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HEADER HYDROLASE 03-FEB-06 2FX5
TITLE PSEUDOMONAS MENDOCINA LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS MENDOCINA;
SOURCE 3 EXPRESSION_SYSTEM: BACILLUS SUBTILIS
KEYWDS ALPHA-BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BOTT,S.WU
REVDAT 1 01-AUG-06 2FX5 0
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 19100
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 19100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1947
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.013 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 3.100 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.020 ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FX5 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-2006.
REMARK 100 THE RCSB ID CODE IS RCSB036416.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-1991
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU 200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19100
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MIR
REMARK 200 SOFTWARE USED: PROTEIN
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM SODIUM ACETATE, 18% SATURATED
REMARK 280 POTASSIUM TARTRATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 1/2-Y,1/2+X,3/4+Z
REMARK 290 4555 1/2+Y,1/2-X,1/4+Z
REMARK 290 5555 1/2-X,1/2+Y,3/4-Z
REMARK 290 6555 1/2+X,1/2-Y,1/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,1/2-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.50000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 29.25000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 29.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 108.75000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 29.25000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 29.25000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.25000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 29.25000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 29.25000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 108.75000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 29.25000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 29.25000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.25000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 72.50000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 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
REMARK 500 OE1 GLN A 165 O HOH 359 2.02
REMARK 500 NE ARG A 190 O HOH 301 2.10
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 NE2 GLN A 44 OH TYR A 182 8566 2.19
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 M RES CSSEQI PSI PHI
REMARK 500 TYR A 203 -33.17 71.08
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE WAS NO SEQUENCE DATABASE REFERENCE
REMARK 999 AT TIME OF PROCESSING.
SEQRES 1 A 258 ALA PRO LEU PRO ASP THR PRO GLY ALA PRO PHE PRO ALA
SEQRES 2 A 258 VAL ALA ASN PHE ASP ARG SER GLY PRO TYR THR VAL SER
SEQRES 3 A 258 SER GLN SER GLU GLY PRO SER CYS ARG ILE TYR ARG PRO
SEQRES 4 A 258 ARG ASP LEU GLY GLN GLY GLY VAL ARG HIS PRO VAL ILE
SEQRES 5 A 258 LEU TRP GLY ASN GLY THR GLY ALA GLY PRO SER THR TYR
SEQRES 6 A 258 ALA GLY LEU LEU SER HIS TRP ALA SER HIS GLY PHE VAL
SEQRES 7 A 258 VAL ALA ALA ALA GLU THR SER ASN ALA GLY THR GLY ARG
SEQRES 8 A 258 GLU MET LEU ALA CYS LEU ASP TYR LEU VAL ARG GLU ASN
SEQRES 9 A 258 ASP THR PRO TYR GLY THR TYR SER GLY LYS LEU ASN THR
SEQRES 10 A 258 GLY ARG VAL GLY THR SER GLY HIS SER GLN GLY GLY GLY
SEQRES 11 A 258 GLY SER ILE MET ALA GLY GLN ASP THR ARG VAL ARG THR
SEQRES 12 A 258 THR ALA PRO ILE GLN PRO TYR THR LEU GLY LEU GLY HIS
SEQRES 13 A 258 ASP SER ALA SER GLN ARG ARG GLN GLN GLY PRO MET PHE
SEQRES 14 A 258 LEU MET SER GLY GLY GLY ASP THR ILE ALA PHE PRO TYR
SEQRES 15 A 258 LEU ASN ALA GLN PRO VAL TYR ARG ARG ALA ASN VAL PRO
SEQRES 16 A 258 VAL PHE TRP GLY GLU ARG ARG TYR VAL SER HIS PHE GLU
SEQRES 17 A 258 PRO VAL GLY SER GLY GLY ALA TYR ARG GLY PRO SER THR
SEQRES 18 A 258 ALA TRP PHE ARG PHE GLN LEU MET ASP ASP GLN ASP ALA
SEQRES 19 A 258 ARG ALA THR PHE TYR GLY ALA GLN CYS SER LEU CYS THR
SEQRES 20 A 258 SER LEU LEU TRP SER VAL GLU ARG ARG GLY LEU
HET TLA 259 10
HETNAM TLA L(+)-TARTARIC ACID
FORMUL 2 TLA C4 H6 O6
FORMUL 3 HOH *104(H2 O1)
HELIX 1 1 GLY A 43 VAL A 47 5 5
HELIX 2 2 GLY A 61 THR A 64 5 4
HELIX 3 3 TYR A 65 HIS A 75 1 11
HELIX 4 4 GLY A 90 THR A 106 1 17
HELIX 5 5 GLN A 127 GLY A 136 1 10
HELIX 6 6 ASP A 157 ARG A 163 5 7
HELIX 7 7 PHE A 180 ALA A 185 1 6
HELIX 8 8 ALA A 185 ALA A 192 1 8
HELIX 9 9 GLY A 213 ALA A 215 5 3
HELIX 10 10 TYR A 216 ASP A 230 1 15
HELIX 11 11 ASP A 231 ALA A 236 1 6
HELIX 12 12 CYS A 243 SER A 248 1 6
SHEET 1 A 6 VAL A 25 GLU A 30 0
SHEET 2 A 6 CYS A 34 PRO A 39 -1 O ILE A 36 N GLN A 28
SHEET 3 A 6 VAL A 78 ALA A 82 -1 O VAL A 79 N TYR A 37
SHEET 4 A 6 HIS A 49 GLY A 55 1 N PRO A 50 O VAL A 78
SHEET 5 A 6 LEU A 115 SER A 126 1 O ARG A 119 N VAL A 51
SHEET 6 A 6 THR A 143 PRO A 149 1 O ILE A 147 N GLY A 124
SHEET 1 B 3 MET A 168 GLY A 173 0
SHEET 2 B 3 VAL A 196 ARG A 201 1 O GLY A 199 N LEU A 170
SHEET 3 B 3 TRP A 251 ARG A 256 -1 O GLU A 254 N TRP A 198
SSBOND 1 CYS A 34 CYS A 96
SSBOND 2 CYS A 243 CYS A 246
CISPEP 1 ALA A 1 PRO A 2 0 -0.03
CRYST1 58.500 58.500 145.000 90.00 90.00 90.00 P 43 21 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 0.017094 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017094 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006897 0.00000
TER 1948 LEU A 258
MASTER 253 0 1 12 9 0 0 6 2061 1 14 20
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