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HEADER HYDROLASE 18-JUL-01 1JMK
TITLE STRUCTURAL BASIS FOR THE CYCLIZATION OF THE LIPOPEPTIDE
TITLE 2 ANTIBIOTIC SURFACTIN BY THE THIOESTERASE DOMAIN SRFTE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SURFACTIN SYNTHETASE;
COMPND 3 CHAIN: C, O;
COMPND 4 FRAGMENT: THIOESTERASE DOMAIN;
COMPND 5 SYNONYM: SRFTE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: SRFA-C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS THIOESTERASE, NON-RIBOSOMAL PEPTIDE SYNTHESIS, ALPHA-BETA
KEYWDS 2 HYDROLASE, CYCLIC PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.D.BRUNER,T.WEBER,R.M.KOHLI,D.SCHWARZER,M.A.MARAHIEL,
AUTHOR 2 C.T.WALSH,M.T.STUBBS
REVDAT 1 27-MAR-02 1JMK 0
JRNL AUTH S.D.BRUNER,T.WEBER,R.M.KOHLI,D.SCHWARZER,
JRNL AUTH 2 M.A.MARAHIEL,C.T.WALSH,M.T.STUBBS
JRNL TITL STRUCTURAL BASIS FOR THE CYCLIZATION OF THE
JRNL TITL 2 LIPOPEPTIDE ANTIBIOTIC SURFACTIN BY THE
JRNL TITL 3 THIOESTERASE DOMAIN SRFTE
JRNL REF STRUCTURE FOLD DES. V. 10 301 2002
JRNL REFN UK ISSN 0969-2126
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 62391
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 SET) : 0.230
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2838
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.71
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 896
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3531
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 238
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.18
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) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.73
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JMK COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-2001.
REMARK 100 THE RCSB ID CODE IS RCSB013939.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-2001; 27-FEB-2001
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG ; CHESS
REMARK 200 BEAMLINE : BW6; A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95, 0.9799, 0.9807; 0.979
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62391
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
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: 1.8M AMMONIUM SULFATE, 0.1M HEPES
REMARK 280 7.5, 2% MPD
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-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 31.50500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.85500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.18500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.85500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.50500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.18500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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: C, O
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 ASP C 116
REMARK 465 LEU C 117
REMARK 465 ASP C 118
REMARK 465 GLY C 119
REMARK 465 ARG C 120
REMARK 465 THR C 121
REMARK 465 VAL C 122
REMARK 465 GLU C 123
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER C 115 OG
REMARK 470 ASP C 135 CG OD1 OD2
REMARK 470 ASN C 140 CG OD1 ND2
REMARK 470 GLN C 230 CG CD OE1 NE2
REMARK 470 GLU O 137 CG CD OE1 OE2
REMARK 470 GLN O 230 CG CD OE1 NE2
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 LEU C 68 N GLY O 6 2664 1.93
REMARK 500 OD2 ASP C 16 OG SER O 141 2664 1.97
REMARK 500 O VAL C 10 O HOH 2 2664 2.11
REMARK 500 O VAL O 10 O HOH 89 2665 2.11
REMARK 500 N GLY C 6 O LEU O 68 2664 2.12
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 GLY C 2 CA GLY C 2 N 0.039
REMARK 500 MET C 105 CE MET C 105 SD 0.049
REMARK 500 SER C 124 CA SER C 124 N 0.033
REMARK 500 HIS C 146 CD2 HIS C 146 CG 0.045
REMARK 500 MET C 200 CE MET C 200 SD -0.055
REMARK 500 THR C 231 CB THR C 231 CA -0.034
REMARK 500 GLY O 2 CA GLY O 2 N 0.042
REMARK 500 PRO O 25 CD PRO O 25 CG 0.033
REMARK 500 MET O 105 CE MET O 105 SD 0.035
REMARK 500 HIS O 146 CD2 HIS O 146 CG 0.045
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 GLN C 15 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 PRO C 25 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 GLY C 29 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 CYS C 47 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 ASP C 50 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 VAL C 100 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP C 107 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 LEU C 175 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 ALA C 208 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 MET C 210 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 GLN O 15 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 PRO O 25 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 GLY O 29 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 CYS O 47 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ASP O 50 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 ASP O 107 N - CA - C ANGL. DEV. = 7.7 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 O 141 143.67 63.78
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 HOH 262 DISTANCE = 6.53 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAIN C REFERS TO CLOSED MONOMER.
REMARK 999 CHAIN O REFERS TO OPEN MONOMER.
REMARK 999 SEQUENCE IS PUBLISHED IN BIOCHEMISTRY. 2001
REMARK 999 JUN 19;40(24):7099-108
SEQRES 1 C 230 GLY GLY SER ASP GLY LEU GLN ASP VAL THR ILE MET ASN
SEQRES 2 C 230 GLN ASP GLN GLU GLN ILE ILE PHE ALA PHE PRO PRO VAL
SEQRES 3 C 230 LEU GLY TYR GLY LEU MET TYR GLN ASN LEU SER SER ARG
SEQRES 4 C 230 LEU PRO SER TYR LYS LEU CYS ALA PHE ASP PHE ILE GLU
SEQRES 5 C 230 GLU GLU ASP ARG LEU ASP ARG TYR ALA ASP LEU ILE GLN
SEQRES 6 C 230 LYS LEU GLN PRO GLU GLY PRO LEU THR LEU PHE GLY TYR
SEQRES 7 C 230 SER ALA GLY CYS SER LEU ALA PHE GLU ALA ALA LYS LYS
SEQRES 8 C 230 LEU GLU GLY GLN GLY ARG ILE VAL GLN ARG ILE ILE MET
SEQRES 9 C 230 VAL ASP SER TYR LYS LYS GLN GLY VAL SER ASP LEU ASP
SEQRES 10 C 230 GLY ARG THR VAL GLU SER ASP VAL GLU ALA LEU MET ASN
SEQRES 11 C 230 VAL ASN ARG ASP ASN GLU ALA LEU ASN SER GLU ALA VAL
SEQRES 12 C 230 LYS HIS GLY LEU LYS GLN LYS THR HIS ALA PHE TYR SER
SEQRES 13 C 230 TYR TYR VAL ASN LEU ILE SER THR GLY GLN VAL LYS ALA
SEQRES 14 C 230 ASP ILE ASP LEU LEU THR SER GLY ALA ASP PHE ASP ILE
SEQRES 15 C 230 PRO GLU TRP LEU ALA SER TRP GLU GLU ALA THR THR GLY
SEQRES 16 C 230 ALA TYR ARG MET LYS ARG GLY PHE GLY THR HIS ALA GLU
SEQRES 17 C 230 MET LEU GLN GLY GLU THR LEU ASP ARG ASN ALA GLY ILE
SEQRES 18 C 230 LEU LEU GLU PHE LEU ASN THR GLN THR
SEQRES 1 O 230 GLY GLY SER ASP GLY LEU GLN ASP VAL THR ILE MET ASN
SEQRES 2 O 230 GLN ASP GLN GLU GLN ILE ILE PHE ALA PHE PRO PRO VAL
SEQRES 3 O 230 LEU GLY TYR GLY LEU MET TYR GLN ASN LEU SER SER ARG
SEQRES 4 O 230 LEU PRO SER TYR LYS LEU CYS ALA PHE ASP PHE ILE GLU
SEQRES 5 O 230 GLU GLU ASP ARG LEU ASP ARG TYR ALA ASP LEU ILE GLN
SEQRES 6 O 230 LYS LEU GLN PRO GLU GLY PRO LEU THR LEU PHE GLY TYR
SEQRES 7 O 230 SER ALA GLY CYS SER LEU ALA PHE GLU ALA ALA LYS LYS
SEQRES 8 O 230 LEU GLU GLY GLN GLY ARG ILE VAL GLN ARG ILE ILE MET
SEQRES 9 O 230 VAL ASP SER TYR LYS LYS GLN GLY VAL SER ASP LEU ASP
SEQRES 10 O 230 GLY ARG THR VAL GLU SER ASP VAL GLU ALA LEU MET ASN
SEQRES 11 O 230 VAL ASN ARG ASP ASN GLU ALA LEU ASN SER GLU ALA VAL
SEQRES 12 O 230 LYS HIS GLY LEU LYS GLN LYS THR HIS ALA PHE TYR SER
SEQRES 13 O 230 TYR TYR VAL ASN LEU ILE SER THR GLY GLN VAL LYS ALA
SEQRES 14 O 230 ASP ILE ASP LEU LEU THR SER GLY ALA ASP PHE ASP ILE
SEQRES 15 O 230 PRO GLU TRP LEU ALA SER TRP GLU GLU ALA THR THR GLY
SEQRES 16 O 230 ALA TYR ARG MET LYS ARG GLY PHE GLY THR HIS ALA GLU
SEQRES 17 O 230 MET LEU GLN GLY GLU THR LEU ASP ARG ASN ALA GLY ILE
SEQRES 18 O 230 LEU LEU GLU PHE LEU ASN THR GLN THR
HET SO4 501 5
HET SO4 502 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S1 2-)
FORMUL 5 HOH *238(H2 O1)
HELIX 1 1 TYR C 30 MET C 33 5 4
HELIX 2 2 TYR C 34 LEU C 41 1 8
HELIX 3 3 ASP C 56 GLN C 69 1 14
HELIX 4 4 SER C 80 GLN C 96 1 17
HELIX 5 5 ASP C 125 ASN C 133 1 9
HELIX 6 6 GLU C 137 ASN C 140 5 4
HELIX 7 7 SER C 141 LEU C 162 1 22
HELIX 8 8 TRP C 190 ALA C 193 5 4
HELIX 9 9 THR C 206 MET C 210 5 5
HELIX 10 10 GLN C 212 ASN C 228 1 17
HELIX 11 11 TYR O 30 MET O 33 5 4
HELIX 12 12 TYR O 34 LEU O 41 1 8
HELIX 13 13 ASP O 56 GLN O 69 1 14
HELIX 14 14 ALA O 81 GLN O 96 1 16
HELIX 15 15 THR O 121 MET O 130 1 10
HELIX 16 16 ASN O 136 LEU O 139 5 4
HELIX 17 17 ASN O 140 LEU O 162 1 23
HELIX 18 18 TRP O 190 ALA O 193 5 4
HELIX 19 19 THR O 206 MET O 210 5 5
HELIX 20 20 GLN O 212 ASN O 228 1 17
SHEET 1 A14 VAL C 10 MET C 13 0
SHEET 2 A14 TYR C 44 PHE C 49 -1 O LEU C 46 N MET C 13
SHEET 3 A14 GLN C 19 PHE C 24 1 O GLN C 19 N LYS C 45
SHEET 4 A14 LEU C 74 TYR C 79 1 O THR C 75 N PHE C 22
SHEET 5 A14 VAL C 100 VAL C 106 1 N GLN C 101 O LEU C 74
SHEET 6 A14 ASP C 171 THR C 176 1 O ASP C 171 N ILE C 103
SHEET 7 A14 TYR C 198 ARG C 202 1 N ARG C 199 O ILE C 172
SHEET 8 A14 TYR O 198 ARG O 202 -1 N TYR O 198 O MET C 200
SHEET 9 A14 ASP O 171 THR O 176 1 O ILE O 172 N ARG O 199
SHEET 10 A14 VAL O 100 VAL O 106 1 O GLN O 101 N ASP O 171
SHEET 11 A14 LEU O 74 TYR O 79 1 O LEU O 74 N GLN O 101
SHEET 12 A14 GLN O 19 PHE O 24 1 N PHE O 22 O THR O 75
SHEET 13 A14 TYR O 44 PHE O 49 1 N LYS O 45 O GLN O 19
SHEET 14 A14 VAL O 10 MET O 13 -1 O THR O 11 N ALA O 48
SHEET 1 B 2 LYS C 110 LYS C 111 0
SHEET 2 B 2 LEU C 187 ALA C 188 -1 O ALA C 188 N LYS C 110
SHEET 1 C 2 LYS O 110 LYS O 111 0
SHEET 2 C 2 LEU O 187 ALA O 188 -1 O ALA O 188 N LYS O 110
CRYST1 63.010 76.370 119.710 90.00 90.00 90.00 P 21 21 21 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 0.015870 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013094 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008354 0.00000
END |