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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 01-AUG-08 3E0X
TITLE THE CRYSTAL STRUCTURE OF A LIPASE-ESTERASE RELATED PROTEIN
TITLE 2 FROM CLOSTRIDIUM ACETOBUTYLICUM ATCC 824
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE-ESTERASE RELATED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACETOBUTYLICUM;
SOURCE 3 STRAIN: ATCC 824;
SOURCE 4 ATCC: 824;
SOURCE 5 GENE: CA_C0816;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS APC60309, LIPASE-ESTERASE RELATED PROTEIN, CLOSTRIDIUM
KEYWDS 2 ACETOBUTYLICUM ATCC 824, STRUCTURAL GENOMICS, PSI-2,
KEYWDS 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, PROTEIN
KEYWDS 4 STRUCTURE INITIATIVE, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,A.SATHER,G.COBB,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 30-SEP-08 3E0X 0
JRNL AUTH K.TAN,A.SATHER,G.COBB,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF A LIPASE-ESTERASE RELATED
JRNL TITL 2 PROTEIN FROM CLOSTRIDIUM ACETOBUTYLICUM ATCC 824
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.45 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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 72029
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3810
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4190
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.1630
REMARK 3 BIN FREE R VALUE SET COUNT : 229
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4771
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.087
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.292
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4110 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5586 ; 1.387 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 541 ; 5.139 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;39.864 ;26.557
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 805 ;11.934 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;35.774 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 645 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3038 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2031 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2887 ; 0.315 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 593 ; 0.132 ; 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): 73 ; 0.169 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 62 ; 0.146 ; 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): 2563 ; 1.221 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4080 ; 1.761 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1707 ; 2.726 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1478 ; 3.963 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4270 ; 1.544 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 759 ; 5.259 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4017 ; 3.835 ; 3.000
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3E0X COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB048735.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-2008
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97929
REMARK 200 MONOCHROMATOR : SI CRYSTAL 111
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75965
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 38.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.280
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/RESOLVE/HKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LICL 20% PEG3350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
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,1/2+Y,-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 37.57650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL ASSEMBLY IS
REMARK 300 EXPERIMENTALLY UNKNOWN. FROM MOLECULAR PACKING, THE
REMARK 300 MOLECULE IS EXPECTED TO BE A MONOMER.
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 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 350
REMARK 350 BIOMOLECULE: 2
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: B
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 SER B -2
REMARK 465 ASN B -1
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 CYS A 24 -159.83 -126.07
REMARK 500 LEU A 198 -71.34 -99.22
REMARK 500 LYS A 223 -148.51 48.86
REMARK 500 LEU B 198 -70.03 -101.52
REMARK 500 LYS B 223 -147.15 53.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXE B 243
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXE A 243
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC60309 RELATED DB: TARGETDB
DBREF 3E0X A 1 242 UNP Q97KV0 Q97KV0_CLOAB 1 242
DBREF 3E0X B 1 242 UNP Q97KV0 Q97KV0_CLOAB 1 242
SEQADV 3E0X SER A -2 UNP Q97KV0 EXPRESSION TAG
SEQADV 3E0X ASN A -1 UNP Q97KV0 EXPRESSION TAG
SEQADV 3E0X ALA A 0 UNP Q97KV0 EXPRESSION TAG
SEQADV 3E0X SER B -2 UNP Q97KV0 EXPRESSION TAG
SEQADV 3E0X ASN B -1 UNP Q97KV0 EXPRESSION TAG
SEQADV 3E0X ALA B 0 UNP Q97KV0 EXPRESSION TAG
SEQRES 1 A 245 SER ASN ALA MSE LEU HIS TYR VAL HIS VAL GLY ASN LYS
SEQRES 2 A 245 LYS SER PRO ASN THR LEU LEU PHE VAL HIS GLY SER GLY
SEQRES 3 A 245 CYS ASN LEU LYS ILE PHE GLY GLU LEU GLU LYS TYR LEU
SEQRES 4 A 245 GLU ASP TYR ASN CYS ILE LEU LEU ASP LEU LYS GLY HIS
SEQRES 5 A 245 GLY GLU SER LYS GLY GLN CYS PRO SER THR VAL TYR GLY
SEQRES 6 A 245 TYR ILE ASP ASN VAL ALA ASN PHE ILE THR ASN SER GLU
SEQRES 7 A 245 VAL THR LYS HIS GLN LYS ASN ILE THR LEU ILE GLY TYR
SEQRES 8 A 245 SER MSE GLY GLY ALA ILE VAL LEU GLY VAL ALA LEU LYS
SEQRES 9 A 245 LYS LEU PRO ASN VAL ARG LYS VAL VAL SER LEU SER GLY
SEQRES 10 A 245 GLY ALA ARG PHE ASP LYS LEU ASP LYS ASP PHE MSE GLU
SEQRES 11 A 245 LYS ILE TYR HIS ASN GLN LEU ASP ASN ASN TYR LEU LEU
SEQRES 12 A 245 GLU CYS ILE GLY GLY ILE ASP ASN PRO LEU SER GLU LYS
SEQRES 13 A 245 TYR PHE GLU THR LEU GLU LYS ASP PRO ASP ILE MSE ILE
SEQRES 14 A 245 ASN ASP LEU ILE ALA CYS LYS LEU ILE ASP LEU VAL ASP
SEQRES 15 A 245 ASN LEU LYS ASN ILE ASP ILE PRO VAL LYS ALA ILE VAL
SEQRES 16 A 245 ALA LYS ASP GLU LEU LEU THR LEU VAL GLU TYR SER GLU
SEQRES 17 A 245 ILE ILE LYS LYS GLU VAL GLU ASN SER GLU LEU LYS ILE
SEQRES 18 A 245 PHE GLU THR GLY LYS HIS PHE LEU LEU VAL VAL ASN ALA
SEQRES 19 A 245 LYS GLY VAL ALA GLU GLU ILE LYS ASN PHE ILE
SEQRES 1 B 245 SER ASN ALA MSE LEU HIS TYR VAL HIS VAL GLY ASN LYS
SEQRES 2 B 245 LYS SER PRO ASN THR LEU LEU PHE VAL HIS GLY SER GLY
SEQRES 3 B 245 CYS ASN LEU LYS ILE PHE GLY GLU LEU GLU LYS TYR LEU
SEQRES 4 B 245 GLU ASP TYR ASN CYS ILE LEU LEU ASP LEU LYS GLY HIS
SEQRES 5 B 245 GLY GLU SER LYS GLY GLN CYS PRO SER THR VAL TYR GLY
SEQRES 6 B 245 TYR ILE ASP ASN VAL ALA ASN PHE ILE THR ASN SER GLU
SEQRES 7 B 245 VAL THR LYS HIS GLN LYS ASN ILE THR LEU ILE GLY TYR
SEQRES 8 B 245 SER MSE GLY GLY ALA ILE VAL LEU GLY VAL ALA LEU LYS
SEQRES 9 B 245 LYS LEU PRO ASN VAL ARG LYS VAL VAL SER LEU SER GLY
SEQRES 10 B 245 GLY ALA ARG PHE ASP LYS LEU ASP LYS ASP PHE MSE GLU
SEQRES 11 B 245 LYS ILE TYR HIS ASN GLN LEU ASP ASN ASN TYR LEU LEU
SEQRES 12 B 245 GLU CYS ILE GLY GLY ILE ASP ASN PRO LEU SER GLU LYS
SEQRES 13 B 245 TYR PHE GLU THR LEU GLU LYS ASP PRO ASP ILE MSE ILE
SEQRES 14 B 245 ASN ASP LEU ILE ALA CYS LYS LEU ILE ASP LEU VAL ASP
SEQRES 15 B 245 ASN LEU LYS ASN ILE ASP ILE PRO VAL LYS ALA ILE VAL
SEQRES 16 B 245 ALA LYS ASP GLU LEU LEU THR LEU VAL GLU TYR SER GLU
SEQRES 17 B 245 ILE ILE LYS LYS GLU VAL GLU ASN SER GLU LEU LYS ILE
SEQRES 18 B 245 PHE GLU THR GLY LYS HIS PHE LEU LEU VAL VAL ASN ALA
SEQRES 19 B 245 LYS GLY VAL ALA GLU GLU ILE LYS ASN PHE ILE
MODRES 3E0X MSE A 1 MET SELENOMETHIONINE
MODRES 3E0X MSE A 90 MET SELENOMETHIONINE
MODRES 3E0X MSE A 126 MET SELENOMETHIONINE
MODRES 3E0X MSE A 165 MET SELENOMETHIONINE
MODRES 3E0X MSE B 1 MET SELENOMETHIONINE
MODRES 3E0X MSE B 90 MET SELENOMETHIONINE
MODRES 3E0X MSE B 126 MET SELENOMETHIONINE
MODRES 3E0X MSE B 165 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 90 8
HET MSE A 126 8
HET MSE A 165 8
HET MSE B 1 13
HET MSE B 90 8
HET MSE B 126 8
HET MSE B 165 8
HET OXE A 243 8
HET OXE B 243 8
HETNAM MSE SELENOMETHIONINE
HETNAM OXE ORTHO-XYLENE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 OXE 2(C8 H10)
FORMUL 5 HOH *754(H2 O)
HELIX 1 1 ASN A 25 GLY A 30 5 6
HELIX 2 2 GLU A 31 LEU A 36 5 6
HELIX 3 3 THR A 59 SER A 74 1 16
HELIX 4 4 SER A 89 LEU A 100 1 12
HELIX 5 5 ASP A 122 HIS A 131 1 10
HELIX 6 6 ASP A 135 GLY A 144 1 10
HELIX 7 7 ASN A 148 GLU A 156 1 9
HELIX 8 8 ASP A 161 ILE A 175 1 15
HELIX 9 9 LEU A 177 ILE A 184 5 8
HELIX 10 10 LEU A 200 VAL A 211 1 12
HELIX 11 11 GLY A 222 HIS A 224 5 3
HELIX 12 12 PHE A 225 ASN A 230 1 6
HELIX 13 13 ASN A 230 ASN A 240 1 11
HELIX 14 14 ASN B 25 GLY B 30 5 6
HELIX 15 15 GLU B 31 LEU B 36 5 6
HELIX 16 16 THR B 59 SER B 74 1 16
HELIX 17 17 SER B 89 LYS B 101 1 13
HELIX 18 18 ASP B 122 HIS B 131 1 10
HELIX 19 19 ASP B 135 GLY B 144 1 10
HELIX 20 20 ASN B 148 GLU B 156 1 9
HELIX 21 21 ASP B 161 ILE B 175 1 15
HELIX 22 22 LEU B 177 ILE B 184 5 8
HELIX 23 23 LEU B 200 VAL B 211 1 12
HELIX 24 24 GLY B 222 HIS B 224 5 3
HELIX 25 25 PHE B 225 ASN B 230 1 6
HELIX 26 26 ASN B 230 ASN B 240 1 11
SHEET 1 A 7 TYR A 4 GLY A 8 0
SHEET 2 A 7 ASN A 40 LEU A 44 -1 O LEU A 43 N VAL A 5
SHEET 3 A 7 THR A 15 VAL A 19 1 N LEU A 16 O ILE A 42
SHEET 4 A 7 ILE A 83 TYR A 88 1 O ILE A 86 N VAL A 19
SHEET 5 A 7 VAL A 106 LEU A 112 1 O LEU A 112 N GLY A 87
SHEET 6 A 7 VAL A 188 ALA A 193 1 O LYS A 189 N SER A 111
SHEET 7 A 7 SER A 214 PHE A 219 1 O PHE A 219 N VAL A 192
SHEET 1 B 7 TYR B 4 GLY B 8 0
SHEET 2 B 7 ASN B 40 LEU B 44 -1 O LEU B 43 N VAL B 5
SHEET 3 B 7 THR B 15 VAL B 19 1 N LEU B 16 O ILE B 42
SHEET 4 B 7 ILE B 83 TYR B 88 1 O ILE B 86 N VAL B 19
SHEET 5 B 7 VAL B 106 LEU B 112 1 O LEU B 112 N GLY B 87
SHEET 6 B 7 VAL B 188 ALA B 193 1 O LYS B 189 N SER B 111
SHEET 7 B 7 SER B 214 PHE B 219 1 O LYS B 217 N ALA B 190
LINK C ALA A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N LEU A 2 1555 1555 1.32
LINK C SER A 89 N MSE A 90 1555 1555 1.33
LINK C MSE A 90 N GLY A 91 1555 1555 1.33
LINK C PHE A 125 N MSE A 126 1555 1555 1.33
LINK C MSE A 126 N GLU A 127 1555 1555 1.33
LINK C ILE A 164 N MSE A 165 1555 1555 1.34
LINK C MSE A 165 N ILE A 166 1555 1555 1.33
LINK C ALA B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N LEU B 2 1555 1555 1.33
LINK C SER B 89 N MSE B 90 1555 1555 1.34
LINK C MSE B 90 N GLY B 91 1555 1555 1.33
LINK C PHE B 125 N MSE B 126 1555 1555 1.33
LINK C MSE B 126 N GLU B 127 1555 1555 1.35
LINK C ILE B 164 N MSE B 165 1555 1555 1.34
LINK C MSE B 165 N ILE B 166 1555 1555 1.32
SITE 1 AC1 10 GLY B 21 SER B 22 CYS B 24 TYR B 88
SITE 2 AC1 10 SER B 89 LEU B 139 ILE B 143 LEU B 198
SITE 3 AC1 10 HIS B 224 HOH B 473
SITE 1 AC2 10 GLY A 21 SER A 22 CYS A 24 TYR A 88
SITE 2 AC2 10 SER A 89 LEU A 139 LEU A 158 LEU A 198
SITE 3 AC2 10 HIS A 224 HOH A 428
CRYST1 44.611 75.153 68.206 90.00 97.89 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 0.022416 0.000000 0.003107 0.00000
SCALE2 0.000000 0.013306 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014802 0.00000
END |