| content |
HEADER HYDROLASE 07-AUG-00 1FJ2
TITLE CRYSTAL STRUCTURE OF THE HUMAN ACYL PROTEIN THIOESTERASE 1
TITLE 2 AT 1.5 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL PROTEIN THIOESTERASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.4.39;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA
KEYWDS ALPHA/BETA HYDROLASE, SERINE HYDROLASE, SAD, ANOMALOUS
KEYWDS 2 DIFFRACTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.DEVEDJIEV,Z.DAUTER,S.KUZNETSOV,T.JONES,Z.DEREWENDA
REVDAT 1 29-NOV-00 1FJ2 0
JRNL AUTH Y.DEVEDJIEV,Z.DAUTER,S.KUZNETSOV,T.JONES,
JRNL AUTH 2 Z.DEREWENDA
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN ACYL PROTEIN
JRNL TITL 2 THIOESTERASE I FROM A SINGLE X-RAY DATA SET TO 1.5A
JRNL REF STRUCTURE FOLD DES. V. 8 1137 2000
JRNL REFN UK ISSN 0969-2126
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.0
REMARK 3 NUMBER OF REFLECTIONS : 50223
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) : 0.183
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1293
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3445
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 465
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.20
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): 0.11
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.12
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.08
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.019 ; 0.250
REMARK 3 ANGLE DISTANCE (A) : 0.031 ; 0.400
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.038 ; 0.500
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.013 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.089 ; 0.100
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.180 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.260 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.120 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; 0.300
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 7.000 ; 10.000
REMARK 3 STAGGERED (DEGREES) : 14.700; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 23.300; 25.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.400 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.100 ; 2.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.100 ; 2.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FJ2 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 6
REMARK 6 IN SOLUTION, THERE IS AN EQUILLIBRIUM OF MONOMERIC
REMARK 6 AND DIMERIC SPECIES OF HUMAN ACYL PROTEIN THIOESTERASE
REMARK 6 1. BIOLOGICAL UNIT OF THE ENZYME IS STILL UNCERTAIN.
REMARK 7
REMARK 7 FLEXIBILITY.
REMARK 7 DUE TO STATIC DISORDER THERE IS NO DENSITY
REMARK 7 FOR THE FIRST TWO AMINO ACIDS OF THE CLONING
REMARK 7 ARTIFACT, GLY-ALA AND THE C-TERMINAL
REMARK 7 ASP225. LOOPS A183-A158 AND B80-B84 ARE NOT AS
REMARK 7 WELL DEFINED ON THE ELECTRON DENSITY MAP AS
REMARK 7 THE REMAINDER OF THE STRUCTURE. FINAL ELECTRON
REMARK 7 DENSITY SUGGESTS ALTERNATIVE CONFORMATIONS FOR
REMARK 7 A TOTAL OF 18 SIDE CHAINS IN THE TWO MOLECULES.
REMARK 7 AT THIS STAGE DISORDER IS NOT MODELED YET.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-2000.
REMARK 100 THE RCSB ID CODE IS RCSB011628.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91374
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : QUANTUM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50736
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.0
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 27.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SNB, SHARP,DM,WARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28 - 32% OF SATURATED AMMONIUM
REMARK 280 SULFATE, 0.1 M SODIUM ACETATE, DI-THIO-THREITOL
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 63.94500
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
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 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 GLY A -7
REMARK 465 ALA A -6
REMARK 465 ASP A 225
REMARK 465 GLY B -7
REMARK 465 ALA B -6
REMARK 465 ASP B 225
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 387 O HOH 458 0.08
REMARK 500 O HOH 194 O HOH 292 0.15
REMARK 500 O HOH 433 O HOH 263 0.20
REMARK 500 O HOH 455 O HOH 373 0.25
REMARK 500 O HOH 464 O HOH 135 0.60
REMARK 500 O HOH 19 O HOH 458 1.07
REMARK 500 O HOH 388 O HOH 19 1.55
REMARK 500 BR BR 822 O HOH 458 1.77
REMARK 500 BR BR 822 O HOH 388 1.95
REMARK 500 O HOH 225 OG SER A 42 1.97
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 202 CE MET A 202 SD -0.229
REMARK 500 MET B 202 CE MET B 202 SD -0.268
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 40 CG - CD - NE ANGL. DEV. = 18.2 DEGREES
REMARK 500 VAL A 188 N - CA - CB ANGL. DEV. =-19.7 DEGREES
REMARK 500 ILE A 224 C - N - CA ANGL. DEV. = 20.5 DEGREES
REMARK 500 ILE B 224 C - N - CA ANGL. DEV. = 25.1 DEGREES
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 281 DISTANCE = 5.35 ANGSTROMS
REMARK 525 0 HOH 390 DISTANCE = 6.06 ANGSTROMS
REMARK 525 0 HOH 110 DISTANCE = 5.04 ANGSTROMS
REMARK 525 0 HOH 448 DISTANCE = 5.40 ANGSTROMS
REMARK 525 0 HOH 215 DISTANCE = 5.35 ANGSTROMS
REMARK 525 0 HOH 86 DISTANCE = 5.43 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACA
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE IN CHAIN A
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACB
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE IN CHAIN B
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AUO RELATED DB: PDB
REMARK 900 HUMAN ACYL PROTEIN THIOESTERASE 1 AND CARBOXYLESTERASE FROM
REMARK 900 PSEUDOMONAS FLUORESCENCE (1AUO) ARE 34% IDENTICAL ACCORDING
REMARK 900 TO THE SEQUENCE, HOWEVER, OVERALL FOLD OF THE BOTH ENZYMES
REMARK 900 IS CLOSE WITH R.M.S. VALUE OF 1.34 FOR 212 COMMON C-ALFA
REMARK 900 ATOMS.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AMINO ACID SEQUENCE OF THE PRESENT PDB ENTRY
REMARK 999 IS IDENTICAL WITH GENBANK ENTRY ACC31610.
REMARK 999 HOWEVER, THERE ARE TWO DIFFERENCES BETWEEN PDB
REMARK 999 1FJ2 AND GENBANK ENTRY ACC31610. FIRST,
REMARK 999 THE READING FRAME OF OUR CONSTRUCT STARTS WITH
REMARK 999 MET 5 OF GENBANK ENTRY ACC31610, SO IT IS
REMARK 999 FIVE RESIDUES SHORTER. SECOND, PDB 1FJ2 CONTAINS A
REMARK 999 SEVEN RESIDUE N-TERMINAL CLONING ARTIFACT. THE
REMARK 999 SEQUENCE OF THE CLONING ARTIFACT IS GAMDPEF.
REMARK 999 RESIDUES OF THE CLONING ARTIFACT ARE NUMBERED
REMARK 999 FROM -5 TO -1.
DBREF 1FJ2 A 6 230 SWS 3415123 AAC31610 6 230
DBREF 1FJ2 B 6 230 SWS 3415123 AAC31610 6 230
SEQADV 1FJ2 GLY A -7 GB 3415123 SEE REMARK 999
SEQADV 1FJ2 ALA A -6 GB 3415123 SEE REMARK 999
SEQADV 1FJ2 MET A -5 GB 3415123 SEE REMARK 999
SEQADV 1FJ2 ASP A -4 GB 3415123 SEE REMARK 999
SEQADV 1FJ2 PRO A -3 GB 3415123 SEE REMARK 999
SEQADV 1FJ2 GLU A -2 GB 3415123 SEE REMARK 999
SEQADV 1FJ2 PHE A -1 GB 3415123 SEE REMARK 999
SEQRES 1 A 232 GLY ALA MET ASP PRO GLU PHE MET SER THR PRO LEU PRO
SEQRES 2 A 232 ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA VAL
SEQRES 3 A 232 ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY TRP
SEQRES 4 A 232 ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE LYS
SEQRES 5 A 232 TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR LEU
SEQRES 6 A 232 ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE ILE
SEQRES 7 A 232 GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY ILE
SEQRES 8 A 232 LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP GLN
SEQRES 9 A 232 GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE LEU
SEQRES 10 A 232 GLY GLY PHE SER GLN GLY GLY ALA LEU SER LEU TYR THR
SEQRES 11 A 232 ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR ALA
SEQRES 12 A 232 LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO GLN
SEQRES 13 A 232 GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE LEU
SEQRES 14 A 232 GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU MET
SEQRES 15 A 232 PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU VAL
SEQRES 16 A 232 ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY MET
SEQRES 17 A 232 MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL LYS
SEQRES 18 A 232 GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP
SEQRES 1 B 232 GLY ALA MET ASP PRO GLU PHE MET SER THR PRO LEU PRO
SEQRES 2 B 232 ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA VAL
SEQRES 3 B 232 ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY TRP
SEQRES 4 B 232 ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE LYS
SEQRES 5 B 232 TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR LEU
SEQRES 6 B 232 ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE ILE
SEQRES 7 B 232 GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY ILE
SEQRES 8 B 232 LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP GLN
SEQRES 9 B 232 GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE LEU
SEQRES 10 B 232 GLY GLY PHE SER GLN GLY GLY ALA LEU SER LEU TYR THR
SEQRES 11 B 232 ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR ALA
SEQRES 12 B 232 LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO GLN
SEQRES 13 B 232 GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE LEU
SEQRES 14 B 232 GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU MET
SEQRES 15 B 232 PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU VAL
SEQRES 16 B 232 ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY MET
SEQRES 17 B 232 MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL LYS
SEQRES 18 B 232 GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP
HET BR 801 1
HET BR 802 1
HET BR 803 1
HET BR 804 1
HET BR 805 1
HET BR 806 1
HET BR 807 1
HET BR 808 1
HET BR 809 1
HET BR 810 1
HET BR 811 1
HET BR 812 1
HET BR 813 1
HET BR 814 1
HET BR 815 1
HET BR 816 1
HET BR 817 1
HET BR 818 1
HET BR 819 1
HET BR 820 1
HET BR 821 1
HET BR 822 1
HET BR 823 1
HET BR 824 1
HET BR 825 1
HET BR 826 1
HET BR 827 1
HET BR 828 1
HET BR 829 1
HET BR 830 1
HET BR 831 1
HET BR 832 1
HET BR 833 1
HET BR 834 1
HET BR 835 1
HET BR 836 1
HET BR 837 1
HET BR 838 1
HET BR 839 1
HET BR 840 1
HETNAM BR BROMIDE ION
FORMUL 3 BR 40(BR1 1-)
FORMUL 43 HOH *465(H2 O1)
HELIX 1 1 ASP A -4 THR A 3 5 7
HELIX 2 2 THR A 28 GLY A 38 1 11
HELIX 3 3 THR A 57 MET A 60 5 4
HELIX 4 4 ASP A 80 ASN A 101 1 22
HELIX 5 5 PRO A 104 ASN A 106 5 3
HELIX 6 6 SER A 114 LEU A 125 1 12
HELIX 7 7 LEU A 143 PHE A 147 5 5
HELIX 8 8 PRO A 173 VAL A 188 1 16
HELIX 9 9 ASN A 189 ALA A 191 5 3
HELIX 10 10 CYS A 206 LEU A 221 1 16
HELIX 11 11 PRO B -3 SER B 2 5 5
HELIX 12 12 THR B 28 GLY B 38 1 11
HELIX 13 13 THR B 57 MET B 60 5 4
HELIX 14 14 ASP B 80 ASN B 101 1 22
HELIX 15 15 PRO B 104 ASN B 106 5 3
HELIX 16 16 SER B 114 THR B 127 1 14
HELIX 17 17 LEU B 143 PHE B 147 5 5
HELIX 18 18 PRO B 173 VAL B 188 1 16
HELIX 19 19 ASN B 189 ALA B 191 5 3
HELIX 20 20 CYS B 206 LEU B 221 1 16
SHEET 1 A 7 ALA A 7 VAL A 9 0
SHEET 2 A 7 ILE A 44 CYS A 48 -1 N TYR A 46 O VAL A 9
SHEET 3 A 7 ALA A 17 LEU A 22 1 O ALA A 17 N LYS A 45
SHEET 4 A 7 ILE A 108 PHE A 113 1 O ILE A 109 N ILE A 20
SHEET 5 A 7 GLY A 133 LEU A 137 1 O GLY A 133 N LEU A 110
SHEET 6 A 7 ILE A 161 GLY A 166 1 O LEU A 162 N ALA A 136
SHEET 7 A 7 VAL A 193 TYR A 198 1 N THR A 194 O ILE A 161
SHEET 1 B 2 VAL A 53 PRO A 55 0
SHEET 2 B 2 ALA A 63 PRO A 65 -1 N MET A 64 O ARG A 54
SHEET 1 C 7 ALA B 7 VAL B 9 0
SHEET 2 C 7 ILE B 44 CYS B 48 -1 N TYR B 46 O VAL B 9
SHEET 3 C 7 ALA B 17 LEU B 22 1 O ALA B 17 N LYS B 45
SHEET 4 C 7 ILE B 108 PHE B 113 1 O ILE B 109 N ILE B 20
SHEET 5 C 7 GLY B 133 LEU B 137 1 O GLY B 133 N LEU B 110
SHEET 6 C 7 ILE B 161 GLY B 166 1 O LEU B 162 N ALA B 136
SHEET 7 C 7 VAL B 193 TYR B 198 1 O THR B 194 N GLN B 163
SHEET 1 D 2 VAL B 53 PRO B 55 0
SHEET 2 D 2 ALA B 63 PRO B 65 -1 N MET B 64 O ARG B 54
SITE 1 ACA 3 SER A 114 ASP A 169 HIS A 203
SITE 1 ACB 3 SER B 114 ASP B 169 HIS B 203
CRYST1 39.590 127.890 39.660 90.00 102.80 90.00 P 1 21 1 4
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 0.025260 0.000000 0.005740 0.00000
SCALE2 0.000000 0.007820 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025860 0.00000
END |