HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 13-SEP-05 2B0A
TITLE CRYSTAL STRUCTURE OF PROTEIN MJ0783 FROM METHANOCOCCUS JANNASCHII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN MJ0783;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 2190;
SOURCE 4 GENE: MJ0783;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS HYPOTHETICAL PROTEIN, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 NYSGXRC, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PATSKOVSKY,U.RAMAGOPAL,S.C.ALMO,S.K.BURLEY,NEW YORK SGX RESEARCH
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 5 14-FEB-24 2B0A 1 REMARK
REVDAT 4 03-FEB-21 2B0A 1 AUTHOR SEQADV
REVDAT 3 13-JUL-11 2B0A 1 VERSN
REVDAT 2 24-FEB-09 2B0A 1 VERSN
REVDAT 1 20-SEP-05 2B0A 0
JRNL AUTH Y.PATSKOVSKY,U.RAMAGOPAL,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN MJ0783 FROM
JRNL TITL 2 METHANOCOCCUS JANNASCHII
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 32334
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 + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1052
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2335
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1487
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 126
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.02000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : -1.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.74000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.069
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.359
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1558 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1468 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2113 ; 1.392 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3439 ; 0.649 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 195 ; 5.651 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 69 ;28.945 ;24.493
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 291 ;12.931 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;12.381 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 237 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1707 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 304 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 294 ; 0.219 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1471 ; 0.193 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 772 ; 0.184 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 970 ; 0.087 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 176 ; 0.225 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 11 ; 0.131 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 57 ; 0.233 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.173 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1253 ; 4.791 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 384 ; 1.095 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1545 ; 5.131 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 713 ; 5.172 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 564 ; 6.784 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2B0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034514.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 87.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.29
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTAM Q315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34059
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.48100
REMARK 200 R SYM FOR SHELL (I) : 0.35000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 550, 100 MM TRIS-HCL, PH 6.50,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 33.97100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.57800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.97100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.57800
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 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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED
REMARK 300 BY THE TWO FOLD AXIS: -X+1, Y, -Z+1
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 42.66684
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 39.11434
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 A 249 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 281 LIES ON A SPECIAL POSITION.
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 CYS A 42 -139.08 58.94
REMARK 500 ILE A 57 70.82 -113.92
REMARK 500 PRO A 77 -71.29 -90.83
REMARK 500 LYS A 170 69.40 -65.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T1168 RELATED DB: TARGETDB
DBREF 2B0A A 1 185 UNP Q58193 Y783_METJA 2 186
SEQADV 2B0A ARG A 14 UNP Q58193 TYR 15 CLONING ARTIFACT
SEQADV 2B0A PRO A 77 UNP Q58193 GLU 78 CLONING ARTIFACT
SEQADV 2B0A GLY A 78 UNP Q58193 ARG 79 CLONING ARTIFACT
SEQADV 2B0A GLU A 186 UNP Q58193 CLONING ARTIFACT
SEQRES 1 A 186 GLU ILE LEU ASP LEU THR GLN THR LEU ILE ASN PHE PRO
SEQRES 2 A 186 ARG PRO GLY ASP PRO GLU LEU ARG ILE ILE GLU LYS LYS
SEQRES 3 A 186 ILE ASP GLY PHE ILE VAL SER GLU ILE ILE MET GLY SER
SEQRES 4 A 186 HIS LEU CYS THR HIS ILE ASP TYR PRO LYS HIS VAL GLY
SEQRES 5 A 186 LEU GLU ASN ARG ILE PRO PHE LYS ASP GLY ILE ILE LYS
SEQRES 6 A 186 GLY LYS GLY TYR CYS ILE SER LEU ASP ASP PHE PRO GLY
SEQRES 7 A 186 ASN LYS LEU PRO ALA CYS ASP ILE LEU LEU ILE TYR THR
SEQRES 8 A 186 GLY PHE SER LYS TYR TRP GLY ARG ASP GLU TYR PHE GLU
SEQRES 9 A 186 LYS ILE PRO GLU ILE PRO PHE LEU ASP ASP ILE ILE LYS
SEQRES 10 A 186 SER ASN ILE LYS CYS VAL GLY ILE ASP ALA CYS THR ILE
SEQRES 11 A 186 GLY GLY PHE GLU GLU HIS LYS ARG LEU LEU SER ASN ASN
SEQRES 12 A 186 ILE LEU ILE ILE GLU ASN LEU ASN GLU ASN LEU LYS ASN
SEQRES 13 A 186 LEU VAL GLY LYS SER PHE TYR PHE LEU GLY LEU PRO LEU
SEQRES 14 A 186 LYS ILE PHE ASP ILE ASP ALA SER PRO ILE ARG CYS ILE
SEQRES 15 A 186 ALA ILE LEU GLU
FORMUL 2 HOH *126(H2 O)
HELIX 1 1 PRO A 48 GLY A 52 5 5
HELIX 2 2 PHE A 59 ILE A 63 5 5
HELIX 3 3 GLY A 92 TRP A 97 5 6
HELIX 4 4 ARG A 99 LYS A 105 5 7
HELIX 5 5 PHE A 111 SER A 118 1 8
HELIX 6 6 GLY A 132 ASN A 142 1 11
HELIX 7 7 ASN A 151 VAL A 158 5 8
SHEET 1 A 9 ILE A 2 ASP A 4 0
SHEET 2 A 9 ALA A 176 ILE A 184 -1 O ALA A 183 N LEU A 3
SHEET 3 A 9 SER A 161 PRO A 168 -1 N TYR A 163 O ILE A 184
SHEET 4 A 9 ILE A 64 SER A 72 -1 N ILE A 64 O GLY A 166
SHEET 5 A 9 ILE A 86 TYR A 90 1 O LEU A 88 N TYR A 69
SHEET 6 A 9 CYS A 122 ILE A 125 1 O GLY A 124 N ILE A 89
SHEET 7 A 9 LEU A 145 GLU A 148 1 O ILE A 147 N VAL A 123
SHEET 8 A 9 HIS A 44 ASP A 46 -1 N ASP A 46 O ILE A 146
SHEET 9 A 9 ALA A 176 ILE A 184 -1 O SER A 177 N ILE A 45
SHEET 1 W 2 ARG A 21 ILE A 27 0
SHEET 2 W 2 PHE A 30 ILE A 36 -1 O VAL A 32 N LYS A 25
CRYST1 67.942 73.156 46.570 90.00 122.87 90.00 C 1 2 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 0.014718 0.000000 0.009511 0.00000
SCALE2 0.000000 0.013669 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025566 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
