HEADER HYDROLASE 12-OCT-08 3EV4
TITLE CRYSTAL STRUCTURE OF RIBONUCLEASE A IN 50% TRIFLUOROETHANOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE PANCREATIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RNASE 1, RNASE A;
COMPND 5 EC: 3.1.27.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: PANCREAS
KEYWDS RNASE, ORGANIC SOLVENTS, MULTIPLE SOLVENT CRYSTAL STRUCTURES,
KEYWDS 2 ENDONUCLEASE, GLYCATION, GLYCOPROTEIN, HYDROLASE, NUCLEASE, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DECHENE,G.WINK,M.SMITH,P.SWARTZ,C.MATTOS
REVDAT 4 27-DEC-23 3EV4 1 REMARK
REVDAT 3 25-OCT-17 3EV4 1 REMARK
REVDAT 2 28-JUL-09 3EV4 1 JRNL
REVDAT 1 23-JUN-09 3EV4 0
JRNL AUTH M.DECHENE,G.WINK,M.SMITH,P.SWARTZ,C.MATTOS
JRNL TITL MULTIPLE SOLVENT CRYSTAL STRUCTURES OF RIBONUCLEASE A: AN
JRNL TITL 2 ASSESSMENT OF THE METHOD
JRNL REF PROTEINS V. 76 861 2009
JRNL REFN ISSN 0887-3585
JRNL PMID 19291738
JRNL DOI 10.1002/PROT.22393
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 17423
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1720
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1868
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 222
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.53900
REMARK 3 B22 (A**2) : -0.12100
REMARK 3 B33 (A**2) : -1.41800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.59400
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.203
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 1.483 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.410 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.043 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.025 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 35.21
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.PARAM
REMARK 3 PARAMETER FILE 2 : TFE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : TFE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3EV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049804.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17788
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.25200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM CITRATE, PH 5.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 50.27800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.41350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.27800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.41350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1006 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1009 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1039 LIES ON A SPECIAL POSITION.
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 SER A 18
REMARK 465 ALA A 19
REMARK 465 ALA A 20
REMARK 465 SER A 21
REMARK 465 SER B 18
REMARK 465 SER B 21
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 14 70.01 -152.95
REMARK 500 SER A 16 -74.99 -73.06
REMARK 500 GLN A 60 -139.66 -98.88
REMARK 500 ASN A 71 37.37 -94.46
REMARK 500 SER B 16 -55.78 -25.75
REMARK 500 ASP B 38 -45.14 77.04
REMARK 500 GLN B 60 -131.36 -104.41
REMARK 500 ALA B 122 171.92 179.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETF A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETF A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETF A 923
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETF B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETF B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETF B 922
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EUX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CROSSLINKED RIBONUCLEASE A
REMARK 900 RELATED ID: 3EUY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A IN 50% DIOXANE
REMARK 900 RELATED ID: 3EUZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A IN 50% DIMETHYLFORMAMIDE
REMARK 900 RELATED ID: 3EV0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A IN 70% DIMETHYL SULFOXIDE
REMARK 900 RELATED ID: 3EV1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A IN 70% HEXANEDIOL
REMARK 900 RELATED ID: 3EV2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A IN 70% ISOPROPANOL
REMARK 900 RELATED ID: 3EV3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A IN 70% T-BUTANOL
REMARK 900 RELATED ID: 3EV5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A IN 1M TRIMETHYLAMINE N-OXIDE
REMARK 900 RELATED ID: 3EV6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A IN 50% R,S,R-BISFURANOL
DBREF 3EV4 A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 3EV4 B 1 124 UNP P61823 RNAS1_BOVIN 27 150
SEQRES 1 A 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 A 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 A 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 A 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 A 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 A 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 A 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 A 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 A 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 A 124 VAL HIS PHE ASP ALA SER VAL
SEQRES 1 B 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 B 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 B 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 B 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 B 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 B 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 B 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 B 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 B 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 B 124 VAL HIS PHE ASP ALA SER VAL
HET ETF A 903 6
HET ETF A 905 6
HET ETF A 923 6
HET ETF B 901 6
HET ETF B 902 6
HET ETF B 922 6
HETNAM ETF TRIFLUOROETHANOL
FORMUL 3 ETF 6(C2 H3 F3 O)
FORMUL 9 HOH *222(H2 O)
HELIX 1 1 THR A 3 MET A 13 1 11
HELIX 2 2 ASN A 24 ARG A 33 1 10
HELIX 3 3 SER A 50 ALA A 56 1 7
HELIX 4 4 VAL A 57 GLN A 60 5 4
HELIX 5 5 THR B 3 MET B 13 1 11
HELIX 6 6 ASN B 24 ARG B 33 1 10
HELIX 7 7 SER B 50 ALA B 56 1 7
HELIX 8 8 VAL B 57 GLN B 60 5 4
SHEET 1 A 5 VAL A 43 VAL A 47 0
SHEET 2 A 5 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 A 5 TYR A 97 GLU A 111 -1 O THR A 100 N ASP A 83
SHEET 4 A 5 CYS A 72 GLN A 74 -1 N TYR A 73 O VAL A 108
SHEET 5 A 5 LYS A 61 VAL A 63 -1 N LYS A 61 O GLN A 74
SHEET 1 B 4 VAL A 43 VAL A 47 0
SHEET 2 B 4 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 B 4 TYR A 97 GLU A 111 -1 O THR A 100 N ASP A 83
SHEET 4 B 4 VAL A 116 VAL A 124 -1 O VAL A 118 N ALA A 109
SHEET 1 C 5 VAL B 43 VAL B 47 0
SHEET 2 C 5 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 C 5 TYR B 97 GLU B 111 -1 O THR B 100 N ASP B 83
SHEET 4 C 5 CYS B 72 GLN B 74 -1 N TYR B 73 O VAL B 108
SHEET 5 C 5 LYS B 61 VAL B 63 -1 N LYS B 61 O GLN B 74
SHEET 1 D 4 VAL B 43 VAL B 47 0
SHEET 2 D 4 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 D 4 TYR B 97 GLU B 111 -1 O THR B 100 N ASP B 83
SHEET 4 D 4 VAL B 116 VAL B 124 -1 O VAL B 118 N ALA B 109
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.03
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.03
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.03
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.03
SSBOND 5 CYS B 26 CYS B 84 1555 1555 2.04
SSBOND 6 CYS B 40 CYS B 95 1555 1555 2.03
SSBOND 7 CYS B 58 CYS B 110 1555 1555 2.04
SSBOND 8 CYS B 65 CYS B 72 1555 1555 2.03
CISPEP 1 TYR A 92 PRO A 93 0 0.28
CISPEP 2 ASN A 113 PRO A 114 0 0.31
CISPEP 3 TYR B 92 PRO B 93 0 0.16
CISPEP 4 ASN B 113 PRO B 114 0 0.23
SITE 1 AC1 5 LYS A 7 VAL A 118 HIS A 119 HOH A 936
SITE 2 AC1 5 HOH A 939
SITE 1 AC2 6 ASN A 62 VAL A 63 ALA A 64 THR A 70
SITE 2 AC2 6 HOH A 974 HOH B 964
SITE 1 AC3 2 ASN A 67 HOH A 957
SITE 1 AC4 8 PHE B 120 ALA B 122 SER B 123 VAL B 124
SITE 2 AC4 8 ETF B 902 HOH B 992 HOH B1006 HOH B1039
SITE 1 AC5 5 VAL B 43 ASN B 44 THR B 45 PHE B 120
SITE 2 AC5 5 ETF B 901
SITE 1 AC6 5 ASP A 53 ALA A 56 GLN B 28 MET B 29
SITE 2 AC6 5 SER B 32
CRYST1 100.556 32.827 72.515 90.00 90.59 90.00 C 1 2 1 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 0.009945 0.000000 0.000102 0.00000
SCALE2 0.000000 0.030463 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013791 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
