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HEADER HYDROLASE 13-MAY-20 6WYN
TITLE TRANSITION METAL INHIBITION AND STRUCTURAL REFINEMENT OF THE M.
TITLE 2 TUBERCULOSIS ESTERASE, RV0045C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POSSIBLE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: RV0045C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VARIANT: LOBSTR;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-28
KEYWDS SERINE ESTERASE, ALLOSTERIC REGULATION, CONFORMATIONAL CHANGE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.MACBETH,R.J.JOHNSON,G.C.HOOPS
REVDAT 1 19-MAY-21 6WYN 0
JRNL AUTH I.E.BOWLES,E.H.POOL,B.S.LANCASTER,E.K.LAWSON,C.P.SAVAS,
JRNL AUTH 2 Z.J.KARTJE,L.SEVERINAC,D.H.CHO,M.R.MACBETH,R.J.JOHNSON,
JRNL AUTH 3 G.C.HOOPS
JRNL TITL TRANSITION METAL CATION INHIBITION OF MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS ESTERASE RV0045C.
JRNL REF PROTEIN SCI. 2021
JRNL REFN ESSN 1469-896X
JRNL PMID 33914998
JRNL DOI 10.1002/PRO.4089
REMARK 2
REMARK 2 RESOLUTION. 1.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 113.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.2
REMARK 3 NUMBER OF REFLECTIONS : 34042
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1774
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 REFLECTION IN BIN (WORKING SET) : 170
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 5.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.3270
REMARK 3 BIN FREE R VALUE SET COUNT : 11
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2201
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 212
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.58
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) : -0.01000
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): 0.129
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.969
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2255 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2074 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3073 ; 1.890 ; 1.630
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4774 ; 1.451 ; 1.571
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 291 ; 7.601 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 128 ;29.793 ;20.781
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 340 ;14.941 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;18.390 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 285 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2618 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 504 ; 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 : 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6WYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-20.
REMARK 100 THE DEPOSITION ID IS D_1000249215.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.279
REMARK 200 MONOCHROMATOR : KOHZU HLD-4 DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42576
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 113.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.5
REMARK 200 DATA REDUNDANCY : 17.00
REMARK 200 R MERGE (I) : 0.18900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 29.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 4.44400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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 2.8.3
REMARK 200 STARTING MODEL: 3P2M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 0.1 M IMIDAZOLE PH 7.4,
REMARK 280 18% PEG 4000, 0.01 M SPERMIDINE, 1X10^-7 M ZNCL2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 16.29000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.58000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 32.58000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 16.29000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 0
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 SER A 10
REMARK 465 SER A 11
REMARK 465 GLY A 12
REMARK 465 LEU A 13
REMARK 465 VAL A 14
REMARK 465 PRO A 15
REMARK 465 ARG A 16
REMARK 465 GLY A 17
REMARK 465 SER A 18
REMARK 465 HIS A 19
REMARK 465 MET A 20
REMARK 465 ALA A 21
REMARK 465 SER A 22
REMARK 465 MET A 23
REMARK 465 THR A 24
REMARK 465 GLY A 25
REMARK 465 GLY A 26
REMARK 465 GLN A 27
REMARK 465 GLN A 28
REMARK 465 MET A 29
REMARK 465 GLY A 30
REMARK 465 ARG A 31
REMARK 465 GLY A 32
REMARK 465 SER A 33
REMARK 465 LEU A 34
REMARK 465 SER A 35
REMARK 465 ASP A 36
REMARK 465 ASP A 37
REMARK 465 GLU A 38
REMARK 465 LEU A 39
REMARK 465 ARG A 330
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 A 640 O HOH A 686 2.01
REMARK 500 O HOH A 501 O HOH A 705 2.12
REMARK 500 O HOH A 671 O HOH A 704 2.12
REMARK 500 O HOH A 681 O HOH A 682 2.13
REMARK 500 O HOH A 553 O HOH A 626 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG A 253 NH1 ARG A 253 6555 1.36
REMARK 500 CZ ARG A 253 NH1 ARG A 253 6555 2.08
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 ALA A 144 50.00 -147.04
REMARK 500 SER A 154 -120.53 46.11
REMARK 500 LEU A 170 -75.19 -58.45
REMARK 500 GLU A 204 -12.61 64.33
REMARK 500 ARG A 205 161.73 73.92
REMARK 500 ALA A 221 62.71 -150.74
REMARK 500 ALA A 251 130.39 -33.72
REMARK 500 PHE A 255 -136.70 -103.19
REMARK 500 ASP A 257 126.68 54.21
REMARK 500 PHE A 258 -34.64 -136.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6WYM RELATED DB: PDB
REMARK 900 6WYM CONTAINS THE SAME PROTEIN CRYSTALLIZED IN THE ABSENCE OF ZN(2+)
DBREF 6WYN A 34 330 UNP I6XU97 I6XU97_MYCTU 2 298
SEQADV 6WYN MET A 0 UNP I6XU97 INITIATING METHIONINE
SEQADV 6WYN GLY A 1 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN SER A 2 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN SER A 3 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN HIS A 4 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN HIS A 5 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN HIS A 6 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN HIS A 7 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN HIS A 8 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN HIS A 9 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN SER A 10 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN SER A 11 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN GLY A 12 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN LEU A 13 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN VAL A 14 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN PRO A 15 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN ARG A 16 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN GLY A 17 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN SER A 18 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN HIS A 19 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN MET A 20 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN ALA A 21 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN SER A 22 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN MET A 23 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN THR A 24 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN GLY A 25 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN GLY A 26 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN GLN A 27 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN GLN A 28 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN MET A 29 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN GLY A 30 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN ARG A 31 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN GLY A 32 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYN SER A 33 UNP I6XU97 EXPRESSION TAG
SEQRES 1 A 331 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 331 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 331 GLY GLN GLN MET GLY ARG GLY SER LEU SER ASP ASP GLU
SEQRES 4 A 331 LEU THR GLY LEU ASP GLU PHE ALA LEU LEU ALA GLU ASN
SEQRES 5 A 331 ALA GLU GLN ALA GLY VAL ASN GLY PRO LEU PRO GLU VAL
SEQRES 6 A 331 GLU ARG VAL GLN ALA GLY ALA ILE SER ALA LEU ARG TRP
SEQRES 7 A 331 GLY GLY SER ALA PRO ARG VAL ILE PHE LEU HIS GLY GLY
SEQRES 8 A 331 GLY GLN ASN ALA HIS THR TRP ASP THR VAL ILE VAL GLY
SEQRES 9 A 331 LEU GLY GLU PRO ALA LEU ALA VAL ASP LEU PRO GLY HIS
SEQRES 10 A 331 GLY HIS SER ALA TRP ARG GLU ASP GLY ASN TYR SER PRO
SEQRES 11 A 331 GLN LEU ASN SER GLU THR LEU ALA PRO VAL LEU ARG GLU
SEQRES 12 A 331 LEU ALA PRO GLY ALA GLU PHE VAL VAL GLY MET SER LEU
SEQRES 13 A 331 GLY GLY LEU THR ALA ILE ARG LEU ALA ALA MET ALA PRO
SEQRES 14 A 331 ASP LEU VAL GLY GLU LEU VAL LEU VAL ASP VAL THR PRO
SEQRES 15 A 331 SER ALA LEU GLN ARG HIS ALA GLU LEU THR ALA GLU GLN
SEQRES 16 A 331 ARG GLY THR VAL ALA LEU MET HIS GLY GLU ARG GLU PHE
SEQRES 17 A 331 PRO SER PHE GLN ALA MET LEU ASP LEU THR ILE ALA ALA
SEQRES 18 A 331 ALA PRO HIS ARG ASP VAL LYS SER LEU ARG ARG GLY VAL
SEQRES 19 A 331 PHE HIS ASN SER ARG ARG LEU ASP ASN GLY ASN TRP VAL
SEQRES 20 A 331 TRP ARG TYR ASP ALA ILE ARG THR PHE GLY ASP PHE ALA
SEQRES 21 A 331 GLY LEU TRP ASP ASP VAL ASP ALA LEU SER ALA PRO ILE
SEQRES 22 A 331 THR LEU VAL ARG GLY GLY SER SER GLY PHE VAL THR ASP
SEQRES 23 A 331 GLN ASP THR ALA GLU LEU HIS ARG ARG ALA THR HIS PHE
SEQRES 24 A 331 ARG GLY VAL HIS ILE VAL GLU LYS SER GLY HIS SER VAL
SEQRES 25 A 331 GLN SER ASP GLN PRO ARG ALA LEU ILE GLU ILE VAL ARG
SEQRES 26 A 331 GLY VAL LEU ASP THR ARG
HET CL A 401 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
FORMUL 3 HOH *212(H2 O)
HELIX 1 AA1 LEU A 47 ALA A 55 1 9
HELIX 2 AA2 ASN A 93 THR A 96 5 4
HELIX 3 AA3 TRP A 97 GLY A 105 1 9
HELIX 4 AA4 SER A 128 ALA A 144 1 17
HELIX 5 AA5 SER A 154 ALA A 167 1 14
HELIX 6 AA6 THR A 180 LEU A 200 1 21
HELIX 7 AA7 SER A 209 ALA A 221 1 13
HELIX 8 AA8 ASP A 225 ASN A 236 1 12
HELIX 9 AA9 PHE A 258 LEU A 268 1 11
HELIX 10 AB1 THR A 284 ALA A 295 1 12
HELIX 11 AB2 SER A 310 GLN A 315 1 6
HELIX 12 AB3 GLN A 315 ASP A 328 1 14
SHEET 1 AA1 8 VAL A 64 ALA A 69 0
SHEET 2 AA1 8 ILE A 72 TRP A 77 -1 O ALA A 74 N VAL A 67
SHEET 3 AA1 8 ALA A 108 VAL A 111 -1 O ALA A 108 N TRP A 77
SHEET 4 AA1 8 VAL A 84 LEU A 87 1 N PHE A 86 O LEU A 109
SHEET 5 AA1 8 PHE A 149 MET A 153 1 O VAL A 151 N ILE A 85
SHEET 6 AA1 8 GLU A 173 VAL A 177 1 O VAL A 177 N GLY A 152
SHEET 7 AA1 8 ILE A 272 GLY A 277 1 O THR A 273 N LEU A 176
SHEET 8 AA1 8 PHE A 298 VAL A 304 1 O HIS A 302 N ARG A 276
SHEET 1 AA2 2 SER A 237 ARG A 239 0
SHEET 2 AA2 2 TRP A 245 TRP A 247 -1 O VAL A 246 N ARG A 238
SITE 1 AC1 3 GLY A 90 SER A 154 LEU A 155
CRYST1 130.810 130.810 48.870 90.00 90.00 120.00 P 31 2 1 6
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 0.007645 0.004414 0.000000 0.00000
SCALE2 0.000000 0.008827 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020462 0.00000
TER 2205 THR A 329
MASTER 363 0 1 12 10 0 1 6 2414 1 0 26
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