HEADER LYASE 24-JUL-12 4G9Q
TITLE CRYSTAL STRUCTURE OF A 4-CARBOXYMUCONOLACTONE DECARBOXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-CARBOXYMUCONOLACTONE DECARBOXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI;
SOURCE 3 ORGANISM_TAXID: 266834;
SOURCE 4 STRAIN: 1021;
SOURCE 5 GENE: RA0292, SMA0559;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS PSI-BIOLOGY, NYSGRC, STRUCTURAL GENOMICS, NEW YORK STRUCTURAL
KEYWDS 2 GENOMICS RESEARCH CONSORTIUM, ALL ALPHA STRUCTURE, TRIMER, BENZOATE
KEYWDS 3 DEGRADATION, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.D.HICKEY,B.E.MCGILLICK,S.ESWARAMOORTHY,S.CHAMALA,B.EVANS,R.FOTI,
AUTHOR 2 A.GIZZI,B.HILLERICH,A.KAR,J.LAFLEUR,R.SEIDEL,G.VILLIGAS,W.ZENCHECK,
AUTHOR 3 S.C.ALMO,S.SWAMINATHAN,NEW YORK STRUCTURAL GENOMICS RESEARCH
AUTHOR 4 CONSORTIUM (NYSGRC)
REVDAT 1 15-AUG-12 4G9Q 0
JRNL AUTH H.D.HICKEY,B.E.MCGILLICK,S.ESWARAMOORTHY,S.C.ALMO,
JRNL AUTH 2 S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF A 4-CARBOXYMUCONOLACTONE DECARBOXYLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 23678
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1272
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) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1739
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.2100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1844
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 154
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.41000
REMARK 3 B22 (A**2) : -0.41000
REMARK 3 B33 (A**2) : 0.62000
REMARK 3 B12 (A**2) : -0.21000
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): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.697
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1884 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2567 ; 0.995 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 237 ; 4.371 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;34.256 ;23.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 295 ;13.736 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;15.671 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 285 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1468 ; 0.005 ; 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): 1186 ; 0.408 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1901 ; 0.836 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 698 ; 1.694 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 666 ; 2.811 ; 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 : 1.40
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 4G9Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB073915.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24950
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.300
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.30
REMARK 200 R MERGE FOR SHELL (I) : 0.10400
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: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350; 0.1M MAGNESIUM FORMATE,
REMARK 280 SODIUM IODIDE, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.17250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.12181
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 21.06367
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 52.17250
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 30.12181
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 21.06367
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 52.17250
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 30.12181
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 21.06367
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.24361
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 42.12733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 60.24361
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 42.12733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 60.24361
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 42.12733
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 MSE A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 SER A 0
REMARK 465 MSE A 1
REMARK 465 MSE A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 SER A 5
REMARK 465 ASN A 6
REMARK 465 ALA A 7
REMARK 465 GLY A 8
REMARK 465 ALA A 9
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 28 80.80 -156.23
REMARK 500 ASP A 42 -65.15 -125.72
REMARK 500 LEU A 166 -68.32 -95.27
REMARK 500 ASP A 169 -77.24 -143.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGRC-020704 RELATED DB: TARGETTRACK
DBREF 4G9Q A 1 247 UNP Q930A6 Q930A6_RHIME 1 247
SEQADV 4G9Q MSE A -21 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q HIS A -20 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q HIS A -19 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q HIS A -18 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q HIS A -17 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q HIS A -16 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q HIS A -15 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q SER A -14 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q SER A -13 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q GLY A -12 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q VAL A -11 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q ASP A -10 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q LEU A -9 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q GLY A -8 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q THR A -7 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q GLU A -6 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q ASN A -5 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q LEU A -4 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q TYR A -3 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q PHE A -2 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q GLN A -1 UNP Q930A6 EXPRESSION TAG
SEQADV 4G9Q SER A 0 UNP Q930A6 EXPRESSION TAG
SEQRES 1 A 269 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 269 GLY THR GLU ASN LEU TYR PHE GLN SER MSE MSE THR THR
SEQRES 3 A 269 SER ASN ALA GLY ALA GLN GLN PRO ASN VAL GLU GLY ARG
SEQRES 4 A 269 ARG PHE SER PRO ASP GLN VAL ARG SER VAL ALA PRO ALA
SEQRES 5 A 269 LEU GLU GLN TYR THR GLN GLN ARG LEU TYR GLY ASP VAL
SEQRES 6 A 269 TRP GLN ARG PRO GLY LEU ASN ARG ARG ASP ARG SER LEU
SEQRES 7 A 269 VAL THR ILE ALA ALA LEU ILE ALA ARG GLY GLU ALA PRO
SEQRES 8 A 269 ALA LEU THR TYR TYR ALA ASP GLN ALA LEU GLU ASN GLY
SEQRES 9 A 269 VAL LYS PRO SER GLU ILE SER GLU THR ILE THR HIS LEU
SEQRES 10 A 269 ALA TYR TYR SER GLY TRP GLY LYS ALA MSE ALA THR VAL
SEQRES 11 A 269 GLY PRO VAL SER GLU ALA PHE ALA LYS ARG GLY ILE GLY
SEQRES 12 A 269 GLN ASP GLN LEU ALA ALA VAL GLU SER THR PRO LEU PRO
SEQRES 13 A 269 LEU ASP GLU GLU ALA GLU ALA GLN ARG ALA THR THR VAL
SEQRES 14 A 269 GLY ASN GLN PHE GLY SER VAL ALA PRO GLY LEU VAL GLN
SEQRES 15 A 269 TYR THR THR ASP TYR LEU PHE ARG ASP LEU TRP LEU ARG
SEQRES 16 A 269 PRO ASP LEU ALA PRO ARG ASP ARG SER LEU VAL THR ILE
SEQRES 17 A 269 ALA ALA LEU ILE SER VAL GLY GLN VAL GLU GLN ILE THR
SEQRES 18 A 269 PHE HIS LEU ASN LYS ALA LEU ASP ASN GLY LEU SER GLU
SEQRES 19 A 269 GLU GLN ALA ALA GLU VAL ILE THR HIS LEU ALA PHE TYR
SEQRES 20 A 269 ALA GLY TRP PRO ASN ALA MSE SER ALA LEU PRO VAL ALA
SEQRES 21 A 269 LYS ALA VAL PHE GLU LYS ARG ARG GLY
MODRES 4G9Q MSE A 105 MET SELENOMETHIONINE
MODRES 4G9Q MSE A 232 MET SELENOMETHIONINE
HET MSE A 105 8
HET MSE A 232 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 2 HOH *154(H2 O)
HELIX 1 1 ASN A 13 ARG A 17 5 5
HELIX 2 2 SER A 20 SER A 26 1 7
HELIX 3 3 ALA A 28 ARG A 38 1 11
HELIX 4 4 ASP A 42 ARG A 46 5 5
HELIX 5 5 ASN A 50 ARG A 65 1 16
HELIX 6 6 GLU A 67 PRO A 69 5 3
HELIX 7 7 ALA A 70 ASN A 81 1 12
HELIX 8 8 LYS A 84 SER A 99 1 16
HELIX 9 9 GLY A 100 ALA A 106 1 7
HELIX 10 10 THR A 107 ARG A 118 1 12
HELIX 11 11 GLY A 121 LEU A 125 5 5
HELIX 12 12 ASP A 136 GLY A 152 1 17
HELIX 13 13 ALA A 155 LEU A 166 1 12
HELIX 14 14 ASP A 169 ARG A 173 5 5
HELIX 15 15 ALA A 177 VAL A 192 1 16
HELIX 16 16 GLY A 193 GLU A 196 5 4
HELIX 17 17 GLN A 197 ASN A 208 1 12
HELIX 18 18 SER A 211 GLY A 227 1 17
HELIX 19 19 GLY A 227 ARG A 246 1 20
LINK C ALA A 104 N MSE A 105 1555 1555 1.33
LINK C MSE A 105 N ALA A 106 1555 1555 1.33
LINK C ALA A 231 N MSE A 232 1555 1555 1.33
LINK C MSE A 232 N SER A 233 1555 1555 1.33
CRYST1 104.345 104.345 63.191 90.00 90.00 120.00 H 3 9
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 0.009584 0.005533 0.000000 0.00000
SCALE2 0.000000 0.011066 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015825 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
