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HEADER HYDROLASE 03-OCT-13 3WJ1
TITLE CRYSTAL STRUCTURE OF SSHESTI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 3 ORGANISM_TAXID: 2286;
SOURCE 4 GENE: SSHESTI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTC99A
KEYWDS ALPHA/BETA-HYDRORASE FOLD, CARBOXYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.OHARA,H.UNNO,Y.OSHIMA,K.FURUKAWA,N.FUJINO,K.HIROOKA,H.HEMMI,
AUTHOR 2 S.TAKAHASHI,T.NISHINO,M.KUSUNOKI,T.NAKAYAMA
REVDAT 1 30-JUL-14 3WJ1 0
JRNL AUTH K.OHARA,H.UNNO,Y.OSHIMA,M.HOSOYA,N.FUJINO,K.HIROOKA,
JRNL AUTH 2 S.TAKAHASHI,S.YAMASHITA,M.KUSUNOKI,T.NAKAYAMA
JRNL TITL STRUCTURAL INSIGHTS INTO THE LOW-PH ADAPTATION OF A UNIQUE
JRNL TITL 2 CARBOXYLESTERASE FROM FERROPLASMA: ALTERING THE PH OPTIMA OF
JRNL TITL 3 TWO CARBOXYLESTERASES
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M113.521856
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 43087
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2301
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3176
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.1800
REMARK 3 BIN FREE R VALUE SET COUNT : 169
REMARK 3 BIN FREE R VALUE : 0.2190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2362
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.03
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) : 0.00000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.069
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.036
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2475 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2310 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3364 ; 1.455 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5375 ; 0.826 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 305 ; 5.868 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;33.115 ;23.458
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 403 ;11.838 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.937 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 383 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2731 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 517 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 567 ; 0.226 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2428 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1280 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1331 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 198 ; 0.178 ; 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): 18 ; 0.332 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 88 ; 0.284 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.203 ; 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): 1946 ; 1.114 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 618 ; 0.204 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2470 ; 1.300 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1122 ; 2.249 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 891 ; 3.057 ; 4.500
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 : BABINET MODEL WITH 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 3WJ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB096396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : 90.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45391
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 24.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.29800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG MME 2000, 100MM TRIS-HCL, PH
REMARK 280 7.00, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 29.20150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.97100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 68.66600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.20150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.97100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.66600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.20150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 35.97100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.66600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.20150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 35.97100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.66600
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 71.94200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 71.94200
REMARK 350 BIOMT3 4 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 1
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 OE1 GLU A 55 O HOH A 622 1.84
REMARK 500 OH TYR A 172 O HOH A 652 1.89
REMARK 500 O HOH A 617 O HOH A 767 2.01
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 CG GLN A 33 O HOH A 764 8555 2.15
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 VAL A 16 152.98 -42.31
REMARK 500 SER A 151 -117.98 63.60
REMARK 500 LYS A 167 -64.20 -140.90
REMARK 500 ASP A 169 74.31 -114.07
REMARK 500 TYR A 177 61.74 32.69
REMARK 500 PHE A 197 -64.77 78.40
REMARK 500 SER A 223 76.17 -119.53
REMARK 500 TYR A 243 40.34 -103.80
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 BOG A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WJ2 RELATED DB: PDB
REMARK 900 RELATED ID: 4P9N RELATED DB: PDB
DBREF 3WJ1 A 1 305 UNP Q5NU42 Q5NU42_SULSH 1 305
SEQRES 1 A 305 MET PRO LEU ASP PRO ARG ILE LYS LYS LEU LEU GLU SER
SEQRES 2 A 305 GLY PHE VAL VAL PRO ILE GLY LYS ALA SER VAL ASP GLU
SEQRES 3 A 305 VAL ARG LYS ILE PHE ARG GLN LEU ALA SER ALA ALA PRO
SEQRES 4 A 305 LYS ALA GLU VAL ARG LYS VAL GLU ASP ILE LYS ILE PRO
SEQRES 5 A 305 GLY SER GLU THR SER ILE ASN ALA ARG VAL TYR PHE PRO
SEQRES 6 A 305 LYS ALA LYS GLY PRO TYR GLY VAL LEU VAL TYR LEU HIS
SEQRES 7 A 305 GLY GLY GLY PHE VAL ILE GLY ASP VAL GLU SER TYR ASP
SEQRES 8 A 305 PRO LEU CYS ARG ALA ILE THR ASN ALA CYS ASN CYS VAL
SEQRES 9 A 305 VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU TYR LYS
SEQRES 10 A 305 PHE PRO SER ALA VAL ILE ASP SER PHE ASP ALA THR ASN
SEQRES 11 A 305 TRP ILE TYR ASN ASN LEU ASP LYS PHE ASP GLY GLU MET
SEQRES 12 A 305 GLY ILE ALA ILE ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 13 A 305 ALA ALA VAL VAL ALA LEU LEU SER LYS GLY LYS LEU ASP
SEQRES 14 A 305 LEU LYS TYR GLN ILE LEU ILE TYR PRO ALA VAL GLY PHE
SEQRES 15 A 305 ASP SER VAL SER ARG SER MET ILE GLU TYR SER ASP GLY
SEQRES 16 A 305 PHE PHE LEU THR ARG GLU HIS ILE GLU TRP PHE GLY SER
SEQRES 17 A 305 GLN TYR LEU ARG SER PRO ALA ASP LEU LEU ASP PHE ARG
SEQRES 18 A 305 PHE SER PRO ILE ILE ALA GLN ASP LEU SER GLY LEU PRO
SEQRES 19 A 305 PRO ALA LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG
SEQRES 20 A 305 ASP GLN GLY GLU ALA TYR ALA ASN ARG LEU LEU GLN ALA
SEQRES 21 A 305 GLY VAL PRO VAL THR SER VAL ARG PHE ASN ASN VAL ILE
SEQRES 22 A 305 HIS GLY PHE LEU SER PHE PHE PRO LEU ILE ASP GLN GLY
SEQRES 23 A 305 LYS ASP ALA ILE GLY LEU ILE GLY SER VAL LEU ARG ARG
SEQRES 24 A 305 THR PHE TYR ASP LYS SER
HET BOG A 401 20
HETNAM BOG B-OCTYLGLUCOSIDE
FORMUL 2 BOG C14 H28 O6
FORMUL 3 HOH *273(H2 O)
HELIX 1 1 ASP A 4 SER A 13 1 10
HELIX 2 2 SER A 23 ALA A 37 1 15
HELIX 3 3 TYR A 90 ASN A 102 1 13
HELIX 4 4 PRO A 119 ASN A 135 1 17
HELIX 5 5 LEU A 136 ASP A 140 5 5
HELIX 6 6 SER A 151 LYS A 165 1 15
HELIX 7 7 SER A 186 TYR A 192 1 7
HELIX 8 8 THR A 199 LEU A 211 1 13
HELIX 9 9 SER A 213 ASP A 219 5 7
HELIX 10 10 SER A 223 ALA A 227 5 5
HELIX 11 11 LEU A 246 ALA A 260 1 15
HELIX 12 12 GLY A 275 PHE A 280 5 6
HELIX 13 13 ILE A 283 ASP A 303 1 21
SHEET 1 A 8 LYS A 45 PRO A 52 0
SHEET 2 A 8 SER A 57 PHE A 64 -1 O VAL A 62 N GLU A 47
SHEET 3 A 8 VAL A 104 VAL A 108 -1 O SER A 107 N ARG A 61
SHEET 4 A 8 GLY A 72 LEU A 77 1 N LEU A 74 O VAL A 104
SHEET 5 A 8 GLY A 144 ASP A 150 1 O GLY A 144 N VAL A 73
SHEET 6 A 8 LEU A 170 ILE A 176 1 O LYS A 171 N ILE A 145
SHEET 7 A 8 ALA A 236 ALA A 241 1 O LEU A 237 N LEU A 175
SHEET 8 A 8 VAL A 264 PHE A 269 1 O PHE A 269 N THR A 240
SSBOND 1 CYS A 101 CYS A 103 1555 1555 2.51
CISPEP 1 GLY A 69 PRO A 70 0 0.85
CISPEP 2 ALA A 113 PRO A 114 0 -0.81
CISPEP 3 PHE A 118 PRO A 119 0 0.36
SITE 1 AC1 10 SER A 151 ILE A 203 GLU A 204 GLY A 207
SITE 2 AC1 10 SER A 208 LEU A 211 LEU A 217 PHE A 222
SITE 3 AC1 10 HOH A 741 HOH A 745
CRYST1 58.403 71.942 137.332 90.00 90.00 90.00 I 2 2 2 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 0.017122 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013900 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007282 0.00000
TER 2396 SER A 305
MASTER 336 0 1 13 8 0 3 6 2655 1 22 24
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