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HEADER HYDROLASE 11-JAN-00 1DT3
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
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.BROZOZOWSKI,H.SAVAGE
REVDAT 1 20-DEC-00 1DT3 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. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 26160
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : 5% OF TOTAL DATA SET
REMARK 3 USED
REMARK 3 R VALUE (WORKING + TEST SET) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1390
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 : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.00
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: RMS BOND = 0.013A RMS ANGLE =
REMARK 3 0.041A
REMARK 4
REMARK 4 1DT3 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 RCSB010343.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-1999
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 : AREA DETECTOR
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 : 26160
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 20.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 26.00
REMARK 200 R MERGE FOR SHELL (I) : 0.04800
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 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 -X,-Y,1/2+Z
REMARK 290 5555 Y,-X+Y,5/6+Z
REMARK 290 6555 X-Y,X,1/6+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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.89333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.78667
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 40.34000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 67.23333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 13.44667
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: 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 ARG A 205 CD - NE - CZ ANGL. DEV. = 29.5 DEGREES
REMARK 500 GLY A 246 C - N - CA ANGL. DEV. = 23.8 DEGREES
REMARK 500 ASN B 25 C - N - CA ANGL. DEV. = 23.4 DEGREES
REMARK 500 ARG B 195 CD - NE - CZ ANGL. DEV. = 51.0 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 LYS A 24 79.83 -31.87
REMARK 500 THR A 199 24.08 -118.05
REMARK 500 PHE A 262 68.76 -32.02
REMARK 500 THR B 199 28.88 -107.55
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 58 DISTANCE = 5.66 ANGSTROMS
REMARK 525 0 HOH 60 DISTANCE = 5.36 ANGSTROMS
REMARK 525 0 HOH 87 DISTANCE = 5.42 ANGSTROMS
REMARK 525 0 HOH 105 DISTANCE = 5.26 ANGSTROMS
REMARK 525 0 HOH 130 DISTANCE = 5.12 ANGSTROMS
REMARK 525 0 HOH 148 DISTANCE = 5.77 ANGSTROMS
REMARK 525 0 HOH 162 DISTANCE = 6.71 ANGSTROMS
REMARK 525 0 HOH 181 DISTANCE = 5.38 ANGSTROMS
REMARK 525 0 HOH 211 DISTANCE = 5.29 ANGSTROMS
REMARK 525 0 HOH 230 DISTANCE = 5.24 ANGSTROMS
DBREF 1DT3 A 1 269 GB 2997733 AF054513 23 291
DBREF 1DT3 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 *242(H2 O1)
HELIX 1 1 SER A 3 CYS A 22 1 20
HELIX 2 2 CYS A 41 ALA A 47 1 7
HELIX 3 3 SER A 85 ASN A 92 1 8
HELIX 4 4 ASP A 111 SER A 119 1 9
HELIX 5 5 VAL A 120 HIS A 135 1 16
HELIX 6 6 SER 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 ASP A 254 LEU A 259 1 6
HELIX 12 12 SER B 3 ALA B 20 1 18
HELIX 13 13 CYS B 41 ALA B 47 1 7
HELIX 14 14 SER B 85 ASN B 92 1 8
HELIX 15 15 ASN B 101 CYS B 104 5 4
HELIX 16 16 ASP B 111 HIS B 135 1 25
HELIX 17 17 SER B 146 ARG B 160 1 15
HELIX 18 18 ASN B 178 GLN B 188 1 11
HELIX 19 19 ILE B 202 LEU B 206 5 5
HELIX 20 20 PRO B 208 GLY B 212 5 5
HELIX 21 21 THR B 231 ASN B 233 5 3
HELIX 22 22 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 O VAL A 63 N 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 ASP A 167 TYR A 171 1 O ASP A 167 N PHE A 142
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 N GLY A 109 O 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 O ASP B 167 N PHE B 142
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 N TYR B 220 O ARG B 195
SHEET 8 C 8 ILE B 235 ILE B 238 -1 N VAL B 236 O 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 N GLY B 109 O 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 -8.75
CISPEP 2 SER A 217 PRO A 218 0 4.21
CISPEP 3 LEU B 206 PRO B 207 0 -7.30
CISPEP 4 SER B 217 PRO B 218 0 -2.31
CRYST1 139.920 139.920 80.680 90.00 90.00 120.00 P 61 12
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 0.007147 0.004126 0.000000 0.00000
SCALE2 0.000000 0.008253 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012395 0.00000
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