HEADER LYASE 16-JUL-13 3WEW
TITLE CRYSTAL STRUCTURE OF HTDX (RV0241C) OF MYCOBACTERIUM TUBERCULOSIS AT
TITLE 2 2.4 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HTDX DEHYDRATASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 29-280;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RV0242C, RVBD_0241C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SG13009;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS HOTDOG FOLD, DEHYDRATASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BISWAS,D.DUTTA,A.K.DAS
REVDAT 2 20-MAR-24 3WEW 1 REMARK SEQADV
REVDAT 1 16-JUL-14 3WEW 0
JRNL AUTH R.BISWAS,D.DUTTA,A.K.DAS
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE DEHYDRATASE HTDX OF
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 9922
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 500
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 754
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 28
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1757
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 78
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.23000
REMARK 3 B22 (A**2) : 1.23000
REMARK 3 B33 (A**2) : -2.45000
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): 0.339
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.242
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.177
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.925
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
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): 1805 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1731 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2477 ; 1.655 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3944 ; 0.835 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 231 ; 7.486 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 72 ;36.991 ;22.222
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 245 ;17.482 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;19.676 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 292 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2058 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 429 ; 0.001 ; 0.020
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 252
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9987 19.5036 -0.3801
REMARK 3 T TENSOR
REMARK 3 T11: 0.0270 T22: 0.0335
REMARK 3 T33: 0.0411 T12: -0.0100
REMARK 3 T13: 0.0060 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.2002 L22: 0.4163
REMARK 3 L33: 0.8690 L12: -0.1972
REMARK 3 L13: 0.0443 L23: -0.0622
REMARK 3 S TENSOR
REMARK 3 S11: 0.0161 S12: 0.0177 S13: 0.0503
REMARK 3 S21: 0.0196 S22: -0.0120 S23: -0.0013
REMARK 3 S31: 0.0081 S32: 0.0452 S33: -0.0041
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 3WEW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000096248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8.0
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) : 1.54
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11816
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 56.552
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 15.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 14.90
REMARK 200 R MERGE FOR SHELL (I) : 0.69700
REMARK 200 R SYM FOR SHELL (I) : 0.69700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
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 (%): 49.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3M NACL, 0.1M HEPES PH 8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 300K, PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 30.75200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 30.75200
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.90150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.75200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.95075
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.75200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 107.85225
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.75200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.75200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 71.90150
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 30.75200
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 107.85225
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 30.75200
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 35.95075
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 436 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 469 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 ASN A 1
REMARK 465 ARG A 122
REMARK 465 THR A 123
REMARK 465 SER A 124
REMARK 465 LEU A 125
REMARK 465 SER A 126
REMARK 465 GLY A 127
REMARK 465 GLU A 128
REMARK 465 PRO A 129
REMARK 465 LYS A 130
REMARK 465 PRO A 131
REMARK 465 PRO A 132
REMARK 465 PRO A 133
REMARK 465 GLN A 134
REMARK 465 LYS A 135
REMARK 465 LYS A 136
REMARK 465 PRO A 137
REMARK 465 LYS A 138
REMARK 465 LEU A 139
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 2 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 7 CG CD OE1 OE2
REMARK 470 ARG A 92 CD NE CZ NH1 NH2
REMARK 470 GLN A 121 CG CD OE1 NE2
REMARK 470 ARG A 205 NE CZ NH1 NH2
REMARK 470 LYS A 240 CG CD CE NZ
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 147 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH2 ANGL. DEV. = -3.4 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 PHE A 55 108.34 -171.94
REMARK 500 ARG A 92 -58.24 158.11
REMARK 500 ALA A 211 -105.80 -120.19
REMARK 500 LYS A 240 -36.62 119.93
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 MG A 301
DBREF 3WEW A 1 252 UNP O53664 O53664_MYCTU 29 280
SEQADV 3WEW HIS A -5 UNP O53664 EXPRESSION TAG
SEQADV 3WEW HIS A -4 UNP O53664 EXPRESSION TAG
SEQADV 3WEW HIS A -3 UNP O53664 EXPRESSION TAG
SEQADV 3WEW HIS A -2 UNP O53664 EXPRESSION TAG
SEQADV 3WEW HIS A -1 UNP O53664 EXPRESSION TAG
SEQADV 3WEW HIS A 0 UNP O53664 EXPRESSION TAG
SEQRES 1 A 258 HIS HIS HIS HIS HIS HIS ASN ARG THR VAL THR VAL GLU
SEQRES 2 A 258 GLU LEU PRO ILE ASP PRO ALA ASN VAL ALA ALA TYR ALA
SEQRES 3 A 258 ALA VAL THR GLY LEU ARG TYR GLY ASN GLN VAL PRO LEU
SEQRES 4 A 258 THR TYR PRO PHE ALA LEU THR PHE PRO SER VAL MET SER
SEQRES 5 A 258 LEU VAL THR GLY PHE ASP PHE PRO PHE ALA ALA MET GLY
SEQRES 6 A 258 ALA ILE HIS THR GLU ASN HIS ILE THR GLN TYR ARG PRO
SEQRES 7 A 258 ILE ALA VAL THR ASP ALA VAL GLY VAL ARG VAL ARG ALA
SEQRES 8 A 258 GLU ASN LEU ARG GLU HIS ARG ARG GLY LEU LEU VAL ASP
SEQRES 9 A 258 LEU VAL THR ASN VAL SER VAL GLY ASN ASP VAL ALA TRP
SEQRES 10 A 258 HIS GLN VAL THR THR PHE LEU HIS GLN GLN ARG THR SER
SEQRES 11 A 258 LEU SER GLY GLU PRO LYS PRO PRO PRO GLN LYS LYS PRO
SEQRES 12 A 258 LYS LEU PRO PRO PRO ALA ALA VAL LEU ARG ILE THR PRO
SEQRES 13 A 258 ALA LYS ILE ARG ARG TYR ALA ALA VAL GLY GLY ASP HIS
SEQRES 14 A 258 ASN PRO ILE HIS THR ASN PRO ILE ALA ALA LYS LEU PHE
SEQRES 15 A 258 GLY PHE PRO THR VAL ILE ALA HIS GLY MET PHE THR ALA
SEQRES 16 A 258 ALA ALA VAL LEU ALA ASN ILE GLU ALA ARG PHE PRO ASP
SEQRES 17 A 258 ALA VAL ARG TYR SER VAL ARG PHE ALA LYS PRO VAL LEU
SEQRES 18 A 258 LEU PRO ALA THR ALA GLY LEU TYR VAL ALA GLU GLY ASP
SEQRES 19 A 258 GLY GLY TRP ASP LEU THR LEU ARG ASN MET ALA LYS GLY
SEQRES 20 A 258 TYR PRO HIS LEU THR ALA THR VAL ARG GLY LEU
HET MG A 301 1
HETNAM MG MAGNESIUM ION
FORMUL 2 MG MG 2+
FORMUL 3 HOH *78(H2 O)
HELIX 1 1 ASP A 12 GLY A 24 1 13
HELIX 2 2 THR A 34 THR A 40 1 7
HELIX 3 3 THR A 40 GLY A 50 1 11
HELIX 4 4 THR A 149 GLY A 161 1 13
HELIX 5 5 ASN A 169 PHE A 176 1 8
HELIX 6 6 HIS A 184 VAL A 192 1 9
HELIX 7 7 LEU A 193 ALA A 194 5 2
HELIX 8 8 ASN A 195 PHE A 200 5 6
SHEET 1 A10 THR A 3 PRO A 10 0
SHEET 2 A10 ALA A 78 GLU A 90 -1 O VAL A 79 N LEU A 9
SHEET 3 A10 GLY A 94 VAL A 105 -1 O VAL A 100 N ARG A 84
SHEET 4 A10 ASP A 108 GLN A 120 -1 O TRP A 111 N VAL A 103
SHEET 5 A10 ILE A 61 GLN A 69 -1 N THR A 68 O HIS A 112
SHEET 6 A10 VAL A 204 PHE A 210 -1 O VAL A 208 N ASN A 65
SHEET 7 A10 PRO A 243 GLY A 251 -1 O ARG A 250 N ARG A 205
SHEET 8 A10 GLY A 230 ASN A 237 -1 N LEU A 235 O HIS A 244
SHEET 9 A10 ALA A 218 ALA A 225 -1 N TYR A 223 O THR A 234
SHEET 10 A10 ALA A 144 ILE A 148 -1 N ILE A 148 O ALA A 218
CISPEP 1 LEU A 216 PRO A 217 0 -2.46
CISPEP 2 ASP A 228 GLY A 229 0 -0.55
SITE 1 AC1 4 ASN A 65 ILE A 67 TYR A 206 VAL A 208
CRYST1 61.504 61.504 143.803 90.00 90.00 90.00 I 41 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 0.016259 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016259 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006954 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
