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HEADER HYDROLASE 12-JAN-00 1DTE
TITLE THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN
TITLE 2 THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;
SOURCE 3 ORGANISM_COMMON: FUNGI
KEYWDS LIPASE, THERMOMYCES LINUGINOSA, INTERFACIAL ACTIVATION,
KEYWDS 2 ALPA-BETA STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.BROZOZOWSKI,H.SAVAGE
REVDAT 1 20-DEC-00 1DTE 0
JRNL AUTH A.M.BROZOZOWSKI,H.SAVAGE,C.S.VERMA,J.P.TURKENBURG,
JRNL AUTH 2 D.M.LAWSON,A.SVENDSEN,S.PATKAR
JRNL TITL STRUCTURAL ORIGINS OF THE INTERFACIAL ACTIVATION
JRNL TITL 2 IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE.
JRNL REF BIOCHEMISTRY V. 39 15071 2000
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 3 NUMBER OF REFLECTIONS : 21611
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.263
REMARK 3 FREE R VALUE : 0.352
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1108
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4142
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 286
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.00
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; 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: DATA WAS TWINNED AND DETWINNED.
REMARK 3 THUS, PROBABLY THE REASON FOR HIGHER THAN NORMAL R-
REMARK 3 FACTORS.
REMARK 4
REMARK 4 1DTE COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-2000.
REMARK 100 THE RCSB ID CODE IS RCSB010351.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-1998
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 8.10
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24301
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 49.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.11600
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000, MAGNESIUM CHLORIDE,
REMARK 280 C8E5
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 48.06350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.54800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.06350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.54800
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 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 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 O HOH 266 O HOH 235 0.04
REMARK 500 O HOH 266 O HOH 177 0.06
REMARK 500 O HOH 263 O HOH 244 0.07
REMARK 500 O HOH 273 O HOH 250 0.09
REMARK 500 O HOH 281 O HOH 272 0.10
REMARK 500 O HOH 252 O HOH 281 0.10
REMARK 500 O HOH 243 O HOH 281 0.10
REMARK 500 O HOH 281 O HOH 262 0.10
REMARK 500 O HOH 228 O HOH 281 0.10
REMARK 500 O HOH 216 O HOH 273 0.10
REMARK 500 O HOH 99 O HOH 273 0.11
REMARK 500 O HOH 281 O HOH 214 0.11
REMARK 500 O HOH 270 O HOH 259 0.11
REMARK 500 O HOH 193 O HOH 281 0.11
REMARK 500 O HOH 270 O HOH 249 0.11
REMARK 500 O HOH 270 O HOH 224 0.11
REMARK 500 O HOH 205 O HOH 270 0.11
REMARK 500 O HOH 239 O HOH 270 0.11
REMARK 500 O HOH 268 O HOH 171 0.12
REMARK 500 O HOH 270 O HOH 181 0.12
REMARK 500 O HOH 236 O HOH 202 0.14
REMARK 500 O HOH 236 O HOH 55 0.15
REMARK 500 O HOH 154 O HOH 263 0.20
REMARK 500 O HOH 263 O HOH 229 0.20
REMARK 500 O HOH 263 O HOH 195 0.20
REMARK 500 O HOH 263 O HOH 215 0.20
REMARK 500 O HOH 283 O HOH 264 0.22
REMARK 500 O HOH 105 O HOH 281 0.25
REMARK 500 O HOH 135 O HOH 206 0.26
REMARK 500 O HOH 22 O HOH 266 0.35
REMARK 500 O HOH 246 O HOH 274 0.35
REMARK 500 O HOH 197 O HOH 175 0.44
REMARK 500 O HOH 200 O HOH 282 0.46
REMARK 500 O HOH 131 O HOH 179 0.47
REMARK 500 N GLU B 1 O HOH 183 0.78
REMARK 500 O HOH 151 O HOH 13 0.86
REMARK 500 O HOH 172 N GLU A 1 0.91
REMARK 500 O HOH 183 CA GLU B 1 1.22
REMARK 500 CA GLU A 1 O HOH 172 1.27
REMARK 500 O HOH 13 O HOH 121 1.68
REMARK 500 O HOH 183 CB GLU B 1 2.01
REMARK 500 O HOH 123 O HOH 7 2.07
REMARK 500 CG GLU B 1 O HOH 183 2.17
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 O HOH 246 O HOH 12 2664 1.74
REMARK 500 O HOH 274 O HOH 12 2664 2.02
REMARK 500 O HOH 61 O HOH 111 3657 2.14
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 (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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 1 N VAL A 2 C 0.254
REMARK 500 GLU B 1 N VAL B 2 C 0.216
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 ASN A 162 CA - CB - CG ANGL. DEV. = 26.9 DEGREES
REMARK 500 GLU B 210 CA - CB - CG ANGL. DEV. = 24.4 DEGREES
REMARK 500 THR B 244 CA - C - N ANGL. DEV. = 23.3 DEGREES
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 SER A 146 55.33 -116.76
REMARK 500 THR A 199 36.68 -114.04
REMARK 500 THR B 199 34.14 -113.62
REMARK 500 PHE B 262 76.91 -31.31
DBREF 1DTE A 1 269 GB 2997733 AF054513 23 291
DBREF 1DTE B 1 269 GB 2997733 AF054513 23 291
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 SER 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 SER 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
FORMUL 3 HOH *286(H2 O1)
HELIX 1 1 SER A 3 ALA A 20 1 18
HELIX 2 2 TYR A 21 TYR A 21 5 1
HELIX 3 3 CYS A 22 ASP A 27 5 6
HELIX 4 4 CYS A 36 ALA A 40 5 5
HELIX 5 5 CYS A 41 ALA A 47 1 7
HELIX 6 6 SER A 85 ASN A 92 1 8
HELIX 7 7 ASP A 111 ALA A 121 1 11
HELIX 8 8 VAL A 120 HIS A 135 1 16
HELIX 9 9 SER A 146 ARG A 160 1 15
HELIX 10 10 ASN A 178 GLN A 188 1 11
HELIX 11 11 ILE A 202 LEU A 206 5 5
HELIX 12 12 PRO A 208 GLY A 212 5 5
HELIX 13 13 THR A 231 ASN A 233 5 3
HELIX 14 14 ILE A 255 LEU A 259 5 5
HELIX 15 15 SER B 3 ALA B 19 1 17
HELIX 16 16 ALA B 20 TYR B 21 5 2
HELIX 17 17 CYS B 22 ASP B 27 5 6
HELIX 18 18 CYS B 41 ALA B 47 1 7
HELIX 19 19 SER B 85 ASN B 94 1 10
HELIX 20 20 ASP B 111 HIS B 135 1 25
HELIX 21 21 SER B 146 ARG B 160 1 15
HELIX 22 22 ASN B 178 GLN B 188 1 11
HELIX 23 23 ILE B 202 LEU B 206 5 5
HELIX 24 24 PRO B 208 GLY B 212 5 5
HELIX 25 25 THR B 231 ASN B 233 5 3
HELIX 26 26 ILE B 255 LEU B 259 5 5
SHEET 1 A 8 ALA A 49 SER A 58 0
SHEET 2 A 8 VAL A 63 ASP A 70 -1 N VAL A 63 O SER A 58
SHEET 3 A 8 LEU A 75 PHE A 80 -1 O LEU A 75 N ASP A 70
SHEET 4 A 8 ARG A 139 HIS A 145 1 O ARG A 139 N ILE A 76
SHEET 5 A 8 ILE A 166 TYR A 171 1 N ASP A 167 O VAL A 140
SHEET 6 A 8 LEU A 193 HIS A 198 1 N TYR A 194 O VAL A 168
SHEET 7 A 8 GLU A 219 ILE A 222 1 O TYR A 220 N THR A 197
SHEET 8 A 8 ILE A 235 ILE A 238 -1 O VAL A 236 N TRP A 221
SHEET 1 B 2 LEU A 97 GLU A 99 0
SHEET 2 B 2 ARG A 108 HIS A 110 -1 O GLY A 109 N LYS A 98
SHEET 1 C 8 ALA B 49 SER B 58 0
SHEET 2 C 8 VAL B 63 ASP B 70 -1 O VAL B 63 N SER B 58
SHEET 3 C 8 LEU B 75 PHE B 80 -1 O LEU B 75 N ASP B 70
SHEET 4 C 8 ARG B 139 HIS B 145 1 O ARG B 139 N ILE B 76
SHEET 5 C 8 ILE B 166 TYR B 171 1 N ASP B 167 O VAL B 140
SHEET 6 C 8 LEU B 193 HIS B 198 1 N TYR B 194 O VAL B 168
SHEET 7 C 8 GLU B 219 ILE B 222 1 O TYR B 220 N THR B 197
SHEET 8 C 8 ILE B 235 ILE B 238 -1 O VAL B 236 N TRP B 221
SHEET 1 D 2 LEU B 97 GLU B 99 0
SHEET 2 D 2 ARG B 108 HIS B 110 -1 O GLY B 109 N LYS B 98
SSBOND 1 CYS A 22 CYS A 268
SSBOND 2 CYS A 36 CYS A 41
SSBOND 3 CYS A 104 CYS A 107
SSBOND 4 CYS B 22 CYS B 268
SSBOND 5 CYS B 36 CYS B 41
SSBOND 6 CYS B 104 CYS B 107
CISPEP 1 LEU A 206 PRO A 207 0 -14.25
CISPEP 2 SER A 217 PRO A 218 0 7.21
CISPEP 3 LEU B 206 PRO B 207 0 -13.27
CISPEP 4 SER B 217 PRO B 218 0 3.37
CRYST1 96.127 71.096 82.830 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 0.010403 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014065 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012073 0.00000
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