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HEADER HYDROLASE 11-JAN-00 1DT5
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, C, D, E, F, G, H;
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 ALPHA-BETA PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.BROZOZOWSKI,H.SAVAGE
REVDAT 1 20-DEC-00 1DT5 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. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 91415
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) : 0.244
REMARK 3 FREE R VALUE : 0.315
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4488
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16568
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 715
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.00
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: USED REFMAC
REMARK 4
REMARK 4 1DT5 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 RCSB010345.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-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) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
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 : 91415
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 98.4
REMARK 200 DATA REDUNDANCY : 2.750
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 0.00
REMARK 200 R MERGE FOR SHELL (I) : 0.37400
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 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -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 81.43900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 8 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 350 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 BIOMOLECULE: 4
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 5
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 6
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 7
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 8
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
REMARK 350 BIOMT1 8 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 8 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 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 96 O HOH 2 1.89
REMARK 500 N GLY D 245 O HOH 329 1.89
REMARK 500 O HOH 92 O HOH 37 2.00
REMARK 500 O HOH 513 OD1 ASP C 242 2.00
REMARK 500 O HOH 25 O HOH 349 2.02
REMARK 500 O HOH 21 NH2 ARG H 179 2.03
REMARK 500 O HOH 298 O HOH 43 2.04
REMARK 500 O HOH 559 O HOH 562 2.05
REMARK 500 O HOH 93 O HOH 6 2.05
REMARK 500 O HOH 666 O HOH 169 2.12
REMARK 500 O HOH 342 OE2 GLU E 239 2.13
REMARK 500 O HOH 295 O HOH 171 2.14
REMARK 500 O HOH 21 O HOH 648 2.16
REMARK 500 O HOH 43 O HOH 449 2.17
REMARK 500 O HOH 102 O HOH 13 2.17
REMARK 500 OD2 ASP G 242 OG SER G 214 2.18
REMARK 500 OG SER C 214 OD2 ASP C 242 2.19
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 550 O HOH 194 2556 1.97
REMARK 500 O ASP D 102 NH2 ARG E 232 2657 2.13
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 ARG A 81 NE ARG A 81 CD -0.069
REMARK 500 ARG A 205 NE ARG A 205 CD -0.073
REMARK 500 ILE A 238 CG1 ILE A 238 CB 0.070
REMARK 500 GLY A 245 CA GLY A 245 N 0.075
REMARK 500 ARG B 81 NE ARG B 81 CD -0.095
REMARK 500 ARG B 205 NE ARG B 205 CD -0.079
REMARK 500 ARG C 205 CD ARG C 205 CG -0.067
REMARK 500 ARG C 205 NE ARG C 205 CD -0.066
REMARK 500 ARG D 205 NE ARG D 205 CD -0.078
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 ASP A 48 CA - CB - CG ANGL. DEV. = 16.0 DEGREES
REMARK 500 ARG A 81 CG - CD - NE ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG A 205 CG - CD - NE ANGL. DEV. = 19.1 DEGREES
REMARK 500 ARG A 205 CD - NE - CZ ANGL. DEV. = 27.8 DEGREES
REMARK 500 ASP B 48 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG B 205 CG - CD - NE ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG B 205 CD - NE - CZ ANGL. DEV. = 34.6 DEGREES
REMARK 500 ARG C 205 CB - CG - CD ANGL. DEV. = 19.4 DEGREES
REMARK 500 ARG C 205 CD - NE - CZ ANGL. DEV. = 19.9 DEGREES
REMARK 500 ARG D 205 CD - NE - CZ ANGL. DEV. = 29.1 DEGREES
REMARK 500 ARG E 205 CD - NE - CZ ANGL. DEV. = 16.6 DEGREES
REMARK 500 ARG F 205 CD - NE - CZ ANGL. DEV. = 18.6 DEGREES
REMARK 500 ARG G 205 CB - CG - CD ANGL. DEV. = 16.8 DEGREES
REMARK 500 ARG G 205 CD - NE - CZ ANGL. DEV. = 18.7 DEGREES
REMARK 500 ARG H 205 CD - NE - CZ ANGL. DEV. = 33.1 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 THR A 199 24.10 -105.80
REMARK 500 SER B 146 67.88 -117.41
REMARK 500 THR B 199 27.59 -116.00
REMARK 500 THR C 199 26.63 -110.01
REMARK 500 PHE C 262 81.49 -36.19
REMARK 500 THR D 199 25.01 -110.98
REMARK 500 THR E 199 23.67 -112.55
REMARK 500 THR F 199 25.75 -112.08
REMARK 500 THR G 199 25.22 -117.27
REMARK 500 PHE G 262 76.92 -45.29
REMARK 500 THR H 199 22.71 -109.32
REMARK 500 PHE H 262 83.27 -31.56
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 656 DISTANCE = 6.72 ANGSTROMS
DBREF 1DT5 A 1 269 GB 2997733 AF054513 23 291
DBREF 1DT5 B 1 269 GB 2997733 AF054513 23 291
DBREF 1DT5 C 1 269 GB 2997733 AF054513 23 291
DBREF 1DT5 D 1 269 GB 2997733 AF054513 23 291
DBREF 1DT5 E 1 269 GB 2997733 AF054513 23 291
DBREF 1DT5 F 1 269 GB 2997733 AF054513 23 291
DBREF 1DT5 G 1 269 GB 2997733 AF054513 23 291
DBREF 1DT5 H 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
SEQRES 1 C 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 C 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 C 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 C 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 C 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 C 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 C 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 C 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 C 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 C 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 C 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 C 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 C 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 C 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 C 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 C 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 C 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 C 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 C 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 C 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 C 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
SEQRES 1 D 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 D 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 D 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 D 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 D 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 D 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 D 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 D 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 D 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 D 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 D 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 D 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 D 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 D 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 D 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 D 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 D 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 D 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 D 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 D 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 D 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
SEQRES 1 E 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 E 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 E 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 E 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 E 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 E 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 E 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 E 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 E 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 E 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 E 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 E 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 E 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 E 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 E 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 E 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 E 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 E 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 E 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 E 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 E 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
SEQRES 1 F 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 F 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 F 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 F 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 F 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 F 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 F 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 F 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 F 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 F 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 F 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 F 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 F 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 F 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 F 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 F 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 F 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 F 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 F 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 F 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 F 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
SEQRES 1 G 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 G 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 G 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 G 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 G 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 G 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 G 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 G 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 G 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 G 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 G 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 G 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 G 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 G 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 G 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 G 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 G 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 G 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 G 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 G 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 G 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
SEQRES 1 H 269 GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE
SEQRES 2 H 269 ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN
SEQRES 3 H 269 ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN
SEQRES 4 H 269 ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU
SEQRES 5 H 269 TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY
SEQRES 6 H 269 PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU
SEQRES 7 H 269 SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY
SEQRES 8 H 269 ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS
SEQRES 9 H 269 SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP
SEQRES 10 H 269 ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP
SEQRES 11 H 269 ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR
SEQRES 12 H 269 GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY
SEQRES 13 H 269 ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE
SEQRES 14 H 269 SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA
SEQRES 15 H 269 GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG
SEQRES 16 H 269 ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO
SEQRES 17 H 269 ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP
SEQRES 18 H 269 ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP
SEQRES 19 H 269 ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN
SEQRES 20 H 269 ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP
SEQRES 21 H 269 TYR PHE GLY LEU ILE GLY THR CYS LEU
FORMUL 9 HOH *513(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 36 ALA A 40 5 5
HELIX 4 4 CYS A 41 ALA A 47 1 7
HELIX 5 5 SER A 85 LEU A 93 1 9
HELIX 6 6 ASP A 111 HIS A 135 1 25
HELIX 7 7 SER A 146 ARG A 160 1 15
HELIX 8 8 ASN A 178 GLN A 188 1 11
HELIX 9 9 ILE A 202 LEU A 206 5 5
HELIX 10 10 PRO A 208 GLY A 212 5 5
HELIX 11 11 THR A 231 ASN A 233 5 3
HELIX 12 12 ILE A 255 LEU A 259 5 5
HELIX 13 13 SER B 3 ALA B 20 1 18
HELIX 14 14 TYR B 21 ASP B 27 5 7
HELIX 15 15 CYS B 36 ALA B 40 5 5
HELIX 16 16 CYS B 41 ALA B 47 1 7
HELIX 17 17 SER B 85 LEU B 93 1 9
HELIX 18 18 ASP B 111 HIS B 135 1 25
HELIX 19 19 SER B 146 ARG B 160 1 15
HELIX 20 20 ASN B 178 GLN B 188 1 11
HELIX 21 21 ILE B 202 LEU B 206 5 5
HELIX 22 22 PRO B 208 GLY B 212 5 5
HELIX 23 23 THR B 231 ASN B 233 5 3
HELIX 24 24 ILE B 255 LEU B 259 5 5
HELIX 25 25 SER C 3 TYR C 21 1 19
HELIX 26 26 CYS C 22 ASN C 26 5 5
HELIX 27 27 CYS C 36 ALA C 40 5 5
HELIX 28 28 CYS C 41 ALA C 47 1 7
HELIX 29 29 SER C 85 ASN C 92 1 8
HELIX 30 30 ASP C 111 HIS C 135 1 25
HELIX 31 31 SER C 146 ARG C 160 1 15
HELIX 32 32 ASN C 178 GLN C 188 1 11
HELIX 33 33 ILE C 202 LEU C 206 5 5
HELIX 34 34 PRO C 208 GLY C 212 5 5
HELIX 35 35 THR C 231 ASN C 233 5 3
HELIX 36 36 ILE C 255 LEU C 259 5 5
HELIX 37 37 SER D 3 ALA D 20 1 18
HELIX 38 38 TYR D 21 ASP D 27 5 7
HELIX 39 39 CYS D 36 ALA D 40 5 5
HELIX 40 40 CYS D 41 ALA D 47 1 7
HELIX 41 41 SER D 85 ASN D 92 1 8
HELIX 42 42 ASP D 111 HIS D 135 1 25
HELIX 43 43 SER D 146 ARG D 160 1 15
HELIX 44 44 ASN D 178 GLN D 188 1 11
HELIX 45 45 ILE D 202 LEU D 206 5 5
HELIX 46 46 PRO D 208 GLY D 212 5 5
HELIX 47 47 THR D 231 ASN D 233 5 3
HELIX 48 48 ILE D 255 LEU D 259 5 5
HELIX 49 49 SER E 3 ALA E 20 1 18
HELIX 50 50 TYR E 21 ASN E 26 5 6
HELIX 51 51 CYS E 36 ALA E 40 5 5
HELIX 52 52 CYS E 41 ALA E 47 1 7
HELIX 53 53 SER E 85 LEU E 93 1 9
HELIX 54 54 ASP E 111 HIS E 135 1 25
HELIX 55 55 SER E 146 ARG E 160 1 15
HELIX 56 56 ASN E 178 GLN E 188 1 11
HELIX 57 57 ILE E 202 LEU E 206 5 5
HELIX 58 58 PRO E 208 GLY E 212 5 5
HELIX 59 59 THR E 231 ASN E 233 5 3
HELIX 60 60 ILE E 255 LEU E 259 5 5
HELIX 61 61 SER F 3 ALA F 20 1 18
HELIX 62 62 TYR F 21 ASP F 27 5 7
HELIX 63 63 CYS F 36 ALA F 40 5 5
HELIX 64 64 CYS F 41 ALA F 47 1 7
HELIX 65 65 SER F 85 LEU F 93 1 9
HELIX 66 66 ASP F 111 HIS F 135 1 25
HELIX 67 67 SER F 146 ARG F 160 1 15
HELIX 68 68 ASN F 178 GLN F 188 1 11
HELIX 69 69 ILE F 202 LEU F 206 5 5
HELIX 70 70 PRO F 208 GLY F 212 5 5
HELIX 71 71 THR F 231 ASN F 233 5 3
HELIX 72 72 ILE F 255 LEU F 259 5 5
HELIX 73 73 SER G 3 ALA G 20 1 18
HELIX 74 74 TYR G 21 ASP G 27 5 7
HELIX 75 75 CYS G 36 ALA G 40 5 5
HELIX 76 76 CYS G 41 ALA G 47 1 7
HELIX 77 77 SER G 85 LEU G 93 1 9
HELIX 78 78 ASP G 111 HIS G 135 1 25
HELIX 79 79 SER G 146 ARG G 160 1 15
HELIX 80 80 ASN G 178 GLN G 188 1 11
HELIX 81 81 ILE G 202 LEU G 206 5 5
HELIX 82 82 PRO G 208 GLY G 212 5 5
HELIX 83 83 THR G 231 ASN G 233 5 3
HELIX 84 84 ILE G 255 LEU G 259 5 5
HELIX 85 85 SER H 3 ALA H 20 1 18
HELIX 86 86 TYR H 21 ASP H 27 5 7
HELIX 87 87 CYS H 36 ALA H 40 5 5
HELIX 88 88 CYS H 41 ALA H 47 1 7
HELIX 89 89 SER H 85 LEU H 93 1 9
HELIX 90 90 ASP H 111 HIS H 135 1 25
HELIX 91 91 SER H 146 ARG H 160 1 15
HELIX 92 92 ASN H 178 GLN H 188 1 11
HELIX 93 93 ILE H 202 LEU H 206 5 5
HELIX 94 94 PRO H 208 GLY H 212 5 5
HELIX 95 95 THR H 231 ASN H 233 5 3
HELIX 96 96 ILE H 255 LEU H 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 ILE A 166 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 N TYR A 220 O ARG A 195
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 N VAL B 63 O 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 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 N GLY B 109 O LYS B 98
SHEET 1 E 8 ALA C 49 SER C 58 0
SHEET 2 E 8 VAL C 63 ASP C 70 -1 O VAL C 63 N SER C 58
SHEET 3 E 8 LEU C 75 PHE C 80 -1 O LEU C 75 N ASP C 70
SHEET 4 E 8 ARG C 139 HIS C 145 1 O ARG C 139 N ILE C 76
SHEET 5 E 8 ILE C 166 TYR C 171 1 O ASP C 167 N PHE C 142
SHEET 6 E 8 LEU C 193 HIS C 198 1 N TYR C 194 O VAL C 168
SHEET 7 E 8 GLU C 219 ILE C 222 1 N TYR C 220 O ARG C 195
SHEET 8 E 8 ILE C 235 ILE C 238 -1 O VAL C 236 N TRP C 221
SHEET 1 F 2 LEU C 97 GLU C 99 0
SHEET 2 F 2 ARG C 108 HIS C 110 -1 O GLY C 109 N LYS C 98
SHEET 1 G 8 ALA D 49 SER D 58 0
SHEET 2 G 8 VAL D 63 ASP D 70 -1 O VAL D 63 N SER D 58
SHEET 3 G 8 LEU D 75 PHE D 80 -1 O LEU D 75 N ASP D 70
SHEET 4 G 8 ARG D 139 HIS D 145 1 O ARG D 139 N ILE D 76
SHEET 5 G 8 ILE D 166 TYR D 171 1 O ASP D 167 N PHE D 142
SHEET 6 G 8 LEU D 193 HIS D 198 1 N TYR D 194 O VAL D 168
SHEET 7 G 8 GLU D 219 ILE D 222 1 N TYR D 220 O ARG D 195
SHEET 8 G 8 ILE D 235 ILE D 238 -1 O VAL D 236 N TRP D 221
SHEET 1 H 2 LEU D 97 GLU D 99 0
SHEET 2 H 2 ARG D 108 HIS D 110 -1 N GLY D 109 O LYS D 98
SHEET 1 I 8 ALA E 49 SER E 58 0
SHEET 2 I 8 VAL E 63 ASP E 70 -1 O VAL E 63 N SER E 58
SHEET 3 I 8 LEU E 75 PHE E 80 -1 O LEU E 75 N ASP E 70
SHEET 4 I 8 ARG E 139 HIS E 145 1 O ARG E 139 N ILE E 76
SHEET 5 I 8 ILE E 166 TYR E 171 1 O ASP E 167 N PHE E 142
SHEET 6 I 8 LEU E 193 HIS E 198 1 N TYR E 194 O VAL E 168
SHEET 7 I 8 GLU E 219 ILE E 222 1 N TYR E 220 O ARG E 195
SHEET 8 I 8 ILE E 235 ILE E 238 -1 O VAL E 236 N TRP E 221
SHEET 1 J 2 LEU E 97 GLU E 99 0
SHEET 2 J 2 ARG E 108 HIS E 110 -1 O GLY E 109 N LYS E 98
SHEET 1 K 8 ALA F 49 SER F 58 0
SHEET 2 K 8 VAL F 63 ASP F 70 -1 N VAL F 63 O SER F 58
SHEET 3 K 8 LEU F 75 PHE F 80 -1 O LEU F 75 N ASP F 70
SHEET 4 K 8 ARG F 139 HIS F 145 1 O ARG F 139 N ILE F 76
SHEET 5 K 8 ILE F 166 TYR F 171 1 O ASP F 167 N PHE F 142
SHEET 6 K 8 LEU F 193 HIS F 198 1 N TYR F 194 O VAL F 168
SHEET 7 K 8 GLU F 219 ILE F 222 1 O TYR F 220 N THR F 197
SHEET 8 K 8 ILE F 235 ILE F 238 -1 O VAL F 236 N TRP F 221
SHEET 1 L 2 LEU F 97 GLU F 99 0
SHEET 2 L 2 ARG F 108 HIS F 110 -1 O GLY F 109 N LYS F 98
SHEET 1 M 8 ALA G 49 SER G 58 0
SHEET 2 M 8 VAL G 63 ASP G 70 -1 O VAL G 63 N SER G 58
SHEET 3 M 8 LEU G 75 PHE G 80 -1 N LEU G 75 O ASP G 70
SHEET 4 M 8 ARG G 139 HIS G 145 1 O ARG G 139 N ILE G 76
SHEET 5 M 8 ASP G 167 TYR G 171 1 O ASP G 167 N PHE G 142
SHEET 6 M 8 LEU G 193 HIS G 198 1 N TYR G 194 O VAL G 168
SHEET 7 M 8 GLU G 219 ILE G 222 1 O TYR G 220 N THR G 197
SHEET 8 M 8 ILE G 235 ILE G 238 -1 O VAL G 236 N TRP G 221
SHEET 1 N 2 LEU G 97 GLU G 99 0
SHEET 2 N 2 ARG G 108 HIS G 110 -1 N GLY G 109 O LYS G 98
SHEET 1 O 8 ALA H 49 SER H 58 0
SHEET 2 O 8 VAL H 63 ASP H 70 -1 N VAL H 63 O SER H 58
SHEET 3 O 8 LEU H 75 PHE H 80 -1 O LEU H 75 N ASP H 70
SHEET 4 O 8 ARG H 139 HIS H 145 1 O ARG H 139 N ILE H 76
SHEET 5 O 8 ILE H 166 TYR H 171 1 O ASP H 167 N PHE H 142
SHEET 6 O 8 LEU H 193 HIS H 198 1 N TYR H 194 O VAL H 168
SHEET 7 O 8 GLU H 219 ILE H 222 1 N TYR H 220 O ARG H 195
SHEET 8 O 8 ILE H 235 ILE H 238 -1 N VAL H 236 O TRP H 221
SHEET 1 P 2 LEU H 97 GLU H 99 0
SHEET 2 P 2 ARG H 108 HIS H 110 -1 N GLY H 109 O LYS H 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
SSBOND 7 CYS C 22 CYS C 268
SSBOND 8 CYS C 36 CYS C 41
SSBOND 9 CYS C 104 CYS C 107
SSBOND 10 CYS D 22 CYS D 268
SSBOND 11 CYS D 36 CYS D 41
SSBOND 12 CYS D 104 CYS D 107
SSBOND 13 CYS E 22 CYS E 268
SSBOND 14 CYS E 36 CYS E 41
SSBOND 15 CYS E 104 CYS E 107
SSBOND 16 CYS F 22 CYS F 268
SSBOND 17 CYS F 36 CYS F 41
SSBOND 18 CYS F 104 CYS F 107
SSBOND 19 CYS G 22 CYS G 268
SSBOND 20 CYS G 36 CYS G 41
SSBOND 21 CYS G 104 CYS G 107
SSBOND 22 CYS H 22 CYS H 268
SSBOND 23 CYS H 36 CYS H 41
SSBOND 24 CYS H 104 CYS H 107
CISPEP 1 LEU A 206 PRO A 207 0 -12.32
CISPEP 2 SER A 217 PRO A 218 0 1.71
CISPEP 3 LEU B 206 PRO B 207 0 -10.06
CISPEP 4 SER B 217 PRO B 218 0 0.74
CISPEP 5 LEU C 206 PRO C 207 0 -7.94
CISPEP 6 SER C 217 PRO C 218 0 -2.36
CISPEP 7 LEU D 206 PRO D 207 0 -9.68
CISPEP 8 SER D 217 PRO D 218 0 1.14
CISPEP 9 LEU E 206 PRO E 207 0 -6.68
CISPEP 10 SER E 217 PRO E 218 0 1.33
CISPEP 11 LEU F 206 PRO F 207 0 -10.47
CISPEP 12 SER F 217 PRO F 218 0 1.11
CISPEP 13 LEU G 206 PRO G 207 0 -6.34
CISPEP 14 SER G 217 PRO G 218 0 4.55
CISPEP 15 LEU H 206 PRO H 207 0 -11.79
CISPEP 16 SER H 217 PRO H 218 0 0.35
CRYST1 85.435 162.878 86.717 90.00 98.45 90.00 P 1 21 1 16
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 0.011700 0.000000 0.001740 0.00000
SCALE2 0.000000 0.006140 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011660 0.00000
END |