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HEADER LIPASE 11-JAN-02 1GT6
TITLE S146A MUTANT OF THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE
TITLE 2 COMPLEX WITH OLEIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 4 CHAIN: A, B;
COMPND 5 EC: 3.1.1.3;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: OLEIC ACID
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS
KEYWDS HYDROLASE, LIPID DEGRADATION, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.BRZOZOWSKI,S.YAPOUDJIAN,M.G.IVANOVA,S.A.PATKAR,J.VIND,
AUTHOR 2 A.SVENDSEN,R.VERGER
REVDAT 1 23-JAN-03 1GT6 0
JRNL AUTH S.YAPOUDJIAN,M.G.IVANOVA,A.M.BRZOZOWSKI,S.A.PATKAR,
JRNL AUTH 2 J.VIND,A.SVENDSEN,R.VERGER
JRNL TITL BINDING OF THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE
JRNL TITL 2 TO THE MIXED MICELLES OF CIS-PARINARIC ACID/NATDC:
JRNL TITL 3 FLUORESCENCE RESONANCE ENERGY TRANSFER AND
JRNL TITL 4 CRYSTALLOGRAPHIC STUDY
JRNL REF EUR.J.BIOCHEM. V. 269 1613 2002
JRNL REFN ASTM EJBCAI IX ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.2
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 30644
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) : 0.21564
REMARK 3 R VALUE (WORKING SET) : 0.21432
REMARK 3 FREE R VALUE : 0.23939
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1642
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NONE
REMARK 3 BIN RESOLUTION RANGE HIGH : NONE
REMARK 3 BIN RESOLUTION RANGE LOW : NONE
REMARK 3 REFLECTION IN BIN (WORKING SET) : NONE
REMARK 3 BIN R VALUE (WORKING SET) : NONE
REMARK 3 BIN FREE R VALUE SET COUNT : NONE
REMARK 3 BIN FREE R VALUE : NONE
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4140
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 169
REMARK 3
REMARK 3 B VALUES
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.158
REMARK 3 B11 (A**2) : 5.76
REMARK 3 B22 (A**2) : -3.57
REMARK 3 B33 (A**2) : -2.18
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.27451
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.20358
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.15322
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.96346
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9407
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9214
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4196 ; 0.009 ; 0.021
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5699 ; 1.322 ; 1.935
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 525 ; 3.522 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 650 ;18.120 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 614 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3297 ; 0.005 ; 0.020
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 20 ; 0.247 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.118 ; 0.500
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2616 ; 0.212 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4183 ; 0.408 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1580 ; 0.763 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1516 ; 1.288 ; 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 : NONE
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NONE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.4
REMARK 3 ION PROBE RADIUS : 0.8
REMARK 3 SHRINKAGE RADIUS : 0.8
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: OLEIC ACID IN MOLECULE B IS COMPLETE BUT
REMARK 3 IN MOLECULE A ALKYL CHAIN IS VISIBLE TILL C10 CARBON SO THE
REMARK 3 OCCUPANCY OF THE C11-C18 WERE SET TO 0 (BUT MODELLED).
REMARK 4
REMARK 4 1GT6 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 14-JAN-2002.
REMARK 100 THE EBI ID CODE IS EBI-9260.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.51
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33614
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.2
REMARK 200 RESOLUTION RANGE LOW (A) : 20
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.5
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.075
REMARK 200 FOR THE DATA SET : 9.3
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.2
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.50
REMARK 200 FOR SHELL : 2.5
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1DT5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5 TRIS BUFFER, 25 MM MGCL2,
REMARK 280 25% W/V PEG 5K MME, 10 MM PROTEIN CONC 10-20 MG/ML IN 10 MM
REMARK 280 TRIS BUFFER PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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 1/2-X,1/2+Y,-Z
REMARK 290 4555 1/2+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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 58.55050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.65200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.55050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.65200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
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 350 BIOMOLECULE: 2
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED MUTATION SER 168 ALA CHAINS A AND B
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ILE A 76 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 ASP B 27 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 ALA B 30 C - N - CA ANGL. DEV. = 13.8 DEGREES
REMARK 500 THR B 35 CA - C - N ANGL. DEV. = -11.2 DEGREES
REMARK 500 CYS B 36 C - N - CA ANGL. DEV. = -16.6 DEGREES
REMARK 500 ILE B 86 CB - CG1 - CD1 ANGL. DEV. = 16.8 DEGREES
REMARK 500 ARG B 118 CB - CG - CD ANGL. DEV. = -10.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 24 CB LYS A 24 CG -0.226
REMARK 500 ASP B 27 N ASP B 27 CA 0.273
REMARK 500 ILE B 86 CB ILE B 86 CG2 -0.353
REMARK 500 ARG B 118 CG ARG B 118 CD 0.275
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500 OD2 ASP A 48 OG1 THR A 72 2.14
REMARK 500 ND2 ASN A 94 O HOH Z 42 2.18
REMARK 500 ND2 ASN B 94 O HOH Y 14 2.18
REMARK 500 O HOH Y 29 O HOH Y 31 2.12
REMARK 500 O HOH Z 9 O HOH Z 17 2.11
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 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
REMARK 500 ALA A 146 57.34 -117.48
REMARK 500 THR A 199 29.37 -118.16
REMARK 500 PHE A 262 73.87 -35.92
REMARK 500 ALA B 146 59.20 -119.51
REMARK 500 THR B 199 30.41 -115.37
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: OLA
REMARK 800 SITE_DESCRIPTION: OLA BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: OLB
REMARK 800 SITE_DESCRIPTION: OLA BINDING SITE FOR CHAIN B
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DT3 RELATED DB: PDB
REMARK 900 THE STRUCTURAL ORIGINS OF INTERFACIAL
REMARK 900 ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA
REMARK 900 LIPASE
REMARK 900 RELATED ID: 1DT5 RELATED DB: PDB
REMARK 900 THE STRUCTURAL ORIGINS OF INTERFACIAL
REMARK 900 ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA
REMARK 900 LIPASE
REMARK 900 RELATED ID: 1DTE RELATED DB: PDB
REMARK 900 THE STRUCTURAL ORIGINS OF INTERFACIAL
REMARK 900 ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA
REMARK 900 LIPASE
REMARK 900 RELATED ID: 1DU4 RELATED DB: PDB
REMARK 900 THE STRUCTURAL ORIGINS OF INTERFACIAL
REMARK 900 ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA
REMARK 900 LIPASE OTHER STRUCTURE DETAILS
DBREF 1GT6 A 1 269 SWS O59952 LIP_THELA 23 291
DBREF 1GT6 B 1 269 SWS O59952 LIP_THELA 23 291
SEQADV 1GT6 ALA A 146 SWS O59952 SER 168 ENGINEERED MUTATION
SEQADV 1GT6 ALA B 146 SWS O59952 SER 168 ENGINEERED MUTATION
SEQRES 1 A 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 A 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 A 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 A 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 A 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 A 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 A 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 A 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 A 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 A 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 A 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 A 269 GLY HIS ALA LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 A 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 A 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 A 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 A 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 A 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 A 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 A 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 A 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 A 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
SEQRES 1 B 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 B 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 B 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 B 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 B 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 B 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 B 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 B 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 B 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 B 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 B 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 B 269 GLY HIS ALA LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 B 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 B 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 B 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 B 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 B 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 B 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 B 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 B 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 B 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
HET OLA A1270 20
HET OLA B1270 20
HETNAM OLA OLEIC ACID
FORMUL 3 OLA 2(C18 H34 O2)
FORMUL 4 HOH *169(H2 O1)
HELIX 1 1 SER A 3 ALA A 20 1 18
HELIX 2 2 TYR A 21 ASP A 27 5 7
HELIX 3 3 CYS A 41 ALA A 47 1 7
HELIX 4 4 SER A 85 LEU A 93 1 9
HELIX 5 5 ASP A 111 HIS A 135 1 25
HELIX 6 6 ALA A 146 ARG A 160 1 15
HELIX 7 7 ASN A 178 GLN A 188 1 11
HELIX 8 8 ILE A 202 LEU A 206 5 5
HELIX 9 9 PRO A 208 GLY A 212 5 5
HELIX 10 10 THR A 231 ASN A 233 5 3
HELIX 11 11 ILE A 255 LEU A 259 5 5
HELIX 12 12 SER B 3 ALA B 20 1 18
HELIX 13 13 TYR B 21 ASN B 26 5 6
HELIX 14 14 SER B 85 LEU B 93 1 9
HELIX 15 15 ASP B 111 HIS B 135 1 25
HELIX 16 16 ALA B 146 ARG B 160 1 15
HELIX 17 17 ASN B 178 GLN B 188 1 11
HELIX 18 18 ILE B 202 LEU B 206 5 5
HELIX 19 19 PRO B 208 GLY B 212 5 5
HELIX 20 20 THR B 231 ASN B 233 5 3
HELIX 21 21 ILE B 255 LEU B 259 5 5
SHEET 1 AA 8 ALA A 49 SER A 58 0
SHEET 2 AA 8 VAL A 63 ASP A 70 -1 O VAL A 63 N SER A 58
SHEET 3 AA 8 LEU A 75 PHE A 80 -1 O LEU A 75 N ASP A 70
SHEET 4 AA 8 ARG A 139 HIS A 145 1 O ARG A 139 N ILE A 76
SHEET 5 AA 8 ILE A 166 TYR A 171 1 O ASP A 167 N PHE A 142
SHEET 6 AA 8 LEU A 193 HIS A 198 1 O TYR A 194 N SER A 170
SHEET 7 AA 8 GLU A 219 ILE A 222 1 O TYR A 220 N THR A 197
SHEET 8 AA 8 ILE A 235 ILE A 238 -1 O VAL A 236 N TRP A 221
SHEET 1 AB 2 LEU A 97 GLU A 99 0
SHEET 2 AB 2 ARG A 108 HIS A 110 -1 O GLY A 109 N LYS A 98
SHEET 1 BA 8 THR B 50 SER B 58 0
SHEET 2 BA 8 VAL B 63 ASP B 70 -1 O VAL B 63 N SER B 58
SHEET 3 BA 8 LEU B 75 PHE B 80 -1 O LEU B 75 N ASP B 70
SHEET 4 BA 8 ARG B 139 HIS B 145 1 O ARG B 139 N ILE B 76
SHEET 5 BA 8 ILE B 166 TYR B 171 1 O ASP B 167 N PHE B 142
SHEET 6 BA 8 LEU B 193 HIS B 198 1 O TYR B 194 N SER B 170
SHEET 7 BA 8 GLU B 219 ILE B 222 1 O TYR B 220 N THR B 197
SHEET 8 BA 8 ILE B 235 ILE B 238 -1 O VAL B 236 N TRP B 221
SHEET 1 BB 2 LEU B 97 GLU B 99 0
SHEET 2 BB 2 ARG B 108 HIS B 110 -1 O GLY B 109 N LYS B 98
SSBOND 1 CYS A 22 CYS A 268 1555 1555
SSBOND 2 CYS A 36 CYS A 41 1555 1555
SSBOND 3 CYS A 104 CYS A 107 1555 1555
SSBOND 4 CYS B 22 CYS B 268 1555 1555
SSBOND 5 CYS B 36 CYS B 41 1555 1555
SSBOND 6 CYS B 104 CYS B 107 1555 1555
CISPEP 1 LEU A 206 PRO A 207 0 -8.89
CISPEP 2 SER A 217 PRO A 218 0 0.37
CISPEP 3 LEU B 206 PRO B 207 0 -9.96
CISPEP 4 SER B 217 PRO B 218 0 0.72
CISPEP 5 ALA A 47 ASP A 48 0 2.48
SITE 1 OLA 7 GLY A 82 SER A 83 ASN A 92 HIS A 145
SITE 2 OLA 7 ALA A 146 LEU A 147 HIS A 258
SITE 1 OLB 6 TYR B 21 SER B 83 ASN B 92 HIS B 110
SITE 2 OLB 6 ALA B 146 HIS B 258
CRYST1 117.101 97.304 55.508 90.00 90.00 90.00 P 21 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 0.008540 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010277 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018015 0.00000
END |