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HEADER HYDROLASE 30-DEC-05 2FJ0
TITLE CRYSTAL STRUCTURE OF JUVENILE HORMONE ESTERASE FROM MANDUCA
TITLE 2 SEXTA, WITH OTFP COVALENTLY ATTACHED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: JUVENILE HORMONE ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRICHOPLUSIA NI;
SOURCE 3 ORGANISM_COMMON: CABBAGE LOOPER;
SOURCE 4 EXPRESSION_SYSTEM: BACULOVIRUS;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: VIRUS
KEYWDS ESTERASE, JUVENILE HORMONE, MANDUCA SEXTA, ALPHA-BETA
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WOGULIS,D.K.WILSON
REVDAT 1 23-MAY-06 2FJ0 0
JRNL AUTH M.WOGULIS,C.E.WHEELOCK,S.G.KAMITA,A.C.HINTON,
JRNL AUTH 2 P.A.WHETSTONE,B.D.HAMMOCK,D.K.WILSON
JRNL TITL STRUCTURAL STUDIES OF A POTENT INSECT MATURATION
JRNL TITL 2 INHIBITOR BOUND TO THE JUVENILE HORMONE ESTERASE
JRNL TITL 3 OF MANDUCA SEXTA.
JRNL REF BIOCHEMISTRY V. 45 4045 2006
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 130877.600
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 20453
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 SET) : 0.204
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 945
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2893
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4221
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 101
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.80000
REMARK 3 B22 (A**2) : 8.80000
REMARK 3 B33 (A**2) : -17.60000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.36
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.48
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.240 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.120 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.790 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.780 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 27.02
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : OTFP2.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : INH2.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FJ0 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-2006.
REMARK 100 THE RCSB ID CODE IS RCSB035932.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-2004
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21455
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.41800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 3000, 80 MM SODIUM CITRATE,
REMARK 280 20 MM CITRIC ACID, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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,1/4+Z
REMARK 290 4555 1/2+Y,1/2-X,3/4+Z
REMARK 290 5555 1/2-X,1/2+Y,1/4-Z
REMARK 290 6555 1/2+X,1/2-Y,3/4-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 82.69750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 48.41000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.41000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.34875
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.41000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.41000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 124.04625
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.41000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.41000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 41.34875
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.41000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.41000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 124.04625
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 82.69750
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ARG A 23
REMARK 465 ILE A 24
REMARK 465 PRO A 25
REMARK 465 SER A 26
REMARK 465 THR A 27
REMARK 465 ALA A 128
REMARK 465 ALA A 129
REMARK 465 ASP A 130
REMARK 465 LYS A 131
REMARK 465 ASN A 132
REMARK 465 ARG A 133
REMARK 465 PHE A 134
REMARK 465 ALA A 135
REMARK 465 ASN A 566
REMARK 465 GLY A 567
REMARK 465 THR A 568
REMARK 465 SER A 569
REMARK 465 TYR A 570
REMARK 465 CYS A 571
REMARK 465 ILE A 572
REMARK 465 LYS A 573
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 MET A 555 SD MET A 555 CE -0.083
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 LEU A 65 N - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 THR A 95 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 SER A 226 CB - CA - C ANGL. DEV. = 17.4 DEGREES
REMARK 500 SER A 226 N - CA - CB ANGL. DEV. =-19.2 DEGREES
REMARK 500 SER A 226 CA - CB - OG ANGL. DEV. = 38.0 DEGREES
REMARK 500 VAL A 320 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 ASN A 325 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 CYS A 358 N - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 LEU A 419 CA - CB - CG ANGL. DEV. = 11.9 DEGREES
DBREF 2FJ0 A 23 573 GB 73921301 AAG42021 23 573
SEQRES 1 A 551 ARG ILE PRO SER THR GLU GLU VAL VAL VAL ARG THR GLU
SEQRES 2 A 551 SER GLY TRP ILE ARG GLY LEU LYS ARG ARG ALA GLU GLY
SEQRES 3 A 551 ASN LYS SER TYR ALA SER PHE ARG GLY VAL PRO TYR ALA
SEQRES 4 A 551 LYS GLN PRO LEU GLY GLU LEU ARG PHE LYS GLU LEU GLN
SEQRES 5 A 551 PRO LEU GLU PRO TRP GLN ASP GLU LEU ASP ALA THR GLN
SEQRES 6 A 551 GLU GLY PRO VAL CYS GLN GLN THR ASP VAL LEU TYR GLY
SEQRES 7 A 551 ARG ILE MET ARG PRO ARG GLY MET SER GLU ALA CYS ILE
SEQRES 8 A 551 HIS ALA ASN ILE HIS VAL PRO TYR TYR ALA LEU PRO ARG
SEQRES 9 A 551 ASP ALA ALA ASP LYS ASN ARG PHE ALA GLY LEU PRO VAL
SEQRES 10 A 551 LEU VAL PHE ILE HIS GLY GLY GLY PHE ALA PHE GLY SER
SEQRES 11 A 551 GLY ASP SER ASP LEU HIS GLY PRO GLU TYR LEU VAL SER
SEQRES 12 A 551 LYS ASP VAL ILE VAL ILE THR PHE ASN TYR ARG LEU ASN
SEQRES 13 A 551 VAL TYR GLY PHE LEU SER LEU ASN SER THR SER VAL PRO
SEQRES 14 A 551 GLY ASN ALA GLY LEU ARG ASP MET VAL THR LEU LEU LYS
SEQRES 15 A 551 TRP VAL GLN ARG ASN ALA HIS PHE PHE GLY GLY ARG PRO
SEQRES 16 A 551 ASP ASP VAL THR LEU MET GLY GLN SER ALA GLY ALA ALA
SEQRES 17 A 551 ALA THR HIS ILE LEU SER LEU SER LYS ALA ALA ASP GLY
SEQRES 18 A 551 LEU PHE ARG ARG ALA ILE LEU MET SER GLY THR SER SER
SEQRES 19 A 551 SER ALA PHE PHE THR THR ASN PRO VAL PHE ALA GLN TYR
SEQRES 20 A 551 ILE ASN LYS LEU PHE VAL THR ASN ILE GLY ILE THR ALA
SEQRES 21 A 551 THR ASP PRO GLU GLU ILE HIS GLN LYS LEU ILE GLU MET
SEQRES 22 A 551 PRO ALA GLU LYS LEU ASN GLU ALA ASN ARG PHE LEU LEU
SEQRES 23 A 551 GLU GLN PHE GLY LEU THR THR PHE PHE PRO VAL VAL GLU
SEQRES 24 A 551 SER PRO ILE ASN GLY VAL THR THR ILE LEU ASP GLY ASP
SEQRES 25 A 551 PRO GLU GLN LEU ILE ALA LYS GLY ARG GLY LYS HIS ILE
SEQRES 26 A 551 PRO LEU ILE ILE GLY PHE THR ASP ALA GLU CYS GLU ILE
SEQRES 27 A 551 PHE ARG ARG GLN PHE GLU GLN ILE ASP ILE VAL SER LYS
SEQRES 28 A 551 ILE LYS GLU ASN PRO GLY ILE LEU VAL PRO LEU SER VAL
SEQRES 29 A 551 LEU PHE SER SER ALA PRO ASP THR VAL ALA GLU ILE THR
SEQRES 30 A 551 LYS ALA MET HIS GLU LYS TYR PHE LYS LYS SER VAL ASP
SEQRES 31 A 551 MET GLU GLY TYR ILE GLU LEU CYS THR ASP SER TYR PHE
SEQRES 32 A 551 MET TYR PRO ALA ILE SER LEU ALA ILE LYS ARG ALA ARG
SEQRES 33 A 551 SER ASN GLY ALA PRO VAL TYR LEU TYR GLN PHE SER PHE
SEQRES 34 A 551 ASP GLY ASP TYR SER VAL PHE ARG GLU VAL ASN HIS LEU
SEQRES 35 A 551 ASN PHE GLU GLY ALA GLY HIS ILE GLU ASP LEU THR TYR
SEQRES 36 A 551 VAL PHE ARG THR ASN SER MET LEU GLY GLY HIS ALA SER
SEQRES 37 A 551 PHE PRO PRO HIS ASP LYS ASP ASP HIS MET LYS TYR TRP
SEQRES 38 A 551 MET THR SER PHE ILE THR ASN PHE MET LYS TYR SER ASN
SEQRES 39 A 551 PRO VAL THR ASP ALA LYS LEU TRP PRO GLU VAL ARG ALA
SEQRES 40 A 551 ASP ASN LEU ARG TYR GLN ASP ILE ASP THR PRO ASP VAL
SEQRES 41 A 551 TYR GLN ASN VAL LYS PRO HIS SER GLU GLN ARG ASP MET
SEQRES 42 A 551 LEU ASP PHE PHE ASP SER ILE TYR ASN TRP ASN GLY THR
SEQRES 43 A 551 SER TYR CYS ILE LYS
HET TFC A 600 16
HETNAM TFC 1,1,1-TRIFLUORO-3-(OCTYLTHIO)ACETONE
FORMUL 2 TFC C11 H19 O1 F3 S1
FORMUL 3 HOH *101(H2 O1)
HELIX 1 1 TYR A 99 MET A 103 5 5
HELIX 2 2 TYR A 122 LEU A 124 5 3
HELIX 3 3 TYR A 162 ASP A 167 5 6
HELIX 4 4 LEU A 177 LEU A 183 1 7
HELIX 5 5 ASN A 193 ALA A 210 1 18
HELIX 6 6 HIS A 211 PHE A 213 5 3
HELIX 7 7 SER A 226 SER A 236 1 11
HELIX 8 8 LEU A 237 ASP A 242 5 6
HELIX 9 9 ASN A 263 ILE A 278 1 16
HELIX 10 10 ASP A 284 GLU A 294 1 11
HELIX 11 11 PRO A 296 GLY A 312 1 17
HELIX 12 12 ASP A 334 LYS A 341 1 8
HELIX 13 13 ALA A 356 ILE A 360 5 5
HELIX 14 14 PHE A 361 ASP A 369 1 9
HELIX 15 15 ASP A 369 ASN A 377 1 9
HELIX 16 16 PRO A 383 PHE A 388 1 6
HELIX 17 17 ALA A 391 PHE A 407 1 17
HELIX 18 18 ASP A 412 PHE A 425 1 14
HELIX 19 19 PHE A 425 ARG A 438 1 14
HELIX 20 20 SER A 456 HIS A 463 1 8
HELIX 21 21 GLU A 473 VAL A 478 5 6
HELIX 22 22 ASP A 495 SER A 515 1 21
HELIX 23 23 HIS A 549 ASN A 564 1 16
SHEET 1 A 3 GLU A 29 THR A 34 0
SHEET 2 A 3 GLY A 37 ARG A 45 -1 O ILE A 39 N VAL A 32
SHEET 3 A 3 GLU A 82 ASP A 84 1 O LEU A 83 N TRP A 38
SHEET 1 B12 GLU A 29 THR A 34 0
SHEET 2 B12 GLY A 37 ARG A 45 -1 O ILE A 39 N VAL A 32
SHEET 3 B12 SER A 51 PRO A 59 -1 O TYR A 52 N ARG A 44
SHEET 4 B12 HIS A 114 PRO A 120 -1 O ALA A 115 N VAL A 58
SHEET 5 B12 ILE A 169 PHE A 173 -1 O THR A 172 N ASN A 116
SHEET 6 B12 LEU A 137 ILE A 143 1 N LEU A 140 O ILE A 171
SHEET 7 B12 GLY A 215 GLN A 225 1 O MET A 223 N ILE A 143
SHEET 8 B12 ARG A 247 MET A 251 1 O ILE A 249 N LEU A 222
SHEET 9 B12 LEU A 349 GLY A 352 1 O GLY A 352 N LEU A 250
SHEET 10 B12 VAL A 444 PHE A 449 1 O TYR A 445 N ILE A 351
SHEET 11 B12 TYR A 534 ILE A 537 1 O GLN A 535 N LEU A 446
SHEET 12 B12 ASN A 545 VAL A 546 -1 O VAL A 546 N TYR A 534
SSBOND 1 CYS A 92 CYS A 112
SSBOND 2 CYS A 358 CYS A 420
LINK OG SER A 226 C10 TFC A 600
CISPEP 1 PHE A 491 PRO A 492 0 -0.10
CRYST1 96.820 96.820 165.395 90.00 90.00 90.00 P 41 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 0.010328 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010328 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006046 0.00000
TER 4222 TRP A 565
MASTER 298 0 1 23 15 0 0 6 4338 1 21 43
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