU ILE CYS VAL MET PRO
SEQRES 9 A 325 GLU ASN THR SER VAL GLU ARG ARG GLN LEU LEU GLU LEU
SEQRES 10 A 325 TYR GLY ALA GLN ILE ILE PHE SER ALA ALA GLU GLY GLY
SEQRES 11 A 325 SER ASN THR ALA VAL ALA THR ALA LYS GLU LEU ALA ALA
SEQRES 12 A 325 THR ASN PRO SER TRP VAL MET LEU TYR GLN TYR GLY ASN
SEQRES 13 A 325 PRO ALA ASN THR ASP SER HIS TYR CYS GLY THR GLY PRO
SEQRES 14 A 325 GLU LEU LEU ALA ASP LEU PRO GLU ILE THR HIS PHE VAL
SEQRES 15 A 325 ALA GLY LEU GLY THR THR GLY THR LEU MET GLY THR GLY
SEQRES 16 A 325 ARG PHE LEU ARG GLU HIS VAL ALA ASN VAL LYS ILE VAL
SEQRES 17 A 325 ALA ALA GLU PRO ARG TYR GLY GLU GLY VAL TYR ALA LEU
SEQRES 18 A 325 ARG ASN MET ASP GLU GLY PHE VAL PRO GLU LEU TYR ASP
SEQRES 19 A 325 PRO GLU ILE LEU THR ALA ARG TYR SER VAL GLY ALA VAL
SEQRES 20 A 325 ASP ALA VAL ARG ARG THR ARG GLU LEU VAL HIS THR GLU
SEQRES 21 A 325 GLY ILE PHE ALA GLY ILE SER THR GLY ALA VAL LEU HIS
SEQRES 22 A 325 ALA ALA LEU GLY VAL GLY ALA GLY ALA LEU ALA ALA GLY
SEQRES 23 A 325 GLU ARG ALA ASP ILE ALA LEU VAL VAL ALA ASP ALA GLY
SEQRES 24 A 325 TRP LYS TYR LEU SER THR GLY ALA TYR ALA GLY SER LEU
SEQRES 25 A 325 ASP ASP ALA GLU THR ALA LEU GLU GLY GLN LEU TRP ALA
SEQRES 1 B 325 ARG HIS MET THR ARG TYR ASP SER LEU LEU GLN ALA LEU
SEQRES 2 B 325 GLY ASN THR PRO LEU VAL GLY LEU GLN ARG LEU SER PRO
SEQRES 3 B 325 ARG TRP ASP ASP GLY ARG ASP GLY PRO HIS VAL ARG LEU
SEQRES 4 B 325 TRP ALA LYS LEU GLU ASP ARG ASN PRO THR GLY SER ILE
SEQRES 5 B 325 LYS ASP ARG PRO ALA VAL ARG MET ILE GLU GLN ALA GLU
SEQRES 6 B 325 ALA ASP GLY LEU LEU ARG PRO GLY ALA THR ILE LEU GLU
SEQRES 7 B 325 PRO THR SER GLY ASN THR GLY ILE SER LEU ALA MET ALA
SEQRES 8 B 325 ALA ARG LEU LYS GLY TYR ARG LEU ILE CYS VAL MET PRO
SEQRES 9 B 325 GLU ASN THR SER VAL GLU ARG ARG GLN LEU LEU GLU LEU
SEQRES 10 B 325 TYR GLY ALA GLN ILE ILE PHE SER ALA ALA GLU GLY GLY
SEQRES 11 B 325 SER ASN THR ALA VAL ALA THR ALA LYS GLU LEU ALA ALA
SEQRES 12 B 325 THR ASN PRO SER TRP VAL MET LEU TYR GLN TYR GLY ASN
SEQRES 13 B 325 PRO ALA ASN THR ASP SER HIS TYR CYS GLY THR GLY PRO
SEQRES 14 B 325 GLU LEU LEU ALA ASP LEU PRO GLU ILE THR HIS PHE VAL
SEQRES 15 B 325 ALA GLY LEU GLY THR THR GLY THR LEU MET GLY THR GLY
SEQRES 16 B 325 ARG PHE LEU ARG GLU HIS VAL ALA ASN VAL LYS ILE VAL
SEQRES 17 B 325 ALA ALA GLU PRO ARG TYR GLY GLU GLY VAL TYR ALA LEU
SEQRES 18 B 325 ARG ASN MET ASP GLU GLY PHE VAL PRO GLU LEU TYR ASP
SEQRES 19 B 325 PRO GLU ILE LEU THR ALA ARG TYR SER VAL GLY ALA VAL
SEQRES 20 B 325 ASP ALA VAL ARG ARG THR ARG GLU LEU VAL HIS THR GLU
SEQRES 21 B 325 GLY ILE PHE ALA GLY ILE SER THR GLY ALA VAL LEU HIS
SEQRES 22 B 325 ALA ALA LEU GLY VAL GLY ALA GLY ALA LEU ALA ALA GLY
SEQRES 23 B 325 GLU ARG ALA ASP ILE ALA LEU VAL VAL ALA ASP ALA GLY
SEQRES 24 B 325 TRP LYS TYR LEU SER THR GLY ALA TYR ALA GLY SER LEU
SEQRES 25 B 325 ASP ASP ALA GLU THR ALA LEU GLU GLY GLN LEU TRP ALA
SEQRES 1 C 93 MET ASN VAL THR VAL SER ILE PRO THR ILE LEU ARG PRO
SEQRES 2 C 93 HIS THR GLY GLY GLN LYS SER VAL SER ALA SER GLY ASP
SEQRES 3 C 93 THR LEU GLY ALA VAL ILE SER ASP LEU GLU ALA ASN TYR
SEQRES 4 C 93 SER GLY ILE SER GLU ARG LEU MET ASP PRO SER SER PRO
SEQRES 5 C 93 GLY LYS LEU HIS ARG PHE VAL ASN ILE TYR VAL ASN ASP
SEQRES 6 C 93 GLU ASP VAL ARG PHE SER GLY GLY LEU ALA THR ALA ILE
SEQRES 7 C 93 ALA ASP GLY ASP SER VAL THR ILE LEU PRO ALA VAL ALA
SEQRES 8 C 93 GLY GLY
HET PLP A 401 15
HET PLP B 401 15
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 4 PLP 2(C8 H10 N O6 P)
FORMUL 6 HOH *985(H2 O)
HELIX 1 1 LEU A 7 LEU A 11 5 5
HELIX 2 2 LYS A 51 ASP A 65 1 15
HELIX 3 3 GLY A 80 GLY A 94 1 15
HELIX 4 4 SER A 106 GLY A 117 1 12
HELIX 5 5 GLY A 128 ASN A 143 1 16
HELIX 6 6 ASN A 154 GLY A 164 1 11
HELIX 7 7 GLY A 164 LEU A 173 1 10
HELIX 8 8 THR A 186 VAL A 200 1 15
HELIX 9 9 GLY A 213 ALA A 218 5 6
HELIX 10 10 ASN A 221 GLY A 225 5 5
HELIX 11 11 ASP A 232 LEU A 236 5 5
HELIX 12 12 ALA A 244 GLY A 259 1 16
HELIX 13 13 GLY A 263 GLY A 284 1 22
HELIX 14 14 ALA A 296 GLY A 304 5 9
HELIX 15 15 SER A 309 GLU A 318 1 10
HELIX 16 16 SER B 6 LEU B 11 5 6
HELIX 17 17 ASP B 43 ASN B 45 5 3
HELIX 18 18 LYS B 51 ASP B 65 1 15
HELIX 19 19 GLY B 80 GLY B 94 1 15
HELIX 20 20 SER B 106 GLY B 117 1 12
HELIX 21 21 THR B 131 ASN B 143 1 13
HELIX 22 22 ASN B 154 GLY B 164 1 11
HELIX 23 23 GLY B 164 LEU B 173 1 10
HELIX 24 24 THR B 186 VAL B 200 1 15
HELIX 25 25 LEU B 219 ASP B 223 5 5
HELIX 26 26 VAL B 227 ASP B 232 5 6
HELIX 27 27 ALA B 244 GLY B 259 1 16
HELIX 28 28 GLY B 263 ALA B 283 1 21
HELIX 29 29 GLY B 297 LEU B 301 5 5
HELIX 30 30 SER B 309 GLY B 319 1 11
HELIX 31 31 PRO C 8 THR C 15 5 8
HELIX 32 32 THR C 27 TYR C 39 1 13
HELIX 33 33 GLY C 41 MET C 47 1 7
HELIX 34 34 ARG C 69 SER C 71 5 3
HELIX 35 35 GLY C 72 THR C 76 5 5
SHEET 1 A 7 ARG A 3 TYR A 4 0
SHEET 2 A 7 LEU B 16 GLY B 18 1 O GLY B 18 N TYR A 4
SHEET 3 A 7 VAL B 35 LEU B 41 -1 O ALA B 39 N VAL B 17
SHEET 4 A 7 ALA B 287 VAL B 293 1 O ILE B 289 N ARG B 36
SHEET 5 A 7 HIS B 178 GLY B 182 1 N VAL B 180 O ALA B 290
SHEET 6 A 7 LYS B 204 ARG B 211 1 O VAL B 206 N PHE B 179
SHEET 7 A 7 ALA B 238 GLY B 243 1 O VAL B 242 N ARG B 211
SHEET 1 B 7 ALA A 238 GLY A 243 0
SHEET 2 B 7 LYS A 204 ARG A 211 1 N GLU A 209 O TYR A 240
SHEET 3 B 7 HIS A 178 GLY A 182 1 N PHE A 179 O VAL A 206
SHEET 4 B 7 ALA A 287 VAL A 293 1 O ALA A 290 N VAL A 180
SHEET 5 B 7 VAL A 35 LEU A 41 1 N ARG A 36 O ILE A 289
SHEET 6 B 7 LEU A 16 GLY A 18 -1 N VAL A 17 O ALA A 39
SHEET 7 B 7 ARG B 3 TYR B 4 1 O TYR B 4 N GLY A 18
SHEET 1 C 3 THR A 73 PRO A 77 0
SHEET 2 C 3 ARG A 96 PRO A 102 1 O ARG A 96 N ILE A 74
SHEET 3 C 3 GLN A 119 SER A 123 1 O ILE A 121 N CYS A 99
SHEET 1 D 4 GLN B 119 SER B 123 0
SHEET 2 D 4 ARG B 96 PRO B 102 1 N CYS B 99 O GLN B 119
SHEET 3 D 4 THR B 73 GLU B 76 1 N ILE B 74 O ARG B 96
SHEET 4 D 4 VAL B 147 MET B 148 1 O VAL B 147 N THR B 73
SHEET 1 E 5 SER C 20 ALA C 23 0
SHEET 2 E 5 VAL C 3 SER C 6 -1 N VAL C 3 O ALA C 23
SHEET 3 E 5 SER C 83 PRO C 88 1 O VAL C 84 N SER C 6
SHEET 4 E 5 VAL C 59 VAL C 63 -1 N ASN C 60 O LEU C 87
SHEET 5 E 5 GLU C 66 ASP C 67 -1 O GLU C 66 N VAL C 63
LINK NZ LYS A 51 C4A PLP A 401 1555 1555 1.16
LINK NZ LYS B 51 C4A PLP B 401 1555 1555 1.24
SITE 1 AC1 13 LYS A 51 ASN A 81 GLY A 184 THR A 185
SITE 2 AC1 13 THR A 186 GLY A 187 THR A 188 SER A 265
SITE 3 AC1 13 ALA A 294 ASP A 295 HOH A 404 HOH A 411
SITE 4 AC1 13 HOH A 448
SITE 1 AC2 16 LYS B 51 ASN B 81 GLY B 184 THR B 185
SITE 2 AC2 16 THR B 186 GLY B 187 THR B 188 SER B 265
SITE 3 AC2 16 ALA B 294 ASP B 295 TRP B 322 ALA B 323
SITE 4 AC2 16 HOH B 616 HOH B 618 HOH B 628 HOH B 757
CRYST1 55.810 80.426 89.619 90.00 105.74 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 0.017918 0.000000 0.005050 0.00000
SCALE2 0.000000 0.012434 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011593 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
