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HEADER HYDROLASE 13-MAY-20 6WYM
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: PET28
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 6WYM 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. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 113.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.3
REMARK 3 NUMBER OF REFLECTIONS : 25224
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1344
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 363
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 15.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 23
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2211
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 205
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.04000
REMARK 3 B12 (A**2) : -0.01000
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): 0.177
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.169
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.406
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2255 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2074 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3072 ; 1.728 ; 1.628
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4774 ; 1.337 ; 1.571
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 290 ; 7.464 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;29.989 ;21.024
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 339 ;16.047 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;21.323 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 284 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2616 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 499 ; 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 6WYM 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_1000249212.
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 : 25604
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.998
REMARK 200 RESOLUTION RANGE LOW (A) : 113.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 200 DATA REDUNDANCY : 18.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 42.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
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: 3P2M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM MGCL2, 100 MM IMIDAZOLE PH 7.4,
REMARK 280 18% PEG 4000, VAPOR DIFFUSION, HANGING 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 16.27133
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 32.54267
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 32.54267
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 16.27133
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 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 THR A 329
REMARK 465 ARG A 330
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 205 CB - CA - C ANGL. DEV. = 28.8 DEGREES
REMARK 500 ARG A 205 N - CA - C ANGL. DEV. = -21.4 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 294 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ALA A 144 49.57 -147.50
REMARK 500 SER A 154 -118.96 42.40
REMARK 500 ARG A 205 176.96 151.30
REMARK 500 PHE A 255 -169.29 -127.41
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
DBREF 6WYM A 34 330 UNP I6XU97 I6XU97_MYCTU 2 298
SEQADV 6WYM MET A 0 UNP I6XU97 INITIATING METHIONINE
SEQADV 6WYM GLY A 1 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM SER A 2 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM SER A 3 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM HIS A 4 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM HIS A 5 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM HIS A 6 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM HIS A 7 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM HIS A 8 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM HIS A 9 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM SER A 10 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM SER A 11 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM GLY A 12 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM LEU A 13 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM VAL A 14 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM PRO A 15 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM ARG A 16 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM GLY A 17 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM SER A 18 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM HIS A 19 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM MET A 20 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM ALA A 21 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM SER A 22 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM MET A 23 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM THR A 24 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM GLY A 25 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM GLY A 26 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM GLN A 27 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM GLN A 28 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM MET A 29 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM GLY A 30 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM ARG A 31 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM GLY A 32 UNP I6XU97 EXPRESSION TAG
SEQADV 6WYM 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 *205(H2 O)
HELIX 1 AA1 LEU A 47 GLY A 56 1 10
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 ALA A 199 1 20
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 ASP A 257 LEU A 268 1 12
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 LEU A 327 1 13
SHEET 1 AA1 8 VAL A 64 ALA A 69 0
SHEET 2 AA1 8 ILE A 72 TRP A 77 -1 O ARG A 76 N GLU A 65
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 ARG A 299 N ILE A 272
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 5 GLY A 90 SER A 154 LEU A 155 HOH A 635
SITE 2 AC1 5 HOH A 694
CRYST1 130.618 130.618 48.814 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 0.007656 0.004420 0.000000 0.00000
SCALE2 0.000000 0.008840 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020486 0.00000
TER 2212 ASP A 328
MASTER 337 0 1 12 10 0 2 6 2417 1 0 26
END |